ID L_BDVV Reviewed; 1711 AA. AC P52639; Q912Z6; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 2. DT 04-NOV-2026, entry version 122. DE RecName: Full=RNA-directed RNA polymerase L; DE Short=Protein L; DE EC=2.7.7.48; DE AltName: Full=Large structural protein; DE AltName: Full=Replicase; DE AltName: Full=Transcriptase; GN Name=L; OS Borna disease virus (strain V) (BDV). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina; OC Monjiviricetes; Mononegavirales; Bornaviridae; Borna disease virus. OX NCBI_TaxID=928296; OH NCBI_TaxID=9913; Bos taurus (Bovine). OH NCBI_TaxID=9352; Bradypodidae (three-fingered sloths). OH NCBI_TaxID=9925; Capra hircus (Goat). OH NCBI_TaxID=9850; Cervidae (Deer). OH NCBI_TaxID=109474; Crocidura leucodon (Bicoloured white-toothed shrew) (Celebes shrew). OH NCBI_TaxID=9788; Equidae (horses). OH NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus). OH NCBI_TaxID=56798; Hexaprotodon liberiensis (Pygmy hippopotamus) (Choeropsis liberiensis). OH NCBI_TaxID=9844; Lama glama (Llama). OH NCBI_TaxID=9986; Oryctolagus cuniculus (Rabbit). OH NCBI_TaxID=9940; Ovis aries (Sheep). OH NCBI_TaxID=8801; Struthio camelus (Common ostrich). OH NCBI_TaxID=9455; Varecia variegata (Black-and-white ruffed lemur) (Lemur macaco variegatus). OH NCBI_TaxID=30538; Vicugna pacos (Alpaca) (Lama pacos). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=8183914; DOI=10.1073/pnas.91.10.4362; RA Briese T., Schneemann A., Lewis A.J., Park Y.-S., Kim S., Ludwig H., RA Lipkin W.I.; RT "Genomic organization of Borna disease virus."; RL Proc. Natl. Acad. Sci. U.S.A. 91:4362-4366(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RC STRAIN=V/FR; RX PubMed=11602780; DOI=10.1099/0022-1317-82-11-2681; RA Pleschka S., Staeheli P., Kolodziejek J., Richt J.A., Nowotny N., RA Schwemmle M.; RT "Conservation of coding potential and terminal sequences in four different RT isolates of Borna disease virus."; RL J. Gen. Virol. 82:2681-2690(2001). RN [3] RP INTERACTION WITH P PROTEIN. RX PubMed=10756058; DOI=10.1128/jvi.74.9.4425-4428.2000; RA Walker M.P., Jordan I., Briese T., Fischer N., Lipkin W.I.; RT "Expression and characterization of the Borna disease virus polymerase."; RL J. Virol. 74:4425-4428(2000). RN [4] RP SUBCELLULAR LOCATION. RX PubMed=12134049; DOI=10.1128/jvi.76.16.8460-8467.2002; RA Walker M.P., Lipkin W.I.; RT "Characterization of the nuclear localization signal of the borna disease RT virus polymerase."; RL J. Virol. 76:8460-8467(2002). RN [5] RP REVIEW. RX PubMed=11815287; DOI=10.2741/a789; RA Ikuta K., Ibrahim M.S., Kobayashi T., Tomonaga K.; RT "Borna disease virus and infection in humans."; RL Front. Biosci. 7:470-495(2002). RN [6] RP FUNCTION. RX PubMed=14557662; DOI=10.1128/jvi.77.21.11781-11789.2003; RA Schneider U., Naegele M., Staeheli P., Schwemmle M.; RT "Active borna disease virus polymerase complex requires a distinct RT nucleoprotein-to-phosphoprotein ratio but no viral X protein."; RL J. Virol. 77:11781-11789(2003). RN [7] RP FUNCTION. RX PubMed=18653450; DOI=10.1128/jvi.00639-08; RA Poenisch M., Wille S., Staeheli P., Schneider U.; RT "Polymerase read-through at the first transcription termination site RT contributes to regulation of borna disease virus gene expression."; RL J. Virol. 82:9537-9545(2008). RN [8] RP REVIEW. RX PubMed=22138959; DOI=10.1038/nrmicro2675; RA Decroly E., Ferron F., Lescar J., Canard B.; RT "Conventional and unconventional mechanisms for capping viral mRNA."; RL Nat. Rev. Microbiol. 10:51-65(2011). CC -!- FUNCTION: Displays RNA-directed RNA polymerase activity. The mRNA CC guanylyl transferase and mRNA (guanine-N(7)-)-methyltransferase CC activities are supposedly provided by cellular enzymes CC (PubMed:22138959). The template is composed of the viral RNA tightly CC encapsidated by the nucleoprotein (N). Functions either as CC transcriptase or as replicase. The transcriptase synthesizes CC subsequently three subgenomic RNAs, assuring their capping and CC polyadenylation by a stuttering mechanism. In replicase mode, the CC polymerase replicates the whole viral genome without recognizing the CC transcriptional signals. {ECO:0000303|PubMed:22138959, CC ECO:0000305|PubMed:14557662, ECO:0000305|PubMed:18653450}. CC -!- CATALYTIC ACTIVITY: CC Reaction=RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + CC diphosphate; Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA- CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CC -!- SUBUNIT: Interacts with the P protein. {ECO:0000269|PubMed:10756058}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host nucleus CC {ECO:0000269|PubMed:12134049}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=Large structural protein; CC IsoId=P52639-1; Sequence=Displayed; CC Name=Matrix protein; CC IsoId=P0C795-1; Sequence=External; CC Name=Envelope glycoprotein p57 precursor; CC IsoId=P52638-1; Sequence=External; CC -!- SEQUENCE CAUTION: CC Sequence=AAA20228.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U04608; AAA20228.1; ALT_INIT; Genomic_RNA. DR EMBL; AJ311521; CAC70639.1; -; Genomic_RNA. DR RefSeq; NP_042024.3; NC_001607.1. DR PDB; 9H1G; EM; 3.07 A; A=1-1711. DR PDB; 9H1Q; EM; 2.95 A; A=1-1711. DR PDB; 9H1Y; EM; 3.07 A; A=1-1711. DR PDB; 9N0Q; EM; 3.09 A; A=1-1711. DR PDB; 9N0R; EM; 2.71 A; A=1-1711. DR PDB; 9N0S; EM; 3.47 A; A=1-1711. DR PDB; 9N0T; EM; 3.37 A; A=1-1711. DR PDB; 9N0U; EM; 3.46 A; A=1-1711. DR PDB; 9X1V; EM; 2.72 A; A=1-1711. DR PDB; 9X28; EM; 2.83 A; A=1-1711. DR PDB; 9X5R; EM; 2.70 A; A=1-1711. DR EMDB; EMD-51765; -. DR EMDB; EMD-51770; -. DR EMDB; EMD-51785; -. DR EMDB; EMD-66467; -. DR EMDB; EMD-66473; -. DR EMDB; EMD-66595; -. DR SMR; P52639; -. DR Proteomes; UP000007804; Segment. DR GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity; IEA:InterPro. DR GO; GO:0003968; F:RNA-directed RNA polymerase activity; IEA:UniProtKB-KW. DR InterPro; IPR026890; Mononeg_mRNAcap. DR InterPro; IPR014023; Mononeg_RNA_pol_cat. DR Pfam; PF14318; Mononeg_mRNAcap; 1. DR Pfam; PF00946; Mononeg_RNA_pol; 1. DR PROSITE; PS52108; MNV_L_PRNTASE; 1. DR PROSITE; PS50526; RDRP_SSRNA_NEG_NONSEG; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Host nucleus; Magnesium; KW Metal-binding; mRNA capping; mRNA processing; Multifunctional enzyme; KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome; KW RNA-directed RNA polymerase; S-adenosyl-L-methionine; Transferase; KW Viral RNA replication; Virion; Zinc. FT CHAIN 1..1711 FT /note="RNA-directed RNA polymerase L" FT /id="PRO_0000079207" FT DOMAIN 543..715 FT /note="RdRp catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539" FT DOMAIN 787..1238 FT /note="PRNTase (capping)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01452" FT REGION 1066..1082 FT /note="priming-capping loop" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01452" FT MOTIF 844..852 FT /note="Nuclear localization signal" FT /evidence="ECO:0000269|PubMed:12134049" FT MOTIF 1002..1016 FT /note="PRNTase motif A" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01452" FT MOTIF 1061..1066 FT /note="PRNTase motif B" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01452" FT MOTIF 1096 FT /note="PRNTase motif C" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01452" FT MOTIF 1135..1136 FT /note="PRNTase motif D" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01452" FT MOTIF 1174..1183 FT /note="PRNTase motif E" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01452" FT ACT_SITE 1135 FT /note="Nucleophile; for GDP polyribonucleotidyltransferase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01452" FT BINDING 550 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic; for RNA-directed RNA polymerase FT activity" FT /evidence="ECO:0000250|UniProtKB:P28887" FT BINDING 657 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic; for RNA-directed RNA polymerase FT activity" FT /evidence="ECO:0000250|UniProtKB:P28887" FT BINDING 993 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="structural" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01452" FT BINDING 1020 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="structural" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01452" FT BINDING 1210 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="structural" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01452" FT BINDING 1213 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="structural" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01452" FT VARIANT 1526 FT /note="A -> G" FT HELIX 34..40 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 46..53 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 57..60 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 62..64 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 65..69 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 82..98 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 105..117 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 119..138 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 139..142 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 144..151 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 154..159 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 162..175 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 176..201 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 203..205 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 209..220 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 226..248 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 250..252 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 256..258 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 262..265 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 267..279 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 281..288 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 292..294 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 301..311 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 319..345 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 350..353 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 354..356 FT /evidence="ECO:0007829|PDB:9N0S" FT HELIX 359..367 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 374..376 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 379..382 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 383..386 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 398..401 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 402..404 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 406..409 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 411..416 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 420..427 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 443..448 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 451..453 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 455..464 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 469..471 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 473..478 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 489..494 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 495..507 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 508..512 FT /evidence="ECO:0007829|PDB:9N0R" FT TURN 513..515 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 517..523 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 525..541 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 545..550 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 554..557 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 560..573 FT /evidence="ECO:0007829|PDB:9N0R" FT TURN 579..581 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 582..585 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 586..589 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 591..594 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 599..602 FT /evidence="ECO:0007829|PDB:9N0S" FT STRAND 603..608 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 612..617 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 620..622 FT /evidence="ECO:0007829|PDB:9N0S" FT STRAND 624..627 FT /evidence="ECO:0007829|PDB:9N0T" FT HELIX 628..644 FT /evidence="ECO:0007829|PDB:9N0R" FT TURN 645..647 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 650..655 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 658..663 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 667..669 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 671..688 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 695..697 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 699..707 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 710..713 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 721..725 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 739..755 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 760..778 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 781..784 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 787..794 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 798..800 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 806..808 FT /evidence="ECO:0007829|PDB:9N0R" FT TURN 810..813 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 814..816 FT /evidence="ECO:0007829|PDB:9N0U" FT HELIX 820..833 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 839..846 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 856..861 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 871..873 FT /evidence="ECO:0007829|PDB:9N0Q" FT STRAND 878..880 FT /evidence="ECO:0007829|PDB:9N0S" FT HELIX 881..889 FT /evidence="ECO:0007829|PDB:9N0R" FT TURN 893..899 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 903..914 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 917..920 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 922..930 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 933..945 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 946..950 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 951..956 FT /evidence="ECO:0007829|PDB:9N0R" FT TURN 957..960 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 961..978 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 988..990 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 994..1006 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 1018..1021 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 1022..1026 FT /evidence="ECO:0007829|PDB:9N0R" FT TURN 1027..1029 FT /evidence="ECO:0007829|PDB:9N0U" FT HELIX 1033..1035 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 1036..1045 FT /evidence="ECO:0007829|PDB:9N0R" FT TURN 1049..1053 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 1085..1099 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 1105..1117 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 1149..1151 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 1152..1155 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 1158..1160 FT /evidence="ECO:0007829|PDB:9N0R" FT TURN 1165..1167 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 1168..1172 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 1179..1195 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 1204..1208 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 1211..1213 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 1234..1237 FT /evidence="ECO:0007829|PDB:9N0T" FT HELIX 1256..1277 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 1280..1283 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 1298..1302 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 1305..1319 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 1323..1334 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 1339..1347 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 1352..1356 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 1358..1363 FT /evidence="ECO:0007829|PDB:9N0R" FT TURN 1364..1366 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 1372..1380 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 1382..1385 FT /evidence="ECO:0007829|PDB:9N0R" FT TURN 1388..1394 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 1399..1402 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 1406..1408 FT /evidence="ECO:0007829|PDB:9N0T" FT HELIX 1409..1419 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 1447..1449 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 1451..1463 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 1467..1471 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 1477..1485 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 1486..1488 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 1490..1493 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 1500..1508 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 1510..1513 FT /evidence="ECO:0007829|PDB:9N0R" FT TURN 1514..1516 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 1520..1524 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 1531..1539 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 1542..1547 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 1562..1567 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 1587..1589 FT /evidence="ECO:0007829|PDB:9N0S" FT HELIX 1591..1593 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 1598..1615 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 1624..1637 FT /evidence="ECO:0007829|PDB:9N0R" FT TURN 1638..1641 FT /evidence="ECO:0007829|PDB:9N0S" FT STRAND 1646..1648 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 1651..1655 FT /evidence="ECO:0007829|PDB:9N0R" FT STRAND 1658..1664 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 1684..1688 FT /evidence="ECO:0007829|PDB:9N0R" FT TURN 1693..1699 FT /evidence="ECO:0007829|PDB:9N0R" FT HELIX 1702..1708 FT /evidence="ECO:0007829|PDB:9N0R" SQ SEQUENCE 1711 AA; 191734 MW; 554DF018E0E17877 CRC64; MSFHASLLRE EETPRPVAGI NRTDQSLKNP LLGTEVSFCL KSSSLPHHVR ALGQIKARNL ASCDYYLLFR QVVLPPEVYP IGVLIRAAEA ILTVIVSAWK LDHMTKTLYS SVRYALTNPR VRAQLELHIA YQRIVGQVSY SREADIGPKR LGNMSLQFIQ SLVIATIDTT SCLMTYNHFL AAADTAKSRC HLLIASVVQG ALWEQGSFLD HIINMIDIID SINLPHDDYF TIIKSIFPYS QGLVMGRHNV SVSSDFASVF AIPELCPQLD SLLKKLLQLD PVLLLMVSSV QKSWYFPEIR MVDGSREQLH KMRVELETPQ ALLSYGHTLL SIFRAEFIKG YVSKNAKWPP VHLLPGCDKS IKNARELGRW SPAFDRRWQL FEKVVILRIA DLDMDPDFND IVSDKAIISS RRDWVFEYNA AAFWKKYGER LERPPARSGP SRLVNALIDG RLDNIPALLE PFYRGAVEFE DRLTVLVPKE KELKVKGRFF SKQTLAIRIY QVVAEAALKN EVMPYLKTHS MTMSSTALTH LLNRLSHTIT KGDSFVINLD YSSWCNGFRP ELQAPICRQL DQMFNCGYFF RTGCTLPCFT TFIIQDRFNP PYSLSGEPVE DGVTCAVGTK TMGEGMRQKL WTILTSCWEI IALREINVTF NILGQGDNQT IIIHKSASQN NQLLAERALG ALYKHARLAG HNLKVEECWV SDCLYEYGKK LFFRGVPVPG CLKQLSRVTD STGELFPNLY SKLACLTSSC LSAAMADTSP WVALATGVCL YLIELYVELP PAIIQDESLL TTLCLVGPSI GGLPTPATLP SVFFRGMSDP LPFQLALLQT LIKTTGVTCS LVNRVVKLRI APYPDWLSLV TDPTSLNIAQ VYRPERQIRR WIEEAIATSS HSSRIATFFQ QPLTEMAQLL ARDLSTMMPL RPRDMSALFA LSNVAYGLSI IDLFQKSSTV VSASQAVHIE DVALESVRYK ESIIQGLLDT TEGYNMQPYL EGCTYLAAKQ LRRLTWGRDL VGVTMPFVAE QFHPHSSVGA KAELYLDAII YCPQETLRSH HLTTRGDQPL YLGSNTAVKV QRGEITGLAK SRAANLVKDT LVLHQWYKVR KVTDPHLNTL MARFLLEKGY TSDARPSIQG GTLTHRLPSR GDSRQGLTGY VNILSTWLRF SSDYLHSFSK SSDDYTIHFQ HVFTYGCLYA DSVIRSGGVI STPYLLSASC KTCFEKIDSE EFVLACEPQY RGAEWLISKP VTVPEQITDA EVEFDPCVSA SYCLGILIGK SFLVDIRASG HDIMEQRTWA NLERFSVSDM QKLPWSIVIR SLWRFLIGAR LLQFEKAGLI RMLYAATGPT FSFLMKVFQD SALLMDCAPL DRLSPRINFH SRGDLVAKLV LLPFINPGIV EIEVSGINSK YHAVSEANMD LYIAAAKSVG VKPTQFVEET NDFTARGHHH GCYSLSWSKS RNQSQVLKMV VRKLKLCVLY IYPTVDPAVA LDLCHLPALT IILVLGGDPA YYERLLEMDL CGAVSSRVDI PHSLAARTHR GFAVGPDAGP GVIRLDRLES VCYAHPCLEE LEFNAYLDSE LVDISDMCCL PLATPCKALF RPIYRSLQSF RLALMDNYSF VMDLIMIRGL DIRPHLEEFD ELLVVGQHIL GQPVLVEVVY YVGVVRKRPV LARHPWSADL KRITVGGRAP CPSAARLRDE DCQGSLLVGL PAGLTQLLII D //