ID A0A5M6CC33_9TREE Unreviewed; 506 AA. AC A0A5M6CC33; DT 26-FEB-2020, integrated into UniProtKB/TrEMBL. DT 26-FEB-2020, sequence version 1. DT 17-JUN-2020, entry version 3. DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767}; GN ORFNames=CI109_000839 {ECO:0000313|EMBL:KAA5530659.1}; OS Kwoniella shandongensis. OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes; OC Tremellales; Cryptococcaceae; Kwoniella. OX NCBI_TaxID=1734106 {ECO:0000313|EMBL:KAA5530659.1, ECO:0000313|Proteomes:UP000322225}; RN [1] {ECO:0000313|EMBL:KAA5530659.1, ECO:0000313|Proteomes:UP000322225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 12478 {ECO:0000313|EMBL:KAA5530659.1, RC ECO:0000313|Proteomes:UP000322225}; RA Cuomo C., Billmyre B., Heitman J.; RT "The Genome Sequence of Kwoniella shandongensis CBS 12478."; RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the peptidase A1 family. CC {ECO:0000256|RuleBase:RU000454, ECO:0000256|SAAS:SAAS01079896}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KAA5530659.1}. 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; NQVO01000003; KAA5530659.1; -; Genomic_DNA. DR Proteomes; UP000322225; Unassembled WGS sequence. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW. DR CDD; cd05471; pepsin_like; 1. DR Gene3D; 2.40.70.10; -; 2. DR InterPro; IPR001461; Aspartic_peptidase_A1. DR InterPro; IPR001969; Aspartic_peptidase_AS. DR InterPro; IPR034164; Pepsin-like_dom. DR InterPro; IPR033121; PEPTIDASE_A1. DR InterPro; IPR021109; Peptidase_aspartic_dom_sf. DR PANTHER; PTHR13683; PTHR13683; 1. DR Pfam; PF00026; Asp; 1. DR PRINTS; PR00792; PEPSIN. DR SUPFAM; SSF50630; SSF50630; 1. DR PROSITE; PS00141; ASP_PROTEASE; 1. DR PROSITE; PS51767; PEPTIDASE_A1; 1. PE 3: Inferred from homology; KW Aspartyl protease {ECO:0000256|RuleBase:RU000454}; KW Hydrolase {ECO:0000256|RuleBase:RU000454}; KW Protease {ECO:0000256|RuleBase:RU000454}; KW Reference proteome {ECO:0000313|Proteomes:UP000322225}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 21..506 FT /note="Peptidase A1 domain-containing protein" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5024298427" FT DOMAIN 156..497 FT /note="Peptidase A1" FT /evidence="ECO:0000259|PROSITE:PS51767" SQ SEQUENCE 506 AA; 53497 MW; 8D243790A6FE57A0 CRC64; MPIFGRALLP LLCFFLTAQA QILTLPLLSD PSFKLLSGEI SVRQQLNSWG ITLGPLSVDL GLNLGSLFSR DEKRRSRLPS DHQEDAEKRL LGLNLGLLNL GLSFGGGSSA TSKGAKSSTA PAGKALIDLN LGLDLSLFGW GDADNAARGE RGDTEWYTYI TVGSPPQSLP VLPDTGSSDL FVFGPSCTTC HLNNHTSFLP LSSSTYTNLS SSWSFLYADG SGASGHASND IVSFGDAATS TSMGFAIADV VAGDDFAVSQ RSGVLGLGLD AMSTMPLTDD EIRTNGATLF SRLVKSQGLT ENVLSVRLEK GQQSRGVVTK EGSGQYTLGG VESGYVLGGR AGLTWANVIS SSYWGVGLDD ISVGTNSILR TDNTTPRRAI IDTGTTLIIT STPASAAIHA QIPGSYQDRS SSVWYIPCTV SFPDVKNVFF TISGRRFGVP IEDLAWKVSN QYRGMCISGV QGGMSSFTVL GDMFIKNHYV VLSYGSDGEG SIQVGLGDRT DIISIL //