ID A0A5D2ZL83_GOSMU Unreviewed; 921 AA. AC A0A5D2ZL83; DT 13-NOV-2019, integrated into UniProtKB/TrEMBL. DT 13-NOV-2019, sequence version 1. DT 02-OCT-2024, entry version 11. DE RecName: Full=Formin-like protein {ECO:0000256|RuleBase:RU361260}; GN ORFNames=E1A91_A04G026000v1 {ECO:0000313|EMBL:TYJ38893.1}; OS Gossypium mustelinum (Cotton) (Gossypium caicoense). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium. OX NCBI_TaxID=34275 {ECO:0000313|EMBL:TYJ38893.1, ECO:0000313|Proteomes:UP000323597}; RN [1] {ECO:0000313|EMBL:TYJ38893.1, ECO:0000313|Proteomes:UP000323597} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1408120.09 {ECO:0000313|EMBL:TYJ38893.1}; RA Chen Z.J., Sreedasyam A., Ando A., Song Q., De L., Hulse-Kemp A., Ding M., RA Ye W., Kirkbride R., Jenkins J., Plott C., Lovell J., Lin Y.-M., Vaughn R., RA Liu B., Li W., Simpson S., Scheffler B., Saski C., Grover C., Hu G., RA Conover J., Carlson J., Shu S., Boston L., Williams M., Peterson D., RA Mcgee K., Jones D., Wendel J., Stelly D., Grimwood J., Schmutz J.; RT "WGS assembly of Gossypium mustelinum."; RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the formin-like family. Class-I subfamily. CC {ECO:0000256|ARBA:ARBA00025793}. 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; CM017639; TYJ38893.1; -; Genomic_DNA. DR AlphaFoldDB; A0A5D2ZL83; -. DR Proteomes; UP000323597; Chromosome a04. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0051015; F:actin filament binding; IEA:InterPro. DR GO; GO:0045010; P:actin nucleation; IEA:InterPro. DR Gene3D; 1.20.58.2220; Formin, FH2 domain; 1. DR InterPro; IPR015425; FH2_Formin. DR InterPro; IPR042201; FH2_Formin_sf. DR InterPro; IPR027643; Formin-like_plant. DR PANTHER; PTHR23213:SF269; FORMIN-LIKE PROTEIN 5; 1. DR PANTHER; PTHR23213; FORMIN-RELATED; 1. DR Pfam; PF02181; FH2; 1. DR SMART; SM00498; FH2; 1. DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1. DR PROSITE; PS51444; FH2; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000323597}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 268..289 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 479..910 FT /note="FH2" FT /evidence="ECO:0000259|PROSITE:PS51444" FT REGION 150..259 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 298..317 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 362..483 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 895..921 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 826..853 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 170..192 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 219..241 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 362..384 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 412..460 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 468..483 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 907..921 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 921 AA; 98874 MW; B9A8ED2D5B55639A CRC64; MERGPLSACD NAYDTRKYGW QKNSLSAAEE AFLNVLVDPS TGEINENRVG LLWINCRQDL NDLLYAFVDP KLRRLEEILS NVIHTAGYSS AKENIRSLVN IRHPELKHVL SNCIRNNHLI FQVSKEDSKP WYTSYVKLLF RRHDVPRRIL GSKNTEEAPD SDLGPSPSPS SSPSSSPSSS PSPSPSSSPS SSPNLAPAPS DSKVPESEAA DSKAPDVRPT PLKRPPFSLP PPVPTRSNQH PPPVLSPQNN SHHDEDHLEE KGTSLRTLII ACIVTALVTA IAALLFLSLC SRKQINKKPI SGGEIGKASN EHKDSTDDSI ALEISSDGKS SPGTVGVAGA AATAVAATAT AAAAAGAGSG ASKASAESSA TSGDTNSVVP QPAGKAGTST AAVPLVNGLS GGVDAAPSEP PNQVGANPPP APTGSANVPR PPEPMSPPKP PTSPPKPPPP VPPGPKVPKL PGGPQHSNAK SGDGSSAAGN DANTSKAKLK PFFWDKVAAK PNNAMVWDQI KAGSFQFSEE LIETLFGASG QKNKKTGKKE PSAQDQGPQY VQLIEPKKAQ NLAILLRALN VTTKEVCDAL REGNDLPVEL LQTLLKMAPT SDEEHKLKTF RGEFSQLGLS EQFLKQLLDI PFAFKRIEAL IFMCSLKEDV SATKESFKTL EVACKDLRGS RLFLKLLEAV LKTGNRMNDG TFHGGAQAFK LDTLLKLSDV KGVDGKTTLL HFVVLEIIRT EGLKAAHAER ESESFNSLKS NDILEDVSHD PEDHYHDLGF KAVSHLSSEL ENVKKAAAID AENLTGTVIK LGHSLLKARD FLNSEMKGLE EDSGFQKALK SLVEKAEVEV KSLIEEEKRI MELVKKTGNY FHGNVKKDEG IRLFVVVRDF LVILDKVCKE VRDKPKISHK KEGSHASSST DSSIRSPSPY C //