ID A0A484FIN0_COLOR Unreviewed; 1710 AA.
AC A0A484FIN0;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Cytokinesis protein sepA {ECO:0000313|EMBL:TDZ17718.1};
GN Name=sepA {ECO:0000313|EMBL:TDZ17718.1};
GN ORFNames=Cob_v009298 {ECO:0000313|EMBL:TDZ17718.1};
OS Colletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 / LARS
OS 414 / MAFF 240422) (Cucumber anthracnose fungus) (Colletotrichum
OS lagenarium).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum orbiculare species complex.
OX NCBI_TaxID=1213857 {ECO:0000313|EMBL:TDZ17718.1, ECO:0000313|Proteomes:UP000014480};
RN [1] {ECO:0000313|Proteomes:UP000014480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC {ECO:0000313|Proteomes:UP000014480};
RX PubMed=23252678; DOI=10.1111/nph.12085;
RA Gan P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA Takano Y., Kubo Y., Shirasu K.;
RT "Comparative genomic and transcriptomic analyses reveal the hemibiotrophic
RT stage shift of Colletotrichum fungi.";
RL New Phytol. 197:1236-1249(2013).
RN [2] {ECO:0000313|Proteomes:UP000014480}
RP GENOME REANNOTATION.
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC {ECO:0000313|Proteomes:UP000014480};
RX PubMed=30893003; DOI=10.1094/MPMI-12-18-0352-A;
RA Gan P., Tsushima A., Narusaka M., Narusaka Y., Takano Y., Kubo Y.,
RA Shirasu K.;
RT "Genome sequence resources for four phytopathogenic fungi from the
RT Colletotrichum orbiculare species complex.";
RL Mol. Plant Microbe Interact. 32:1088-1090(2019).
CC -!- SIMILARITY: Belongs to the formin homology family. BNI1 subfamily.
CC {ECO:0000256|ARBA:ARBA00037935}.
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:TDZ17718.1}.
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; AMCV02000027; TDZ17718.1; -; Genomic_DNA.
DR STRING; 1213857.A0A484FIN0; -.
DR Proteomes; UP000014480; Unassembled WGS sequence.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:UniProt.
DR GO; GO:0005938; C:cell cortex; IEA:UniProt.
DR GO; GO:0032153; C:cell division site; IEA:UniProt.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProt.
DR Gene3D; 6.10.30.50; -; 1.
DR Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR Gene3D; 1.10.238.150; Formin, FH3 diaphanous domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR014767; DAD_dom.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR010472; FH3_dom.
DR InterPro; IPR014768; GBD/FH3_dom.
DR InterPro; IPR010473; GTPase-bd.
DR PANTHER; PTHR47102; PROTEIN BNI1; 1.
DR PANTHER; PTHR47102:SF2; PROTEIN BNI1; 1.
DR Pfam; PF06367; Drf_FH3; 1.
DR Pfam; PF06371; Drf_GBD; 1.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM01139; Drf_FH3; 1.
DR SMART; SM01140; Drf_GBD; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR PROSITE; PS51231; DAD; 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000014480}.
FT DOMAIN 234..659
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 1095..1517
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT DOMAIN 1532..1564
FT /note="DAD"
FT /evidence="ECO:0000259|PROSITE:PS51231"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 939..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1235..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1497..1710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 690..760
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1386..1413
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..882
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..963
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..1076
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1497..1514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1515..1529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1569..1585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1639..1674
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1710 AA; 190510 MW; 6C4EB8B46302B140 CRC64;
MSSTDKSRQS SGGKSFFSRN RKDKRNTSDE GRHLAGGDSF DTASVHSRAS RHHRDSSSVS
IDQFPDSGLT AGPMTSIPYD SVPDSRSPVP VEHLPKAEQI ALMRNGSSPH HLNKNAGDFH
QYPTFDPSTM AGGAGSHASA QRAPQSNITM ASTGRQTQYQ QWGPGPGRVS MASTINGSHN
PRYDSIFSSA LPSASSQSSY SSHMSYRDSS HPSSHRLTKF PGMGPTGHDG FHFPRPDNDE
IIGQMFLALM QKRGWHNLPE QARRQMVAYP ADKKWTLLYQ DRLTEWQGEQ KRRQTAKPNQ
YSTPEILVNS DEEGSPEWYV RRVMDNSLDT KGLGSLEVNL RTQQIGWVKR FIECQGQVAL
TNVLMKINRK TALGPAPDQR ADRHLDREYD IIKCLKALMN NKFGADDALV HQQVIIALAT
SLISPRLTTR KLVSEVLTFL CHWGDGEGHL KVIQALDSVK AQQGENGRFD AWMRLVEVTV
DGRGKMGSLV GASDEVRSGG IGMENLLMEY AVATLILVNM IVDAPERDLQ LRMHVRAQFT
ACGIRRILTK MESFQYDLID KQIEHFRTNE AIDYEDMLEK ENNSIKDSVE GEVKDLNDPV
QIVDAIQQRL RGSKTQDYFV SALQHLLLLR DNDGEERLRT FQLVDSMLSY VAMDRRLPNM
DLKQSLNFTV QSLLDKLHTD SEARQALDEA LEARQIADAA MAERDEMRER LELGADGLVA
KLQKQLDEQS RFIEAQRRQA EGLKAELENI QTLRQKEAQR YELETRELYL MLRDAQDVAA
SNAVKSNNNN KLGEEDPTRM QGILDRDRLM ERLQMQIERQ KTQFKLEGRV WGEAVGPSDR
LRALREEMDD SGMGSGPGTP PRDFTNSMLG SVNRNTKISR KPVNGRGEQL GGDLLEGEEG
EEDEDGVVYE KPRVVEIRRP VMDPSQKAGL FGEMAGKIKR FDASDSEDGE ATTGPSHPSL
ESGSPITPAE GEPPKIQVTG AGAPPPPPPP PMPPGLGGPP PPPPPPMPPG LGGPPPPPPP
PPMPGMLSPT GAAPPPPPPP PPMPPGLGGP PPPPPPPMPP GMGGLPPPPP PPLPGAISGH
FLSQATPSFS PSSLGMPVVR PKKKLKALHW DKVDSPLTTH WAAHAPSAEE REEKYMELSR
KGILDEVEKL FLAKETRKLG IGSGAKKDDK KQIINGDLRK AFEIAFAKFS QVSVEKIVQM
IIHCDKDMLD NPVVMDFLRK DDLCNIPDNT AKQMAPYSKD WTGANPDKAE REQDPSELTR
QDQLYLYTAF ELHHYWKARM RALALTRSFE PDFDEITDKM RHVSAVSESL RDSVSLMNVL
GLILDIGNYM NDANKQARGF KLSSLARLGM VKDDKNESTL ADLVERIVRN QYPEWENFAD
DIAGVMAAQK INIEQLQSDA KQYIDTVKNV QMSLDAGNLS DSKKFHPQDR VSQVVQRVMK
DARRKAEEMQ LYLEEMMKTY NDIMVFYGED PTDENARRDF FAKLASFVGD WKKSRDKNVK
LEEQRRRNEA SMKRKHQQLQ VSSGKVEGAP PSPSSAGAMD SLLEKLRAAA PQTRDQRDRR
RRARLKDRHQ VRIASGQKIP DPDEDPVVEA ALAEPPKEPT IDEDGNPISP GLSSPREAGE
DDVAERAALL LQGMRGGDAA EEADPEKRES LRRSRRQTAE EERRMRRRRR EKATSTNTAA
IGEEESTVTE ASKEEDIPVK PSVENTPVEP
//