ID T0K6R7_COLGC Unreviewed; 1727 AA.
AC T0K6R7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Cytokinesis protein sepA {ECO:0008006|Google:ProtNLM};
GN ORFNames=CGLO_09308 {ECO:0000313|EMBL:EQB51172.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB51172.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
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:EQB51172.1}.
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DR EMBL; AMYD01001872; EQB51172.1; -; Genomic_DNA.
DR STRING; 1237896.T0K6R7; -.
DR eggNOG; KOG1922; Eukaryota.
DR HOGENOM; CLU_001313_1_0_1; -.
DR OMA; NHYWKAR; -.
DR OrthoDB; 1118745at2759; -.
DR Proteomes; UP000015530; 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:UP000015530}.
FT DOMAIN 260..685
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 1109..1531
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT DOMAIN 1546..1578
FT /note="DAD"
FT /evidence="ECO:0000259|PROSITE:PS51231"
FT REGION 1..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 966..1110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1518..1727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 716..786
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1400..1427
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1089
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1653..1688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1689..1703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1710..1727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1727 AA; 192166 MW; 2DBEB18E5FB9AF42 CRC64;
MSSTDKSRQS SGGKSFFSRN RKDKRNTSDE GRYLAGGADN FDTASIHSRA SRHHRDSSSV
SIDQFPDSGL SAGPMTSIPY EAVPDSRSPV PVEYLPKPDQ IALLRGGPSP HHLNKGGDFH
QYPNFDPSSM AGGSNSSRTP QSNITMASTG RQTQYQQWGP GPARVSMAST INGSHNPRYD
SYMTSGGRSS ADQASIFSSG NGGTLDKTAN RSSRPALPSA SSQSSYSSHT SYRDSSHPSS
HRLTKFPGMV PTGHDGFHFP RPDNDDIINQ MFLALMQKRG WHNLPEQARR QMVAYPPDKK
WTLLYQDRLT EWQGEQKRRQ TAKPNQYATP EILVNSDEEG SPEWYVRRVM DNSLDTKGLG
SLEVNLRTQQ IGWVKRFIEC QGQVALTNVL MKINRKTALG PAPDQKADRH LDREYDIIKC
LKALMNNKFG ADDALAHQQV MIALATSLIS PRLTTRKLVS EVLTFLCHWG EGEGHLKVIQ
ALDSVKAQQG ENGRFDAWMR LVEVTVDGRG KMGSLVGASD EVRSGGIGME NLLMEYAVAT
LILINMIVDA PERDLQLRMH IRAQFTACGM RRILTKMESF QYDLIDKQIE HFRSNEAIDY
EDMLEKENSS IKDSVEGEVK DLNDPVQIVD AIQQRLRGSK TQDYFISALQ HLLLLRDNDG
EERLRTFQLV DSMLSYVAMD RRLPNMDLKQ SLNFTVQSLL DKLHTDSEAR QALDEAVEAR
QIADAAMAER DEMKERIELG ADGLVAKLQK QLDEQARFID AQRRQAEGLK AELENIQTLR
QKEAQRYELE TRELYLMLRD AQDVAASTAI KGAGSKLGEE DPAKMQGILD RDRLMERLQM
QIERQKTQFK LEGRVWGEAV GPSDRLRALR EEMDDSAMAG SGPGTPPRDF TNSMLGSVNR
NTKIARKPVQ GRELVEGELL ETEEYEDEDG VVYERPRVVE IRRPVMDPSQ KAGLFGEMAG
KVKRYDADSD SEMGEGATTG PSHPSLESGS PITPAEGEPP KIQVTGAGAP PPPPPPPPMP
GQAGAPPPPP PPPPMPGMLS PTGAPAPPPP PPPPPMPGAA GGPPPPPPPP PMPGAAGMPP
PPPPPLPGAI SGHFLSQATP NFSSAPSLGL PAVRPKKKLK ALHWDKVDSP MTTHWAAHAP
SAEEREEKYI ELSKKGILDE VEKLFMAKEI KKLGLGGGGK KDDKKQIING DLRKAYEIAF
AKFSQYSVDK IVQMIIHCDK DILDNPVVMD FLGKDDLCNI PDNTARQLAP YSKDWTGANP
DKADREQDPA ELTRQDQLYL FTAFELHHYW KARMRALSLT RSFEPEFDEI TDKMRHVVGV
SESLRDSVSL MNVLGLILDI GNYMNDANKQ ARGFKLSSLA RLGMVKDDKN ESTLADLVER
IVRNQYPEWE DFSNDISGVM AAQKINIEQL QSDAKQYIDT VKNVQMSLDV GNLSDSKKFH
PQDRVSQVVQ RIMKDARRKA EEMSLYLEEM MKTYNDIMVF YGEDPADENA RRDFFAKLAM
FIGEWKKSRE KNIKYEEQRR RNEASMKRKH QQLNVAGGKV EGAPPSPSSA GAMDSLLEKL
RAAAPQTRDQ RDRRRRARLK DRHQVRIASG QKIPDPDENP EIEANLAQPP KENPIDEDGN
LLSPGLSSPR EGGEDDVAER AAMLLQGMRG GDGADDADPE KRESLRRSRR QTAEEERRMR
RRRREKASST NTAAISEGGE GETTVTEASK EEEIPTTPSV ENTPVES
//
