ID A0A066XGB9_COLSU Unreviewed; 1768 AA.
AC A0A066XGB9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Cytokinesis protein sepA {ECO:0008006|Google:ProtNLM};
GN ORFNames=CSUB01_04884 {ECO:0000313|EMBL:KDN68213.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN68213.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
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:KDN68213.1}.
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DR EMBL; JMSE01000706; KDN68213.1; -; Genomic_DNA.
DR STRING; 1173701.A0A066XGB9; -.
DR eggNOG; KOG1922; Eukaryota.
DR HOGENOM; CLU_001313_1_0_1; -.
DR OrthoDB; 1118745at2759; -.
DR Proteomes; UP000027238; 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; SSF81995; beta-sandwich domain of Sec23/24; 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:UP000027238}.
FT DOMAIN 264..689
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 1157..1578
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT DOMAIN 1593..1625
FT /note="DAD"
FT /evidence="ECO:0000259|PROSITE:PS51231"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 971..1160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1296..1316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1563..1768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 720..790
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 158..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..996
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1138
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1576..1597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1637..1653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1699..1735
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1768 AA; 197713 MW; 3467FF881E101059 CRC64;
MSSIDKSRQS SGGKSFFSRN RKDKRNTSDE GRHLAGADYS DTASTHSRAS RHQRDSSVVS
IDQYPESGMS AGPMTSIPYD SYHDSRSPVP TEYLPRGDQL GVLRQSPLPH HLNKVTSDFH
QYPSFDPSTM AGGTGSHMSA QRVPQSNITM ATTGRQTQYQ QWGPGPGRGS TASTINGSHN
PRYDSYMTSA GRSSADQASI FSSGNGGTYD MTANHSSRPA LPSASSQSSY SSHMSYRDSS
HPPSHRLTKF PGMAPTGHDG FHFPRPDNDE VINQMFLALM QKRGWHNLPE QARRQMVAYA
PDKKWTLLYQ DRLTEWQGEQ KRRQTAKPNQ YAAPEILVNS DEEGSPEWYV RRVMDNSLDT
KGLGSLEVNL RTQQIGWVKR FIECQGQVAL TNVLMKINRK TAIGPVPDGK SDRNSDREYD
IIKCLKALMN NKFGADDALA HQQVLIALAT SLTSQRLTTR KLVSEVLTFL CHWGDGEGHL
KVIQALDSVK TQQGENGRFD AWMRLVEVTV DGRGKMGSMV GASDEVRSGG IGMENLLMEY
AVATLILINM IVDAPEKDLQ LRMHIRAQFT ACGIRRILTK MESFQYDLID KQVEHFRTNE
AIDYEDMLEK ENNSVKDSVE GEVKDLNDPV QIVDAIQQRL RGSKTQDYFI SALQHLLLIR
DNDGEERLRM FQLVDSMLSY VAMDRRLPNM DLKQSLNFTV QSLLDKLHTD SEARQALDEA
LEARQVADAA MAERDEMRER LELGADGLVA KLQKQLDEQA RFIEAQRRQA DGLKAELENI
QTLRQKEAQR YELETRELYL MLRDAQDVAA SNAAKGSKLG EDPGRMQGIL DRDRLMERLQ
MQIERQKTQF KLEGRVWGEA VGPSDRLRAL REEMDDAATG SGGSGPGTPP RDFTNSMLGS
VKRNTKIPRK PVNERGEYLE GDFPEGEEDE EVDKDEEGVV YEKPRVVEIR RPVMDSSQKA
GLFGEMAGKV KRYEGSDSED VEGATTGPSH PSLESGSPIT PAEXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXP PPPPPPMPGQ TGPPPPPPPP
PMPGQAGGPP PPPPPPPMPG MLSPTGAPPP PPPPPPPPPP MGGAPGMPPP PPPPLPGAIS
GHFLSQATPF TSGPSFGLPV VRPKKKLKAL HWDKVDSPMT THWAAHAPSA EEREEKYLEL
SRKGILDEVE KLFMAKEIKR LGIGGAKKDD KKQIISGDLR KAFEIAFAKF SQVSVERIVQ
MIIHCDKEIL DNTVVMEFLR KDDLCNIPDN TAKQMAPYSK DWTGADPDKA DREQDPAELT
RQDQIYLFTA FELHHYWKAR MRALALTRSF EPDFDEITEK MRQVVNVSES LRDSVSLMNV
LGLILDIGNY MNDANKQARG FKLSSLARLA MVKDDKNEST LADLVERIVR NQYPEWEDFA
NDISGVMMAQ KINIEQLQSD AKQYIDTVKN VQMSLDAGNL SDSKKFHPQD RVSQVVQRIM
KDARRKAEEM QLYLEEMMKS YNDIMVFYGE DPTDDNARRD FFAKLAVFIS EWKKSREKNI
QLEETRKRNE ASMKRKHAQL QASNAKAEGQ PPSPSSAGAM DSLLEKLRAA APQTRDQRDR
RRRARLKDRH QVRIASGQNI PDPNENPEVE ATLQQSPREA PIDEDGNPIS PGLSSPREAG
EDDVADRAAM LLQGIRGDGA DDADPEKMEN LRRSRRQTAE EERRMRRRRR EKATSTNTAV
SDGDTTVTEA KEEEIPPTPS VENTPVEP
//
