ID A0A395N7C7_TRIAR Unreviewed; 1038 AA.
AC A0A395N7C7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Cytokinesis sepa {ECO:0000313|EMBL:RFU71794.1};
DE Flags: Fragment;
GN ORFNames=TARUN_10468 {ECO:0000313|EMBL:RFU71794.1};
OS Trichoderma arundinaceum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=490622 {ECO:0000313|EMBL:RFU71794.1, ECO:0000313|Proteomes:UP000266272};
RN [1] {ECO:0000313|EMBL:RFU71794.1, ECO:0000313|Proteomes:UP000266272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40837 {ECO:0000313|EMBL:RFU71794.1,
RC ECO:0000313|Proteomes:UP000266272};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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:RFU71794.1}.
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DR EMBL; PXOA01001223; RFU71794.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395N7C7; -.
DR STRING; 490622.A0A395N7C7; -.
DR Proteomes; UP000266272; 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; 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; 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 SMART; SM01139; Drf_FH3; 1.
DR SMART; SM01140; Drf_GBD; 1.
DR SUPFAM; SSF48371; ARM repeat; 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:UP000266272}.
FT DOMAIN 278..712
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT REGION 1..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 772..806
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1017
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1038
FT /evidence="ECO:0000313|EMBL:RFU71794.1"
SQ SEQUENCE 1038 AA; 115835 MW; D6A5CC82C355AB15 CRC64;
MSSAADKSRQ SSGGRSLFSR GKHRADKRYT DIDPKSSSDQ FETASIISSR SSRHKRESSS
ISIDQPSSPD AGINQMAGVI TSIPYDGPPG SRSPVSLEFL PKPDQVPQRR EPVPHQLNIS
GFDFHQYPSI DPSSMASHHS HTPVRPGTSS NMSPNNITMA TTGKQAQYQQ WGPGPGPGLG
PGPARGSTSS SATNGSYPVR YDSYQNPHYG RSSGESFNNP YGGGQGFLNP ASARSSHTTL
APSPPSSSHH APHSPRESHR LTKMSAYGPT SHDGFYFPKP DDNYVVEQMF MQLMQKRGWH
NLPEQARRQM TAYPAEKKWT LLHQDRLTEW QGEQKRKQTA RAHQYATPDV TTYSDEEGTP
EWYVRRVMED KLDAKGMGSL EVNLRTQQIG WVKRFVECQG QVALVTLLLK INRKNTNGGP
ASSSSSSTID TRVEKNLDRE YDIVKCLKAL MNNKFGADDA LMQSKVLLAL ATCLISSRLT
TRKLVSEILT FLCTWGSHGE GHMKVIQALD EVRTQAGENG RFDAWMRLVE VTVDGRGKMG
SLVGASDELR TGGIGMENLL MEYAVATLIL VNMIIDAPEK DLQMRVHIRA QFHACGIKRI
LTKMEGFQYE LLDKQIDRFR TNEAIDYEDM LERENSSMKD NVEGDAKDLT DPIQIADTIQ
QRLQGTKTHD YFVSALQHLM LIRANDGEER LRMFQLVDSM LSYVAMDRRL PNMDLKQSLN
FTVQSLLDKL HTDSEARQAL DEALESRQIA EAAMAERDEM RAKLELGADG LVAKLQRQLD
EQSRFIEAQK RQADGLKVEL NNIQSVRAKE AQRYELETRE LYLMLRDAQD IAASNAIKSS
NGKPSVKENS VQMQGILDRE RLMERLQKQL ERQKTQYKLE GRIWGDQDGP SDRLRALREA
MDGGDEPSTP PGGGTPPRDF TNSMLGTIHR QPRASRRPAK RESVIDEDDV EMDDEGVIIE
RPRIIEMRRP VVDPKQQAQL LGEMSSKVKR YDGSDSEGDD GATTGPSHPS MESSSPITPA
EGEPPKVEIT DTAGPPPP
//
