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Database: UniProt
Entry: A0A175W430_9PEZI
LinkDB: A0A175W430_9PEZI
Original site: A0A175W430_9PEZI 
ID   A0A175W430_9PEZI        Unreviewed;      1783 AA.
AC   A0A175W430;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Cytokinesis protein sepA {ECO:0000313|EMBL:KXX78423.1};
GN   ORFNames=MMYC01_203485 {ECO:0000313|EMBL:KXX78423.1};
OS   Madurella mycetomatis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariales incertae sedis; Madurella.
OX   NCBI_TaxID=100816 {ECO:0000313|EMBL:KXX78423.1, ECO:0000313|Proteomes:UP000078237};
RN   [1] {ECO:0000313|Proteomes:UP000078237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA   van de Sande W.W.J.;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KXX78423.1, ECO:0000313|Proteomes:UP000078237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA   Van De Sande W.;
RT   "Madurella mycetomatis genome sequencing.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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:KXX78423.1}.
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DR   EMBL; LCTW02000120; KXX78423.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A175W430; -.
DR   STRING; 100816.A0A175W430; -.
DR   VEuPathDB; FungiDB:MMYC01_203485; -.
DR   OrthoDB; 1118745at2759; -.
DR   Proteomes; UP000078237; 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:UP000078237}.
FT   DOMAIN          263..689
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000259|PROSITE:PS51232"
FT   DOMAIN          1125..1546
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   DOMAIN          1559..1591
FT                   /note="DAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51231"
FT   REGION          1..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          139..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          212..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          879..916
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          971..1029
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1268..1287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1531..1761
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1415..1442
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..36
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..239
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        978..998
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1273..1287
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1692..1727
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1783 AA;  198700 MW;  D3210FCC01B69742 CRC64;
     MSSYDKSRAS STGKASSFFH RSKNKADKKN TGDDGRHLAA NNDNTSGSVS SRTSRHQRES
     SVISIDRPSS AESGINMMAG VMTTIPYESV SADHRSPVPV DYIPQGDQMP VRREPLPHQL
     NKATSDFHQY PSFEHVSTPY LSGQRPPPGA SNITMASTGR QAQYQQWGPP RDSSLAGSHS
     SRYNSYMTSG GRSSADNLSV LSGNGGPFFE QRAAHRSSRL AQAAAPGASS PTSSYLSPHS
     PRDGHRLTKF PSGYQTSEGF QLPKPEDDGV IEQMFLALMQ KRGWHNLPDQ AKRQMVAYPA
     QKKWTLIYQD ALTEWQGEQK RRNTAKIGQY SNVDLSQLPD EEGSPEWYVR KVMENSLDTK
     GFGSLEVNLR TQQIGWVKRF IECQGQVALT NVLMKLNRRG AMGQAQDAGK GDKNLDREYD
     IVKCLKALMN NKFGADDALA HQQVLVALAT CLISPRLSTR KLVSEVLTFL CHWSDGKGHV
     KVIEAMDVAK NQQGENGRFD AWMRLVEVTV DGRGKMGSLV GASDEVRSGG IGMENLLMEY
     AVATLILINM LIDAPEKDLQ LRVHIRAQFT ACGIKRMLTK MESFQYELID KQIERFRTNE
     AIDYEDMLER ENSSIKDSVD GEVRDLNDPV QIVDAIQQRL KGSKTQDYFI SALQHLLLIR
     DNDGEERLRM FQLVDSMLSY VAMDRRLPDM DLKQSLNFTV QSLLDKLHTD SEARQAFDEA
     TESRQIAEAA MAERDELREK LALGADGLVA KLQKQIDEQA RFIEAQRRLT EGLKSELESM
     QTVRAKEAQR YELETRELYL MLRDAQDVAA SNAAKGNKLG DEDPARMQGI LDREKLMERL
     QMQLERQKTV YKLEGRVWGE AIGPSDRLRA LREEMDGFGD SGLGAGTPPR DFTNSMLGSV
     QRSTRIPRKP VGARAEHADD ILEEEVEDTV EDEEGVVYEK PRLVEIKRPV MDPKQAAGMF
     NELQDKVKRF DASDSEGEGV TTGPSHPSLE SQFPVTPSDT EPPKIKITDT YPPGPASTAS
     GGPPPPPRRL LHHYRVTYPV RRPLWLPRSP AKSQVVLLHL LHHPLPLRPA ISRVLRLRLR
     LLRLLRPANF PGMPPPPPPP MPGPGAMSGH FLSRQQDFTQ APSLGLSIAR PKKKLKALHW
     EKVDSPVATH WAAHTPSAEE REEKYLELSR KGILDEVEKL FMAKEIKQIG QGTAKKDDKK
     QIISNDLRKA FEIALAKYSQ YSVEKVVQMI IHCDKEVLDN PVVMEFLQKE EICNIPDNTA
     KLMAPYSKDW TGPEANKENR EQDPSELTRQ DQIYLQTAFE LHHYWKSRMR ALSLTRSFEA
     DYDEITEKMR QVVSVSESLR DSVSLMNILG LILDIGNYMN DANKQARGFK LSSLARLGMV
     KDDKNQSTLA DLVERIVRHQ YPEWGNFADD IGGVLTAQKI NIEQLQADAK KYIDNVRNVQ
     MSLDSGNLAD PKKFHPQDRV AQVVQRCMKD ARRKAEQMQV YLEEMVRTYN DIMAFYGEDP
     TDDNARRDFF SKLALFITDW KKSHTKNLEL EEQRKKNEAS MKRKNALKTA QAAEGMPASP
     TSTGAMDSLL EKLRAAAPQA RDQRDRRRRA RLKDRHQVRI ASGQKMPDLD QEASEGQAQG
     ETGGVPPGQG PGSEVTDEDG KASKTDLLSP TAAKDADASA AAAAGGAGGE EDDVAQRAAL
     LLQGMRSGAD GADDPADAEK RENLRRSRRQ TADEERRMRR RRREMAQSSA SNGDVSGKED
     GPGGGGSADV PPTPSAEEFA AAVAAAGVEV ASPTAGGHVN GTS
//
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