SEPA_EMENI
ID SEPA_EMENI Reviewed; 1790 AA.
AC P78621; C8V0K5; Q00760; Q5AYV7;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Cytokinesis protein sepA;
DE AltName: Full=Forced expression inhibition of growth A;
DE AltName: Full=Protein FH1/2;
GN Name=sepA; Synonyms=figA; ORFNames=AN6523;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9218790; DOI=10.1093/emboj/16.12.3474;
RA Harris S.D., Hamer L., Sharpless K.E., Hamer J.E.;
RT "The Aspergillus nidulans sepA gene encodes an FH1/2 protein involved in
RT cytokinesis and the maintenance of cellular polarity.";
RL EMBO J. 16:3474-3483(1997).
RN [2]
RP SEQUENCE REVISION TO 143-153; 207; 1071-1109 AND 1644.
RA Hamer L., Harris S.D., Sharpless K.E., Hamer J.E.;
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 559-1790, AND FUNCTION.
RC STRAIN=FGSC 26;
RX PubMed=7713416; DOI=10.1093/genetics/139.2.537;
RA Marhoul J.F., Adams T.H.;
RT "Identification of developmental regulatory genes in Aspergillus nidulans
RT by overexpression.";
RL Genetics 139:537-547(1995).
CC -!- FUNCTION: Involved in cytokinesis. Overexpression results in growth
CC inhibition. {ECO:0000269|PubMed:7713416}.
CC -!- DOMAIN: The DAD domain regulates activation via by an autoinhibitory
CC interaction with the GBD/FH3 domain. This autoinhibition is released
CC upon competitive binding of an activated GTPase. The release of DAD
CC allows the FH2 domain to then nucleate and elongate nonbranched actin
CC filaments (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the formin homology family. BNI1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA33306.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAA33306.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CBF70912.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CBF70912.1; Type=Miscellaneous discrepancy; Note=An additional intron is predicted in this sequence to correct a probable sequencing error.; Evidence={ECO:0000305};
CC Sequence=EAA57863.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA57863.1; Type=Miscellaneous discrepancy; Note=An additional intron is predicted in this sequence to correct a probable sequencing error.; Evidence={ECO:0000305};
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DR EMBL; U83658; AAB63335.3; -; Genomic_DNA.
DR EMBL; AACD01000109; EAA57863.1; ALT_SEQ; Genomic_DNA.
DR EMBL; L36341; AAA33306.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001301; CBF70912.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_664127.1; XM_659035.1.
DR AlphaFoldDB; P78621; -.
DR SMR; P78621; -.
DR STRING; 162425.CADANIAP00007295; -.
DR PRIDE; P78621; -.
DR EnsemblFungi; EAA57863; EAA57863; AN6523.2.
DR GeneID; 2870211; -.
DR KEGG; ani:AN6523.2; -.
DR eggNOG; KOG1922; Eukaryota.
DR HOGENOM; CLU_001313_1_0_1; -.
DR InParanoid; P78621; -.
DR OrthoDB; 1204639at2759; -.
DR Proteomes; UP000000560; Chromosome I.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0043332; C:mating projection tip; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0051017; P:actin filament bundle assembly; IBA:GO_Central.
DR GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IBA:GO_Central.
DR Gene3D; 1.20.58.2220; -; 1.
DR Gene3D; 1.25.10.10; -; 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 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; SSF48371; 1.
DR PROSITE; PS51231; DAD; 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Coiled coil; Reference proteome.
FT CHAIN 1..1790
FT /note="Cytokinesis protein sepA"
FT /id="PRO_0000194903"
FT DOMAIN 274..702
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 955..1136
FT /note="FH1"
FT DOMAIN 1141..1564
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT DOMAIN 1581..1613
FT /note="DAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00577"
FT REGION 1..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 975..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1465..1484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1596..1790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 724..811
FT /evidence="ECO:0000255"
FT COILED 1435..1566
FT /evidence="ECO:0000255"
FT COMPBIAS 17..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1119
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1469..1484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1640..1675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1693..1714
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1722..1777
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 713
FT /note="Missing (in Ref. 3; EAA57863/CBF70912)"
FT /evidence="ECO:0000305"
FT CONFLICT 1104
FT /note="P -> T (in Ref. 5; AAA33306)"
FT /evidence="ECO:0000305"
FT CONFLICT 1476
FT /note="D -> V (in Ref. 5; AAA33306)"
FT /evidence="ECO:0000305"
FT CONFLICT 1504
FT /note="V -> L (in Ref. 5; AAA33306)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1790 AA; 197356 MW; 192136DE2EF2A75B CRC64;
MPTSDKSRQT SAGKSFFGRK LHKERPVEDR WDAHGSWESL APPSSAAGSR SSRYSKRSSI
QSVDFGADID PSLLSTSAGP ITSIPFESLS TDTQSPIPVD YLSKAETSPR KEPSPGHLAK
GVGDFHQYPA WDPSAMRNHQ QFSHPTGPRP PPHAAGVAMS SSATGDKGAR YQQWGRPGSS
AGNAGLSHHS SSTVDSSTNS RMSIDQASIH SSLSSNTRGS SYISTDGSSR TTLPSHSNDR
SNYYAAMNSG RGSSAQGAIP PAQPRVQNTE QYLTRPRDDR VVDQLFLELM QKRGWQNLPE
QARRQMMAYP ASKKWTLVHQ DRLTELQGEQ KRKQKARETH GYDGPSGILE RADEEGSPEW
YVKKVMDDTI TSKQLASLSV SLRTQPISWV KAFVEAQGQI ALTNVLVKIN RKKVTGPVPA
PPSGDKDLDR EYDIVKCLKA LMNNKYGADD ALAHQQIIVA LISSLLSPRL NTRKLVSEVL
TFLCHWAEGQ GHERVLQAMD HVKNHQGETG RFDAWMRIVE VTIDGRGKMG SLVGASEEYR
SGGIGMENLL MEYAVSTMIL INMLVDAPEN DLQLRCHIRA QFISCGIKRL LSKMEGFQYE
VIDKQIEHFR ENEAIDYEDL LQRESSSTKD SIEGEVKDMT DPLQITDAIA SRLNGTRAHD
YFLSALQHLL LIRENSGEDG LRMYQLVDAM LSYVAMDRRL PDLDLRQGLT FTVQSLLDRL
HTDAEARRAY DESLEARQIA EAALAERDEM KAQVELGADG LVRKLQKQIE EQTGIIELQS
RQNEMLKAEL ADVQRLRAQE LQRNELETRE LYLMLRDAQD IAASNAKKSN MGEAETDPAH
MRGILDREKL LTRLEKQLER TKTQFKLEGK VWGQHDPSDR LRELREQMDG DAGPREAFEE
QARLNLSLNP VGSVYRKKTY IQGMEDTATE ELGQTDDEVV YAKARLVDLH RPRMDPEQAT
GLLGEIAAKV PKIDADDAKD EGKPTESEQP AEGAATKGDE QGVDDTVAVD KATAAPPPPP
PPPPAHPGLS GAAPPPPPPP PPPPPGAGAA PPPPPPPPPP PPGGLGGPPP PPPPPPPGGF
GGPPPPPPPP GGFGGPPPPP PPPPGGAFGV PPPPPPPGTV IGGWRANYLA SQGAPSHAIP
VMSSIRPKKK LKALHWDKVD TPQVTVWATH GTTPQEKEEK YVELAKRGVL DEVERLFMAK
ETRIFGGGVA AKQRKDKKQI ISNDLSKNFQ IALSKFSQFP AEEVVRRIIH CDAEILDNMV
VMEFLQRDEM CTVPENVSKL MAPYSKDWTG PDAANTEREQ DPSELTREDQ IYLYTAFELN
HYWKARMRAL ALTRSFEPDY EHISAKLREV VRVSESLRDS VSLMNVLGLI LDIGNFMNDA
NKQAQGFKLS SLARLGMVKD DKNETTFADL VERIVRNQYP EWEDFTEQIS GVIGLQKLNV
DQLRTDAKKY IDNIKNVQAS LDAGNLSDPK KFHPQDRVSQ ITQRSMKDAR RKAEQMQLYL
EEMVKTYDDI MVFYGEDNTD DGARRDFFAK LAAFLQEWKK SKEKNIALEE ARRRTEASLA
RKRINVGLAN GAGAAGDAPV SPATSGAMDS LLEKLRAAAP QAKDQRDRRR RARLKERHQV
RVASGQKIPD LEGAEAPGSG GQNSGATDTN ATDSSLLSPT IQEPEGGSSP IASQSEDVAD
RAASMLQDML RNSPDPERTR RRRESAEEER RKRRLRRRNG ATSGSKDSND TTPLSPVTEP
TSTQGESAEP ENLSLSSPPN GEDPTLNPPT IVLSSDASDT PDDEHRPSTS
