ID A0A1L9UC39_ASPBC Unreviewed; 1801 AA.
AC A0A1L9UC39;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Cytokinesis protein sepA {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASPBRDRAFT_132141 {ECO:0000313|EMBL:OJJ69218.1};
OS Aspergillus brasiliensis (strain CBS 101740 / IMI 381727 / IBT 21946).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=767769 {ECO:0000313|EMBL:OJJ69218.1, ECO:0000313|Proteomes:UP000184499};
RN [1] {ECO:0000313|Proteomes:UP000184499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101740 / IMI 381727 / IBT 21946
RC {ECO:0000313|Proteomes:UP000184499};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC -!- SIMILARITY: Belongs to the formin homology family. BNI1 subfamily.
CC {ECO:0000256|ARBA:ARBA00037935}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV878689; OJJ69218.1; -; Genomic_DNA.
DR STRING; 767769.A0A1L9UC39; -.
DR VEuPathDB; FungiDB:ASPBRDRAFT_132141; -.
DR OMA; NHYWKAR; -.
DR OrthoDB; 1118745at2759; -.
DR Proteomes; UP000184499; 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 Reference proteome {ECO:0000313|Proteomes:UP000184499}.
FT DOMAIN 286..714
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 1125..1548
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT DOMAIN 1566..1598
FT /note="DAD"
FT /evidence="ECO:0000259|PROSITE:PS51231"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 986..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1266..1288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1581..1801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1021
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1104
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1661..1679
FT /note="Basic and acidic 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"
SQ SEQUENCE 1801 AA; 199656 MW; F61A12CBD166186D CRC64;
MPTTTSAPDK SRQTSAGKSF FGRKLHKEKP VDDRHDAYGG SETLAPPGSA PGSRSSRHSK
RSSVQSMDFS NDIDPAALSM TAGVITSIPY ESLPADTKSP IPIDYLSKAE TSPRKEPSPN
HLAKGGSDFH QYPAWNPATI RDNNVYSHPT GPRPPPHASN VTMAGSSSGD KGARYQQWGR
PGSSAANTGF SHNSSSTVDS SSHSRISFDQ ASVHSSLSSN TRDTRGSSYF SSDGSSRTLT
TSHSADRNTY SSSGTSSRLS NAQAAWQSAQ PAQPAKLPVN PEHYLTRPRD DRIVDQLFLE
LMQKRGWQNL PEQAKRQMLA YPASKKWTLV HQDRLTEIQG EQKRRQNARQ THGHDGPSGI
LERADEEGSP EWYVKKVMDD SITSKQLASL SVSLRTQPIS WVKAFVEAQG QIALTNVLAK
INRRKASGPV PAPPTGDKDL DREYDIVKCL KALMNNKYGA DDALAHQQVI VALVSSLLSP
RLNTRKLVSE VLTFLCHWAE GQGHQKVLQA MDHVKNHHGE TGRFDAWMRI VEVTIDGRGK
MGSLVGASEE YRSGGIGMEN LLMEYAVSTM LLINMLVDAP ENDLQLRCHI RAQFTSCGIK
RLMTKMEGFQ YEVIDKQIER FRENEAIDYE DLLQRESSSV KDSIEGEVKD MSDPLQITDA
IASRITGTRA HDYFLSAMQH MLLIRENSGE DGLRMYQLVD AMLSYVAMDR RLPDLDLRQG
LTFTVQSLLD KLHTDSEARQ AYDESLEARQ IAEAALAERD EMKAQIELGA DGLVKKLQKQ
IEEQTGIIEL QRRREESIRA ELADVQRLRA QELQRNELET RELYLMLRDA QDIAASNAKK
NNLAEVDPSH MRGIMDREKL LERLEMQLER TKTQFKLEGK VWGQHVTSDR LRELREQMDG
DIEPQDGFQE QAHQNVVGLG SVQRKRSHLP GMETGTFEGQ QQEGQVDENG EIIYEKARLV
DFHRPRLNPK QANGLLGEIA SKVPKIDADD NETAPAVSEI DEPTAAVTDE PKVESEIEKP
EAKGAPAPPP PPPPPPPPPP PGAVGIPPPP PPPPPPPPPG GKAGIPPPPP PPPPPGGARF
PPPPPPPPGV SFGAPPPPPP PGAGFGGWRA NYMASQALPQ HKTALMPSIR PKKKLKALHW
EKVDTPQVTV WAAHAPTAQE KEEKYVELAK KGVLDEVERL FMAKETKIFG GNAAAKQRKD
KKQLISNELS KNFQIAMAKF SQFPADDVVR MIIHCDTEIL DNQVVMEFLQ RDEMCTIPEN
ISKSMAPYSR DWTGPDAASA EREQDPNELT REDQIYLYTA YELNHYWKAR MRALALTRSF
EMDYEHISAK LQQVVKVSES LRDSVSLMNV LGLILDIGNF MNDANKQAQG FKLSSLARLG
MVKDDKNETT FADLVERIVR NQYPEWEGFV DEINGVIAIQ KLNVDQLRTD AKKYIDNIKN
VQASLDAGNL SDPKKFHPQD RVSQIVQRSM KDARRKAEQM QLYLDEMIKS YDDIMVFYGE
DNSDEGARRD FFAKLASFLL EWKKSKEKNI SLEESRRRTE ASLARKRNIN AGLANGAASA
SDAPPSPATS GAMDSLLEKL RAAAPQARDQ RDRRRRARLK ERHQIRVASG QKIPDVAGAE
APEGGNEAED DGSSNKAGNE NDNEASAAES GLLSPPLLEA ESSESKKKDP QHVSESEDVA
DRAASMLQGL RDNMDGDRMR RRRETAEEER RKRRLLRRRN GGSTSNNNAE ASAATPVPEP
ISPPRTDLEP DDAASPRSGD DPLPQPPLTP AIVVSPTADQ QLRSPGDDES LEGSPSSRSI
E
//
