ID A0A3D8SC55_9EURO Unreviewed; 1701 AA.
AC A0A3D8SC55;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Putative Cytokinesis protein SepA {ECO:0000313|EMBL:RDW83927.1};
GN ORFNames=DSM5745_04253 {ECO:0000313|EMBL:RDW83927.1};
OS Aspergillus mulundensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1810919 {ECO:0000313|EMBL:RDW83927.1, ECO:0000313|Proteomes:UP000256690};
RN [1] {ECO:0000313|EMBL:RDW83927.1, ECO:0000313|Proteomes:UP000256690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5745 {ECO:0000313|EMBL:RDW83927.1,
RC ECO:0000313|Proteomes:UP000256690};
RX PubMed=30018880; DOI=10.5598/imafungus.2018.09.01.13;
RA Wingfield B.D., Bills G.F., Dong Y., Huang W., Nel W.J.,
RA Swalarsk-Parry B.S., Vaghefi N., Wilken P.M., An Z., de Beer Z.W.,
RA De Vos L., Chen L., Duong T.A., Gao Y., Hammerbacher A., Kikkert J.R.,
RA Li Y., Li H., Li K., Li Q., Liu X., Ma X., Naidoo K., Pethybridge S.J.,
RA Sun J., Steenkamp E.T., van der Nest M.A., van Wyk S., Wingfield M.J.,
RA Xiong C., Yue Q., Zhang X.;
RT "IMA Genome-F 9: Draft genome sequence of Annulohypoxylon stygium,
RT Aspergillus mulundensis, Berkeleyomyces basicola (syn. Thielaviopsis
RT basicola), Ceratocystis smalleyi, two Cercospora beticola strains,
RT Coleophoma cylindrospora, Fusarium fracticaudum, Phialophora cf. hyalina,
RT and Morchella septimelata.";
RL IMA Fungus 9:199-223(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:RDW83927.1}.
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DR EMBL; PVWQ01000004; RDW83927.1; -; Genomic_DNA.
DR STRING; 1810919.A0A3D8SC55; -.
DR OrthoDB; 1118745at2759; -.
DR Proteomes; UP000256690; 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:UP000256690}.
FT DOMAIN 271..699
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 1051..1474
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT DOMAIN 1491..1523
FT /note="DAD"
FT /evidence="ECO:0000259|PROSITE:PS51231"
FT REGION 1..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 975..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1477..1496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1506..1701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1029
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1556..1582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1604..1625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1633..1689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1701 AA; 188889 MW; E483E7FDF5F6A416 CRC64;
MPTTDKSRQT SAGKSFFGRK LHKEKPAEDR YDSHGSWESL APPSSAAGSR SSRYSKRSSV
QSVDFGDIDP SYLSTSAGPI TSIPFESLST DTKTPISVDY LSKAETSPRK EPSPGHLAKG
VGDFHQYPAW DPANMRNNKQ YSQPTGPRPP PHGVAMSSSA TGDKGARYQQ WGRPGSSAGN
AGFSHHSSST VDSSTNSRMS IDQASVHSSL SSNTRGSSYI STDGSSRTVV PSPSTDRNNY
YGAVNSGRGS STQGAIPPAQ PRQQNTEQYL TRPRDDRIVD QLFLELMQKR GWQNLPEQAR
RQMMAYPASK KWTLVHQDRL TELQGEQKRK QKARETHGYD GPSGILERAD EEGSPEWYVK
KVMDDTITSK QLASLSVSLR TQPISWVKAF VEAQGQIALT NVLVKINRKK VTGPVPAPPS
GDKDLDREYD IVKCLKALMN NKYGADDALG HQQIIVALIS SLLSPRLNTR KLVSEVLTFL
CHWAEGQGHE RVLQAMDHVK NHQGETGRFD AWMRIVEVTI DGRGKMGSLV GASEEYRSGG
IGMENLLMEY AVSTMILINM LVDAPENDLQ LRCHIRAQFI SCGIKRLLSK MEGFQYEVID
KQIEHFRENE AIDYEDLLQR ESSSTKDSIE GDVKDMNDPL QITDAIATRI NGTRAHDYFL
SALQHLLLIR ENSGEDGLRM YQLVDAMLSY VAMDRRLPDL DLRQGLTFTV QSLLDRLHTD
AEARQAYDES LEARQIAEAA IAERDEMKAQ VELGADGLVK KLQKQIEEQT GIIELQSRQN
EMVKAELADV QRLRAQELQR NELETRELYL MLRDAQDIAA SNAKKSNIEE TETDPAHMRG
ILDRERLLGR LEKQLERTKT QFKLEGKVWG QHGPSDRLRE LREQMDGDAG FSEDFEEQAR
LNLSLNPVGS VYRKRTYIQG MEGTSTEEQC QTDDKVVYAT ARLVDLHRPR MDPDQATGLL
GEIAAKVPKI DADDAKIDSK PAEPGQPAEG FGGPPPPPPP PGGFGGPPPP PPPPGGAFGV
PPPPPPPGTV IGGWRANYLA SQGAPSHAIP VMSSIRPKKK LKALHWDKVD TPQVTVWATH
GTTPQEKEEK YVELAKRGVL DEVERLFMAK ETRIFGGGSA TKQRKDKKQI ISNDLSKNFQ
IALSKFSQFP ADDVVRRIIH CDTEILDNMV VMEFLQRDEM CTIPENVSKL MAPYSKDWTG
PDAASSQREQ DPGELTREDQ IYLYTAFELN HYWKARMRAL ALTRSFEPDY EHISAKLREV
VRVSESLRDS VSLMNVLGLI LDIGNFMNDA NKQAQGFKLS SLARLGMVKD DKNETTFADL
VERIVRNQYP EWEDFTEQIS GVIGLQKLNV DQLRTDAKKY IDNIKNVQAS LDAGNLSDPK
KFHPQDRVSQ ITQRSMKEAR RKAEQMQLYL GEMVKSYDDI MVFYGEDNTD DGARRDFFAK
LATFLQEWKK SKEKNIALEE VKRRTEASLA RKRINAGLAN GVGPGGDAPV SPASSGAMDS
LLEKLRAAAP QAKDQRDRRR RARLKERHQV RVASGQKIPD LEGAEAPGTA ADGDSGTADP
NASDSGLLSP PIQGSEGDIG SPNVSESEDV ADRAASMLQG LRDNPDPERT RRRRESAEEE
RRKRRLRRRN GATSGSKDST DTMPLSPVTE PTSTVGESAE PDSLALSSPP NGEEPSSNPP
TIVLSSNASE TPDDDHRPSP S
//
