ID A0A168FYM9_CORDF Unreviewed; 1736 AA.
AC A0A168FYM9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Cytokinesis protein sepA {ECO:0000313|EMBL:OAA75786.1};
GN ORFNames=LEL_07774 {ECO:0000313|EMBL:OAA75786.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA75786.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA75786.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA75786.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:OAA75786.1}.
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; AZHF01000005; OAA75786.1; -; Genomic_DNA.
DR STRING; 1081108.A0A168FYM9; -.
DR OrthoDB; 1118745at2759; -.
DR Proteomes; UP000076881; 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:UP000076881}.
FT DOMAIN 227..654
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 1111..1532
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT DOMAIN 1547..1579
FT /note="DAD"
FT /evidence="ECO:0000259|PROSITE:PS51231"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1514..1736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..879
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..919
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..951
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..969
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1060
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1096
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1514..1531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1540..1554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1656..1736
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1736 AA; 192943 MW; 7DF5B83A78F225CF CRC64;
MSDKTRQSSG GRSIFSRNKN KDKRATESES YDALSTMSSR SSRHNRDSSA ISIDGLPPPD
PSTSMMSSVI SSVPYDAIAP GSRSPIPVDY LPKADQVPVR REPLPHQLNK GHDFHQYPTF
DPSAGNAGSH TSRMGPPATN VTMASTGRTT QFQQWGPSRG SMVSTTNGSH TSRYDSLLSP
NNRISDASVF SVQPSASSLS SYGTPHRESH RLTKFPGPGA HDTFNFPKPD DDNVIEQMFA
HLMHRRGWHN LPEQARRQMM AYKPDKKWTL LHQDRLAEWQ GEQKRRMTAR VSQFAQPDVT
TYSDEEGTPE WYVRRVMEDK LDGKGMGSLE VNLRTQQIGW VRRFVECQGQ VALVTLLLKI
NRKIANAPAS ESSKVEKGLD REYDIIKCLK TLMNNKFGAD DALMQQKVLL ALGTSLVSPR
LTTRKLVSEI LTFLCTWGDN GEGHYKVIQA LDEVKAQTGA NGRFDEWMQL VEATVDGRGK
MGSMVGASDD IRTGGVGMEN LLMEYSVATI ILVNMMIDAP EKDLQLRVHI RAQFTGCGIK
RTLSKMEAFQ YELLDKQIER FRSNEAIDYE DMLERENSSI KDSIEGEVKD LSDPVQIADA
IQQRLRGSRT NDYFVSALQH LLLMRANDGE ERLRMFQLVD SMLSYVAMDR RLPNMDLKQS
LNFTVQSLLD KLHTDSEARQ AQDESLESRQ IAAAAMAERD EMRARLELGA DGLVAKLQKQ
VDEQSRFIDA QRRRTEGLKA ELEGVQTIRA KEAQRNELET RELYLMLRDA QDIAASNAAK
GAAATSAPAA VANGTNPEQM QGILDRQRLM ERLQMQLERQ KTQYKLEGRV WGEAAGPSDR
LRALREEMED EEAEAAPGAP RDFTNSVLGS INRQTRIPRK PVNANGEVSD RETIEEVSEM
EEEDGVVYER PRIVEYKRPV MDPRQQAVFV DELGNKLKKY DGSDDDDEGV TTGPSHPSLE
STSPQTPADG DTPKAGFTTP ATSAATPATG AAPPPPPPPP PPPMPGQIVG APPPPPPMPG
QTSGAPPPPP PPPPPPMPGQ ISGAPRPPPP PPPPPMPGMR SPAMGTDGTA SPGLPSSDSA
GSMPPPPPPM PGPKSGGFLP QPTYSATPSV GLPVARPKKK LKALHWEKVD APETSHWAAH
TPSAEAREEK YIELSRKGIL DEVEKLFMAK EIKKIGAATG RKDDKKQVIS ADLRKAYEIA
LAKFSQHSVE KIVQMIIHCD VQVLDNVVVM DFLQKDDLCN ISDNTSKQMA PYSRDLTGPD
AATQIREMDP ADLTRQDQIY LYTAFELHHY WKSRMRALAL TRNFEVEYEE IYEKMHQVIS
VSESLRDSVS LMNVLGLILD IGNYMNDANK QARGFKLSSL SRLGMVKDDK NESSLADLVE
RIVRGQYPEW ENFASEIGGV IPAQKMNVEQ LEADAKRYID NIRNVQMSLD SGNLSDPKKF
HPEDRVNLIV QRCMKDARRK AEQMQLYLDE MIRTFKDIMI FYGEDPADEN ARRDFFTKLA
NFLTEWKKSR EKNIQLEETR KRNEASMKRK HAAQKAAQAA SEPGSASATS TGAMDSLLEK
LRAAAPQARD QRDRRRRARL KDRHQVRVAS GQKIPDLNEI PEVEAVLKTS DQTIEEEENS
TAGPAGPASP DRTQSRDGDD DVADRAAALL QGMRGGDADD SEKRESLRKA RRQTAEEERR
MRRRRRDKAS VSNAEDVGKT ADGTEEDAST AGHDESARAS IAGRSEDGEA GEERTS
//
