ID S9W4M3_SCHCR Unreviewed; 322 AA.
AC S9W4M3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=GTPase activating protein {ECO:0000313|EMBL:EPY53469.1};
GN ORFNames=SPOG_04529 {ECO:0000313|EMBL:EPY53469.1};
OS Schizosaccharomyces cryophilus (strain OY26 / ATCC MYA-4695 / CBS 11777 /
OS NBRC 106824 / NRRL Y48691) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=653667 {ECO:0000313|EMBL:EPY53469.1, ECO:0000313|Proteomes:UP000015464};
RN [1] {ECO:0000313|EMBL:EPY53469.1, ECO:0000313|Proteomes:UP000015464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OY26 / ATCC MYA-4695 / CBS 11777 / NBRC 106824 / NRRL Y48691
RC {ECO:0000313|Proteomes:UP000015464};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
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DR EMBL; KE546988; EPY53469.1; -; Genomic_DNA.
DR RefSeq; XP_013021982.1; XM_013166528.1.
DR AlphaFoldDB; S9W4M3; -.
DR STRING; 653667.S9W4M3; -.
DR EnsemblFungi; EPY53469; EPY53469; SPOG_04529.
DR GeneID; 25038842; -.
DR eggNOG; KOG0703; Eukaryota.
DR HOGENOM; CLU_023062_3_1_1; -.
DR OMA; CIKCAGV; -.
DR OrthoDB; 1022106at2759; -.
DR Proteomes; UP000015464; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd08839; ArfGap_SMAP; 1.
DR Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR044732; ArfGAP_SMAP1-like.
DR PANTHER; PTHR45705; FI20236P1; 1.
DR PANTHER; PTHR45705:SF1; FI20236P1; 1.
DR Pfam; PF01412; ArfGap; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR PROSITE; PS50115; ARFGAP; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00288};
KW Reference proteome {ECO:0000313|Proteomes:UP000015464};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00288};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00288}.
FT DOMAIN 11..128
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REGION 134..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 322 AA; 35536 MW; 9B45814F83C5C41A CRC64;
MSLGKKKETN AIALKSLLRE PANKICADCK RNEQPRWASW SLGVFICIRC SGIHRSLGVH
ISRVKSVDLD AWTDEQTENM QRWGNQRANM YWEANLTDGH IPSDSKVATF IRTKYELRKW
VLSREIPSPE TLIPFEKMNP SISSPEPIAP GKPAAASMPS ISKEPLRSQS EASMIDIASM
NTSENYRLPN PGASSTASTP NLTSLSSNNT STAQANRQKD LKSSILSLYA SPRPMSAVNS
PVSSFSNIPS TSTSTVQGAQ QYASLQSPVS SASFVADKWK MPLFGSTNPY SYAREPGMQP
QPPRRTQSAM DHNIMNTHDV WK
//
