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Database: UniProt
Entry: S9VY75_SCHCR
LinkDB: S9VY75_SCHCR
Original site: S9VY75_SCHCR 
ID   S9VY75_SCHCR            Unreviewed;       663 AA.
AC   S9VY75;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=RhoGAP {ECO:0000313|EMBL:EPY52593.1};
GN   ORFNames=SPOG_01915 {ECO:0000313|EMBL:EPY52593.1};
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:EPY52593.1, ECO:0000313|Proteomes:UP000015464};
RN   [1] {ECO:0000313|EMBL:EPY52593.1, 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; KE546989; EPY52593.1; -; Genomic_DNA.
DR   RefSeq; XP_013022473.1; XM_013167019.1.
DR   AlphaFoldDB; S9VY75; -.
DR   STRING; 653667.S9VY75; -.
DR   EnsemblFungi; EPY52593; EPY52593; SPOG_01915.
DR   GeneID; 25036239; -.
DR   eggNOG; ENOG502QQWB; Eukaryota.
DR   HOGENOM; CLU_416283_0_0_1; -.
DR   OMA; REDYFCE; -.
DR   OrthoDB; 1328399at2759; -.
DR   Proteomes; UP000015464; Unassembled WGS sequence.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProt.
DR   GO; GO:0032153; C:cell division site; IEA:UniProt.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR   PANTHER; PTHR23065:SF17; RHO-GTPASE-ACTIVATING PROTEIN RGD2; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000015464}.
FT   DOMAIN          421..614
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          151..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          632..663
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..178
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        632..653
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   663 AA;  75886 MW;  275B2FCC56FB8F34 CRC64;
     MTAMWDGFAD SFWTRDYITG VKSAQELINQ GIEQNKSLLS LLQAKSKALI ACSDILVKAC
     AKHDKQYPFS HDTNILLTSA AINELREDYF CEASLQKKWS EQLEYLVIGP FEKWNKNYAK
     RVGSLSSTIQ VKIENYNSRL LHVQRLKSSL LNPKQRGHRK SSSLSSINSR TQGSNKKLES
     EMPFILAGKN YSNDEFSKFL STLKKTMNKV SNSQPAEYVT HDVDFQKALS YTLPGSEKSK
     LEQMTDELAA LDMVNVKERT DKSVGTPNSN VQLTQKAINL INTNQEDSLD SSSFFSTQNE
     NKPVSFSNDL DKYYLAFSNL EQSRIELEQY LFTYYKELEK CEIDRLSAIE TILADHSGCF
     SSFTTRLESV VSNQTKTTRS LDKLQDLSNQ VKRYYTGYFT SVSNADLFLQ NGYESPIKSY
     SFLDTQISRV VPEVLMYLVD GYSYIKDFDA LYTIWTKEVP LKKAYELKSI LLNNAIIDVV
     PILEKYPLHT IAFSLKLCLL EFSDSLIRSS FYDYFNALYS TYTEDKDIEH RVYSIRQCLL
     HLHSTPLRLL EDLISHFKFF ADSAQFSRDD LYKIAKIIAP CILRPPKNVT RISVEDTHPV
     SLVLDLLQEF KQLFGNLERS VTPPIEMERA LTPINTSPTK LKSSRSSSPI KLPSPTKLFR
     PFS
//
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