ID A3M0P0_PICST Unreviewed; 644 AA.
AC A3M0P0;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 2.
DT 24-JAN-2024, entry version 77.
DE SubName: Full=GTPase activating protein (GAP) for RHO {ECO:0000313|EMBL:ABN68564.2};
GN Name=SAC7 {ECO:0000313|EMBL:ABN68564.2};
GN ORFNames=PICST_91378 {ECO:0000313|EMBL:ABN68564.2};
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN68564.2, ECO:0000313|Proteomes:UP000002258};
RN [1] {ECO:0000313|EMBL:ABN68564.2, ECO:0000313|Proteomes:UP000002258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC {ECO:0000313|Proteomes:UP000002258};
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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DR EMBL; CP000502; ABN68564.2; -; Genomic_DNA.
DR RefSeq; XP_001386593.2; XM_001386556.1.
DR AlphaFoldDB; A3M0P0; -.
DR STRING; 322104.A3M0P0; -.
DR GeneID; 4841110; -.
DR KEGG; pic:PICST_91378; -.
DR eggNOG; KOG2710; Eukaryota.
DR HOGENOM; CLU_016108_1_0_1; -.
DR InParanoid; A3M0P0; -.
DR OMA; MDPIEYA; -.
DR OrthoDB; 25175at2759; -.
DR Proteomes; UP000002258; Chromosome 8.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd04396; RhoGAP_fSAC7_BAG7; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR15228; SPERMATHECAL PHYSIOLOGY VARIANT; 1.
DR PANTHER; PTHR15228:SF25; SPERMATHECAL PHYSIOLOGY VARIANT; 1.
DR Pfam; PF00620; RhoGAP; 2.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000002258}.
FT DOMAIN 138..461
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 29..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 369..396
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 61..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 644 AA; 70409 MW; EB45F4A1C618F85A CRC64;
MSHSSSPNSK PSIFGWVKNL KRGNLLSSDS VNDITSDNEN LQSVDSRSPT KAKNIALSLS
QSQSSSILPT SQASPPNAGH QDFLRPLLHQ KSRSTNNVNR VRSNSLNQSE KSSSLRQHRD
SFLQHNPLVD ENSKYFGVPL EVAIREASAK ISILNPDPSD HGLQYGEIPI VVAKCGVFLK
NNGLTVEGIF RVGGSSKRLK ELQHIFNTPP IYGKKLKWDG YTVHDAASIL RRYLNALPEP
LIPLGLYESF RDPLRKRTRI INYMKYKAEN PSKTSKSALS SSTALPVETE STSSQLTEAN
IDRLNETGST VTAAAAASHP TITVVSESQQ QNPGEEQSTG EINAAIMEGS SSQLTEEEQR
KSLKKSKNYK KLTRDVHEAI EEYKQLLDEL PTASRQLLFY ILDLLAMVQN HSGENLMSSR
NLAAIFQPSI LSHPNHDLDP EEYALSQSVV EFLVQYAYKL LPQQSPPSGK IVPAGEAAEQ
ATEDPNAHID ANSNGNTGVV APAPLKSEDS HSSVTSTSTT PIEETGLLSK PTSAKFKRQH
SKSLPSADDV DNDLVGYHNS VKSKNSIPVI DSDNDFEITD DEIEGDNSEE DLHLRLNNGS
VQSQDQVQHH NTLPIETSSS SVAIIVSTPS SKVVPVLVKD SSTQ
//
