ID A3GH21_PICST Unreviewed; 1119 AA.
AC A3GH21;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 2.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=GTPase-activating protein of the rho/rac family {ECO:0000313|EMBL:EAZ64017.2};
GN ORFNames=PICST_74324 {ECO:0000313|EMBL:EAZ64017.2};
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:EAZ64017.2, ECO:0000313|Proteomes:UP000002258};
RN [1] {ECO:0000313|EMBL:EAZ64017.2, 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).
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:EAZ64017.2}.
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DR EMBL; AAVQ01000001; EAZ64017.2; -; Genomic_DNA.
DR RefSeq; XP_001388040.2; XM_001388003.1.
DR AlphaFoldDB; A3GH21; -.
DR STRING; 322104.A3GH21; -.
DR GeneID; 4851570; -.
DR KEGG; pic:PICST_74324; -.
DR eggNOG; KOG1703; Eukaryota.
DR eggNOG; KOG2710; Eukaryota.
DR HOGENOM; CLU_001321_1_0_1; -.
DR InParanoid; A3GH21; -.
DR OMA; QCSAKFF; -.
DR OrthoDB; 1329523at2759; -.
DR Proteomes; UP000002258; Chromosome 1.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd09391; LIM1_Lrg1p_like; 1.
DR CDD; cd09392; LIM2_Lrg1p_like; 1.
DR CDD; cd09393; LIM3_Lrg1p_like; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 4.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR14963; RHO GTPASE ACTIVATING PROTEIN 18,19-RELATED; 1.
DR PANTHER; PTHR14963:SF1; RHO GTPASE-ACTIVATING PROTEIN CONUNDRUM; 1.
DR Pfam; PF00412; LIM; 3.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00132; LIM; 3.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 3.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW LIM domain {ECO:0000256|PROSITE-ProRule:PRU00125};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00125};
KW Reference proteome {ECO:0000313|Proteomes:UP000002258};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 17..82
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 85..145
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 439..503
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 831..1040
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1094..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1119 AA; 127509 MW; 7C694C6048D63D90 CRC64;
MPEISDQKRL TKRKSKKVCR KCGLDITGQF VRALHNAYHV ECFCCHECGN QCSAKFFPFD
VVDEATGVKT QVPLCEYDYF KKLDLICFTC HSALRGPYIT ALGNKYHLEH FKCAVCQKVF
ESDESYYEHE SNIYCHYHYS KLYASHCEGC HSSIVKQFVE LFRGGRNQQW HPECYMVHKF
WNVCIMADSV GLQSSFNVTE NEIANLREIE EKDDFGIDPK LLLSIEQQIE NVVMRCWLTL
SGYEETTATC ISDMLLNACT GNQRQGLLVT GKLILNVEVL FKALDCVLDL CDKSFPLVLD
AQKSKPQVGQ HADDSESSFN QLEEDFFQPL KKEPRNISGK IMSYLAILRK SNHIAQSGSL
SAELLSVITG CAHYLKLLIR IGLNNALKVN KLNGNTIASD KFLELTSSYE LYNKKSENSS
QDNTFSILSK LAIPPKSTDA CMSCTKSIEK SCIKFENKRW HPKCFNCSVC SRFISSEELP
DTKFHENGLE IICQLCSSPG EAKVGFEIVS DLSQLVYLLK IAHTRSKAVM KVDFRKQSQT
TVEQIQRPTE EAKRQHVAED NYSKTINDVT RMRTRRQSQK LSNSIKKNAR KSVIVEAPEA
NKAKQDDLAY SNLTDDNIAE ELADVSFENN RGADTQFSRS DRNFSASSQL SYVASQRENE
HFNVKKSLKI REEPQRQLTN THLDRTSDLL KNEKSLTLDD IPRIVAAEQA RDQRPNAFKH
HQTLYQKPNH LQNVRTSPNM ISPSSHLDSI LTTPVGQGHI EKKQKYYSEL TKEEHFIMRH
IAVEALGEVA GNKFNKDELL SLIQTKKSPT FWDKFKFGSD KKDKHLGVFG VDLQDLTKKY
GIDSDLGVGP SRLRIPIVVD DVISALKQKD MSVEGIFRLN GNIKKLRDLT EQINKSPLKS
PDFSIQTAVQ LAALMKKWLR ELPNPLLTYT LYDMWISSQS FENPVLRKRV LQLTYCMLPR
SHRNLLEVLL YFFSWVASFA EIDEETGSKM DIHNLATVIA PNILFSKQNS QADAQPQGGD
TYFLAIEVVN QLIDMHEELC VIPDDLLQFF DKCGFVSDNI TTKEIMNRVD KVLKENSKYF
QNFEIKNPEG ISNQEVRSNT ISRGQSKAIH ESHVEASDV
//
