ID W1Q7H6_OGAPD Unreviewed; 795 AA.
AC W1Q7H6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein {ECO:0000256|RuleBase:RU369028};
GN ORFNames=HPODL_02949 {ECO:0000313|EMBL:ESW96323.1};
OS Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL
OS Y-7560 / DL-1) (Yeast) (Hansenula polymorpha).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea.
OX NCBI_TaxID=871575 {ECO:0000313|EMBL:ESW96323.1, ECO:0000313|Proteomes:UP000008673};
RN [1] {ECO:0000313|EMBL:ESW96323.1, ECO:0000313|Proteomes:UP000008673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC {ECO:0000313|Proteomes:UP000008673};
RX PubMed=24279325; DOI=10.1186/1471-2164-14-837;
RA Ravin N.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V., Schneider J.,
RA Mardanova E.S., Smekalova E.M., Zvereva M.I., Dontsova O.A., Mardanov A.V.,
RA Skryabin K.G.;
RT "Genome sequence and analysis of methylotrophic yeast Hansenula polymorpha
RT DL1.";
RL BMC Genomics 14:837-837(2013).
RN [2] {ECO:0000313|Proteomes:UP000008673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC {ECO:0000313|Proteomes:UP000008673};
RA Ravin N.V., Mardanov A.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V.,
RA Zvereva M.I., Smekalova E.M., Dontsova O.A., Skryabin K.G.;
RT "Genome sequence of the methylotrophic yeast Hansenula polymorpha DL1.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: GTPase-activating protein for the ADP ribosylation factor
CC family. {ECO:0000256|RuleBase:RU369028}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU369028}.
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:ESW96323.1}.
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DR EMBL; AEOI02000010; ESW96323.1; -; Genomic_DNA.
DR RefSeq; XP_013932753.1; XM_014077278.1.
DR AlphaFoldDB; W1Q7H6; -.
DR STRING; 871575.W1Q7H6; -.
DR GeneID; 25772396; -.
DR KEGG; opa:HPODL_02949; -.
DR eggNOG; KOG0521; Eukaryota.
DR HOGENOM; CLU_325422_0_0_1; -.
DR OMA; GWHKQWV; -.
DR OrthoDB; 1449795at2759; -.
DR Proteomes; UP000008673; Chromosome VII.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd08204; ArfGap; 1.
DR CDD; cd00821; PH; 1.
DR Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR045258; ACAP1/2/3-like.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR23180:SF160; ADP-RIBOSYLATION FACTOR GTPASE-ACTIVATING PROTEIN EFFECTOR PROTEIN 1; 1.
DR PANTHER; PTHR23180; CENTAURIN/ARF; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|RuleBase:RU369028};
KW Cytoplasm {ECO:0000256|RuleBase:RU369028};
KW GTPase activation {ECO:0000256|RuleBase:RU369028};
KW Metal-binding {ECO:0000256|RuleBase:RU369028};
KW Reference proteome {ECO:0000313|Proteomes:UP000008673};
KW Repeat {ECO:0000256|RuleBase:RU369028};
KW Zinc {ECO:0000256|RuleBase:RU369028};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00288}.
FT DOMAIN 379..477
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 529..651
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REGION 501..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 795 AA; 89883 MW; C82240022257902C CRC64;
MDVFVSILLS DVQVNRGSSK LTKVTFKTQT QQAVEIDLVA KKISQTTPME FIQDRSKLLL
KLPSSFSIVE AKFVKGSNLY LIESIDADNK AMKHPIEADS TQMTIQLSSK LNGKFTLQLK
EGSQTLSKLS VYFYSDTSSS GPSQKTEIIH PANLTDHSGN PFPISLEDGP VFRETLNDYE
TKITKLKQAI RSTNDLLINY ESLSNQLYNS RASLIKSFSV IESTFPTFYY CEFDKSIVYS
FENLTDENKS AIRQLKSRLS STNKLSGLES YLASKKRVFE DESKKYYDWL SRLLSSGKSK
DDKLLQKRKS FELAKIDYFV FLFDTLVDLV LDFCNPQNPF INAYSSSKSQ RQKIRAAVER
ASSMAELNAE LSKIHGIAGP NKSGILFTQG GQGKSGWHKQ WVVLNNGKLS EFMDWRKGTS
RRNEPIDISL SSIKPLDMEK RKNCFRVITS TGIEHYFQAT SEEDRDSWIQ ALYDAGQQIN
FHKSRGDLAG DPLFVNAKKT REIQSSSNDS KKESLQNDGR QRRVSSVSLE NLRMVQKADS
SNTRCSECGS TESVEWISMN LLVIFCVKCS SCHRSLGTSI SKVRSLKLDV FTQEGYKLLQ
YINNKSSNAI YEELLPKESH ISPDSNDKDR LRFITNKYAA KQYVNQKDAS KASEFLIHGV
RTHNIPEISK SFALGVDRDL KLYKPTDQLT NLEPPAFSVL EYALNYPSLE GKDKSIKVFD
LAEYLILNGT KCGDKVQNVI GLSPEALDYW QSKIDRFKGN STKTPTTQLL SQTAAAPKST
PKEHKFNLLK KKMKN
//
