ID K0KM03_WICCF Unreviewed; 1188 AA.
AC K0KM03;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein {ECO:0000256|RuleBase:RU369028};
GN ORFNames=BN7_1703 {ECO:0000313|EMBL:CCH42158.1};
OS Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM
OS 3599 / NBRC 0793 / NRRL Y-1031 F-60-10) (Yeast) (Pichia ciferrii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX NCBI_TaxID=1206466 {ECO:0000313|EMBL:CCH42158.1, ECO:0000313|Proteomes:UP000009328};
RN [1] {ECO:0000313|EMBL:CCH42158.1, ECO:0000313|Proteomes:UP000009328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL
RC Y-1031 F-60-10 {ECO:0000313|Proteomes:UP000009328};
RX PubMed=23193139; DOI=10.1128/EC.00258-12;
RA Schneider J., Andrea H., Blom J., Jaenicke S., Ruckert C., Schorsch C.,
RA Szczepanowski R., Farwick M., Goesmann A., Puhler A., Schaffer S.,
RA Tauch A., Kohler T., Brinkrolf K.;
RT "Draft genome sequence of Wickerhamomyces ciferrii NRRL Y-1031 F-60-10.";
RL Eukaryot. Cell 11:1582-1583(2012).
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:CCH42158.1}.
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DR EMBL; CAIF01000039; CCH42158.1; -; Genomic_DNA.
DR AlphaFoldDB; K0KM03; -.
DR STRING; 1206466.K0KM03; -.
DR eggNOG; ENOG502QU87; Eukaryota.
DR HOGENOM; CLU_001720_0_0_1; -.
DR InParanoid; K0KM03; -.
DR Proteomes; UP000009328; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR CDD; cd13280; PH_SIP3; 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; IPR004148; BAR_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR042067; Sip3_PH.
DR InterPro; IPR031968; VASt.
DR PANTHER; PTHR23180:SF160; ADP-RIBOSYLATION FACTOR GTPASE-ACTIVATING PROTEIN EFFECTOR PROTEIN 1; 1.
DR PANTHER; PTHR23180; CENTAURIN/ARF; 1.
DR Pfam; PF16746; BAR_3; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF16016; VASt; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS51778; VAST; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU369028};
KW Reference proteome {ECO:0000313|Proteomes:UP000009328};
KW Repeat {ECO:0000256|RuleBase:RU369028};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|RuleBase:RU369028};
KW Zinc-finger {ECO:0000256|RuleBase:RU369028}.
FT TRANSMEM 993..1012
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1024..1041
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 317..418
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 773..948
FT /note="VASt"
FT /evidence="ECO:0000259|PROSITE:PS51778"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1188 AA; 136292 MW; 0B2CF788CE16A922 CRC64;
MSNGARVQIR EQSHEQKDKL HRDAAEKAKL NINPKLVKLI SVKLKEAALD SPSFRASVNY
FNSQVDQTEH WIEGLLKSLK KYPQQFNDFK EVNNVLFNQL IPDFLKDGLI NQDNSVAILD
TSKTNLGSLW ESNTKALELK EAEITELLSE FSKNEIRHFK DFKKNFEFFQ NKFDTLISKY
SSQNKSKDPS ALREDAFQLY EVRKSYLAAS LDICVEISKL HQQLDFTFVN LAELLFKGKV
SFDEKYFEKA RAWSVAVSKS VKTLIDDMIY SRNQIEEATI SQFTPSRDLA SHNPALINPQ
TLINEETEPN NNNNQQSFEK HGWLFMKTTV GKPARTIWVR RWVFVKSGIF GLFSLAPSKN
FVQETDKIGV LLSNIRYAPD EDRRFCFEIK TIDVTIMFQA ESLEELKSWL TVFSMEKKRA
IENSDSDSGK YAFGRYPPLL YEFASTSLTS IDMELTTSKA ENTKDDDTQT TVVSSFLSQL
VGGKEHLDFR LSGTVGDFQE PDISAPMITK MTKLSILAHA FLNSTIIPTA VTANIWGSVN
WGTYYVSDHD ISYKLNQPVS DSNISSLSKT HKYPDFYPQD LKTYDIQLKS LFDTSVPKDE
LVVLHFSCLW ALNPKQELSG RCFVTTENCY FYLNSTGFVA LLKKSIADLV AVDVTNEKDW
EVLKVYGIEG LNMKGRIFLD DGKLIQKKLD FLINNLSKDE PKLQNEVIQI LKQIETDEIK
KIEKKNSIKR KNTDASVQST SGSTQINSEL YSFQPFSGVV SHNKNMKTNY NDEYHQCTVR
TFDAPAKAIF HILFGDHSSI LRDSIRFIDN DEYEVSPWYS KGSELIREIE LKLKLSKKLF
SLKNNNAGES VVQQTIEDFV DMKYYRIRED RTPLKIAMGQ VLQLTKKYVI IETDTKTSKL
YIYTKLDSID PGVRSLFAPA LRKTSKSFFK DEDLTMIEQI EHNVSRLGSH GKIIKAIRTF
GNLSKSDEVY IPKERQVFNF TLNLMFRLYF KKFWYDLASA ILCGSKLIFS YLGKILGELA
MNKLILLLLG ISLLFNSFLV GKSTVSFWTA KKAEHLVKDF TKELNMNKME RAIYINEIDA
LSSSNFNESS ICFTKFMNSG NIEDYASQSV DKRFRNSRHE IAVKRNELLV ELKILEKVEK
ELINGSWKNF LLSELNLCKK ALEDLNVTNP DLEIYCSSCI EDFQKVSA
//