ID A0A0J8UWK1_COCIT Unreviewed; 962 AA.
AC A0A0J8UWK1;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein {ECO:0000256|RuleBase:RU369028};
GN ORFNames=CIHG_09987 {ECO:0000313|EMBL:KMU92303.1};
OS Coccidioides immitis H538.4.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=396776 {ECO:0000313|EMBL:KMU92303.1, ECO:0000313|Proteomes:UP000054563};
RN [1] {ECO:0000313|Proteomes:UP000054563}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H538.4 {ECO:0000313|Proteomes:UP000054563};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
CC -!- FUNCTION: GTPase-activating protein for the ADP ribosylation factor
CC family. {ECO:0000256|RuleBase:RU369028}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU369028}.
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DR EMBL; DS017063; KMU92303.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J8UWK1; -.
DR STRING; 396776.A0A0J8UWK1; -.
DR VEuPathDB; FungiDB:CIHG_09987; -.
DR eggNOG; KOG0521; Eukaryota.
DR Proteomes; UP000054563; Unassembled WGS sequence.
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; cd07608; BAR_ArfGAP_fungi; 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; IPR004148; BAR_dom.
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; PF16746; BAR_3; 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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW GTPase activation {ECO:0000256|RuleBase:RU369028};
KW Metal-binding {ECO:0000256|RuleBase:RU369028};
KW Reference proteome {ECO:0000313|Proteomes:UP000054563};
KW Repeat {ECO:0000256|RuleBase:RU369028};
KW Transferase {ECO:0000256|ARBA:ARBA00022676};
KW Zinc {ECO:0000256|RuleBase:RU369028};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00288}.
FT DOMAIN 540..590
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 654..778
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REGION 592..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 962 AA; 106272 MW; B2889D59CB2C718D CRC64;
MGNISSRPDD PAALYLKDQT KLTIASLTIT NYRGHAILHI GPNGFPATRV TAKRDTGDDT
PIEFVLDPDS TTTSQPSFLL RLSNEDELTF KFSFIIRQTQ IPPVTTSTIN GVASTLPEAI
DTTLKGVTFA HASNSKELDN LITREFHANP NLQNNSNVQH VGTFSTEGSP SIQFDWSWKW
KPPKRAEDRG GGWRNCCSFL DYDERTNRLN TLATFTFWVQ NATRPLSSPV VLSPRLELAV
PPRNRTVSSQ SVMSKGSELE ALGDVPQSPI ETESLLGGAA PAVPVKLDIC QRPGEDMSAV
EDGPLFRATM KALEQKTGNM RTKMKKLLKK AEAVHQRQVA YNESVSAFII ALNEASTSNA
NAIQPALEHY FDKIAKEILI WEQQNSTNLQ KLIIDPLTRL YNNDIKQAES KKKDFEDESR
DYYAYVGRYL GQRQDSLKEK KRAESDSKYQ TKRRNFELKR FDYSSFMQDL HGGRKEQEVL
SHLTNTLSPS TPQRFTALDK RSTLALPPPP LCWFWIVLDQ GKLSEYSNWK QKLDLHMDPI
DLRMASVREA RNAERRFCFE VITPQFKRIY QATSEEDMGN WITAINNALQ SAVESGRGVP
PPPTSEGGSR KDIGSALMGK TTSSSNTSNV SRRTTVGARP SYVRNDSSYE DNPSKLLQVI
READQGNNWC ADCNSASKVE WVSINLGIVL CIECSGIHRS LGTHISKIRS LTLDIHSFSN
DIVEILLQIG NRVSNMIWEA TLNPTHKPTA QSSRDQRLKF ITAKYSERAF VRPLSSTLSR
YGTADETLLA SIKQNDIQGV LYGIALRASP NATDRSRNTH AVFLALAAAD PASPSQSMTS
ISTWTKSAPQ PPTGIKAIPF PIAELLVQNG ADIPAEMPAI PLSPAAQLYV NQRTGRALGS
GNPTASSGGD TLSALPTIRD FGSGGDGLMP SPAEMNNKER ERLHKRGSAG ARFAGKVTSF
GS
//
