ID U7PR67_SPOS1 Unreviewed; 1211 AA.
AC U7PR67;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein {ECO:0000256|RuleBase:RU369028};
GN ORFNames=HMPREF1624_04928 {ECO:0000313|EMBL:ERS98148.1};
OS Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERS98148.1, ECO:0000313|Proteomes:UP000018087};
RN [1] {ECO:0000313|Proteomes:UP000018087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58251 / de Perez 2211183
RC {ECO:0000313|Proteomes:UP000018087};
RX PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA Goldberg J., Young S., Zeng Q., Birren B.W.;
RT "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT 58251).";
RL Genome Announc. 2:E0044614-E0044614(2014).
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; KI440846; ERS98148.1; -; Genomic_DNA.
DR AlphaFoldDB; U7PR67; -.
DR STRING; 1391915.U7PR67; -.
DR eggNOG; KOG0521; Eukaryota.
DR HOGENOM; CLU_002728_0_0_1; -.
DR OrthoDB; 1449795at2759; -.
DR Proteomes; UP000018087; 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 GTPase activation {ECO:0000256|RuleBase:RU369028};
KW Metal-binding {ECO:0000256|RuleBase:RU369028};
KW Reference proteome {ECO:0000313|Proteomes:UP000018087};
KW Repeat {ECO:0000256|RuleBase:RU369028};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW Zinc {ECO:0000256|RuleBase:RU369028};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00288}.
FT DOMAIN 687..794
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 896..1020
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REGION 285..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1073..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1151..1211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..305
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1211 AA; 131024 MW; C40FED38DF5BF9EC CRC64;
MGITSSRPDE GGVLYLRDQN RLSISSLVIT SARRRTSVNI VPNAFPATRV SATRSLGDNA
PLDFVQDTDA SAAPGPSFLL KLSNDEELTF TFTFVIRQTP TSASTQGRQP APGAASAIDT
VINGLTFVQA SNLREVDNLL TREFHADPNL HKNSNVELVG DFSTGGSPSV TFDWSWRWKP
PKNLEDKGGG WRNSCSFVEY NQRAHSLNTL ASFSFFVSNT NPHPTPSSPT PPFLLSAPPK
IRVASAQSVD SRLSSTIEAI EDVPNSPRIG IPDPIGASGA TAAATLQAQP APTTAPPPPP
EPVKVDVSCP RPGDDVSVAD DGPLFRATIK ALEQKTGNMR MQMKKVIKRA EHAYATMVDS
NEAFSSFIDA LKETSSTNAN AVQPAIDHYF DKIAREILAY ERQNTFNLQR IVIDPLTKLY
TWDIKQAEAK KRDFEEESKD YYAYVGRYLG QRQDSLKSKK LAESDTKYQT KRRNFELKRF
DYSSFMQDLS GGRKEQEVLS HLTRYADGQA KSFLNTAKKV DVLLPQLEAL SNEVQLADKE
YQYQRREREE KRRLLEKSNG APSNAPYADS DTFSTAPTVN SNSVGVVNNG TNGGQSTTAT
IANNASSAQS NSDSELGRAD STGSQLRVGA APGTAGATTT DLSRSPGSLG SHHLSVGSPP
QNSKFKGIRD LEERDPAQTV NLEKNGNQRK EGLLWALNRP GGHVDPRSAL NKQGWHKFWI
VLDQGKLSEY SNWKQKLDLH MDPIDLRMAS VREARNAERR FTFEVITPQF KRVYQATSEE
DMNSWISSIN NALQSAMEGR ERSSAAPVVP TDNGSSNFPS RDIGSVFTNK STSLTHGHRG
RDGHGIGAVG GAVAQAMSGG SSSGSGNTGI PTRRITVGGR PSAPRAPSSS YEENPDKLLQ
MLRDNDRGNC WCADCGSGAK VEWVSINLAI ILCIECSGIH RSLGTHISKV RSLTLDITSF
TTDIIELLLL VGNRVANMVW EAKLEPAAKL TPTANREQRL RFITAKYVDR AYIEPISATL
SHYSTADETL LASVKKNDIQ HVIYALALKA NVNATDLSRG THVVYLALAA ADPASPSPTP
SPMTTPRPGT SGANAGPADP KSKQVPFPVA ELLLQNGAQI PAALPAFPLS RSAQQYVEAK
RGRVGGLNIL HNNSGNSGSK TGSGAVAGAH PSSTPSSGVG AMERLAREKE ARLQKRVSAG
GRLAKSPIPE R
//