ID W8B4M6_CERCA Unreviewed; 1058 AA.
AC W8B4M6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 13-SEP-2023, entry version 49.
DE SubName: Full=Centaurin-gamma-1A {ECO:0000313|EMBL:JAB88246.1};
DE Flags: Fragment;
GN Name=CEG1A {ECO:0000313|EMBL:JAB88246.1};
OS Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC Tephritidae; Ceratitis; Ceratitis.
OX NCBI_TaxID=7213 {ECO:0000313|EMBL:JAB88246.1};
RN [1] {ECO:0000313|EMBL:JAB88246.1}
RP NUCLEOTIDE SEQUENCE.
RA Geib S.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAB88246.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24495485; DOI=10.1186/1471-2164-15-98;
RA Calla B., Hall B., Hou S., Geib S.M.;
RT "A genomic perspective to assessing quality of mass-reared SIT flies used
RT in Mediterranean fruit fly (Ceratitis capitata) eradication in
RT California.";
RL BMC Genomics 15:98-98(2014).
CC -!- SIMILARITY: Belongs to the centaurin gamma-like family.
CC {ECO:0000256|ARBA:ARBA00005430}.
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DR EMBL; GAMC01018313; JAB88242.1; -; mRNA.
DR EMBL; GAMC01018310; JAB88245.1; -; mRNA.
DR EMBL; GAMC01018309; JAB88246.1; -; mRNA.
DR AlphaFoldDB; W8B4M6; -.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd08836; ArfGap_AGAP; 1.
DR CDD; cd04103; Centaurin_gamma; 1.
DR CDD; cd01250; PH_AGAP; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001806; Small_GTPase.
DR PANTHER; PTHR45819; CENTAURIN-GAMMA-1A; 1.
DR PANTHER; PTHR45819:SF5; CENTAURIN-GAMMA-1A; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00173; RAS; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS51419; RAB; 1.
DR PROSITE; PS51421; RAS; 1.
PE 2: Evidence at transcript level;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00288}.
FT DOMAIN 465..705
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 702..845
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REPEAT 885..917
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 245..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:JAB88246.1"
SQ SEQUENCE 1058 AA; 115726 MW; 9B617922F980E7B6 CRC64;
QQQQQHAQPQ PLISNSLAIR QEIQRFESVH PSIYAIYDLI DLLPIADAQI AQQIRDHVVC
IEDSFVNSQE WTISRSVPDL RLGIVGALNS GKSALVHRYL TGSYMQEESP EGGRFKKEVF
IDGQSYLLLI RDEGGPPEMQ FAAWVDAVIF VFSLENESSF NTIYNYYNKM AHFRNGQDLP
MILVGTQDAI SERNPRVIDD SRARKLANDL KRCSYYETCA TYGLNVERVF QDACQKILQQ
RIPLPPTVNS RPTTPQGTRL GIASYHHNSN NHSGANANGF SASTSSVQGA VSTSNLTLPH
RHHALSTSSH HIPMRMSADF MQSEQQQSLP PSQRSWQQQK EQQQQRDREL SMLTNENNNI
TKFTPTHHQH QQQQQQIQSQ SQQSIHHQTA ESLPPLSLVP LRENKDNGSG GGGGGSGGGK
DLPTPTSTPT TSRKSRRRSN LFIPSSSKKG EKDLKNGELG SGRSIPIKQG YLYKRSSKSL
NKEWKKKYVT LCDDGRLTYH PSLHDYMDDV HGKEIPLQYV TVKVPGQKPR GSKSIITNSA
LTTSMHSNGR NHGQNGLSEG IGCLSIVKDN KDKKMTEKVL LTAFDTLREP VKSNSSQQTS
GDEGIAMSNS NSQTFIAGSD SQQQLQQQQR ELLAVNAANK LESQTPNVKK RHRRMKSSSV
KSNEVDDSDI YEFFIVSLDS KQWHFEAASS EDRDEWVAAI EQEIFKSLQG IESTKTKPAT
TSELASMVAI RTRVPGNGYC VDCDAPNPEW ASLNLGVLMC IECSGIHRNL GSHISKVRSL
GLDDWPAGHL SVMLAIGNSL ANSVWEANTR QRTKPKPNST REEKETWIRS KYEAKEFLAQ
SNANTNTTPG QQLIEAVIRS DIKSIVLILA NANSEVTNAN VSPRDVRTPL LLACAIGNLA
IAQLLIWNGA NIKHTDHEGR TCLAYARAAQ SLATAKSMKA AAAAAAASAN TTNGCNTNTN
SSTASNTSSC SSTASNTATT TTTSNATNSA SVSGAAASAV TNGGIPAPQY SVEETTALVD
LLTSLGCPES APLTASGTLP RRRDTLGTPY EKTVSGVI
//
