ID A0A1V9X5R8_9ACAR Unreviewed; 1613 AA.
AC A0A1V9X5R8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 08-NOV-2023, entry version 22.
DE SubName: Full=GTPase-activating protein and VPS9 domain-containing protein 1-like {ECO:0000313|EMBL:OQR68766.1};
GN ORFNames=BIW11_12694 {ECO:0000313|EMBL:OQR68766.1};
OS Tropilaelaps mercedesae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Mesostigmata; Gamasina; Dermanyssoidea; Laelapidae;
OC Tropilaelaps.
OX NCBI_TaxID=418985 {ECO:0000313|EMBL:OQR68766.1, ECO:0000313|Proteomes:UP000192247};
RN [1] {ECO:0000313|EMBL:OQR68766.1, ECO:0000313|Proteomes:UP000192247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wuxi-XJTLU {ECO:0000313|EMBL:OQR68766.1};
RX PubMed=28327890; DOI=10.1093/gigascience/gix008;
RA Dong X., Armstrong S.D., Xia D., Makepeace B.L., Darby A.C., Kadowaki T.;
RT "Draft genome of the honey bee ectoparasitic mite, Tropilaelaps mercedesae,
RT is shaped by the parasitic life history.";
RL Gigascience 6:1-17(2017).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the GAPVD1 family.
CC {ECO:0000256|ARBA:ARBA00008489}.
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:OQR68766.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MNPL01023343; OQR68766.1; -; Genomic_DNA.
DR STRING; 418985.A0A1V9X5R8; -.
DR InParanoid; A0A1V9X5R8; -.
DR OrthoDB; 20678at2759; -.
DR Proteomes; UP000192247; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.246.120; -; 1.
DR Gene3D; 1.20.1050.80; VPS9 domain; 1.
DR InterPro; IPR041545; DUF5601.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR003123; VPS9.
DR InterPro; IPR045046; Vps9-like.
DR InterPro; IPR037191; VPS9_dom_sf.
DR PANTHER; PTHR23101:SF25; GTPASE-ACTIVATING PROTEIN AND VPS9 DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR23101; RAB GDP/GTP EXCHANGE FACTOR; 1.
DR Pfam; PF18151; DUF5601; 1.
DR Pfam; PF00616; RasGAP; 1.
DR Pfam; PF02204; VPS9; 1.
DR SMART; SM00167; VPS9; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF109993; VPS9 domain; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR PROSITE; PS51205; VPS9; 1.
PE 3: Inferred from homology;
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000192247}.
FT DOMAIN 147..357
FT /note="Ras-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50018"
FT DOMAIN 1454..1613
FT /note="VPS9"
FT /evidence="ECO:0000259|PROSITE:PS51205"
FT REGION 400..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1067..1086
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..698
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1613 AA; 176523 MW; 07DC43AB54A4C2FE CRC64;
MARVACRELL ELVHSLRQEQ LFVSAEKRKI LALNDEVRRC SDRLFERAWT TRHQRVNLDR
YILSLQDILS AHRKALQLDN VHFVDSYKWL GNADPPVCEL IKALRENPKL LALFLDRCEQ
VKISASILQS LICAVMISLY GACLLPEDNN YALVLLYELM HLQLPRTEQL RRLLQYGSCA
FSRCYKAFVE AHLPAKLFLT SALRNAIIQV LVNDDLYLDI EPNDAAARFV PEERVRHFGS
EGTPQYESTL RTYRLWSIRK LTGLVQLFLD GISESMFCFP PALAWLVRQF YGIILDENKI
EPRQIAVICA DLVFYFFICP AICNPELYGV IEEGLHIGQC ARFNLMQVAR IIQALSMARY
EPIDTRLEEV YRHFDKELLP NILEEIIRGN QQPDLLSDLL NGSAVTTDPS TSSQDNGPLT
RNAVLISPAE LHYLVSTVHQ ILDLESDGSL LHEWLQPLME HVPTELPLNT HGMNNLNGHS
SEDGTLKTAL MTKVNKMRNS GGRNLHHGGN LDSSVETVDE LLANHAGAII TEVLVVPLPS
SGRREFPGAM PEEKVLTLEQ NKRSATKVRL NLDNLEEKSS TGSGKRTRFF GDQESIAGAS
DNMEAGLSEA ASVASSLDLE ENADNLSDMV SANVSGPGTP SVSGRDTPSS HGAAPVPPHP
AQIAEQLQML QGGANQPEQP QLPAQAQLPP PANIPSRRRG PPRPEAQKQM DIEDRFGRFG
ISNGSAMGSS VVEEETKSMV SDTWSTDVLG SDSEAHYGSG AAGVAASAQE QQLHIESHLN
AMQQHIHGHL SQHNVHVLQQ QQQQQLIEFS ETQSDAWSTA AMTSYSDLDR LQEVDPEDDL
MMLMPSERRR SAEDVGAAMD VGAGEAAGGV GGAAMFAGRG MASVNGRQNP DRQSTPTNLI
KLNSVENNEP PPLIDIGDGG PSIRMRGGNL QQQAISGASA DTPLVEIDPP QQEEMLPGAF
AHSLSNGSVS SFGSSTPFAS VIECAGQGSQ SLGRLSFAMK EHSPSRENLL ERDLTQFSNG
SIVDNARNSG ATAAGVVKPQ GSADSSDGNS ESSSDLLAGV VAAGSGGVAG RSSCPGSAGD
DSERQVQMRS GAIPKTPRIH LQQQQSSGPG DRTSGGSSNG RHSRQSGSGA QRGFLRKIGT
IRQSISSRVK TLDRNSVSRR GLATPDGENG SGVHDETGAL GGAGHQIVGT LSTPTVQFMD
PSEILEKYRG KNRGDAEALA SGLMADNASS VSGGDLIELD ESEASELSPE EVAFLDAKRK
LRTVFATANT QTLHLDRSRI ELLLLLKMML AESIGLQNHQ LTAQLHEAIR CVSKLDASMQ
RSAYISYLVR ARQGLETTLA GLQTLLAHVK KDKNVSHGYL TTQCVLEFLQ IIRRKDVSLN
LDGLVAEFKD LDVSDEKAVL VEKYLERVFK EMGSHALWYG SSEEYLALSE STVERLIMGK
LYVHALFPNG DIDLHRDQVL TVHIKKLAQI ITPQHRALRI PRGYLLECPW PSAQAAIATL
NAYKRIRYNG LVDLFDLRIA EMNLQAPRDK LSCVFLCCKT ILDLLHLASN SAAAADDLFP
ILVYVLIQAN PQYLLSNIEY VKHFCPGYQE GEAGYYWTML DSAVVFIKSL EYN
//
