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Database: UniProt
Entry: A0A016SYG1_9BILA
LinkDB: A0A016SYG1_9BILA
Original site: A0A016SYG1_9BILA 
ID   A0A016SYG1_9BILA        Unreviewed;      1103 AA.
AC   A0A016SYG1;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=RhoGAP domain protein {ECO:0008006|Google:ProtNLM};
GN   Name=Acey_s0160.g3321 {ECO:0000313|EMBL:EYB95369.1};
GN   Synonyms=Acey-gei-1 {ECO:0000313|EMBL:EYB95369.1};
GN   ORFNames=Y032_0160g3321 {ECO:0000313|EMBL:EYB95369.1};
OS   Ancylostoma ceylanicum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB95369.1, ECO:0000313|Proteomes:UP000024635};
RN   [1] {ECO:0000313|Proteomes:UP000024635}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX   PubMed=25730766; DOI=10.1038/ng.3237;
RA   Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA   Aroian R.V.;
RT   "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT   ceylanicum identify infection-specific gene families.";
RL   Nat. Genet. 47:416-422(2015).
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:EYB95369.1}.
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DR   EMBL; JARK01001496; EYB95369.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A016SYG1; -.
DR   Proteomes; UP000024635; Unassembled WGS sequence.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 1.10.287.2070; -; 1.
DR   Gene3D; 3.30.530.20; -; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR023393; START-like_dom_sf.
DR   InterPro; IPR002913; START_lipid-bd_dom.
DR   PANTHER; PTHR12659:SF7; CROSSVEINLESS C, ISOFORM C; 1.
DR   PANTHER; PTHR12659; RHO-TYPE GTPASE ACTIVATING PROTEIN; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF01852; START; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00234; START; 1.
DR   SUPFAM; SSF55961; Bet v1-like; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50848; START; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000024635}.
FT   DOMAIN          652..865
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   DOMAIN          898..1099
FT                   /note="START"
FT                   /evidence="ECO:0000259|PROSITE:PS50848"
FT   REGION          127..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          262..370
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          436..515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..173
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..188
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..224
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..308
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..368
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        444..469
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..515
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1103 AA;  124242 MW;  4808DF612854B239 CRC64;
     MQLIDSVLIS EEDALECCHW LRQAGFPQYA KQYQEGRFPI DIRSVQSDHE FLGPDSLRAL
     YRRLNTLNRC AIMRIDQVVL RRRNDDYSYG MYDGFDDDDS IALSGNWRYQ RHSHTWSRVG
     NEQMYGVPGR TVCPKPNWDS YRDQLDPRSR YDVREMRDPY AGKRSDRQLE RYTESPDCNG
     NSASNKLQRS HSERIKERAR AIMKKMDLRS SSRRRKDSRH RDPNAMVIGD PVLVSYDSAS
     PETMRMMPRP NNLDARSARV TNATTANVAS DRHSRSKSAR RQGMVVLSPS SPDSSDDSFL
     SSTHRRPTGS SAHARRDRSV PPQLVDTTEY DYAPQDRLRR ERMPPYETYL YPTSPNSLTR
     TTAPPRPSRR ALQQAVSAAA AAGGYDASSG GSPYYGSGGY SSSPAYSSPY STRSYQSPPV
     VARNLVIQPD GYFMHDVSPD TSLSRLRPPR SESPSTSSGV PQLRVDTHAN KSESSLDNTD
     EEQSSGTTTM NHNRRDSGVG SSLSRSPSGP SSQRLRQSIL PYSTNSFSFL LNANHVGSLQ
     SKRRAADRNL MSSSILSSCS SDDAFFTDVQ LARCVDSLSV LELARLNKLA YLRVTAILEK
     HMGPGSTVKI GDVSPTQNGA VKNWTVQKLF KKIKMDGKTG REIEVANQVF GQPLTVIYRR
     SGLCLPRTIL EVLRYLRQMA PDTVGIFRKN GVKSRILEVR ALCDRDADAD VFVDENRLDP
     GQVHDVADML KQYLRELPEP LMTARLSETF ANIFIHVPEN ERLLALQYAI LLLPDENREA
     LQTLLLFLSD ISKHSDNNSM PAQNLAVCFT PSLFQLSASR LDKVTPTRRH KTIGAAGMPT
     EREMRETRAA QQCLTYLIQH CRSVFVAAET GPEDRIQADS DAPLLKELGL NGPRAYLIDR
     VLDLVKEHSD RWKSWIVEGI HEDVEISCKV PNDCHPLKLF RVWVDVAAPP KQVMNRIMRE
     RSVWDTSVVN WRTIDVLHAP DTDLHQYVLN DTVGHPTRDC FVARFHRADL SEIRGACAIA
     ERSVQCSETQ LLGGTSAAVL DSRFLIEPKA GHSRVTYISR IDLRGRGPAW YNKVYGNIVA
     RQMIRLRDSF QSSSENIGPE TKV
//
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