ID A0A4Z2D9R7_SCHJA Unreviewed; 1560 AA.
AC A0A4Z2D9R7;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 10-JUN-2026, entry version 18.
DE SubName: Full=Rho GTPase-activating protein {ECO:0000313|EMBL:TNN13196.1};
GN ORFNames=EWB00_003127 {ECO:0000313|EMBL:TNN13196.1};
OS Schistosoma japonicum (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6182 {ECO:0000313|EMBL:TNN13196.1, ECO:0000313|Proteomes:UP000311919};
RN [1] {ECO:0000313|EMBL:TNN13196.1, ECO:0000313|Proteomes:UP000311919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HuSjv2 {ECO:0000313|EMBL:TNN13196.1};
RC TISSUE=Worms {ECO:0000313|EMBL:TNN13196.1};
RA Hu W., Luo F., Yin M., Mo X., Sun C., Wu Q., Zhu B., Xiang M., Wang J.,
RA Wang Y., Zhang T., Xu B., Zheng H., Feng Z.;
RT "An improved genome assembly of the fluke Schistosoma japonicum.";
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
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:TNN13196.1}.
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DR EMBL; SKCS01000198; TNN13196.1; -; Genomic_DNA.
DR STRING; 6182.A0A4Z2D9R7; -.
DR OrthoDB; 120383at2759; -.
DR Proteomes; UP000311919; Unassembled WGS sequence.
DR GO; GO:0097060; C:synaptic membrane; IEA:TreeGrafter.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IEA:TreeGrafter.
DR GO; GO:0030030; P:cell projection organization; IEA:TreeGrafter.
DR GO; GO:0046578; P:regulation of Ras protein signal transduction; IEA:TreeGrafter.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00030; C2; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR052118; Rho-GAP_regulator.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR057459; SYDE1/2_C2.
DR PANTHER; PTHR46150; RHO GTPASE-ACTIVATING PROTEIN 100F; 1.
DR PANTHER; PTHR46150:SF3; RHO GTPASE-ACTIVATING PROTEIN 100F; 1.
DR Pfam; PF25336; C2_SYDE; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468, ECO:0000256|PROSITE-
KW ProRule:PRU00172}; Reference proteome {ECO:0000313|Proteomes:UP000311919}.
FT DOMAIN 878..995
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1090..1306
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 370..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1336..1463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1477..1560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..452
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..515
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1424..1434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1452..1461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1499..1514
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1531..1545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1546..1560
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1560 AA; 176104 MW; 094FEC41CF63060D CRC64;
MPKLVFIHQC CHLFQWFVPA SICSVYYCYY FDCCYCYCYF IHYSQVGIVN NLKLNIKIFY
TQNYCHHYYN HLILETGVKH LNRFHSELNN CNHWHLTYFT YFLFNLVNFG YIITTLIKQL
LLNYNITINI ANYSNIFFLA QILHNSASKF FKYNQLHLEH QMAEESVDSG ISSELYTTKS
DQTSCNLNTE LQQSEKYNNI QNLKLIQPID NFTYNLHSNH FNKGCTKSNS HVVFLQNALY
ENSKLDRDIF LHSVDQGYIF NNSKFNKKQI LNKFKKYNIN SFDSAFETSS ESTLSLVSNL
SGSYQNLNCT IKPNYSLNYN NLNNPTEQPS KNMTEDNKPV YQDFYTCDKQ ANRYTVNEGK
SLNPRVHFVQ EEEGNRSNLP GPSRPSSGYT MDSAGNIYDQ NKMLSHLLSS RDYVYMPANR
IATSGIHNIR SGPRLSNWPR QQQPNQHQTH LQGPYPENMI HNLDQVTENK SGNIPYYMQQ
QASQNRNLID QAYDSPKGSN QSQQAHLQNQ QNSQQANYQQ LISALLAAAS ANKSRLEPQS
SHTSDLSPIG VDITMNQQKS STSNRWSDSE LATNNAKDMQ YHFQQQQQIR QQQQQQATAA
AAAAAAAAAA MAALQCSAKS SGNIPLNIQR QVPLTFSSGG SGISHRHPAY LRSSYSSGDE
SSAIRIMNPA SLVTSMQKLR RFCTPGMNLN EPSPSQPLLL PQHSLPTMSE NIPLSEQNSK
VQRATQQLIT QLNKFQDLSV SGDDYANYQC LESLLGQVSR QPLAPAPSVQ MENVVCTDPA
GTRSSYPNES LYMSSKIPGQ IIGSTRTTTV PSSLSCQSNL ETPNLNLDSQ SFGTSNVLSD
RFGDFLTLPS ERCLSASQAS SHPTQSSVYE WDSCNIPSRT VNLQNVDRVP KSNNLNGLFV
LHVIAGKGLN STHIIVRDLY CVIEMDSVRK ARSMIRTSTS YFEWNEVFEL DMEDNRFLAV
LLYQWDPRTK HRLCFYGGID LKNLLSRLTS ANNTASTSQT STSEIILSPA VSILTKQLHK
IALQLEPRGV LYLEFAHIPL EKVFHRNQNL LSTTPLSSTS TERLLFGVSI DELIERERVI
CQITELYSPK QLTYQNTSDY MFIPLFIKKC VEEIDKRGSD VVGVYRLAGS VWMKLQVREL
FNRVTKSTLK ALVHEDAKAL RDIIQLVDLS AQRIPDIHAI TAVFKDFLRE LPEPLFTSAL
YPMFYDAMQI ALPGFTQSGA KLVLNILDCL PANNQEILLY LLDHFKRLTN NCEVNKMDTQ
NLATCLAPVL FYPSPSSARN LDPNILEPRK MAEIFKFILE IWPDDRSKTY KFSPSDTWTS
PYSSNVPLLE EQHQTGFYPQ PHHHHPKHRY DQSGHRASSA IRSTISGPAG TGLGYRSPHT
VQRSSILASK AESDKSDYAG IGRSGAVKYG NGSNGSSRQG VSQDGHRRAS RDPRQTVSFG
NAKTMRAHSA QRKTLSQTDI TFGSGREHTV GFDFRDQQVI PPGDESSIHV HPRFQDIPTT
GSTGTDSGTR SSLSVGSRQP CPPSHLSSSV DRGEIIRSTS QERQHYGRTH RLSRRSHPFS
//