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Database: UniProt
Entry: A0A0V1HT68_9BILA
LinkDB: A0A0V1HT68_9BILA
Original site: A0A0V1HT68_9BILA 
ID   A0A0V1HT68_9BILA        Unreviewed;      1060 AA.
AC   A0A0V1HT68;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   22-FEB-2023, entry version 30.
DE   SubName: Full=WW domain-containing protein {ECO:0000313|EMBL:KRZ13788.1};
GN   Name=tag-325 {ECO:0000313|EMBL:KRZ13788.1};
GN   ORFNames=T11_5466 {ECO:0000313|EMBL:KRZ13788.1};
OS   Trichinella zimbabwensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ13788.1, ECO:0000313|Proteomes:UP000055024};
RN   [1] {ECO:0000313|EMBL:KRZ13788.1, ECO:0000313|Proteomes:UP000055024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ13788.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) 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:KRZ13788.1}.
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DR   EMBL; JYDP01000029; KRZ13788.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1HT68; -.
DR   STRING; 268475.A0A0V1HT68; -.
DR   Proteomes; UP000055024; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd13233; PH_ARHGAP9-like; 1.
DR   CDD; cd00201; WW; 1.
DR   Gene3D; 2.20.70.10; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR23176:SF129; RHO GTPASE ACTIVATING PROTEIN AT 16F, ISOFORM E-RELATED; 1.
DR   PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00456; WW; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   SUPFAM; SSF51045; WW domain; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        48..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        84..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          441..474
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          629..729
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          832..1056
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          347..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          470..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          512..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          765..795
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          994..1023
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        525..548
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        778..795
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1060 AA;  119304 MW;  E46E4D2D0B073DAA CRC64;
     MFFGIRVLSL HVASKELKKA FPPTRRCSVY TQDGIHWLPL YRFKWMPIIA SISRIKLAQT
     VLSVIFVPVA YSAYQEKQIS LNQLYVLVFI CVFALFMLFV MSGIFRRLIG VVSLDESRNV
     IRIGHLTFWG ARRNVEIPLE DLTPLSEVNF RPGDVYAAIR RYSDSKMCLS LVEVLYNYDS
     TTSRGHRVHV LAGEKFYLVS DADEHWWFVC KDWSNIDGFY LPKSYLRVLS VQSGILSSDQ
     TPAVISDDDD DDDDVCGGVS KDEMIRTSVA NGHRPFVVAE EEPEVEVEES LPAHRWPAVL
     ANGKAGKLSS ARLVSASIPV GLEMYCLERA DQRSAHLNGD HGLVGVETSS SSGRCSTMGT
     VGAQSRSLDN DLPMSSTCSS STGSRNHSNN SSSSSVVIAL DSVSVSDALV NARSRSPIYA
     NIEECTDMSI PAITPDMQPI RTLSNGWQEY ISESGRPFFY HPLIEIASWK PPRSSTSTTN
     QQQSNVASST RAMLDSSSSV LDNLSMFDKA KSDHCKRSKS KLTDVDVEPQ QQQQQQQQQQ
     HKQQVQRSGF SIDEEADDGR GEHCVRVSIR DFSDLNRLLS TSQQHPATRP TSTSLYGQCM
     SASDGALKFS AFHSSTGTVI KCGNLNRCKV MEAGKRIRKH WSTCFVYLTN AHMIFYKDKK
     SSEKQGNQYC APLGVCDLHG AKIKWLVDDK NKRKRLFQLE LVDGTAYLFH TEVDNEIVDW
     YDALQKIVNE LPNPGFQRTP VIERSSYKTS SRRVCTTTGQ KIAKDAKNLH DQKEKQSTSR
     GINNGPTSDS VEASVPSKQS ILEKLVRFFR NRPSVEFLKE RGIYKPEPVF GSSLTEICRR
     EKNTVPKFVT VCMSLIEERG LETDGLYRMS GNLSQIQKIR CSVDQEKYNV LMNENDIHVL
     TGTLKLFFRE LQEPLFPPFL MKEFMNAIKL QNAKMRYCAF RDLVARLPPP HHDTLDALLV
     HLLKVAEKSS TNRMQIHNLA IVFGPTLFSS CPKPDKVESG GQRRKKMMMK KSASKYSEPS
     TSGHVDVIQS NSHLAFSMIM HGQIVEYMLK EHSKLFKVKV
//
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