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Database: UniProt
Entry: T1KVT6_TETUR
LinkDB: T1KVT6_TETUR
Original site: T1KVT6_TETUR 
ID   T1KVT6_TETUR            Unreviewed;      1017 AA.
AC   T1KVT6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 2.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Rho-GAP domain-containing protein {ECO:0008006|Google:ProtNLM};
OS   Tetranychus urticae (Two-spotted spider mite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC   Tetranychoidea; Tetranychidae; Tetranychus.
OX   NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur23g01800.1, ECO:0000313|Proteomes:UP000015104};
RN   [1] {ECO:0000313|Proteomes:UP000015104}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA   Rombauts S.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:tetur23g01800.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
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DR   EMBL; CAEY01000614; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; T1KVT6; -.
DR   STRING; 32264.T1KVT6; -.
DR   EnsemblMetazoa; tetur23g01800.1; tetur23g01800.1; tetur23g01800.
DR   eggNOG; KOG1453; Eukaryota.
DR   HOGENOM; CLU_2545552_0_0_1; -.
DR   Proteomes; UP000015104; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd20816; C1_GMIP-like; 1.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR031160; F_BAR.
DR   InterPro; IPR001060; FCH_dom.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   PANTHER; PTHR15228; SPERMATHECAL PHYSIOLOGY VARIANT; 1.
DR   PANTHER; PTHR15228:SF25; SPERMATHECAL PHYSIOLOGY VARIANT; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00055; FCH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   PROSITE; PS51741; F_BAR; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW   ProRule:PRU01077}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015104};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          39..324
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51741"
FT   DOMAIN          438..484
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          501..700
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          894..971
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          991..1017
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        894..936
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        946..971
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1017 AA;  113327 MW;  FA6D7703788551F5 CRC64;
     MGGVKSNGNN NDMTGFDSIS SSSPPELDDP EARSLLTPND CDNRFLHLPE GIDLALHRTK
     LWSKYAKDLI NYIDKRTNLE ADHVRNLTKL AQSVKPILKE EKYLPLQSIY LQALDNDLDN
     SCATLANCSL LMGHKFIEPL AARRAEHEKM RKQIKSEWNR ELKRTHEALS NLRKARMVYF
     QRKQEYERLR ALSNLAPELS HSSEMQGSII GGPGAIVGGC YGGSDQASKC ERKKRIEEEA
     CLRAQEAEII YRNAINEANA RTRSCEELKK NLLTRIRELI YQCDQTLKAV TIGYFECQHN
     LLKPIVGQFG ALSDLTKLYE PASEYADYVQ HLPEFTEKLR KCNGSYGNYK FDPSINSMTS
     IKEQPQRVNC NNKHHNLSNC PENGVDSVNK DHLKSSNNIG LPINSSGDEI DGVTNYSTVG
     NGYECTSKSS TLPITAQSHH FRKLKTPSRC RHCDAYVCFQ GLECINCGLT CHTKCRIELT
     TIKCSNRRMR GLSKKMTTFG VDLKSHGDEI PYIIVKCITE LDNRGIMVKG LYRVSGVKSK
     VDKLCQFFES STDSIDIEDV HPNVIANVLK LYLRQLPEPL ITFKLYSEFI RIAKQYPSNA
     DGNGPDSDDA SIAVQIINQF KQVTQNLPTV HYQTLAFLCH HLKRVADQSE VNNMPSSNLG
     IVFGPTLLRS SEGDSLSSLV DTGHQARAVQ LLITYVDQIF GPSEKLTNSI YNEIDGNEPD
     LVDKHFSQNE LKETNRTQIT LTLEGNNNLY DRGELNDKPQ SKNNRIISNN YSIKNIKNSN
     NNNNTVTINN NNNNNNKNNN KINENDNNNV IGLNNGVDGK RSLDRERLSP TPSIYSSSAV
     IKLSGQQIIT GPSSLIHSSL PNYDDSDDRL NRSNVIGGSR HSLYEARRQF FASPTSLTSS
     SSLSSSPLST STSNSSIRPH SLVSGSISLN SQNHSTHHNH SHSHHQSIKQ TSSQPSSSTL
     SSPATSPSNT NELQMAMSSL SLTRPRKASI ISNGPSLSLG TNNNDNSNNM FNTETNG
//
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