ID A0A553PFB1_TIGCA Unreviewed; 1410 AA.
AC A0A553PFB1;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 10-JUN-2026, entry version 19.
DE RecName: Full=Rho-GAP domain-containing protein {ECO:0000259|PROSITE:PS50238};
GN ORFNames=TCAL_15926 {ECO:0000313|EMBL:TRY76372.1};
OS Tigriopus californicus (Marine copepod).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Hexanauplia; Copepoda; Harpacticoida; Harpacticidae; Tigriopus.
OX NCBI_TaxID=6832 {ECO:0000313|EMBL:TRY76372.1, ECO:0000313|Proteomes:UP000318571};
RN [1] {ECO:0000313|EMBL:TRY76372.1, ECO:0000313|Proteomes:UP000318571}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=San Diego {ECO:0000313|EMBL:TRY76372.1,
RC ECO:0000313|Proteomes:UP000318571};
RX PubMed=29988158; DOI=.1038/s41559-018-0588-1;
RA Barreto F.S., Watson E.T., Lima T.G., Willett C.S., Edmands S., Li W.,
RA Burton R.S.;
RT "Genomic signatures of mitonuclear coevolution across populations of
RT Tigriopus californicus.";
RL Nat. Ecol. Evol. 2:1250-1257(2018).
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:TRY76372.1}.
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DR EMBL; VCGU01000004; TRY76372.1; -; Genomic_DNA.
DR STRING; 6832.A0A553PFB1; -.
DR Proteomes; UP000318571; Chromosome 5.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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; IPR047887; ARHGAP20_PH.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR23179:SF3; RHO GTPASE-ACTIVATING PROTEIN 20; 1.
DR PANTHER; PTHR23179; T-CELL ACTIVATION RHO GTPASE ACTIVATING PROTEIN-RELATED; 1.
DR Pfam; PF22286; RHG20_PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 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:UP000318571}.
FT DOMAIN 374..559
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 745..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1000..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1113..1143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1254..1277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1314..1349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1389..1410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..826
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..849
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..868
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..881
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..892
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..904
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..933
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1015
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1034..1044
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1060
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1320..1343
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1397..1410
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1410 AA; 155701 MW; E3EA09F821F7D76F CRC64;
MIVVEANMWS HDNTERGMGM MTIMMICRLC MMISELTCFG TAHVEEIAVV VSRTWSLIRF
ISLLQKLKGL VRQKTNNSMP NPMAMGRAIF QKANNLTHKT SQNGRTESTI ADVFGSKDAG
LIPNKHRTFL MDTQVKYTVG LQSQERNLFL FNDLLLVAKE RSASHFKLKD QSPKLNYTSW
SPLVLYLQIP LSDIWLSTCI SEVSEVTLDP TTSFVIGWPI TNAVITFSSP SQKSLWWDKL
RELVEKERSH TPQSTNVQVT YFDQATNFEH STPNPIPITK AQLPLAIDPL ERRGCQNATL
EVSLIGLRKV GQMPNLDIIG SQKTKLKKVK SSIKLQNVFR RVSQGSKASD LGVDGSNPGS
SPKSDKKLGK LFCLPLDEVC PNNLMPKAIE AMLVQILKEG PSTVGIFRRS PNARAMRELR
EKLDQNEVVD FTECSVFVTA ALLKDFLRSL PDCLLMCEHY NTWNQLAQVF EDNKNVESIK
SFISTLPRMN GLLLQHVLYL LFQIASHSQE NMMTASNLAI CVGPSILWSS DNAVMMDQQF
SKQVSCVAQI LIEEYNTLYK GDLTPYAFSE PSDKTIHHPS QKSSRKLYDN SSLDSLLDAN
HFGESDLLLS QQSGTEGVSL TNLSHDSGLT TSDSQLYAFE ENNSLSSDEF CIENVAKDRP
HNNNNGSSNN KHRIMPKYPT YNQDLTGDFI LPGQVPNGSV RSGKQGSSKI PIHQNHFAIS
SGGSKTGKHR VINNHRDRIY KRMQRHNNTN SQSHPNVPTT PTSHFGSKYA SGINDADQAF
MIDTTSFTLR RTASEESVSH GPAQVSSVPS SSRSSRRRPV VHRKGKAPAP PNDGPFLSSN
IVRSNSVNQV RGRDMEHGSK HRSSDWYRSR STTRLNHNPP NQHHHHHHHH HHTQDMTSSS
CSTLSDEDST PHVSRSNSYG KTEETNQGYA SSTKITNDGS YDIYLHDDHL TVGGEAFITT
TPVPKGTPTS NPNCDTPPGY EETISRQRLL KHYNRSNSFV LSTSNISPSP NTTSSQKRLS
EIQNSSAKAR LFNESPQPHV TTSGNPPPLP PKTERPPLPP KQRIMRLSAE DTYVNSDDLK
LLEDEKDSDV LVYPNFTPAR IHVNPSPVPF VNGVKVPQLP PKESASGSES DTPRKARRSV
TKIKGVTAAS TQTKTMCNAE TQTDETDFYL LYGEDEWEAM LNAEEQMNED FSESHRSLSP
EYYPAFNRGA PLDNPEYISH NGNRNSVPGH LVNGTSITAP TRNATSVLEL RQAGRRKLEP
VQSVPLTASH GSGTPVPGKL GVAGVAGVAG VDPVIQGEIN WSVSQLRSLF NQSGQATANG
SQHSPTGGGS SSSASSTTSH LGGRFTNGEY IDSSSSATKA VARQIMLNGG VNANGHSLYE
DRGNKASTIY SSKDCENNDL ADDSDQESYV
//
