ID A0A498LAF3_LABRO Unreviewed; 1398 AA.
AC A0A498LAF3;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Rho GTPase-activating 35-like protein {ECO:0000313|EMBL:RXN05212.1};
GN ORFNames=ROHU_033559 {ECO:0000313|EMBL:RXN05212.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN05212.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN05212.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN05212.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN05212.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) 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:RXN05212.1}.
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DR EMBL; QBIY01013414; RXN05212.1; -; Genomic_DNA.
DR STRING; 84645.A0A498LAF3; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd00882; Ras_like_GTPase; 1.
DR Gene3D; 1.10.10.440; FF domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR002713; FF_domain.
DR InterPro; IPR036517; FF_domain_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039007; pG1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR032835; RhoGAP-FF1.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR045786; RhoGAP_pG1_pG2.
DR InterPro; IPR039006; RhoGAP_pG2.
DR InterPro; IPR001806; Small_GTPase.
DR PANTHER; PTHR46005; RHO GTPASE-ACTIVATING PROTEIN 190; 1.
DR PANTHER; PTHR46005:SF5; RHO GTPASE-ACTIVATING PROTEIN 35B; 1.
DR Pfam; PF00071; Ras; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF16512; RhoGAP-FF1; 1.
DR Pfam; PF19518; RhoGAP_pG1_pG2; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00441; FF; 4.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF81698; FF domain; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51676; FF; 2.
DR PROSITE; PS51852; PG1; 1.
DR PROSITE; PS51853; PG2; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 432..486
FT /note="FF"
FT /evidence="ECO:0000259|PROSITE:PS51676"
FT DOMAIN 488..553
FT /note="FF"
FT /evidence="ECO:0000259|PROSITE:PS51676"
FT DOMAIN 595..775
FT /note="PG1 pseudoGTPase"
FT /evidence="ECO:0000259|PROSITE:PS51852"
FT DOMAIN 803..973
FT /note="PG2 pseudoGTPase"
FT /evidence="ECO:0000259|PROSITE:PS51853"
FT DOMAIN 1267..1398
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1109..1129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1142..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1142..1160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1398 AA; 157998 MW; 3F4C29AD123BFB88 CRC64;
MCTMMMAKKQ DSRMPIYNLV VVGLSGTEKE KGQCGVGKSC LCNRFVRPSA DDFHLDHTSV
LSTSDFGGRV VNNDHFLFWG EVGRVLEDGA DCRMHVVEQT EFIDDQTFQP HRSTALQPYI
KRAASTKLAS AEKLMYFCTD QLGLEQDFEQ KQMPEGKLQV DGFLLCVDVS RGMNRNFDDQ
MKFVTNLYNH LSKTKKPIVL VLTKCDEGVE RYIKDSHTFA ITKKNLQVVE TSARSNVNVD
LAFLTLIQLI DKGRGKPKII PYFEALKHQS QLIASAKDRY EWLVNHIVKN HNETWPNVSR
RMQTSPEYKE YVFLEGTGKA KKLFQQHIHR LKQEHIERRR KAYLSALPLA LSSLVSELDE
IEHLSWSGVQ KVLESKKDFD HWFVVLDDAP WEDTPHLDNM EDERIPFDVL DTTAAEIIFD
AHLEHLRNEC KRAQMRHEFK AKLASSPFVT PGKPWEEARS FIMNEDFYQW LEEPEYLDIY
NRHQKAIIDR AKEDFQELLL EYSELFYELE VDAKPSKEKM GAIQEVLGEE QRFKALQKLQ
AERDALVLKH IHFVYHPTKE TCPNCPHCVD NKIEQILASC FPAQYPSFGK SNMFDGKVDR
INLVILGKDG LARELANEIR ALCTNDDHYM LEGRMYELVL RPIEGNVRLP VNSFHTSTFI
PHGCLCLYNS KESLSYVVES IEKLRESTLG RRDNHMAQLP LSLLLVTKRG VGGLGDIGGE
TAQALISQGQ QVAIKLQCNY LEPASPGSGY GRNVNEKQIN QVLKVLLETR RTSTFRSCSP
PAPPLPPCIR ELQQDQSPEA ELRIVMCLMC GDSYDVDQLL APFLHPQHCK PTSPQTSGTS
VLLEQTIGGH KHTIELSLMS YHASFATRKS RLVHGYIAVY SASRKASFET LCAFLCEVQD
IVPVQLLAVG ETRTELLDSE FAHELLVQGE ELARELEGRF CSIVCGAGGV VGGLHKLDLL
EHFFTEVLEK RTIVEASHMY ENVAEASSTN ENVYSPHCGS PSPVTMLLDS EEDMEASPPY
HDGTLTSHGG FKLPDLDSGD TFSVISDLST FENKLNNKVP PQVRPKPSVT FDLRKPNFNP
YVDAVSHRRS LTSNVTWPLG GDYDPSDYAE PMDAVSKPRP SYEDSIYSVP HDSTQGKIIT
IRNSNRIHSN GGGNGSDSEG DGSSLERRRK FSAARVKPRL YRDRSKRLGK FSSFRTSFSI
GSDDEIGTLT RSKDDDVSGL KADILSEEGE DPKKRNILKS LRRPGKKTRP KPRHSISKPL
ESTYFGVPLV NVVSFERPIP VFIDKCIRYI EATGLTTEGI YRVSGNKAEI ESMQRQFEQD
HNLDLVEKDF TVNTVAGAMK SFFSELPDPL VPYSSQEELV EAFIESSYIS FDNSTRSFSL
YVSICICGIE DTVVHEAP
//
