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Database: UniProt
Entry: A0A498L9E8_LABRO
LinkDB: A0A498L9E8_LABRO
Original site: A0A498L9E8_LABRO 
ID   A0A498L9E8_LABRO        Unreviewed;      2892 AA.
AC   A0A498L9E8;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=ROHU_034640 {ECO:0000313|EMBL:RXN03054.1};
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:RXN03054.1, ECO:0000313|Proteomes:UP000290572};
RN   [1] {ECO:0000313|EMBL:RXN03054.1, ECO:0000313|Proteomes:UP000290572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN03054.1};
RC   TISSUE=Testis {ECO:0000313|EMBL:RXN03054.1};
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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:RXN03054.1}.
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DR   EMBL; QBIY01013490; RXN03054.1; -; Genomic_DNA.
DR   STRING; 84645.A0A498L9E8; -.
DR   Proteomes; UP000290572; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:UniProt.
DR   GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR   GO; GO:0016020; C:membrane; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009966; P:regulation of signal transduction; IEA:UniProt.
DR   CDD; cd19497; RecA-like_ClpX; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR   Gene3D; 3.30.70.1390; ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR032171; COR.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR020859; ROC_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR010603; Znf_CppX_C4.
DR   PANTHER; PTHR48102:SF7; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   Pfam; PF16095; COR; 1.
DR   Pfam; PF00560; LRR_1; 1.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF08477; Roc; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SMART; SM00364; LRR_BAC; 5.
DR   SMART; SM00369; LRR_TYP; 6.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF48371; ARM repeat; 2.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS51902; CLPX_ZB; 1.
DR   PROSITE; PS51450; LRR; 3.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS51424; ROC; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:RXN03054.1};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:RXN03054.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          1203..1384
FT                   /note="Roc"
FT                   /evidence="ECO:0000259|PROSITE:PS51424"
FT   DOMAIN          1752..2000
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          2357..2410
FT                   /note="ClpX-type ZB"
FT                   /evidence="ECO:0000259|PROSITE:PS51902"
FT   REGION          881..909
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2335..2367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2501..2523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2864..2892
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2501..2517
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1779
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   2892 AA;  322145 MW;  0F0A3034C337C528 CRC64;
     MADKEELGIR LKKLLVRLNL QEGKQLGTIV QIIQDLLFLS HTDHCVELFA DQNVHMPLML
     VLSSHFNSKV QQVGWSLLCR LMEICPTTLD SLACPVENEF TEVHKQILKV LSMYPKDSKM
     MMVGLRALSL LLKSGEIAMQ VLHEEEQDVF FLILEAMRSF NDKEEVQLQG CAALQLLLQR
     VSDAHLVEFI ENKDHEVILN ALRRFMDSEN MVLQALRVLI PLAAPASNIE ILMSKPVKCY
     SLLCQAMDMW LESEAIQVAG CCLLRKFTSE SYYNILVLNG VHKVAVKACV SYPENATVQT
     DAFSCLSALA ECIVQNEGLD KEWNEEDEAK QKVLVKKVAT QVEEMLIWRE ACYTALERHA
     DNATVQEAAC VALNSLLLHC NSSNHVELEG RMRALLLSHG IHVNIVVLMR KHESSSAVCE
     SACKLLHILF QGARASLDDA ILILGQILIA LKTHNFIPEV QLEGLRASLV LLNPDRSLRE
     HGTSVADPDT VDVSLRVLKN QCVLEGAHTV YLEALNRFIS SVEIQECGLG VLSALADSSG
     AVDLMCQQGA IDTVLHTLQM FPQGRDVHYW GLSLLFHLIS KKKLSRMMVP VLASVLVSSI
     RQHKEDTVML LKGFQVVWKL LDTCSSAAAW LQKEAFEKDI FQILRENMAD QCRDPLQGMS
     CLCLSKMVAD SEIMYALLER ACEDGDVDMA ECLIQLGADI NKKTKSDSLI YQVCDRGAPL
     ALLELLVSAG VHEQQLRGAL SVCIRRGDDP AVTLLLTRLG LDHTNNALCL GSFRLGQMKA
     MWLSALLSER KTQSPVNKKK SKGQRLARQI LSIQRNKGFV GVGRLRSDAS TSEYFTDEES
     DDSHVSLDES LAFMLDDMES DGSDGPSQGL LLFNDSPEVG RKPAWRHSRR RRANSEGCRG
     DTNPSAPLHK RFNSHNTRGQ GFIESSTPGA FPLAVDKEPI RLLDLSGNEL GNLSCLMGMS
     ALKQQIENLL RLDLSSNSLS EFPSVLCQNL RSLTRLDLQG NQLQSLPVEL LGLPALSTLN
     VSRNCIGPLL LLDPTVRSPA LRQLNLSFNQ ITVFPFQLGQ AMDRLEELSL EGLRSVDMRN
     NSISDLPGPS FWVSVNLREL MFSHNQISVL DLSGPAYKWA RLEKLHLSSN KLTEIPPQIG
     MLEDLTSLDV SQNEGLRSFP DEMGKLVHLW DLPLDGLQLQ MNLKHIGNKT KDIIRFLQQR
     LKKAVPYYRM KLIVVGSPRS GKSSLIHQLM KLKRSHWQSD QHTIGVSVRD WAIRNKDKRN
     MLLNVWEFSG GEECSGFHPH FMSSRALYLV LYDLSKGSSE IDTIKPWLFN IKAVAGQSPV
     IVVGTHADVC EERHLQECVL KLREELMSQP GFPVIKENHI LCACEESESI SRLRKAICKE
     LIGFKIQSQP VMGQLIPDCY VELERRVLQE RSHVPTDFPV LRHSRLLEII QETQLQLEEG
     ELPHAIHFLS EAGVLLHFDD PVLQLKDLYF IDPQWLCNII SQTLTLRSTG PWDGTRGVMQ
     RTTVEKFLNK SRCFPMDHLT QFFKLLEKFQ IALPFGDDQL LIPSSLSDHR PVIELPHCEN
     SEVIVRLYEM PYFPMGYWPR QISRLLEVSA YLLYGKEKAL RPNRIYWRKG IYLSWSAEAY
     CLVEALSLED NPASFIKITV PCSRKGCVLF GQVVDHIDSL LEEWFPGLLA TDVHGAGETL
     LKKWALYSFS DGQNCQKILL EDLLSKINAD GLLVNPEDPS CTLPISQISP DLVLSDQPSS
     TILDPEQLEM ELSMEYMLGD GGFGSVYKAV YKNEEVAVKI FNKHASTLYV HRLVRQELAV
     LGRLCHPSLV GLLAAGCNPH ILVMELAPCG SLDSLFEREN SSLSRKLQHR IALHVADGLR
     YLHSSMIIYR DLKPHNILLF NLKTDAEVIA KITDYGIAQY CCSMGVRSSE GTPGFRAPEV
     ARGNVIYNVQ ADVYSFGLLL YDLLTYGERI SDGMKFPSEF DEAAVQGKLP GFESLMRVCL
     RENPQDRPTS AQEIDSSPIL CMVIVRAPGS CSDWLVAGTQ SGSLYIMDTI SAEVLHCLKS
     VKDSVTSLYF HTHRHLKNYL LVGTADGSLI IYEDSVLKVK DGGPVKTLQV GDVNTPLMCI
     GPFSQNQERR ELWAACGSRV FSLSVEYDMS RSIDTKPKHL YTLSPTKKPK AQSEDQSRQM
     VPSSATVKAL LVQHSGTLWI GTKAGHILLV EVSSCQLLQT ISPHCHSIRC MGSVLLADSL
     NRKNVILVLG RRQRMPQDQI KTQAPAEDSV LTVWNSSLPL EVRDLIRHYL VLNMSCSCGP
     AVRVILKSVH KGFPRSRVQL FSHTRAVCDE VHLPPFVHVR LFSQTAVCFA SKDGTTRDGD
     GGKKGVSEAG GKRASGAGGS GKGGSQLRCP KCGDPCTHVE TFVSSTRFVK CEKCHHFFVV
     LSEADSKKGL NKEADSSEHV KFALAQKPPP PPKKIYAYLD KYVVGQSYAK KVLAVAVYNH
     YKRIYNNLPA AGRQQAETEK QSSLSPRELL QIAGINPHGN ALGASVQQQT NQQAPQDKRG
     RDVLDSAPTD IKLEKSNIVL LGPTGSGKTL LAQTLAKCLD VPFAICDCTT LTQAGYVGED
     IESVIAKLLQ DANYSVEKAQ QGIVFLDEVD KIGSVPGIHQ LRDVGGEGVQ QGLLKLLEGT
     IVNVPEKNSR KLRGETVQVD TTNILFVASG AFNGLDRIIS RRKNEKYVVL SSYHLQYLGF
     GTPSNLGKGR RAAAAADLAN SSGNEMDAMA EIEEKDRLLR HVEARDLIEF GMIPEFVGRL
     PVVVPLHSLD EEMLVQILTE PRNAVVPQYQ ALFSMDKCEL NVTPEALRAI ARFALERKTG
     ARGLRSIMEK LLLEPMFEVP QSDIIAVELT KEVVQGKCGP RYIRAPPKET EEEFDSASEE
     DNWPRHADAA NN
//
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