ID A0A151NV04_ALLMI Unreviewed; 1281 AA.
AC A0A151NV04;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=Y1Q_0009627 {ECO:0000313|EMBL:KYO40618.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO40618.1};
RN [1] {ECO:0000313|EMBL:KYO40618.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO40618.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
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 -!- 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:KYO40618.1}.
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DR EMBL; AKHW03001922; KYO40618.1; -; Genomic_DNA.
DR RefSeq; XP_006273723.1; XM_006273661.3.
DR STRING; 8496.A0A151NV04; -.
DR GeneID; 102557821; -.
DR KEGG; amj:102557821; -.
DR CTD; 9748; -.
DR eggNOG; KOG0579; Eukaryota.
DR OrthoDB; 2880940at2759; -.
DR PhylomeDB; A0A151NV04; -.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR CDD; cd06643; STKc_SLK; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR022165; PKK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR001943; UVR_dom.
DR PANTHER; PTHR46538:SF1; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR46538; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF12474; PKK; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50151; UVR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 34..292
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 921..956
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 309..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 873..974
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1018..1052
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1081..1115
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1163..1197
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 315..329
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..725
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..792
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1281 AA; 146957 MW; 21E8F3070A8842D9 CRC64;
MSFFNFRKIF KLGGEKKKKQ YEHVKRDLNP EEFWEIIGEL GDGAFGKVFK AQNKETKVLA
AAKVIDTKSE EELEDYMVEI DILASCDHPN IVKLLDAFYY ENNLWILIEF CAGGAVDAVM
LELERPLTEP QIKVVCKQTL EALNYLHENK IIHRDLKAGN ILFTLDGDIK LADFGVSAKN
TRTIQRRDSF IGTPYWMAPE VVMCETSKDR PYDYKADVWS LGITLIEMAQ IEPPHHELNP
MRVLLKIAKS DPPALAQPSK WSSDFKDFLK KCLEKNVDAR WTATQLLQHP FVTVTSNKPI
RELIAEAKAE VTEEVEDGKD EDEEEETENS LQLPADKRAS SDLSIASSEE DKLSQNASVL
ESLSEKTENS AAEEKNSGML PDDKTAADEP ANIEDGKAID NTSDATHEEV VKVQNGSVLI
EENELKKIPG VEKKTGKAEE VNEGAGLQKE GKAVDTVLPL ETNDEHGVKT EKANDTDNEQ
TAENNQKIGP ETEEPSAQIT DVISEETGEK EEKESKADFQ ENKNEEGTVE KVAEQMEETM
DSTKETPIQV VDEMADREEE PLKFGGDSAP ETGSSSETQI TDGDKIAGTG QKLMESGLEP
AHETVSAEQT ESKSEDTVTD TDQKSVDDNT VTDTDRKSVE SGNEDVCKRS NTEETEVKES
GSMGDPDQKS VESKTEDILG VNDTEEIVKA SDTVEIPEKD ADKIAKVNQN SEIKRPEDTQ
KNGIQIDTER SEVPGDPLIK NKPQETTTEQ TGLIPVPRIN ISTEENEEKV KIDNEANAET
LRQLEPETVK ENDADSGTGS TADNSSIDLN LSISSFLSKN KDTGSISLQD TRRQKKTLKK
TRKFVVDGVE VSVTTSKIVT ENDSKSEEMR FLRRQELREL RLLQKEEQRA QQQLSNKLLQ
QREQMFRRFE QEMTSKKRQY DQEIENLEKQ QKQTIERLEQ EHTNRLRDEA KRIKAEQEKE
LSKFQNMLKN RKKEVFNEVE KAPKELRKEL MKRKKEELAH SQHAQEQEFV QKQQQELDAS
LKKIIQQQKT ELANIERECL NNKQQLMRAR EAAIWELEER HLQEKHQLLK QQLKDQYFMQ
RHQLLKRHEK ETEQMQRYNQ RLIEELKNKQ TQERARLPKI QRSEAKTRMA MFKKSLRINS
SATPDQDRDK IKQFAGQEEK RQKNERLAQH QKHENQMRDL QLQCEANIRE LHQLQNEKCH
LLVEHETQKL KELDEEHSLE LKEWREKLRP RKKTLEEEFA RKLQEQEVFF KMTGESECLN
PSTQSRISKF YPIPSLHSTG S
//
