ID A0A1V4KIL1_PATFA Unreviewed; 1227 AA.
AC A0A1V4KIL1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=SLK {ECO:0000313|EMBL:OPJ84245.1};
GN ORFNames=AV530_015710 {ECO:0000313|EMBL:OPJ84245.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ84245.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ84245.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ84245.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ84245.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) 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 -!- 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:OPJ84245.1}.
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DR EMBL; LSYS01003057; OPJ84245.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4KIL1; -.
DR STRING; 372326.A0A1V4KIL1; -.
DR Proteomes; UP000190648; 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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 Kinase {ECO:0000313|EMBL:OPJ84245.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000190648};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 34..292
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 898..933
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 311..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 850..961
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1027..1061
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1102..1173
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 315..329
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..604
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..724
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..755
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..784
FT /note="Polar 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 1227 AA; 142019 MW; D90214ADFA22A3B2 CRC64;
MSFFNFRKIF KLGGEKKKKQ YEHVKRDLNP EEFWEIIGEL GDGAFGKVFK AQNKETKVLA
AAKVIDTKSE EELEDYMVEI DILASCDHPN IVKLLDAFYY ENNLWILIEF CAGGAVDAVM
LELERPLTEP QIKVVCRQTL EALNYLHENK IIHRDLKAGN ILFTLDGDIK LADFGVSAKN
TRTIQRRDSF IGTPYWMAPE VVMCETSKDR PYDYKADIWS LGITLIEMAQ IEPPHHELNP
MRVLLKIAKS DPPTLAQPSK WSADFKDFLK KCLEKNVDAR WSATQLLQHP FVTVTSNKPI
RELIAEAKAE VTEEVEDGKD EDEEEETENS LQLPSDKRAS SDLSIASSEE DKLSQNASFL
ESLSEKTESN AIEDKASTIF LDDKTKGDES EDIKFRKTAD NICDTTVDDM KVQNGSVPSG
EDKQSKILPA EKNMESLEKP HEDMEPQKGG KELDMVTKSE IKDEPDLKTE KENDIGNEQT
EVNKLKTVPT TENSVETEEC ISKETGEKEE KENRTDLLES KEEKVPEEDT AEQKEEKDEA
QKEAITDTTT ETLPNAVDKV ADEEKELIKH GIHSIKEIGG IAETQISVGD KTPEAEDKPV
ESQAKQVHEI ISSAETPSES QDTVIKVDKK AAESENEDIC SRNSMEETEM KDSGKDSVDH
KSIQNKPEDI SNKVVDKLTD MDQNSEEGKP DKIQENTIQV DKEHLEVTSD EIMKNKRQDI
ASEQADDSEV TPVPSISIST EENEEKVKRD NQDNTEALQQ LESENLKEND ADSGTGSTAD
NSSIDLNLSI SSFLSKNKET GSISLQETRR QKKTLKKTRK FVVDGVEVSV TTSKIVTEND
SKSEEMRFLR RQELRELRLL QKEEQRAQQQ LSNKLLQQRE QMYRRCEQEM TSKKRQYDQE
IENLEKQQKQ TIERLEQEHT NRLRDEAKRI KAEQEKELSK FQNILKNKKK EEQEFVQKQQ
QELDASLKKI IQQQKTELAT IERDCLNNKQ QLMRAREAAI WELEERHLQE KHQLLKQQLK
DQYFMQRHQL LKRHEKETEQ MQRYNQRLIE ELKNKQTQER ARLPKIQRSE AKTRMAMFKK
SLRINSLASP DQDREKIKQF AIQEEKRQKN ERLAQHQKHE NQMRDLQLQC EANIRELHQL
QNEKCHLLVE HETQKLKELD EEHSQELKEW REKLRPRKKT LEEEFARKLQ EQEVFFKMTG
ESECLNPSTQ SRISKFYPIP SLHSTGS
//
