ID A0A1R1YF10_9FUNG Unreviewed; 918 AA.
AC A0A1R1YF10;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-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=AYI70_g855 {ECO:0000313|EMBL:OMJ25511.1};
OS Smittium culicis.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133412 {ECO:0000313|EMBL:OMJ25511.1, ECO:0000313|Proteomes:UP000187283};
RN [1] {ECO:0000313|EMBL:OMJ25511.1, ECO:0000313|Proteomes:UP000187283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GSMNP {ECO:0000313|EMBL:OMJ25511.1,
RC ECO:0000313|Proteomes:UP000187283};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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:OMJ25511.1}.
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DR EMBL; LSSN01000155; OMJ25511.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R1YF10; -.
DR STRING; 133412.A0A1R1YF10; -.
DR Proteomes; UP000187283; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24346:SF93; KP78A-RELATED; 1.
DR PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:OMJ25511.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000187283};
KW Transferase {ECO:0000313|EMBL:OMJ25511.1}.
FT DOMAIN 26..358
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 128..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 918 AA; 103754 MW; 501F3CD55B12CB98 CRC64;
MDSKNSSKSK YRVSSTEKKQ HVIGKYIIGK TVGSGSMGKV KLGFDILVNE WVAIKIINKS
ENDFDFFELP NYKNITWKKH MSGDAESNHP VLTSKRLERG SAISSPFSKS EINFLSLVKK
SLHSSPTQLQ HYSHFDPNQK RKSKKKKDLR VLREVSISQL VIHPHICELK DIIINSDRYF
LVSELVVGKQ LLEIIVKKGK LDEEVSRHYS RQIASALMYL HKHSIVHRDL KIENIMVNDK
NDIKLIDFGL SNLFSAQKQL NTFCGSLYFA APELLEAKNY YGPEIDCWSF GIVIYVLVCG
KVPFDDVSIS NLHARIKLGV FELPRHLSEP CKTLISSLIV IDPTKRATIA HAISSVWMNI
GHSSPPQLYF PSATKVNPPL VHTSQIDESI VQIISKHYSS CYFDGVHNNS YEKVYNEISN
LINSNWYKSF LINKYGKYIN QMNQSIYKSI TPQKSFNPNT LSISLKNSFP ISSFSDQKHI
SSAKSFSFAK KNNDINSLSA VKSFISTNDS RNKPLSTPKS INLFSNSFKS SKFTFIDDQS
AKSPHFLKPP VSGNSKLAYA GDSQFVAPEI IDYNFPSAED LTSSSPLKLN NLELMPFELS
QNDSSSLDFE PNDNLKQIIH NFSYLSGTSP ILSIYYMVQA KIYYYLKNIE NLELSYSGSD
SNHYTNSNNS HFNKPLPQKP QKIENSDASD KSAIEDAASS NSSVFNQDTF YDSLNEDQDS
DSDSIDSSKP KERKLETFLE TLRFLDANPN YFNLSSNPLN SNNIRQNPAI SNLVSSNLKS
KPISSKITSK IPKVRSRAFN PTSWIIPNQS SKVDKPPSFI QQRNTRPTKS FILPNKKAES
SFNSSKLSSF KNKLKKPSNT IEPQDGFKNN YENRDSLLSL FSILNATPSS KNIHAHTHSQ
QNGDKKKSGW FRSVLKKL
//
