ID V2Y3L9_9FIRM Unreviewed; 698 AA.
AC V2Y3L9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Kinase domain protein {ECO:0000313|EMBL:ESL02672.1};
GN ORFNames=GCWU0000282_001542 {ECO:0000313|EMBL:ESL02672.1};
OS Catonella morbi ATCC 51271.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Catonella.
OX NCBI_TaxID=592026 {ECO:0000313|EMBL:ESL02672.1, ECO:0000313|Proteomes:UP000018227};
RN [1] {ECO:0000313|EMBL:ESL02672.1, ECO:0000313|Proteomes:UP000018227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51271 {ECO:0000313|EMBL:ESL02672.1,
RC ECO:0000313|Proteomes:UP000018227};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (JUN-2013) 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 -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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:ESL02672.1}.
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DR EMBL; ACIL03000013; ESL02672.1; -; Genomic_DNA.
DR RefSeq; WP_023354414.1; NZ_KI535368.1.
DR AlphaFoldDB; V2Y3L9; -.
DR STRING; 592026.GCWU0000282_001542; -.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_000288_135_2_9; -.
DR OrthoDB; 9788659at2; -.
DR Proteomes; UP000018227; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd06577; PASTA_pknB; 3.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.10.20; -; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR005543; PASTA_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR NCBIfam; NF033483; PknB_PASTA_kin; 1.
DR PANTHER; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF03793; PASTA; 3.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51178; PASTA; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ESL02672.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000018227};
KW Transferase {ECO:0000313|EMBL:ESL02672.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 345..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..271
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 402..469
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 470..536
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 541..605
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 304..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 698 AA; 75685 MW; 693D1AF358A9AD14 CRC64;
MLNKGKLIGG RYEIISLVGS GGMADVYNAV DNRLSRQVAI KVLKEEYSSD KNFVMKFRAE
AQSAAGLSHP NIVNVYDVGE DEGLHYIVME LVEGITLKKF IERKGKLELK EAVGIAIQIA
QGMEAAHANH IIHRDIKPQN IIISKEGKVK VTDFGIAKAA TSNTIAAGQA VGSVHYISPE
QARGGYSDEK SDIYSLGVTL YEMISGKMPF AADNTVSVAL LHINEEAVPL RELDPEIPAS
IEKIVQKCMQ KKPERRYLTA TELIADLRKA VSEPEGDYVD FNQAVVTDSP TINISGEELE
TIKKGRYNTD RNNRTNEKVR KREPREVREV PEDEEESMDP KMEKLILFGG IAAIVILAIV
VIVLLMKGFN LFSNGGDSSS SGKTASSHTA SSSSIASETS SKTDKVKVPE VKGHTLTEAM
AILADAGITN YKSKYESSKD VEKEKVMDVT PAEGTEIKKD DKVLIIVSKG DDSQTVPDVK
NISKETATST LEDMKFVVNT QEKPSETVEK GKVIDTIPTA GTEVKEGDTV TIVVSSGPEN
KKELVPNVLG KSEADATTIL NNSGFKVSIA YKEDDSAEKG NVISQSIAGG NEADRGTTIV
LSISKGPKPV TYTYSASLTI DESPFAEAGE SGDIVVKMDQ DGKTKTVYSG TVSDEDFPLQ
IDDITSSSES EAVCYLLVNG EVYDGKVWRI TNWSKAEN
//
