ID D6SAD6_FINMA Unreviewed; 632 AA.
AC D6SAD6;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFH92436.1};
GN ORFNames=HMPREF0391_11408 {ECO:0000313|EMBL:EFH92436.1};
OS Finegoldia magna ATCC 53516.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Finegoldia.
OX NCBI_TaxID=525282 {ECO:0000313|EMBL:EFH92436.1};
RN [1] {ECO:0000313|EMBL:EFH92436.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53516 {ECO:0000313|EMBL:EFH92436.1};
RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL Submitted (MAY-2010) 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:EFH92436.1}.
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DR EMBL; ACHM02000003; EFH92436.1; -; Genomic_DNA.
DR AlphaFoldDB; D6SAD6; -.
DR STRING; 525282.HMPREF0391_11408; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG2815; Bacteria.
DR HOGENOM; CLU_000288_135_2_9; -.
DR Proteomes; UP000004063; Chromosome.
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 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 327..346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..281
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 355..422
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 423..490
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 493..560
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 296..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 632 AA; 70331 MW; 398B874FC31D01C3 CRC64;
MKGKIMIGKV LGDRYEIIEE VGVGGMAKVY KALDTVLNRY VAVKVLKNEY MEDQDFLRKF
AMEAQSAASL THANIVSVFD VGSSYVDGRK YNYIVMEYVD GKTLKDIIDE KQILPIEDIV
NYGVQIASAL ECAHKNGIIH RDIKPHNMLI DKSNNLKATD FGIARISSSA TLTYTSTVLG
TVHYISPEQA KGKFIDEKSD IYSLGVVLYQ MATGEVPFDA PNAVGIALKH IQDPLVPPIN
LRHDLPQGLN DIIVKAMAKD PNDRFKSATE LKEMLKNYQS YSSDLYQKTT KNPIIKESDE
QPEVKEAVYK TPKQSSTKDN KNKSKKFMWI LLPVLLAALV FVAFIFGKKY INKNKQDLVL
VPALTGLTEN EALNKAKANN LIAVVSEYKT ESNVEPGKVL EQDPESSTEV KKGTIIKLVV
SKGEEQVSVP NLSNMTLENA KIQLNKLGLE IGEITKENSD NFEAGKIMQQ HPDAGTSINK
DSKVDVVISL GKKEELVEMV DLIGTDISQA SNKLKSIGLN IGNIEKKFSN SYDTNQVIWQ
QYDAGKKLKK DSSIDVIISK GKKEPEMIDK VFRISKPVEK GIYTVTVKDE TENNIIYEEN
HDASEGDIRI KVKAKPNNDI KVYINGELVN VG
//
