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Database: UniProt
Entry: A0A1V2YIF1_9FIRM
LinkDB: A0A1V2YIF1_9FIRM
Original site: A0A1V2YIF1_9FIRM 
ID   A0A1V2YIF1_9FIRM        Unreviewed;       679 AA.
AC   A0A1V2YIF1;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OOB79266.1};
GN   ORFNames=BEN19_00180 {ECO:0000313|EMBL:OOB79266.1};
OS   Epulopiscium sp. Nuni2H_MBin003.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Candidatus Epulonipiscium.
OX   NCBI_TaxID=1884657 {ECO:0000313|EMBL:OOB79266.1, ECO:0000313|Proteomes:UP000189211};
RN   [1] {ECO:0000313|EMBL:OOB79266.1, ECO:0000313|Proteomes:UP000189211}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nuni2H_MBin003 {ECO:0000313|EMBL:OOB79266.1};
RA   Ngugi D.K., Miyake S., Stingl U.;
RL   Submitted (JUL-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:OOB79266.1}.
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DR   EMBL; MDJN01000112; OOB79266.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V2YIF1; -.
DR   STRING; 1884657.BEN19_00180; -.
DR   Proteomes; UP000189211; 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:0010506; P:regulation of autophagy; IEA:InterPro.
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; IPR045269; Atg1-like.
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   PANTHER; PTHR24348; SERINE/THREONINE-PROTEIN KINASE UNC-51-RELATED; 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   4: Predicted;
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}; Reference proteome {ECO:0000313|Proteomes:UP000189211};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        327..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          13..274
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          360..425
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          428..494
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          497..564
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   BINDING         42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   679 AA;  74954 MW;  B684F9D801BA26CE CRC64;
     MLLEPGRLLG DRYTIISKIG AGATSIVYKA EDNRLKRFVA IKILKGELSI DKEFVKKFHG
     EALSVASLSH TNIVGVYDVG NDKELNYIVM EYIKGSTLKD LIGKEAPFTE QRTIDYAIQI
     LTGLKEAHQK NIIHRDIKPQ NIMVTEDGIL KVTDFGIAKA VNTSTIVLNG DAYGSVHYFS
     PEQAKGRHSS ETSDLYSCGI ILFEMITKQL PFESDNHVTI AIKHINDPLP KPSIYNSYIS
     SALEEVIIKA TNKSTSMRFE SADSMIFALQ HAKTNPNTVL QNDDFLSQTI LATPDEVNSD
     NLMTQGLYNE SQSLEGNKEV LSTVSKWVAI VSGISVTLVL LAVIVLMFFF FKKPADGVVK
     SQEVPNLIGK TIEQAGEIAG ESLFLVEQVG ERETTTAKEG TIIEQMPDSN STLVPNSTIQ
     VVLAITPEDT SVKVPDVISL DNAKAQTLIE ESGLLFTIER ETSNYVEIGK VIDQHPKGNT
     TLNKGDVVEL VVSLGAGQKY IIMPNLYGLS INNATSTLAS YGLSLGDIDH EYSNTDDVGI
     VIYQSIPANR NIDPSTKIDI SVSLGPEPVS IVDDLEETLE EILQEPEEEF NLDDIEQDIM
     IAIPKMYNIK LPEQLAEDET KTTVHVLVTF QSDEGERTMF DSVVDKDQFP YAISLTGQGE
     GTLVVYFDSQ AWWKDPFKF
//
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