ID F0LMF4_THEBM Unreviewed; 637 AA.
AC F0LMF4;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=ChlI-like cobalt chelatase {ECO:0000313|EMBL:ADT85177.1};
GN OrderedLocusNames=TERMP_02203 {ECO:0000313|EMBL:ADT85177.1};
OS Thermococcus barophilus (strain DSM 11836 / MP).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=391623 {ECO:0000313|EMBL:ADT85177.1, ECO:0000313|Proteomes:UP000007478};
RN [1] {ECO:0000313|EMBL:ADT85177.1, ECO:0000313|Proteomes:UP000007478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11836 / MP {ECO:0000313|Proteomes:UP000007478};
RX PubMed=21217005; DOI=10.1128/JB.01490-10;
RA Vannier P., Marteinsson V.T., Fridjonsson O.H., Oger P., Jebbar M.;
RT "Complete genome sequence of the hyperthermophilic, piezophilic,
RT heterotrophic, and carboxydotrophic archaeon Thermococcus barophilus MP.";
RL J. Bacteriol. 193:1481-1482(2011).
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.
CC {ECO:0000256|ARBA:ARBA00005799}.
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DR EMBL; CP002372; ADT85177.1; -; Genomic_DNA.
DR RefSeq; WP_013468473.1; NC_014804.1.
DR AlphaFoldDB; F0LMF4; -.
DR GeneID; 10042518; -.
DR KEGG; tba:TERMP_02203; -.
DR PATRIC; fig|391623.17.peg.2198; -.
DR eggNOG; arCOG00438; Archaea.
DR HOGENOM; CLU_016684_5_0_2; -.
DR OrthoDB; 25914at2157; -.
DR Proteomes; UP000007478; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.80; Magnesium chelatase subunit I, C-Terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041628; ChlI/MoxR_AAA_lid.
DR InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR43473; MAGNESIUM-CHELATASE SUBUNIT CHLD, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43473:SF2; MAGNESIUM-CHELATASE SUBUNIT CHLD, CHLOROPLASTIC; 1.
DR Pfam; PF17863; AAA_lid_2; 1.
DR Pfam; PF01078; Mg_chelatase; 1.
DR Pfam; PF13519; VWA_2; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007478}.
FT DOMAIN 470..606
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 320..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 637 AA; 71578 MW; 32F8C23139F6DA11 CRC64;
MEPREKRLVF PFSAIVGQEK AKLALLCVAV NPLIGGVLLK GDKGTGKSTL VRALANVLPE
IEVVDGCPFN CNPRNPLEMC DSCYERYERG EELPVAKRKM RVVDLPLSVT IDRLVGTVDV
ERFLKEGKKA LQPGILAEAN RNVLYIDEVN LLDDYIADSL LDAAAMGWNT IEREGISFRH
PARFILIGSM NPEEGELRPQ ILDRFGLCVE VSAPMNPEER IEIVKRVEEF HEDPISFYKK
FESEENKLTE RVVKAREILP KIEISDDLLK LLAETVVNLG IKTNRAEIAT IKTAKAIAAL
NGRRRVSLED LEKAMELALP HRLRDKPFQK PPQMRPPKPK EDKEHNHDHK HNHKHEHKKE
EKSESTRSQG IGNLEQNFRS SEAKIPRIES KNFGSNDFTG YRSSRDASVT VINFPRGVPV
SYLPPTNGKI KDVDFYSSLV WAVLNGKKPP IRLDLKDVRV RVRKAKAPTL WVLLLDSSGS
MAVQKRISIA KGIAEKLVEN GYIKKSKVAL IVAKGSQAEI FVPPTKNYLK VLDAIENVPT
GGRTPLSSAL YNLLLLAERE RRKDKSLKVR AFLITDGKAN VPLFGKRIKD EIIELAKALR
RKEIELNIYD TRGGGINPGI SYVSLLKEVA KAKVYRA
//
