ID A0A1U7P1Y6_9DEIO Unreviewed; 549 AA.
AC A0A1U7P1Y6;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=ChlI component of cobalt chelatase involved in B12 biosynthesis {ECO:0000313|EMBL:OLV19176.1};
GN ORFNames=BOO71_0003604 {ECO:0000313|EMBL:OLV19176.1};
OS Deinococcus marmoris.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=249408 {ECO:0000313|EMBL:OLV19176.1, ECO:0000313|Proteomes:UP000186607};
RN [1] {ECO:0000313|EMBL:OLV19176.1, ECO:0000313|Proteomes:UP000186607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KOPRI26562 {ECO:0000313|EMBL:OLV19176.1,
RC ECO:0000313|Proteomes:UP000186607};
RA Kim J.H., Oh H.-M.;
RT "Genome Analysis of Deinococcus marmoris KOPRI26562.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.
CC {ECO:0000256|ARBA:ARBA00005799}.
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:OLV19176.1}.
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DR EMBL; MSTI01000040; OLV19176.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U7P1Y6; -.
DR STRING; 249408.BOO71_0003604; -.
DR Proteomes; UP000186607; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
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; IPR011704; ATPase_dyneun-rel_AAA.
DR InterPro; IPR041628; ChlI/MoxR_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR35023; CHELATASE-RELATED; 1.
DR PANTHER; PTHR35023:SF1; MG-PROTOPORPHYRIN IX CHELATASE; 1.
DR Pfam; PF07728; AAA_5; 1.
DR Pfam; PF17863; AAA_lid_2; 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;
FT DOMAIN 389..549
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 266..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..302
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 549 AA; 57746 MW; EBBF9E3C2B9E8175 CRC64;
MALSLLAVAP SVGGLLIRGD RGAAKSTAAR GLAALLPQEG GHSAPFVNLP LGATEDRVVG
TLDLDAALRG EARLKHGLMV QAHGGLLYID EVNLLPDHLV DVLLDAAALG VVRVERDGLS
AAARADFALI GSMNPEEGSL RPQFMDRFGL CVDVQAPTDP RQRAEIVRRR MRFETDSQGF
TEQWQAEELR LRERLQAARL LFPSVHLPDA LLSQIAGLSA AAQVRSLRAD LVMHRAARAF
AALEGRSEVS KADIERVAPL VLLHRRDPRL PPPFPSPTSQ HPPGNPEPEA GQPPPPPDFN
PQAEEIFAPT SNAAPLPVLV GKGAASSGSS LGEQPGRVIR SVPTSPQSNA PLHLPDTLKA
ALGRNLGGEF KLTSDDLRSA IHEPVGGRRV LFVVDASGSM GVAGRMGALK GTLLGVLNDK
ARRDRAALIV FRGTGAALAL PWTTDAAEAE AVIAAVPTGG RTPLAHALEL AAELVNAESS
AELVIFTDGR ANVPLTAGSD AWTDALHAAQ ALKNVSALVV DTETGRIRLG RAAQLAEVLG
ARYSVLETL
//
