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Database: UniProt
Entry: Q6AQR1_DESPS
LinkDB: Q6AQR1_DESPS
Original site: Q6AQR1_DESPS 
ID   Q6AQR1_DESPS            Unreviewed;       254 AA.
AC   Q6AQR1;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   SubName: Full=Probable hydrogenase accessory protein HypB {ECO:0000313|EMBL:CAG35312.1};
GN   Name=hypB {ECO:0000313|EMBL:CAG35312.1};
GN   OrderedLocusNames=DP0583 {ECO:0000313|EMBL:CAG35312.1};
OS   Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC   Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC   Desulfocapsaceae; Desulfotalea.
OX   NCBI_TaxID=177439 {ECO:0000313|EMBL:CAG35312.1, ECO:0000313|Proteomes:UP000000602};
RN   [1] {ECO:0000313|Proteomes:UP000000602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12343 / LSv54 {ECO:0000313|Proteomes:UP000000602};
RX   PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA   Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA   Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA   Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT   "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT   permanently cold Arctic sediments.";
RL   Environ. Microbiol. 6:887-902(2004).
CC   -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. HypB/HupM
CC       subfamily. {ECO:0000256|ARBA:ARBA00006211}.
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DR   EMBL; CR522870; CAG35312.1; -; Genomic_DNA.
DR   RefSeq; WP_011187828.1; NC_006138.1.
DR   AlphaFoldDB; Q6AQR1; -.
DR   STRING; 177439.DP0583; -.
DR   KEGG; dps:DP0583; -.
DR   eggNOG; COG0378; Bacteria.
DR   HOGENOM; CLU_056148_0_0_7; -.
DR   OrthoDB; 9802035at2; -.
DR   Proteomes; UP000000602; Chromosome.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR   GO; GO:0051604; P:protein maturation; IEA:InterPro.
DR   CDD; cd05390; HypB; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003495; CobW/HypB/UreG_dom.
DR   InterPro; IPR004392; Hyd_mat_HypB.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00073; hypB; 1.
DR   PANTHER; PTHR30134:SF2; HYDROGENASE MATURATION FACTOR HYPB; 1.
DR   PANTHER; PTHR30134; HYDROGENASE PROTEIN ASSEMBLY PROTEIN, NICKEL CHAPERONE; 1.
DR   Pfam; PF02492; cobW; 1.
DR   PIRSF; PIRSF005624; Ni-bind_GTPase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nickel {ECO:0000256|ARBA:ARBA00022596};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000602};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          63..222
FT                   /note="CobW/HypB/UreG nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02492"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   254 AA;  28136 MW;  262D3C58B87D6E1B CRC64;
     MCTTCGCPSP SDTAHSHDHD HDHDHSHTHK TVDVHTSLFA ANDALAKMNR EHFNEIGAVA
     LNLISSPGSG KTTLLEHTIE ALKGEIKIGV IEGDIETERD ADRIRAKGVP VVQLTTGGAC
     HLDAAMTHKG FHRLEKEPGY ETVDLLFIEN VGNLVCPCSF DLGEHERVVL VSVPEGPDKP
     AKYPKAFTSS DTFVITKTDL LPYFDFPVEE ARAEALHLNH HLRTMELCAT KQDEGFQQWL
     DYLRELVAKK RGLK
//
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