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SRMB_HAEIN
ID   SRMB_HAEIN              Reviewed;         439 AA.
AC   P44701;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=ATP-dependent RNA helicase SrmB {ECO:0000255|HAMAP-Rule:MF_00967};
DE            EC=3.6.4.13 {ECO:0000255|HAMAP-Rule:MF_00967};
GN   Name=srmB {ECO:0000255|HAMAP-Rule:MF_00967}; OrderedLocusNames=HI_0422;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: DEAD-box RNA helicase involved in the assembly of the 50S
CC       ribosomal subunit at low temperature. Exhibits RNA-stimulated ATP
CC       hydrolysis and RNA unwinding activity. {ECO:0000255|HAMAP-
CC       Rule:MF_00967}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00967};
CC   -!- SUBUNIT: Interacts with the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00967}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00967}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. SrmB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00967}.
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DR   EMBL; L42023; AAC22078.1; -; Genomic_DNA.
DR   PIR; H64066; H64066.
DR   RefSeq; NP_438583.1; NC_000907.1.
DR   RefSeq; WP_005693742.1; NC_000907.1.
DR   AlphaFoldDB; P44701; -.
DR   SMR; P44701; -.
DR   STRING; 71421.HI_0422; -.
DR   EnsemblBacteria; AAC22078; AAC22078; HI_0422.
DR   KEGG; hin:HI_0422; -.
DR   PATRIC; fig|71421.8.peg.442; -.
DR   eggNOG; COG0513; Bacteria.
DR   HOGENOM; CLU_003041_28_3_6; -.
DR   OMA; YDIELYQ; -.
DR   PhylomeDB; P44701; -.
DR   BioCyc; HINF71421:G1GJ1-437-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 2.
DR   HAMAP; MF_00967; DEAD_helicase_SrmB; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR028621; DEAD_helicase_SrmB.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Helicase; Hydrolase; Nucleotide-binding;
KW   Reference proteome; Ribosome biogenesis.
FT   CHAIN           1..439
FT                   /note="ATP-dependent RNA helicase SrmB"
FT                   /id="PRO_0000055110"
FT   DOMAIN          35..209
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00967"
FT   DOMAIN          237..387
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00967"
FT   REGION          381..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           4..32
FT                   /note="Q motif"
FT   MOTIF           157..160
FT                   /note="DEAD box"
FT   COMPBIAS        381..414
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        415..429
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         48..55
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00967"
SQ   SEQUENCE   439 AA;  49805 MW;  7543942CE35B20C4 CRC64;
     MNLSQFEQFD LSPELLKALE KKGYSRPTAI QMEAIPAAME ESDVLGSAPT GTGKTAAFLL
     PALQHLLDYP RRKPGPPRIL VLTPTRELAM QVAEQAEELA QFTHLNIATI TGGVAYQNHG
     DVFNTNQDLV VATPGRLLQY IKEENFDCRS VEMLIFDEAD RMLQMGFGQD AEKIAAETRW
     RKQTLLFSAT LEGELLVDFA ERLLNDPVKV DAEPSRRERK KINQWYYHAD SNEHKIKLLA
     RFIETEEVTR GIVFIRRRED ARELSETLRK RGIRSAYLEG EMAQTQRNNA IDKLKSGIVT
     VLVATDVAAR GIDIDDVSHV MNFDLPYSAD TYLHRIGRTA RAGKKGTAVS FVEAHDYKLL
     GKIKRYTEEI LKARILAGLE PRTKPPKDGE VKSVSKKQKA RIKEKREEKK KTEAKKKVKL
     RHKDTKNIGK RRKPSNSNV
 
 
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