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Database: UniProt
Entry: A0A077HK74_9CORY
LinkDB: A0A077HK74_9CORY
Original site: A0A077HK74_9CORY 
ID   A0A077HK74_9CORY        Unreviewed;       698 AA.
AC   A0A077HK74;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=ATP-dependent RNA helicase DeaD {ECO:0000256|HAMAP-Rule:MF_00964};
DE            EC=3.6.4.13 {ECO:0000256|HAMAP-Rule:MF_00964};
DE   AltName: Full=Cold-shock DEAD box protein A {ECO:0000256|HAMAP-Rule:MF_00964};
GN   Name=deaD {ECO:0000256|HAMAP-Rule:MF_00964};
GN   Synonyms=csdA {ECO:0000256|HAMAP-Rule:MF_00964};
GN   ORFNames=CUREI_04880 {ECO:0000313|EMBL:AIL96710.1};
OS   Corynebacterium ureicelerivorans.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=401472 {ECO:0000313|EMBL:AIL96710.1, ECO:0000313|Proteomes:UP000028939};
RN   [1] {ECO:0000313|EMBL:AIL96710.1, ECO:0000313|Proteomes:UP000028939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMMIB RIV-2301 {ECO:0000313|EMBL:AIL96710.1,
RC   ECO:0000313|Proteomes:UP000028939};
RA   Tippelt A., Albersmeier A., Brinkrolf K., Ruckert C., Tauch A.;
RT   "Complete genome sequence of Corynebacterium ureicelerivorans DSM 45051, a
RT   lipophilic and urea-splitting isolate from a blood culture of a septicaemia
RT   patient.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DEAD-box RNA helicase involved in various cellular processes
CC       at low temperature, including ribosome biogenesis, mRNA degradation and
CC       translation initiation. {ECO:0000256|HAMAP-Rule:MF_00964}.
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:0000256|HAMAP-Rule:MF_00964};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00964}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DeaD/CsdA
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00964}.
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DR   EMBL; CP009215; AIL96710.1; -; Genomic_DNA.
DR   RefSeq; WP_038611015.1; NZ_CP009215.1.
DR   AlphaFoldDB; A0A077HK74; -.
DR   STRING; 401472.CUREI_04880; -.
DR   KEGG; cuv:CUREI_04880; -.
DR   HOGENOM; CLU_003041_21_1_11; -.
DR   Proteomes; UP000028939; 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:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070417; P:cellular response to cold; IEA:InterPro.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00268; DEADc; 1.
DR   CDD; cd12499; RRM_EcCsdA_like; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   HAMAP; MF_00964; DEAD_helicase_DeaD; 1.
DR   InterPro; IPR034415; CsdA_RRM.
DR   InterPro; IPR005580; DbpA/CsdA_RNA-bd_dom.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR028618; DEAD_helicase_DeaD.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   PANTHER; PTHR47963:SF8; ATP-DEPENDENT RNA HELICASE DEAD; 1.
DR   PANTHER; PTHR47963; DEAD-BOX ATP-DEPENDENT RNA HELICASE 47, MITOCHONDRIAL; 1.
DR   Pfam; PF03880; DbpA; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00964}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00964};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_00964};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00964};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00964}; Reference proteome {ECO:0000313|Proteomes:UP000028939};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00964};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW   Rule:MF_00964}.
FT   DOMAIN          97..125
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          128..299
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          326..470
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          525..573
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          645..698
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           97..125
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        1..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..102
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        527..573
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        653..698
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   698 AA;  77218 MW;  FF6EF35137577B28 CRC64;
     MSNSENATGG ENEPDMNVSE NQENPQDVAA EIVEAVAEDT RDAGVSDQTG AADAVAIEEN
     NDVLKLSDEP SAEPSADKAP EPASEQEAPA EKAEPENGFE KLDLPDAVVE AVKRVGFEQP
     SPIQAQTIPL LMQGRDVVGL AQTGTGKTAA FALPVLSQID PDKRYPQALV LAPTRELALQ
     VSDSFQSFAD HLGGVHILPI YGGQAYGIQL SGLRRGAQVI VGTPGRVIDH LEKGSLDISN
     LEFLVLDEAD EMLNMGFQED VERILEDTPE TKQVALFSAT MPNAIRRISR DYLNNPEEVT
     VKSETRTNTN ITQRYLFTAH RNKLDAITRI LEVTEFEAMI VFVRTKNETE EIAEKLRARG
     FSAAAINGDI AQQQRERTVD QLRDGRLDIL VATDVAARGL DVERISHVLN YDIPNDTESY
     VHRIGRTGRA GRTGEAILFV TPRERRMLRS IERVTNATIE EMDLPTVDEV NESRKAKFMD
     SITESLEATD IQVFKTMVRE YSAANNVPMD DIAAALATQA LAGDEFLMKE PPRDKRDRRD
     RFDRDDRRDR GGRGRDRFDR DDRGDRRGGR RFDDSGNFDT YRLDVGKRQH VRPGAIVGAL
     ANEGGLNSKD FGRITIGGDF TLVELPKNLD QSVLDRLEDT RISGQLINIQ RDHGAPPRDR
     GGRGGYRGGR GRDDDRGGRG RGRGGYRGGR GRDRYDRG
//
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