ID A0A327YQ39_9BACI Unreviewed; 436 AA.
AC A0A327YQ39;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=DEAD-box ATP-dependent RNA helicase CshB {ECO:0000256|HAMAP-Rule:MF_01494};
DE EC=3.6.4.13 {ECO:0000256|HAMAP-Rule:MF_01494};
GN Name=cshB {ECO:0000256|HAMAP-Rule:MF_01494};
GN ORFNames=B0I26_102411 {ECO:0000313|EMBL:RAK22416.1};
OS Anoxybacillus vitaminiphilus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=581036 {ECO:0000313|EMBL:RAK22416.1, ECO:0000313|Proteomes:UP000248555};
RN [1] {ECO:0000313|EMBL:RAK22416.1, ECO:0000313|Proteomes:UP000248555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.8979 {ECO:0000313|EMBL:RAK22416.1,
RC ECO:0000313|Proteomes:UP000248555};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable DEAD-box RNA helicase. May work in conjunction with
CC the cold shock proteins to ensure proper initiation of transcription at
CC low and optimal temperatures. {ECO:0000256|HAMAP-Rule:MF_01494}.
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_01494};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01494}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. CshB subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01494}.
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:RAK22416.1}.
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DR EMBL; QLMH01000002; RAK22416.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A327YQ39; -.
DR OrthoDB; 9805696at2; -.
DR Proteomes; UP000248555; Unassembled WGS sequence.
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:0009409; P:response to cold; IEA:InterPro.
DR GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00268; DEADc; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_01494; DEAD_helicase_CshB; 1.
DR InterPro; IPR030881; CshB.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR47963; DEAD-BOX ATP-DEPENDENT RNA HELICASE 47, MITOCHONDRIAL; 1.
DR PANTHER; PTHR47963:SF1; DEAD-BOX ATP-DEPENDENT RNA HELICASE CSHB; 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; 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_01494}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01494};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01494};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01494};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01494}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_01494};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_01494}.
FT DOMAIN 4..32
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 35..209
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 236..389
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT MOTIF 4..32
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
SQ SEQUENCE 436 AA; 50425 MW; DBBF1DC49BAC9493 CRC64;
MEQTLFERFN LKPFIIEAVK YLQFYKPTEI QERIIPSIIR GESVIGQSQT GTGKTHAYLL
PIIERIDPKL DEVQAVITAP TRELATQIYH EILKITKFCS EEEQITARCF VGGTDKLRTI
EKLKVQPHIA VGTPGRINDL AKEQALNVHT AKTLVIDEAD LMLDMGFIYD VDQIAARMPK
ELQMLVFSAT IPEKLKPFLR KYMENPKYIH VAPKQVAAEK IEHVLVPLRH RDKVKLLHDM
LLLYNPYLAI VFTNTKKMAD EVAEALSEKG LKVGILHGDL TPRERKKMIK QIRDLEFQYI
VATDLAARGI DIEGVSHVIN YELPRDLEFY VHRVGRTARA GYSGIAATIY EPSDQDALTK
LEKMGIEFVH RDIVRDEWVD LPEWNKRSKR KKEDNEIEQI IKKTVKKSKK VKPGYKKKLK
EEIEKQKKRL LRLKRK
//
