ID A0A3P1ZI99_9BACT Unreviewed; 620 AA.
AC A0A3P1ZI99;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 02-APR-2025, entry version 24.
DE SubName: Full=DEAD/DEAH box helicase {ECO:0000313|EMBL:RRD80843.1};
GN ORFNames=EII14_00615 {ECO:0000313|EMBL:RRD80843.1};
OS Alloprevotella sp. OH1205_COT-284.
OC Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
OC Prevotellaceae; Alloprevotella.
OX NCBI_TaxID=2491043 {ECO:0000313|EMBL:RRD80843.1, ECO:0000313|Proteomes:UP000272376};
RN [1] {ECO:0000313|EMBL:RRD80843.1, ECO:0000313|Proteomes:UP000272376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OH1205_COT-284 {ECO:0000313|EMBL:RRD80843.1,
RC ECO:0000313|Proteomes:UP000272376};
RA Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA Eisen J.A., Holcombe L.J., O'Flynn C.;
RT "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT for Automated Genome-Based Taxonomic Assignment.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC {ECO:0000256|ARBA:ARBA00038437, ECO:0000256|RuleBase:RU000492}.
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:RRD80843.1}.
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DR EMBL; RQYI01000001; RRD80843.1; -; Genomic_DNA.
DR RefSeq; WP_124930634.1; NZ_RQYI01000001.1.
DR AlphaFoldDB; A0A3P1ZI99; -.
DR OrthoDB; 9785240at2; -.
DR Proteomes; UP000272376; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR CDD; cd00268; DEADc; 1.
DR CDD; cd12252; RRM_DbpA; 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 InterPro; IPR005580; DbpA/CsdA_RNA-bd_dom.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR050079; DEAD_box_RNA_helicase.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C-like.
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; PTHR47959:SF13; ATP-DEPENDENT RNA HELICASE RHLE; 1.
DR PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 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|RuleBase:RU000492};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000492};
KW Reference proteome {ECO:0000313|Proteomes:UP000272376}.
FT DOMAIN 2..30
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 40..211
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 241..383
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 447..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2..30
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 450..463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 620 AA; 70383 MW; 45D5E05A7E248507 CRC64;
MKTFAELGVK DEILTAISEI GYASPTPVQE AVIPCLLHND ESNTPQNDII ALAQTGTGKT
AAYGLPVLHN IDADDRTTQA VILSPTRELC LQIADDLKDY SRYIDGLHVA AVYGGTSIEG
QIRQLKKGCQ VIVATPGRLI DLMNRGVARL ENVKNIVLDE ADEMLNMGFT ESIDEILAGM
PEERQTLLFS ATMGPAIERI AKSYLKEYRE IVVGSRNEGA EHVNHVYYMV KAQDKYHALK
RIVDYYPRIY AIVFCRTRME TQEVADQLIK DGYNAEALHG DLAQAQRDLT MQKFRQHRTQ
LLVATDVAAR GLDVEELTHV INYGLPDDVE NYTHRSGRTG RAGKRGTSIS IIHLREKSKV
KLIEKVIGKK FEAGLLPDPK EICTKQLYKV IDELEHVDVD EEQIAPFLLE VTHKLEWLSK
EDLIKRIVQS EFGRFANYYA NAPQIVQPSE RPEKESAKGG ERPKRQRNAN GEHVAEEGYK
RLFLNFGKRD NFFAREIINL LNRYIKGKVE IGRIDLLPNC SFFEVPEEDA EMVIRKMAKA
KVGERRVVVD SADKSEHERA EDKQRRQNNK RRTEHSRNGK QNAEGGNGAK DKKKNRKGTE
KDFATPSKKY GKDDWRQFFD
//
