ID A0A0F5AU78_9GAMM Unreviewed; 654 AA.
AC A0A0F5AU78;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=ATP-dependent helicase {ECO:0000313|EMBL:KKA46085.1};
GN ORFNames=WN56_02990 {ECO:0000313|EMBL:KKA46085.1};
OS Salinivibrio sp. KP-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Salinivibrio.
OX NCBI_TaxID=1406902 {ECO:0000313|EMBL:KKA46085.1, ECO:0000313|Proteomes:UP000033449};
RN [1] {ECO:0000313|EMBL:KKA46085.1, ECO:0000313|Proteomes:UP000033449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KP-1 {ECO:0000313|EMBL:KKA46085.1,
RC ECO:0000313|Proteomes:UP000033449};
RA Kaur G., Kumar A., Mathan Kumar R., Kumar N., Singh N.K., Arora A.,
RA Kaur N., Bala M., Mayilraj S.;
RT "Taxonomic description and genome sequence of Salinivibrio halophilus sp.
RT nov., a novel halotolerant gammaproteobacterium isolated from marine
RT sediment and emended description of the genus Salinivibrio.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the helicase family. DinG subfamily.
CC {ECO:0000256|ARBA:ARBA00038058}.
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:KKA46085.1}.
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DR EMBL; LAQR01000001; KKA46085.1; -; Genomic_DNA.
DR RefSeq; WP_046073541.1; NZ_LAQR01000001.1.
DR AlphaFoldDB; A0A0F5AU78; -.
DR PATRIC; fig|1406902.3.peg.629; -.
DR OrthoDB; 9805194at2; -.
DR Proteomes; UP000033449; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR PANTHER; PTHR11472:SF47; FANCONI ANEMIA GROUP J PROTEIN; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000313|EMBL:KKA46085.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000033449}.
FT DOMAIN 11..275
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT REGION 635..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 654 AA; 72838 MW; FD214FFCF67CE628 CRC64;
MIRKVFSDTG ALAKAIDGFV PRQPQTDMAI AVDAAIRDQG QLVVEAGTGT GKTYAYLAPV
LLSGKKAIIS TGSKNLQEQL YHRDLPLMKS ALGYTGTTAL LKGRVNYLCP ERLERQISEC
HRPDSEPGQL SQLVKIREWS SYTESGDLSE CDALAEDSPL IPVVTSTNDN CLGKDCPSYE
DCYVVKARRR AMDADVVVVN HHLFLADVAI KETGFGELIP EADVMVFDEA HQLPDIASQY
FGQSLSSRQL QDVAKDIHIA YRTELRDTRQ LEKVADRLSQ AAMDMRLVMG EPGYRGNWRE
LQTSPSVEKE LVRLSDALDL AHDVVKLSLG RSQLLDAAFD RITLFKARLA RLKDTSITGY
SYWYECTRHH FSLNITPLSV ADRFREQMAE QGGAWIFTSA TLAVEGDFAH FNHRLGIDAK
QQMTLESPFD YPNQARLCVP RHVPETNSFR RANKLAALLG PVIERNQGRC FFLCTSHQMV
RELSALFREQ LSLPVLMQGE MPKQRLLAEY LSLGNALLVA TGAFWEGIDV RGQALSCVII
DKLPFASPDD PLLKARIEDC KLQGGDPFAQ VQIPEAVITL KQGVGRLIRD QQDFGALVIC
DNRLVTRAYG ATFLRSLPAI PRTRDLHHID DFLSGSDTDS NTMQSHLLDQ PIEG
//