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Database: UniProt
Entry: G2E3N3_9GAMM
LinkDB: G2E3N3_9GAMM
Original site: G2E3N3_9GAMM 
ID   G2E3N3_9GAMM            Unreviewed;      1335 AA.
AC   G2E3N3;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=ATP-dependent helicase HrpA {ECO:0000313|EMBL:EGV30146.1};
GN   ORFNames=ThidrDRAFT_2896 {ECO:0000313|EMBL:EGV30146.1};
OS   Thiorhodococcus drewsii AZ1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thiorhodococcus.
OX   NCBI_TaxID=765913 {ECO:0000313|EMBL:EGV30146.1, ECO:0000313|Proteomes:UP000004200};
RN   [1] {ECO:0000313|EMBL:EGV30146.1, ECO:0000313|Proteomes:UP000004200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AZ1 {ECO:0000313|EMBL:EGV30146.1,
RC   ECO:0000313|Proteomes:UP000004200};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V.,
RA   Frigaard N.-U., Bryant D.A., Woyke T.J.;
RT   "The draft genome of Thiorhodococcus drewsii AZ1.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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:EGV30146.1}.
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DR   EMBL; AFWT01000020; EGV30146.1; -; Genomic_DNA.
DR   RefSeq; WP_007041609.1; NZ_AFWT01000020.1.
DR   STRING; 765913.ThidrDRAFT_2896; -.
DR   PATRIC; fig|765913.3.peg.2961; -.
DR   eggNOG; COG1643; Bacteria.
DR   OrthoDB; 9805617at2; -.
DR   Proteomes; UP000004200; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR048333; HA2_WH.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR024590; HrpA_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010222; RNA_helicase_HrpA.
DR   NCBIfam; TIGR01967; DEAH_box_HrpA; 1.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF83; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE DHX16; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF11898; DUF3418; 1.
DR   Pfam; PF21010; HA2_C; 1.
DR   Pfam; PF04408; HA2_N; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 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.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000313|EMBL:EGV30146.1};
KW   Hydrolase {ECO:0000313|EMBL:EGV30146.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          89..252
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          281..452
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1335 AA;  150992 MW;  3EC162FE85630A10 CRC64;
     MTAVLPDASQ FPTEADLDAC LIRDRHGARA RLRGLRKRQR AGQPFDQGLA KLWQDIQRSR
     SILEQRRASI PEIQYPPELP VSERRDEVAE LIERHQVVIL CGETGSGKST QLPKICLDLG
     RGIAGRIGHT QPRRIAARTL AGRVAQELGA ETGGLVGYKV RFHDQVRPET AIKLMTDGML
     LAEIQQDRFL TEYDTLIIDE AHERSLNIDF LLGYLRGILP KRPDLKVIVT SATIDPERFA
     RHFAGAQGDP APVIEISGRT YAVEVRYRPP EEESAAERDD AMQQAISDAV GELAHSGPGD
     VLVFLSGERE IRETAETLRK HHPPSTEVLP LFARQGPQEQ ARIFHSHSTR RVVLATNVAE
     TSLTVPGIHY VIDPGFARIS RYSHRTKVQR LPVERVSQAS ANQRKGRCGR VASGICIRLY
     SEDNFTSRAE FTEPEISRTN LASVILQMKL LGFGAIERFP FVDPPDTRLV SDGYRTLEEL
     GAIDDKGDLT QLGRQLARLP VDPRIGRMLL AATEHRCLEE VLVIAAALSV QDPRERPLDK
     QQAADEIHAT FADEDSDFLT YLNLWRFIEQ ERKALSRNKF IKLCQRHFLS WNRVQEWRDI
     HAQLREQMLE MGFQLSAASH QPPAQKLQAQ AGDWKLEADS SEKIHRALLA GLLGNIGFRE
     AEREFQGARN SRFFVHPSSA LFAKPPKWVM VAERVETTRQ YGRIAAKIQP AWVEEAGRHL
     IQRSYSEPHW QAKSGQVAAF EKVMLYGVTL VPKRRVNYGP INPAESREIF LRFALAEGDF
     DTRAPFWRHN RELVESIHHL EAKSRRRDIL VDEESIYAFY AERVPSGIYS KPLFEQWLKT
     ASRKDPKILH MRMSDLMRHE AADITQQAFP DSLQVGATAL PLEYHFDPGH TADGVTLVVP
     LPLINQVSPD RLEWLVPGLI EERIIALLRG LPKQLRKSFV PIPDTAARLA ARLVPSDRPL
     IQALGEEVKA MTGIQIPEDA WDASDIPEHL RMKIRLVDES GKRLAVGDDP VRLKRQFGEQ
     AQEGFAHIPT SGLEREGVTR WDFGDLPEHV DLTRAGIRLR GFPALVDRGD CVAIQVLDSA
     ESAALAQRDG LRRLFMLHLG PDLRRLRKDL PNLDRMRLQY AKAPKPPGGV STASSGGGKE
     PDLADELVAL ALDLTFVEDL HPIRGQSVFE QRLAGRKSHL FATAKEVGVL IGGILASYQS
     LRKRLATITQ VNWMPSVMDM RDQLDALVFR GFTQRVPYRR LKEYPRYLKA IEQRIERLGH
     APGRDRQWMA EMAEVHTRWR ERDKAAQAAG RQDPRLEEIR WLLEELRVSL FAQQLGTPVP
     VSIKRLQGRW RELGL
//
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