ID K9EGW0_9ACTO Unreviewed; 1460 AA.
AC K9EGW0;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=ATP-dependent helicase HrpA {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF9233_00655 {ECO:0000313|EMBL:EKU95868.1};
OS Actinobaculum massiliense ACS-171-V-Col2.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinobaculum.
OX NCBI_TaxID=883066 {ECO:0000313|EMBL:EKU95868.1, ECO:0000313|Proteomes:UP000009888};
RN [1] {ECO:0000313|EMBL:EKU95868.1, ECO:0000313|Proteomes:UP000009888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-171-V-Col2 {ECO:0000313|Proteomes:UP000009888};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., Vaneechoutte M.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Actinobaculum massiliae ACS-171-V-COL2.";
RL Submitted (SEP-2012) 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:EKU95868.1}.
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DR EMBL; AGWL01000002; EKU95868.1; -; Genomic_DNA.
DR RefSeq; WP_007000861.1; NZ_JH992955.1.
DR STRING; 202789.GCA_001457435_01477; -.
DR PATRIC; fig|883066.3.peg.673; -.
DR eggNOG; COG1643; Bacteria.
DR HOGENOM; CLU_001832_3_3_11; -.
DR Proteomes; UP000009888; 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 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; 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 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; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000009888}.
FT DOMAIN 58..221
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 294..477
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1105..1136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1460 AA; 161542 MW; EB79E83EE84C8ECB CRC64;
MGMNKENSHH QSKKRGRRPR RHAPRAFSEK QIAQRRASLP AITYPEELPV SARREDIKKA
IAENQVVIVA GETGSGKTTQ LPKICLELGR GIEKLIGHTQ PRRIAARSVA ERIAHELGQS
VGETIGFQVR FTEDVSQNTL VKLMTDGILL NEIQSDPQLL RYDTLIIDEA HERSLNIDFI
LGYLARLLPQ RPDLKIIITS ATIDTERFAK HFGEHSYRGR KGASAPIIEV SGRTYPVEIR
YRPLDDNAVD ASGAGDNSAF STTPSRTGDN SAKVMRATAN PSPRTPGRAS AKDQIDGIIE
AAEELMSEGA GDILVFLSGE GEIRDTLHAF QDELGPKFVG PGEKSSLPGA IEVLPLFGRM
SNQEQNRIFH PGQLPRIILA TNIAETSITV PRIKYVIDPG TARISRYSNK TKVQRLPIEP
ISQASANQRS GRSGRVQDGI TIRLYSEEDF LARPEFTQPE IQRTSLASVI LQMLSLGLGS
VEEFPFIDPP EQRAVRAGVQ LLEEIGAITG GPAPRLTHIG RQLARLPIDP RLGRMLIEAD
KNGCASEVLV LVAALSVQDV RERPTEKRQQ ADQYHARFNA ASSDFLTYLT IWRYLRTQQR
ELSGTAFRRL MRAEFLNYLR FREWLDVVHQ LEEMARPLRL RVRRLPIPSH ADVRRAIEER
KGGGHPGGEP NAAAVAEACR EFGRSTDTPE AGAIHRSLLV GLLSNIGNYR ERTRDYEGAR
GTHFVIWPGS GLHRRTPAWV MAAELVETSR LFARTVAAIK PEWIEPLASS LVKRSYSDPY
WSIKNGAAMC KEKVTLYGLT LVADRPVLLS STGTPGANAL AREMFIEHAL VNGEWHSHQK
FMERNRQALA EAADTESKLR VRGLVADERA LAMFYDERIP DSIVSAAHFN SWWKDERQRH
GKLLDFTQEF LLGGRSAGAE DFPSQLRQGE LTFDAEYSFA PNSHSDGITL DIPVSILPQV
TEAGFDWLVP GMLDDLVIGT IRALPKRVRR QLVPAPDVAR ELRALLPEWS EVAGGRPGAP
TFREAFTGAV ERLRGFQIND AAWDELDLPD YLQMHFRIRS ERGAVLDESN SLERLKHDLA
PSTKKAVESV VAGAVAQALD EARRKLEAGG RSRDAKNPRV STSSDHSANS SRSDHSAAFS
LTDNSANFAV AAGLVSRGSE ALNDWPNDLT DGMIPAVMET SGPHGSVVRA YPALVVRGEE
VFLDVLASPG EQVRAHSSGV VQLLTRSLAL PEARITSRWD GDLALKLAAS PARSTAALVA
DLQWAAARNL AERWGNSNDT SPAELRSGED FAQLRAWARD EFEDEVYLLA QGTAKAAEEW
AQLELAIREN TSVSMLATVT DERAHVDALM PADFVRATPA ERFWDLPRYL KAGQLRIEKA
KINPSGDDSL AWQIQGASEA VEQARAEAEY GTYSPRAARI LTEARWMIEE LRVSLFAQQL
GTKGKVSVKR IQKKLAELED
//
