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Database: UniProt
Entry: K0JUG2_SACES
LinkDB: K0JUG2_SACES
Original site: K0JUG2_SACES 
ID   K0JUG2_SACES            Unreviewed;      1300 AA.
AC   K0JUG2;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=ATP-dependent RNA helicase HrpA {ECO:0000313|EMBL:CCH31485.1};
DE            EC=3.6.4.13 {ECO:0000313|EMBL:CCH31485.1};
GN   Name=hrpA {ECO:0000313|EMBL:CCH31485.1};
GN   OrderedLocusNames=BN6_41980 {ECO:0000313|EMBL:CCH31485.1};
OS   Saccharothrix espanaensis (strain ATCC 51144 / DSM 44229 / JCM 9112 / NBRC
OS   15066 / NRRL 15764).
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharothrix.
OX   NCBI_TaxID=1179773 {ECO:0000313|EMBL:CCH31485.1, ECO:0000313|Proteomes:UP000006281};
RN   [1] {ECO:0000313|EMBL:CCH31485.1, ECO:0000313|Proteomes:UP000006281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51144 / DSM 44229 / JCM 9112 / NBRC 15066 / NRRL 15764
RC   {ECO:0000313|Proteomes:UP000006281};
RX   PubMed=22958348; DOI=10.1186/1471-2164-13-465;
RA   Strobel T., Al-Dilaimi A., Blom J., Gessner A., Kalinowski J.,
RA   Luzhetska M., Puhler A., Szczepanowski R., Bechthold A., Ruckert C.;
RT   "Complete genome sequence of Saccharothrix espanaensis DSM 44229T and
RT   comparison to the other completely sequenced Pseudonocardiaceae.";
RL   BMC Genomics 13:465-465(2012).
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DR   EMBL; HE804045; CCH31485.1; -; Genomic_DNA.
DR   RefSeq; WP_015101597.1; NC_019673.1.
DR   STRING; 1179773.BN6_41980; -.
DR   KEGG; sesp:BN6_41980; -.
DR   PATRIC; fig|1179773.3.peg.4202; -.
DR   eggNOG; COG1643; Bacteria.
DR   HOGENOM; CLU_001832_3_3_11; -.
DR   OrthoDB; 9805617at2; -.
DR   BioCyc; SESP1179773:BN6_RS20320-MONOMER; -.
DR   Proteomes; UP000006281; Chromosome.
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:UniProtKB-EC.
DR   CDD; cd17989; DEXHc_HrpA; 1.
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:CCH31485.1};
KW   Hydrolase {ECO:0000313|EMBL:CCH31485.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006281}.
FT   DOMAIN          84..247
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          277..444
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          525..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..545
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1300 AA;  145705 MW;  D60A5574FDE166E7 CRC64;
     MNTTAHSDLH RRLSDLMSGD QRRLGRRLDG ARRVRDEQAR AAVHAEIAAE IEQAELRVAL
     RRAAVPKITY PGELPVSARK DDIAALIRDH QVVIVAGETG SGKTTQIPKI CLELGRGVLG
     QIGHTQPRRL AARTVAERVA QELGTQLGQA VGYKVRFTDQ SGDETLVKLM TDGILLAEIQ
     TDRTLSRYDT IIIDEAHERS LNVDFLLGYL KQLLPRRPDL KVVITSATID PERFSRHFAD
     APIIEVSGRT YPVEVRYRPV VDPDDPDADP DRDQTQAVCD AVRELQAEGP GDVLVFLSGE
     REIRDTADAL AALGLPHTEI LPLYARLSFG EQHKVFQSHR GRRVVLATNV AETSLTVPGI
     KYVVDPGTAR ISRYSNRLKV QRLPIEPISQ ASANQRKGRC GRVSAGICVR LYSEDSFDAR
     PEFTDPEILR TNLASVILQM TAIGLGDIAA FPFIDPPEAR NINDGVQLLH ELGAIVPAEQ
     KLTPLGRKLA QLPVDPRLAR MVIEADRNGC VREVMVIASA LSIQDPRERP SDKQQAADEQ
     HNRFKDPDSD FVAYLNLWQY LREQQKALSS NQFRRLCRAE FLNYLRVREW QDIYSQLRQV
     AKTLGVHVNE QPAEPRAVHL SLLSGLLSHI GLKDVVKRDP GKRQSSEYLG ARNAKFAIFP
     GSALFRKPPQ WVMAAELVET SRLWGRIVAR IEPEWAEGLA EHLVKRSYSE PHWEAKRGAV
     MAMEKVTLYG VPIVGARKVN YGQIDPGLCR ELFIRHALVQ GEWTTHHKFF HHNRALLDEV
     AELENRARRR DIVVDDDTLY EFYDQRVGED VVSARHFDTW WKKTRHTQPD LLTFDKQMLV
     NDRAQVTPEA YPDELTRGGV ALPLTYRFEP GTAVDGVTVR LPLPALTTVP DDALSWQVPG
     LRTELVVALI RSLPKPVRRN FVPVPDVAAA ALSRIDADEP LLPALERELR ALTGVVVPRE
     EWQLDQVPEH LKLTFQVVDE NNRELAQGKD LAALKQQLRG QLRETLAAAA SNLTRTGLTT
     WDLDELPKTV QRRQSGIVVT AYPALVDKGD SVAVEILDTP GRQAAAMRRG TRRLLLLAVP
     SPVKLLQRGL TNAEKLTLTR NPHGGVAALL ADCISAAVDH LVTSAGGPAW NAKGFTRLTE
     YVRKYLGETV FDVVREVRNV LDAAQEVELR LAGVKGAVYD ESVADVRAQL KGLVHNGFVT
     EAGAARLSDL HRYLQGIARR LEKLPENVRR DQDWMDRVHQ VHAEYRDLKA RLPADEPHPE
     LDEVRWMIEE LRLSYFAQTI PTRYTVSDKR VFKALDAVPR
//
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