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Database: UniProt
Entry: A0A1Q5GPR4_9ACTN
LinkDB: A0A1Q5GPR4_9ACTN
Original site: A0A1Q5GPR4_9ACTN 
ID   A0A1Q5GPR4_9ACTN        Unreviewed;      1333 AA.
AC   A0A1Q5GPR4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=ATP-dependent helicase {ECO:0000313|EMBL:OKJ34573.1};
GN   ORFNames=AMK22_18740 {ECO:0000313|EMBL:OKJ34573.1};
OS   Streptomyces sp. CB01580.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703933 {ECO:0000313|EMBL:OKJ34573.1, ECO:0000313|Proteomes:UP000186318};
RN   [1] {ECO:0000313|EMBL:OKJ34573.1, ECO:0000313|Proteomes:UP000186318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB01580 {ECO:0000313|EMBL:OKJ34573.1,
RC   ECO:0000313|Proteomes:UP000186318};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
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:OKJ34573.1}.
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DR   EMBL; LIXJ01000012; OKJ34573.1; -; Genomic_DNA.
DR   RefSeq; WP_073786656.1; NZ_LIXJ01000012.1.
DR   STRING; 1703933.AMK22_18740; -.
DR   OrthoDB; 9805617at2; -.
DR   Proteomes; UP000186318; 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; 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:OKJ34573.1};
KW   Hydrolase {ECO:0000313|EMBL:OKJ34573.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186318}.
FT   DOMAIN          83..247
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          278..445
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          479..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..503
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1333 AA;  151119 MW;  10B8620EB4C01AA1 CRC64;
     MSTSFADLQS RLEELSLRDA HRLGRRLEGA RRIRKPEARQ AVLDEIATEA GKAAERLVLR
     AGRVPAVSYP EQLPVSQKKD EILEAIRDHQ VVIVAGETGS GKTTQIPKIC MELGRGVRGM
     IGHTQPRRIA ARTVAERVAD ELRTPLGEAV GWKVRFTDQV NPDATFVKLM TDGILLAEIQ
     TDRELRAYDT IIIDEAHERS LNIDFLLGYL ARLLPRRPDL KVVITSATID PERFARHFGE
     APIIEVSGRT YPVEVRYRPL LEEVTEDSAD ADRDQITAIC DAVDELQSEG PGDILVFLSG
     EREIRDTADA LNKRNLRHTE VLPLYARLSH AEQHRVFQRH TGRRIVLATN VAETSLTVPG
     IKYVIDPGTA RISRYSHRTK VQRLPIERIS QASANQRKGR CGRTSDGICI RLYSEDDFLT
     RPEFTDPEIL RTNLASVILQ MTAAGLGDIE RFPFIDPPDH RNIRDGIQLL QELGALEQGE
     KPAREVRAGE REARPEGKKG QRLTPLGRKL SQLPVDPRLA RMVIEAERNG CVREVMVIAA
     ALSIQDPRER PAEKQTQADQ QHARFKDETS DFLAFLNLWR YIREQQKERG SSSFRRMCKQ
     EYLNFLRIRE WQDIYAQLRT VVKQMGVQPN TEDAPEQSVH VSLLAGLLSH IGLKDTEKNE
     YLGARNAKFA VFPGSALFKK QPRFVMSAEL VETSRLWARV NAKVEPEWIE PLAQHLLKHT
     YSEPHWEKDQ AAVMAYERVT LYGVPIIAQR KVNFGRIDAE TSRDLFIRHA LVEGDWRTHH
     QFFQDNRKLL GEVEELEHRA RRRDILVDDE TLFDFYDRRI PEHVVSGAHF DSWWKHKRRD
     EPDALDFERS MLINEKAGAV TKDDYPDSWR QGKLKFRVTY QFEPGADADG VTVHIPLQVL
     NQVTAEGFDW QIPGLREEVV TELIRSLPKP IRRHYVPAPN YAEKFLDRAV PSASGGPTSQ
     QEPLTVTLAR ELQRMVGVPV TADDFDLSRV PDHLKITFRI VDERRRKVAE DKDLEALRLQ
     LRPRARQALS KAAAATAGPS GESVERSGLT DWTIGTLNRV FETRRAGQPV KAYPALVDQG
     ATVAVRLFDT EAEQQRAMWL GTRRLILLNV PVNPAKFASD RLSNQQKLAL SANPHGSVQA
     LFEDCATAAA DRLIGAHGGP AWDEESYRKL YDKVRADLVA LTEHTVKQVQ QVLAAWQACE
     RRLKATNSLV LAANVADVRK QLAGLVPAGF VTATGLRRLP DLMRYLVAAD RRLQQMPTAV
     QRDTTRMEKV HEMQDEYAWL LEQLPQGRPV PQEVLDIRWM IEELRVSYFA HALGTAYPVS
     DKRIVKAIDA AAP
//
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