ID A0A176L368_9ACTN Unreviewed; 601 AA.
AC A0A176L368;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Helicase ATP-binding domain-containing protein {ECO:0000259|PROSITE:PS51192};
GN ORFNames=A6P39_21050 {ECO:0000313|EMBL:OAA98917.1};
OS Streptomyces sp. FXJ1.172.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=710705 {ECO:0000313|EMBL:OAA98917.1};
RN [1] {ECO:0000313|EMBL:OAA98917.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FXJ1.172 {ECO:0000313|EMBL:OAA98917.1};
RA Liu M., Liu N., Shang F., Huang Y.;
RT "Activation and identification of NC-1, a novel cryptic cyclodepsipeptide
RT from red soil-derived Streptomyces sp. FXJ1.172.";
RL Submitted (APR-2016) 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:OAA98917.1}.
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DR EMBL; LWRP01000104; OAA98917.1; -; Genomic_DNA.
DR RefSeq; WP_067048470.1; NZ_CP119133.1.
DR AlphaFoldDB; A0A176L368; -.
DR STRING; 710705.A6P39_21050; -.
DR OrthoDB; 5165890at2; -.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR CDD; cd18785; SF2_C; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47396:SF1; ATP-DEPENDENT HELICASE IRC3-RELATED; 1.
DR PANTHER; PTHR47396; TYPE I RESTRICTION ENZYME ECOKI R PROTEIN; 1.
DR Pfam; PF04851; ResIII; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE 4: Predicted;
FT DOMAIN 42..199
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 601 AA; 66672 MW; 4C6D17B8FE46A47D CRC64;
MTTTAASASS SHSHHLSPAF PGRAPWGTAS KLRAWQQGAM EKYVQEQPRD FLAVATPGAG
KTTFALTLAS WLLHHHVVQQ VTVVAPTEHL KKQWAEAAAR IGIKLDPEYS AGPLGREYDG
VAVTYAGVGV RPMLHRNRVE QRKTLVILDE IHHAGDSKSW GEACLEAFEP ATRRLALTGT
PFRSDTNPIP FVTYEEGTDG IRRSSADYTY GYGNALADHV VRPVIFLSYS GNMRWRTKAG
DEIAARLGEP MTKDAISQAW RTALDPRGEW MPSVLRAADQ RLTEVRKAIP DAGALVIASD
QDSARAYAKL IREITGTKAT LVLSDDAGAS KRIDEFSESN DRWMVAVRMV SEGVDVPRLA
VGVYATTIST PLFFAQAVGR FVRSRRRGET ASVFLPTVPD LLTFANEMEK ERDHALDKPK
KEGEEDPYAE SEKEMEEANK QQDEDTGEQE QFSFEALESE AVFDRVLYDG AEFGMQAHPG
SEEEQDYLGI PGLLEPDQVQ LLLQKRQARQ IAHSRKKPDA EADLLELPAE RRPVVSHKEM
MELRKRLNTM VSAYVHQSGK PHGVIHTELR RVCGGPPSAE ATAGQLEQRI AKVQEWATRM
K
//