ID A0A163IQH8_ABSGL Unreviewed; 1061 AA.
AC A0A163IQH8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=ATP-dependent RNA helicase DOB1 {ECO:0008006|Google:ProtNLM};
GN Name=ABSGL_00111.1 scaffold 249 {ECO:0000313|EMBL:SAL94822.1};
OS Absidia glauca (Pin mould).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=4829 {ECO:0000313|EMBL:SAL94822.1};
RN [1] {ECO:0000313|EMBL:SAL94822.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAL94822.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000256|ARBA:ARBA00010140}.
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DR EMBL; LT549980; SAL94822.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163IQH8; -.
DR STRING; 4829.A0A163IQH8; -.
DR InParanoid; A0A163IQH8; -.
DR OMA; IMLKNYN; -.
DR OrthoDB; 1352at2759; -.
DR Proteomes; UP000078561; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0006401; P:RNA catabolic process; IEA:InterPro.
DR CDD; cd18024; DEXHc_Mtr4-like; 1.
DR CDD; cd13154; KOW_Mtr4; 1.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 1.10.3380.30; -; 1.
DR Gene3D; 2.40.30.300; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR048392; MTR4-like_stalk.
DR InterPro; IPR025696; MTR4_beta-barrel.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016438; SKI2-like.
DR InterPro; IPR012961; Ski2/MTR4_C.
DR PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR PANTHER; PTHR12131:SF7; EXOSOME RNA HELICASE MTR4; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF08148; DSHCT; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF21408; MTR4-like_stalk; 1.
DR Pfam; PF13234; MTR4_beta-barrel; 1.
DR PIRSF; PIRSF005198; Antiviral_helicase_SKI2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01142; DSHCT; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000078561}.
FT DOMAIN 149..305
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 418..590
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 23..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1061 AA; 119769 MW; 34B7F2C8107310C2 CRC64;
MFDEGNTDPL FNVFGGKAID DQFDDFDDSE TEMNSTMDSH KRARSSSPLA DDASEETEIK
RLRAEEATHA QPIVADSFEE ESSRQVTNVA GLQGSLASEE TELVLNHQVR HQVALPLNYD
YKPISQHVPP EDPARTYPFT LDPFQRVAVS SIERNESVLV SAHTSAGKTV VAEYAIAQCL
KNKQRVIYTS PIKALSNQKF REFTEEFGDV GLMTGDVTIN PEASCLVMTT EILRSMLYRG
SEIIREVAWV VYDEIHYMRD SERGVVWEES IILLPHAVRY VFLSATIPNA MEFAEWICKI
HEQPCHIVYT DFRPTPLQHY LFPAGGEGIH LVVDEKSVFR EDNFTRAIAA LSDGQADDPS
GAMARGGRGK KGPKTAKGGP NDGPSDIYRI IKMIMMKNYH PVIVFSFSKK ECESNALQLS
KLDFNDSNES AMVTQVFNNA ISSLSEDDRE LPQIQQLLPL LKRGIGVHHG GLLPIMKETI
EVLFQENLLK VLFATETFSI GLNMPAKTVV FTSVQKYDGK SQRWVTSGEY IQMSGRAGRR
GLDERGVVIM MIDSKMEPAV AKGMVKGDSD RMNSAFHLSY NMVLNLLRVE GVSPEYMLER
CFYTFQNDAN IPQFESQLLA LEQKKNGIFI ENEDEIKSYY EIRQQIDSFA ENIRQVITHP
TYCLPFMQPG RLLHIKHNDL DFGWGAVVNY NRTIDRSKPK DDPDHFYYIV DVLLCCTTDS
SLSKDAQGRS VGIYPSDPMA SSNSMIVVPV LLNTIQGISH IRLKLPNDIK GRDGRASVLR
SIKEVRKRFG DQVPLLDPIQ NMGITDPVFK KLVNKIVILE KQLTTHPLAE SEDLSTLYDA
YGEKMKIAID IKNMKRKITD AQSIVQLDEL KSRKRVMRRL GFTTAADVVE MKGRVACEIS
TGDELLLTEM MFQGVFNDLV VDQCVALLSC FVFDEKVDQA ARLQEELAGP LRLMQETARR
IAKVSIECKM NLDEEAYLAK FKPELMDVVF AWCQGAKFSQ ICKMTDVYEG SLIRIFRRLE
ELLRQMASAA KSIGNTELEN KFSEGINRIH RDIIFAASLY L
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