ID A0A068S565_9FUNG Unreviewed; 1123 AA.
AC A0A068S565;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=LCOR_08080.1 {ECO:0000313|EMBL:CDH57095.1};
OS Lichtheimia corymbifera JMRC:FSU:9682.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH57095.1, ECO:0000313|Proteomes:UP000027586};
RN [1] {ECO:0000313|EMBL:CDH57095.1, ECO:0000313|Proteomes:UP000027586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA Voigt K.;
RT "Gene expansion shapes genome architecture in the human pathogen
RT Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT terrestrial Mucorales (Mucoromycotina).";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001556};
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:CDH57095.1}.
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DR EMBL; CBTN010000043; CDH57095.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068S565; -.
DR STRING; 1263082.A0A068S565; -.
DR VEuPathDB; FungiDB:LCOR_08080.1; -.
DR OrthoDB; 5480645at2759; -.
DR Proteomes; UP000027586; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR CDD; cd17967; DEADc_DDX3_DDX4; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 5.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044763; Ded1/Dbp1_DEADc.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR PANTHER; PTHR47958:SF2; DEAD BOX RNA HELICASE-PL10B; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00641; zf-RanBP; 5.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00547; ZnF_RBZ; 5.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 5.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 4.
DR PROSITE; PS50199; ZF_RANBP2_2; 5.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:CDH57095.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000027586};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT DOMAIN 104..133
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 143..172
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 182..211
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 292..320
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 323..512
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 524..695
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 740..769
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 782..810
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..1123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 292..320
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 25..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..970
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1016
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1089
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1123 AA; 119934 MW; 957D1045C2940B12 CRC64;
MSWDSGNNAN GGDSWGAGGG SGGGQWDGGN STPWDGGSST PWGGSGDAAG GQDNNPFASG
NFGGGEFATS NDTSNDYGAS GDYGSGGDYG GGDDYDSRPA RTPRPGDWDC PDCGVNNFAS
RDACFKCSAP RPEGMGRPKR EPRPGDWDCP SCGVNNFASR QECFKCNEPR PEGMGPPKRE
PRPGDWDCPS CNINNFGTRT ECFKCGAARP EGMGVPPPED RPERAYNWAS NRARYEFNEN
AIGEDGMAPR DEKLEAELFG FDPTEQHTPL DFSKYANIPI NIERGEAPAP VKDFDSANLH
PVMKENIRLA RYTQPTPVQT MSIPIVTNGK DLMACAQTGS GKTAAFLIPT LSGLFGRAKE
LAQPRPAPFE YRSFKAEPLV VIIAPTRELC SQIFDECRKF TYRSMLRPCA VYGGADTLSQ
IRQLERGCDI LAASPGRLMD FIERGKISLK RVRYLVLDEA DRMLDMGFEA VIRAIVEKRG
LNPERQTLMY SATFPRAIRK LARDFLQPDY LFLKVGRVGG TTSSITQKML YVEEENKREE
LRTLLNSQPP SRTLIFVETK RSADSLDQYL YERGFPSTSI HGDRTQMERE DALIAFKHGR
CPILVATAVA ARGIDIRNVM HVINYDMPES MDEYIHRIGR TARVGRSGLA TSFYNERTSH
LAPELAKLLK ECKQEIPEFL QMYIPEDITW EEDLPEEDVP APSYAGQEYV PMERPGFGAP
PGAPAGGDAH GDSAGGAPAR EGDWNCPSCG INNYARRTEC FKCNTPNPNP STGGGGGARE
RRDGDWDCTC GVVNYARRTE CFKCGAQREG GAGGDDYGYG ASGDYGAGTA DAGTAGWDAN
AASAGWDSGN NGATGGGWDA NAASAGWDSG NNGATGGGWD AKCCFCWMGF CCWWWMGVNL
LLLNNLLLLL VVDGVNLLLL NNLLLLLVDG VSLHLLNNLL LKLLVDGGEP QQQQASPAQQ
PVSTSGGWGE PAPAQQPAPQ AAGGWGEPQK QPSPAPQAAG GWGEPQQQQS PAQQPAAANG
GWGEPAPKQP AAQQPASGGW GEPAAPTPQQ PPVSNGWGSP APPAQTPPAA ATPPPQQQPP
APAAQPAPAA PAPAADDGWG AAPAQPAGDG WGAPPAKPDG FGW
//
