ID A0A0D2DB46_9EURO Unreviewed; 1133 AA.
AC A0A0D2DB46;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=PV07_04427 {ECO:0000313|EMBL:KIW32914.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW32914.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW32914.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW32914.1,
RC ECO:0000313|Proteomes:UP000054466};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN847041; KIW32914.1; -; Genomic_DNA.
DR RefSeq; XP_016253130.1; XM_016391228.1.
DR AlphaFoldDB; A0A0D2DB46; -.
DR STRING; 569365.A0A0D2DB46; -.
DR GeneID; 27343621; -.
DR VEuPathDB; FungiDB:PV07_04427; -.
DR HOGENOM; CLU_276938_0_0_1; -.
DR OrthoDB; 1095660at2759; -.
DR Proteomes; UP000054466; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd17917; DEXHc_RHA-like; 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; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR048333; HA2_WH.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR18934:SF203; -; 1.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF04408; HA2_N; 1.
DR Pfam; PF00271; Helicase_C; 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; PS00690; DEAH_ATP_HELICASE; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054466}.
FT DOMAIN 199..374
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 479..655
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 77..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1071..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1096
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1115
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1133 AA; 127045 MW; DF23E3B2E986C534 CRC64;
MRAWCARNLH PRGLQCVAPQ IHDISSLRSI PTGGLAFRTY LRPTNARCIW TPLRYPPPAR
LLHTGSEADD HVPSLVASRR DNDNSDGDDP QSLSTQEEKA VKARKSFRIN IPKVNLDSAL
ETMRQAHAHG LTLDEVVLKP SRVQTDSSVH VVSLKNEERL AIKMKVDLEV ARQQGKMKET
LRLRQTLPLM AGETQQTLLK LINDNDVVIV LAKTGSGKTT QVPQIILDDK IMSGEGPCTN
IVCTQPRRIA ATSVAHRVAY ERHDTIRSSV GYHIRHENWS PSPLGSITYC TTGILLNRLI
ANPQATLSSH SHIIVDEVHE RDIQIDLVLS LLRKAIRARK ATQESFPKVI LMSATIDPTT
FLDYFKQPAE DGTALKVDCL DVEGRRAHVE THYLPEILTE LSQGGDLHPS IRQLIQGGHH
QSSARHIEHE MHFSAQKIKL GKPLSSENGA NENSPLQSAV DETDSAELTG PMRVGLAVSV
IVHIAKTKPD GDVLVFFPGS TDMEKVELLL TSGRFASLGL DFLDPNRFRL FKLHSLRRET
NDQVFEPVPE GCRRIILTTN IAETSITLPD VVYVVDTGKE RNSLFDPSTL ARSLPYTWIS
KTSSIQRRGR AGRVRNGHYY ALFSKERHDS LRPMQRPKIE QSDLAEMALQ FKAFPQHGDV
ESFLLETIDP PTSESVASAI RQLQSLGALT ESGDITDLGR LLWRLGVHPA LGKGILLGSL
FGCLEPMLII ACHDPGAPLV STLELSIDRL RAVKQQYLPE FESDFAWIIE AFREYHAANL
AGDENLMQEL RDTKHIRHRA YLDMMMTSKA LHDVLAEVGF VPSPQPEKTI FESLPDSLNA
NSDNMVLVKA LLINTVSAEL AAWRGATSFK GRQYGWSTDS RDLKGMLSKH GVNEANTRRD
RRKKKRYRSH GRLMAYTWKQ AGLDGPDDVV WLEQASMVTP LMAILFCRSL KLQIDEVLEL
NEWLRLRLSA PDDVPSEFSD RAAVILTELR KTIDRFVNLA WLELERLNYP RGPHHSGSHR
QATTPNSMGL ELRNVMVEAV VKMLDVDEAY WREWRKRRRV EIALDVERRK REEEEAEAVV
EDEGQGKEHL EDAIATEMEE MDSDAEAEDD VESDAEGDLG HSAANQGLDK ATA
//
