ID A0A0M8MXD2_9BASI Unreviewed; 1128 AA.
AC A0A0M8MXD2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=Malapachy_2053 {ECO:0000313|EMBL:KOS15451.1};
OS Malassezia pachydermatis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=77020 {ECO:0000313|EMBL:KOS15451.1, ECO:0000313|Proteomes:UP000037751};
RN [1] {ECO:0000313|EMBL:KOS15451.1, ECO:0000313|Proteomes:UP000037751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 1879 {ECO:0000313|EMBL:KOS15451.1,
RC ECO:0000313|Proteomes:UP000037751};
RA Triana S., Ohm R., Gonzalez A., DeCock H., Restrepo S., Celis A.;
RT "Draft Genome Sequence of Malassezia furfur CBS1878 and Malassezia
RT pachydermatis CBS1879.";
RL Submitted (JUL-2015) 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:KOS15451.1}.
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DR EMBL; LGAV01000002; KOS15451.1; -; Genomic_DNA.
DR RefSeq; XP_017993083.1; XM_018136546.1.
DR AlphaFoldDB; A0A0M8MXD2; -.
DR STRING; 77020.A0A0M8MXD2; -.
DR GeneID; 28728421; -.
DR VEuPathDB; FungiDB:Malapachy_2053; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000037751; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR CDD; cd17971; DEXHc_DHX8; 1.
DR CDD; cd21691; GH2-like_DHX8; 1.
DR CDD; cd05684; S1_DHX8_helicase; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044762; DHX8/Prp22_DEXHc.
DR InterPro; IPR049588; DHX8_GH2-like.
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; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR049621; S1_DHX8_helicase.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF85; ATP-DEPENDENT RNA HELICASE DHX8; 1.
DR Pfam; PF00270; DEAD; 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 Pfam; PF00575; S1; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 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.
DR PROSITE; PS50126; S1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000313|EMBL:KOS15451.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000037751}.
FT DOMAIN 163..235
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 473..636
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 654..834
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 125..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1128 AA; 125383 MW; 71C871AB00850C6B CRC64;
MDDPLYKLEF LSLVSKITTE IENHVGINDR VLAEFVISLH EQAGSLDAFQ RKLDEAGAEF
PSDFVQSLDR LITTLHPTHK KAKAAATAAA SATSTDDALA ARERQAHKLP GLAIKDQAWE
EPDYYREAPP KRPKPASTAP PDEPERGRPR APRPPPDQAP IVSKIYEGRV AAIKDFGAFV
TLEDVQGRPD GLVHISALGS GGGRIQHPSD VVSRNQPVKV KVLAVDGKRI SLSMRDVDQI
TGRDLSASQR PAPDRSWRAT GANTAPLGGG PAPPPSADDR RGRTAKRLTS PERWEIKQLI
ASGVAKASDY PELMDEDFTT PASRLAGDDA DEEVEIEVNE KEAPFLAGQT AASLELSPVR
VVKAPDGSLN RAAQAGTALA KERRELRQQE MNEAADKQAK DMSTGWLDPM AQASDKKFAQ
DMRGSALGQQ AQQQPAWKKH TFNKATTFGK ITNLSMQEQR ESLPIFKLRE QLVQAVRDNQ
VLVVVGDTGS GKTTQLTQYL AEEGMADHGK IGCTQPRRVA AVSVAKRVAE EVGCRVGQEV
GYTIRFEDCT SPETRIKYMT DGMLQRECLV DPDVRAYSVL MLDEAHERTI ATDVLFGLLK
KALKKRPELK LIVTSATLDA EKFSNYFFNC PIFTIPGRTY PVEILYTKEP EPDYLDASLI
TVMQIHLSEP PGDILVFLTG QEEIDTSCEI LYERMRALGP GVPELIILPV YSALPSEMQS
RIFEPAPPGA RKVVLATNIA ETSITIDGIY YVVDPGFVKQ NAYDPRLGMD SLVVTPISQA
QARQRAGRAG RTGPGKCYRL YTEAAYRNEM LPNPIPDIQR QNLASTILSL KAMGINDLLH
FDFMDPPPAQ TMLTALESLY ALSALDDEGL LTRLGRKMAD FPMDPPMAKM LIASVDLGCS
EELLSIVAML SIPNVFYRPK DKQAQADAKR AKFFQPEGDH LTLLTVYNGW VASRFSMPWC
IDNFIQGRAL RRAQDVRKQL VGIMDRYHHD ILSCGSNYNR IRRAICSGYF RNAAKRDPQE
GYRTLAEGGG NVYLHPSSSL FHRPPEYVVY HEVVMTSKEY MREVTAIEPK WLVEVAPRFF
RTADPANISK RKRQEKIQPL FDRYAKDQDD WRLSKQQRLA RVVQSQTF
//