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Database: UniProt
Entry: A0A0D2HQJ0_9EURO
LinkDB: A0A0D2HQJ0_9EURO
Original site: A0A0D2HQJ0_9EURO 
ID   A0A0D2HQJ0_9EURO        Unreviewed;       762 AA.
AC   A0A0D2HQJ0;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=Z520_00823 {ECO:0000313|EMBL:KIY04131.1};
OS   Fonsecaea multimorphosa CBS 102226.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIY04131.1, ECO:0000313|Proteomes:UP000053411};
RN   [1] {ECO:0000313|EMBL:KIY04131.1, ECO:0000313|Proteomes:UP000053411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 102226 {ECO:0000313|EMBL:KIY04131.1,
RC   ECO:0000313|Proteomes:UP000053411};
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 Fonsecaea multimorphosa CBS 102226.";
RL   Submitted (JAN-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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
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DR   EMBL; KN848062; KIY04131.1; -; Genomic_DNA.
DR   RefSeq; XP_016638253.1; XM_016771343.1.
DR   AlphaFoldDB; A0A0D2HQJ0; -.
DR   STRING; 1442371.A0A0D2HQJ0; -.
DR   GeneID; 27706569; -.
DR   VEuPathDB; FungiDB:Z520_00823; -.
DR   OrthoDB; 161833at2759; -.
DR   Proteomes; UP000053411; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   CDD; cd17913; DEXQc_Suv3; 1.
DR   CDD; cd18805; SF2_C_suv3; 1.
DR   Gene3D; 1.20.272.40; -; 1.
DR   Gene3D; 1.20.58.1080; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR022192; SUV3_C.
DR   InterPro; IPR041082; Suv3_C_1.
DR   InterPro; IPR044774; Suv3_DEXQc.
DR   PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR   PANTHER; PTHR12131:SF1; ATP-DEPENDENT RNA HELICASE SUPV3L1, MITOCHONDRIAL; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF12513; SUV3_C; 1.
DR   Pfam; PF18147; Suv3_C_1; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053411};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          361..531
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          36..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   762 AA;  85229 MW;  C3966DB64D7D1744 CRC64;
     MLTPSTRRAQ CLFCSFRAFF ASAPKRCYGN IRSFSTTTGQ TDRQHHKSSP TARSALSESS
     KARRPSRRPA PETLQISPDA SYNRVRVSLS RLKKRLESTK VAAESEVTQL AALDPCGTYW
     PAFREQLENT IAPQGDSGSA DFDGLISDIG RAQLGEWETE LPRVLHFGFI DYVLWRRAQD
     APKEGSALDD LQFPTEWYTN ARQVQRDVHL HIGPTNSGKT YNALKRLEES GDGFYAGPLR
     LLAHEVYSRF KAKGVPCDLV TGDDVRLEDD PNTKLRASTV EMVDISARFE VAVIDEVQMV
     ADQDRGWAWT RALLGANAKE VHICGETRVL PLIRELTAST GDILHVHEYK RLNPLKVMTK
     SLRGDLKNLR KGDCIVAFSV VNIHALKKQI EMDTGRRCAI VYGSLPPETR AQQAALFNDP
     NNDYDFLVAS DAIGMGLNLS VKRIVFHTVS KFNGTSIVRL STPQIKQIGG RAGRFRNAHQ
     AMHNTAAASE SNVGLVTTLN DEDLPLVRAA MESEAAPIKR AGMLPPAEAM EELEGRLPKG
     IPFEYILRRL CGKAATHPRF RVCSIRDQSR ISRVIESVRG LTMTQRIMLT AAPATTASQA
     MDEVMRAFAR CVAERRQVTV VDVPEVRLEV LEKPISGDRA YLVSLEDLHK SLVLYLWLSY
     RFLGIFKDRE MAVYAKELVE DRINTCLLEF SANPDLRKRV LSYKKRFALP QIETEESAPA
     NQGSQLEQPE EAEALPMDWI RSYPAVEFED SPPSQPYNVA HG
//
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