ID R9P2B9_PSEHS Unreviewed; 932 AA.
AC R9P2B9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=PHSY_003037 {ECO:0000313|EMBL:GAC95461.1};
OS Pseudozyma hubeiensis (strain SY62) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1305764 {ECO:0000313|EMBL:GAC95461.1, ECO:0000313|Proteomes:UP000014071};
RN [1] {ECO:0000313|Proteomes:UP000014071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY62 {ECO:0000313|Proteomes:UP000014071};
RX PubMed=23814110; DOI=10.1128/genomea.00409-13;
RA Konishi M., Hatada Y., Horiuchi J.;
RT "Draft genome sequence of the basidiomycetous yeast-like fungus Pseudozyma
RT hubeiensis SY62, which produces an abundant amount of the biosurfactant
RT mannosylerythritol lipids.";
RL Genome Announc. 1:E0040913-E0040913(2013).
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};
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DR EMBL; DF238795; GAC95461.1; -; Genomic_DNA.
DR RefSeq; XP_012189048.1; XM_012333658.1.
DR AlphaFoldDB; R9P2B9; -.
DR STRING; 1305764.R9P2B9; -.
DR GeneID; 24108327; -.
DR eggNOG; KOG0922; Eukaryota.
DR HOGENOM; CLU_001832_5_3_1; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000014071; 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; cd17978; DEXHc_DHX33; 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; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
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; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF118; ATP-DEPENDENT RNA HELICASE DHX33; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 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:UP000014071}.
FT DOMAIN 122..340
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 387..570
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 932 AA; 101136 MW; F3C1FBB077E9E9E0 CRC64;
MSLSQGSPQK KRHHHDGLTS PKSFSNPSSP TKKLKKSKYA NAPSAMLSNA DELLRSVSAS
PSKALGSSSR SAPPSPSRSN HASTSNGSDP AAWIRDALKN VDQRILDSRT ALPITSGKEA
IIEAVRNNDT VVILGETGSG KTTQIPQFLF EAGFARRAPI QMIGVTQPRR VAATSLARRV
AVEMGQPDPA VLPSVKGKAR TAAGGLVGYS IRFEDRTTRN TRVKFMTDGM VLREMIGDAA
ASSTNSASAS SPALRSNLLL KYSVLIIDEA HERTLRTDQV LGLAKRIQRE RKAIRQSWIA
RGKPSGEPEV TELKIIVMSA TLDADRFANF FATPSTALAV SPSIADSKIL VAANGKQEVP
ILYVKGRQHE VTMFHTDQPA QEWTDAALRT VLQIHVSRPP GDILVFMTGQ EEIDTLARSL
ELYSSELPAW AEAEGKQLPM AVMIAPLYAA LGPSASAKVF GPTPPRTRKI VLATNIAETS
ITIPGIVFVV DCGLAKEKMY TPGTAVETLQ VQEISQSAAR QRAGRAGRER AGECYRLYTQ
EAFQNLPLAG TPEIVRTDLA AAVLQLCAMG QDPYTFDWLD QPDRIGLQES VLQLIQLGAL
KIEAVPPTPT SNGQVNGKQA KTSAKLALTP IGSKMAMLPV SPAYSRSLIA AADRGPTVAR
QTRDLIAILS SDRSILIEPS DPEKRDEANR AKSTFVHPTG DHATLLTVLY SYLAEVDKSR
SMAKGRKLEG KVDVKVVEKE AREGVKAWCS NHYVYEKAVK NVLHIRKQLR NICRQQKIVC
DDDPDQLVNG ADAESDPDNL DSDSDTSSSS QPNRDGLFVT RKPTSTVTQD TEEDQHYIGL
RQSLLEGRIS NAALKNPSAP NTFKRIITSA SSSGLFKVHP SSTLHPSKMA REGGGRKMDA
ILFEELVFTS QTFARTVSTI EPSWLQEFAQ RG
//
