ID A0A1R0H211_9FUNG Unreviewed; 1615 AA.
AC A0A1R0H211;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 28-JAN-2026, entry version 32.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=AYI68_g2711 {ECO:0000313|EMBL:OLY83158.1};
OS Smittium mucronatum.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133383 {ECO:0000313|EMBL:OLY83158.1, ECO:0000313|Proteomes:UP000187455};
RN [1] {ECO:0000313|EMBL:OLY83158.1, ECO:0000313|Proteomes:UP000187455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALG-7-W6 {ECO:0000313|EMBL:OLY83158.1,
RC ECO:0000313|Proteomes:UP000187455};
RX PubMed=27343289; DOI=10.1093/molbev/msw126;
RA Wang Y., White M.M., Kvist S., Moncalvo J.M.;
RT "Genome-Wide Survey of Gut Fungi (Harpellales) Reveals the First
RT Horizontally Transferred Ubiquitin Gene from a Mosquito Host.";
RL Mol. Biol. Evol. 33:2544-2554(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + phosphate + H(+); 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:ARBA00047984};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC PRP16 sub-subfamily. {ECO:0000256|ARBA:ARBA00038040}.
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:OLY83158.1}.
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DR EMBL; LSSL01001044; OLY83158.1; -; Genomic_DNA.
DR STRING; 133383.A0A1R0H211; -.
DR OrthoDB; 10253254at2759; -.
DR Proteomes; UP000187455; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-ARBA.
DR GO; GO:0034458; F:3'-5' RNA helicase activity; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:TreeGrafter.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:UniProtKB-ARBA.
DR CDD; cd18791; SF2_C_RHA; 1.
DR FunFam; 3.40.50.300:FF:003016; DEAH-box helicase 9; 1.
DR FunFam; 3.40.50.300:FF:000615; pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH7; 1.
DR FunFam; 1.20.120.1080:FF:000018; Pre-mRNA-splicing factor ATP-dependent RNA helicase prp16; 1.
DR Gene3D; 1.10.2020.20; -; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 2.30.29.70; Proteasomal ubiquitin receptor Rpn13/ADRM1; 1.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044867; DEUBAD_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-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR044868; Rpn13/ADRM1_Pru.
DR InterPro; IPR038633; Rpn13/ADRM1_Pru_sf.
DR InterPro; IPR032368; RPN13_DEUBAD.
DR InterPro; IPR038108; RPN13_DEUBAD_sf.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF91; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE PRP16; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR Pfam; PF04683; Rpn13_ADRM1_Pru; 1.
DR Pfam; PF16550; RPN13_C; 1.
DR Pfam; PF04408; WHD_HA2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51916; DEUBAD; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51917; PRU; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:OLY83158.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000187455}.
FT DOMAIN 1..118
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
FT DOMAIN 223..334
FT /note="DEUBAD"
FT /evidence="ECO:0000259|PROSITE:PS51916"
FT DOMAIN 923..1086
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1108..1298
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 466..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..513
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..573
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..723
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..867
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..881
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..904
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1615 AA; 182726 MW; 8BD6E613D23CB627 CRC64;
MTSLFDSNPH SRFRNLSNPN YLLEFKAGRC IRDGETDWDD DDGMAKFCWK PLGSSEAEES
WIVFPGDIVF SKVKESSGRV YVLKFFSSPE RQFFWMQEPD EKKDRSIAAT VSKLINGSEM
DFEMEEVHDT PLSNTFSDPN NFSGSNSGLN SAINNHNEHS AVAQEAHTNL NSTLSTAFVG
GVPSNMASSS SSHIIHDDIS SSLASTKPDL QDLKSIIENI RVPQTYKDSP LKLSNVISPD
VLLPLLNDPD FCNVLFPQLP EGVPKTKEEL ENTIRSPQFE NSIQSLSFAL ESGQMAPLAQ
SLGLHPDSLS SRMDKSHSQI ISNLQDIVKN NVIVDKIIQF ARDNSSFDTF KIRCGALARL
DADFLSKIYN EFQNSTKIPV PISKPSSQPS LENDFSSGGL IIMKKNSDKK QNDQPKTSIL
GLDKLADLKR SQALSFDLED SPNPNPVKVR DFEFKKPDGS ILSQFKRKHR ADTPSLGTGL
SQEAESRVLD RKRRARPSGT SSAITNSNSK SSTLDSNRSY YHEHSKYNNH DSRTQKKDFQ
NNDSFRNTLH HHHQERLDSD RSSSSNRFSS NSDYPKFENS RTRDHNSDQS RAHDRSYTRS
SSKFDYNNDS RTQKKSSEWD YPTPKINSSR YRDTIPEYPR QSTRSDRSNT RVGSKYSISE
KNINEIDPLD EKNWKEEQTR LDREWYSIDE TGAQDDVHNS FADYTDYDNQ REQKLKSSSK
PDPDSTESLS ARQKQYNQDT QMWERNRLLQ SGIAMNRLEA NDDDDMTEDR VHLLVHDIKP
PFLDGRMVYS TQIGTVSTVR DPTSDLAIFS RKGSRLVIEK RSQREREKAT AAAANLAGTV
LGNVLGVKDA DVENEESQDV DPQDTDINES KNSYSNSSFN NKNKHKHPDG SSTSKGSSNF
STTKSLKEQR EYLPAFACRD DLMRIIRDNQ VVIVVGETGS GKTTQLAQYM MENGFSKYGL
IGCTQPRRVA AMSVAKRVSE EMGVSLGEEV GYAIRFEDCT SQKTKIKYMT DGVLLRESLN
DRDLDKYSAI IMDEAHERAL NTDVLLGLLK QVVSRRNDLK LIVTSATMNA ERFSNFFANA
PIFTIPGRTF PVEVLFSKTP CEDYVESAVK QIIAIHLSQP AGDILVFMTG QEDIEVTCQV
VSERLKDVDG APKLSVLPIY SQLPADLQSK IFDASEDGVV FFFFFFHSEA GFLFNHRIQK
ITFFLFYGKV DGVRYVVDSG YYKLKVYNQR IGMDTLQITP ISQANANQRS GRAGRTGPGV
AYRLYTESAY KNEMFQSPIP EIQRTNLSNV VLLLKSLGIK NLLEFDFMDP PPQDNILNSM
YQLWILGALD NLGQITELGL RMVELPLDPS LAKLMVSAVD LGCVAEAATI VSMLSVPSVF
YRPKERVEES DAMREKFFVP ESDHLTLLNV YALWKSNGCR DYWCAKHFIQ SKSMRKANEV
RSQLIEIMTN KLKIKYTSSG KDWDIVRKCI CNAYFHHAAL VRSLGTYRNL RTGMPCHLHP
TSALYGMGYT PDYIVYHELI YTSKEYMQCV TAVDPHWLAE MGPMFFSIKQ TGYSRLDMLK
DNSIIQKNLE IEHRAMTRAD TLNKNESFKN RRIKTGSAAS RSEIVTPGLK SKFKN
//