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Database: UniProt
Entry: A0A1R0H211_9FUNG
LinkDB: A0A1R0H211_9FUNG
Original site: A0A1R0H211_9FUNG 
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
//
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