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Database: UniProt
Entry: A0A0D7A406_9AGAR
LinkDB: A0A0D7A406_9AGAR
Original site: A0A0D7A406_9AGAR 
ID   A0A0D7A406_9AGAR        Unreviewed;      1447 AA.
AC   A0A0D7A406;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Pre-mRNA-splicing factor ATP-dependent RNA helicase prp22 {ECO:0000313|EMBL:KIY45455.1};
GN   ORFNames=FISHEDRAFT_49464 {ECO:0000313|EMBL:KIY45455.1};
OS   Fistulina hepatica ATCC 64428.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Fistulinaceae; Fistulina.
OX   NCBI_TaxID=1128425 {ECO:0000313|EMBL:KIY45455.1, ECO:0000313|Proteomes:UP000054144};
RN   [1] {ECO:0000313|EMBL:KIY45455.1, ECO:0000313|Proteomes:UP000054144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 64428 {ECO:0000313|EMBL:KIY45455.1,
RC   ECO:0000313|Proteomes:UP000054144};
RX   PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA   Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA   Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA   LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA   Hibbett D.S.;
RT   "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT   genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL   Fungal Genet. Biol. 76:78-92(2015).
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DR   EMBL; KN882048; KIY45455.1; -; Genomic_DNA.
DR   OrthoDB; 1095660at2759; -.
DR   Proteomes; UP000054144; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   CDD; cd17917; DEXHc_RHA-like; 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; IPR048333; HA2_WH.
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:SF197; DEPENDENT RNA HELICASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G07950)-RELATED; 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   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; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000313|EMBL:KIY45455.1};
KW   Hydrolase {ECO:0000313|EMBL:KIY45455.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054144}.
FT   DOMAIN          630..808
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          896..1075
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          259..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          349..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1447 AA;  161821 MW;  5697E86E32A7B149 CRC64;
     MAKKKKQVKP NRGFATVSVP KKVVPADDPP EQPALDNAAV DADKLAQNAS SNGHSDQRRS
     DSLSSEDAAL QMLVDKYQER TEKEITRSRF DSAQQAIQVD RRFAMTFPTL DLDPALREQI
     LALALKESVI EDKRPLDDSE DKALAKLGIT YGVVRRLGFS DARVLECMSS ISEVDLDGAF
     GWLYLHCSED ELVFNKAKCS EEVSEPHTPV RGGNPGKHNP RTPAGFLASS TFPLTKKLFK
     LDANAAIFVP SRLSSPVLGN NIAGDKSTNT LDSESSDEES PHEQYVRTKL KLDELSTVPK
     SNASALSQLP ALRARLATIQ KNYFFDAKEA ELMYEARRKE LLQAKLRGEL PVEAKDPQPA
     SPSLKEPVPM KPHPASSDVF DDNSDTGDDS GGMLELLEMP TTEVTPQGVT VQVRDMALPK
     NWSGRSPKHL LQDNVSKTDK YAAISFSIMS GSSRAKRASV SIRWASSRTS QWSMEDVACH
     DDSQAEQYIA TVALHALSFP PSEGFSTSGA STTGNVTFFR SFPPQFRDLW NELEAKRKLE
     EDRINREIWG KLRSIIQSKM ETGKVAGKIA KSIADAKESK LHRQVLAKDN GGPNEQLRLS
     LLARRESPLY QKMLVHRNAL PIAAYRQTIV QALEESQVLV LSGETGCGKS TQLPTFLLED
     QLSRGKRCKI YCTEPRRISA ISLAQRVSRE LGEPAGAVGT INSLVGYSIR LESNTSKNTR
     LAFVTYGIAL RMLESGSGQD GQGMAFDDIT HIIIDEVHER SIESDFLLIV LKQLLRHRPD
     LKVVLMSATV NAEKISEYFD GCPMLHVPGR TFPVEVKYLE DAIEYTGWSI SPNSAYARRP
     HDKYFHGKTE WSEEQNVVDD DDDEEEQDNI KLEKRYSPST AETINRLDDR QIPYDLIVRL
     LERICFEDTD KIAFSPAVLI FMPGMGEIRR LNDMLSEHPA FSSDDFIIYP LHSTLPSESQ
     TAVFDIPPHG VRKIVIATNI AETGITIPDI TTVIDTGKHR EMRFDEKRQI SRLVESHIAK
     SNAAQRRGRA GRVREGLCYH LFTKVRHDTK MAEHPLPEMM RLSLSDLALR IKIMKVNLGP
     SIEDVLSRAL DPPSSINIQR AINMLVEVQA LTPSEQITPM GRLLSKLPTD VHLGKFLLMA
     TIFRCLDPAL TIAAALNSKS PFVTPFGLEH EADRVRASFR LGNSDFLTLH NVFASWRRAS
     ENTGYAWKFC RVNYLSHQNL QQIEELRQQF LGYLIDTDFM QVDRQFSREF SRRDYFFQSR
     YSRGRATFIS VPESVNVNSE NIALVNAALV AGLYPKVLAV DSSNGQMRTV SSNQSVSFHP
     SSVSFGKRPT DLGVNYINYF TLMHSKKLYA WETGPVDDLA LAILCGDSDF KLIADSVAVD
     RRIRFKVDPK TNVALKCLRD RVTSILAQIF GGRLLTESHV RWNDIATMVL GRMKVEGNEP
     ETYAVLS
//
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