(data stored in ACNUC9543 zone)

HOGENOM: SCHPO_1_PE484

ID   SCHPO_1_PE484                        STANDARD;      PRT;   1168 AA.
AC   SCHPO_1_PE484; O42643;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Pre-mRNA-splicing factor ATP-dependent RNA helicase prp22;
DE   EC=3.6.4 13; (SCHPO_1.PE484).
GN   Name=prp22; ORFNames=SPAC10F6.02c;
OS   SCHIZOSACCHAROMYCES POMBE.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SCHPO_1.PE484.
CC       Schizosaccharomyces pombe chromosome I EF1 full sequence 1..5579133
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:PRP22_SCHPO
CC   -!- FUNCTION: Acts late in the splicing of pre-mRNA. Required for the
CC       splicing of introns with a branch nucleotide to 3'-splice site
CC       distance greater or equal to 15. Mediates the release of the
CC       spliced mRNA from spliceosomes.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC       subfamily. DDX8/PRP22 sub-subfamily.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 S1 motif domain.
CC   -!- GENE_FAMILY: HOG000175261 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Schizosaccharomyces_pombe;SPAC10F6.02C;SPAC10F6.02C-1;SPAC10F6.02C-1.
DR   UniProtKB/Swiss-Prot; O42643; -.
DR   EMBL; CU329670; CAA15715.1; -; Genomic_DNA.
DR   PIR; T37496; T37496.
DR   RefSeq; NP_593253.1; NM_001018650.1.
DR   ProteinModelPortal; O42643; -.
DR   IntAct; O42643; 1.
DR   STRING; O42643; -.
DR   EnsemblFungi; SPAC10F6.02c-1; SPAC10F6.02c-1; SPAC10F6.02c.
DR   GeneID; 2542978; -.
DR   GenomeReviews; CU329670_GR; prp22.
DR   KEGG; spo:SPAC10F6.02c; -.
DR   NMPDR; fig|4896.1.peg.3223; -.
DR   GeneDB_Spombe; SPAC10F6.02c; -.
DR   eggNOG; fuNOG04413; -.
DR   GeneTree; EFGT00050000000163; -.
DR   OMA; KTMGIND; -.
DR   OrthoDB; EOG45TGW9; -.
DR   PhylomeDB; O42643; -.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-000945-MON; -.
DR   ArrayExpress; O42643; -.
DR   GO; GO:0005634; C:nucleus; IDA:GeneDB_Spombe.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR014001; DEAD-like_helicase.
DR   InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR011709; DUF1605.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR016027; NA-bd_OB-fold-like.
DR   InterPro; IPR003029; Rbsml_prot_S1_RNA-bd_dom.
DR   InterPro; IPR022967; RNA-binding_domain_S1.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF04408; HA2; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   Pfam; PF00575; S1; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; Nucleic_acid_OB; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50126; S1; 1.
DR   HOGENOMDNA; SCHPO_1.PE484; -.
KW   SPAC10F6.02cc37236820036002503210000011;
KW   O42643;
KW   ATP-binding; Complete proteome; Helicase; Hydrolase; mRNA processing;
KW   mRNA splicing; Nucleotide-binding; Nucleus; Reference proteome.
SQ   SEQUENCE   1168 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MDDLKELEYL SLVSKVASEI RNHTGIDDNT LAEFIINLHD QSKNYDEFKN NVLSCGGEFT
     DSFLQNISRL IKEIKPKDDI PTDNVNNGSN SVNGASHDLD SKDVDKQHQR KMFPGLSIPN
     STNNLRDRPA LMDNAMDELE ELSTLAKTRR NDRDSRRDER HYLNGIRERR ERSISPSFSH
     HSRTSISGQS HSSRSSRGPL LNAPTLYGIY SGVVSGIKDF GAFVTLDGFR KRTDGLVHIS
     NIQLNGRLDH PSEAVSYGQP VFVKVIRIDE SAKRISLSMK EVNQVTGEDL NPDQVSRSTK
     KGSGANAIPL SAQNSEIGHV NPLETFTSNG RKRLTSPEIW ELQQLAASGA ISATDIPELN
     DGFNTNNAAE INPEDDEDVE IELREEEPGF LAGQTKVSLK LSPIKVVKAP DGSLSRAAMQ
     GQILANDRRE IRQKEAKLKS EQEMEKQDLS LSWQDTMSNP QDRKFAQDVR DSAARQLTSE
     TPSWRQATRN ANISYGKRTT LSMKEQREGL PVFKLRKQFL EAVSKNQILV LLGETGSGKT
     TQITQYLAEE GYTSDSKMIG CTQPRRVAAM SVAKRVAEEV GCRVGEEVGY TIRFEDKTSR
     MTQIKYMTDG MLQRECLVDP LLSKYSVIIL DEAHERTVAT DVLFGLLKGT VLKRPDLKLI
     VTSATLDAER FSSYFYKCPI FTIPGRSYPV EIMYTKQPEA DYLDAALMTV MQIHLSEGPG
     DILVFLTGQE EIDTSCEILY ERSKMLGDSI PELVILPVYS ALPSEIQSRI FEPAPPGGRK
     VVIATNIAET SLTIDGIYYV VDPGFVKQSC FDPKLGMDSL IVTPISQAQA RQRSGRAGRT
     GPGKCYRLYT ESAYRNEMLP SPIPEIQRQN LSHTILMLKA MGINDLLNFD FMDPPPAQTM
     IAALQNLYAL SALDDEGLLT PLGRKMADFP MEPQLSKVLI TSVELGCSEE MLSIIAMLSV
     PNIWSRPREK QQEADRQRAQ FANPESDHLT LLNVYTTWKM NRCSDNWCYE HYIQARGMRR
     AEDVRKQLIR LMDRYRHPVV SCGRKRELIL RALCSGYFTN VAKRDSHEGC YKTIVENAPV
     YMHPSGVLFG KAAEWVIYHE LIQTSKEYMH TVSTVNPKWL VEVAPTFFKF ANANQVSKTK
     KNLKVLPLYN RFEKPDEWRI SKQRKGGR
//

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