(data stored in ACNUC9543 zone)

HOGENOM: SCHPO_2_PE640

ID   SCHPO_2_PE640                        STANDARD;      PRT;   1055 AA.
AC   SCHPO_2_PE640; Q10752; Q9URU1; Q9USV9; Q9UUD7;
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-like
DE   protein cdc28; EC=3.6.4 13;AltName: Full=Pre-mRNA-processing protein 8;
DE   (SCHPO_2.PE640).
GN   Name=cdc28; Synonyms=prp8;
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_2.PE640.
CC       Schizosaccharomyces pombe chromosome II EF1 full sequence 1..4539804
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:CDC28_SCHPO
CC   -!- FUNCTION: Involved in pre-mRNA splicing. Is required together with
CC       ATP and at least one other factor, for the first cleavage-ligation
CC       reaction. Functions as a molecular motor in the activation of the
CC       precatalytic spliceosome for the first transesterification
CC       reaction of pre-mRNA splicing by hydrolyzing ATP to cause the
CC       activation of the spliceosome without the occurrence of splicing
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Cells show pre-mRNA splicing defects. Cdc28-
CC       P8 temperature-sensitive mutant causes cell-cycle arrest in G2 and
CC       exhibits a splicing defect that leads to accumulation of unspliced
CC       precursors at the restrictive temperature. Temperature-sensitive
CC       pre-mRNA splicing mutant Prp8-1 exhibits a cell-cycle phenotype
CC       identical to cdc28-p8. Prp8-1 mutant produces elongated cells,
CC       accumulates U6 snRNA precursor and has defects in an early step of
CC       TFIID pre-mRNA splicing at the nonpermissive temperature.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC       subfamily. DDX16/PRP8 sub-subfamily.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC49377.1; Type=Frameshift; Positions=80, 1012;
CC   -!- GENE_FAMILY: HOG000175261 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Schizosaccharomyces_pombe;SPBC19C2.01;SPBC19C2.01-1;SPBC19C2.01-1.
DR   UniProtKB/Swiss-Prot; Q10752; Q9URU1; Q9USV9; Q9UUD7; -.
DR   EMBL; U48733; AAC49377.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; CU329671; CAB57929.2; -; Genomic_DNA.
DR   PIR; T46568; T46568.
DR   PIR; T50372; T50372.
DR   RefSeq; NP_595686.2; NM_001021581.2.
DR   ProteinModelPortal; Q10752; -.
DR   STRING; Q10752; -.
DR   EnsemblFungi; SPBC19C2.01-1; SPBC19C2.01-1; SPBC19C2.01.
DR   GeneID; 2540707; -.
DR   GenomeReviews; CU329671_GR; cdc28.
DR   KEGG; spo:SPBC19C2.01; -.
DR   GeneDB_Spombe; SPBC19C2.01; -.
DR   GeneTree; EFGT00050000000163; -.
DR   OMA; SALMIDE; -.
DR   OrthoDB; EOG4SBJ63; -.
DR   PhylomeDB; Q10752; -.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-004862-MON; -.
DR   ArrayExpress; Q10752; -.
DR   GO; GO:0004004; F:ATP-dependent RNA helicase activity; TAS:GeneDB_Spombe.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0045292; P:nuclear mRNA cis splicing, via spliceosome; IMP:GeneDB_Spombe.
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   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF04408; HA2; 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   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   HOGENOMDNA; SCHPO_2.PE640; -.
KW   SPBC19C2.012cc7236820036002503210000011;
KW   Q10752;
KW   ATP-binding; Complete proteome; Helicase; Hydrolase; mRNA processing;
KW   mRNA splicing; Nucleotide-binding; Nucleus; Reference proteome.
SQ   SEQUENCE   1055 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSLEQYVSDK AISLLGMSEP SVVEYLIAEA KGSSSSNNLY QKLVSFGMDG DDPAVKEFAH
     TLYARIPREG SRPKENYNAR KKKEQGILQM ERLNSSYDLL IEPQSHETPG KPLKKKSRSK
     TPKREIARRQ RDEDEWESDE YEEVVDGSAS HPIEEDSVST DFQNHDYEKS SDPETERLND
     LREREEFEER LRRKDLEAAT NEFVEDYSSK FSSEELALRK LADDPESWRK LASELRKKSR
     QQYLKPRAQQ QLEILRREIR DEEQLFAGEK LTQAEIRELE KKKELLRIAE ERQRLEKQAT
     EYQMPEDYFT EQGKLDRKRK EEVLYQRYKD SNEGEQNEVT MGAAEQQRWE AQQINKALLF
     DQNEWLPPGE KQFDFVFDES QQIDFLLDTK LSAENPVDTD KMTDVKVEKS LESSRKSLPV
     YQYKDDLLKA INEYQVLLIV AETGSGKTTQ LPQFLHEAGY TKGNKKICCT QPRRVAAMSV
     AARVAKEMDV RLGQEVGYSI RFENATSEKT VIKYLTDGML LREFLTEPDL ASYSVIIIDE
     AHERTLHTDI LFGLVKDIAR FRPDLKVLIS SATIDAEKFS AYFDEAPVFY VPGRRYPVDI
     YYTPQPEANY IQAAITTILQ IHTTQPAGDI LVFLTGQDEI ELMSENMQEL CRILGKRIPE
     IILCPIYANL PSELQAKIFD PTPPGARKVV LATNIAETSI TIDGVNFVID SGFVKQNMYN
     PRTGMESLVS VPCSRASADQ RAGRAGRVGP GKCFRLYTRR TYNNELDMVT SPEIQRTNLT
     NIVLLLKSLG INNLLDFDFM DAPPPETLMR SLELLYALGA LNNRGELTKL GRQMAEFPTD
     PMLSKSLIAS SKYGCVEEVL SIVSMLGEAS SLFYRPKDKI MEADKARANF TQPGGDHLTL
     LHIWNEWVDT DFSYNWAREN FLQYKSLCRA RDVRDQLANL CERVEIELVT NSSESLDPIK
     KAITAGYFSN AARLDRSGDS YRTVKSNQTV YIHPSSSVAE KKPKVIIYFE LVLTTKEYCR
     QITEIQPEWL LEISPHYFKP ENIEELQKTQ KRHKR
//

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