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CFT1_PHANO
ID   CFT1_PHANO              Reviewed;        1375 AA.
AC   Q0UUE2;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Protein CFT1;
DE   AltName: Full=Cleavage factor two protein 1;
GN   Name=CFT1; ORFNames=SNOG_04622;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
CC   -!- FUNCTION: RNA-binding component of the cleavage and polyadenylation
CC       factor (CPF) complex, which plays a key role in polyadenylation-
CC       dependent pre-mRNA 3'-end formation and cooperates with cleavage
CC       factors including the CFIA complex and NAB4/CFIB. Involved in poly(A)
CC       site recognition. May be involved in coupling transcription termination
CC       and mRNA 3'-end formation (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CFT1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAT88382.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH445330; EAT88382.2; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001795036.1; XM_001794984.1.
DR   AlphaFoldDB; Q0UUE2; -.
DR   SMR; Q0UUE2; -.
DR   STRING; 13684.SNOT_04622; -.
DR   GeneID; 5971904; -.
DR   KEGG; pno:SNOG_04622; -.
DR   eggNOG; KOG1896; Eukaryota.
DR   InParanoid; Q0UUE2; -.
DR   OMA; PMTKFKL; -.
DR   OrthoDB; 360328at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR   Gene3D; 2.130.10.10; -; 2.
DR   InterPro; IPR004871; Cleavage/polyA-sp_fac_asu_C.
DR   InterPro; IPR018846; Cleavage/polyA-sp_fac_asu_N.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   Pfam; PF03178; CPSF_A; 1.
DR   Pfam; PF10433; MMS1_N; 1.
PE   3: Inferred from homology;
KW   mRNA processing; Nucleus; Reference proteome; RNA-binding.
FT   CHAIN           1..1375
FT                   /note="Protein CFT1"
FT                   /id="PRO_0000290634"
FT   REGION          194..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          446..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..462
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        463..477
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1375 AA;  150030 MW;  BEE72D3BAB2E453E CRC64;
     MQAYTEIAPP TAVSHAITLP FLSSRSNNLI VAKNSLLQVF ELKSTVTEVA SGGEGEADNA
     AANFDTEAAD VPLQRIENTA KLVLVGEFPL AGTVISLARV KALNTKSRAE ALLVAFRDAK
     LSLVEWDPET YNLHTISIHY YENPDVPGLA PWDAELKDTY NFLTADPSSR CAALKFGTHN
     LAILPFRQRD LAEDEYDSDN EAAQEGKAER ANGANGDDAV KTPYSSSFVL PLTNLDPTLT
     HPVHLAFLHE YREPTFGVIS SSKATAASLL THRKDILTYT VFTLDLEQKA STTLLSVPGL
     PYDLTQVVPL PHPIGGALLV GSNEIIHVDQ AGKTNGVAVN ELAKACTSFA LSDQADLALR
     LEGCTLELLS QDTGDVMIVL NDGSIFILTF SLDGRNVSAM TIQPVPADNG GNILKTRASC
     STNLGRGRLF IGSEDGESVL MGWTSTSNQL RRKQSNTAQS GDDEDMSDVE EEEVDDLDDD
     LYNDTATTVK KITAAAAEPT APGTYTFRVH DVLPSIAPIR DTVLHPGKDT ESLTKGEIML
     STGRGAAGAI TALNRELHPT MLAQTELPSS NGVWAVHAKK QAPAGIVADF GQDAEANASS
     DVDYDQYLVV SKAWEDGTES TVVYEVHGNE LSETEKGDFE RDEGLTLSVG VLARGTKVVQ
     VLRSEVRTYD SELGMEQIIP MEDEETGNEL NIINASFADP YLLIQREDSS VKIYKATGDG
     EVEDVEATGL SGTEWLSASL FQSSSFTEVF AFLLTPEGGL RIFAMSQLEK PSYVAEALGF
     LPPLLTMDYM PKRSSAKATI TEILAADLGD ATSRSPHLIV RTSNDDLVIY KAIHSPSRSS
     SDLWTHNLRW VKLSQQHVPR YMEDGAQEEA ADEPGFESTL LALDNINGYS TVIQRGRSPA
     FILKESSSAP RVIGLSGNPV KSLTRFHTSS CQRGFAYLDS TDTLRISQLP PSTHYGHLGW
     AARRMPMDAE VHALAYHPSG LYVIGTGQPE EYTLDPNDTF HYELPKEETS FKPKVEHGII
     KVMDEKTWTV IDTHVLDPQE VILCIKTLNL EVSETTHQRK DVIAVGTAIV LGEDLATKGN
     IRIFEVITVV PEPDHPETNK RLKLIVKDEV KGTVSAISDL GTQGFLIMAQ GQKSMVRGLK
     EDGTLLPVAF MDMQCYVTTL KTLPNTGMLL MGDAYKGAWF TGYTEEPYKM MLFGRSKHHL
     ECITADFLPF EEQLHIIVAD ADMNLQVLQF DPDHPKSMGG TRLLQKSTFH TGHFPSTMHL
     LQSRLHMPTA SEFTTSTTSS LPLHQILCTS QSGTLALITP LSESSYRRLS GLATHLQQFL
     DSPCGLNGKA FRAADVMEGG WDAGTQRAML DGGLLMRWGE LGEQRRREGL GKVGW
 
 
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