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CFT1_ASPFU
ID   CFT1_ASPFU              Reviewed;        1401 AA.
AC   Q4WCL1;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 2.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Protein cft1;
DE   AltName: Full=Cleavage factor two protein 1;
GN   Name=cft1; ORFNames=AFUA_8G04040;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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}.
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DR   EMBL; AAHF01000013; EAL85173.2; -; Genomic_DNA.
DR   RefSeq; XP_747211.2; XM_742118.2.
DR   AlphaFoldDB; Q4WCL1; -.
DR   SMR; Q4WCL1; -.
DR   STRING; 746128.CADAFUBP00008129; -.
DR   EnsemblFungi; EAL85173; EAL85173; AFUA_8G04040.
DR   GeneID; 3504725; -.
DR   KEGG; afm:AFUA_8G04040; -.
DR   eggNOG; KOG1896; Eukaryota.
DR   HOGENOM; CLU_002414_2_1_1; -.
DR   InParanoid; Q4WCL1; -.
DR   OMA; PMTKFKL; -.
DR   OrthoDB; 360328at2759; -.
DR   Proteomes; UP000002530; Chromosome 8.
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..1401
FT                   /note="Protein cft1"
FT                   /id="PRO_0000290622"
FT   REGION          434..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        458..474
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1401 AA;  154611 MW;  B43E5464308BF759 CRC64;
     MQCYTELLSP SGVTHALAIP FLSASAENLV VVKTSVLQIF SLLKVQHHSR GETIETKSAR
     PDQVETTKLV LEREYPLSGT VVDICRVKIL NSKSGGEALL LAFRNAKLSL VEWDPERHGI
     STISIHYYER DDLTRSPWVP DLSSCGSILS VDPSSRCAVF NFGIRNLAIL PFHQPGDDLA
     MDDYEFHLHQ DDLNQVSDHV GNGLKSKDST VYQTPYASSF VLPLTALDPS ILHPVSLAFL
     YEYREPTFGI LYSQIATSHA LLSERKDSIF YTVFTLDLEQ RASTTLLSVP KLPSDLFKVV
     ALPPPVGGAL LIGSNELVHV DQAGKTNAVG VNEFARQVSA FSMVDQSDLA LRLEGCVVEH
     ISDSTGDLLL VLSSGNMVLV HFQLDGRSVS GISLRPLPTQ AGGTIMKSAA SSSAFLGSGR
     VFFGSEDADS VLLSWSSMPN PKKSRPRMSN VAEDREEASD DSQSEEDAYE DDLYTAEPET
     PALGRRPSAE TTGVGAYIFQ TLDRLPNIGP LRDITLGKPA STVENTGRLI KNACSELELV
     AAQGSGRNGG LVLMKREIEP DVTASFDAQS VQEVWTAVVA LGSGAPLVLD EQQINQEYRQ
     YVILSKPETP DKETSEVFIA DTQDLKPFRA PEFNPNNDVT IEIGTLSCKK RVVQVLRNEV
     RSYDIDLGLA QIYPVWDEDT SDERMAVSAS LADPYIAILR DDSTLMILQA DDSGDLDEVE
     LNEAARAGKW RSCCLYWDKA EFFSSTGPAL KQGTRCELFL FLLSIDCRLY VYRLPDQQLI
     SVIEGIDCLP PILSTELPKR STTREVLSEA VIADLGESWN PSPHLILRTE SDDLVIYKAF
     ASYIKGESHT RLSFVKESNH TLPRVTTSEK EMQSNEKLSR PRSLRILPNI SNFSAVFMPG
     RPASFILKTA KSCPHVFRLR GEFVRSLSIF DLASPSLDTG FIYVDSKDVL RICRFPSETL
     FDYTWALRKI SIGEQVDHLA YATSSETYVL GTSHSADFKL PDDDELHPDW RNEGLVISFL
     PELRQCSLKV VSPRTWTVID SYSLGPDEYV MAVKNMDLEV SENTHERRNM IVVGTAFARG
     EDIPSRGCIY VFEVIKVVPD PEKPETDRKL KLIGKELVKG AVTALSQIGG QGFLIAAQGQ
     KCMVRGLKED GSLLPVAFMD MQCYVNVLKE LKGTGMCIMG DAVKGLWFAG YSEEPYKMSL
     FGKDQGYLEV VAAEFLPDGD KLFILVADSD CNLHVLQYDP EDPKSSNGDR LLARSKFHMG
     HFATTMTLLP RTMVSSEKAM ANPDSMEIDS QTISQQVLIT SQSGSVGIVT SVPEESYRRL
     SALQSQLANS LEHPCGLNPR AYRAVESDGT AGRGMLDGNL LYQWLDMGQH RKMEIAARVG
     AHEWEIKADL EAIGAEGLGY L
 
 
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