ID   A0A0F4YHZ1_TALEM        Unreviewed;      1414 AA.
AC   A0A0F4YHZ1;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Protein CFT1 {ECO:0000256|ARBA:ARBA00039443};
DE   AltName: Full=Cleavage factor two protein 1 {ECO:0000256|ARBA:ARBA00041264};
DE   AltName: Full=Protein cft1 {ECO:0000256|ARBA:ARBA00039187};
GN   ORFNames=T310_8221 {ECO:0000313|EMBL:KKA17834.1};
OS   Rasamsonia emersonii CBS 393.64.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX   NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA17834.1, ECO:0000313|Proteomes:UP000053958};
RN   [1] {ECO:0000313|EMBL:KKA17834.1, ECO:0000313|Proteomes:UP000053958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA17834.1,
RC   ECO:0000313|Proteomes:UP000053958};
RA   Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA   Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00037232}.
CC   -!- SIMILARITY: Belongs to the CFT1 family.
CC       {ECO:0000256|ARBA:ARBA00038304}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKA17834.1}.
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DR   EMBL; LASV01000544; KKA17834.1; -; Genomic_DNA.
DR   RefSeq; XP_013324446.1; XM_013468992.1.
DR   STRING; 1408163.A0A0F4YHZ1; -.
DR   GeneID; 25320481; -.
DR   OrthoDB; 149432at2759; -.
DR   Proteomes; UP000053958; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   Gene3D; 1.10.150.910; -; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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   PANTHER; PTHR10644:SF2; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 1; 1.
DR   PANTHER; PTHR10644; DNA REPAIR/RNA PROCESSING CPSF FAMILY; 1.
DR   Pfam; PF03178; CPSF_A; 1.
DR   Pfam; PF10433; MMS1_N; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000053958}.
FT   DOMAIN          123..743
FT                   /note="Cleavage/polyadenylation specificity factor A
FT                   subunit N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10433"
FT   DOMAIN          1055..1379
FT                   /note="Cleavage/polyadenylation specificity factor A
FT                   subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03178"
FT   REGION          211..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          470..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..237
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        481..496
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1414 AA;  153844 MW;  25A97E79AF56CB9F CRC64;
     MLSSVESRSP LGLCVCDSLQ LDPDSRMQCY TELLPPSGVT HALSAPFLSP TANNLVVVKT
     SLLQIFTLVN VASELDAREA EDKASRIETS QDTKLHLIAE YDLSGTVTDI CRVKILNSKS
     GGDALLLAFR NAKLSLIEWD PDRHGISTIS IHYYEKEDVT RSPWVPNLST CGSHLTVDPS
     SRCAVLNFGL RNLAILPFHQ AGDDLVMDDY DPDLDEEPAD HEMKDVVQSE KKDERKDSLT
     YQTPYAASFV LPMTALDPAL LHPISLAFLH EYREPTFGIL YSQVATSSAL LSERKDVVFY
     SVFTLDLEQR ASTTLLSVAR LPSDLFKIVA LPPPVGGALL VGSNELIHVD QAGKTNAVGV
     NEFARQVSSF SMADQSDLAL RLEGCVVEHL GNENGDVILL LSSGEMMLVS FKLDGRSVSG
     LSIHPIANGG TIMNAAASCS AVLGSGKLFF GSEDADSILV EWSNVSSSTK RARVQDADQQ
     PEFSDEDGDD NDAYEDDLYS AAPKVSSDHR PSVDNSIAGG YNFRVLDTLT NIGPLRDIAL
     GKASAKAADG DRNVSSVTAD LELVASQGSD KSGGLVLLKR EIDPSVISSF EIDNAESVWS
     VSVSEAKSKT SNDGGSSVQK GADSYVILAK STSTDKEESV VHAVKGKSLE AFRAPEFNPN
     EDCTVDVGTL AGGTRVVQVL TGEVRIYDSS LGLAQIYPVW DEDTSDERIA VSASFADPYL
     LILRDDASVL LLQADESGDL DEVPLNDEIS SKSWLSGCLY ADNSGMFSPI ETDSQGNIHL
     FLLNAECKLF IFRLPSTDLV SVIEGVDYVL PILSAEPPPR RSSTRETITE ILVADIGESY
     CKSPYLILRT GTDDLVIYRP FRINDDLGKD PSSLKFLKEV NHTLPKVPSV ASSKTSSGGQ
     RRTKSLRRLP DISGLSAVFM PGASPSFVIR TSKSMPHLVS LRGGFVRGLS DFNAAGCEKG
     FIYVDSHNVV RTCQLPDDTQ FDFPWTVRRV PLGEQVDHLT YSTSSDTYVL GTSYKADFRL
     PEDDELHPEW RNEDLPKLGE TPEPEELVCH RQVCYPLSAA ERVMAVENIN LEISEQTRER
     KDVIVVGTTF AQGEDVAARG CVYVFDVIEV VPDPERPETN LKLKLIGKES VKGAVTAISG
     IGGQGFLIVA QGQKCMVRGL KNDGSLLPVA FIDVQCYVSV LKELRGTGMC IIGDALKGLW
     FTGYSEEPYK MTLFGKDMDE LEVVAADFLP DGKKLYIIVC DGDCNLHVLQ YDPEDPKSSN
     GDRLLNRSTF HMGHFASTVT LLPRTAVSSE LAMSDSDEMS IDAYVPLHQV LITTQTGSVG
     LVTSVSEESY RRLSALQSQL SNTLEHPCGL NPRAYRAVES DGIGGRGMID GTLLYRWLDL
     SRQRKTEIAS RVGADEWEIR ADLEAIGGSG LGYL
//