ID   A0A0D1ZWJ2_9EURO        Unreviewed;      1359 AA.
AC   A0A0D1ZWJ2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
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=PV08_04228 {ECO:0000313|EMBL:KIW17037.1};
OS   Exophiala spinifera.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW17037.1, ECO:0000313|Proteomes:UP000053328};
RN   [1] {ECO:0000313|EMBL:KIW17037.1, ECO:0000313|Proteomes:UP000053328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW17037.1,
RC   ECO:0000313|Proteomes:UP000053328};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala spinifera CBS89968.";
RL   Submitted (JAN-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}.
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DR   EMBL; KN847494; KIW17037.1; -; Genomic_DNA.
DR   RefSeq; XP_016237253.1; XM_016378576.1.
DR   STRING; 91928.A0A0D1ZWJ2; -.
DR   GeneID; 27331311; -.
DR   VEuPathDB; FungiDB:PV08_04228; -.
DR   HOGENOM; CLU_002414_2_1_1; -.
DR   OrthoDB; 149432at2759; -.
DR   Proteomes; UP000053328; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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:UP000053328}.
FT   DOMAIN          89..683
FT                   /note="Cleavage/polyadenylation specificity factor A
FT                   subunit N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10433"
FT   DOMAIN          981..1323
FT                   /note="Cleavage/polyadenylation specificity factor A
FT                   subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03178"
FT   REGION          169..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          424..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          487..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..450
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..503
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1359 AA;  148275 MW;  7D559CBCB4712639 CRC64;
     MQCYTELLPP SGVTHSLSAS FTSAKAENLI VARTSLLQVF QYKHLDHGTK LILVAEYNLA
     GTVTSLGKVR TADSKSGGDA VLVAFLDAKL SLIEWDPTLH SISTLSIHYY EQHDIQSAPW
     QPDLADCVSR LSIDPSSRCA AYNFGVSNLA IIPFHQTGDD LAMDDFDDLD HDEKGHHTPT
     KNPDGTMNGH SSPYSPSFVL PLTVLDPGLF HPVDIAFLHE YRDPTIGIVY STMARSSNMS
     AERRDVTIYA VYALDLDQKA STTLQSVQKL PNDIYCILAL PPPVGGALLV GGNELIHVDQ
     GGKASAVAVN EFAKDASSFP MTDHSEYRLK LEGCRIEHLG NAAGDMLIIL STGDLVLLTF
     RMDGRSVTGI SLRRIAEGQM QGLQLNAASC TANLGPSCLF IGGEDCDSVV VSLARKSGQL
     KRVQSRIKSE TDGFEPDGDE DDLDDEDDLY GEIYSGANGH NSADASGQNL RVMDRLPSIA
     PINSFALGSK KRKRDDTDTS EESQSQQHEL AVAYGKGHAG GIAFLSRQLT PKVTKRFKFE
     GANGLWCLAS KQAPSEGGQT LDDLVIVSQY TSEGLGLSSL CRLNGGNLDP VPDSEFDEMA
     GPTVSISQLH TSGHTIQVLP TEIRVYDSKF ALSQIFPIVD EDDGQLAKAV KTTFAEPYLA
     VIRDDRVMTL LKADKAGELD EVELPEMLQD KAVLSASLYQ DHHDFFQTSR FYDNAGSPGP
     ILSIFTTDGH FCLLSLPNIS LRVFQCDSLP FLPTYLMQDL QIPKHWRNKD DIGEILLADL
     GNMTDRRPFL AVRNLTGDVI LYEPFAIPDI AGSFKFRKVM TKSAEDLDDQ GEEEGEESSL
     GPMQVVPNVG SRAAIFVPGA HSWIILREAS TLPRVYELNL PGTNSLVGAH TPLCPQGLAF
     LDGQQHVCFG QLPDSTMIGQ SDWSVNRVPL GQDISSIAYF EPSDSYVLAI NYGIDFQLPQ
     DDEWHPEWQT ETTSFLPSSI QSSLKLMSSV SHSIISQYHF DACERVLCVK TLNLEISEET
     HERKDMIVVG TAIVKGENVT TRGNIYIFDV VDVVPEPGVA ESDLKLKLIT KEDVRGAVSA
     ICDIGSQGFL LAAQGQKCMV RGLKEDMSIL PVAFLDMRYY VHVAKELRGT GLCILGDAFS
     GLWLTGYSEE PYKLQIIGRD LENPPVLAAE FLPDGKQLFI VSADEDGTLR VLQYDPENPK
     AERGTKLLLR STFNAGTLPT QMSLLPPRTT GAVVAGGDAD MDLDGGGRMA NFSRILVATQ
     SGSLCMITPL PESAYRRLST LQNTLLATLD FQPCSLNPRA YRKVETDGIG GRGIIDGNLV
     KRWWETSTQQ RVASADKAGG SVWEVRADME LISGGDLTF
//