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Database: UniProt
Entry: V5BSW5_TRYCR
LinkDB: V5BSW5_TRYCR
Original site: V5BSW5_TRYCR 
ID   V5BSW5_TRYCR            Unreviewed;       297 AA.
AC   V5BSW5;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Cleavage and polyadenylation specificity factor subunit 2 {ECO:0000256|RuleBase:RU365006};
DE   AltName: Full=Cleavage and polyadenylation specificity factor 100 kDa subunit {ECO:0000256|RuleBase:RU365006};
GN   ORFNames=TCDM_02045 {ECO:0000313|EMBL:ESS69287.1};
OS   Trypanosoma cruzi Dm28c.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX   NCBI_TaxID=1416333 {ECO:0000313|EMBL:ESS69287.1, ECO:0000313|Proteomes:UP000017861};
RN   [1] {ECO:0000313|EMBL:ESS69287.1, ECO:0000313|Proteomes:UP000017861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Dm28c {ECO:0000313|EMBL:ESS69287.1,
RC   ECO:0000313|Proteomes:UP000017861};
RX   PubMed=24482508;
RA   Grisard E.C., Teixeira S.M., de Almeida L.G., Stoco P.H., Gerber A.L.,
RA   Talavera-Lopez C., Lima O.C., Andersson B., de Vasconcelos A.T.;
RT   "Trypanosoma cruzi Clone Dm28c Draft Genome Sequence.";
RL   Genome Announc. 2:e01114-13(2014).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU365006}.
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC       metabolizing metallo-beta-lactamase-like family. CPSF2/YSH1 subfamily.
CC       {ECO:0000256|RuleBase:RU365006}.
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:ESS69287.1}.
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DR   EMBL; AYLP01000013; ESS69287.1; -; Genomic_DNA.
DR   AlphaFoldDB; V5BSW5; -.
DR   EnsemblProtists; ESS69287; ESS69287; TCDM_02045.
DR   VEuPathDB; TriTrypDB:TCDM_02045; -.
DR   Proteomes; UP000017861; Unassembled WGS sequence.
DR   GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006378; P:mRNA polyadenylation; IEA:InterPro.
DR   InterPro; IPR027075; CPSF2.
DR   InterPro; IPR025069; Cpsf2_C.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   PANTHER; PTHR45922; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 2; 1.
DR   PANTHER; PTHR45922:SF1; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 2; 1.
DR   Pfam; PF13299; CPSF100_C; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE   3: Inferred from homology;
KW   mRNA processing {ECO:0000256|RuleBase:RU365006};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365006};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017861};
KW   RNA-binding {ECO:0000256|RuleBase:RU365006}.
FT   DOMAIN          129..293
FT                   /note="Cleavage and polyadenylation specificity factor 2 C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13299"
SQ   SEQUENCE   297 AA;  33561 MW;  DC3576E2A65C704E CRC64;
     MQFLMRRKAP ARIYSDEGPE GIQMHNDAQA EANIPSKTFV NTAMVRKNSR VFMTDLSGFA
     DAAIMRSLLK SRFSFAKKIV LIRGTVDDHR ALYQFCRSEK VMKCGENVFF PRTQRTHLEL
     ATHVYSYMVQ LDPTLANALP SALRRVKESR SSGFWDVGWV DGALESSFVS LTPEDDERQS
     VKRLRAEGNG GEIKDGVFTL VPLFGERAQQ CARERELRGM QRGLFYVGDV DLHRLREVAR
     NEMGLRGEFH KNAPMLVFDA GLCVRKSANG NFSLSSMISP SVFALRKTVY GQFSQTL
//
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