ID G0VCW5_NAUCC Unreviewed; 814 AA.
AC G0VCW5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 13-SEP-2023, entry version 54.
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 Name=NCAS0C03360 {ECO:0000313|EMBL:CCC69326.1};
GN OrderedLocusNames=NCAS_0C03360 {ECO:0000313|EMBL:CCC69326.1};
OS Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS 1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC69326.1, ECO:0000313|Proteomes:UP000001640};
RN [1] {ECO:0000313|EMBL:CCC69326.1, ECO:0000313|Proteomes:UP000001640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC {ECO:0000313|Proteomes:UP000001640};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Type strain:CBS 4309;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Naumovozyma castellii.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; HE576754; CCC69326.1; -; Genomic_DNA.
DR RefSeq; XP_003675691.1; XM_003675643.1.
DR AlphaFoldDB; G0VCW5; -.
DR STRING; 1064592.G0VCW5; -.
DR GeneID; 11528066; -.
DR KEGG; ncs:NCAS_0C03360; -.
DR eggNOG; KOG1135; Eukaryota.
DR HOGENOM; CLU_002227_3_0_1; -.
DR InParanoid; G0VCW5; -.
DR OMA; YVLEHAW; -.
DR OrthoDB; 198429at2759; -.
DR Proteomes; UP000001640; Chromosome 3.
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 CDD; cd16293; CPSF2-like_MBL-fold; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 2.
DR InterPro; IPR022712; Beta_Casp.
DR InterPro; IPR027075; CPSF2.
DR InterPro; IPR025069; Cpsf2_C.
DR InterPro; IPR035639; CPSF2_MBL.
DR InterPro; IPR001279; Metallo-B-lactamas.
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 Pfam; PF16661; Lactamase_B_6; 1.
DR SMART; SM01027; Beta-Casp; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 3: Inferred from homology;
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|RuleBase:RU365006};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365006};
KW Reference proteome {ECO:0000313|Proteomes:UP000001640};
KW RNA-binding {ECO:0000256|RuleBase:RU365006}.
FT DOMAIN 255..379
FT /note="Beta-Casp"
FT /evidence="ECO:0000259|SMART:SM01027"
FT REGION 438..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..483
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 814 AA; 92079 MW; 49E73CAF1C619E73 CRC64;
MTYKVSCCND GSNGTVGTIL KFDNVTILID PGWTSTEVSY VDCVKYWSNL IPEIDVILIS
QPTIECLGAY TLLYENFLSH FLSRIAVYAT LPVANLGRVS TIEWYASQGI IGPFLDSNKM
EVEDIEAAFD HIQILKYSQM IDLRSKFDGL TFFALNSGVN PGGSIWCIST YSEKLVYAPR
WNHTRDTILN AASLLDNMGK PLSTLMRPSG IITSFDKFGS VKPYKKRARI FKDSLKKALS
NNGTALIPID IGGKFLDVFV LVHDFLYENL KNGMFNRLPI LLVSYSRGRA LTYAKSMLEW
LSSTLLKTWE SRSNETPFEL GGRFEFKVVT PDELNRYSGS SKICFVSQVD PLLNDVFDKL
GSMEQTTVLL TSKYNGNQYV PSIMFNQWSK MEKEQGVQEG ESLNFAQTVA VKKVRFSTLN
AEDVEKFQEM TKQRKIEKEQ LKKGDDFRQK SITSFNGGPT SGQNEGAEEQ DEDEDEDEDE
DPLSSRTQDT QKFQTPVDVI LQKTSLLKHK MFQFHPVKIK RDDYGTIFDF NMLIPKDQEE
IEETSKSKRR AIIHSDSAHD EDSYDPAKQI NKKRKGTPEL EMNNFDNLSY LDTSNTVKSR
SETNEQLILR CMITYINLES LVDQRSASVI WPSLRARKLI IQGPEEVQDE KLINMLRKKG
TDTLVLPLGE DVEFTTTIKT LEISLDPDLD SLLKWQKISD RYTVAHVTGH LVNEKSLVNG
QPTSKSKLVL KPMDNITKIH ASGTLSVGDV RLVELKRKLT EIHHVAEFKG EGMLVIDDKV
AVMKVSDGET IIDGSPSELF DLVKKMVTDM LAQV
//
