ID G7PBB8_MACFA Unreviewed; 782 AA.
AC G7PBB8; A0A2K5WUJ1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=CPSF2 {ECO:0000313|Ensembl:ENSMFAP00000040877.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000040877.1, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000040877.1, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000040877.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 RefSeq; XP_005562103.1; XM_005562046.2.
DR RefSeq; XP_005562104.1; XM_005562047.2.
DR RefSeq; XP_005562106.1; XM_005562049.2.
DR RefSeq; XP_015309621.1; XM_015454135.1.
DR AlphaFoldDB; G7PBB8; -.
DR SMR; G7PBB8; -.
DR STRING; 9541.ENSMFAP00000040896; -.
DR Ensembl; ENSMFAT00000015147.2; ENSMFAP00000040877.1; ENSMFAG00000041212.2.
DR GeneID; 102146350; -.
DR KEGG; mcf:102146350; -.
DR CTD; 53981; -.
DR VEuPathDB; HostDB:ENSMFAG00000041212; -.
DR eggNOG; KOG1135; Eukaryota.
DR GeneTree; ENSGT00910000144260; -.
DR OMA; YVLEHAW; -.
DR OrthoDB; 198429at2759; -.
DR Proteomes; UP000233100; Chromosome 7.
DR Bgee; ENSMFAG00000041212; Expressed in skeletal muscle tissue and 13 other cell types or tissues.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IEA:Ensembl.
DR GO; GO:0098794; C:postsynapse; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006398; P:mRNA 3'-end processing by stem-loop binding and cleavage; IEA:Ensembl.
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; 1.
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 InterPro; IPR011108; RMMBL.
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; PF10996; Beta-Casp; 1.
DR Pfam; PF13299; CPSF100_C; 1.
DR Pfam; PF16661; Lactamase_B_6; 1.
DR Pfam; PF07521; RMMBL; 1.
DR SMART; SM01027; Beta-Casp; 1.
DR SMART; SM00849; Lactamase_B; 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:UP000233100};
KW RNA-binding {ECO:0000256|RuleBase:RU365006}.
FT DOMAIN 17..223
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT DOMAIN 243..368
FT /note="Beta-Casp"
FT /evidence="ECO:0000259|SMART:SM01027"
SQ SEQUENCE 782 AA; 88473 MW; 067B4812B988FBF5 CRC64;
MTSIIKLTTL SGVQEESALC YLLQVDEFRF LLDCGWDEHF SMDIIDSLRK HVHQIDAVLL
SHPDPLHLGA LPYAVGKLGL NCAIYATIPV YKMGQMFMYD LYQSRHNTED FTLFTLDDVD
AAFDKIQQLK FSQIVNLKGK GHGLSITPLP AGHMIGGTIW KIVKDGEEEI VYAVDFNHKR
EIHLNGCSLE MLSRPSLLIT DSFNATYVQP RRKQRDEQLL TNVLETLRGD GNVLIAVDTA
GRVLELAQLL DQIWRTKDAG LGVYSLALLN NVSYNVVEFS KSQVEWMSDK LMRCFEDKRN
NPFQFRHLSL CHGLSDLARV PSPKVVLASQ PDLECGFSRD LFIQWCQDPK NSIILTYRTT
PGTLARFLID NPSEKITEIE LRKRVKLEGK ELEEYLEKEK LKKEAAKKLE QSKEADIDSS
DESDIEEDID QPSAHKTKHD LMMKGEGSRK GSFFKQAKKS YPMFPAPEER IKWDEYGEII
KPEDFLVPEL QATEEEKSKL ESGLTNGDEP MDQDLSDVPT KCISTTESIE IKARVTYIDY
EGRSDGDSIK KIINQMKPRQ LIIVHGPPEA SQDLAECCRA FGGKDIKVYM PKLHETVDAT
SETHIYQVRL KDSLVSSLQF CKAKDAELAW IDGVLDMRVS KVDTGVILEE GELKDDGEDS
EMQVDAPSDS SVIAQQKAMK SLFGDDEKET GEESEIIPTL EPLPPHEVPG HQSVFMNEPR
LSDFKQVLLR EGIQAEFVGG VLVCNNQVAV RRTETGRIGL EGCLCQDFYR IRDLLYEQYA
IV
//
