ID M3Y8A5_MUSPF Unreviewed; 801 AA.
AC M3Y8A5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, 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=CPSF2 {ECO:0000313|Ensembl:ENSMPUP00000007562.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000007562.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000007562.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AEYP01004231; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01004232; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01004233; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01004234; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01004235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3Y8A5; -.
DR STRING; 9669.ENSMPUP00000007562; -.
DR Ensembl; ENSMPUT00000007683.1; ENSMPUP00000007562.1; ENSMPUG00000007617.1.
DR eggNOG; KOG1135; Eukaryota.
DR GeneTree; ENSGT00910000144260; -.
DR HOGENOM; CLU_002227_1_1_1; -.
DR InParanoid; M3Y8A5; -.
DR OMA; YVLEHAW; -.
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 RNA-binding {ECO:0000256|RuleBase:RU365006}.
FT DOMAIN 36..242
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT DOMAIN 262..387
FT /note="Beta-Casp"
FT /evidence="ECO:0000259|SMART:SM01027"
FT REGION 426..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 801 AA; 90681 MW; 77C2BD90AAB80602 CRC64;
MEDQLGTGKL DFLDCYWTKM TSIIKLTTLS GVQEESALCY LLQVDEFRFL LDCGWDEHFS
MDIIDSLRKH VHQIDAVLLS HPDPLHLGAL PYAVGKLGLN CAIYATIPVY KMGQMFMYDL
YQSRHNTEDF TLFTLDDVDA AFDKIQQLKF SQIVNLKGKG HGLSITPLPA GHMIGGTIWK
IVKDGEEEIV YAVDFNHKRE IHLNGCSLEM LSRPSLLITD SFNATYVQPR RKQRDEQLLT
NVLETLRGDG NVLIAVDTAG RVLELAQLLD QIWRTKDAGL GVYSLALLNN VSYNVVEFSK
SQVEWMSDKL MRCFEDKRNN PFQFRHLSLC HGLSDLARVP SPKVVLASQP DLECGFSRDL
FIQWCQDPKN SIILTYRTTP GTLARFLIDN PSEKITEIEL RKRVKLEGKE LEEYLEKEKL
KKEAAKKLEQ SKEADIDSSD ESDVEEDIDQ PSAHKTKHDL MMKGEGSRKG SFFKQAKKSY
PMFPAPEERI KWDEYGEIIK PEDFLVPELQ ATEEEKSKLE SGLTNGDEPM DQDLSDVPTK
CISTTESIEI KARVTYIDYE GRSDGDSIKK IINQMKPRQL IIVHGPPEAS QDLAECCRAF
GGKDIKVYMP KLHETVDATS ETHIYQVRLK DSLVSSLQFC KAKDAELAWI DGVLDMRVSK
VDTGVILEEG ELKDDGEDSE MQVDAPSDSS VIAQQKAMKS LFGDDEKETG EESEIIPTLE
PLPPNEVPGH QSVFMNEPRL SDFKQVLLRE GIQAEFVGGV LVCNNQVAVR RTETGRIGLE
GCLCQDFYRI RDLLYEQYAI V
//
