ID   A0A3B4H966_9CICH        Unreviewed;       788 AA.
AC   A0A3B4H966;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
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};
OS   Pundamilia nyererei.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX   NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000030989.1, ECO:0000313|Proteomes:UP000261460};
RN   [1] {ECO:0000313|Ensembl:ENSPNYP00000030989.1}
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   AlphaFoldDB; A0A3B4H966; -.
DR   STRING; 303518.ENSPNYP00000030989; -.
DR   Ensembl; ENSPNYT00000031738.1; ENSPNYP00000030989.1; ENSPNYG00000023356.1.
DR   GeneTree; ENSGT00910000144260; -.
DR   Proteomes; UP000261460; Unplaced.
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; 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          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"
FT   REGION          408..429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   788 AA;  89241 MW;  DB5D8E5CD30795DD CRC64;
     MTSIIKLTAV SGVLEESALC YLLQVDEFRF LLDCGWDENF STEIIDAMKR HVHQVDAVLL
     SHPDPIHLGA LPYAVGKLGL NCTIYATIPV YKMGQMFMYD LYQSRNNSED FTLFTLDDVD
     AAFDKIQQLK YSQIVNLKGK GHGLSITPLP AGHMIGGTIW KIVKDGEEEI VYAVDFNHKR
     EIHLNGCSLE SLSRPSLLIT DSFNAAYVQP RRKQRDEQLL TNVMETLRGD GNVLIAVDTA
     GRVLELAQLL DQIWRTKDAG LGAYPLALLN NVSYNVVEFS KSQVEWMSDK LMRCFEDKRN
     NPFQFRHLTL CHSLADLARV PSPKVVLCSQ PDLESGFSRE LFIQWCQNAK NSIILTYRTT
     PGTLARYLID NPGEMMLDLE VRPKRVKLEG KELEEYLEKE KLKKETAKKL EQAKEVDVDS
     SDESDMDDDL DQSAVVKTKH HDLMMKGEGS RKGSFFKQAK KSYPMFPTHE ERIKWDEYGE
     IIRLEEFLVP ELQATEEEKS KLESGLTNGD EPMDQDLSVV PTKCISSIES LEIRARVMYI
     DYEGRSDGDS IKKIINQMKP RQLVIVRGPP EASLDLAESC KAFSKDIKVY TPKLQETVDA
     TSETHIYQVR LKDSLVSSLQ FCKAKDTELA WIDGVLDMRV VKVDTGVILE EGVKDEAEES
     ELAMDIAPDL DIDPINIAVT AQRAMKNLFG EDEKEFSEES DVIPTLEPLP PNEVGRHQSV
     FINEPRLSDF KQVLLREGIQ AEFVGGVLVC NNMVAVRRTE AGRIGLEGCL CDDYYKIREL
     LYQQYAVV
//