ID   F4WAT5_ACREC            Unreviewed;       737 AA.
AC   F4WAT5;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 46.
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=G5I_02628 {ECO:0000313|EMBL:EGI68691.1};
OS   Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS   echinatior).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Acromyrmex.
OX   NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN   [1] {ECO:0000313|EMBL:EGI68691.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Nygaard S., Zhang G.;
RT   "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT   adaptations to social evolution and fungus farming.";
RL   Submitted (FEB-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; GL888053; EGI68691.1; -; Genomic_DNA.
DR   RefSeq; XP_011049258.1; XM_011050956.1.
DR   AlphaFoldDB; F4WAT5; -.
DR   STRING; 103372.F4WAT5; -.
DR   EnsemblMetazoa; XM_011050956.1; XP_011049258.1; LOC105142998.
DR   GeneID; 105142998; -.
DR   KEGG; aec:105142998; -.
DR   eggNOG; KOG1135; Eukaryota.
DR   InParanoid; F4WAT5; -.
DR   OrthoDB; 198429at2759; -.
DR   Proteomes; UP000007755; 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   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   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:UP000007755};
KW   RNA-binding {ECO:0000256|RuleBase:RU365006}.
FT   DOMAIN          243..368
FT                   /note="Beta-Casp"
FT                   /evidence="ECO:0000259|SMART:SM01027"
FT   REGION          406..428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   737 AA;  83655 MW;  075CA06C9843AB9A CRC64;
     MTSIIKLHAI SGAMNESPPC YILQVDELRI LLDCGWDENF DQDFIKELKR HVHQIDAVLL
     SYPDPLHLGA LPYLVGKCGL NCPIYATIPV YKMGQMFMYD IYQSRHNMED FDLFTLDDVD
     AAFDKIVQLK YNQSISMKGK GYGVTLTPLP AGHMIGGTIW KIVKVGEEDI IYAVDFNHKK
     ERHLNGCELE RLQRPSLLIT DAFNATYQQA RRRTRDEKLM TNILQTLRGG GNVLVSVDTA
     GRVLELAHML DQLWRNKESG LLAYSLALLN NVSYNVVEFA KSQIEWMSDK LMRSFEGARN
     NPFQFKHLQL CHSMAELNQV PSPKVVLAST PDMECGFSRE LFLQWCSNPQ NSIILTSRTS
     PGTLARDLVE KGGNRNITLE VKRRVKLEGI ELEEYQKREK LKQEQLKQEQ METADVSSES
     EDEIEVGGSR GKHDLLVKQE SKPGFFKQSK KQHPMFPFVE EKIKIDEYGE IIKPEDYKIA
     EIVPEVEDNK ENVEMKQDEF NYHPEVAVDI PTKCVQVSRM MTVNAAVTYI DFEGRSDGES
     LQKILAQLRP RRVVLVRGSP KDTEILAQQA QSTGARVFIP GRGETLDATT ETHIYQVRLT
     DALVSGLNFS KGKGDSEVAW IDAMITARDQ ICRDAIADTE SENAIDESDK ILTLEPLPLN
     EVPGHQTTFI NELKLSDFKQ VLNKSNIPSE FSGGVLWCCN NTIAVRRHEA GKVILEGCIS
     EDYYKVRELL YEQYAIV
//