ID   A0A1A9Z6W8_GLOPL        Unreviewed;       713 AA.
AC   A0A1A9Z6W8;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
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   Glossina pallidipes (Tsetse fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC   Glossinidae; Glossina.
OX   NCBI_TaxID=7398 {ECO:0000313|EnsemblMetazoa:GPAI005723-PA, ECO:0000313|Proteomes:UP000092445};
RN   [1] {ECO:0000313|Proteomes:UP000092445}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAEA {ECO:0000313|Proteomes:UP000092445};
RA   Aksoy S., Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:GPAI005723-PA}
RP   IDENTIFICATION.
RC   STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GPAI005723-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) 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; A0A1A9Z6W8; -.
DR   STRING; 7398.A0A1A9Z6W8; -.
DR   EnsemblMetazoa; GPAI005723-RA; GPAI005723-PA; GPAI005723.
DR   VEuPathDB; VectorBase:GPAI005723; -.
DR   Proteomes; UP000092445; 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; 3.40.50.10890; -; 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   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   RNA-binding {ECO:0000256|RuleBase:RU365006}.
FT   DOMAIN          206..331
FT                   /note="Beta-Casp"
FT                   /evidence="ECO:0000259|SMART:SM01027"
SQ   SEQUENCE   713 AA;  81846 MW;  2B5E19F417C7A9B0 CRC64;
     MSRPPVTFCR LMRHVHTIDA VLLSHPDVYH LGALPYLVGK LGLNCPIYAT IPVHKMGQMF
     MYDLYMSHFN MYDFDLFSLD DVDAAFDKII QLKYNQTFSL KGKGYGITIT PLPAGHMIGG
     TIWKILKVGE EDIVYAMDFN HKKERHLNGC ELERFQRPSL LITDAFNALY QQARRRARDE
     KLMTNILQTV RNNGNVLIAV DTAGRVLELA HMLDQLWKNR ESGLMAYSLA LLNNFSYNVV
     EFAKSQIEWM SDKLMKTFEG ARNNPFQFKH MQLCHNLAEL SLLPGPKVVL ASTPDLESGF
     TRELFVQWAG NPINSVIFTS RTSQGTLATD LVENHIPGRK IELDLRRRVE LEGAELEEYL
     RTQGEKVNRL IVKQDVEEES SSDSDDDIEM SIITGKHDIV IRSEGRQHSG FFKSNKRHNV
     MFPFQEEKIK CDEYGEVINL DDYRIADMNY EASLEEHNKE NIKKEEMKGE KSKTEDEIQL
     LEKPTKCFNQ RKTIEVNCQI QRIDFEGRSD GESMLKILSQ LRPRRVIVVH GSEDATQVVA
     KHCQQNIGAR IFTPHKGETI DVTTETHIYQ VRLTEGLVTQ LQFQKSKNAE IAWVDARIGM
     RKQAIESPNN ENNADNDVTE AAEEEKTFTL ESLEADEIPV HNAVLINELK LSDFKQVLMR
     HNINSEFSGG VLWCCNGTLA LRRIDTGKVT MEGCLSEEYY RIRELLYEQY AFV
//