ID   A0A183TBD5_SCHSO        Unreviewed;       983 AA.
AC   A0A183TBD5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
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   Schistocephalus solidus (Tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Diphyllobothriidea; Diphyllobothriidae; Schistocephalus.
OX   NCBI_TaxID=70667 {ECO:0000313|Proteomes:UP000050788, ECO:0000313|WBParaSite:SSLN_0001430401-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SSLN_0001430401-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU365006}.
CC   -!- SIMILARITY: Belongs to the SIKE family.
CC       {ECO:0000256|ARBA:ARBA00005537}.
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; A0A183TBD5; -.
DR   WBParaSite; SSLN_0001430401-mRNA-1; SSLN_0001430401-mRNA-1; SSLN_0001430401.
DR   Proteomes; UP000050788; 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   InterPro; IPR008555; SIKE.
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   Pfam; PF05769; SIKE; 1.
DR   SMART; SM01027; Beta-Casp; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
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..348
FT                   /note="Beta-Casp"
FT                   /evidence="ECO:0000259|SMART:SM01027"
FT   COILED          942..969
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   983 AA;  109849 MW;  B601EBB7480FBD1B CRC64;
     LEDNPPSFAK ELSKWVKMID AVLISHPSMR HLGLLPVLVG KYGLKCPIYA TTPVYKLGQL
     VLYDAYQSRY VSGDSSSFSL DDVDAAFELI VQVKYQQTIN LQGRGHGLSV TPLPSGHMLG
     GTIWKLIKDE TDIIYAIDFN HKKGRHLNGA TFDACIRPRL LIIDVSNALY THSRRKNREE
     ALRQLLLRTL RRGGNVLIAV DTAGYCLEIA HLLETLWHIQ DSGFMAYGLA MLTHVAYNVF
     DSAKSLVEWM SDKIVRTFED QRSNPFHLRH LQLCHTLDEL DFVPDPKVIL ASEPDLRSGF
     SRLLFTEWSD SDLNTVIVTS RNGDFRQVED LSEFFSPVGP GLSLGRRLIG LANNESWARV
     GVPTGANGAL MLPFTFSQRV VVECPPEAST ADLSSSLNDS NFARRISSFG GKDQQLYNDL
     NTLENVVDDD DDAYNDEDED IGQTDLRRQL SSTSALVSEN ASHVAPSNTY QPYELTLSST
     PTLTHGRHHA GYDIFPGAYN HSGGQFFRMT KRTQLVFPTV EKTVSWDEYG ERVDPAVYKM
     SAEPFEVSTV DKRGKPPPRD ISRLLSESAM DLSKGSDLPG QPAQFDIVSA SQDQLLDLLV
     LQNSTSLIPG ATLPNNFTTK CVVKKLELPL RCELSFIDYE SRSDGEALKK IITGLRPQEV
     ILVGGTNKAI THIAEHCQSV LMLKSDLIHV PQGLDVVNCT KEGDIYQARM KDSLVTGLKF
     TKIREYELAW VEADIAESDS PSSKKDESAQ MDAEGELGAP AIRASVVSDS LPMLVPASNH
     VVQHDTVFVN EPKLSDLKQI LLNLGMSAEF VSGVLVVDNC VAIKRSEAGR LLLEGMLCKV
     YYDVRAVLYR QFAILFSSFR SALTLPPFQT HFYSTYVCCC LKRQIQIFTL TVFILCLYSL
     FFSIDAPLGI SENADYREES LEYVEIAKRA EKSPRRPLVL CLAAENKQLE QLKMQNLTLE
     KSLTEHQSAL EMIMTKYLNL FRY
//