ID   A0A075AQM7_ROZAC        Unreviewed;       742 AA.
AC   A0A075AQM7;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   13-SEP-2023, entry version 35.
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=O9G_002305 {ECO:0000313|EMBL:EPZ32528.1};
OS   Rozella allomycis (strain CSF55).
OC   Eukaryota; Fungi; Fungi incertae sedis; Cryptomycota;
OC   Cryptomycota incertae sedis; Rozella.
OX   NCBI_TaxID=988480 {ECO:0000313|EMBL:EPZ32528.1, ECO:0000313|Proteomes:UP000030755};
RN   [1] {ECO:0000313|EMBL:EPZ32528.1, ECO:0000313|Proteomes:UP000030755}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CSF55 {ECO:0000313|EMBL:EPZ32528.1,
RC   ECO:0000313|Proteomes:UP000030755};
RX   PubMed=23932404; DOI=10.1016/j.cub.2013.06.057;
RA   James T.Y., Pelin A., Bonen L., Ahrendt S., Sain D., Corradi N.,
RA   Stajich J.E.;
RT   "Shared signatures of parasitism and phylogenomics unite Cryptomycota and
RT   microsporidia.";
RL   Curr. Biol. 23:1548-1553(2013).
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; KE561145; EPZ32528.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A075AQM7; -.
DR   STRING; 988480.A0A075AQM7; -.
DR   EnsemblFungi; EPZ32528; EPZ32528; O9G_002305.
DR   HOGENOM; CLU_002227_3_0_1; -.
DR   OMA; YVLEHAW; -.
DR   OrthoDB; 198429at2759; -.
DR   Proteomes; UP000030755; 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:UP000030755};
KW   RNA-binding {ECO:0000256|RuleBase:RU365006}.
FT   DOMAIN          244..357
FT                   /note="Beta-Casp"
FT                   /evidence="ECO:0000259|SMART:SM01027"
FT   REGION          408..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..422
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   742 AA;  84981 MW;  1DA427AB9CC19DAC CRC64;
     MTSFVKFTPI SGAFGDEPLC YLLEIDQQKI LLDCGCDPAF EVLPDLLSRI TKLTKTIDVI
     LLSHSNLEYL GGLVYVYKEM ALHCPIYATI PIMNFGPLTI QEALRAKCLD GPFSYFSMGD
     IMPVFEKCIG LRYLQNITLP GIVRGIHAVP YNAGHSLGAC IWRLRKDTDD IVYAVGYNHR
     KEKYVNEASL DAISRPTLLI TDSKHSLSST NPRKQREGEL FGICVKVLDN HGTVIIPVDT
     CSRSLELIYT FEQYWQNNKL DKPIFFLSSC SQKVIEYAKS TIEWMSENVK RSFENSRENP
     FNLKNIKLIS SMEELRDYRG GKIILATSES LENGFSRDLL VEFGKDKKNC LILPFKLSNS
     KFYSQILKFA ETKNREASIQ ISYQKEDDLV GEELESFLRE EIERKRKEEE EEEYKKQLEA
     ASDGEESDDE STNDKKRARL AEIEQERYWT LTQFDLNVKD ASFGGDFFKK SFTHQMFPYF
     EKRLKFDDYG ESIQAEDYLT ADDLEERRRA IEKERRLNQL KEDEPQKSQR PKKWVGYDFT
     LHLRLYMRAI DFGGYADGRS IKNILTHISP KKIILIGGSP EATTALAQYC NFSNDITNDV
     ISPKLLEVVN VSSNTNIYQI KLTDAILSSL QFEKLASYEL SFINGIVGKK SEEDTSTVPT
     LDIISDQSKV ADVRQPIFIG DVKLSEFRKL CNQSGLMTQF YKGDLVCNDS VIDSTGKLTI
     EGNLTDAYYK VRNLLYRQHA II
//