ID   A0A1Z5TFR2_HORWE        Unreviewed;       963 AA.
AC   A0A1Z5TFR2;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   13-SEP-2023, entry version 20.
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=BTJ68_05364 {ECO:0000313|EMBL:OTA34849.1};
OS   Hortaea werneckii EXF-2000.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX   NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA34849.1, ECO:0000313|Proteomes:UP000194280};
RN   [1] {ECO:0000313|EMBL:OTA34849.1, ECO:0000313|Proteomes:UP000194280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA34849.1,
RC   ECO:0000313|Proteomes:UP000194280};
RA   Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA   Nislow C.E.;
RT   "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT   insights from long-read sequencing.";
RL   Submitted (JAN-2017) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OTA34849.1}.
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DR   EMBL; MUNK01000053; OTA34849.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z5TFR2; -.
DR   STRING; 1157616.A0A1Z5TFR2; -.
DR   VEuPathDB; FungiDB:BTJ68_05364; -.
DR   InParanoid; A0A1Z5TFR2; -.
DR   OrthoDB; 198429at2759; -.
DR   Proteomes; UP000194280; 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   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; 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|RuleBase:RU365006};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365006};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194280};
KW   RNA-binding {ECO:0000256|RuleBase:RU365006}.
FT   DOMAIN          288..438
FT                   /note="Beta-Casp"
FT                   /evidence="ECO:0000259|SMART:SM01027"
FT   REGION          492..532
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          613..746
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        492..511
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        512..527
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        613..650
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        662..686
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        715..736
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   963 AA;  104391 MW;  061BF119DD14CCE4 CRC64;
     MFTLTPLLGA RTPSSPAAST LLELDGGIRI LVDIGWDASF SSHQIVAALE KHVSTLSIIL
     LTHPTIDHLG AYAWCCKHVP LFRHVPCYAT VPVVDLGRGV CLDIHGCPGG VSGGTVPTSS
     VASADAAAAD DHIAESKSPH ILLEPPSPDE IAACFNAIHP LKYSQPHQPI AASFSPSVGG
     LTITAYGAGH TLGGTIWHIQ HGLESIVYAT DWSQARESLY PGAAWLTNGS EIIEPLRRPT
     ALVCSSKGVE KTEVLSRKKR DDTILSLVRE TIAQGGKVLI PTDSSARVLE LAFLLNQTWR
     ENVDGPHSST YRHCRIYMAS RSATTSVRYL NSMLEWVDET VRQEAEAAMS SKGKKGDQAT
     VNPLEWDFVR QIERQSQVQK ALNRRRPCVM LASDQDMEWG FSKEVFEGMA RDSRNLVLLS
     ERQPEVRSSG RKGLGRQLWE LFNNSDGQTS SQSGAKVVSM DGTSVTLHEP KTESLNADEL
     ALYQTYTARQ QQLHSTLQGD NTSTDPTSAA NMTEEADEED ESESEDEDAE HQGRALNLSA
     QMTQQSKRKG GVTGGALSEV ELGINILIRG KGVYDYDVRG KRGREKVFPF VAKRIRDDEF
     GELIKAEDYL RAEERDEVDG VDTSSRPEAE KKETAVGQKR KWDDIAPASD AKGRKGQQKT
     QQNKRPKQER SKKDRKPREP DDIDAAIARA TGESMPNGGG DATAAAAAAA SPAADDESED
     SDSDEEDEES DYEPSDEAGD SQGPRKVIWE ERTVEVKCRV SFVDFAGLHE KRDLQMIIPL
     IRPRKLILIA GTESETTLLA DECRRLLGSI DNGADGSEGG ADVFAPAINE VIDASVDTNA
     WSLKLSRELV KRNLSAGSAT SGTSGGAGPL TRPVHVGDLR LASLRHLLAS AGHLCEFRGE
     GTLLVDGVVV VRKRAGGRLE VESDVRGLVA AAAAARQKKR VSPGSFFKVR DEVYKGLAVV
     AGV
//