ID E4XDJ0_OIKDI Unreviewed; 764 AA.
AC E4XDJ0;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=GSOID_T00008233001 {ECO:0000313|EMBL:CBY19228.1};
OS Oikopleura dioica (Tunicate).
OC Eukaryota; Metazoa; Chordata; Tunicata; Appendicularia; Copelata;
OC Oikopleuridae; Oikopleura.
OX NCBI_TaxID=34765 {ECO:0000313|EMBL:CBY19228.1};
RN [1] {ECO:0000313|EMBL:CBY19228.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21097902; DOI=10.1126/science.1194167;
RA Denoeud F., Henriet S., Mungpakdee S., Aury J.M., Da Silva C.,
RA Brinkmann H., Mikhaleva J., Olsen L.C., Jubin C., Canestro C.,
RA Bouquet J.M., Danks G., Poulain J., Campsteijn C., Adamski M., Cross I.,
RA Yadetie F., Muffato M., Louis A., Butcher S., Tsagkogeorga G., Konrad A.,
RA Singh S., Jensen M.F., Cong E.H., Eikeseth-Otteraa H., Noel B.,
RA Anthouard V., Porcel B.M., Kachouri-Lafond R., Nishino A., Ugolini M.,
RA Chourrout P., Nishida H., Aasland R., Huzurbazar S., Westhof E., Delsuc F.,
RA Lehrach H., Reinhardt R., Weissenbach J., Roy S.W., Artiguenave F.,
RA Postlethwait J.H., Manak J.R., Thompson E.M., Jaillon O., Du Pasquier L.,
RA Boudinot P., Liberles D.A., Volff J.N., Philippe H., Lenhard B.,
RA Roest Crollius H., Wincker P., Chourrout D.;
RT "Plasticity of animal genome architecture unmasked by rapid evolution of a
RT pelagic tunicate.";
RL Science 330:1381-1385(2010).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FN653039; CBY19228.1; -; Genomic_DNA.
DR AlphaFoldDB; E4XDJ0; -.
DR InParanoid; E4XDJ0; -.
DR Proteomes; UP000001307; 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:UP000001307};
KW RNA-binding {ECO:0000256|RuleBase:RU365006}.
FT DOMAIN 241..366
FT /note="Beta-Casp"
FT /evidence="ECO:0000259|SMART:SM01027"
FT REGION 409..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 764 AA; 87745 MW; 4E5DA6599D5122BE CRC64;
MTSIVKFQSL SGFDDEAPHC HLLQIDDFKF LLDCGWAEQH HEKIIDGLKR HGRQIDAILI
SHPDLLHCGM LPYLSKLGIT CPIYMTMPAC KMGQMFLYDF VLSRTAVEDF DMFTLDDVDA
VFDRATQLKH NQTEAVRGQD YGIQIMPVQG HMIGGTTWKI MKDEEEEYVY CVDVNHKRET
HLNGIQLDAF DKPTLMITDC STYGYQQERR AKRTERLVQR IQNTTSKGGN VLITTDTAGR
SLEMALMLEG IWNDERYGLG RVNLVMVSNV ATSTIEAAKG MIEWMSEKII SKFTHKRENI
FDLTKMKLRS SIQEIARIPE PKVILATPMD MDTGFSRELF VMMAAHPKNA VIMSGRSTKG
SLCRKIIENE GMSSITLEMN KRLPLVGPEL EEYEKQKEQE RNANLIKRLE EESSDESENE
MSETISVRKK TVKGKRTHDI IMPHHVQKKE GGFFKKARKE KFPLFPFNEN RIKWDDYGEI
INPDDYKTHE LIPESEPVNI NNLTENQQSV TFGRHKPNDS RKKQKEEPVE EEKAPTKCIK
TREQVSIRCS IEFINFEGRV DGESQLQLLS TIKPKELILI RTKEKYKEKL FKDIKSRVQG
IRIHMPVHHE LIDATKESFI YQLKLKDSLL SNLNFVRVGS KDIEVARIRG RVDYFGGRLE
LEAENGENDE PKKLEIDDIP TLQPVTNNYS SGHDSIFIND TKLTELKSNL IDCGMHAEFI
GGNLVCNNKV SIKRSANGVI QVEGTLSEDY FIVRKMVYDN YAIV
//
