ID F7W3I1_SORMK Unreviewed; 1003 AA.
AC F7W3I1;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 13-SEP-2023, entry version 52.
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=SMAC_05921 {ECO:0000313|EMBL:CCC12183.1};
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC12183.1, ECO:0000313|Proteomes:UP000001881};
RN [1] {ECO:0000313|EMBL:CCC12183.1, ECO:0000313|Proteomes:UP000001881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC {ECO:0000313|Proteomes:UP000001881};
RC TISSUE=Mycelium {ECO:0000313|EMBL:CCC12183.1};
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(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 -!- 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:CCC12183.1}.
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; CABT02000024; CCC12183.1; -; Genomic_DNA.
DR RefSeq; XP_003345764.1; XM_003345716.1.
DR AlphaFoldDB; F7W3I1; -.
DR STRING; 771870.F7W3I1; -.
DR GeneID; 10803121; -.
DR KEGG; smp:SMAC_05921; -.
DR VEuPathDB; FungiDB:SMAC_05921; -.
DR eggNOG; KOG1135; Eukaryota.
DR HOGENOM; CLU_002227_3_0_1; -.
DR InParanoid; F7W3I1; -.
DR OMA; YVLEHAW; -.
DR OrthoDB; 198429at2759; -.
DR Proteomes; UP000001881; 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; 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:UP000001881};
KW RNA-binding {ECO:0000256|RuleBase:RU365006}.
FT DOMAIN 288..447
FT /note="Beta-Casp"
FT /evidence="ECO:0000259|SMART:SM01027"
FT REGION 515..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..539
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1003 AA; 109261 MW; 1E653B75D65FCDA5 CRC64;
MFSFCPLQGA LSDSSASQSL LELDGGVKIL IDVGWDETFD VEKLRELGRI APTLSLILLT
HATVPHLAAY AHCCKHFPPF QRIPVYATRP VIDLGRTLTQ DLYASTPLAA TTISSASLAE
VSYASGYSQA ASAENTFLLQ PPTPEEITKY FSLIQPLKYS QPHQPLPSPF SPPLNGLTIT
AYNSGHTLGG TIWHIQHGLE SIVYAVDWNH SRENVFAGAA WLSGNHGGAG STQVIEQLHK
PTALVCSSRT PDASLSRLKR DEQLMESIKL CIARGGTVLI PVDSSARVLE LSYLLEHAWR
KEVAKDNDVF KSAKLFLAGR TISSTMKNAR SMLEWMDDNI IKEFEAFADE SRRNNRRDEG
NHQTGPGPFD FKYLRLLERK AQIEKILKQS EDTEPRAKVI LASDASLDWG FSKDILKSIA
ADARNLVILT EKPNFEPNHK PSIARTLWEW WKERRDGVAT ERTSNGDTFE QVYAGNRELE
VETAERKGLE GDELNVYQQW LATQRQLQAT LQSGGTTTLE APGDVLDDAD TDTDTDSEGS
DTEQQGKALN IATTMAQASR KKVALKDEDL GVTILIKKEN TYDFNVRGKK GRDRMFPVAM
RRRRADEFGE LIRPEDYLRA EEREDAENAE AGQANNNTQE LEGLGKKRKW EDVGTAGRGR
GGLGPNKRPH HNDRRRLSAG EADAAPFSEN GPAGDDLSDL EDEEDDTLNG PAKLVVTKET
IPVHLRIAFV DFSGLHDKRS LTMLIPLIQP RKLVLVAGGK DETLALAADV KKLLIAQSTG
TESAIEVLTP AVGTTVDASV DTNAWVLKLA DPLVKGLKWQ NVRGLGIVTV TGLLLPGGEF
QPTSTEDADS AKRPKLEDGS APSEPSTALV KTGTNTLPTT TASLPTLDLV PPTLASSLSV
RSQAAQPLHV GELRLADLRR AMLSAGHKVE FKGEGTLLID DVVVVRKSTA QGGRVELESV
GLPSDTMPGT TSGGLLNAAM KVGGTFYAVR KKIYEGLAVV AGA
//