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Database: UniProt
Entry: F7W3I1_SORMK
LinkDB: F7W3I1_SORMK
Original site: F7W3I1_SORMK 
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}.
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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
//
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