ID H6CA91_EXODN Unreviewed; 948 AA.
AC H6CA91;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=HMPREF1120_08027 {ECO:0000313|EMBL:EHY60055.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY60055.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY60055.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY60055.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) 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 ---------------------------------------------------------------------------
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; JH226136; EHY60055.1; -; Genomic_DNA.
DR RefSeq; XP_009160516.1; XM_009162268.1.
DR AlphaFoldDB; H6CA91; -.
DR STRING; 858893.H6CA91; -.
DR GeneID; 20312666; -.
DR VEuPathDB; FungiDB:HMPREF1120_08027; -.
DR eggNOG; KOG1135; Eukaryota.
DR HOGENOM; CLU_002227_3_0_1; -.
DR InParanoid; H6CA91; -.
DR OMA; YVLEHAW; -.
DR OrthoDB; 198429at2759; -.
DR Proteomes; UP000007304; 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:UP000007304};
KW RNA-binding {ECO:0000256|RuleBase:RU365006}.
FT DOMAIN 283..426
FT /note="Beta-Casp"
FT /evidence="ECO:0000259|SMART:SM01027"
FT REGION 339..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..527
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..666
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 948 AA; 103521 MW; 7D0A594D4928559C CRC64;
MFTFTPLLGA QSDSRASQSL LELDGGVKIL VDVGWDERFD TRQLTEIEKH TSTLSFILLT
HPTISHIGAF AHCCKHIPLF SQVPIYATPP VIAFGRTLLE DLYSSSPLAA TFIPGSASPE
DGTSADDKSR SNILRQAPTF EEINKYFQLI SPLKYSQPLQ PTASQFSAPV EGLTLTAYNA
GHTLGGTIWH IQQGMESIVY AVDWNQAREN VVAGAAWFGG VGGAEVIEQL RKPSALVCSS
VGATRVALSG GRKARDDALL GHIKTSVAKG GTVLIPTDSS ARVLELAWLL EKAWSDPAHS
ASFKDVKVYM ASRSGNATLR HARSLLEWMD DSIVREFEGE DENPTTQPYN RRGGNKAAGT
NKPSRPFEFK NVKVVERKHQ LEKLLKVEGP RVILASDVTL DWGFSRSLLE HVVQKPENLV
ILTERLNVRP GSESPGQAFW QWFEQRQDGV ALERTEGGGQ LEQVHSGGRM LKLKNPEKAP
LSAQESQRYQ QYMATQRQIQ ESLTTTERDQ TVADDNIDDE SSSSSSEESD DEQQGRVLNV
SAALGHGARN KLALSDEDLG VNILLRKKGV YDYDVRNKKG RNAVFPYTHS RKRGDEFGEF
IKPEDFLREE EKEEQDAANS GKTGGTLGQK RKWEDTNNAN DSRSKRARGQ GPKGHAPDGH
GDESDSEASD IEGEVEVEGI QGPAKVVYTT TEITVNARLT FVDFAGLHDQ RSLQMLIPLI
GPKKLILVGG TEAETLSLAS DCKELLGMKV AGAEEQTSTE IFSPTIGQTV DASVDTNAWI
VKLSRALVRT LRWQNVKNMG VVTVQGQLKA EQEQENDLPD DPLLKKQKLE TEAAAQAQAP
PPPPLVPVLD VLPASLAAST RSVTQPIHVG DLRLADLRRI IAMDGHVAEF RGEGTLLVDG
TVVVKKLATG KIIVEGIPAN GSAMTRSAAD NYTRVKRKVY EGLAVVAA
//
