ID R1GDC7_BOTPV Unreviewed; 746 AA.
AC R1GDC7;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Putative cleavage and polyadenylation specifity factor protein {ECO:0000313|EMBL:EOD49565.1};
GN ORFNames=UCRNP2_3642 {ECO:0000313|EMBL:EOD49565.1};
OS Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS (Neofusicoccum parvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Neofusicoccum.
OX NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD49565.1, ECO:0000313|Proteomes:UP000013521};
RN [1] {ECO:0000313|Proteomes:UP000013521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA Blanco-Ulate B., Rolshausen P., Cantu D.;
RT "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT vascular pathogen associated with grapevine cankers.";
RL Genome Announc. 1:E0033913-E0033913(2013).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC metabolizing metallo-beta-lactamase-like family. CPSF2/YSH1 subfamily.
CC {ECO:0000256|ARBA:ARBA00010624}.
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DR EMBL; KB916070; EOD49565.1; -; Genomic_DNA.
DR RefSeq; XP_007582936.1; XM_007582874.1.
DR AlphaFoldDB; R1GDC7; -.
DR STRING; 1287680.R1GDC7; -.
DR KEGG; npa:UCRNP2_3642; -.
DR eggNOG; KOG1137; Eukaryota.
DR HOGENOM; CLU_009673_2_1_1; -.
DR OMA; CKQHITL; -.
DR OrthoDB; 169081at2759; -.
DR Proteomes; UP000013521; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR CDD; cd16292; CPSF3-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; IPR021718; CPSF73-100_C.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR PANTHER; PTHR11203; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR FAMILY MEMBER; 1.
DR PANTHER; PTHR11203:SF11; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 3; 1.
DR Pfam; PF10996; Beta-Casp; 1.
DR Pfam; PF11718; CPSF73-100_C; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM01027; Beta-Casp; 1.
DR SMART; SM01098; CPSF73-100_C; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000013521}.
FT DOMAIN 36..251
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT DOMAIN 263..407
FT /note="Beta-Casp"
FT /evidence="ECO:0000259|SMART:SM01027"
FT DOMAIN 450..702
FT /note="Pre-mRNA 3'-end-processing endonuclease
FT polyadenylation factor C-term"
FT /evidence="ECO:0000259|SMART:SM01098"
FT REGION 427..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 746 AA; 82457 MW; BC17A1F4E9D87D8E CRC64;
MAAKRKAAAM SPGSDEPVDP ADELLFYCLG GGNEVGRSSH IIQYKGKTVM LDAGMHPAYD
GLAALPFYDE FDLSTVDVLL ISHFHIDHAA SLPYVLSKTN FKGRVFMTHP TKAIYKWLIQ
DSVRVGNISS SSESRIQLYT EADHLSTFPQ IEAIDYYTTH TISSIRITPY PAGHVLGAAM
FLIEIAGLKI LFTGDYSREE DRHLISAEVP KNVKVDVLIT ESTFGIASHI PRLEREAALM
KSITSIINRG GRALLPVFAL GRAQELLLIL DEYWAKHPEF QKIPIYYASN IARKCMVVYQ
TYVYAMNDNI KRLFRERMEE AERNGDASKA GPWDFKYVRS LKSLERFDDV GGCVMLASPG
MMQNGVSREL LERWAPDQRN GVIMTGYSVE DKKQPVKVFS PANCEELRIP FKADKIAKVV
GKLAQIPPPM PYRPRQEDGA VEAEDEEEQQ PQLISGVLVQ NDFKMSLMAP EDLREYAGLT
TTTIVCRQHL TLSAAGIDLI RWALEGTFGA LRQINGKDAA INGKTETNGN GEHKVDEDEA
DEEIDRSTTS FIVMDCVTIH CHNGGRVEVE WEGNMINDGI ADAVLAVLFT VESSPAAVKQ
STSKHSHAHA HTPNPHAAAD PRTRFDRLCM FLEAQFGASN TTPIAHPKLP ESASGESTES
PAADQPAKTV SIAGLPLSEG DDAFSAAEQA ELKRLHALGI PVPGIAIKVD KLVARVWLET
LDVECPNGVL RDRCEYVVKL VWKSDY
//