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Database: UniProt
Entry: A0A365MU40_GIBIN
LinkDB: A0A365MU40_GIBIN
Original site: A0A365MU40_GIBIN 
ID   A0A365MU40_GIBIN        Unreviewed;       832 AA.
AC   A0A365MU40;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Endoribonuclease YSH1 {ECO:0000313|EMBL:RBA12060.1};
GN   ORFNames=FPRO05_03510 {ECO:0000313|EMBL:RBA12060.1};
OS   Gibberella intermedia (Bulb rot disease fungus) (Fusarium proliferatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=948311 {ECO:0000313|EMBL:RBA12060.1, ECO:0000313|Proteomes:UP000251714};
RN   [1] {ECO:0000313|EMBL:RBA12060.1, ECO:0000313|Proteomes:UP000251714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ITEM 2341 {ECO:0000313|EMBL:RBA12060.1,
RC   ECO:0000313|Proteomes:UP000251714};
RA   Almiman B.F., Shittu T.A., Muthumeenakshi S., Baroncelli R.,
RA   Sreenivasaprasada S.;
RT   "Genome sequence of the mycotoxigenic crop pathogen Fusarium proliferatum,
RT   strain ITEM 2341 from Date Palm.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:RBA12060.1}.
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DR   EMBL; PKMI01000039; RBA12060.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A365MU40; -.
DR   Proteomes; UP000251714; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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   InterPro; IPR011108; RMMBL.
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; PF16661; Lactamase_B_6; 1.
DR   Pfam; PF07521; RMMBL; 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   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT   DOMAIN          37..246
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
FT   DOMAIN          263..398
FT                   /note="Beta-Casp"
FT                   /evidence="ECO:0000259|SMART:SM01027"
FT   DOMAIN          532..784
FT                   /note="Pre-mRNA 3'-end-processing endonuclease
FT                   polyadenylation factor C-term"
FT                   /evidence="ECO:0000259|SMART:SM01098"
FT   REGION          599..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          685..706
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          739..768
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        599..620
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        689..706
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   832 AA;  92225 MW;  EB08D42DB587F14E CRC64;
     MASKRKASAM NAAAAEEPVD PSDELMFLCL GGGNEVGRSC HIIQYKGKTV MLDAGQHPAY
     DGLAALPFYD DFDLSTVDVL LISHFHIDHA ASLPYVLAKT NFRGRVFMTH PTKAIYKWLI
     QDSVRVGNTS SNPTTQPVYT EQDHLNTFPQ IEAIDYHTTH TISSIRITPY PAGHVLGAAM
     FLIEIAGLNI FFTGDYSREQ DRHLVSAEVP KGVKIDVLIT ESTYGIASHV PRLEREQALM
     KSITSILNRG GRVLMPVFAL GRAQELLLIL DEYWGKHADF QKYPIYYASN LARKCMLIYQ
     TYVGAMNDNI KRLFRERMAE AEASGDGAGK GGPWDFKYIR SLKNLDRFDD VGGCVMLASP
     GMLQNGVSRE LLERWAPSEK NGVIITGYSV EGTMAKQIMQ EPDQIQAVMS RSMAGARRMP
     GGDGEKVLIP RRCSVQEYSF AAHVDGVENR EFIEEVAAPV VILVHGEQHN MMRLKSKLLS
     LNANKTAKVK VYSPRNCEEL RIPFKADKTA KVVGKLASIQ PPQSIHPDQS AAPPLVTGVL
     VQNDFKLSLM APEDLREYAG LNTTTITCKQ RLTLSAAGVD LVKWALEGTF GNIEELPEMR
     RGKNGQSNGH GDHMITDGEE TNQEDADEEV ASLVAAYLVM GCVSVRYRTN GEVELEWEGN
     MLNDGIADSV MAVLFSVESS PAAVKRSSAK HSHSHELPDV NPHHSASPEE RLERLLWFLE
     AQFGQDNVAP VTTPKLPAVE DTEDKIKKDE ADDAMKTEED SEDTQLQERQ QKEIDRLHKI
     GIPVPGVSIK VDRMNATVWL EDLEVESNNK VFADRVRAVV ERAVEVTAPL WG
//
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