ID A0A179UYM1_BLAGS Unreviewed; 1275 AA.
AC A0A179UYM1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=ribonuclease Z {ECO:0000256|ARBA:ARBA00012477};
DE EC=3.1.26.11 {ECO:0000256|ARBA:ARBA00012477};
GN ORFNames=BDBG_07583 {ECO:0000313|EMBL:OAT12207.1};
OS Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=559298 {ECO:0000313|EMBL:OAT12207.1, ECO:0000313|Proteomes:UP000002038};
RN [1] {ECO:0000313|Proteomes:UP000002038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SLH14081 {ECO:0000313|Proteomes:UP000002038};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of RNA, removing extra 3' nucleotides
CC from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy
CC group is left at the tRNA terminus and a 5'-phosphoryl group is left
CC at the trailer molecule.; EC=3.1.26.11;
CC Evidence={ECO:0000256|ARBA:ARBA00000402};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the RNase Z family.
CC {ECO:0000256|ARBA:ARBA00007823}.
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DR EMBL; GG657466; OAT12207.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A179UYM1; -.
DR STRING; 559298.A0A179UYM1; -.
DR VEuPathDB; FungiDB:BDBG_07583; -.
DR OrthoDB; 296811at2759; -.
DR Proteomes; UP000002038; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0042781; F:3'-tRNA processing endoribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd07718; RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 2.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR047151; RNZ2-like.
DR InterPro; IPR027794; tRNase_Z_dom.
DR PANTHER; PTHR12553; ZINC PHOSPHODIESTERASE ELAC PROTEIN 2; 1.
DR PANTHER; PTHR12553:SF49; ZINC PHOSPHODIESTERASE ELAC PROTEIN 2; 1.
DR Pfam; PF12706; Lactamase_B_2; 2.
DR Pfam; PF13691; Lactamase_B_4; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002038};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 141..203
FT /note="tRNase Z endonuclease"
FT /evidence="ECO:0000259|Pfam:PF13691"
FT DOMAIN 781..833
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF12706"
FT DOMAIN 943..1036
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF12706"
FT REGION 315..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1200..1275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1086
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1200..1243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1275 AA; 141789 MW; DF4C8A7E30449968 CRC64;
MSWCLLVDIR RPDRENSGKL ASLRAAGTLL TNAIRRTSLF PVPAPYSCLL KYKPPGKSRH
FNANARRTTP NELPYRTSDF PREPTLELPI FLAPKLDPYK LGGVHWDRYL FYDPDNISLY
PGTRAFDSKA SGHHPMIFFC EFITTPTADT PGTSLIIHFD DKRYLFGHIP EGLQRACNHR
NIRLSYVTDI FMSGRTSWTN NGGLLGIILT LAESVNTSAW SQREVRQAKT LRLKRLAEQT
ENREQWQYYR DRIELLEESN RRLAEGFDLR GKLAIHGGPN LTRTVATARK FIFRTGMPVY
INEFNEFSNE FAVGKEEGQG GREGEGKGEG CERNVAKPTW TDSHLKVWAL SVSPTSSRGS
PVGSAEDTKN ARKRSLDEFQ EGAGAAAANE LRSEGKNVSD SDKRAQDQIV CQAVVSDMFN
SDWRLDSLVE MRLPEVRLPA KVFVRNRETH KLEPYTGPVP DGTQPVPDIP VLVRKPWPGA
MTQTLPPTTP SDVSISYIIQ HHDVRGKFNP AKAIALGVKK GPKFGKLTSG QSVESSDGKI
ITPDMVLGES QPGGGLAFVD IPTPDYVENL VNRPEWTTPE VMKGLASFIW ILGPGVGSHP
LLQEFVSKMS QYKHIVSSPD YCPNYLAFSL GSTETAHFSF IDNERFHLPH HNNEEVPQKT
FLTPGPLPDS STKDPLKSVF IPARPNLRVE LQPKFQINSS GVHQPLDGEG IRNNVSFRVK
RAARAANQDI QSPQFQEFLE NVRRNVPNQD AEIITLGTGS SLPSKYRTVS ATLLRVPGVG
NYLFDCGENT LGQLQRAFSP EELREVLRDL KVIWISHLHA DHHLGTVSVI RAWHEVTHGA
LSSTAPVPEP EYDLTKLLSE KRLFVASDAK MIEWLAEYSG IENYGFDKLL PVEADTSFGD
NFKYSHLSRD RQPILDENGN PVKIHLSFNP DRSPFATQLQ QATGLSSLLT VPVMHCHGAM
ATSFVFPSGF KVSYSGDCRP SREFARIGAD STVLIHEATF EDDMLRDAKA KRHSTCGEAL
RVAERMRARN VILTHFSQRY AHKPTVPRLK IWDASNCGSP SRSPSRSPSR SPSSPAARSE
SGSPQPNRRP HDIGEWRANN PPDVPVSKND LGNDNGSDYG NGDGRGSGSR WRDQIRSGPA
PAMMQLDGVP VPVIVAFDLL RVRVGDMLCA QRYVPVHNLY YDSRLARAAH YGGWRQRENR
HTEADAGADA SAGDGAKEKQ KPWKKGWMKE EEGNKDKRRG KRQSSSSSTS SATTRVDHGG
HGEDAPQKVA GSMGD
//
