ID   A0A0M8VL29_9ACTN        Unreviewed;       850 AA.
AC   A0A0M8VL29;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=MPN domain-containing protein {ECO:0000259|PROSITE:PS50249};
GN   ORFNames=ADL01_23590 {ECO:0000313|EMBL:KOV67989.1};
OS   Streptomyces sp. NRRL WC-3618.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1519490 {ECO:0000313|EMBL:KOV67989.1, ECO:0000313|Proteomes:UP000037738};
RN   [1] {ECO:0000313|EMBL:KOV67989.1, ECO:0000313|Proteomes:UP000037738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL WC-3618 {ECO:0000313|EMBL:KOV67989.1,
RC   ECO:0000313|Proteomes:UP000037738};
RA   Noorani M.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KOV67989.1}.
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DR   EMBL; LGDW01000303; KOV67989.1; -; Genomic_DNA.
DR   RefSeq; WP_053743995.1; NZ_LGDW01000303.1.
DR   AlphaFoldDB; A0A0M8VL29; -.
DR   PATRIC; fig|1519490.3.peg.5147; -.
DR   OrthoDB; 6377837at2; -.
DR   Proteomes; UP000037738; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR028090; JAB_dom_prok.
DR   InterPro; IPR037518; MPN.
DR   InterPro; IPR032865; Prok-E2_A.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR43267; TRNA THREONYLCARBAMOYLADENOSINE DEHYDRATASE; 1.
DR   PANTHER; PTHR43267:SF1; TRNA THREONYLCARBAMOYLADENOSINE DEHYDRATASE; 1.
DR   Pfam; PF14457; Prok-E2_A; 1.
DR   Pfam; PF14464; Prok-JAB; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR   SUPFAM; SSF102712; JAB1/MPN domain; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS50249; MPN; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037738};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          650..792
FT                   /note="MPN"
FT                   /evidence="ECO:0000259|PROSITE:PS50249"
FT   REGION          806..850
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   850 AA;  91127 MW;  6F11FE771719944D CRC64;
     MSDRTTTAVT AGQQLALDQL RQITGSARGG VFLAHVDTAP AKAPTGFVEA RISVGCAGLS
     RAEGGLRLRS EEPVTLYIPP DFPFEVPLVY TRHSRFAGAP HVVWAHFPCL YRSTATEWDP
     ADGMYGFITR LLDWFRAAAA GELDAPGEPL HPPHAVGDYA DGLLVVRRDA PAAEDDEPWL
     GAALLHRISD ERSDVVGWLP FGQPWPPTLA DARAAAQLPN GAEVFLAPAV ITADHLTFEY
     PDTARALITA LARGRITARM VLGLVGVAAD HNRRLRTAAE QTGPDGTPHP LAPVHLLLGT
     PSRGTSGHGP RRTHLVAWHL PDFADKLTRR AVTAYVDRQL PELGDEIMQI GEEWLDTLTT
     RWIRLYEARP EVTVRRDHHT PAAWLHGKRI LVLGAGALGA PAADICARAG AAHLTVVDQS
     LVHPGIPARQ PYADADIGYP KADVLAARLN QIAPHATRIE PVVADITRGL PALDVHSFDL
     ILDCTANRVV RAFLERARRT DPTHWPHLAT VMIGHQATRG IAALSPHGAT GGGADVLRRT
     ALTARTDPTG ALADMVEDFF PTEPRTELFQ PEPGCSDATF TGSAADVTAL AGQLMTGILH
     ALNTPADQHT MAALTVRTPS GPTDPQPAGP RWLTWPNDTI ITDDATGYDV RIAPAALAEM
     RAEARRGARV RGPRVETGGM LLGAIDDSTG IIYVDEATGP PPDSLLAETY FQHGLDGVPR
     HLAARRTATG NTSRFLGLWH THPHSPAQPS ATDRTAMELL TLPLDDAPAR ALVLIAGGPQ
     PVWQKWLATG DGPDLYARLA ARTTAATTPP ATTVPPGRPR SALWWPGGYA TRPTTDNPLP
     APRRSDDARP
//