ID A0A0Q5RBD6_9SPHN Unreviewed; 758 AA.
AC A0A0Q5RBD6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=JAB domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASG11_04440 {ECO:0000313|EMBL:KQS03591.1};
OS Sphingomonas sp. Leaf357.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736350 {ECO:0000313|EMBL:KQS03591.1, ECO:0000313|Proteomes:UP000051080};
RN [1] {ECO:0000313|EMBL:KQS03591.1, ECO:0000313|Proteomes:UP000051080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf357 {ECO:0000313|EMBL:KQS03591.1,
RC ECO:0000313|Proteomes:UP000051080};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS03591.1, ECO:0000313|Proteomes:UP000051080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf357 {ECO:0000313|EMBL:KQS03591.1,
RC ECO:0000313|Proteomes:UP000051080};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQS03591.1}.
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DR EMBL; LMPM01000001; KQS03591.1; -; Genomic_DNA.
DR RefSeq; WP_055775668.1; NZ_LMPM01000001.1.
DR AlphaFoldDB; A0A0Q5RBD6; -.
DR STRING; 1736350.ASG11_04440; -.
DR OrthoDB; 891532at2; -.
DR Proteomes; UP000051080; 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; 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.
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:UP000051080};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 339..448
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT DOMAIN 622..723
FT /note="JAB"
FT /evidence="ECO:0000259|Pfam:PF14464"
SQ SEQUENCE 758 AA; 82470 MW; 9D622ADE76FF7FB3 CRC64;
MTLSRGQELA RDQLAEIADR SAGALELLRE PTLSESGLLR IYFAVATRGY RRPGGLVLRD
RERMLLLVGT DFPFKPPTLW FSHRRFAGTP HVQWGHHVCL YQSVEAEWRP ADGMYGLIER
IDEWLAAAGA GTLDPDDAPL HPPVAYTEAS TTVVIRADAP ATDGALWVGR ADLRTIGATR
RDLVGWASMA DWDATPVDGT PAVAILLDRP LPSEYPTNVN DLFTSIEEAG VSFRTVWSAL
RLSSVLVPGG EPGHVVLGAP MRRRAAGEPL RQHLTVWQLD ADALATVRAY VLNDDDAELR
GQVAKWMVHS KVGWCTVLED RPEIVNRRDR GALVEAVAGR RVALLGCGAL GSAVAETLVR
AGVSRLRLLD SGIVRPGILV RQRFTDDDVG AGKAARLKAR LDGLGLGCEI DVRQENLSTG
VLAKVAELEP ELVIDATASR AVAHRLETEL DDGRLGCPLI TISVSASAEH GSVAVRMPDC
PGGPLAVERQ AKLAALARDR TQPLVQAFWP DEPRKELFLP EPGCSSPTFT GSAADIDHHA
GGLLNVGLRR AAELAPDAAS MDLAAPPWSA MPAGGARLLS YRLDGIETTV ERVRRYRTFT
TKAARTGMAT EIRRVGRVKS SKCETGGLLF GEIDDSHEHI WIDSVSGPPP DSELSPERFL
CGTAGTRALA RRRLEGSGGS SRFIGLWHTH PVSRGRPSDE DMAAMVQLLH LQPHPPRQVA
MLIIGFAERR PDPNLYLFHR DDFRFTRIDE LPYDIGDG
//