ID A0A1Q9VA56_9MICO Unreviewed; 605 AA.
AC A0A1Q9VA56;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Phosphohydrolase {ECO:0000313|EMBL:OLT46842.1};
GN ORFNames=BJF88_04520 {ECO:0000313|EMBL:OLT46842.1};
OS Cellulosimicrobium sp. CUA-896.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Cellulosimicrobium.
OX NCBI_TaxID=1517881 {ECO:0000313|EMBL:OLT46842.1, ECO:0000313|Proteomes:UP000185790};
RN [1] {ECO:0000313|EMBL:OLT46842.1, ECO:0000313|Proteomes:UP000185790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CUA-896 {ECO:0000313|EMBL:OLT46842.1,
RC ECO:0000313|Proteomes:UP000185790};
RX PubMed=27902408; DOI=10.1099/mic.0.000386;
RA Schorn M.A., Alanjary M.M., Aguinaldo K., Korobeynikov A., Podell S.,
RA Patin N., Lincecum T., Jensen P.R., Ziemert N., Moore B.S.;
RT "Sequencing rare marine actinomycete genomes reveals high density of unique
RT natural product biosynthetic gene clusters.";
RL Microbiology 162:2075-2086(2016).
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:OLT46842.1}.
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DR EMBL; MKKH01000066; OLT46842.1; -; Genomic_DNA.
DR RefSeq; WP_075829530.1; NZ_MKKH01000066.1.
DR AlphaFoldDB; A0A1Q9VA56; -.
DR OrthoDB; 9758038at2; -.
DR Proteomes; UP000185790; Unassembled WGS sequence.
DR GO; GO:0008773; F:[protein-PII] uridylyltransferase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR CDD; cd05401; NT_GlnE_GlnD_like; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.3090.10; cca-adding enzyme, domain 2; 1.
DR InterPro; IPR005105; GlnD_Uridyltrans_N.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase.
DR InterPro; IPR010043; UTase/UR.
DR PANTHER; PTHR47320; BIFUNCTIONAL URIDYLYLTRANSFERASE/URIDYLYL-REMOVING ENZYME; 1.
DR PANTHER; PTHR47320:SF1; BIFUNCTIONAL URIDYLYLTRANSFERASE_URIDYLYL-REMOVING ENZYME; 1.
DR Pfam; PF03445; DUF294; 1.
DR Pfam; PF08335; GlnD_UR_UTase; 1.
DR Pfam; PF01966; HD; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81593; Nucleotidyltransferase substrate binding subunit/domain; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:OLT46842.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000185790};
KW Transferase {ECO:0000256|ARBA:ARBA00022695}.
FT DOMAIN 37..132
FT /note="Protein-PII uridylyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03445"
FT DOMAIN 191..299
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT DOMAIN 451..531
FT /note="HD"
FT /evidence="ECO:0000259|Pfam:PF01966"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 605 AA; 64520 MW; AF83B2963F84B802 CRC64;
MTDHASSPVG SGGGPADRTE VPHPEGVRDL RARTLGLARS MSGRGRSGVA RRAAVVELVT
TSLESLWKEA TDDVAPDGIA LAAVGSLGRG DMGPVSDLDL VLVHDGRSHS ADEVAQVAQR
LWYPLWDAGV DLDHAVRSLA QCRQVASKDV PAAVGWLDVR AVAGDAVVVH RASSAVLTDW
RSASRRRLPE LLSSTRERAE RAGELAYLVE PDLKEARGGI RDAVVLSALA ATWLTDRPHG
SVDRAYAHLL DVRDTLQVVT GRHSSRLLLA DLDEVADLSG FDDPDELLAS LAEAGREISY
ALDTTVRRAR QALQRPSVAR RPVLVRGRRA APRLRSVGDG LVEHDGELVL AVDAHPESDP
LLSLRAAATA ARTGLTLSPV SVASLAQCPP LPEPWPKPAR TAFLSLLASG QAQVAVWEAL
DLAGVVTRWI PEWAGVRNRP QRAAVHRHTV DRHLVEVVAR AARDRKDVAR ADVLLLSAVL
HDIGKRAGAA DHSVEGARLA PPILRRMGFD EGVVADVARL VRHHLTLSRL AVTQDPDDPA
TVAELAAAVD HRVDLLEVLR ALTEADASSL RPGAWTAWRA RLVDDLVGAT ASALRAEGGQ
EGSAG
//