ID A0A0D1E1I8_USTMA Unreviewed; 1095 AA.
AC A0A0D1E1I8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
GN ORFNames=UMAG_02496 {ECO:0000313|EMBL:KIS69984.1};
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631 {ECO:0000313|EMBL:KIS69984.1, ECO:0000313|Proteomes:UP000000561};
RN [1] {ECO:0000313|EMBL:KIS69984.1, ECO:0000313|Proteomes:UP000000561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kamper J., Kahmann R., Bolker M., Ma L.J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Muller O., Perlin M.H., Wosten H.A.,
RA de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M.,
RA Perez-Martin J., Feldbrugge M., Basse C.W., Steinberg G., Ibeas J.I.,
RA Holloman W., Guzman P., Farman M., Stajich J.E., Sentandreu R.,
RA Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA Mendoza-Mendoza A., Greilinger D., Munch K., Rossel N., Scherer M.,
RA Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA Ho E.C., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J.,
RA Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H.,
RA Hauser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schluter T.,
RA Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V.,
RA Mannhaupt G., Guldener U., Munsterkotter M., Haase D., Oesterheld M.,
RA Mewes H.W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.,
RA Jaffe D.B., Calvo S., Nusbaum C., Galagan J., Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2] {ECO:0000313|Proteomes:UP000000561}
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CM003144; KIS69984.1; -; Genomic_DNA.
DR RefSeq; XP_011388773.1; XM_011390471.1.
DR AlphaFoldDB; A0A0D1E1I8; -.
DR EnsemblFungi; KIS69984; KIS69984; UMAG_02496.
DR GeneID; 23563230; -.
DR KEGG; uma:UMAG_02496; -.
DR VEuPathDB; FungiDB:UMAG_02496; -.
DR eggNOG; ENOG502QSHE; Eukaryota.
DR InParanoid; A0A0D1E1I8; -.
DR OMA; NAMNFAY; -.
DR OrthoDB; 5475921at2759; -.
DR Proteomes; UP000000561; Chromosome 5.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd01300; YtcJ_like; 1.
DR Gene3D; 3.10.310.70; -; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR013108; Amidohydro_3.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR033932; YtcJ-like.
DR PANTHER; PTHR22642; IMIDAZOLONEPROPIONASE; 1.
DR PANTHER; PTHR22642:SF2; PROTEIN LONG AFTER FAR-RED 3; 1.
DR Pfam; PF07969; Amidohydro_3; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000561};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 42..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 194..711
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
FT REGION 147..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1095 AA; 120497 MW; E823F2307D5E06CB CRC64;
MSSSSRKRDG VPLTDDKQPG KVVVLQPMKA TSKGTSGFRR RFLVSVAAVS LIFSVWILST
SKRNPHLQAS QFASLSVRYA ICSANERGGL HISSSVVTVG SIYTGDEHRF AKEQGFTQCV
GVDHGLITHA GAEEDVIPNF CGQIDETTSS GSAHNQQWRR PRSNKAARLG RQLNSKKDGA
LRRKRKCDVR RLKKGQTLFP GFHDAHGHIL DYGWSCTVAN LVGSTSVQDV IDRLENYIRS
QPHLLEIALA EPTPTAANAS STPWIEGIGW DQTKWTPSEF PTATDLDRSP LLRRFPIVLR
RVDVHALWLN EKGIDLVVLG ARGFPSSPKE DRNVEGGLVV RDANGKPTGI LIDNAMNFAY
QVVPEWTDVQ RKIFLDAATE GLLRVGITAV GDASTDLQAA AFYKRMDAHG QLRFRIYSML
ACPPDERRCA HRIEQITPSS KDSGKSSSMF TLRAVKLFDD GALGSWGSAM WDEYSDKPGE
RGLLLIPQHE LPSLVEYWME RGWQVCTHAI GDRANTLTLD AYERYLRLHP HVDRQSLRPR
VEHAQLMKPS DIDRFASLGV IASMQPTHCT SDMGYAESRI GQTRAAHGAY AWKSLLAANA
SLALGSDFPV ELPDPLHGIY SSITRLDPAG NSPHGPGGWF PNERLTRREA LRGFTQDAAY
AQFEEHIAGR ISVGRRADFT LLDRNILDEV HVSPSMLRSA QVDATFVGGK VGFDRLAAAK
LTSTHRAGSS LAERLVQRID YLGKYAYALT SGPSFNSTSA IWAALFFGVL FFLLRSGKQE
PYQSMSCLAL NAPSPTTAWM NMGFWTPQLA GSQLDFPLAC QTLAQQLYAA AGVKPGLKVL
DVGCGAGQST LYLLDKYRPE VLHAVTSLPE EAAFASERLQ HRLQQGDGKA GQTTQVRVWA
QDVLEWLRSE EGGGEKYDVI LALDCAFHFS DRAEYIRLAT KRLTAAGRLG FVDLLSAYPA
PSATPSENVV LGKPPYPSRA PSLVQRLKHS FTCALASTKP ANLWPVDRYF DVLRHDGGFQ
AQAIQMRDIT ADVFPGFARF LRSFATEGAA WRGGGWAMRK GLGAFSNVVQ GWSEEGGLVR
MFIVVAQRDG AKERV
//
