ID A0A1L9SGX4_9EURO Unreviewed; 528 AA.
AC A0A1L9SGX4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Amidohydrolase-related domain-containing protein {ECO:0000259|Pfam:PF01979};
DE Flags: Fragment;
GN ORFNames=ASPZODRAFT_96676 {ECO:0000313|EMBL:OJJ46432.1};
OS Penicilliopsis zonata CBS 506.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicilliopsis.
OX NCBI_TaxID=1073090 {ECO:0000313|EMBL:OJJ46432.1, ECO:0000313|Proteomes:UP000184188};
RN [1] {ECO:0000313|Proteomes:UP000184188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 506.65 {ECO:0000313|Proteomes:UP000184188};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PTM: Carbamylation allows a single lysine to coordinate two divalent
CC metal cations. {ECO:0000256|PIRSR:PIRSR611778-50}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Hydantoinase/dihydropyrimidinase family.
CC {ECO:0000256|ARBA:ARBA00008829}.
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DR EMBL; KV878342; OJJ46432.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9SGX4; -.
DR STRING; 1073090.A0A1L9SGX4; -.
DR VEuPathDB; FungiDB:ASPZODRAFT_96676; -.
DR OrthoDB; 1772494at2759; -.
DR Proteomes; UP000184188; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd01314; D-HYD; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011778; Hydantoinase/dihydroPyrase.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11647:SF99; D-PHENYLHYDANTOINASE-RELATED; 1.
DR PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 2.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000184188}.
FT DOMAIN 54..485
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT MOD_RES 166
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR611778-50"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OJJ46432.1"
SQ SEQUENCE 528 AA; 58506 MW; 1CF0A5EAE58E1CC8 CRC64;
MAFDLVVVNA TVVTASDVSH CCIGIQNGKI KTLVDSFTSE EIGDAEVIDA EGAYVMPGGV
DGHVHLCQDL KTGPHGLGGE CADNFETGSR SAVAGGTTTI LTFATQTRAE QDRSLLDVVK
AYRARAEETG SYIDYGFHVI IVRNDAEILD RELPVLMHDW GISSCKLFLT YETQRLTDAQ
LLDVMFAARK NSMTTMIHAE NGDMIEWLTD KLESKGMVAP YYHALSRPPL VEGEATNRAI
ALAQLIQNPI LFVHVGSALG AANVRRAQTQ GLPVYAETCP QYFNLTWDDL KRFHSPTCFE
NSKMICSPPP PPDTTDQEDL FIGLHNGTFT IYSSDHCPFR YDHPHGKPSG VLEDAKSMAG
EPEEPEDLGA LLKRKQGAFR LIPNGIPGVE TRLPLLYNAL ARGRITPSRF VELTATNPAK
LYGLYPRKGA LMPGSDADLV IWHPDKTFTP FRLTNSMLHH NVDYTPYEGV EFVNWPRYTI
LRGKVMWANG QLQGQVRDGQ YLKRGPSQLS QGVSRKDSRQ VAMWLYEQ
//
