ID D4B5U4_ARTBC Unreviewed; 433 AA.
AC D4B5U4;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Agmatinase, putative {ECO:0000313|EMBL:EFE29280.1};
GN ORFNames=ARB_03851 {ECO:0000313|EMBL:EFE29280.1};
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE29280.1, ECO:0000313|Proteomes:UP000008866};
RN [1] {ECO:0000313|Proteomes:UP000008866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|PROSITE-
CC ProRule:PRU00742, ECO:0000256|RuleBase:RU003684}.
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:EFE29280.1}.
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DR EMBL; ABSU01000050; EFE29280.1; -; Genomic_DNA.
DR RefSeq; XP_003009925.1; XM_003009879.1.
DR AlphaFoldDB; D4B5U4; -.
DR STRING; 663331.D4B5U4; -.
DR GeneID; 9525270; -.
DR KEGG; abe:ARB_03851; -.
DR eggNOG; KOG2964; Eukaryota.
DR HOGENOM; CLU_039478_1_1_1; -.
DR OMA; YELTTIM; -.
DR OrthoDB; 161483at2759; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd11592; Agmatinase_PAH; 1.
DR Gene3D; 3.40.800.10; Ureohydrolase domain; 1.
DR InterPro; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR PANTHER; PTHR11358:SF26; AGMATINASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11358; ARGINASE/AGMATINASE; 1.
DR Pfam; PF00491; Arginase; 1.
DR PRINTS; PR00116; ARGINASE.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
DR PROSITE; PS01053; ARGINASE_1; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003684};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008866}.
FT REGION 160..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 433 AA; 47075 MW; 04255CF2A5806DCC CRC64;
MVYLKYKTLA VAGAILSAQV VDCHSRHGEE QIPLSQEELE HKWAPELSAF ATMGSFGGLK
HVPCLTKPNE LYDIAIIGAP FDTATSYRPG ARFGPRAIRE ASGRQVAARS YNVRAGINPY
LDWAKVIDCG NIPITQMDNR IAEKQMFEAF LELGTRKAAY QPQEKGDKPK RQARISDGKP
KLVTLGGDHS IILPALRALN QIYKKPITVI HFDAHQDTWE SSRYDGYWKP DVDGLNHGTW
LFHAGQEGLI SNTTSAHAGL RSYLGGSDDR DYRTGVEKGF MRIHADDVDD IGTQGVVDAI
VSRVGLDPDQ PVYISLDIDV LDPSIAPGTG TPESGGWTSR ELARILRGLE KLNVVGADVV
EVSPSYDHRA GGTALAAAHV VNEIIASMVK LGVEDPGTVG GWFGRKGNKS VKEGVMESYQ
EGAAGSEARK DEL
//