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Database: UniProt
Entry: A0A0C9LV74_9FUNG
LinkDB: A0A0C9LV74_9FUNG
Original site: A0A0C9LV74_9FUNG 
ID   A0A0C9LV74_9FUNG        Unreviewed;       876 AA.
AC   A0A0C9LV74;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   03-JUL-2019, entry version 24.
DE   SubName: Full=Urease {ECO:0000313|EMBL:GAN06280.1};
GN   ORFNames=MAM1_0118d05760 {ECO:0000313|EMBL:GAN06280.1};
OS   Mucor ambiguus.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN06280.1, ECO:0000313|Proteomes:UP000053815};
RN   [1] {ECO:0000313|Proteomes:UP000053815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 6742 {ECO:0000313|Proteomes:UP000053815};
RA   Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S.,
RA   Koike H.;
RT   "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT   ambiguus NBRC6742.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC         Evidence={ECO:0000256|PIRSR:PIRSR001222-51};
CC       Note=Binds 2 nickel ions per subunit.
CC       {ECO:0000256|PIRSR:PIRSR001222-51};
CC   -!- PTM: Carbamylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000256|PIRSR:PIRSR001222-50}.
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DR   EMBL; DF836407; GAN06280.1; -; Genomic_DNA.
DR   EnsemblFungi; GAN06280; GAN06280; MAM1_0118d05760.
DR   OrthoDB; 183108at2759; -.
DR   Proteomes; UP000053815; Unassembled WGS sequence.
DR   GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR   GO; GO:0009039; F:urease activity; IEA:InterPro.
DR   GO; GO:0043419; P:urea catabolic process; IEA:InterPro.
DR   CDD; cd00375; Urease_alpha; 1.
DR   CDD; cd00407; Urease_beta; 1.
DR   CDD; cd00390; Urease_gamma; 1.
DR   Gene3D; 2.10.150.10; -; 1.
DR   Gene3D; 2.30.40.10; -; 1.
DR   Gene3D; 3.30.280.10; -; 1.
DR   HAMAP; MF_01953; Urease_alpha; 1.
DR   HAMAP; MF_01954; Urease_beta; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR008221; Urease.
DR   InterPro; IPR011612; Urease_alpha_N_dom.
DR   InterPro; IPR017950; Urease_AS.
DR   InterPro; IPR005848; Urease_asu.
DR   InterPro; IPR017951; Urease_asu_c.
DR   InterPro; IPR002019; Urease_beta.
DR   InterPro; IPR036461; Urease_betasu_sf.
DR   InterPro; IPR002026; Urease_gamma/gamma-beta_su.
DR   InterPro; IPR036463; Urease_gamma_sf.
DR   InterPro; IPR029754; Urease_Ni-bd.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   Pfam; PF00449; Urease_alpha; 1.
DR   Pfam; PF00699; Urease_beta; 1.
DR   Pfam; PF00547; Urease_gamma; 1.
DR   PIRSF; PIRSF001222; Urease; 1.
DR   PRINTS; PR01752; UREASE.
DR   SUPFAM; SSF51278; SSF51278; 1.
DR   SUPFAM; SSF51338; SSF51338; 2.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   SUPFAM; SSF54111; SSF54111; 1.
DR   TIGRFAMs; TIGR01792; urease_alph; 1.
DR   TIGRFAMs; TIGR00192; urease_beta; 1.
DR   TIGRFAMs; TIGR00193; urease_gam; 1.
DR   PROSITE; PS01120; UREASE_1; 1.
DR   PROSITE; PS00145; UREASE_2; 1.
DR   PROSITE; PS51368; UREASE_3; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000053815};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00700};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001222-51};
KW   Nickel {ECO:0000256|PIRSR:PIRSR001222-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053815}.
FT   DOMAIN      396    835       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   ACT_SITE    587    587       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR611612-52, ECO:0000256|PROSITE-
FT                                ProRule:PRU00700}.
FT   METAL       401    401       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       403    403       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       484    484       Nickel 1; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       484    484       Nickel 2; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       513    513       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       539    539       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       627    627       Nickel 1. {ECO:0000256|PIRSR:PIRSR001222-
FT                                51}.
FT   BINDING     486    486       Substrate. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     484    484       N6-carboxylysine. {ECO:0000256|PIRSR:
FT                                PIRSR001222-50}.
SQ   SEQUENCE   876 AA;  94842 MW;  AAA49B60D027787D CRC64;
     MRLIPREIDK LLLHQVGFLA QKRLARGVKL NRTEATALIA SQLLELMRDG CYSVSQLMDI
     GKQMLGRRHV MSDVFQTLHE VQVEGTFPDG TYLVTVHDPI CTDSGNLEMA LYGTFFPIPS
     EDKFPLPPPV QARDAPGAII VKPGKIELNA GRRRLSLSVT NYGDRPIQVG SHYHFIESNA
     ALHFNRALSY GMRLDIPAGS AVRFEPGDFK TVTLVEISGN KIITGGNGLA TGPVDFIRLP
     DIINTIMTKG FKHDSLAPLL PAPATNTLDR EYYADHFGPT TGDLVRLGDT ELWARVEKDF
     TVYGDECKFG GGKVLREGMG QATAKLDAEV LDLVITNALI IDHTGIYKAD IGIKKGLIAG
     IGKAGNPDVM DGVTPGMVVG AGTEALAGEG KIFTAGAIDS HIHYICPQLC YEALSSGVTT
     LIGGGTGPNT GTNATTCTPG NHHIEMMMKA TDDIPMNFGF TGKGNCSNKD ELVEHIKAGC
     LGLKLHEDWG TTPAAIDACL QVCDDLDVQA TIHTDTLNEA GFVESTIGAF KGRTIHTYHS
     EGAGGGHAPD IITVCSEPNV LPSSTNPTRP FTANTLDEHV DMLMVCHHLS KTIPEDVAFA
     ESRIRAETIA AEDVLHDIGA ISMISSDSQA MGRAGEVILR TWKTASKMKQ QRGTLKEDQN
     DEGDNFRIRR YIAKYTINVA LAHGIGHAVG SIEVGKVADL VCFTPEYFGS KPELILKAGI
     IVWGQMGDAN GSIPTTEPII SRPMYGANAS SLGVSCLVFV SQLSVDEGIV QSYNLRKKIE
     PVKGCRKVTK KDMRLNDAMP KITVDPETYK VMADGEECVC DPVASLPLTQ SQVVFNIDQD
     CNMNMYGIVR IVWVSDKNTE RVYTARRVKE SAESVR
//
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