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Database: UniProt
Entry: A0A1F5LA29_9EURO
LinkDB: A0A1F5LA29_9EURO
Original site: A0A1F5LA29_9EURO 
ID   A0A1F5LA29_9EURO        Unreviewed;       951 AA.
AC   A0A1F5LA29;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   31-JUL-2019, entry version 19.
DE   RecName: Full=Urease domain-containing protein {ECO:0000259|PROSITE:PS51368};
GN   ORFNames=PENARI_c018G00609 {ECO:0000313|EMBL:OGE50055.1};
OS   Penicillium arizonense.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1835702 {ECO:0000313|EMBL:OGE50055.1, ECO:0000313|Proteomes:UP000177622};
RN   [1] {ECO:0000313|EMBL:OGE50055.1, ECO:0000313|Proteomes:UP000177622}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 141311 {ECO:0000313|EMBL:OGE50055.1,
RC   ECO:0000313|Proteomes:UP000177622};
RX   PubMed=27739446; DOI=10.1038/srep35112;
RA   Grijseels S., Nielsen J.C., Randelovic M., Nielsen J., Nielsen K.F.,
RA   Workman M., Frisvad J.C.;
RT   "Penicillium arizonense, a new, genome sequenced fungal species,
RT   reveals a high chemical diversity in secreted metabolites.";
RL   Sci. Rep. 6:35112-35112(2016).
CC   -!- COFACTOR:
CC       Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC         Evidence={ECO:0000256|PIRSR:PIRSR611612-51};
CC       Note=Binds 2 nickel ions per subunit.
CC       {ECO:0000256|PIRSR:PIRSR611612-51};
CC   -!- PTM: Carbamylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000256|PIRSR:PIRSR611612-50}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OGE50055.1}.
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DR   EMBL; LXJU01000018; OGE50055.1; -; Genomic_DNA.
DR   OrthoDB; 183108at2759; -.
DR   Proteomes; UP000177622; 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; cd00407; Urease_beta; 1.
DR   CDD; cd00390; Urease_gamma; 1.
DR   Gene3D; 2.10.150.10; -; 1.
DR   Gene3D; 3.30.280.10; -; 1.
DR   HAMAP; MF_01953; Urease_alpha; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR011612; Urease_alpha_N_dom.
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; 2.
DR   Pfam; PF00449; Urease_alpha; 1.
DR   Pfam; PF00699; Urease_beta; 1.
DR   Pfam; PF00547; Urease_gamma; 1.
DR   PRINTS; PR01752; UREASE.
DR   SUPFAM; SSF51278; SSF51278; 1.
DR   SUPFAM; SSF51338; SSF51338; 2.
DR   SUPFAM; SSF51556; SSF51556; 2.
DR   SUPFAM; SSF54111; SSF54111; 1.
DR   TIGRFAMs; TIGR00192; urease_beta; 1.
DR   PROSITE; PS01120; UREASE_1; 1.
DR   PROSITE; PS51368; UREASE_3; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000177622};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00700};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR611612-51};
KW   Nickel {ECO:0000256|PIRSR:PIRSR611612-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000177622}.
FT   DOMAIN      446    951       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   REGION      353    378       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    363    378       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   ACT_SITE    638    638       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR611612-52, ECO:0000256|PROSITE-
FT                                ProRule:PRU00700}.
FT   METAL       451    451       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       453    453       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       534    534       Nickel 1; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       534    534       Nickel 2; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       563    563       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       590    590       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       678    678       Nickel 1. {ECO:0000256|PIRSR:PIRSR611612-
FT                                51}.
FT   BINDING     536    536       Substrate. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     534    534       N6-carboxylysine. {ECO:0000256|PIRSR:
FT                                PIRSR611612-50}.
SQ   SEQUENCE   951 AA;  104540 MW;  44C91B2B878ED34D CRC64;
     MHLIPRELER LAILYPLGNL AQRRLSRGVR LNHAEAVLIR DGHYAVADLM SIGRTILGRR
     HVLPSTWFTA RQIQIEGTFP TGTYLVTVVE PIATEAGNIE LALYGANLTP PPDNLFPEVN
     FEDYAPNKAP GYIWCEVIDN PGPYKTDILL NDKEIVNNEQ RKRKRLRLKV VNHGTRPIQV
     GSHFHFIETN RELEFDRIKA NGFRLDTPSG SSIRFEPGQC RQVDLVKIAG KGLIAGGNGV
     AEYFKVHQRI HPEFRHKVQD NPDNARSERR MKRNEYVKLF GPTKGDVVRL GSTDLYVMVE
     KDYRDLTDHC AEDCPNGQEE CQRSRRGNRK CPKSRTYYGD ECNFGGGKSV RDGMAQTSYG
     SSKEHHDPNR NETSDPPHYD KCVDTVITNA LIIDYTGIIK ADIGIKGGYI TAIGRAGNPD
     IMDDVDIIIG ANTDVIGAEN KIVTAGGLDT HVHTLDPAQV PEALCNGLTT LVGGGTGPST
     ASNATTVAPG PEHIKRMLQA FDHLPINVGI TGKGNNSDPE GLIEQVEAGA IGLKLHEDWG
     ATHKAIDTCL KVCEDYDVQS TLHTDTMNEG GYVDDTINSI GPERTIHSYH TEGAGGGHAP
     DIIAVVKTQN ILPASTNPTR PYTFNTVDEH VDMVMVAHHL SKDIPADVAF AESRIRAETI
     AAEDYLLDNG SISIMSSDTQ AMGRVGEVVL RTWTSAHKMA VLDIPPPEAA KRKGSKDGSY
     NSINQFRDDL ANKGCHDQEH QKGLANDAPT INNFRVKRYI SKYTINPAIA HGMSHLIGSV
     EKNKFADLVI WQPSNFGTKP DIVLKGGMIA VALGGDPNGS IPTIQPRIMR PRFGALVPET
     SITFVSQASV SVYNRDEAPP HAPTLEELPT VPDEPKPFVV KSNTSIDTYK LKKRVEPVKG
     CRVAKKKDME FNDTTPRMDV DAETFIVKAD NYVCDVPPAT SVALAQDYFI C
//
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