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Database: UniProt
Entry: A0A1Q7LWY7_9CREN
LinkDB: A0A1Q7LWY7_9CREN
Original site: A0A1Q7LWY7_9CREN 
ID   A0A1Q7LWY7_9CREN        Unreviewed;       399 AA.
AC   A0A1Q7LWY7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=PKD domain-containing protein {ECO:0000259|PROSITE:PS50093};
GN   ORFNames=AUJ07_02990 {ECO:0000313|EMBL:OLD04946.1};
OS   Crenarchaeota archaeon 13_1_40CM_3_53_5.
OC   Archaea; Thermoproteota.
OX   NCBI_TaxID=1805098 {ECO:0000313|EMBL:OLD04946.1, ECO:0000313|Proteomes:UP000186658};
RN   [1] {ECO:0000313|EMBL:OLD04946.1, ECO:0000313|Proteomes:UP000186658}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(2016).
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:OLD04946.1}.
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DR   EMBL; MNGL01000019; OLD04946.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q7LWY7; -.
DR   STRING; 1805098.AUJ07_02990; -.
DR   Proteomes; UP000186658; Unassembled WGS sequence.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0008131; F:primary amine oxidase activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   GO; GO:0009308; P:amine metabolic process; IEA:InterPro.
DR   CDD; cd00146; PKD; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR036460; Cu_amine_oxidase_C_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR022409; PKD/Chitinase_dom.
DR   InterPro; IPR000601; PKD_dom.
DR   InterPro; IPR035986; PKD_dom_sf.
DR   Pfam; PF18911; PKD_4; 1.
DR   SMART; SM00089; PKD; 1.
DR   SUPFAM; SSF49998; Amine oxidase catalytic domain; 1.
DR   SUPFAM; SSF49299; PKD domain; 1.
DR   PROSITE; PS50093; PKD; 1.
PE   4: Predicted;
FT   DOMAIN          38..117
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
SQ   SEQUENCE   399 AA;  45749 MW;  6F4BC6006235308E CRC64;
     MQFEKSRRLR RSLLAVTVLY VVVFAQVPFF TARSAPPPTV NFDWTPKSAV IGNLLNFNAT
     ATGGTPPYTY SWNFGDGQTG TGVTVLHPYN RPGFYSVALN VSDSSGAFNV LTQSVMIYDW
     PVRTYNWLIH WNATADDGFN IWDVSYKGVP LIRDARLAYV VNDYLENFCG PFQDETASSG
     LQGTLASGNL RYENFTTASD PYFQIRTEYP VGGYNYQEVF RFYLSGRWEP EILIGRGGCI
     ADHIYKPMWR IDIVLGEDSN NFMSQYTPYR TWENLIWEGN YVDNGFRDPT HNAAQWRMGH
     QGMYYYMIPK IFRVDTDLPN LPTSIYLVRA HPNEIQFQHS LECYPNPCED PSEFINGELA
     FRRDIAIWFI PRIWDHGPID TTSPQKVATL SFYPGGSWP
//
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