ID A0A1Q8B3F4_9CREN Unreviewed; 616 AA.
AC A0A1Q8B3F4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=PKD domain-containing protein {ECO:0000259|PROSITE:PS50093};
GN ORFNames=AUF79_15160 {ECO:0000313|EMBL:OLE86563.1};
OS Crenarchaeota archaeon 13_1_20CM_2_51_8.
OC Archaea; Thermoproteota.
OX NCBI_TaxID=1805093 {ECO:0000313|EMBL:OLE86563.1, ECO:0000313|Proteomes:UP000186073};
RN [1] {ECO:0000313|EMBL:OLE86563.1, ECO:0000313|Proteomes:UP000186073}
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:OLE86563.1}.
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DR EMBL; MNKD01000695; OLE86563.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q8B3F4; -.
DR Proteomes; UP000186073; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR CDD; cd00146; PKD; 2.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR007312; Phosphoesterase.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR PANTHER; PTHR31956:SF8; ACID PHOSPHATASE PHOA (AFU_ORTHOLOGUE AFUA_1G03570); 1.
DR PANTHER; PTHR31956; NON-SPECIFIC PHOSPHOLIPASE C4-RELATED; 1.
DR Pfam; PF05345; He_PIG; 1.
DR Pfam; PF04185; Phosphoesterase; 1.
DR Pfam; PF00801; PKD; 2.
DR SMART; SM00089; PKD; 2.
DR SUPFAM; SSF49313; Cadherin-like; 1.
DR SUPFAM; SSF49299; PKD domain; 2.
DR PROSITE; PS50093; PKD; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 581..601
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 284..365
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 371..452
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
SQ SEQUENCE 616 AA; 63038 MW; 8E4D1588BB3DA17D CRC64;
MASAPFDHIV TILMENQGLC DVYVGCGGSA AYMSQFANQN VLVMTWGTTS HPSEGNYISL
IGGDNFGHTN DGYCCWGINA PNIVDRMESA GLTWKAFAED ASGSGTCSFN PPRGADHFAF
LTFADMNTPA RCANLLTTTS SSDTEFLNSL NSATPANFIW LTPNDCNNMH DCGIAAGDSY
LSKLVPQILS SKEFTTTKAT LLIVFDEGYT GCSNTGGTGE CVYASFSGPV AKKGLQLSPP
GASHYSYLST IEAAWGLASL TSNDAGAPNL LSAFGAICTT NCPLATSFAF LPANPSVNSL
VTFTAVTTGG ILPYTVSWNF GDGGSGTGPI VTHTYTSAQS FTITETAKDS STPTQTAISS
QSVTIFAMPQ LSTTFQASSS SPQVGQAVTF TESATGGTSP YAYTLTFGDG GTGTGDPVTY
AYSSPGSYTA TVTVTDSASP QASVSASMTL NVQALIPPTL TVPGNQTVTA GTWINVTVTA
SSVNIGGTII LSATGLPAGA SFDPTTGLLS WKPSTSQTGS YAIIFTASDS SYPSTPTSKP
MEIQVNQAAP GGSNGGNGGS GGGSNGSCAL CGIFPKISTS IGIFVVGGLL GLVSALAVLT
IRTRASLERT RRRLGN
//