ID C6A0H6_THESM Unreviewed; 271 AA.
AC C6A0H6;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Membrane-bound phosphoesterase, PAP2 superfamily {ECO:0000313|EMBL:ACS89121.1};
GN OrderedLocusNames=TSIB_0051 {ECO:0000313|EMBL:ACS89121.1};
OS Thermococcus sibiricus (strain DSM 12597 / MM 739).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=604354 {ECO:0000313|EMBL:ACS89121.1, ECO:0000313|Proteomes:UP000009079};
RN [1] {ECO:0000313|EMBL:ACS89121.1, ECO:0000313|Proteomes:UP000009079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12597 / MM 739 {ECO:0000313|Proteomes:UP000009079};
RX PubMed=19447963; DOI=10.1128/AEM.00718-09;
RA Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V.,
RA Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT "Metabolic versatility and indigenous origin of the archaeon Thermococcus
RT sibiricus, isolated from a siberian oil reservoir, as revealed by genome
RT analysis.";
RL Appl. Environ. Microbiol. 75:4580-4588(2009).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001463; ACS89121.1; -; Genomic_DNA.
DR RefSeq; WP_012766082.1; NC_012883.1.
DR AlphaFoldDB; C6A0H6; -.
DR STRING; 604354.TSIB_0051; -.
DR GeneID; 8095018; -.
DR KEGG; tsi:TSIB_0051; -.
DR eggNOG; arCOG03951; Archaea.
DR HOGENOM; CLU_089553_0_0_2; -.
DR OrthoDB; 329477at2157; -.
DR Proteomes; UP000009079; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR Pfam; PF01569; PAP2; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000009079};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 109..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 207..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 241..264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 111..223
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|Pfam:PF01569"
SQ SEQUENCE 271 AA; 30628 MW; 8C5A76A0DA9DCEC3 CRC64;
MNLLQRSLQD PKVLLRLNAF FLSSFGWIAF GVLYGIIGLW SVDLTPQFLK LPLTSRDLVV
GLVEFIKGVP PIHTFFTVVY YLGFAGSIAL MIAYLLLYMR DLEASDRLLA RYLLAYAVAG
LVYLIAHIHA PHIVYNLPGY TSSNTLLTRQ EFVLPSLHNT FIMINIITLW KYRNRLGGKV
LILTNSLISF ATVFLGHHWI YDVIVGFFLG IAVSKVSWEW STMISEVVYK WEVSSLQRIT
VFNLFLVVIV LIVATDPARV LAIFRGLLGA P
//