ID A0A135VVM9_9ARCH Unreviewed; 652 AA.
AC A0A135VVM9;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Phospholipase C {ECO:0000256|ARBA:ARBA00018391};
DE EC=3.1.4.3 {ECO:0000256|ARBA:ARBA00012018};
DE AltName: Full=Phosphatidylcholine cholinephosphohydrolase {ECO:0000256|ARBA:ARBA00031285};
GN ORFNames=AM326_06665 {ECO:0000313|EMBL:KXH76746.1};
OS Candidatus Thorarchaeota archaeon SMTZ-45.
OC Archaea; Asgard group; Candidatus Thorarchaeota.
OX NCBI_TaxID=1706443 {ECO:0000313|EMBL:KXH76746.1, ECO:0000313|Proteomes:UP000070599};
RN [1] {ECO:0000313|EMBL:KXH76746.1, ECO:0000313|Proteomes:UP000070599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMTZ-45 {ECO:0000313|EMBL:KXH76746.1};
RX PubMed=26824177;
RA Seitz K.W., Lazar C.S., Hinrichs K.U., Teske A.P., Baker B.J.;
RT "Genomic reconstruction of a novel, deeply branched sediment archaeal
RT phylum with pathways for acetogenesis and sulfur reduction.";
RL ISME J. 0:0-0(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:10604,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:295975; EC=3.1.4.3;
CC Evidence={ECO:0000256|ARBA:ARBA00000291};
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:KXH76746.1}.
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DR EMBL; LRSM01000031; KXH76746.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135VVM9; -.
DR Proteomes; UP000070599; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0034480; F:phosphatidylcholine phospholipase C activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 1.10.575.10; P1 Nuclease; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR008947; PLipase_C/P1_nuclease_dom_sf.
DR InterPro; IPR029002; PLPC/GPLD1.
DR InterPro; IPR001531; Zn_PLipaseC.
DR Pfam; PF00882; Zn_dep_PLPC; 1.
DR SMART; SM00770; Zn_dep_PLPC; 1.
DR SUPFAM; SSF48537; Phospholipase C/P1 nuclease; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 628..648
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..234
FT /note="Zn-dependent PLC"
FT /evidence="ECO:0000259|SMART:SM00770"
FT REGION 593..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 652 AA; 71056 MW; 7C3C54E5F1DC4411 CRC64;
MRKASVILII MLLPLFSATI ITPTITQVDA WGHATHFFIV DKAVAGISNA SWADAFDYYL
PELMSGSIYP DTAWQDWDNH LYYPETGEHN APTAAERWYN FTRNNFTIGS WEDGFFAAGI
MSHYFSDPCI PVHTGDSWPG HSGYESDINQ NLDLLTLATP SEDYITNVSQ LVIDSATYSH
QYYDDVYLQY VDDNSEAIAT NATIKTLTED CLNLAIDGLL DLFFNATQGV NAPDVTITYE
YKAMLDVAHG NDYATGYLDT INSTLYIKGF ELILQSAAIT TESLAGVDLF IATCASTAYT
ADELTAITNW ANSGNKALLL TGRGDHASSS TNTAYPDALL AAISSNIRNN DDNVYMEGTY
NAWTNDLTVI PAPEETVNLT AFVSTMTFFS PSSLYFLDDG PVLPIIYADV TGYQTNQEPP
SPTVIYDNVM DGQWGNQIPL AAAEEIGSTR LLVTGTTFFS DYDYGKPQFD NIQLLENFLD
WSVGNRSEWS ILDVDEVGPR IGDISWDPAS PDNGEKVNVS ATVTDPSGVV RVYLKYNNGT
HDVSLTMTSE GGGLYSGEIS DVSSGSLSFY VEAVDNSDNV AIRASFTITW TAPTTTTTTP
TDTTTTEAPT TSTTPTETPT AIPPPDDMIL VLGIGGAIIV LIVIVVIVKM RR
//
