ID C5KT03_PERM5 Unreviewed; 599 AA.
AC C5KT03;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Phospholipase B-like {ECO:0000256|RuleBase:RU364138};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU364138};
GN ORFNames=Pmar_PMAR001152 {ECO:0000313|EMBL:EER12353.1};
OS Perkinsus marinus (strain ATCC 50983 / TXsc).
OC Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC Perkinsus.
OX NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN [1] {ECO:0000313|EMBL:EER12353.1, ECO:0000313|Proteomes:UP000007800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Putative phospholipase. {ECO:0000256|RuleBase:RU364138}.
CC -!- SIMILARITY: Belongs to the phospholipase B-like family.
CC {ECO:0000256|ARBA:ARBA00007835, ECO:0000256|RuleBase:RU364138}.
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; GG676168; EER12353.1; -; Genomic_DNA.
DR RefSeq; XP_002780558.1; XM_002780512.1.
DR AlphaFoldDB; C5KT03; -.
DR EnsemblProtists; EER12353; EER12353; Pmar_PMAR001152.
DR GeneID; 9057400; -.
DR InParanoid; C5KT03; -.
DR OMA; IMTETSE; -.
DR OrthoDB; 180150at2759; -.
DR Proteomes; UP000007800; Unassembled WGS sequence.
DR GO; GO:0004620; F:phospholipase activity; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.60.60.30; -; 1.
DR InterPro; IPR007000; PLipase_B-like.
DR PANTHER; PTHR12370:SF3; PHOSPHOLIPASE B-LIKE 2-RELATED; 1.
DR PANTHER; PTHR12370; PHOSPHOLIPASE B-RELATED; 1.
DR Pfam; PF04916; Phospholip_B; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364138};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|RuleBase:RU364138};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU364138};
KW Reference proteome {ECO:0000313|Proteomes:UP000007800};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364138}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU364138"
FT CHAIN 22..599
FT /note="Phospholipase B-like"
FT /evidence="ECO:0000256|RuleBase:RU364138"
FT /id="PRO_5011331275"
SQ SEQUENCE 599 AA; 66727 MW; FB1B2EC476145E08 CRC64;
MAIRGLTIMV GLLCGASAAA GEIREVISRG GGFGSLDKDV SVQEAVVVKV DGKFDVIPMA
RDTPLAVASG LYTDTLFELG WDQIQLDSGS DYYSDLDRMY ALGYLESYFL HDRIYDFWTN
YKHNDVDKAP EGVREWFEDQ RAYVKIMTET SEDPFWKRMA YVQAQTQGYI DGYQRYHSKG
KEIDPLDMYI LQSWGDLGDV AAAFNDAKSL EGARVLSETT PESTAPFVAG PGTLDEGSCT
GLIRLLPNGE ITVAHNTWRL YEGFIRVFKR ITYPNKLTVT MSSTPGLIHS KDDFYVQENG
NLIAMETTNA MHDKKISATI ATDPEARHVA LSWQQVTSAV IFSTTSEEFV HTMADKYNSG
TYNNQWMVVD VAKHRAGERE GVAMIAELSV GYTHLGDVSS VLYKKGYWKS YNIPYFPDVF
EQMGYNDSDP QSSYHQASRS LISDRDAPKL SNVADVMLFS RYNEYLTDPL SHECSRLTIA
SRYDLSDEAK CGAGAGPRAF GAIDAKIVNS GDMKTVHAVS GPTNDPDNGI PVFQWSTSVV
DDQIMHVGMP DRYDFPWVRF NSHSWDTEAL TDADKQCADN DDARIVAVQV EKSGKTLLI
//