ID I0YWI8_COCSC Unreviewed; 443 AA.
AC I0YWI8;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Phospholipase B-like {ECO:0000256|RuleBase:RU364138};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU364138};
DE Flags: Fragment;
GN ORFNames=COCSUDRAFT_3787 {ECO:0000313|EMBL:EIE22757.1};
OS Coccomyxa subellipsoidea (strain C-169) (Green microalga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Trebouxiophyceae incertae sedis; Elliptochloris clade; Coccomyxa;
OC Coccomyxa subellipsoidea.
OX NCBI_TaxID=574566 {ECO:0000313|EMBL:EIE22757.1, ECO:0000313|Proteomes:UP000007264};
RN [1] {ECO:0000313|EMBL:EIE22757.1, ECO:0000313|Proteomes:UP000007264}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C-169 {ECO:0000313|EMBL:EIE22757.1,
RC ECO:0000313|Proteomes:UP000007264};
RX PubMed=22630137; DOI=10.1186/gb-2012-13-5-r39;
RA Blanc G., Agarkova I., Grimwood J., Kuo A., Brueggeman A., Dunigan D.,
RA Gurnon J., Ladunga I., Lindquist E., Lucas S., Pangilinan J., Proschold T.,
RA Salamov A., Schmutz J., Weeks D., Yamada T., Claverie J.M., Grigoriev I.,
RA Van Etten J., Lomsadze A., Borodovsky M.;
RT "The genome of the polar eukaryotic microalga coccomyxa subellipsoidea
RT reveals traits of cold adaptation.";
RL Genome Biol. 13:R39-R39(2012).
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 -!- 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:EIE22757.1}.
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DR EMBL; AGSI01000009; EIE22757.1; -; Genomic_DNA.
DR RefSeq; XP_005647301.1; XM_005647244.1.
DR AlphaFoldDB; I0YWI8; -.
DR GeneID; 17040744; -.
DR KEGG; csl:COCSUDRAFT_3787; -.
DR eggNOG; KOG3774; Eukaryota.
DR OrthoDB; 180150at2759; -.
DR Proteomes; UP000007264; 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:SF1; PHOSPHOLIPASE B-LIKE 1; 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:UP000007264};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EIE22757.1"
FT NON_TER 443
FT /evidence="ECO:0000313|EMBL:EIE22757.1"
SQ SEQUENCE 443 AA; 49718 MW; 7B2BD18F518B37FF CRC64;
AAGFLEGYLT AHRIYDHHVN MEAFFNISTS GPSDWLLAQD AWAQEQVATG ATPYWTTLGL
ILQQHEGLMD GYNLAANETQ NSAAGSSPLP KLDRIDFLKL SAVGDLDASD MEGTLASMGH
CSALVKVTGN YSDLFLAHSS WFTYSGMVRI YKHYDFAVAS PHHKLRRTSF SSYPGELSSD
DDFYLMDTGL ALLQTTNDIL DTELYKLLTP KSVLNWQRVR LANAMADTGK EWADIVSENN
SGTYNNQYII VDLKLFRPGQ ELQPNLLWVV EQIPGLTVAE DQTEILSRGY WPSYNVPFYP
EIYRFEAAPT SQLSFFQTWF IIYQLAPRAT IFRRDAGNVT DLDSLKRLMR SNNYQNDPYS
DGKALNAICG RGDLDGAKPR AYGCYDSKVA NFEMARRLAA QGIVGPAGKE AGLKPFEWTE
SRFENVSHQG QPRVFDFKYE PLS
//
