CAZyme Information: KAF5656986.1

Basic Information

• Species: Fusarium circinatum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium circinatum
• CAZyme ID: KAF5656986.1
• CAZy Family: GT90
• CAZyme Description: phospholipase A2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1074		120415.64	8.9448

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FcircinatumNRRL25331	13905	N/A	0	13905

• Gene Location: location=JAAQPE010000678:32965-37066(-)

Full Sequence      

MWMIKACSVLAAVCTVAADSAGPTIDFSSNIGTPKHLASGILYGIPDNTDQIPDSLLSGF
GFNYYRGAGAQVSHGWSYNEASFQERFASAHNNYIVTRRHNGGYVLLLNDLWGFDCSSNN
NTSPGPGDNGDWSSYDKFVQAIIKNIKKYKMQKGLVIDIWNEPEGGCFWGRSIDQWLQMW
GRGWHQFNDAFGNKVLTSGPTLAGQPGTDNPWWTEWAQFVKNNNSIPDQYVWHEEGGSGS
DFEYSYGVLQQILSQYGLPQRQININEYATYNEQVPAGSAFWISQLERRNAIGLRGNWLG
GTQLHDLAASLLFKPDPNNYASTGYYPNGDWWVYNYYSQNMTGKRVPTSVSSDGRFDAYA
TVDKTTRTARVLLGCHPLQLVKTLKFAVGDDVHYSQMGPPQDLGNYGHTIMQATPVSSRV
REKSHTKLAPSSPSRVSLPQKTRDIVERWYQRAVDLASVKTLLQRDETDVATYPELQWDA
QVRHGSSLHHEEKKFIKLRKLRISSQGEDSLHHFLDLPPDEKVDPRDVPLIALGGSGGGY
KVMYGFTGFISAAKKHGLWDCITWTAGVSGSCWTIAAYYTIARHDAQRLIDHYLTVASEL
AHPMSIHALNMVARSKRGVYFLIGPLVSKAQKSIIGLGIMDLYSTLTATYQLLSREPKGR
LSRATFQWSKIWHRSGIDKGLEPMPLLAAVRRVPKYSYEPKTISAKARDVKKQPTSRQLD
SAEGNDPANQVVSANRRSKKLFQYFEISPLEVGSPDLNRYVPTWAWGRTFISGYSVDRRP
EQSFSLLLGQCTSAPAGPLAECIKALLVTIPKNTIVARLVTIFNNLLQSKYFEGFWGNPI
RAGHDSNPFYGLERPLGMREHTSEHSMYISRVPHQHQRGMHSSDQSISDPAALQPHPLPQ
WEAQGRTRLMDSGMANNLPNHILARPERGVDVFISFDASSDIHTGAAIQRLHHFAADFNV
ELQEVTWEFHKPQRNEVLSSTQGLDIESRYIDHYARVFRGTRQSGQNIYIIYCPLLPNGT
NPGYNPTTASFSTSTNLMWTPDQVKSVLTTAEANVSNYAIDTIKRVRYMGAKPR

Enzyme Prediction     

No EC number prediction in KAF5656986.1.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
132835	cPLA2_like	1.05e-56	482	1064	1	433	Cytosolic phospholipase A2, catalytic domain; hydrolyses arachidonyl phospholipids. Catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms. Movement of the cPLA2 lid possibly exposes a greater hydrophobic surface and the active site. cPLA2 belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Calcium is required for cPLA2 to bind with membranes or phospholipids. Group IV cPLA2 includes six intercellular enzymes: cPLA2alpha, cPLA2beta, cPLA2gamma, cPLA2delta, cPLA2epsilon, and cPLA2zeta.
132839	cPLA2_Grp-IVA	1.23e-27	483	940	2	356	Group IVA cytosolic phospholipase A2; catalytic domain; Ca-dependent. Group IVA cPLA2, an 85 kDa protein, consists of two domains: the regulatory C2 domain and the alpha/beta hydrolase PLA2 domain. Group IVA cPLA2 is also referred to as cPLA2-alpha. The catalytic domain of cytosolic phospholipase A2 (cPLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms. Movement of the cPLA2 lid possibly exposes a greater hydrophobic surface and the active site. cPLA2 belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Calcium is required for cPLA2 to bind with membranes or phospholipids. A calcium-dependent phospholipid binding domain resides in the N-terminal region of cPLA2; it is homologous to the C2 domain superfamily which is not included in this hierarchy. Includes PLA2G4A from chicken, human, and frog.
132841	cPLA2_Grp-IVC	1.06e-20	480	1067	1	424	Group IVC cytoplasmic phospholipase A2; catalytic domain; Ca-independent. Group IVC cPLA2, a small 61 kDa protein, is a single domain alpha/beta hydrolase. It lacks a C2 domain; therefore, it has no Ca-dependence. Group IVC cPLA2 is also referred to as cPLA2-gamma. The cPLA2-gamma enzyme is predominantly found in cardiac and skeletal muscles, and to a lesser extent in the brain. Human cPLA2-gamma is approximately 30% identical to cPLA2-alpha. The catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms. Movement of the cPLA2 lid possibly exposes a greater hydrophobic surface and the active site. cPLA2 belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Includes PLA2G4C protein from human and Pla2g4c protein from mouse.
132840	cPLA2_Grp-IVB-IVD-IVE-IVF	2.92e-14	477	940	7	406	Group IVB, IVD, IVE, and IVF cytosolic phospholipase A2; catalytic domain; Ca-dependent. Group IVB, IVD, IVE, and IVF cPLA2 consists of two domains: the regulatory C2 domain and alpha/beta hydrolase PLA2 domain. Group IVB, IVD, IVE, and IVF cPLA2 are also referred to as cPLA2-beta, -delta, -epsilon, and -zeta respectively. cPLA2-beta is approximately 30% identical to cPLA2-alpha and it shows low enzymatic activity compared to cPLA2alpha. cPLA2-beta hydrolyzes palmitic acid from 1-[14C]palmitoyl-2-arachidonoyl-PC and arachidonic acid from 1-palmitoyl-2[14C]arachidonoyl-PC, but not from 1-O-alkyl-2[3H]arachidonoyl-PC. cPLA2-delta, -epsilon, and -zeta are approximately 45-50% identical to cPLA2-beta and 31-37% identical to cPLA2-alpha. It's possible that cPLA2-beta, -delta, -epsilon, and -zeta may have arisen by gene duplication from an ancestral gene. The catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms. Movement of the cPLA2 lid possibly exposes a greater hydrophobic surface and the active site. cPLA2 belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Calcium is required for cPLA2 to bind with membranes or phospholipids. The calcium-dependent phospholipid binding domain resides in the N-terminal region of cPLA2; it is homologous to the C2 domain superfamily which is not included in this hierarchy. It includes PLA2G4B, PLA2G4D, PLA2G4E, and PLA2G4F from humans.
214474	PLAc	1.41e-13	482	942	28	405	Cytoplasmic phospholipase A2, catalytic subunit. Cytosolic phospholipases A2 hydrolyse arachidonyl phospholipids. Family includes phospholipases B isoforms.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGJ01251.1|GH39	1.09e-273	1	410	1	432
QGI70362.1|GH39	1.09e-273	1	410	1	432
CCT74970.1|GH39	3.09e-273	1	410	1	432
QGI87720.1|GH39	8.78e-273	1	410	1	432
QKD60357.1|GH39	1.76e-272	1	410	1	432

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1CJY_A	3.07e-10	482	580	144	239	Human Cytosolic Phospholipase A2 [Homo sapiens],1CJY_B Human Cytosolic Phospholipase A2 [Homo sapiens]
5U22_A	2.90e-09	24	374	26	347	Structure of N2152 from Neocallimastix frontalis [Neocallimastix frontalis]
5IXC_A	1.11e-08	482	579	284	375	Human GIVD cytosolic phospholipase A2 in complex with Methyl gamma-Linolenyl Fluorophosphonate [Homo sapiens],5IXC_B Human GIVD cytosolic phospholipase A2 in complex with Methyl gamma-Linolenyl Fluorophosphonate [Homo sapiens],5IZR_A Human GIVD cytosolic phospholipase A2 in complex with Methyl gamma-Linolenyl Fluorophosphonate inhibitor and Terbium Chloride [Homo sapiens],5IZR_B Human GIVD cytosolic phospholipase A2 in complex with Methyl gamma-Linolenyl Fluorophosphonate inhibitor and Terbium Chloride [Homo sapiens],5IZR_C Human GIVD cytosolic phospholipase A2 in complex with Methyl gamma-Linolenyl Fluorophosphonate inhibitor and Terbium Chloride [Homo sapiens],5IZR_D Human GIVD cytosolic phospholipase A2 in complex with Methyl gamma-Linolenyl Fluorophosphonate inhibitor and Terbium Chloride [Homo sapiens]
5IZ5_A	1.11e-08	482	579	284	375	Human GIVD cytosolic phospholipase A2 [Homo sapiens],5IZ5_B Human GIVD cytosolic phospholipase A2 [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|B1WAZ6|PA24A_XENTR	3.67e-14	482	940	144	578	Cytosolic phospholipase A2 OS=Xenopus tropicalis OX=8364 GN=pla2g4a PE=2 SV=1
sp|Q7T0T9|PA24A_XENLA	6.35e-14	482	940	144	578	Cytosolic phospholipase A2 OS=Xenopus laevis OX=8355 GN=pla2g4a PE=2 SV=1
sp|P50392|PA24A_DANRE	1.50e-11	482	940	138	569	Cytosolic phospholipase A2 OS=Danio rerio OX=7955 GN=pla2g4a PE=2 SV=1
sp|Q68DD2|PA24F_HUMAN	2.15e-11	479	801	311	570	Cytosolic phospholipase A2 zeta OS=Homo sapiens OX=9606 GN=PLA2G4F PE=1 SV=3
sp|Q50L41|PA24F_MOUSE	1.45e-10	452	939	286	713	Cytosolic phospholipase A2 zeta OS=Mus musculus OX=10090 GN=Pla2g4f PE=1 SV=3

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000298	0.999658	CS pos: 18-19. Pr: 0.9767

TMHMM  Annotations     

There is no transmembrane helices in KAF5656986.1.