CAZyme Information: KAF6517995.1

Basic Information

• Species: Fusarium oxysporum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
• CAZyme ID: KAF6517995.1
• CAZy Family: PL1
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1076		120517.52	8.8669

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FoxysporumFo5176	17912	660025	0	17912

• Gene Location: location=JACDXP010000010:555299-559381(-)

Full Sequence      

MWIIKACSVLAAVCTVAADSAGPKIDFYSTTGAPQHLAAGILYGIPDNTNQIPDSLLSGF
GFNYYRGAGAQVSHGWSYNEASFQQRFSSAHNNYIVTRRHNGGFVLLLNDLWGFDCSSNN
NTSPGPGDNGDWSSYDKFVQAIIANVKKYNMQEGLVIDIWNEPEGGCFWGRSIDQWLQMW
GRGWHQFNDAFGKNVLTSGPTLASQPGTTNSWWTRWAQFVKNNNSVPDQYVWHEEGGSGS
NFEYSYGVLQQILTNYGLPQRQININEYATFNEQVPAGSAFWISQLERRNAIGLRGNWLG
GTQLHDLAASLLSKPNPSNYASTGYFANGDWWVYNYYSHNMTGQRVATSVSSDGQLDAYA
TVDTAARTARVLLGCHPPTTGTYDVTFSGLAKLGLPSSGTLQVRTWKFAVGSDVHYSQMG
PPQDLGNYGHTISNGQKTRGIVERWYQRAVDLASVKTLLQRDETDFATYPELKWDAHVRH
GSSLHHEEQKFIGLRKLRISSQGEDSLHRFLDLSPDEKVDLRDVPLIALGGSGGGYKVMY
GFAGFISAAKKHGLWDCITWTAGVSGSCWTLAAYYTIARHDIQRLIDHYLTVASELAHPM
SIHALNMVARSKRGVYFLIGPLVSKAQKSIIGLGIMDLYSTLTATYQLLSREPKGRLSRA
TFQWSKIWHRSGIDKGLEPMPLLAAVRRVPKYSYEPKTISAKARDVKKQPTSRQLDTVEG
NDQANSTVSLNRRSKKLFQYFEISPLEVGSPDLNRYVPTWAWGRTFISGYSVDRRPEQSF
SLLLGQCTSAPAGPLAECIKALLVTIPKNTMVARLITLFNNLLQSKHFEGFWGNPIRAGH
DPNPFYGLERPVGMREHTSEHSMYLSRVPHQHQRGMHSSDKSVSDPVALQPHSFPPWEAQ
GRTRLMDSGMANNLPNHILARPERSVDVFLSFDASSDIHTGAAVQRLHHFAADFDIELRD
VTREFHNPQRNKVLSSSYASEVESRYIDHYARVFYGRRQSGQDMYIIYCPLLPNALNPDY
NPTTASFSTSTNLMWTPDQVKSVLTTSETNVSHYAIDTIKRVMRKVYEDKKAYRLV

Enzyme Prediction     

No EC number prediction in KAF6517995.1.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
132835	cPLA2_like	5.65e-59	478	1064	1	437	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	2.14e-26	479	936	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	2.13e-19	478	935	3	316	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.
214474	PLAc	1.11e-16	478	938	28	405	Cytoplasmic phospholipase A2, catalytic subunit. Cytosolic phospholipases A2 hydrolyse arachidonyl phospholipids. Family includes phospholipases B isoforms.
132840	cPLA2_Grp-IVB-IVD-IVE-IVF	3.41e-16	474	936	8	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKD60357.1|GH39	0.0	1	438	1	438
CCT74970.1|GH39	8.78e-317	1	438	1	438
QGJ01251.1|GH39	1.38e-315	1	438	1	438
QGI70362.1|GH39	1.38e-315	1	438	1	438
QGI87720.1|GH39	1.12e-314	1	438	1	438

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5U22_A	7.17e-10	139	436	124	402	Structure of N2152 from Neocallimastix frontalis [Neocallimastix frontalis]
1CJY_A	2.08e-09	478	576	144	239	Human Cytosolic Phospholipase A2 [Homo sapiens],1CJY_B Human Cytosolic Phospholipase A2 [Homo sapiens]
5IZ5_A	2.85e-09	478	935	284	679	Human GIVD cytosolic phospholipase A2 [Homo sapiens],5IZ5_B Human GIVD cytosolic phospholipase A2 [Homo sapiens]
5IXC_A	4.91e-09	478	783	284	527	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q7T0T9|PA24A_XENLA	2.94e-12	513	936	173	578	Cytosolic phospholipase A2 OS=Xenopus laevis OX=8355 GN=pla2g4a PE=2 SV=1
sp|B1WAZ6|PA24A_XENTR	3.87e-12	513	936	173	578	Cytosolic phospholipase A2 OS=Xenopus tropicalis OX=8364 GN=pla2g4a PE=2 SV=1
sp|Q68DD2|PA24F_HUMAN	3.71e-11	475	935	311	708	Cytosolic phospholipase A2 zeta OS=Homo sapiens OX=9606 GN=PLA2G4F PE=1 SV=3
sp|Q50L41|PA24F_MOUSE	4.33e-10	448	935	286	713	Cytosolic phospholipase A2 zeta OS=Mus musculus OX=10090 GN=Pla2g4f PE=1 SV=3
sp|Q50L43|PA24D_MOUSE	7.35e-10	478	785	289	534	Cytosolic phospholipase A2 delta OS=Mus musculus OX=10090 GN=Pla2g4d PE=1 SV=3

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000255	0.999713	CS pos: 18-19. Pr: 0.9775

TMHMM  Annotations     

There is no transmembrane helices in KAF6517995.1.