CAZyme Information: ATY60381.1

Basic Information

• Species: Cordyceps militaris
• Lineage: Ascomycota; Sordariomycetes; ; Cordycipitaceae; Cordyceps; Cordyceps militaris
• CAZyme ID: ATY60381.1
• CAZy Family: CE4
• CAZyme Description: Heat shock Hsp70

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1191		129654.05	6.9451

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CmilitarisATCC34164	9362	N/A	75	9287

• Gene Location: location=CP023323:1144859-1149472(+)

Full Sequence      

MSSINSRLKNFGFGKRKSTASIQTVDGVPPSHTGTPPPGQIPQSNLAGLAPLTSSTSTTS
LPMNHPGAGNRPPSYTANYPQNPAAQPLGRTSPLTNQGPNRTPPSQMVGGPPPINTGAPV
GYPPNMAQGMGGGPPMGHGGPPQGYPPPAGYPPGPPPQPSGPMAQQQFGQNRAEVEGSSQ
SKAQLIVGIDFGTTFSGVAFAFATNNEAKEDIITEWPGAGSYTKQKIPTVLYYDQYQKVV
GWGPDIADALAPTGYPKPGVQKVEWFKLQLMLSGNTYIDPINLPPLPPGKSEIDVAADYL
FKLRQAMRAALQKALGEVFNREERNIRYYLTVPAIWNDAGKAATRAAAIQAGFLRDENDN
RLTLVSEPEAAALFCSKTGLLNLRVHDAVLIVDCGGGTVDLIAYEVEEENPFTVAECTAG
SGDSCGSTALNRNFSNILRTKIRKMKLPEGSKTAGRVYAKCIMDFENRIKADFRNNGQKW
AVDVGIEAEFPEAGIEEGYMTFTNEEILQCFEPVVNRILELVRNQIIAIQAQNRTLQNIL
VVGGFGASEYLFQQIKLHVPPQFQSKVVRPMDSVAAIVKGAVTAGISERIITHRIARRHY
LMGTLQPFKEGYHPEAYRVPSLDGKDRCKFTRQIFVQRGQKVKNGETVKVSFFRQVAPGA
TLMYEDVLYACDDDVCPEYTKDPRIKEVVTLTSDLSRKNLEKDFERMDTPQGTFYRVYFD
IYLTLDGSEFSTELVCQGEVMGRCRYSSNLSICASDGDKLATVEAMLGALLPRQRPDMNG
ISRRRDCFTSTSNRLLLGFGILLSLLQCISASTNHSFLENWQAKFIEQTSPRDTVKRGSL
GAGDDKVPLVITNRCDMTIWPGTATQGGLGPGTGGFELQPGESKNLTVGSNWQGRIWGRT
NCTVNGESCACQTGDCFAKLDCQFSSAVPATLVEFNLAGGVNGMQTFYDISLVDGYNLPV
GIEHIPSENTSFVPPNLTNSACVATAGWLYDVAQPATYSSNETFPIPLEKNETNDMLSKW
CPWRNLAFPPQKPSDGIYPYPDDNIQRPSFSPCKSACATTGSDSDCCIGKYHDPTLCKPS
IYSKNVKAVCPDAYSFAFDDRSSTFIVPKGGGWRIVWCPAGRSTDILNQLAAQMYELASG
GKLSELSMRRLGNVSFVNSRKQSINEESAGERVYYPLVLLLAATGLVLVMT

Enzyme Prediction     

No EC number prediction in ATY60381.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH152	853	1119	1e-63	0.9953703703703703

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
212671	HSPA12_like_NBD	2.44e-129	185	586	1	404	Nucleotide-binding domain of HSPA12A, HSPA12B and similar proteins. Human HSPA12A (also known as 70-kDa heat shock protein-12A) and HSPA12B (also known as 70-kDa heat shock protein-12B, chromosome 20 open reading frame 60/C20orf60, dJ1009E24.2) belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12A or HSPA12B. The gene encoding HSPA12A maps to 10q26.12, a cytogenetic region that might represent a common susceptibility locus for both schizophrenia and bipolar affective disorder; reduced expression of HSPA12A has been shown in the prefrontal cortex of subjects with schizophrenia. HSPA12A is also a candidate gene for forelimb-girdle muscular anomaly, an autosomal recessive disorder of Japanese black cattle. HSPA12A is predominantly expressed in neuronal cells. It may also play a role in the atherosclerotic process. The gene encoding HSPA12B maps to 20p13. HSPA12B is predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. HSPA12B expression is up-regulated in lipopolysaccharide (LPS)-induced inflammatory response in the spinal cord, and mostly located in active microglia; this induced expression may be regulated by activation of MAPK-p38, ERK1/2 and SAPK/JNK signaling pathways. Overexpression of HSPA12B also protects against LPS-induced cardiac dysfunction and involves the preserved activation of the PI3K/Akt signaling pathway.
395248	Thaumatin	6.25e-85	853	1119	1	211	Thaumatin family.
185757	TLP-PA	1.71e-54	851	1118	4	219	allergenic/antifungal thaumatin-like proteins: plant and animal homologs. This subfamily is represented by the thaumatin-like proteins (TLPs), Cherry Allergen Pru Av 2 TLP, Peach PpAZ44 TLP (a propylene-induced TLP in abscission), the Caenorhabditis elegans thaumatin family member (thn-6), and other plant and animal homologs. TLPs are involved in host defense and a wide range of developmental processes in fungi, plants, and animals. Due to their inducible expression by environmental stresses such as pathogen/pest attack, drought and cold, plant TLPs are classified as the pathogenesis-related (PR) protein family 5 (PR5). Several members of the plant TLP family have been reported as food allergens from fruits (i.e., cherry, Pru av 2; bell pepper, Cap a1; tomatoes, Lyc e NP24) and pollen allergens from conifers (i.e., mountain cedar, Jun a 3; Arizona cypress, Cup a3; Japanese cedar, Cry j3). TLPs are three-domain, crescent-fold structures with either an electronegative, electropositive, or neutral cleft occurring between domains I and II. It has been proposed that the antifungal activity of plant PR5 proteins relies on the strong electronegative character of this cleft. Some TLPs hydrolyze the beta-1,3-glucans of the type commonly found in fungal walls. TLPs within this subfamily contain 16 conserved Cys residues.
185754	Thaumatin-like	7.33e-51	849	1118	1	157	the sweet-tasting protein, thaumatin, and thaumatin-like proteins involved in host defense. This family is represented by the sweet-tasting protein thaumatin from the African berry Thaumatococcus daniellii and thaumatin-like proteins (TLPs) involved in host defense and a wide range of developmental processes in fungi, plants, and animals. Plant TLPs are classified as pathogenesis-related (PR) protein family 5 (PR5), their expression is induced by environmental stresses such as pathogen/pest attack, drought and cold. TLPs included in this family are such proteins as zeamatin, found in high concentrations in cereal seeds; osmotin, a salt-induced protein in osmotically stressed plants; and PpAZ44, a propylene-induced TLP in abscission of young fruit. Several members of the plant TLP family have been reported as food allergens from fruits (i.e., cherry, Pru av 2; bell pepper, Cap a1; tomatoes, Lyc e NP24) and pollen allergens from conifers (i.e., mountain cedar, Jun a 3; Arizona cypress, Cup a3; Japanese cedar, Cry j3). Thaumatin and TLPs are three-domain, crescent-fold structures with either an electronegative, electropositive, or neutral cleft occurring between domains I and II. It has been proposed that the antifungal activity of plant PR5 proteins relies on the strong electronegative character of this cleft. Some TLPs hydrolyze the beta-1,3-glucans of the type commonly found in fungal walls. Most TLPs contain 16 conserved Cys residues. A deletion within the third domain (domain II) of the Triticum aestivum thaumatin-like xylanase inhibitor is observed, thus, only 10 conserved Cys residues are present within this smaller TLP and similar homologs.
128501	THN	3.35e-45	851	1119	3	218	Thaumatin family. The thaumatin family gathers proteins related to plant pathogenesis. The thaumatin family includes very basic members with extracellular and vacuolar localization. Thaumatin itsel is a potent sweet-tasting protein. Several members of this family display significant in vitro activity of inhibiting hyphal growth or spore germination of various fungi probably by a membrane permeabilizing mechanism.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
VDB89779.1|GH152	0.0	2	1139	4	1079
UNI24053.1|GH152	7.31e-181	830	1162	34	372
QPG96228.1|GH152	5.86e-179	793	1161	2	370
QLI69933.1|GH152	4.03e-175	788	1161	102	475
QUC17904.1|GH152	7.93e-175	793	1161	19	387

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3ZS3_A	1.51e-35	849	1119	3	222	High resolution structure of Mal d 2, the thaumatin like food allergen from apple [Malus domestica]
2AHN_A	5.31e-31	853	1119	7	222	High resolution structure of a cherry allergen Pru av 2 [Prunus avium]
1DU5_A	1.05e-25	851	1119	5	206	The Crystal Structure Of Zeamatin. [Zea mays],1DU5_B The Crystal Structure Of Zeamatin. [Zea mays]
1Z3Q_A	6.64e-24	851	1119	5	200	Resolution of the structure of the allergenic and antifungal banana fruit thaumatin-like protein at 1.7A [Musa acuminata]
4L5H_A	2.53e-22	851	1119	5	198	Structure of haze forming proteins in white wines: Vitis vinifera thaumatin-like proteins [Vitis vinifera],4L5H_B Structure of haze forming proteins in white wines: Vitis vinifera thaumatin-like proteins [Vitis vinifera],4MBT_A Structure of haze forming proteins in white wines: Vitis vinifera thaumatin-like proteins [Vitis vinifera],4MBT_B Structure of haze forming proteins in white wines: Vitis vinifera thaumatin-like proteins [Vitis vinifera]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A1P8B554|THLP1_ARATH	2.16e-40	843	1120	29	257	Thaumatin-like protein 1 OS=Arabidopsis thaliana OX=3702 GN=TLP1 PE=2 SV=1
sp|O80327|TLP1_PYRPY	5.55e-39	842	1119	18	244	Thaumatin-like protein 1 OS=Pyrus pyrifolia OX=3767 GN=TL1 PE=1 SV=1
sp|P28493|PR5_ARATH	1.23e-36	851	1119	28	239	Pathogenesis-related protein 5 OS=Arabidopsis thaliana OX=3702 GN=At1g75040 PE=1 SV=1
sp|Q5DWG1|CRJ35_CRYJA	1.72e-36	838	1120	16	239	Pathogenesis-related thaumatin-like protein 3.5 OS=Cryptomeria japonica OX=3369 PE=1 SV=1
sp|Q9FSG7|TP1A_MALDO	8.12e-35	842	1119	20	246	Thaumatin-like protein 1a OS=Malus domestica OX=3750 GN=TL1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000045	0.000000

TMHMM  Annotations     

There is no transmembrane helices in ATY60381.1.