CAZyme Information: CDH58106.1

Basic Information

• Species: Lichtheimia corymbifera
• Lineage: Mucoromycota; Mucoromycetes; ; Lichtheimiaceae; Lichtheimia; Lichtheimia corymbifera
• CAZyme ID: CDH58106.1
• CAZy Family: GT22
• CAZyme Description: dolichyl-p-man:man c-pp-dolichyl-alpha-6-mannosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
597		67550.52	8.7136

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_LcorymbiferaJMRCFSU9682	12379	1263082	97	12282

• Gene Location: location=CBTN010000052:224917-226773(-)

Full Sequence      

MKSLALVFIALFCISCPYTKVEESFNLQATHDIIHYGTDISNYDHVEFPGVVPRTFIGSL
VLGAITKMILFVTPSDLQLLVNEQLIVRLVLGTIVAAALTRFQTAVGRLFSSGASTAFAL
LTCCQFHILFWSSRTLPNTLALPLVLMGMAEWIESLAVVQQQQQQRRVQHLQRMIWYLAP
AGIIFRFEAGILLAILVMIEWIVYHNLPLSTLLKHGILSVILSLVLTLSVDSFFWQRWLW
PEGEVFYFNAILNKSSEWGTMPVYAYFLLFLPRILMVSYPLALLAYCRDATVRRLLMPSL
IYIGLFSCLPHKEWRFIIYTIPVWTAAAAASVVGLIRSRMGLALVLSGGLASIVGSVVML
SISMQNYPGGEALARLHLLEPSTQPLHVHLDVPTAMTGASRFGELFRPVWRYSKDESHQS
PDDYIQAEYTHLITSHPELHNDHFIVVDEIRGLDSVRLKTPKTYIQDLRQFISNRHLDAI
LPLNIVTAPKLFIMKLRGHPQTQWVNHIIEKYPMVLYSKTYCPFCRRAKQILNTHCKNYK
VIEVDLRPDGIAMKEALFTISGRRTFPNLFVHGKSIGGSDDIALLQSQGRLAEILPC

Enzyme Prediction     

No EC number prediction in CDH58106.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT22	4	382	5.3e-79	0.9203084832904884

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
239511	GRX_GRXh_1_2_like	1.52e-30	513	594	1	82	Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of proteins similar to human GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, which are members of this subfamily. Also included in this subfamily are the N-terminal GRX domains of proteins similar to human thioredoxin reductase 1 and 3.
281842	Glyco_transf_22	1.13e-28	3	359	4	358	Alg9-like mannosyltransferase family. Members of this family are mannosyltransferase enzymes. At least some members are localized in endoplasmic reticulum and involved in GPI anchor biosynthesis.
274016	GRX_euk	2.92e-27	515	595	2	83	Glutaredoxin. Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system. Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress, reduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides. This model represents eukaryotic glutaredoxins and includes sequences from fungi, plants and metazoans as well as viruses.
239017	GRX_family	3.63e-23	513	585	1	70	Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, as well as E. coli GRX1 and GRX3, which are members of this family. E. coli GRX2, however, is a 24-kDa protein that belongs to the GSH S-transferase (GST) family.
395371	Glutaredoxin	1.97e-16	515	576	2	60	Glutaredoxin.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDS09080.1|GT22	0.0	1	597	1	592
SVE72883.1|GT22	9.89e-88	16	515	16	495
AAI42133.1|GT22	8.45e-87	15	433	29	436
SVE91084.1|GT22	4.02e-86	16	514	16	494
SVE91709.1|GT22	4.02e-86	16	514	16	494

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3UIW_A	1.57e-17	503	597	38	136	Zebrafish Grx2 (APO) [Danio rerio],3UIW_B Zebrafish Grx2 (APO) [Danio rerio]
5ZVL_A	2.38e-17	506	595	57	146	Crystal Structure of Wheat Glutarredoxin [Triticum aestivum],5ZVL_B Crystal Structure of Wheat Glutarredoxin [Triticum aestivum],5ZVL_C Crystal Structure of Wheat Glutarredoxin [Triticum aestivum],5ZVL_D Crystal Structure of Wheat Glutarredoxin [Triticum aestivum],5ZVL_E Crystal Structure of Wheat Glutarredoxin [Triticum aestivum]
7NCV_A	2.91e-17	514	595	19	101	Chain A, Glutaredoxin, CPYC type [Chlamydomonas reinhardtii],7NCW_A Chain A, Glutaredoxin, CPYC type [Chlamydomonas reinhardtii]
5KQA_A	1.98e-16	503	595	28	120	Crystal structure of buckwheat glutaredoxin-glutathione complex [Polygonaceae]
2E7P_A	8.33e-16	513	595	21	103	Crystal structure of the holo form of glutaredoxin C1 from populus tremula x tremuloides [Populus tremula x Populus tremuloides],2E7P_B Crystal structure of the holo form of glutaredoxin C1 from populus tremula x tremuloides [Populus tremula x Populus tremuloides],2E7P_C Crystal structure of the holo form of glutaredoxin C1 from populus tremula x tremuloides [Populus tremula x Populus tremuloides],2E7P_D Crystal structure of the holo form of glutaredoxin C1 from populus tremula x tremuloides [Populus tremula x Populus tremuloides]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q8VDB2|ALG12_MOUSE	2.03e-81	16	462	29	464	Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase OS=Mus musculus OX=10090 GN=Alg12 PE=2 SV=2
sp|Q9BV10|ALG12_HUMAN	8.84e-80	16	433	28	433	Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase OS=Homo sapiens OX=9606 GN=ALG12 PE=1 SV=1
sp|Q9VH78|ALG12_DROME	8.60e-75	1	497	1	478	Probable Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase OS=Drosophila melanogaster OX=7227 GN=Alg12 PE=2 SV=1
sp|A8MR93|ALG12_ARATH	6.34e-72	10	459	25	464	Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase OS=Arabidopsis thaliana OX=3702 GN=ALG12 PE=1 SV=1
sp|Q23361|ALG12_CAEEL	2.10e-61	14	422	17	422	Probable Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase OS=Caenorhabditis elegans OX=6239 GN=algn-12 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.155752	0.844240	CS pos: 21-22. Pr: 0.8375

TMHMM  Annotations     

Start	End
50	72
85	102
109	131
182	204
217	239
263	285
292	309
314	336
341	363