CAZyme Information: RO3G_03273-t26_1-p1

Basic Information

• Species: Rhizopus delemar
• Lineage: Mucoromycota; Mucoromycetes; ; Rhizopodaceae; Rhizopus; Rhizopus delemar
• CAZyme ID: RO3G_03273-t26_1-p1
• CAZy Family: CE4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
430		49174.42	9.4050

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_RdelemarRA99-880	17703	246409	244	17459

• Gene Location: location=CH476733:2680232-2681580(-)

Full Sequence      

MSQYLTFAGIVFRFEVGILLVILMFTEWIFSRFHLISIVKTITATALLSLITTVPLDSYF
WNQLLWPEGMVFYFNAILNKSSEWGTLPFYAYFTNFLPRLLLISYPLMIVAFARDTRVRR
ILCPMILYTLVFSLVPHKEWRFIIYTVPVFTAAAATQVNALLIYQRRSSAGRFGLLLLTG
GILASFFASLIMFQISSLNYPGGQALKSLHVINESTPFISVHMDAETAMTGASLFGQTNT
DWKYSKNEKDATEEDFIEARYTHILTANPEKFNSSLFETVHVTYGIGNIQLILPNKVYQD
TGPKKEIINLFGIVRLEVALTPKIYTLRAIYSQKTWVQALLRKYPVILFSKTYCPYCKRA
KQLIAKYSNSIKIIEVDLEENSRDIQLALHSISGQYTFPNLFIHGQSFGGFDNLSELDRQ
GKLSKLFLEQ

Enzyme Prediction     

EC	2.4.1.260:8

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT22	4	210	3.4e-44	0.5244215938303342

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
239511	GRX_GRXh_1_2_like	6.81e-32	345	426	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.
274016	GRX_euk	6.96e-28	346	427	1	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	2.63e-20	345	419	1	72	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.
223767	GrxC	2.58e-17	345	423	2	79	Glutaredoxin [Posttranslational modification, protein turnover, chaperones].
281842	Glyco_transf_22	3.90e-17	4	155	167	328	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDS09080.1|GT22	2.41e-124	1	426	170	589
SMR52727.1|GT22	4.47e-47	5	271	190	463
SMY24478.1|GT22	4.47e-47	5	271	190	463
SMQ50812.1|GT22	6.83e-47	5	271	217	490
CAD7198266.1|GT22	8.05e-47	8	276	209	476

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5ZVL_A	3.57e-17	345	429	64	148	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]
5KQA_A	2.33e-16	338	429	31	122	Crystal structure of buckwheat glutaredoxin-glutathione complex [Polygonaceae]
5GTX_A	3.62e-15	338	429	28	119	Crystal structure of mutated buckwheat glutaredoxin [Polygonaceae],5GTX_B Crystal structure of mutated buckwheat glutaredoxin [Polygonaceae]
2E7P_A	9.10e-15	345	426	21	102	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]
1Z7P_A	9.33e-15	345	426	22	103	Chain A, glutaredoxin [Populus tremula x Populus tremuloides],1Z7R_A Solution Structure of reduced 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|Q9VH78|ALG12_DROME	7.89e-45	10	280	169	438	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	6.24e-40	3	306	177	487	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|Q8VDB2|ALG12_MOUSE	4.87e-38	7	265	179	431	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	4.48e-36	7	265	178	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|Q9USD4|ALG12_SCHPO	1.69e-32	5	275	167	438	Probable Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=alg12 PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000029	0.000000

TMHMM  Annotations     

Start	End
4	26
33	55
89	111
118	137
142	164
173	195