CAZyme Information: HMPREF1544_02334-t46_1-p1

Basic Information

• Species: Mucor circinelloides
• Lineage: Mucoromycota; Mucoromycetes; ; Mucoraceae; Mucor; Mucor circinelloides
• CAZyme ID: HMPREF1544_02334-t46_1-p1
• CAZy Family: CE4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
587		66428.50	8.4923

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Mcircinelloides1006PhL	12410	1220926	183	12227

• Gene Location: location=KE123916:15259-17095(+)

Full Sequence      

MKLVLACLFALIVSEAYLAPFTKVEESFNLQATYDIIHQTDQFDHVQFPGVVPRTFAGAS
LLSVMAWPVIQFAGLSSIDQQVLVRVILAACVVLSLGKFASGVKSLFGSATANITIMLII
CQFHLVFWSSRTLPNTLALPWVELGLSHWLYSLSQSSGRTYHLNWMIRYLTFAGVVFRFE
VGILLIILLISEYIHATVSPSNALKQMIVTAIISLVVTVPLDSYLWNAWLWPEGMVFYFN
AILNKSSEWGTLPFHAYFASFLPRLLLVSYPLACLAFVTNGRVRRMLMPMLIYIALFSFL
PHKEWRFIVYTIPVFTAAAATCISRSIHAASRSWLHRIALLVMLGGAAASFAIALVMFQV
SRLNYPGGEALFTLHEIEKNEPYVYVHMDADTAMTGASLYGQSNPNWSYSKNETHKTQDD
FLEARYTHIITSKPELFDTSLFEIIDETYGLDKVQLKSVDAYKRSIQNHDISPIEFRMSP
KLYTLRLINPQKTWIQTTLRKYSVVLYSKSYCPYCMAAKQLISKYCKHIEVIEVDRQRNG
YEIQDALIELTGQRTFPNLFKNGKSLGGYDRLSALDREGKLAGLCDS

Enzyme Prediction     

EC	2.4.1.260:8

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT22	5	380	3.4e-72	0.922879177377892

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
239511	GRX_GRXh_1_2_like	1.36e-32	504	584	2	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	9.28e-28	504	584	1	82	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.
281842	Glyco_transf_22	1.25e-27	3	352	1	359	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.
239017	GRX_family	8.82e-21	504	577	2	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	3.94e-18	503	582	2	80	Glutaredoxin [Posttranslational modification, protein turnover, chaperones].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDS09080.1|GT22	3.49e-181	20	582	17	587
SVE74698.1|GT22	2.36e-85	17	513	14	503
SVE86070.1|GT22	4.64e-85	17	513	14	503
SVE87325.1|GT22	4.64e-85	17	513	14	503
SVE87951.1|GT22	4.64e-85	17	513	14	503

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5ZVL_A	1.45e-18	504	584	65	145	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]
4I2T_A	1.64e-16	492	581	5	96	Crystal structure of the oxidized glutaredoxin from Chlorella sorokiniana T-89 [Chlorella sorokiniana],4I2U_A Crystal structure of the reduced glutaredoxin from Chlorella sorokiniana T-89 in complex with glutathione [Chlorella sorokiniana]
5KQA_A	8.00e-15	504	581	39	116	Crystal structure of buckwheat glutaredoxin-glutathione complex [Polygonaceae]
2HT9_A	2.11e-14	454	581	11	128	The structure of dimeric human glutaredoxin 2 [Homo sapiens],2HT9_B The structure of dimeric human glutaredoxin 2 [Homo sapiens]
2CQ9_A	3.58e-14	495	581	20	106	Chain A, GLRX2 protein [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A8MR93|ALG12_ARATH	6.00e-75	18	413	30	424	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|Q9BV10|ALG12_HUMAN	3.60e-74	3	430	12	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	9.84e-72	20	486	17	476	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|Q8VDB2|ALG12_MOUSE	3.12e-69	18	430	28	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|Q23361|ALG12_CAEEL	3.37e-60	18	422	18	429	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
0.000187	0.999810	CS pos: 18-19. Pr: 0.9505

TMHMM  Annotations     

Start	End
50	72
82	99
106	128
169	191
208	230
256	278
285	302
307	329
338	360