CAZyme Information: PHYBL_185479T0-p1

Basic Information

• Species: Phycomyces blakesleeanus
• Lineage: Mucoromycota; Mucoromycetes; ; Phycomycetaceae; Phycomyces; Phycomyces blakesleeanus
• CAZyme ID: PHYBL_185479T0-p1
• CAZy Family: GT15
• CAZyme Description: Protein involved in dolichol pathway for N-glycosylation (mannosyltransferase family)

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
601		68881.02	9.0830

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PblakesleeanusNRRL1555	16528	763407	0	16528

• Gene Location: location=PblaNRRL1555-_SC04:531466-533329(-)

Full Sequence      

MRRVLFFALIAIYCIACPYTKVEESFNLQAIYDVMHGIPLSDYDHFDFPGVVPRTFVGAT
ILGLLSRLIRPFFVGEWISTREQVIPRLILGAMVSVGMGYFERSVRLLLGKRTSTIFMIL
LFCQFHIVFWSSRTLPNTLALPLVLLGLSHWILSMTTRANRTTQLTLMIRYLTFTGLVFR
FEVGILLAIILVFEWALYRHITFRTIIIQGALTTVVSLGLTIPIDSYFWQRWVWPEGSVF
FFNAILNKSSEWGTLPFYAYFVNFLPRVLMVSYPLALMGFFTDRRIRVLLAPALVYTGLF
SMLPHKEWRFIMYTIPIYTTAAAFTVSKLSLKARHSMYATVSLVGVAGALVVCFCGSIMM
LLVSMKNYPGGEALSVMNNMPLQSASIHLDVLTAMTGASRFGQTHSLWSYHKDESHRSID
DYLEAEYTHLISDTPLNNTPFEIISVTYGLEKIKRKSPRIYLQNIMSIFGKDWSWETLLP
VEIELEPKLYIFQLSHPQKVWVDYKIHHSSVLIYSKSYCPYCKRAKEILNKYCPHQYQVV
EIDLRQDGRELQAALIERTGRRTVPAIFMNGKIIGGSDDLAALDNQGVLEPQLPCNLHYL
Q

Enzyme Prediction     

EC	2.4.1.260:8

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT22	5	388	8e-77	0.9254498714652957

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
281842	Glyco_transf_22	1.91e-35	5	351	2	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.
239511	GRX_GRXh_1_2_like	2.15e-35	511	591	2	81	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	3.32e-34	511	593	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	1.80e-25	511	584	2	71	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	1.35e-20	509	590	1	80	Glutaredoxin [Posttranslational modification, protein turnover, chaperones].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDS09080.1|GT22	5.19e-205	10	595	9	592
SVE72883.1|GT22	1.78e-85	12	497	11	479
SVE83607.1|GT22	2.81e-84	17	497	16	479
SVE85441.1|GT22	2.99e-83	17	497	16	479
SVE84817.1|GT22	6.21e-83	17	497	16	479

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7NCV_A	2.58e-21	509	593	17	101	Chain A, Glutaredoxin, CPYC type [Chlamydomonas reinhardtii],7NCW_A Chain A, Glutaredoxin, CPYC type [Chlamydomonas reinhardtii]
4I2T_A	6.24e-19	499	593	5	100	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]
3UIW_A	1.82e-18	506	598	44	139	Zebrafish Grx2 (APO) [Danio rerio],3UIW_B Zebrafish Grx2 (APO) [Danio rerio]
5ZVL_A	6.06e-17	511	589	65	142	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	3.70e-16	506	593	34	120	Crystal structure of buckwheat glutaredoxin-glutathione complex [Polygonaceae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9BV10|ALG12_HUMAN	3.59e-74	8	493	19	482	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|A8MR93|ALG12_ARATH	4.52e-74	11	433	25	442	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	1.08e-70	12	493	24	480	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|Q9VH78|ALG12_DROME	2.67e-70	4	493	3	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|Q23361|ALG12_CAEEL	1.36e-68	12	420	14	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
0.002535	0.997445	CS pos: 16-17. Pr: 0.9553

TMHMM  Annotations     

Start	End
113	132
139	156
171	193
206	228
259	281
288	305
309	331
338	360