CAZyme Information: EPrPRT00000016087-p1

Basic Information

• Species: Pythium arrhenomanes
• Lineage: Oomycota; NA; ; Pythiaceae; Pythium; Pythium arrhenomanes
• CAZyme ID: EPrPRT00000016087-p1
• CAZy Family: GH131
• CAZyme Description: Thioredoxin.

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1038	ParrATCC12531_SC00305|CGC1	116649.27	7.6645

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_ParrhenomanesATCC12531	13857	1223556	52	13805

• Gene Location: location=ParrATCC12531_SC00305:2647-6346(+)

Full Sequence      

MKALARIDFFRKVPEELQVTSGSGKVFTVVSFLTMVLLVFSHYNAYMTQSTRTYVSLDSH
QEDQLRINFNVSLVAVPCQHASVDLSDHMGQRFVNITRHIRHFKLATSKTTQQVTRLDEI
VLDDTVPTWGGVERTTHAGVHYSTPLTEANFFEFMSKYELVLVNYYAPWCPFCQQLNPEW
ERAAAQLQDHPEYSERVVMATVDCTDDAAVYLCQRAGIRAFPSMLIYMYGSTHTRYIYNG
PRKSEYLLQFLDLFYRRLEPDADFAEEVHTDNAPTLPMNVNHENIDSLTLKKVKRTVPGD
AIEGCEVSGSISVNRVPGKLVFTARSPDQSFEHKGINVTHHVNHFSFGQIRASEHLVDGA
RSSFLPSKRFPLDTAMFFAENVNITIEHYLNIVGFDHSDHREYIFDRVPRTYEFSASSNQ
YNATRSEPAAMFTFDISPLVILVFKDNMPLYHFLTSLCAVVGGVFTVIGLVDFAPQKLPI
GVRPRIIIMPPAVDKRAVDAPLVALFGVSVAVKLLLLPSYTSTDFEVHRNWLAITHSLPP
AQWYHEATSEWTLDYPPFFAYFEYALSLVAARVDPALVTISATPVFSARILLFQRLSVIV
SDAVLFYAVYAYCTSWPSVTTTESAFSRHKRLVVMLLTTLDAGLLYVDHIHFQYNGMLLG
LLLLSAAKLRLQQDLQGALLYAVLLMFKHIYLYAAPLYFVYLLGHHCYAVATPRDTERTR
TRSLSNTDVHETIQSQHDGNAAFSLFRFLRLGVLVLVVFAVAFGSVLYAHPDPLAGLQQI
ASRLFPVQRGLVHAYWAPNVWALYAFLDKALVLLKLAPAPAEGVALMSGGLVQEASFAVL
ASVPPLVCAVLTFASMMPVLYTVWRYPDSSLFMSALVYCMHCSFMLGYHVHEKAILQSVN
DMRLYRFASIASSISLFPLLFTPAEQLTKVLIALVHALVAFVTLNPLLKDSLKQRHIRAT
AVGLRTFEKLYLALLACVAAGAMLFPYFPGNIGAKYPFLPLMAISVTCAVANVYVWGFAL
TQHFRKLEAVKSYLLPTK

Enzyme Prediction     

EC	2.4.1.265:13	2.4.1.-:9

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT57	510	1016	3e-140	0.9854469854469855

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
397324	Alg6_Alg8	7.84e-151	509	1016	1	472	ALG6, ALG8 glycosyltransferase family. N-linked (asparagine-linked) glycosylation of proteins is mediated by a highly conserved pathway in eukaryotes, in which a lipid (dolichol phosphate)-linked oligosaccharide is assembled at the endoplasmic reticulum membrane prior to the transfer of the oligosaccharide moiety to the target asparagine residues. This oligosaccharide is composed of Glc(3)Man(9)GlcNAc(2). The addition of the three glucose residues is the final series of steps in the synthesis of the oligosaccharide precursor. Alg6 transfers the first glucose residue, and Alg8 transfers the second one. In the human alg6 gene, a C->T transition, which causes Ala333 to be replaced with Val, has been identified as the cause of a congenital disorder of glycosylation, designated as type Ic OMIM:603147.
239259	PDI_a_family	4.13e-29	144	251	1	101	Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family include PDI and PDI-related proteins like ERp72, ERp57 (or ERp60), ERp44, P5, PDIR, ERp46 and the transmembrane PDIs. PDI, ERp57, ERp72, P5, PDIR and ERp46 are all oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. These proteins usually contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and may also contain one or more redox inactive TRX-like (b) domains. Only one a domain is required for the oxidase function but multiple copies are necessary for the isomerase function. The different types of PDIs may show different substrate specificities and tissue-specific expression, or may be induced by stress. PDIs are in their reduced form at steady state and are oxidized to the active form by Ero1, which is localized in the ER through ERp44. Some members of this family also contain a DnaJ domain in addition to the redox active a domains; examples are ERdj5 and Pfj2. Also included in the family is the redox inactive N-terminal TRX-like domain of ERp29.
400361	COPIIcoated_ERV	2.83e-27	303	472	53	223	Endoplasmic reticulum vesicle transporter. This family is conserved from plants and fungi to humans. Erv46 works in close conjunction with Erv41 and together they form a complex which cycles between the endoplasmic reticulum and Golgi complex. Erv46-41 interacts strongly with the endoplasmic reticulum glucosidase II. Mammalian glucosidase II comprises a catalytic alpha-subunit and a 58 kDa beta subunit, which is required for ER localization. All proteins identified biochemically as Erv41p-Erv46p interactors are localized to the early secretory pathway and are involved in protein maturation and processing in the ER and/or sorting into COPII vesicles for transport to the Golgi.
404692	ERGIC_N	1.16e-23	4	94	1	91	Endoplasmic Reticulum-Golgi Intermediate Compartment (ERGIC). This family is the N-terminal of ERGIC proteins, ER-Golgi intermediate compartment clusters, otherwise known as Ervs, and is associated with family COPIIcoated_ERV, pfam07970.
273454	pdi_dom	8.54e-22	146	252	1	99	protein disulfide-isomerase domain. This model describes a domain of eukaryotic protein disulfide isomerases, generally found in two copies. The high cutoff for total score reflects the expectation of finding both copies. The domain is similar to thioredoxin but the redox-active disulfide region motif is APWCGHCK. [Protein fate, Protein folding and stabilization]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ29794.1|GT57	6.20e-219	494	1034	10	568
CCA20034.1|GT57	6.90e-128	502	1015	12	495
AAI00615.1|GT57	5.05e-92	513	1016	25	507
NP_950200.2|GT57	1.88e-91	513	1016	25	507
AAH61244.1|GT57	1.88e-91	513	1016	25	507

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6SNH_X	1.23e-15	524	919	87	433	Cryo-EM structure of yeast ALG6 in complex with 6AG9 Fab and Dol25-P-Glc [Saccharomyces cerevisiae],6SNI_X Cryo-EM structure of nanodisc reconstituted yeast ALG6 in complex with 6AG9 Fab [Saccharomyces cerevisiae]
2DJ2_A	5.44e-12	146	251	12	109	Chain A, Protein disulfide-isomerase A4 [Mus musculus]
2B5E_A	7.66e-12	146	251	19	117	Crystal Structure of Yeast Protein Disulfide Isomerase [Saccharomyces cerevisiae],3BOA_A Crystal structure of yeast protein disulfide isomerase. [Saccharomyces cerevisiae]
3IDV_A	8.03e-12	146	251	135	232	Crystal structure of the a0a fragment of ERp72 [Homo sapiens]
1MEK_A	1.38e-11	146	251	12	112	Chain A, PROTEIN DISULFIDE ISOMERASE [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q6P8H8|ALG8_MOUSE	3.34e-92	513	1016	25	507	Probable dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase OS=Mus musculus OX=10090 GN=Alg8 PE=2 SV=2
sp|Q0P5D9|ALG8_BOVIN	3.31e-90	513	1016	25	507	Probable dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase OS=Bos taurus OX=9913 GN=ALG8 PE=2 SV=1
sp|O80505|ALG8_ARATH	1.35e-89	506	1016	16	497	Probable dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase OS=Arabidopsis thaliana OX=3702 GN=At2g44660 PE=2 SV=3
sp|Q9BVK2|ALG8_HUMAN	6.30e-89	513	1016	25	507	Probable dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase OS=Homo sapiens OX=9606 GN=ALG8 PE=1 SV=2
sp|Q7RXP5|ALG8_NEUCR	2.64e-78	508	1016	14	495	Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=alg-8 PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000000	0.000007

TMHMM  Annotations     

Start	End
21	43
449	471
632	654
690	712
748	770
785	807
837	859
869	891
904	921
931	948
969	988
998	1020