CAZyme Information: PIW_T006260-RA-p1

Basic Information

• Species: Globisporangium iwayamae
• Lineage: Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium iwayamae
• CAZyme ID: PIW_T006260-RA-p1
• CAZy Family: GH47
• CAZyme Description: ER degradation-enhancing alpha-mannosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1138		126655.44	5.1330

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_GiwayamaeDAOMBR242034	14874	1223558	0	14874

• Gene Location: location=PiwaDAOMBR242034_SC00906:3695-7320(+)

Full Sequence      

MHFSGLRELSGKSYKSFKNRFRRHLTDVQCLKYHEAGNWWHYEWCVDASVRQYHPVRYQP
TPAAEGEQEASVVLGRYATGTPQVLRIHPAENLSRLRHPDYSGYYAQQQYARGDACGSVD
LSIPQPQLRAVDINYKCCVYRANETYIEGIEEPAVCQYTMTVCTPVACGLMQKDQYVLGA
SMRVSEEERLVLAATVKDMFYHAYHGYLENAYPLDALLPISCRGETFELGKIQMLTLIDT
LDTLAILQDAKEFQYAVNLVLSRADFDLDTEVSVFETTIRVLGGLLSAHLFAVDSKLALY
PPGVYKNELLQLAMDLGDRLMPAFETPTGIPYGTVNLRNGVPVGETTIASTAGAGSLSME
FTMLSVLTSDPKYSNAARGAVRALYQRRSSLGLLGKHINTKTGDWTETLSGPGSNSDSFY
EYLFKMYMTFNDEESLEMFASVYPAVLQHNLHGDWYADVSMWSGCGHGSVVFENLAAFWP
GMQASVGHLHSATKSMNSFYRVWRDFGFIPEQFNVLDWKPMQLIESTFYMHEATGDSSWL
RAGAHFVHSLQKHAKTKCGYATIADIETKEQEDNMPSFFLSETSKYLILLFDTSHFYREG
NYVMTTEAHPFPILPASLVDPIIFAEQLAAANQSTAATTTTATLTGESGDAIATAVPAGV
GLSAYKMKQLQCLPQRFWDLFNYQVGYESAAVARTERCQPATTSPNSLKKTTLESAPAAT
AAESHKQPQKKDGSLDTLESWLPELERRLGKTLGQFKVDGTMTTASIDDLVKLDSSADPK
DHAWVKSFMDEHREEFFGKKSFKSIYGGARFGQFRVDQLEHSMRFTREDTGEWLESSGVG
DAVHVLVSSGKEQQRIDFAFGYDDTEATETATKTARHYSEDDLDAELESTKHLVYDMKYD
LTLPGERTCRLGVLISSQREQRPELRYSFPCVGAGFGLTNRMARSQVFPMAEIEIAKPLD
ACGWLANDHVKGKVVVTTRGVCFFESKAWNAARRGALGVIVVNNEDGDRIMVMGGSGTSD
DTAGDDKKVSGDNAPADESEIPVVMVPQRLGAWFDRQLSVAAENGEQLTVEIEFKVRDMT
QQPSSGAQYPYVIGTADNLRVFGPEWGVHLHRTSQGDDQHQDSYTIAIVETPVETVTP

Enzyme Prediction     

EC	3.2.1.113:20

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH47	199	613	2.9e-124	0.9977578475336323

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396217	Glyco_hydro_47	2.40e-128	199	613	1	453	Glycosyl hydrolase family 47. Members of this family are alpha-mannosidases that catalyze the hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man(9)(GlcNAc)(2).
240427	PTZ00470	4.39e-74	170	615	54	520	glycoside hydrolase family 47 protein; Provisional
238300	PA	1.10e-14	954	1072	25	126	PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction of proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins into which the PA domain is inserted include the following: i) various signal peptide peptidases including, hSPPL2a and 2b which catalyze the intramembrane proteolysis of tumor necrosis factor alpha, ii) various proteins containing a C3H2C3 RING finger including, Arabidopsis ReMembR-H2 protein and various E3 ubiquitin ligases such as human GRAIL (gene related to anergy in lymphocytes), iii) EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein), iv) various plant vacuolar sorting receptors such as Pisum sativum BP-80, v) glutamate carboxypeptidase II (GCPII), vi) yeast aminopeptidase Y, vii) Vibrio metschnikovii VapT, a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease, viii) lactocepin (a cell envelope-associated protease from Lactobacillus paracasei subsp. paracasei NCDO 151), ix) various subtilisin-like proteases such as melon Cucumisin, and x) human TfR (transferrin receptor) 1 and 2.
240122	PA_subtilisin_1	5.88e-13	932	1048	1	98	PA_subtilisin_1: Protease-associated domain containing subtilisin-like proteases, subgroup 1. A subgroup of PA domain-containing subtilisin-like proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins into which the PA domain is inserted include the following subtilisin-like proteases: i) melon cucumisin, ii) Arabidopsis thaliana Ara12, iii) Alnus glutinosa ag12, iv) members of the tomato P69 family, and v) tomato LeSBT2. However, these proteins belong to other subtilisin-like subgroups. Relatively little is known about proteins in this subgroup.
239041	PA_EDEM3_like	2.23e-11	948	1044	16	102	PA_EDEM3_like: protease associated domain (PA) domain-containing EDEM3-like proteins. This group contains various PA domain-containing proteins similar to mouse EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein). EDEM3 contains a region, similar to Class I alpha-mannosidases (gylcosyl hydrolase family 47), N-terminal to the PA domain. EDEM3 accelerates glycoprotein ERAD (ER-associated degradation). In transfected mammalian cells, overexpression of EDEM3 enhances the mannose trimming from the N-glycans, of a model misfolded protein [alpha1-antitrypsin null (Hong Kong)] as well as, from total glycoproteins. Mannose trimming appears to be involved in the selection of ERAD substrates. EDEM3 has a different specificity of trimming than ER alpha-mannosidase 1. The significance of the PA domain to EDEM3 has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ27914.1|GH47	0.0	106	1132	2	1041
AIG56334.1|GH47	7.04e-237	22	1110	40	929
AIG55397.1|GH47	3.06e-218	30	623	33	622
ANM69210.1|GH47|3.2.1.113	1.70e-116	177	615	27	475
ANM69209.1|GH47|3.2.1.113	1.86e-116	177	615	27	475

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KIJ_A	5.83e-53	196	613	9	451	Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]
1FMI_A	6.68e-53	196	613	14	456	Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens]
1FO2_A	6.99e-53	196	613	14	456	Crystal Structure Of Human Class I Alpha1,2-Mannosidase In Complex With 1-Deoxymannojirimycin [Homo sapiens],1FO3_A Crystal Structure Of Human Class I Alpha1,2-Mannosidase In Complex With Kifunensine [Homo sapiens]
5KK7_A	2.86e-52	196	613	9	451	Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase T688A mutant and Thio-disaccharide substrate analog complex [Homo sapiens],5KK7_B Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase T688A mutant and Thio-disaccharide substrate analog complex [Homo sapiens]
1X9D_A	3.61e-52	196	613	92	534	Crystal Structure Of Human Class I alpha-1,2-Mannosidase In Complex With Thio-Disaccharide Substrate Analogue [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9FG93|MNS4_ARATH	2.10e-116	177	615	27	475	Alpha-mannosidase I MNS4 OS=Arabidopsis thaliana OX=3702 GN=MNS4 PE=1 SV=1
sp|Q9SXC9|MNS5_ARATH	1.14e-106	168	614	13	479	Alpha-mannosidase I MNS5 OS=Arabidopsis thaliana OX=3702 GN=MNS5 PE=1 SV=1
sp|Q9BV94|EDEM2_HUMAN	3.47e-102	196	618	39	485	ER degradation-enhancing alpha-mannosidase-like protein 2 OS=Homo sapiens OX=9606 GN=EDEM2 PE=1 SV=2
sp|Q8BJT9|EDEM2_MOUSE	4.67e-101	196	618	39	485	ER degradation-enhancing alpha-mannosidase-like protein 2 OS=Mus musculus OX=10090 GN=Edem2 PE=1 SV=1
sp|Q925U4|EDEM1_MOUSE	2.77e-91	174	609	107	577	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Mus musculus OX=10090 GN=Edem1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000049	0.000000

TMHMM  Annotations     

There is no transmembrane helices in PIW_T006260-RA-p1.