CAZyme Information: SPRG_01028-t26_1-p1

Basic Information

• Species: Saprolegnia parasitica
• Lineage: Oomycota; NA; ; Saprolegniaceae; Saprolegnia; Saprolegnia parasitica
• CAZyme ID: SPRG_01028-t26_1-p1
• CAZy Family: AA17
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1082	KK583190|CGC6	118228.56	4.9903

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SparasiticaCBS223-65	20435	695850	314	20121

• Gene Location: location=KK583190:1124843-1128144(+)

Full Sequence      

MKRRAALLVLLVVALGAGALTHVPKPSATTAPPMARPRAADRTSLDGVCRTFHMSGSWWR
YEWCHQEHVRQYSVDPVTGAEASVNIIGRFFGATDGEASPTRARPFLTHVFLNGDMCHGG
SRQSPVARNRSAEVRFSCCSFRPTETYIESISEPLLCEYLVSVCTPLACVTKLQAPDESS
DDTKRLRATVKAMFYHAYNNYMEHAFPLDNLRPISCKGDTFELGKIPMLTLIDTLDTLVV
FGDFDEFRRAVGLVLAGASFDLNTEVSVFETTIRVLGGLLSAHMFAVDASLGIYPDGAYT
DGLLRLAVDLADRLLPAFVTKTGIPYGTVNLRYGVPEGETTVASTAGAGSLTMEFTMLSV
LTGNPVYAIASRKAVRALYERKSSVGLLGKHIDVDSGDWTETISGPGSNSDSFYEYLLKM
YVLFGDDESLAMFQHVYSNVMEHNKHGDWYGDVSMWDGCTGGAAIVFDNLVAFWPGMQTL
LGDFETSAKSLNAYYQVWHKYGFLPEQFDVGRWRPKKASSNRYPLRPELIESTFYMHAAT
RDDTWRKAGAAFVASIERFSKTTCGYASIADVESRAQEDDMPSFFLSETCKYLYLLFDDT
NLLRQGNYVFTTEAHPFPVLSSAQVAAIWTRGSDPSLQPAPRQALTCPRLPFYAPVSFNT
SYQDAFVKMKPRCDAPRRSGAKASKKTPAKVTAPRVLHGGDALGNFLIDQLVGGFRARSD
RFPGDALKVTNLGDPKIVVEFHSSDPAPLADFRIHNFETDVTTRCRLLVYDADDQLLDTI
TCSGALFGPTKTEGASVLVEKRPLELASPLRACAAMEAVSIGAIALVQRGDCYFDDKARR
GMDAGASAVIIVNNDAAEDLMIMARSSSLDAALDETPISVPIVMVAPTAEARLRRPNTRI
SLEHHSVPLDDDDFPYVVGSRYDLKVVGPHGWGLHLALKTSDATGVSAWTIALVDATAPE
EDDSDDVDASTSEETTTQAFARVLQQLKGLGFSDEALHLLENEDDADLRLEALLNGLRDV
GLDEMADKVALKTSDAKLATTSKDDPLTPADAKRSQSMDREADSASSDMCTDADAPTNVP
GR

Enzyme Prediction     

EC	3.2.1.113:20

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH47	193	619	9.1e-137	0.9977578475336323

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396217	Glyco_hydro_47	3.65e-142	193	619	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	1.42e-82	177	619	63	518	glycoside hydrolase family 47 protein; Provisional
239038	PA_C_RZF_like	7.56e-16	772	885	16	125	PA_C-RZF_ like: Protease-associated (PA) domain C_RZF-like. This group includes various PA domain-containing proteins similar to C-RZF (chicken embryo RING zinc finger) protein. These proteins contain a C3H2C3 RING finger. C-RZF is expressed in embryo cells and is restricted mainly to brain and heart, it is localized to both the nucleus and endosomes. Additional C3H2C3 RING finger proteins belonging to this group, include Arabidopsis ReMembR-H2 protein and mouse sperizin. ReMembR-H2 is likely to be an integral membrane protein, and to traffic through the endosomal pathway. Sperizin is expressed in haploid germ cells and localized in the cytoplasm, it may participate in spermatogenesis. The significance of the PA domain to these proteins 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.
239047	PA_GO-like	1.68e-13	778	893	17	125	PA_GO-like: Protease-associated domain containing proteins like Arabidopsis thaliana growth-on protein GRO10. This group contains various PA domain-containing proteins similar to the functionally uncharacterized Arabidopsis GRO10. The PA domain 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.
240122	PA_subtilisin_1	1.16e-11	785	894	3	105	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AIG56334.1|GH47	0.0	1	1037	1	1029
AIG55397.1|GH47	0.0	38	1037	22	1022
UIZ27914.1|GH47	1.66e-235	130	937	19	1012
QCQ78383.1|GH47	1.79e-132	159	618	16	478
BBM97073.1|GH47	2.09e-132	148	619	8	474

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KKB_A	1.02e-60	178	620	13	468	Structure of mouse Golgi alpha-1,2-mannosidase IA and Man9GlcNAc2-PA complex [Mus musculus],5KKB_B Structure of mouse Golgi alpha-1,2-mannosidase IA and Man9GlcNAc2-PA complex [Mus musculus]
1NXC_A	1.26e-60	178	620	11	466	Structure of mouse Golgi alpha-1,2-mannosidase IA reveals the molecular basis for substrate specificity among Class I enzymes (family 47 glycosidases) [Mus musculus]
4AYO_A	1.37e-55	175	615	2	431	Structure of The GH47 processing alpha-1,2-mannosidase from Caulobacter strain K31 [Caulobacter sp. K31],4AYP_A Structure of The GH47 processing alpha-1,2-mannosidase from Caulobacter strain K31 in complex with thiomannobioside [Caulobacter sp. K31],4AYQ_A Structure of The GH47 processing alpha-1,2-mannosidase from Caulobacter strain K31 in complex with mannoimidazole [Caulobacter sp. K31],4AYR_A Structure of The GH47 processing alpha-1,2-mannosidase from Caulobacter strain K31 in complex with noeuromycin [Caulobacter sp. K31],5MEH_A Crystal structure of alpha-1,2-mannosidase from Caulobacter K31 strain in complex with 1-deoxymannojirimycin [Caulobacter sp. K31],5NE5_A Crystal structure of family 47 alpha-1,2-mannosidase from Caulobacter K31 strain in complex with kifunensine [Caulobacter sp. K31]
1FO2_A	7.33e-54	193	623	17	460	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]
5KIJ_A	1.12e-53	193	619	12	451	Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9FG93|MNS4_ARATH	1.50e-130	181	626	35	480	Alpha-mannosidase I MNS4 OS=Arabidopsis thaliana OX=3702 GN=MNS4 PE=1 SV=1
sp|Q9BV94|EDEM2_HUMAN	4.84e-119	176	616	25	479	ER degradation-enhancing alpha-mannosidase-like protein 2 OS=Homo sapiens OX=9606 GN=EDEM2 PE=1 SV=2
sp|Q9SXC9|MNS5_ARATH	4.65e-117	184	622	35	481	Alpha-mannosidase I MNS5 OS=Arabidopsis thaliana OX=3702 GN=MNS5 PE=1 SV=1
sp|Q8BJT9|EDEM2_MOUSE	1.94e-116	163	616	12	479	ER degradation-enhancing alpha-mannosidase-like protein 2 OS=Mus musculus OX=10090 GN=Edem2 PE=1 SV=1
sp|Q925U4|EDEM1_MOUSE	1.05e-105	185	615	124	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 SP

Other	SP_Sec_SPI	CS Position
0.278494	0.721492	CS pos: 30-31. Pr: 0.4218

TMHMM  Annotations     

Start	End
7	24