CAZyme Information: H257_17283-t26_1-p1

Basic Information

• Species: Aphanomyces astaci
• Lineage: Oomycota; NA; ; Saprolegniaceae; Aphanomyces; Aphanomyces astaci
• CAZyme ID: H257_17283-t26_1-p1
• CAZy Family: GT60
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1139		124793.65	4.8349

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AastaciAPO3	19584	N/A	465	19119

• Gene Location: location=KI913216:5823-9287(-)

Full Sequence      

MTHVHVVATSLLTLASILAAAALPPSPSPAAAAEPNEVAGNGPATSASPLLDASSMTDVC
RTFHTSGSWWRYEWCHEGHVRQYSVDPTTGDESQVISLGTYDAAHSNHYHTTSSSTDKDL
RAYISHVFLHGDMCNSTDVARNRSTDVHLTCCVFRPQETYIESVAEPRLCDYLVTVCTPS
ACASPPPPSNMTLKTKEELAATVKSMFYHAYDSYMTHAFPLDNLKPITCQGESFELGKIP
MLTLIDTLDTLVVFGDKDEFRRAVALVTTHATFDLDTEVSVFETTIRVLGGLLSAHLFAV
DPTLQLYSNTSEPAYSGGLLALAADLGDRLLPAFVTPTGIPFGTVNLRRGVPKGETSVAS
TAGAGSLSIEFTMLSILTKNPIYAQAARQAVRGLFFRRSALGLVGKHIDTATGEWTETSS
GPGSNSDSFYEYLLKMYVLYGDSEALDMFEPVYSAVMEHNKHGDWYTDVSMWDGCLSNQH
HQSFIFDNLVAFWPGMQSLLGDFASSTRSLNAFYQVWQQYSFLPEQFDVGRWRPKKQNRN
GYPLRPELLESTYYVHVATNDSSWLTAGALAVQSLERYAKTTCGYAAISDVETRTVEDTM
PSYFLSETCKYLYLLFDETNFLRKANYVFTTEAHPFPVLPSAEVTPILTASDETKYAVPR
TATHWNKYLTCPVIQFWDDVGFRRAFHDRFQMARPRCTTSSSTKPKANKKTTPEDDKIVT
KSLYGGKTLGYFHVEQLLGGFRVTRRSDRGQWLKVTNLGDPHIIVESHSSSEGGGGSSTT
TTSSSSLTEFRVFEFASQTMRRCRLQVLGRWVSCSAAEFGLTKDPSVAVSIQNAPVLYGT
PHLGCTPLESTPHRVVVLHRGECFFDEKANRATQAGAVAAVIVNSEPNPSAAQEEEENSL
MVMGPSKEATDQQQKIDIPVVMVPFAADAMIREAVANGDTISLEVGVVTELEYPRAAGSR
FDVAVAGPDGWGVHLVAKMQPVGTPLWTISITEHDARGLDVDDEEVEEVEEPRNPGTPNP
RQKANKVDVDEYATKLKGLGFSDQQLARMNSDDPDDRLDALVDGLRALGLHDLVAKFVGR
SKDVGVGEGSTNPETPADLASELDAPVSFDQPDEGHDVAQSTREDADDVIDHDDTCAAV

Enzyme Prediction     

EC	3.2.1.113:20

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH47	206	638	1.4e-133	0.9977578475336323

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396217	Glyco_hydro_47	6.33e-135	206	638	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	1.68e-77	194	640	67	520	glycoside hydrolase family 47 protein; Provisional
239047	PA_GO-like	1.31e-12	817	943	24	137	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	4.06e-12	816	943	2	116	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.
238300	PA	1.47e-11	825	945	19	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AIG56334.1|GH47	0.0	59	1101	47	1045
AIG55397.1|GH47	0.0	59	1081	32	1018
UIZ27914.1|GH47	3.87e-227	131	975	9	1011
CAB4097030.1|GH47	2.20e-129	191	640	32	475
QCQ78383.1|GH47	3.56e-129	203	640	50	481

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KKB_A	5.77e-62	188	639	14	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	7.18e-62	188	639	12	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	7.28e-55	189	634	3	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]
5KIJ_A	7.56e-51	203	638	9	451	Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]
1FMI_A	8.64e-51	203	638	14	456	Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9FG93|MNS4_ARATH	7.88e-127	197	640	38	475	Alpha-mannosidase I MNS4 OS=Arabidopsis thaliana OX=3702 GN=MNS4 PE=1 SV=1
sp|Q9SXC9|MNS5_ARATH	6.30e-120	188	641	25	481	Alpha-mannosidase I MNS5 OS=Arabidopsis thaliana OX=3702 GN=MNS5 PE=1 SV=1
sp|Q9BV94|EDEM2_HUMAN	8.21e-115	203	635	39	479	ER degradation-enhancing alpha-mannosidase-like protein 2 OS=Homo sapiens OX=9606 GN=EDEM2 PE=1 SV=2
sp|Q8BJT9|EDEM2_MOUSE	5.98e-113	203	635	39	479	ER degradation-enhancing alpha-mannosidase-like protein 2 OS=Mus musculus OX=10090 GN=Edem2 PE=1 SV=1
sp|Q92611|EDEM1_HUMAN	2.20e-102	196	634	127	582	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Homo sapiens OX=9606 GN=EDEM1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000714	0.999243	CS pos: 32-33. Pr: 0.8770

TMHMM  Annotations     

There is no transmembrane helices in H257_17283-t26_1-p1.