CAZyme Information: EKG16421.1

Basic Information

• Species: Macrophomina phaseolina
• Lineage: Ascomycota; Dothideomycetes; ; Botryosphaeriaceae; Macrophomina; Macrophomina phaseolina
• CAZyme ID: EKG16421.1
• CAZy Family: GH3
• CAZyme Description: Glycoside hydrolase family 47

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
962	AHHD01000269|CGC1	107131.43	4.7407

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_MphaseolinaMS6	14712	1126212	906	13806

• Gene Location: location=AHHD01000269:109443-112482(-)

Full Sequence      

MLRYRRYRVFVVFAVLTVLVLWQFAGSETWSSGLGVTLSGAGSSSSHGQAPAADSIPDVL
VPPKSGSPIATENKDKTPDITVPAAEKPPGKEEPPALPKASKPVQGKPPPALETAAGSLD
DDVNSPYLDTDAVAGVPTEPQIVVPHEGGEGRKEVDVEEKVIHWRKLDEHFPVTSTIQLP
KGSPKPVPKIQATFAEESLSERKERDAKLMAVKEAMVFSWNGYRKYAWMKDELSPVSNGS
RNPFAGWGATLVDALDTLYIMGMEEEFEEAVAAVADIDFTTSFRKDIPLFETVIRYLGGL
VAAYDISGLKHRILLDKAVELAEILMGAFDTPNRMPITFYYWMPTYASQPHRAGTRVVLA
EIGSLSVEFTRLAQLTKEPKYYDAIARITNAFNEWQDTLLPGMWPVHVDASGCKRPEMGA
TSAHPPLKPADKLVPSENSGKTPLSYDEEVSSSYTGAEKPKNQESNKNNPERFGGKNPVP
DDDHDDIDDELVKRQLDDPISLSKAALDESKEDEVRTEKATSSLKKGPSSTKKVAATYTL
ADCEPQGLEASSPYGSQQFTLGGMSDSMYEYFPKEYLLLGGLAPEYQELYEKSADVVKED
LLYRPMLPDGSPDVLFAGTLSVTPPDKKRKQITKKLKAEGTHLTCFAGGMFAYGAKIFGR
TEDVKIGAQLTEGCVWAYNATSTGIMPESFIMTPCESIKGCEWNETKYYEELDPYAESRQ
ETYERQLEHYSSQVALARAKATETPDSEFVIATAAATPEAIPTNAIPNSLNKHRWERRQL
GGVENDSKGKSSTTPTKATTYSDAHEPADYDDSNDPVISHIWKPQKPLSHEEYVEKRIEE
ERLPEGFVRVESRHYILRPEAIESVWYMYRITGDVHWREVGWNMFTAIQTHCRAEFGYSA
IDDVTKTAPTLKDEMESFWLAETLKYFWLLFADEDVVSLDEWVLNTEAHPFRRPDAGEWP
RK

Enzyme Prediction     

EC	3.2.1.113:7

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH47	216	953	1.3e-171	0.9955156950672646

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396217	Glyco_hydro_47	0.0	215	953	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	1.87e-88	169	955	28	520	glycoside hydrolase family 47 protein; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBX98421.1|GH47	2.19e-250	162	954	152	909
QRD01632.1|GH47	4.13e-248	162	954	134	921
CAE7209968.1|GH47	2.88e-246	137	954	105	967
QSS69163.1|GH47	7.66e-223	149	954	139	858
QKX63570.1|GH47	2.65e-222	149	954	151	897

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KKB_A	1.95e-42	203	951	20	465	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	2.30e-42	203	951	18	463	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]
1KKT_A	3.39e-31	166	381	2	218	Structure of P. citrinum alpha 1,2-mannosidase reveals the basis for differences in specificity of the ER and Golgi Class I enzymes [Penicillium citrinum],1KKT_B Structure of P. citrinum alpha 1,2-mannosidase reveals the basis for differences in specificity of the ER and Golgi Class I enzymes [Penicillium citrinum],1KRE_A Structure Of P. Citrinum Alpha 1,2-Mannosidase Reveals The Basis For Differences In Specificity Of The Er And Golgi Class I Enzymes [Penicillium citrinum],1KRE_B Structure Of P. Citrinum Alpha 1,2-Mannosidase Reveals The Basis For Differences In Specificity Of The Er And Golgi Class I Enzymes [Penicillium citrinum],1KRF_A Structure Of P. Citrinum Alpha 1,2-mannosidase Reveals The Basis For Differences In Specificity Of The Er And Golgi Class I Enzymes [Penicillium citrinum],1KRF_B Structure Of P. Citrinum Alpha 1,2-mannosidase Reveals The Basis For Differences In Specificity Of The Er And Golgi Class I Enzymes [Penicillium citrinum]
2RI8_A	9.83e-30	207	381	4	183	Penicillium citrinum alpha-1,2-mannosidase complex with glycerol [Penicillium citrinum],2RI8_B Penicillium citrinum alpha-1,2-mannosidase complex with glycerol [Penicillium citrinum],2RI9_A Penicillium citrinum alpha-1,2-mannosidase in complex with a substrate analog [Penicillium citrinum],2RI9_B Penicillium citrinum alpha-1,2-mannosidase in complex with a substrate analog [Penicillium citrinum]
1X9D_A	6.35e-29	152	389	35	264	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|Q9C512|MNS1_ARATH	7.62e-42	212	952	101	535	Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS1 OS=Arabidopsis thaliana OX=3702 GN=MNS1 PE=1 SV=1
sp|O60476|MA1A2_HUMAN	5.28e-41	196	950	174	623	Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB OS=Homo sapiens OX=9606 GN=MAN1A2 PE=1 SV=1
sp|P45700|MA1A1_MOUSE	1.10e-40	181	951	171	640	Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA OS=Mus musculus OX=10090 GN=Man1a1 PE=1 SV=1
sp|P45701|MA1A1_RABIT	1.50e-40	203	949	9	452	Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA (Fragment) OS=Oryctolagus cuniculus OX=9986 GN=MAN1A1 PE=1 SV=1
sp|O02773|MA1A1_PIG	1.54e-40	187	950	183	643	Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA OS=Sus scrofa OX=9823 GN=MAN1A1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.994633	0.005385

TMHMM  Annotations     

Start	End
7	26