CAZyme Information: AEO53259.1

Basic Information

• Species: Thermothelomyces thermophilus
• Lineage: Ascomycota; Sordariomycetes; ; Chaetomiaceae; Thermothelomyces; Thermothelomyces thermophilus
• CAZyme ID: AEO53259.1
• CAZy Family: AA11
• CAZyme Description: glycoside hydrolase family 47 protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1113	CP003002|CGC24	121729.41	5.5093

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TthermophilusATCC42464	9292	573729	195	9097

• Gene Location: location=CP003002:863080-866550(-)

Full Sequence      

MTCRELAASDGSGTSRPGPALNDLPCPRMQARVRRRCTWLGLHNSTLWLGCMLLALCVGY
WPVAAAMRPDRVRELRQETVNMFYHGFDNYMKIAFPEDELRPVSCSPLTRDRENPRNVEL
NDVLGNYSLTLIDSLSTLAILASAPPEDGETGPKALRDFQDGVAALVEQYGDGTSGPSGV
GLRGRGFDVDSKVQVFETVIRGVGGLLSAHLFAIGALPITGYNPRHPGDDLLHPRPVVWP
NGFRYDGQLLRLALDLGQRLLPAFYTRTGMPYPRVNLRHGIPFYTNSPLHEAAAPGTTAD
GSPEITETCSAGAGSLVLEFTVLSRLTGDPRFEQLAKRAFWAVWYRKSQIGLIGAGVDAE
QGHWIGSYAVIGAGADSFFEYALKSHILLSGHELPNQTAVRPDRASDGWLDPNTLFNPLS
DAENSPDSFLEAWHHAHASIKRHLYSDRDHPHYENVNLWTGSLASSWVDSLGAYYSGLLV
LAGEVSEAIETNLLYAAIWTRYAALPERWSIREKTVEGGLGWWPLRPEFIESTYHLYRAT
KDPWYLYVGEMVLRDIARRCWTPCGWAGLQNVLDGQKSDRMESFFLGETAKYMYLLYDDQ
HPLNSLDAAYVFNTEGHPLIIPKAASASGRRRPRAERKDLAIYNDDAFTNSCPPRPSATP
ISGSVIAARDDIYHAARMLDLHLLSTSPRTVDGGQMSGQHMARSNFTLFPWTLPSELLPS
NGTCAKVHHPTELVLEFASNAGQMVGGGAFNFMIGAQNLERLSADRIRVTSLSGLKLTMH
LEGDLEQEWRVTKVNGIPLGRDEFLVFDRSILGEVSDPRFNLVRDPVMVKLQHLHQVDIP
EDDADTVDDDAPQASNHEPGPEPEPLEDGPNPSVTVTDLGSLVKSLLSRITSSLDNIQLP
TSLPRIGATLLPFNLVLNTTAITSTGIGSAPLPPGASPPSAAQRHRTPPFGPVPDALFPW
STIYASPDDACSSPLPDAAPRDHQIILIRRGGCSFSTKLANIPAFTPSPDSLQLVIVVSD
DGDDADQDNRGGGGGGGGVAGLVRPLLDEVQRTPGGIQRRHPIAMVMVGGGEAVFRQLEA
ASRVGVVRRYFVESQGVKIRNIIVDEGGDEMDW

Enzyme Prediction     

No EC number prediction in AEO53259.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH47	82	620	6.5e-144	0.9955156950672646

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396217	Glyco_hydro_47	2.22e-134	82	621	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	1.12e-59	74	623	70	520	glycoside hydrolase family 47 protein; Provisional
239039	PA_PoS1_like	9.22e-08	965	1005	38	78	PA_PoS1_like: Protease-associated (PA) domain PoS1-like. This group includes various PA domain-containing proteins similar to Pleurotus ostreatus (Po)S1. PoSl, the main extracellular protease in P. ostreatus is a subtilisin-like serine protease belonging to the peptidase S8 family. Ca2+ and Mn2+ both stimulate the protease activity of (Po)S1. Ca2+ protects PoS1 from autolysis. PoS1 is a monomeric glycoprotein, which may play a role in the regulation of laccases in lignin formation. (Po)S1 participates in the degradation of POXA1b, and in the activation of POXA3, (POXA1b and POXA3 are laccase isoenzymes), but its effect may be indirect. The significance of the PA domain to PoS1 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.
239038	PA_C_RZF_like	7.93e-07	949	1001	30	86	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.
240122	PA_subtilisin_1	8.17e-05	947	1001	6	59	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
AEO53259.1|GH47	0.0	1	1113	1	1113
AEO70189.1|GH47	0.0	67	1110	1	1025
VBB71678.1|GH47	0.0	33	1112	43	1144
CDP22661.1|GH47	0.0	33	1112	43	1157
CAP60020.1|GH47	0.0	33	1112	43	1122

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1FMI_A	1.12e-39	66	621	1	456	Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens]
1FO2_A	2.11e-39	69	621	4	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]
5KIJ_A	3.31e-39	79	621	9	451	Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]
1X9D_A	5.62e-39	62	621	75	534	Crystal Structure Of Human Class I alpha-1,2-Mannosidase In Complex With Thio-Disaccharide Substrate Analogue [Homo sapiens]
5KK7_A	1.56e-38	79	621	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|O94726|MNL1_SCHPO	6.96e-121	51	681	11	528	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mnl1 PE=3 SV=2
sp|Q925U4|EDEM1_MOUSE	1.11e-115	64	653	114	628	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Mus musculus OX=10090 GN=Edem1 PE=1 SV=1
sp|Q92611|EDEM1_HUMAN	1.82e-114	64	621	119	586	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Homo sapiens OX=9606 GN=EDEM1 PE=1 SV=1
sp|P38888|MNL1_YEAST	3.17e-100	64	634	24	515	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=MNL1 PE=1 SV=1
sp|Q9SXC9|MNS5_ARATH	7.36e-94	42	621	5	478	Alpha-mannosidase I MNS5 OS=Arabidopsis thaliana OX=3702 GN=MNS5 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999726	0.000280

TMHMM  Annotations     

Start	End
39	61