Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q5B7W2

Entry ID Method Resolution Chain Position Source
AF-Q5B7W2-F1 Predicted AlphaFoldDB

No variants for Q5B7W2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5B7W2

No associated diseases with Q5B7W2

2 regional properties for Q5B7W2

Type Name Position InterPro Accession
domain Glycoside hydrolase, family 2, immunoglobulin-like beta-sandwich 196 - 301 IPR006102
domain Mannosidase Ig/CBM-like domain 679 - 766 IPR041447

Functions

Description
EC Number 3.2.1.25 Glycosidases, ie enzymes hydrolyzing O- and S-glycosyl compounds
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

1 GO annotations of molecular function

Name Definition
beta-mannosidase activity Catalysis of the hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides.

2 GO annotations of biological process

Name Definition
glycoprotein catabolic process The chemical reactions and pathways resulting in the breakdown of a glycoprotein, a protein that contains covalently bound glycose (i.e. monosaccharide) residues; the glycose occurs most commonly as oligosaccharide or fairly small polysaccharide but occasionally as monosaccharide.
mannan catabolic process The chemical reactions and pathways resulting in the breakdown of mannan, the main hemicellulose of soft (coniferous) wood, made up of D-mannose, D-glucose and D-galactose.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MGAFTQHVLS EGWSFKDSGD QSPDAWLSVP TVPSVVHQDL QANGKLDDPF IGLNELSARW
70 80 90 100 110 120
VNEKSWTYRN VFQKPTVPAG SSIFLVFDGL DTFAKVKLDG QVILESDNMF LAHRVDITKA
130 140 150 160 170 180
LDVEGEHTLE IDFDCALLRA RELRKQHPDH KWVGFNGDTA RLSVRKAQYH WGWDWGPVLM
190 200 210 220 230 240
TAGIWKEVRL EVYSAKISDL WTEVHLAEDH SKARITAAAE VETQGTGNSY KATFTLSLQG
250 260 270 280 290 300
QQIGKEVATL DGNVAKTTFD VQEPSLWWPN GYGDQTLYEI SVSLEKEEEQ AHQVSKKFGI
310 320 330 340 350 360
RTAEVIQRPD KHGKSFFFRI NGVDIFCGGA CWIPADSLLT NITPDRYRKW IELMAVGHQV
370 380 390 400 410 420
MIRVWGGGIY EDESFYQACD EVGVMVWQDF MFGCGNYPTW PEILESIEKE AEYNLRRLRH
430 440 450 460 470 480
HPSIVIWVGN NEDYQVQEQQ GLTYNYADKD PESWLKTDFP ARYIYEHLLP KAVQKIIPSA
490 500 510 520 530 540
YYHPGSPWGD GKITSDPTVG DMHQWNVWHG TQEKYQIFDT LGGRFNSEFG MEAFPHMSTI
550 560 570 580 590 600
DHFVTNEADK YPQSHVLDFH NKADGHERRI ATYLVENLRT ATDLEVYIYL TQVVQAETMM
610 620 630 640 650 660
FGYRGWRRQW GDERHCGGAL LWQLNDCWPT ISWAIVDYFL RPKPAFYAVS RVLKPLAIGV
670 680 690 700 710 720
RREHHDWSVS HAQPPKTSKY ELWVVSSLLK EVIGKVELRF ISIKTGLAIH ESIVRENVTI
730 740 750 760 770 780
VPNGTTNILD GVIDHAVDEP HVLAARLWVD GELVARDVDW PQPFKYLDLS DRGLEITRIS
790 800 810 820 830 840
KTESEQVLEL SARKPVKCLV FEERDNVRVS DSAIDIVPGD EQFVTIKGLK RSDAPLKYKF
LGQ