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 P0DN29

Entry ID Method Resolution Chain Position Source
AF-P0DN29-F1 Predicted AlphaFoldDB

No variants for P0DN29

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P0DN29

No associated diseases with P0DN29

3 regional properties for P0DN29

Type Name Position InterPro Accession
domain Carbohydrate binding module family 20 504 - 610 IPR002044
domain GH15-like domain 40 - 449 IPR011613
domain Glucoamylase, CBM20 domain 502 - 609 IPR034836

Functions

Description
EC Number 3.2.1.3 Glycosidases, ie enzymes hydrolyzing O- and S-glycosyl compounds
Subcellular Localization
  • Secreted
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
extracellular region The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.

2 GO annotations of molecular function

Name Definition
glucan 1,4-alpha-glucosidase activity Catalysis of the hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose.
starch binding Binding to starch.

1 GO annotations of biological process

Name Definition
polysaccharide catabolic process The chemical reactions and pathways resulting in the breakdown of a polysaccharide, a polymer of many (typically more than 10) monosaccharide residues linked glycosidically.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MRVTSLLWSS LVIPAAVGFQ VRFKPSEDTA LDTVDDGTLQ SLLDNIGLNG SNAWDTRPGL
70 80 90 100 110 120
VIASPSKKDP NYFFTWTRDS ALVLKCITDA FAAGNTALQE TIHEYISSQA RIQLLNTRSG
130 140 150 160 170 180
GLSSGGLGEP KYRVDETPYN EDWGRPQADG PALRATALIA YARWLLENDY YDVAKSIVWP
190 200 210 220 230 240
VVKNDLSYVS EHWNTTAFDL WEEVNSPSFF TTIVQHRALV EGINIARALD ETCPHCESQA
250 260 270 280 290 300
PQALCYLQSY WTGTAVRSNY GQGRSGLDVA SILGSIHTFD PEGECDDTTF QPCSARALAN
310 320 330 340 350 360
HKAVTDSFRS IYKINGGIKQ GEAVAVGRYP EDVYFNGNPW YLATYAAAEQ LYDAMYQWNK
370 380 390 400 410 420
IGKITVTDVS MPFFKDIYPE VQTGTHESSS PEFGNIIAAV KAYAEGYIEV AKKYTPCTGM
430 440 450 460 470 480
LSEQFSRDNG TPLSVADLTW SYASYLTVMA RRNSVVPASW GEKNARDIPS TCVPSSATGP
490 500 510 520 530 540
YQTATITHWP PNLTPTAQPS PCPTALPTKN NVRFRLLATT QVGEDVFLVG SIPELGSWDV
550 560 570 580 590 600
KKAVPLNADI YADNCHQWYV DIELPTAVAF EYKFIRKRGG EVVWEQDPNR KYTVPQTCGV
SGAIKRDTWR