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 A1A8H7

Entry ID Method Resolution Chain Position Source
AF-A1A8H7-F1 Predicted AlphaFoldDB

No variants for A1A8H7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A1A8H7

No associated diseases with A1A8H7

5 regional properties for A1A8H7

Type Name Position InterPro Accession
domain Creatinase, N-terminal 49 - 183 IPR000587
domain Peptidase M24 361 - 573 IPR000994
conserved_site Peptidase M24B, X-Pro dipeptidase/aminopeptidase P, conserved site 519 - 531 IPR001131
domain Peptidase M24, C-terminal domain 594 - 656 IPR032416
domain Aminopeptidase P 361 - 591 IPR033740

Functions

Description
EC Number 3.5.2.5 In cyclic amides
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

3 GO annotations of molecular function

Name Definition
allantoinase activity Catalysis of the reaction: allantoin + H2O = allantoate.
cobalt ion binding Binding to a cobalt ion (Co).
zinc ion binding Binding to a zinc ion (Zn).

2 GO annotations of biological process

Name Definition
allantoin catabolic process The chemical reactions and pathways resulting in the breakdown of allantoin, (2,5-dioxo-4-imidazolidinyl)urea.
purine nucleobase metabolic process The chemical reactions and pathways involving purine nucleobases, one of the two classes of nitrogen-containing ring compounds found in DNA and RNA, which include adenine and guanine.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSFDLIIKNG TVILENEARV VDIAVKDGKI AAIGQDLGDA KDVMDASGLV VSPGMVDAHT
70 80 90 100 110 120
HISEPGRSHW EGYETGTRAA AKGGITTMIE MPLNQLPATV DRASIELKFD AAKGKLTIDA
130 140 150 160 170 180
AQLGGLVSYN IDRLHELDEV GVVGFKCFVA TCGDRGIDND FRDVNDWQFF KGAQKLGELG
190 200 210 220 230 240
QPVLVHCENA LICDALGEEA KREGRVTAHD YVASRPVFTE VEAIRRVLYL AKVAGCRLHV
250 260 270 280 290 300
CHVSSPEGVE EVTRARQEGQ DVTCESCPHY FVLDTDQFEE IGTLAKCSPP IRDLENQKGM
310 320 330 340 350 360
WEKLFNGEID CLVSDHSPCP PEMKAGNIMK AWGGIAGLQS CMDVMFDEAV QKRGMSLPMF
370 380 390 400 410 420
GKLMATNAAD IFGLQQKGRI APGKDADFVF IQPNSSYVLT NDDLEYRHKV SPYVGRTIGA
430 440 450
RITKTILRGD VIYDIEQGFP VAPKGQFILK HQQ