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 C1CR55

Entry ID Method Resolution Chain Position Source
AF-C1CR55-F1 Predicted AlphaFoldDB

No variants for C1CR55

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for C1CR55

No associated diseases with C1CR55

5 regional properties for C1CR55

Type Name Position InterPro Accession
domain GMP synthase, C-terminal 211 - 525 IPR001674
domain GMP synthase, glutamine amidotransferase 10 - 203 IPR004739
domain Glutamine amidotransferase 11 - 199 IPR017926
domain NAD/GMP synthase 217 - 290 IPR022310
domain GMP synthetase ATP pyrophosphatase domain 207 - 400 IPR025777

Functions

Description
EC Number 1.7.1.7 With NAD(+) or NADP(+) as acceptor
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
GMP reductase complex An oxidoreductase complex which is capable of GMP reductase activity. It catalyses the irreversible reaction: GMP + 2 H(+) + NADPH => IMP + NADP(+) + NH(4)(+).

1 GO annotations of molecular function

Name Definition
GMP reductase activity Catalysis of the reaction: IMP + NADP(+) + NH(4)(+) = GMP + 2 H(+) + NADPH.

1 GO annotations of biological process

Name Definition
purine nucleotide metabolic process The chemical reactions and pathways involving a purine nucleotide, a compound consisting of nucleoside (a purine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLNEFPIFDY EDIQLIPNKC VIKSRAEADT SVTLGNHTFK LPVVPANMQT ILDENVAEQL
70 80 90 100 110 120
AKGGYFYIMH RFDEAGRIPF IKRMHDQGLI ASISVGVKDY EYDFVRQLKT DAPEYITIDI
130 140 150 160 170 180
AHGHADSVIS MIQHIKKELP DTFVIAGNVG TPEAVRELEN AGADATKVGI GPGKVCITKV
190 200 210 220 230 240
KTGFGTGGWQ LAALRWCAKA ARKPIIADGG IRTHGDIAKS IRFGASMIMI GSLFAGHIES
250 260 270 280 290 300
PGKTIEVDGE QFKEYYGSAS QYQKGAYKNV EGKRILLPAK GHLQDTLTEM EQDLQSAISY
310 320
AGGRQVADLK HVDYVIVKNS IWNGDASH