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 Q8ZWK7

Entry ID Method Resolution Chain Position Source
AF-Q8ZWK7-F1 Predicted AlphaFoldDB

No variants for Q8ZWK7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8ZWK7

No associated diseases with Q8ZWK7

15 regional properties for Q8ZWK7

Type Name Position InterPro Accession
domain Immunodeficiency lentiviral matrix, N-terminal 2 - 127 IPR000071
domain Reverse transcriptase domain 631 - 821 IPR000477
domain Integrase, C-terminal, retroviral 1370 - 1417 IPR001037
domain Integrase, catalytic core 1201 - 1351 IPR001584
domain Zinc finger, CCHC-type 392 - 408 IPR001878-1
domain Zinc finger, CCHC-type 413 - 429 IPR001878-2
active_site Aspartic peptidase, active site 510 - 521 IPR001969
domain Peptidase A2A, retrovirus, catalytic 508 - 577 IPR001995
domain Ribonuclease H domain 1021 - 1144 IPR002156
domain Integrase, N-terminal zinc-binding domain 1150 - 1191 IPR003308
domain Reverse transcriptase connection 905 - 1006 IPR010659
domain Reverse transcriptase thumb 829 - 890 IPR010661
domain Retropepsins 494 - 585 IPR018061
domain Retropepsin-like catalytic domain 499 - 579 IPR034170
domain Retroviral nucleocapsid Gag protein p24, C-terminal domain 277 - 349 IPR045345

Functions

Description
EC Number 1.2.1.59 With NAD(+) or NADP(+) as acceptor
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

5 GO annotations of molecular function

Name Definition
4-hydroxy-tetrahydrodipicolinate reductase Catalysis of the reaction: (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+.
glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity Catalysis of the reaction: D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH + H+.
glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity Catalysis of the reaction: phosphate + NADP+ + glyceraldehyde-3-phosphate = NADPH + 3-phospho-D-glyceroyl-phosphate.
NAD binding Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
NADP binding Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.

2 GO annotations of biological process

Name Definition
glycolytic process The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules.
lysine biosynthetic process via diaminopimelate The chemical reactions and pathways resulting in the formation of lysine, via the intermediate diaminopimelate.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MIRVGIVGFG TIGKRIADAV AAQDDMKISG VLKVTPDYEA KIAVERGFKV YTLPDGLDKF
70 80 90 100 110 120
KKAGIEPAGT IEDLIEASDI IVDASPEDVG RENKEKYYIK FNKPVIFQGG EDADVAEVSF
130 140 150 160 170 180
NALANFEEAA GRRYVRVVSC NTTGITRVLS SLMLNGIKIK KARIFIARRG ADPKEHKKGP
190 200 210 220 230 240
INDVVPNPVT VPSHHGPDAQ TVLKNIDIVT MAVAVPVTIM HMHMAYLELD GSYTKEAVIE
250 260 270 280 290 300
AFAKTPRIFL ADVGAGFQSL AQIIEYARDL GRPRGDFPEV AVFRDSVTVN GNELYLMYGV
310 320 330 340
HQESIVVPEN IDAVRAVLGL APKWRSIEKT DKSLKLITEG KRYG