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 Q5AD27

Entry ID Method Resolution Chain Position Source
AF-Q5AD27-F1 Predicted AlphaFoldDB

No variants for Q5AD27

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5AD27

No associated diseases with Q5AD27

14 regional properties for Q5AD27

Type Name Position InterPro Accession
domain Flavodoxin-like 6 - 19 IPR001094-1
domain Flavodoxin-like 56 - 67 IPR001094-2
domain Flavodoxin-like 90 - 100 IPR001094-3
domain Flavodoxin-like 114 - 133 IPR001094-4
domain Oxidoreductase FAD/NAD(P)-binding 447 - 548 IPR001433
domain Flavoprotein pyridine nucleotide cytochrome reductase 236 - 246 IPR001709-1
domain Flavoprotein pyridine nucleotide cytochrome reductase 380 - 387 IPR001709-2
domain Flavoprotein pyridine nucleotide cytochrome reductase 412 - 421 IPR001709-3
domain Flavoprotein pyridine nucleotide cytochrome reductase 446 - 465 IPR001709-4
domain Flavoprotein pyridine nucleotide cytochrome reductase 471 - 480 IPR001709-5
domain Flavoprotein pyridine nucleotide cytochrome reductase 538 - 546 IPR001709-6
domain Sulfite reductase [NADPH] flavoprotein alpha-component-like, FAD-binding 209 - 417 IPR003097
domain Flavodoxin/nitric oxide synthase 5 - 151 IPR008254
domain FAD-binding domain, ferredoxin reductase-type 202 - 439 IPR017927

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Mitochondrion
  • Relocalizes to mitochondria after H(2)O(2) exposure
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.

5 GO annotations of molecular function

Name Definition
flavin adenine dinucleotide binding Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
FMN binding Binding to flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
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.
NADPH-hemoprotein reductase activity Catalysis of the reaction: NADPH + H+ + n oxidized hemoprotein = NADP+ + n reduced hemoprotein.
oxidoreductase activity Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.

1 GO annotations of biological process

Name Definition
iron-sulfur cluster assembly The incorporation of iron and exogenous sulfur into a metallo-sulfur cluster.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTGEITILYG SETGNAEEYA KYLKQRLRSY NLKPINLASL DDYPLKRLVT HTSYLIIICS
70 80 90 100 110 120
TTGQGEIPRN GKKFMKFILK KKLPSDLFQH LQLTTFGVGD SSYVKYNYAI KKIHTRLMQL
130 140 150 160 170 180
GCQLLSPRCE ADEISPEGVD GYYIEWEAEL IAALLNKFPS ASKISSEAVP MPEYRISVSK
190 200 210 220 230 240
SDTTIDPKEV IDNPIVSRLG KDGLKLGTVL ENNRLTSSNH FQDVRDFKFS SNGLNYLPGD
250 260 270 280 290 300
TVSLFPCNFD EDVDALLQSQ PQWLKIADKP LNLKNFPHLE GGFADILTLR TLFKYHLDIM
310 320 330 340 350 360
SIPRRSFFAL LWHFVDPSTE DGEREQEKLK EFGSLDEPEE LYDYANRPRR SILETLLEFE
370 380 390 400 410 420
NNLTIPVSYI LDLFPLIRPR MFSIASCPSS KEVELVVAIV EYKTIIRKIR RGVCTRWLKN
430 440 450 460 470 480
LKPGDQFLFS IQRSSFKYKD DNSPIIMVAP GTGIAPMKSL IDEVIQNNSK QELYLFFGCR
490 500 510 520 530 540
FKEKDNLIES FWHGNENQNL HLVSAYSRDS NSKYRYVQDA LFAHSELIGK LLIEQNAKVF
550 560 570 580
VCGSSGKMPR EVKITFVEIV KKFTGMDEGD AQKYIIGLED NGRYKEDAW