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 Q9FYC2

Entry ID Method Resolution Chain Position Source
AF-Q9FYC2-F1 Predicted AlphaFoldDB

73 variants for Q9FYC2

Variant ID(s) Position Change Description Diseaes Association Provenance
tmp_3_16383895_T_C 13 I>T No 1000Genomes
ENSVATH12466654 19 K>T No 1000Genomes
ENSVATH12466665 25 S>F No 1000Genomes
ENSVATH06218116 26 P>H No 1000Genomes
ENSVATH06218117 29 K>N No 1000Genomes
ENSVATH12466667 41 S>P No 1000Genomes
ENSVATH00398702 45 H>N No 1000Genomes
tmp_3_16383996_C_T 47 P>S No 1000Genomes
ENSVATH06218118 49 R>H No 1000Genomes
ENSVATH06218119 52 A>P No 1000Genomes
tmp_3_16384024_T_C 56 V>A No 1000Genomes
ENSVATH02424653 56 V>I No 1000Genomes
tmp_3_16384038_T_A 61 S>T No 1000Genomes
ENSVATH00398703 62 T>A No 1000Genomes
tmp_3_16384049_G_C 64 E>D No 1000Genomes
ENSVATH06218121 65 K>N No 1000Genomes
ENSVATH02424654 69 E>D No 1000Genomes
ENSVATH06218122 70 E>G No 1000Genomes
tmp_3_16384092_G_T 79 G>W No 1000Genomes
ENSVATH06218124 85 R>K No 1000Genomes
ENSVATH14357609 94 V>L No 1000Genomes
ENSVATH12466668 109 G>A No 1000Genomes
ENSVATH14357610 114 L>I No 1000Genomes
ENSVATH14357611 137 L>F No 1000Genomes
ENSVATH02424676 158 G>S No 1000Genomes
ENSVATH06218140 160 C>Y No 1000Genomes
tmp_3_16384671_A_G 171 T>A No 1000Genomes
tmp_3_16384672_C_A 171 T>N No 1000Genomes
ENSVATH12466745 176 A>T No 1000Genomes
ENSVATH12466746 187 I>M No 1000Genomes
tmp_3_16384738_T_C 193 V>A No 1000Genomes
ENSVATH02424679 199 F>L No 1000Genomes
ENSVATH12466747 201 W>L No 1000Genomes
ENSVATH12466748 203 D>E No 1000Genomes
tmp_3_16384767_G_A 203 D>N No 1000Genomes
ENSVATH06218149 226 E>Q No 1000Genomes
ENSVATH12466769 229 T>M No 1000Genomes
ENSVATH06218151 271 P>A No 1000Genomes
tmp_3_16385160_A_C 273 K>T No 1000Genomes
ENSVATH06218152 283 Q>L No 1000Genomes
ENSVATH12466788 291 R>K No 1000Genomes
tmp_3_16385220_C_T 293 T>I No 1000Genomes
tmp_3_16385349_A_C 308 L>F No 1000Genomes
ENSVATH06218156 310 A>V No 1000Genomes
tmp_3_16385371_G_A 316 G>S No 1000Genomes
tmp_3_16385375_A_G 317 N>S No 1000Genomes
ENSVATH06218157 318 Q>K No 1000Genomes
ENSVATH12466829 348 Q>P No 1000Genomes
tmp_3_16385641_G_A 382 G>R No 1000Genomes
ENSVATH02424712 389 A>S No 1000Genomes
ENSVATH02424713 391 S>A No 1000Genomes
ENSVATH00398720 396 D>G No 1000Genomes
ENSVATH12466833 398 D>N No 1000Genomes
ENSVATH06218159 402 Q>L No 1000Genomes
ENSVATH02424714 438 T>N No 1000Genomes
ENSVATH06218165 439 P>L No 1000Genomes
ENSVATH06218165 439 P>R No 1000Genomes
ENSVATH06218164 439 P>T No 1000Genomes
ENSVATH06218166 440 S>T No 1000Genomes
tmp_3_16385837_C_T 447 T>I No 1000Genomes
tmp_3_16385839_G_A 448 V>I No 1000Genomes
ENSVATH00398725 470 G>E No 1000Genomes
tmp_3_16386043_G_A 485 A>T No 1000Genomes
ENSVATH06218171 492 T>R No 1000Genomes
tmp_3_16386067_G_A 493 A>T No 1000Genomes
ENSVATH12466925 495 V>L No 1000Genomes
ENSVATH12466926 507 G>S No 1000Genomes
ENSVATH14357630 508 L>I No 1000Genomes
ENSVATH02424718 511 I>L No 1000Genomes
ENSVATH02424718 511 I>V No 1000Genomes
ENSVATH02424719 518 A>T No 1000Genomes
ENSVATH12466927 520 H>Y No 1000Genomes
ENSVATH12466928 522 Q>K No 1000Genomes

No associated diseases with Q9FYC2

3 regional properties for Q9FYC2

Type Name Position InterPro Accession
conserved_site Calreticulin/calnexin, conserved site 108 - 123 IPR018124-1
conserved_site Calreticulin/calnexin, conserved site 140 - 148 IPR018124-2
conserved_site Calreticulin/calnexin, conserved site 253 - 265 IPR018124-3

Functions

Description
EC Number 1.14.15.17 With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen
Subcellular Localization
  • Plastid, chloroplast thylakoid membrane
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

7 GO annotations of cellular component

Name Definition
chloroplast A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma.
chloroplast envelope The double lipid bilayer enclosing the chloroplast and separating its contents from the rest of the cytoplasm; includes the intermembrane space.
chloroplast inner membrane The inner, i.e. lumen-facing, lipid bilayer of the chloroplast envelope; also faces the chloroplast stroma.
chloroplast thylakoid Sac-like membranous structures (cisternae) in a chloroplast combined into stacks (grana) and present singly in the stroma (stroma thylakoids or frets) as interconnections between grana. An example of this component is found in Arabidopsis thaliana.
chloroplast thylakoid membrane The pigmented membrane of a chloroplast thylakoid. An example of this component is found in Arabidopsis thaliana.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

6 GO annotations of molecular function

Name Definition
2 iron, 2 sulfur cluster binding Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands.
chlorophyllide a oxygenase [overall] activity Catalysis of the reactions: chlorophyllide a + O2 + NADPH + H+ = 7-hydroxychlorophyllide a + H2O + NADP+; and 7-hydroxychlorophyllide a + O2 + NADPH + H+ = chlorophyllide b + 2 H2O + NADP+.
iron-sulfur cluster binding Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.
metal ion binding Binding to a metal ion.
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.
pheophorbide a oxygenase activity Catalysis of the reaction: pheophorbide a + reduced ferredoxin + 2 O2 = red chlorophyll catabolite + oxidized ferredoxin + H2O.

5 GO annotations of biological process

Name Definition
cell death Any biological process that results in permanent cessation of all vital functions of a cell. A cell should be considered dead when any one of the following molecular or morphological criteria is met: (1) the cell has lost the integrity of its plasma membrane; (2) the cell, including its nucleus, has undergone complete fragmentation into discrete bodies (frequently referred to as apoptotic bodies). The cell corpse (or its fragments) may be engulfed by an adjacent cell in vivo, but engulfment of whole cells should not be considered a strict criteria to define cell death as, under some circumstances, live engulfed cells can be released from phagosomes (see PMID:18045538).
chlorophyll catabolic process The chemical reactions and pathways resulting in the breakdown of chlorophyll, any compound of magnesium complexed in a porphyrin (tetrapyrrole) ring and which functions as a photosynthetic pigment, into less complex products.
defense response to bacterium Reactions triggered in response to the presence of a bacterium that act to protect the cell or organism.
flower development The process whose specific outcome is the progression of the flower over time, from its formation to the mature structure. The flower is the reproductive structure in a plant, and its development begins with the transition of the vegetative or inflorescence meristem into a floral meristem.
fruit development The process whose specific outcome is the progression of the fruit over time, from its formation to the mature structure. The fruit is a reproductive body of a seed plant.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9MBA1 CAO Chlorophyllide a oxygenase, chloroplastic Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MSVVLLSSTS ATITKSQSKK IPFLSPTTKF PLKVSISPSR SKLFHNPLRV AAPPSVPTSD
70 80 90 100 110 120
STEEKRIEEE YGGDKEEEGS EFKWRDHWYP VSLVEDLDPN VPTPFQLLGR DLVLWFDRND
130 140 150 160 170 180
QKWAAFDDLC PHRLAPLSEG RLDENGHLQC SYHGWSFGGC GSCTRIPQAA TSGPEARAVK
190 200 210 220 230 240
SPRACAIKFP TMVSQGLLFV WPDENGWDRA NSIEPPRLPD DFDKPEFSTV TIQRDLFYGY
250 260 270 280 290 300
DTLMENVSDP SHIDFAHHKV TGRRDRAKPL PFKVESSGPW GFQGANDDSP RITAKFVAPC
310 320 330 340 350 360
YSMNKIELDA KLPIVGNQKW VIWICSFNIP MAPGKTRSIV CSARNFFQFS VPGPAWWQVV
370 380 390 400 410 420
PRWYEHWTSN LVYDGDMIVL QGQEKVFLAK SMESPDYDVN KQYTKLTFTP TQADRFVLAF
430 440 450 460 470 480
RNWLRRHGKS QPEWFGSTPS NQPLPSTVLT KRQMLDRFDQ HTQVCSSCKG AYNSFQILKK
490 500 510 520 530
FLVGATVFWA ATAGVPSDVQ IRLVLAGLSL ISAASAYALH EQEKNFVFRD YVHSEIE