Q9I7H9

PR
Gene name
sud1 (CG18761, CG31120, CG44254)
Protein name
Prolyl 3-hydroxylase sudestada1
Names
2-oxoglutarate and iron-dependent oxygenase domain-containing protein 1 homolog, uS12 prolyl 3-hydroxylase
Species
Drosophila melanogaster (Fruit fly)
KEGG Pathway
dme:Dmel_CG44254
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-56 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q9I7H9

Entry ID Method Resolution Chain Position Source
AF-Q9I7H9-F1 Predicted AlphaFoldDB

No variants for Q9I7H9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9I7H9

No associated diseases with Q9I7H9

4 regional properties for Q9I7H9

Type Name Position InterPro Accession
domain Heat shock protein DnaJ, cysteine-rich domain 130 - 214 IPR001305
domain DnaJ domain 7 - 81 IPR001623
domain Chaperone DnaJ, C-terminal 117 - 338 IPR002939
conserved_site DnaJ domain, conserved site 47 - 66 IPR018253

Functions

Description
EC Number
Subcellular Localization
  • Nucleus
  • Cytoplasm
  • Localizes predominantly to the nucleus
  • Present at lower levels are also detected in the cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

3 GO annotations of molecular function

Name Definition
iron ion binding Binding to an iron (Fe) ion.
L-ascorbic acid binding Binding to L-ascorbic acid, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate; L-ascorbic acid is vitamin C and has co-factor and anti-oxidant activities in many species.
peptidyl-proline dioxygenase activity Catalysis of the reaction: peptidyl L-proline + 2-oxoglutarate + O2 = peptidyl hydroxy-L-proline + succinate + CO2.

4 GO annotations of biological process

Name Definition
peptidyl-proline hydroxylation The hydroxylation of peptidyl-proline to form peptidyl-hydroxyproline.
protein hydroxylation The addition of a hydroxy group to a protein amino acid.
regulation of translation Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA.
regulation of translational termination Any process that modulates the frequency, rate or extent of translational termination.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
METSSSSPVK PRRKDKDEDG RAEQEDSADQ VGEPHRKLLR LGDILETNEV LLNEAYQQPE
70 80 90 100 110 120
LTKWLQTAWT EEKSQGTKET QTGAQVFSDP FQICLLPGML EKGQSQALVA EIIQKVQWSR
130 140 150 160 170 180
KQMDLYEFYQ SADLSNMPAC RLLTNFLQVL RKQVRPWLEK VTNLKLDYVS ASCSMYTCGD
190 200 210 220 230 240
YLLVHDDLLK DRQVAFIYYL SPWEGAEEWT DEQGGCLEIF GSDDQCFPQF PVQRKIAPKD
250 260 270 280 290 300
NQFAFFKVGS RSFHQVGEVT TFDYPRLTIN GWFHGDTNEA FVADSLRAFP RLNYLQPDGL
310 320 330 340 350 360
NRPPLGLFLN NVYLKGATRR SIQKRIEENS EICLYEFFKR EKFELARSQL LADSDTLKWR
370 380 390 400 410 420
RQGPANAHNY EVLDLTTARG TILELLQLFR SHAMFDLLRD FTDLDLAGTD AESPTCSVEL
430 440 450 460 470 480
QRWSHGNYTV LGDGLTSEEN TLDLVYYLNA AEGAAVITYL APDAEMPTAK APTDGRRSDY
490 500 510 520 530
DDEEEDDSVL LTITPVDNAL NIVYRCEGTT KFTKYVSRNT PLEKGPVFVI SCSYKE