Q5ZSQ3

PR
Gene name
drrA (sidM, lpg2464)
Protein name
Multifunctional virulence effector protein DrrA
Names
Defects in Rab1 recruitment protein A
Species
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
KEGG Pathway
lpn:lpg2464
EC number
2.7.7.108: Nucleotidyltransferases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-75 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

8 structures for Q5ZSQ3

Entry ID Method Resolution Chain Position Source
2WWX X-ray 150 A B 317-533 PDB
3JZ9 X-ray 180 A A 340-533 PDB
3JZA X-ray 180 A B 340-533 PDB
3L0I X-ray 285 A A/C 193-550 PDB
3L0M X-ray 345 A A/B 317-647 PDB
3N6O X-ray 250 A A/B 340-647 PDB
4MXP X-ray 183 A A 330-647 PDB
AF-Q5ZSQ3-F1 Predicted AlphaFoldDB

No variants for Q5ZSQ3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5ZSQ3

No associated diseases with Q5ZSQ3

2 regional properties for Q5ZSQ3

Type Name Position InterPro Accession
domain DrrA phosphatidylinositol 4-phosphate binding domain 539 - 640 IPR028057
domain DrrA guanine nucleotide-exchange factor domain 340 - 525 IPR033784

Functions

Description
EC Number 2.7.7.108 Nucleotidyltransferases
Subcellular Localization
  • Secreted
  • Host cytoplasmic vesicle membrane ; Peripheral membrane protein
  • Translocated into the host cell via the type IV secretion system (T4SS)
  • Membrane association is mediated by PtdIns(4)P-binding
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
extracellular region The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
host cell cytoplasmic vesicle A vesicle formed of membrane or protein, found in the cytoplasm of a host cell.
host cell cytoplasmic vesicle membrane The lipid bilayer surrounding a host cell cytoplasmic vesicle.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.

6 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
guanyl-nucleotide exchange factor activity Stimulates the exchange of GDP to GTP on a signaling GTPase, changing its conformation to its active form. Guanine nucleotide exchange factors (GEFs) act by stimulating the release of guanosine diphosphate (GDP) to allow binding of guanosine triphosphate (GTP), which is more abundant in the cell under normal cellular physiological conditions.
phosphatidylinositol-4-phosphate binding Binding to phosphatidylinositol-4-phosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 4' position.
protein adenylyltransferase activity Catalysis of the reaction: ATP + protein = diphosphate + adenylyl-protein; mediates the addition of an adenylyl (adenosine 5'-monophosphate; AMP group) to specific residues of target proteins.
protein guanylyltransferase activity Catalysis of the reaction: GTP + protein = diphosphate + guanylyl-protein; mediates the addition of an guanylyl (guanosine 5'-monophosphate; GMP group) to specific residues of target proteins.
small GTPase binding Binding to a small monomeric GTPase.

4 GO annotations of biological process

Name Definition
protein adenylylation The addition of an adenylyl group (adenosine 5'-monophosphate; AMP) to a protein amino acid.
protein guanylylation The addition of phospho-guanosine to a protein amino acid.
protein targeting to membrane The process of directing proteins towards a membrane, usually using signals contained within the protein.
regulation of GTPase activity Any process that modulates the rate of GTP hydrolysis by a GTPase.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSIMGRIKMS VNEEQFGSLY SDERDKPLLS PTAQKKFEEY QNKLANLSKI IRENEGNEVS
70 80 90 100 110 120
PWQEWENGLR QIYKEMIYDA FDALGVEMPK DMEVHFAGSL AKAQATEYSD LDAFVIVKND
130 140 150 160 170 180
EDIKKVKPVF DALNNLCQRI FTASNQIYPD PIGINPSRLI GTPDDLFGML KDGMVADVEA
190 200 210 220 230 240
TAMSILTSKP VLPRYELGEE LRDKIKQEPS FSNMVSAKKF YNKAIKDFTA PKEGAEVVSV
250 260 270 280 290 300
KTHIMRPIDF MLMGLREEFN LYSEDGAHLS APGTIRLLRE KNLLPEEQIA RIESVYNQAM
310 320 330 340 350 360
SKRFELHAEH KKEHDEMPYS DAKAMLDEVA KIRELGVQRV TRIENLENAK KLWDNANSML
370 380 390 400 410 420
EKGNISGYLK AANELHKFMK EKNLKEDDLR PELSDKTISP KGYAILQSLW GAASDYSRAA
430 440 450 460 470 480
ATLTESTVEP GLVSAVNKMS AFFMDCKLSP NERATPDPDF KVGKSKILVG IMQFIKDVAD
490 500 510 520 530 540
PTSKIWMHNT KALMNHKIAA IQKLERSNNV NDETLESVLS SKGENLSEYL SYKYATKDEG
550 560 570 580 590 600
REHRYTASTE NFKNVKEKYQ QMRGDALKTE ILADFKDKLA EATDEQSLKQ IVAELKSKDE
610 620 630 640
YRILAKGQGL TTQLLGLKTS SVSSFEKMVE ETRESIKSQE RQTIKIK