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 Q9RVM9

Entry ID Method Resolution Chain Position Source
AF-Q9RVM9-F1 Predicted AlphaFoldDB

No variants for Q9RVM9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9RVM9

No associated diseases with Q9RVM9

2 regional properties for Q9RVM9

Type Name Position InterPro Accession
conserved_site Mrp, conserved site 197 - 213 IPR000808
domain MIP18 family-like 3 - 74 IPR002744

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

5 GO annotations of molecular function

Name Definition
4 iron, 4 sulfur cluster binding Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
ATP-dependent FeS chaperone activity Binding to and delivering metal ions to a target protein, driven by ATP hydrolysis.
metal ion binding Binding to a metal ion.

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
MNDALLRALS TVNDPELHRD LVSLGMIERA ELSGDVAQVK VNLTTPACPL KGQIELDVRS
70 80 90 100 110 120
ALLQVPGVRD VQIEFGAMVR AATQPALPGV KHVVLVGSGK GGVGKSSVAV NLAASLARDG
130 140 150 160 170 180
ARVGLLDADV YGPSVAHMLG QGQARVTANE DRKMRPIEAH GVRFISMANL SPAGQALVWR
190 200 210 220 230 240
GPMLHSAIQQ FLKDSAWGEL DYLIVDLPPG TGDVQLSLTQ TVQVTGAVIV TTPQDVALID
250 260 270 280 290 300
AARAIDMFRK ASVPVLGVVE NMSYFVAPDT GLTYDIFGRG GSRKLGEQYP LLGEIPLDVE
310 320 330 340
VRKDADAGAP AILAHPESVA AQALRAVART LAGQISVRTL SELPEQLPVL