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 Q6CQA1

Entry ID Method Resolution Chain Position Source
AF-Q6CQA1-F1 Predicted AlphaFoldDB

No variants for Q6CQA1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6CQA1

No associated diseases with Q6CQA1

3 regional properties for Q6CQA1

Type Name Position InterPro Accession
domain Formyl transferase, N-terminal 118 - 220 IPR002376
domain Formyl transferase, C-terminal 243 - 349 IPR005793
domain Methionyl-tRNA formyltransferase, N-terminal domain 48 - 244 IPR041711

Functions

Description
EC Number 3.6.4.13 Acting on ATP; involved in cellular and subcellular movement
Subcellular Localization
  • Mitochondrion matrix
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
mitochondrial matrix The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.

4 GO annotations of molecular function

Name Definition
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.
RNA helicase activity Unwinding of an RNA helix, driven by ATP hydrolysis.
RNA strand annealing activity An activity that facilitates the formation of a complementary double-stranded RNA molecule.

7 GO annotations of biological process

Name Definition
Group I intron splicing The splicing of Group I introns. This occurs by a ribozymic mechanism where the intron sequence forms a distinct 3D structure, characteristic of Group I introns and involved in determining the locations of the splice sites (there do not appear to be consensus splice site sequences) as well as having a role in catalyzing the splicing reactions, though protein factors are also required in vivo. Splicing occurs by a series of two transesterification reactions, generally with exogenous guanosine as the initiating nucleophile. The intron is excised as a linear piece (though it may subsequently circularize).
Group II intron splicing The splicing of Group II introns. This occurs by a ribozymic mechanism where the intron sequence forms a distinct 3D structure, characteristic of Group II introns and containing splice site consensus sequences, that is involved in catalyzing the splicing reactions, though protein factors are also required in vivo. Splicing occurs by a series of two transesterification reactions (mechanistically similar to those for splicing of nuclear mRNAs) initiated by a bulged adenosine residue within the intron sequence as the initiating nucleophile. The intron is excised as a lariat.
mitochondrial RNA processing The conversion of a primary RNA molecule transcribed from a mitochondrial genome into one or more mature RNA molecules; occurs in the mitochondrion.
mRNA processing Any process involved in the conversion of a primary mRNA transcript into one or more mature mRNA(s) prior to translation into polypeptide.
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.
RNA folding The process of assisting in the covalent and noncovalent assembly of single or multimeric RNAs into the correct tertiary structure.
transcription elongation by mitochondrial RNA polymerase The extension of an RNA molecule after transcription initiation and promoter clearance at mitochondrial promoter by the addition of ribonucleotides catalyzed by a mitchondrial RNA polymerase.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLVLQRIPKR ALQFNGVTGT VCSTRLFHHA FNLNLQQSFV PSEERRYRNS NRGFTRGSDS
70 80 90 100 110 120
NSNNKYRNSS YDDNRSRSNY GGDKRNNRNN NNYGNNRNNG SRRRYQDENS DIEVFKSKSF
130 140 150 160 170 180
NVTTLNPESF HEQVTIDSLL EESLLDANVH KAISAMKFES LTPVQQRTIK PILTTENDVV
190 200 210 220 230 240
AKAKTGTGKT LAFLAPLFQH LISTKLQNPL AVKAVIVTPT RDLAIQIASE VKKLQQCNPS
250 260 270 280 290 300
LKSYRSLTLI GGTNLDKSLK DLHTLNPNII VGTPGRINDI LDRVGAKYFK DVDFKVLDEA
310 320 330 340 350 360
DTLLQIGFQT ELSLISRKLN EFNTQGEEHI RTLLFSATMD HNVQELAATI MNKKDCLFID
370 380 390 400 410 420
TVDKNDSEAH DSIDQKLVIT KSFAESMVAL IQSIESELLQ KKNFKAILFL PTVKFVDFFS
430 440 450 460 470 480
ETLSESLTKR IDIIKFHGKI DQKKRTKLVD RFKKTNHGIF VCTDVGARGM HFPSVEHVYQ
490 500 510 520 530 540
LCVPTSLPNY IHRIGRTARA GESGAATIFL FREELKFVDE LRRDTNVVIK NQEDYLNQDK
550 560 570 580 590 600
ENFDMISSII TNNPDFPEAL KSIIGFYKGV QNEYRLNYKV AQNVLRSFSE LHSDSSMLLR
610 620 630 640 650 660
FRPSEINNFF SNRDMRFVSD LIDVKNPHSF GKDREFDDED RYTSRSQNNY KSKQSSKSNR
670 680
FEGRNDYSNS RRSHANQKRN FTFDD