Descriptions

Mfd has little motor activity in isolation but exhibits efficient oligonucleotide displacement activity when bound to a stalled transcription complex. Deletion of the C-terminal domain of Mfd increases the ATPase activity of the protein and allows efficient oligo displacement in the absence of RNAP, suggesting that an autoinhibitory element ensures the motor activity of Mfd is only functional within the correct macromolecular context.

Autoinhibitory domains (AIDs)

Target domain

49-985 (ATP-dependent DNA helicase); 467-545 (RNAP-interacting domain)

Relief mechanism

Partner binding

Assay

Deletion assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

15 structures for P30958

Entry ID Method Resolution Chain Position Source
2B2N X-ray 210 A A/B 1-333 PDB
2EYQ X-ray 320 A A/B 1-1148 PDB
3HJH X-ray 195 A A 1-470 PDB
4DFC X-ray 280 A A/C 127-213 PDB
6X26 EM 410 A A 1-1148 PDB
6X2F EM 400 A A 1-1148 PDB
6X2N EM 390 A A 1-1148 PDB
6X43 EM 360 A A 1-1148 PDB
6X4W EM 380 A A 1-1148 PDB
6X4Y EM 360 A A 1-1148 PDB
6X50 EM 330 A A 1-1148 PDB
6XEO EM 550 A A 1-1148 PDB
6YHZ NMR - A 472-547 PDB
7SSG EM 520 A A 1-1148 PDB
AF-P30958-F1 Predicted AlphaFoldDB

No variants for P30958

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P30958

No associated diseases with P30958

No regional properties for P30958

Type Name Position InterPro Accession
No domain, repeats, and functional sites for P30958

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
PANTHER Family PTHR47964 ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC
PANTHER Subfamily PTHR47964:SF1 ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC
PANTHER Protein Class DNA metabolism protein
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
DNA repair complex A protein complex involved in DNA repair processes including direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.

6 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
damaged DNA binding Binding to damaged DNA.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
DNA translocase activity Generation of movement along a single- or double-stranded DNA molecule, driven by ATP hydrolysis.
hydrolase activity Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
RNA polymerase core enzyme binding Binding to an RNA polymerase core enzyme, containing a specific subunit composition defined as the core enzyme.

6 GO annotations of biological process

Name Definition
DNA damage response Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism.
DNA repair The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
nucleotide-excision repair, preincision complex assembly The aggregation, arrangement and bonding together of proteins on DNA to form the multiprotein complex involved in damage recognition, DNA helix unwinding, and endonucleolytic cleavage at the site of DNA damage. This assembly occurs before the phosphodiester backbone of the damaged strand is cleaved 3' and 5' of the site of DNA damage.
regulation of DNA-templated transcription Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
transcription-coupled nucleotide-excision repair The nucleotide-excision repair process that carries out preferential repair of DNA lesions on the actively transcribed strand of the DNA duplex. In addition, the transcription-coupled nucleotide-excision repair pathway is required for the recognition and repair of a small subset of lesions that are not recognized by the global genome nucleotide excision repair pathway.
transcription-coupled nucleotide-excision repair, DNA damage recognition The identification of lesions on the actively transcribed strand of the DNA duplex as well as a small subset of lesions not recognized by the general nucleotide-excision repair pathway.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MPEQYRYTLP VKAGEQRLLG ELTGAACATL VAEIAERHAG PVVLIAPDMQ NALRLHDEIS
70 80 90 100 110 120
QFTDQMVMNL ADWETLPYDS FSPHQDIISS RLSTLYQLPT MQRGVLIVPV NTLMQRVCPH
130 140 150 160 170 180
SFLHGHALVM KKGQRLSRDA LRTQLDSAGY RHVDQVMEHG EYATRGALLD LFPMGSELPY
190 200 210 220 230 240
RLDFFDDEID SLRVFDVDSQ RTLEEVEAIN LLPAHEFPTD KAAIELFRSQ WRDTFEVKRD
250 260 270 280 290 300
PEHIYQQVSK GTLPAGIEYW QPLFFSEPLP PLFSYFPANT LLVNTGDLET SAERFQADTL
310 320 330 340 350 360
ARFENRGVDP MRPLLPPQSL WLRVDELFSE LKNWPRVQLK TEHLPTKAAN ANLGFQKLPD
370 380 390 400 410 420
LAVQAQQKAP LDALRKFLET FDGPVVFSVE SEGRREALGE LLARIKIAPQ RIMRLDEASD
430 440 450 460 470 480
RGRYLMIGAA EHGFVDTVRN LALICESDLL GERVARRRQD SRRTINPDTL IRNLAELHIG
490 500 510 520 530 540
QPVVHLEHGV GRYAGMTTLE AGGITGEYLM LTYANDAKLY VPVSSLHLIS RYAGGAEENA
550 560 570 580 590 600
PLHKLGGDAW SRARQKAAEK VRDVAAELLD IYAQRAAKEG FAFKHDREQY QLFCDSFPFE
610 620 630 640 650 660
TTPDQAQAIN AVLSDMCQPL AMDRLVCGDV GFGKTEVAMR AAFLAVDNHK QVAVLVPTTL
670 680 690 700 710 720
LAQQHYDNFR DRFANWPVRI EMISRFRSAK EQTQILAEVA EGKIDILIGT HKLLQSDVKF
730 740 750 760 770 780
KDLGLLIVDE EHRFGVRHKE RIKAMRANVD ILTLTATPIP RTLNMAMSGM RDLSIIATPP
790 800 810 820 830 840
ARRLAVKTFV REYDSMVVRE AILREILRGG QVYYLYNDVE NIQKAAERLA ELVPEARIAI
850 860 870 880 890 900
GHGQMREREL ERVMNDFHHQ RFNVLVCTTI IETGIDIPTA NTIIIERADH FGLAQLHQLR
910 920 930 940 950 960
GRVGRSHHQA YAWLLTPHPK AMTTDAQKRL EAIASLEDLG AGFALATHDL EIRGAGELLG
970 980 990 1000 1010 1020
EEQSGSMETI GFSLYMELLE NAVDALKAGR EPSLEDLTSQ QTEVELRMPS LLPDDFIPDV
1030 1040 1050 1060 1070 1080
NTRLSFYKRI ASAKTENELE EIKVELIDRF GLLPDPARTL LDIARLRQQA QKLGIRKLEG
1090 1100 1110 1120 1130 1140
NEKGGVIEFA EKNHVNPAWL IGLLQKQPQH YRLDGPTRLK FIQDLSERKT RIEWVRQFMR
ELEENAIA