Family Search for PF07956 (DUF1690)
PF07956 hits 5 sequences in PaperBLAST's database above the trusted cutoff. Showing all hits. Or show only hits to curated sequences or try another family.
G0S140 MICOS complex subunit mic19 from Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
Aligns to 16:154 / 167 (83.2%), covers 100.0% of PF07956, 152.5 bits
MIC19_EMENI / Q5ASP0 MICOS complex subunit mic19 from Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) (see paper)
AN8690 UPF0726 protein AN8690 from Emericella nidulans (see paper)
Aligns to 18:196 / 209 (85.6%), covers 100.0% of PF07956, 130.0 bits
- function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane (By similarity). Involved in osmoadaptation.
subunit: Component of the mitochondrial contact site and cristae organizing system (MICOS) complex. - CharProtDB Description: ORF that was absent from the original release of version 4 of the A. nidulans annotation, but present in a previous version; reinstated into version 4 in AspGD as of July 2009; Source:AspGD
MIC19_YEAST / P43594 MICOS complex subunit MIC19; Altered inheritance of mitochondria protein 13, mitochondrial; Mitochondrial contact site complex 19 kDa subunit from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 6 papers)
NP_116666 Mic19p from Saccharomyces cerevisiae S288C
YFR011C Aim13p from Saccharomyces cerevisiae
Aligns to 18:168 / 170 (88.8%), covers 100.0% of PF07956, 126.6 bits
- function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
subunit: Component of the mitochondrial contact site and cristae organizing system (MICOS) complex, composed of at least MIC10, MIC12, MIC19, MIC26, MIC27 and MIC60. This complex was also known under the names MINOS or MitOS complex.
disruption phenotype: Increases frequency of mitochondrial genome loss. Partially altered shape of the mitochondrial network with condensed, fragmented mitochondria accumulating at the periphery of cells. 20-40% of mitochondria exhibit an increased inner membrane surface and stacks of lamellar cristae disconnected from the inner boundary membrane. - The Oxidation Status of Mic19 Regulates MICOS Assembly.
Sakowska, Molecular and cellular biology 2015 - GeneRIF: The findings suggest that Mic19 is a redox-dependent regulator of mitochondrial contact site and crista organizing system complex function.
- Pathways shaping the mitochondrial inner membrane
Klecker, Open biology 2021 - “...coupling of Mic10 and Mic60 subcomplexes [ 46 48 , 52 ] Mic19 (Aim13; Mcs19; Yfr011c) MIC19 (CHCHD3; MINOS3) and MIC25 (CHCHD6) assembly and regulation of Mic60 subcomplex [ 46 48 , 53 55 ] Mic26 (Mcs29; Mio27; Mos2; Ygr235c) MIC26 (APOO; MIC23) destabilization of Mic10...”
- Uniform nomenclature for the mitochondrial contact site and cristae organizing system
Pfanner, The Journal of cell biology 2014 - “...et al., 2011 ; Varabyova et al., 2013 Mic19 Aim13, Mcs19, CHCH-3, CHCHD3, and MINOS3 YFR011C Xie et al., 2007 ; Hess et al., 2009 ; Darshi et al., 2011 ; Head et al., 2011 ; Alkhaja et al., 2012 ; Ott et al., 2012 ;...”
- Role of the AAA protease Yme1 in folding of proteins in the intermembrane space of mitochondria
Schreiner, Molecular biology of the cell 2012 - “...RPO41 Matrix RNA polymerase; enhancing DNA bending and melting to facilitate preinitiation open-complex formation 11 YFR011C AIM13 IMS Subunit of mitochondrial IM organizing system (MitOS/MICOS/MINOS), role in maintenance of cristae junctions and IM architecture 12 YGL057C GEP7 IM 1 Unknown function; null mutant exhibits respiratory growth...”
- The mitochondrial contact site complex, a determinant of mitochondrial architecture
Harner, The EMBO journal 2011 - “...are Mcs29 (Ygr235c), Mcs27 (Ynl100w, AIM37), Mcs19 (Yfr011c, AIM13), Mcs12 (Ybr262c, AIM5), Mcs10 (Ycl057c-a) and Fcj1 (Ykr016w, AIM28). The MICOS complex...”
- Transcriptome analysis of a respiratory Saccharomyces cerevisiae strain suggests the expression of its phenotype is glucose insensitive and predominantly controlled by Hap4, Cat8 and Mig1
Bonander, BMC genomics 2008 - “...2.1 2.4 YDR175C RSM24 2.4 2.9 YFR049W YMR31 2.5 2.6 Other YBR262C AIM5 2.3 2.1 YFR011C AIM13 2.1 3.4 YLR168C AIM30 2.6 3.3 YML087C AIM33 4.2 11.6 YBR230C OM14 3.3 2.4 YDL104C QRI7 2.1 2.7 YOR187W TUF1 2.3 2.4 YKL067W YNK1 3.1 2.1 Not characterized YGR110W...”
- Repressors Nrg1 and Nrg2 regulate a set of stress-responsive genes in Saccharomyces cerevisiae
Vyas, Eukaryotic cell 2005 - “...QCR2, RIP1, RPM2, RSM10, SDP1, TUF1, YDR031W, YFR011C, YGL226W, YHR080C, YIL087C, YMR003W, YM31C, YMR157C, YMR252C, YNL200C, YNL274C, YOR161C, YPL183W-A Carbon...”
- Parallel identification of new genes in Saccharomyces cerevisiae
Oshiro, Genome research 2002 - “...opposite within YFR009W different frame opposite of YFR011c opposite of YGL042C intergenic intergenic opposite of YGL014W opposite of YHR073W intergenic within...”
- Transcriptome profiling to identify genes involved in peroxisome assembly and function
Smith, The Journal of cell biology 2002 - “...N/D 2 LSM8 o 1 YJL218W u 1 PSP1 o 13 PEX13 p 2 4 YFR011C u 2 LYS14 o 1 YJR120W o 1 SPC25 o 1 13 PXA1 p 1 4 YGL196W u 2 MCM1 o 1 YKL054C u 1 YHR140W u 1 13 RKI1...”
- More
F9XA20 DUF1690 domain-containing protein from Zymoseptoria tritici (strain CBS 115943 / IPO323)
Aligns to 13:183 / 196 (87.2%), covers 100.0% of PF07956, 123.4 bits
7pv0B / G0S140,G0SHY5 Crystal structure of a mic60-mic19 fusion protein (see paper)
Aligns to 4:68 / 74 (87.8%), covers 40.3% of PF07956, 64.8 bits
- Ligand: o-(o-(2-aminopropyl)-o'-(2-methoxyethyl)polypropylene glycol 500) (7pv0B)
Or search for genetic data about PF07956 in the Fitness Browser
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory