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Conserved domains on  [gi|564378840|ref|XP_006249184|]
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mitochondrial fission 1 protein isoform X2 [Rattus norvegicus]

Protein Classification

mitochondrial fission 1 protein( domain architecture ID 10187549)

mitochondrial fission 1 (Fis1) protein is an essential protein in mediating mitochondrial fission, and is involved in the fragmentation of the mitochondrial network and its perinuclear clustering; contains tandem Tetratricopeptide repeat (TPR) motifs which are known to mediate protein-protein interactions

CATH:  1.25.40.10
Gene Ontology:  GO:0000266|GO:0060090|GO:0008289|GO:0005515
PubMed:  30708253|10517866
SCOP:  4001344

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Fis1 cd12212
Mitochondrial Fission Protein Fis1, cytosolic domain; Fis1, along with Dnm1 and Mdv1, is an ...
 4-113 1.11e-51

Mitochondrial Fission Protein Fis1, cytosolic domain; Fis1, along with Dnm1 and Mdv1, is an essential protein in mediating mitochondrial fission. Dnm1 and Fis1 are highly conserved, with a common mechanism in disparate species. In mutants of these proteins, mitochondrial fission is impaired, resulting in networks of undivided mitochondria. The Fis1 N-terminus is cytosolic and tethered to the mitochondrial outer membrane via a C-terminal transmembrane domain. Fis1 appears to act via the recruitment of division complexes to the mitochondrial outer membrane, via interactions with Mdv1 or Caf4. Fis1 has tandem Tetratricopeptide repeat (TPR) motifs which are known to mediate protein-protein interactions.


:

Pssm-ID: 276936 [Multi-domain]  Cd Length: 115  Bit Score: 161.18  E-value: 1.11e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378840   4 DEAARNFERKFQSEQAAGSVSKSTQFEYAWCLVRSKYNDDIRRGIVLLEELLpKGSKEEQRDYVFYLAVGNYRLKEYEKA 83
Cdd:cd12212    4 PEELAVLEEQYNSELARGSVSPQTQFNYAWALVKSKNPEDIRRGIELLEELY-RDGPERRRECLYYLALGHYKLGEYSEA 82

                         90       100       110
                 ....*....|....*....|....*....|
gi 564378840  84 LKYVRGLLQTEPQNNQAKELERLIDKAMKK 113
Cdd:cd12212   83 RRYVDALLEIEPDNRQALALKELIEDKITK 112
GH43_62_32_68_117_130 super family cl14647
Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl ...
 118-154 4.42e-03

Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl hydrolase families 32, 43, 62, 68, 117 and 130 (GH32, GH43, GH62, GH68, GH117, GH130) all possess 5-bladed beta-propeller domains and comprise clans F and J, as classified by the carbohydrate-active enzymes database (CAZY). Clan F consists of families GH43 and GH62. GH43 includes beta-xylosidases (EC 3.2.1.37), beta-xylanases (EC 3.2.1.8), alpha-L-arabinases (EC 3.2.1.99), and alpha-L-arabinofuranosidases (EC 3.2.1.55), using aryl-glycosides as substrates, while family GH62 contains alpha-L-arabinofuranosidases (EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose sidechains from xylans. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Clan J consists of families GH32 and GH68. GH32 comprises sucrose-6-phosphate hydrolases, invertases (EC 3.2.1.26), inulinases (EC 3.2.1.7), levanases (EC 3.2.1.65), eukaryotic fructosyltransferases, and bacterial fructanotransferases while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), all of which use sucrose as their preferential donor substrate. Members of this clan are retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) that catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. Structures of all families in the two clans manifest a funnel-shaped active site that comprises two subsites with a single route for access by ligands. Also included in this superfamily are GH117 enzymes that have exo-alpha-1,3-(3,6-anhydro)-l-galactosidase activity, removing terminal non-reducing alpha-1,3-linked 3,6-anhydro-l-galactose residues from their neoagarose substrate, and GH130 that are phosphorylases and hydrolases for beta-mannosides, involved in the bacterial utilization of mannans or N-linked glycans.


The actual alignment was detected with superfamily member cd09002:

Pssm-ID: 449341 [Multi-domain]  Cd Length: 271  Bit Score: 36.44  E-value: 4.42e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 564378840 118 HAVCSSSSLRP-GPWEHCPH-PL-HTHSPLSNLPSKGLGS 154
Cdd:cd09002  190 HMVVSARSKSPhGPWENSPYnPLvRTQSREEKWWSKGHGT 229
 
Name Accession Description Interval E-value
Fis1 cd12212
Mitochondrial Fission Protein Fis1, cytosolic domain; Fis1, along with Dnm1 and Mdv1, is an ...
 4-113 1.11e-51

Mitochondrial Fission Protein Fis1, cytosolic domain; Fis1, along with Dnm1 and Mdv1, is an essential protein in mediating mitochondrial fission. Dnm1 and Fis1 are highly conserved, with a common mechanism in disparate species. In mutants of these proteins, mitochondrial fission is impaired, resulting in networks of undivided mitochondria. The Fis1 N-terminus is cytosolic and tethered to the mitochondrial outer membrane via a C-terminal transmembrane domain. Fis1 appears to act via the recruitment of division complexes to the mitochondrial outer membrane, via interactions with Mdv1 or Caf4. Fis1 has tandem Tetratricopeptide repeat (TPR) motifs which are known to mediate protein-protein interactions.


Pssm-ID: 276936 [Multi-domain]  Cd Length: 115  Bit Score: 161.18  E-value: 1.11e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378840   4 DEAARNFERKFQSEQAAGSVSKSTQFEYAWCLVRSKYNDDIRRGIVLLEELLpKGSKEEQRDYVFYLAVGNYRLKEYEKA 83
Cdd:cd12212    4 PEELAVLEEQYNSELARGSVSPQTQFNYAWALVKSKNPEDIRRGIELLEELY-RDGPERRRECLYYLALGHYKLGEYSEA 82

                         90       100       110
                 ....*....|....*....|....*....|
gi 564378840  84 LKYVRGLLQTEPQNNQAKELERLIDKAMKK 113
Cdd:cd12212   83 RRYVDALLEIEPDNRQALALKELIEDKITK 112
Fis1_TPR_C pfam14853
Fis1 C-terminal tetratricopeptide repeat; The mitochondrial fission protein Fis1 consists of ...
 64-113 1.22e-22

Fis1 C-terminal tetratricopeptide repeat; The mitochondrial fission protein Fis1 consists of two tetratricopeptide repeats. This domain is the C-terminal tetratricopeptide repeat


Pssm-ID: 434269 [Multi-domain]  Cd Length: 53  Bit Score: 85.27  E-value: 1.22e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 564378840   64 RDYVFYLAVGNYRLKEYEKALKYVRGLLQTEPQNNQAKELERLIDKAMKK 113
Cdd:pfam14853   1 RECLYYLAVGHYKLGEYSEARRYVDALLEIEPDNRQALALKELIEDKITK 50
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 4-110 2.71e-05

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 41.92  E-value: 2.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378840   4 DEAARNFER--KFQSEQAAgsvsksTQFEYAWCLVRSkynDDIRRGIVLLEELL---PkgskeEQRDYVFYLAVGNYRLK 78
Cdd:COG4235   34 DEALAAYEKalRLDPDNAD------ALLDLAEALLAA---GDTEEAEELLERALaldP-----DNPEALYLLGLAAFQQG 99

                         90       100       110
                 ....*....|....*....|....*....|..
gi 564378840  79 EYEKALKYVRGLLQTEPQNNQAKELERLIDKA 110
Cdd:COG4235  100 DYAEAIAAWQKLLALLPADAPARLLEASIAEA 131
GH43_XYL-like cd09002
Glycosyl hydrolase family 43, beta-D-xylosidase (uncharacterized); This glycosyl hydrolase ...
 118-154 4.42e-03

Glycosyl hydrolase family 43, beta-D-xylosidase (uncharacterized); This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been annotated as having beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity. They are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350116 [Multi-domain]  Cd Length: 271  Bit Score: 36.44  E-value: 4.42e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 564378840 118 HAVCSSSSLRP-GPWEHCPH-PL-HTHSPLSNLPSKGLGS 154
Cdd:cd09002  190 HMVVSARSKSPhGPWENSPYnPLvRTQSREEKWWSKGHGT 229
 
Name Accession Description Interval E-value
Fis1 cd12212
Mitochondrial Fission Protein Fis1, cytosolic domain; Fis1, along with Dnm1 and Mdv1, is an ...
 4-113 1.11e-51

Mitochondrial Fission Protein Fis1, cytosolic domain; Fis1, along with Dnm1 and Mdv1, is an essential protein in mediating mitochondrial fission. Dnm1 and Fis1 are highly conserved, with a common mechanism in disparate species. In mutants of these proteins, mitochondrial fission is impaired, resulting in networks of undivided mitochondria. The Fis1 N-terminus is cytosolic and tethered to the mitochondrial outer membrane via a C-terminal transmembrane domain. Fis1 appears to act via the recruitment of division complexes to the mitochondrial outer membrane, via interactions with Mdv1 or Caf4. Fis1 has tandem Tetratricopeptide repeat (TPR) motifs which are known to mediate protein-protein interactions.


Pssm-ID: 276936 [Multi-domain]  Cd Length: 115  Bit Score: 161.18  E-value: 1.11e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378840   4 DEAARNFERKFQSEQAAGSVSKSTQFEYAWCLVRSKYNDDIRRGIVLLEELLpKGSKEEQRDYVFYLAVGNYRLKEYEKA 83
Cdd:cd12212    4 PEELAVLEEQYNSELARGSVSPQTQFNYAWALVKSKNPEDIRRGIELLEELY-RDGPERRRECLYYLALGHYKLGEYSEA 82

                         90       100       110
                 ....*....|....*....|....*....|
gi 564378840  84 LKYVRGLLQTEPQNNQAKELERLIDKAMKK 113
Cdd:cd12212   83 RRYVDALLEIEPDNRQALALKELIEDKITK 112
Fis1_TPR_C pfam14853
Fis1 C-terminal tetratricopeptide repeat; The mitochondrial fission protein Fis1 consists of ...
 64-113 1.22e-22

Fis1 C-terminal tetratricopeptide repeat; The mitochondrial fission protein Fis1 consists of two tetratricopeptide repeats. This domain is the C-terminal tetratricopeptide repeat


Pssm-ID: 434269 [Multi-domain]  Cd Length: 53  Bit Score: 85.27  E-value: 1.22e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 564378840   64 RDYVFYLAVGNYRLKEYEKALKYVRGLLQTEPQNNQAKELERLIDKAMKK 113
Cdd:pfam14853   1 RECLYYLAVGHYKLGEYSEARRYVDALLEIEPDNRQALALKELIEDKITK 50
Fis1_TPR_N pfam14852
Fis1 N-terminal tetratricopeptide repeat; The mitochondrial fission protein Fis1 consists of ...
 27-55 3.23e-13

Fis1 N-terminal tetratricopeptide repeat; The mitochondrial fission protein Fis1 consists of two tetratricopeptide repeats. This domain is the N-terminal tetratricopeptide repeat


Pssm-ID: 464348  Cd Length: 33  Bit Score: 60.49  E-value: 3.23e-13
                          10        20
                  ....*....|....*....|....*....
gi 564378840   27 TQFEYAWCLVRSKYNDDIRRGIVLLEELL 55
Cdd:pfam14852   2 TKFNYAWALVKSKNRADQQRGIALLEELY 30
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 4-110 2.71e-05

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 41.92  E-value: 2.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378840   4 DEAARNFER--KFQSEQAAgsvsksTQFEYAWCLVRSkynDDIRRGIVLLEELL---PkgskeEQRDYVFYLAVGNYRLK 78
Cdd:COG4235   34 DEALAAYEKalRLDPDNAD------ALLDLAEALLAA---GDTEEAEELLERALaldP-----DNPEALYLLGLAAFQQG 99

                         90       100       110
                 ....*....|....*....|....*....|..
gi 564378840  79 EYEKALKYVRGLLQTEPQNNQAKELERLIDKA 110
Cdd:COG4235  100 DYAEAIAAWQKLLALLPADAPARLLEASIAEA 131
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 4-110 1.53e-03

Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 36.51  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378840   4 DEAARNFErKFQSEQAAGSVSKSTQFEYAWCLVRSKyndDIRRGIVLLEELLPKGSKEEQR-DYVFYLAVGNYRLKEYEK 82
Cdd:COG1729   10 DEAIAAFK-AFLKRYPNSPLAPDALYWLGEAYYALG---DYDEAAEAFEKLLKRYPDSPKApDALLKLGLSYLELGDYDK 85

                         90       100
                 ....*....|....*....|....*...
gi 564378840  83 ALKYVRGLLQTEPQNNQAKELERLIDKA 110
Cdd:COG1729   86 ARATLEELIKKYPDSEAAKEARARLARL 113
GH43_XYL-like cd09002
Glycosyl hydrolase family 43, beta-D-xylosidase (uncharacterized); This glycosyl hydrolase ...
 118-154 4.42e-03

Glycosyl hydrolase family 43, beta-D-xylosidase (uncharacterized); This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been annotated as having beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity. They are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350116 [Multi-domain]  Cd Length: 271  Bit Score: 36.44  E-value: 4.42e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 564378840 118 HAVCSSSSLRP-GPWEHCPH-PL-HTHSPLSNLPSKGLGS 154
Cdd:cd09002  190 HMVVSARSKSPhGPWENSPYnPLvRTQSREEKWWSKGHGT 229
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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