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Conserved domains on  [gi|19112511|ref|NP_595719|]
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protein Fis1 [Schizosaccharomyces pombe]

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 ...
 19-130 2.22e-46

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: 146.93  E-value: 2.22e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112511  19 ISVDEFLQIKEQYDAEQPL--ITLQTKFNLAWALVRSDSTQHVQQGLSLFCSIYKDSPERRLECLYYIALSHYKLKQYEE 96
Cdd:cd12212   2 LSPEELAVLEEQYNSELARgsVSPQTQFNYAWALVKSKNPEDIRRGIELLEELYRDGPERRRECLYYLALGHYKLGEYSE 81

                        90       100       110
                ....*....|....*....|....*....|....
gi 19112511  97 SRRYLNMLLSKDPNSPEALKLKNRLYDAVTKEGY 130
Cdd:cd12212  82 ARRYVDALLEIEPDNRQALALKELIEDKITKEGL 115
 
Name Accession Description Interval E-value
Fis1 cd12212
Mitochondrial Fission Protein Fis1, cytosolic domain; Fis1, along with Dnm1 and Mdv1, is an ...
 19-130 2.22e-46

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: 146.93  E-value: 2.22e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112511  19 ISVDEFLQIKEQYDAEQPL--ITLQTKFNLAWALVRSDSTQHVQQGLSLFCSIYKDSPERRLECLYYIALSHYKLKQYEE 96
Cdd:cd12212   2 LSPEELAVLEEQYNSELARgsVSPQTQFNYAWALVKSKNPEDIRRGIELLEELYRDGPERRRECLYYLALGHYKLGEYSE 81

                        90       100       110
                ....*....|....*....|....*....|....
gi 19112511  97 SRRYLNMLLSKDPNSPEALKLKNRLYDAVTKEGY 130
Cdd:cd12212  82 ARRYVDALLEIEPDNRQALALKELIEDKITKEGL 115
Fis1_TPR_C pfam14853
Fis1 C-terminal tetratricopeptide repeat; The mitochondrial fission protein Fis1 consists of ...
 79-130 5.06e-16

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: 67.55  E-value: 5.06e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 19112511    79 ECLYYIALSHYKLKQYEESRRYLNMLLSKDPNSPEALKLKNRLYDAVTKEGY 130
Cdd:pfam14853   2 ECLYYLAVGHYKLGEYSEARRYVDALLEIEPDNRQALALKELIEDKITKEGL 53
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 70-121 3.96e-06

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: 43.44  E-value: 3.96e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 19112511  70 YKDSPeRRLECLYYIALSHYKLKQYEESRRYLNMLLSKDPNSPEALKLKNRL 121
Cdd:COG1729  60 YPDSP-KAPDALLKLGLSYLELGDYDKARATLEELIKKYPDSEAAKEARARL 110
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 78-117 8.42e-04

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 38.91  E-value: 8.42e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 19112511    78 LECLYYIALSHYKLKQYEESRRYLNMLLSKDPNSPEALKL 117
Cdd:TIGR02917 295 LPALLLAGASEYQLGNLEQAYQYLNQILKYAPNSHQARRL 334
 
Name Accession Description Interval E-value
Fis1 cd12212
Mitochondrial Fission Protein Fis1, cytosolic domain; Fis1, along with Dnm1 and Mdv1, is an ...
 19-130 2.22e-46

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: 146.93  E-value: 2.22e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112511  19 ISVDEFLQIKEQYDAEQPL--ITLQTKFNLAWALVRSDSTQHVQQGLSLFCSIYKDSPERRLECLYYIALSHYKLKQYEE 96
Cdd:cd12212   2 LSPEELAVLEEQYNSELARgsVSPQTQFNYAWALVKSKNPEDIRRGIELLEELYRDGPERRRECLYYLALGHYKLGEYSE 81

                        90       100       110
                ....*....|....*....|....*....|....
gi 19112511  97 SRRYLNMLLSKDPNSPEALKLKNRLYDAVTKEGY 130
Cdd:cd12212  82 ARRYVDALLEIEPDNRQALALKELIEDKITKEGL 115
Fis1_TPR_C pfam14853
Fis1 C-terminal tetratricopeptide repeat; The mitochondrial fission protein Fis1 consists of ...
 79-130 5.06e-16

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: 67.55  E-value: 5.06e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 19112511    79 ECLYYIALSHYKLKQYEESRRYLNMLLSKDPNSPEALKLKNRLYDAVTKEGY 130
Cdd:pfam14853   2 ECLYYLAVGHYKLGEYSEARRYVDALLEIEPDNRQALALKELIEDKITKEGL 53
Fis1_TPR_N pfam14852
Fis1 N-terminal tetratricopeptide repeat; The mitochondrial fission protein Fis1 consists of ...
 41-73 2.52e-12

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: 57.79  E-value: 2.52e-12
                          10        20        30
                  ....*....|....*....|....*....|...
gi 19112511    41 QTKFNLAWALVRSDSTQHVQQGLSLFCSIYKDS 73
Cdd:pfam14852   1 QTKFNYAWALVKSKNRADQQRGIALLEELYRDS 33
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 70-121 3.96e-06

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: 43.44  E-value: 3.96e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 19112511  70 YKDSPeRRLECLYYIALSHYKLKQYEESRRYLNMLLSKDPNSPEALKLKNRL 121
Cdd:COG1729  60 YPDSP-KAPDALLKLGLSYLELGDYDKARATLEELIKKYPDSEAAKEARARL 110
TPR_6 pfam13174
Tetratricopeptide repeat;
79-111 9.66e-05

Tetratricopeptide repeat;


Pssm-ID: 463800 [Multi-domain]  Cd Length: 33  Bit Score: 37.83  E-value: 9.66e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 19112511    79 ECLYYIALSHYKLKQYEESRRYLNMLLSKDPNS 111
Cdd:pfam13174   1 DALLKLALAYLELGDTDEAKEALERLIKKYPDS 33
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 78-117 8.42e-04

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 38.91  E-value: 8.42e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 19112511    78 LECLYYIALSHYKLKQYEESRRYLNMLLSKDPNSPEALKL 117
Cdd:TIGR02917 295 LPALLLAGASEYQLGNLEQAYQYLNQILKYAPNSHQARRL 334
TPR_2 pfam07719
Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ...
 79-110 1.43e-03

Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats (TPR) that are not matched by pfam00515.


Pssm-ID: 429619 [Multi-domain]  Cd Length: 33  Bit Score: 34.42  E-value: 1.43e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 19112511    79 ECLYYIALSHYKLKQYEESRRYLNMLLSKDPN 110
Cdd:pfam07719   2 EALYNLGLAYYKLGDYEEALEAYEKALELDPN 33
 
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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