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Conserved domains on  [gi|158937254|ref|NP_080127|]
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uncharacterized protein C6orf118 homolog isoform 1 [Mus musculus]

Protein Classification

TSNAXIP1_N domain-containing protein( domain architecture ID 11239006)

TSNAXIP1_N domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TSNAXIP1_N pfam15739
Translin-associated factor X-interacting N-terminus; This domain is found at the N-terminus of ...
239-349 2.98e-33

Translin-associated factor X-interacting N-terminus; This domain is found at the N-terminus of translin-associated factor X-interacting protein, a protein which may play a role in spermatogenesis.


:

Pssm-ID: 464835 [Multi-domain]  Cd Length: 111  Bit Score: 121.94  E-value: 2.98e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937254  239 ENRLKEELQKI-CTCNPQQFNRLQVFGEIFEDICNSSLIFGDLLKEIKDEYELYMAALLDSQPTAQYqrLLAEVRGLENS 317
Cdd:pfam15739   1 ERKLEQELQKLgCTEDGPQELRLQVYREVFEDLIEHFTTYKPLLSEIKNEYELYIAHLLESQRELQY--LKAKLKGLSEQ 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 158937254  318 P-RPSCDIDQAKEHLRKVQQAYLEALEHNDKLR 349
Cdd:pfam15739  79 SdKRALELEEKREEIRALEKESKALLERNDKLR 111
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
308-491 3.88e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 3.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937254   308 LAEVRglENSPRPSCDIDQAKEHLRKVQQAYLEALEHNDKLRNELEAESLLLQSAKEKAANGKMKDEKEL-TLVEKVEKR 386
Cdd:TIGR02169  179 LEEVE--ENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLaSLEEELEKL 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937254   387 RCEIFEKLDEIKALEKHIKEnmVHSGVFKIAESGLKSIEDEAIKLETSNRILKKKIKVIESQMKQLLLRSKISEEERQAL 466
Cdd:TIGR02169  257 TEEISELEKRLEEIEQLLEE--LNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKL 334
                          170       180
                   ....*....|....*....|....*
gi 158937254   467 wdlireysdIEDVEDVEGDFEMLRK 491
Cdd:TIGR02169  335 ---------LAEIEELEREIEEERK 350
 
Name Accession Description Interval E-value
TSNAXIP1_N pfam15739
Translin-associated factor X-interacting N-terminus; This domain is found at the N-terminus of ...
239-349 2.98e-33

Translin-associated factor X-interacting N-terminus; This domain is found at the N-terminus of translin-associated factor X-interacting protein, a protein which may play a role in spermatogenesis.


Pssm-ID: 464835 [Multi-domain]  Cd Length: 111  Bit Score: 121.94  E-value: 2.98e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937254  239 ENRLKEELQKI-CTCNPQQFNRLQVFGEIFEDICNSSLIFGDLLKEIKDEYELYMAALLDSQPTAQYqrLLAEVRGLENS 317
Cdd:pfam15739   1 ERKLEQELQKLgCTEDGPQELRLQVYREVFEDLIEHFTTYKPLLSEIKNEYELYIAHLLESQRELQY--LKAKLKGLSEQ 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 158937254  318 P-RPSCDIDQAKEHLRKVQQAYLEALEHNDKLR 349
Cdd:pfam15739  79 SdKRALELEEKREEIRALEKESKALLERNDKLR 111
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
308-491 3.88e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 3.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937254   308 LAEVRglENSPRPSCDIDQAKEHLRKVQQAYLEALEHNDKLRNELEAESLLLQSAKEKAANGKMKDEKEL-TLVEKVEKR 386
Cdd:TIGR02169  179 LEEVE--ENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLaSLEEELEKL 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937254   387 RCEIFEKLDEIKALEKHIKEnmVHSGVFKIAESGLKSIEDEAIKLETSNRILKKKIKVIESQMKQLLLRSKISEEERQAL 466
Cdd:TIGR02169  257 TEEISELEKRLEEIEQLLEE--LNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKL 334
                          170       180
                   ....*....|....*....|....*
gi 158937254   467 wdlireysdIEDVEDVEGDFEMLRK 491
Cdd:TIGR02169  335 ---------LAEIEELEREIEEERK 350
 
Name Accession Description Interval E-value
TSNAXIP1_N pfam15739
Translin-associated factor X-interacting N-terminus; This domain is found at the N-terminus of ...
239-349 2.98e-33

Translin-associated factor X-interacting N-terminus; This domain is found at the N-terminus of translin-associated factor X-interacting protein, a protein which may play a role in spermatogenesis.


Pssm-ID: 464835 [Multi-domain]  Cd Length: 111  Bit Score: 121.94  E-value: 2.98e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937254  239 ENRLKEELQKI-CTCNPQQFNRLQVFGEIFEDICNSSLIFGDLLKEIKDEYELYMAALLDSQPTAQYqrLLAEVRGLENS 317
Cdd:pfam15739   1 ERKLEQELQKLgCTEDGPQELRLQVYREVFEDLIEHFTTYKPLLSEIKNEYELYIAHLLESQRELQY--LKAKLKGLSEQ 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 158937254  318 P-RPSCDIDQAKEHLRKVQQAYLEALEHNDKLR 349
Cdd:pfam15739  79 SdKRALELEEKREEIRALEKESKALLERNDKLR 111
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
308-491 3.88e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 3.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937254   308 LAEVRglENSPRPSCDIDQAKEHLRKVQQAYLEALEHNDKLRNELEAESLLLQSAKEKAANGKMKDEKEL-TLVEKVEKR 386
Cdd:TIGR02169  179 LEEVE--ENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLaSLEEELEKL 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937254   387 RCEIFEKLDEIKALEKHIKEnmVHSGVFKIAESGLKSIEDEAIKLETSNRILKKKIKVIESQMKQLLLRSKISEEERQAL 466
Cdd:TIGR02169  257 TEEISELEKRLEEIEQLLEE--LNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKL 334
                          170       180
                   ....*....|....*....|....*
gi 158937254   467 wdlireysdIEDVEDVEGDFEMLRK 491
Cdd:TIGR02169  335 ---------LAEIEELEREIEEERK 350
 
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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