NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2217375198|ref|XP_047278613|]
View 

endosome-associated-trafficking regulator 1 isoform X7 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
188-351 4.86e-05

chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 4.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217375198  188 DRHLRTLQISYDALKDENSKLRRKLNEVQSFSEAQTEMVRTLERKLEakMIKEESDYHDLESVVQQKRAVKAENHVVKLK 267
Cdd:TIGR02168  259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ--ILRERLANLERQLEELEAQLEELESKLDELA 336
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217375198  268 QEISLLQAQVSNFQRENEALRcGQGASLTVVKQNADVALQNLRVVMNSAQASIKQLVSGAETLNlvAEILKSIDRISEVK 347
Cdd:TIGR02168  337 EELAELEEKLEELKEELESLE-AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN--NEIERLEARLERLE 413

                   ....
gi 2217375198  348 DEEE 351
Cdd:TIGR02168  414 DRRE 417
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
188-351 4.86e-05

chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 4.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217375198  188 DRHLRTLQISYDALKDENSKLRRKLNEVQSFSEAQTEMVRTLERKLEakMIKEESDYHDLESVVQQKRAVKAENHVVKLK 267
Cdd:TIGR02168  259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ--ILRERLANLERQLEELEAQLEELESKLDELA 336
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217375198  268 QEISLLQAQVSNFQRENEALRcGQGASLTVVKQNADVALQNLRVVMNSAQASIKQLVSGAETLNlvAEILKSIDRISEVK 347
Cdd:TIGR02168  337 EELAELEEKLEELKEELESLE-AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN--NEIERLEARLERLE 413

                   ....
gi 2217375198  348 DEEE 351
Cdd:TIGR02168  414 DRRE 417
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
184-283 3.82e-03

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 37.96  E-value: 3.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217375198 184 ESLGDRHLRTLQISYDALKDENSKLRRKLNEVQSFSEAQTEMVRTLERKLEAkmikeESDYHDLESVVQQKRAVKAENHV 263
Cdd:pfam15619  98 LRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLEL-----ENKSFRRQLAAEKKKHKEAQEEV 172
                          90       100
                  ....*....|....*....|
gi 2217375198 264 VKLKQEISLLQAQVSNFQRE 283
Cdd:pfam15619 173 KILQEEIERLQQKLKEKERE 192
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
184-352 8.36e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.21  E-value: 8.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217375198 184 ESLGDRHLRTLQISYDALKDENSKLRRKLNEVQSFSEAQTEmVRTLERKLEAKMIKEESDYHDLESVVQQKRAVKAENHV 263
Cdd:COG4717    56 DELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEELREELEKLEKLLQLLPLYQEL 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217375198 264 VKLKQEISLLQAQVSNFQRENEALRcgqgasltvvkqNADVALQNLRVVMNSAQASIKQL--VSGAETLNLVAEILKSID 341
Cdd:COG4717   135 EALEAELAELPERLEELEERLEELR------------ELEEELEELEAELAELQEELEELleQLSLATEEELQDLAEELE 202
                         170
                  ....*....|.
gi 2217375198 342 RISEVKDEEED 352
Cdd:COG4717   203 ELQQRLAELEE 213
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
188-351 4.86e-05

chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 4.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217375198  188 DRHLRTLQISYDALKDENSKLRRKLNEVQSFSEAQTEMVRTLERKLEakMIKEESDYHDLESVVQQKRAVKAENHVVKLK 267
Cdd:TIGR02168  259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ--ILRERLANLERQLEELEAQLEELESKLDELA 336
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217375198  268 QEISLLQAQVSNFQRENEALRcGQGASLTVVKQNADVALQNLRVVMNSAQASIKQLVSGAETLNlvAEILKSIDRISEVK 347
Cdd:TIGR02168  337 EELAELEEKLEELKEELESLE-AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN--NEIERLEARLERLE 413

                   ....
gi 2217375198  348 DEEE 351
Cdd:TIGR02168  414 DRRE 417
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
184-283 3.82e-03

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 37.96  E-value: 3.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217375198 184 ESLGDRHLRTLQISYDALKDENSKLRRKLNEVQSFSEAQTEMVRTLERKLEAkmikeESDYHDLESVVQQKRAVKAENHV 263
Cdd:pfam15619  98 LRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLEL-----ENKSFRRQLAAEKKKHKEAQEEV 172
                          90       100
                  ....*....|....*....|
gi 2217375198 264 VKLKQEISLLQAQVSNFQRE 283
Cdd:pfam15619 173 KILQEEIERLQQKLKEKERE 192
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
184-352 8.36e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.21  E-value: 8.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217375198 184 ESLGDRHLRTLQISYDALKDENSKLRRKLNEVQSFSEAQTEmVRTLERKLEAKMIKEESDYHDLESVVQQKRAVKAENHV 263
Cdd:COG4717    56 DELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEELREELEKLEKLLQLLPLYQEL 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217375198 264 VKLKQEISLLQAQVSNFQRENEALRcgqgasltvvkqNADVALQNLRVVMNSAQASIKQL--VSGAETLNLVAEILKSID 341
Cdd:COG4717   135 EALEAELAELPERLEELEERLEELR------------ELEEELEELEAELAELQEELEELleQLSLATEEELQDLAEELE 202
                         170
                  ....*....|.
gi 2217375198 342 RISEVKDEEED 352
Cdd:COG4717   203 ELQQRLAELEE 213
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH