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Conserved domains on  [gi|530426673|ref|XP_005266107|]
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endosome-associated-trafficking regulator 1 isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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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 ...
 261-424 8.03e-06

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: 48.13  E-value: 8.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530426673   261 DRHLRTLQISYDALKDENSKLRRKLNEVQSFSEAQTEMVRTLERKLEakMIKEESDYHDLESVVQQKRAVKAENHVVKLK 340
Cdd:TIGR02168  259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ--ILRERLANLERQLEELEAQLEELESKLDELA 336

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530426673   341 QEISLLQAQVSNFQRENEALRcGQGASLTVVKQNADVALQNLRVVMNSAQASIKQLVSGAETLNlvAEILKSIDRISEVK 420
Cdd:TIGR02168  337 EELAELEEKLEELKEELESLE-AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN--NEIERLEARLERLE 413


                   ....
gi 530426673   421 DEEE 424
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 ...
 261-424 8.03e-06

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: 48.13  E-value: 8.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530426673   261 DRHLRTLQISYDALKDENSKLRRKLNEVQSFSEAQTEMVRTLERKLEakMIKEESDYHDLESVVQQKRAVKAENHVVKLK 340
Cdd:TIGR02168  259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ--ILRERLANLERQLEELEAQLEELESKLDELA 336

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530426673   341 QEISLLQAQVSNFQRENEALRcGQGASLTVVKQNADVALQNLRVVMNSAQASIKQLVSGAETLNlvAEILKSIDRISEVK 420
Cdd:TIGR02168  337 EELAELEEKLEELKEELESLE-AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN--NEIERLEARLERLE 413


                   ....
gi 530426673   421 DEEE 424
Cdd:TIGR02168  414 DRRE 417
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
258-416 3.73e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 3.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530426673 258 SLGDRHLRTLQISYDALKDENSKLRRKLNEVQS--------FSEAQTEM------VRTLERKLEAKMIKEESDYHDLESV 323
Cdd:COG4372   27 AALSEQLRKALFELDKLQEELEQLREELEQAREeleqleeeLEQARSELeqleeeLEELNEQLQAAQAELAQAQEELESL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530426673 324 VQQKRavkaenhvvKLKQEISLLQAQVSNFQRENEALRcGQGASLTVVKQNADVALQNLRVVMNSAQASIKQLVSGAETL 403
Cdd:COG4372  107 QEEAE---------ELQEELEELQKERQDLEQQRKQLE-AQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176

                        170
                 ....*....|...
gi 530426673 404 NLvAEILKSIDRI 416
Cdd:COG4372  177 SE-AEAEQALDEL 188
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 257-356 6.02e-04

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: 40.66  E-value: 6.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530426673  257 ESLGDRHLRTLQISYDALKDENSKLRRKLNEVQSFSEAQTEMVRTLERKLEAkmikeESDYHDLESVVQQKRAVKAENHV 336
Cdd:pfam15619  98 LRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLEL-----ENKSFRRQLAAEKKKHKEAQEEV 172

                          90       100
                  ....*....|....*....|
gi 530426673  337 VKLKQEISLLQAQVSNFQRE 356
Cdd:pfam15619 173 KILQEEIERLQQKLKEKERE 192
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 261-424 8.03e-06

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: 48.13  E-value: 8.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530426673   261 DRHLRTLQISYDALKDENSKLRRKLNEVQSFSEAQTEMVRTLERKLEakMIKEESDYHDLESVVQQKRAVKAENHVVKLK 340
Cdd:TIGR02168  259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ--ILRERLANLERQLEELEAQLEELESKLDELA 336

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530426673   341 QEISLLQAQVSNFQRENEALRcGQGASLTVVKQNADVALQNLRVVMNSAQASIKQLVSGAETLNlvAEILKSIDRISEVK 420
Cdd:TIGR02168  337 EELAELEEKLEELKEELESLE-AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN--NEIERLEARLERLE 413


                   ....
gi 530426673   421 DEEE 424
Cdd:TIGR02168  414 DRRE 417
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
258-416 3.73e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 3.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530426673 258 SLGDRHLRTLQISYDALKDENSKLRRKLNEVQS--------FSEAQTEM------VRTLERKLEAKMIKEESDYHDLESV 323
Cdd:COG4372   27 AALSEQLRKALFELDKLQEELEQLREELEQAREeleqleeeLEQARSELeqleeeLEELNEQLQAAQAELAQAQEELESL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530426673 324 VQQKRavkaenhvvKLKQEISLLQAQVSNFQRENEALRcGQGASLTVVKQNADVALQNLRVVMNSAQASIKQLVSGAETL 403
Cdd:COG4372  107 QEEAE---------ELQEELEELQKERQDLEQQRKQLE-AQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176

                        170
                 ....*....|...
gi 530426673 404 NLvAEILKSIDRI 416
Cdd:COG4372  177 SE-AEAEQALDEL 188
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 257-356 6.02e-04

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: 40.66  E-value: 6.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530426673  257 ESLGDRHLRTLQISYDALKDENSKLRRKLNEVQSFSEAQTEMVRTLERKLEAkmikeESDYHDLESVVQQKRAVKAENHV 336
Cdd:pfam15619  98 LRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLEL-----ENKSFRRQLAAEKKKHKEAQEEV 172

                          90       100
                  ....*....|....*....|
gi 530426673  337 VKLKQEISLLQAQVSNFQRE 356
Cdd:pfam15619 173 KILQEEIERLQQKLKEKERE 192
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
257-425 1.03e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530426673 257 ESLGDRHLRTLQISYDALKDENSKLRRKLNEVQSFSEAQTEmVRTLERKLEAKMIKEESDYHDLESVVQQKRAVKAENHV 336
Cdd:COG4717   56 DELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEELREELEKLEKLLQLLPLYQEL 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530426673 337 VKLKQEISLLQAQVSNFQRENEALRcgqgasltvvkqNADVALQNLRVVMNSAQASIKQL--VSGAETLNLVAEILKSID 414
Cdd:COG4717  135 EALEAELAELPERLEELEERLEELR------------ELEEELEELEAELAELQEELEELleQLSLATEEELQDLAEELE 202

                        170
                 ....*....|.
gi 530426673 415 RISEVKDEEED 425
Cdd:COG4717  203 ELQQRLAELEE 213
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 247-359 5.43e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 39.11  E-value: 5.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530426673  247 SPSADFAVHGESLGDRHLRTLQisydaLKDENSKLRRKLNEVQSF---SEAQTEMVRTLERKLEAKMIKEESDYHDLESV 323
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQ-----LQDTITTLTQKLTTAHRKeaeNEALLEELRSLQERLNASERKVEGLGEELSSM 263

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 530426673  324 VQQKRAVKAENHVVKLK-QEISLLQAQVSNFQRENEA 359
Cdd:pfam07888 264 AAQRDRTQAELHQARLQaAQLTLQLADASLALREGRA 300
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 264-361 6.19e-03

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 36.85  E-value: 6.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530426673  264 LRTLQISYDALKDENSKLRRKLNEVQSFSEAQTEMVRTLERKLEAKMIKEESDyhdlesvVQQKRAVKAENHvvKLKQEI 343
Cdd:pfam07926   3 LSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVLHAED-------IKALQALREELN--ELKAEI 73

                          90
                  ....*....|....*...
gi 530426673  344 SLLQAQVSNFQRENEALR 361
Cdd:pfam07926  74 AELKAEAESAKAELEESE 91
 
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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