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Conserved domains on  [gi|1034663602|ref|XP_016869707|]
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endosome-associated-trafficking regulator 1 isoform X1 [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 ...
 310-482 1.05e-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: 48.13  E-value: 1.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663602  310 DRHLRTLQISYDALKDENSKLRRKLNEVQSFSEAQTEMVRTLERKLEakMIKEEsdyhdlesvVQQVEQNLELMTKRAVK 389
Cdd:TIGR02168  259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ--ILRER---------LANLERQLEELEAQLEE 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663602  390 AENHVVKLKQEISLLQAQVSNFQRENEALRcGQGASLTVVKQNADVALQNLRVVMNSAQASIKQLVSGAETLNlvAEILK 469
Cdd:TIGR02168  328 LESKLDELAEELAELEEKLEELKEELESLE-AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN--NEIER 404

                          170
                   ....*....|...
gi 1034663602  470 SIDRISEVKDEEE 482
Cdd:TIGR02168  405 LEARLERLEDRRE 417
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 310-482 1.05e-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: 48.13  E-value: 1.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663602  310 DRHLRTLQISYDALKDENSKLRRKLNEVQSFSEAQTEMVRTLERKLEakMIKEEsdyhdlesvVQQVEQNLELMTKRAVK 389
Cdd:TIGR02168  259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ--ILRER---------LANLERQLEELEAQLEE 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663602  390 AENHVVKLKQEISLLQAQVSNFQRENEALRcGQGASLTVVKQNADVALQNLRVVMNSAQASIKQLVSGAETLNlvAEILK 469
Cdd:TIGR02168  328 LESKLDELAEELAELEEKLEELKEELESLE-AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN--NEIER 404

                          170
                   ....*....|...
gi 1034663602  470 SIDRISEVKDEEE 482
Cdd:TIGR02168  405 LEARLERLEDRRE 417
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
307-482 1.16e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663602 307 SLGDRHLRTLQISYDALKDENSKLRRKLNEvqsfseAQTEMvRTLERKLEAKmiKEEsdyhdlesvVQQVEQNLELMTKR 386
Cdd:COG4372    27 AALSEQLRKALFELDKLQEELEQLREELEQ------AREEL-EQLEEELEQA--RSE---------LEQLEEELEELNEQ 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663602 387 AVKAENHVVKLKQEISLLQAQVSNFQRENEALRcGQGASLTVVKQNADVALQNLRVVMNSAQASIKQLVSGAETL-NLVA 465
Cdd:COG4372    89 LQAAQAELAQAQEELESLQEEAEELQEELEELQ-KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLqEELA 167

                         170
                  ....*....|....*..
gi 1034663602 466 EILKSIDRISEVKDEEE 482
Cdd:COG4372   168 ALEQELQALSEAEAEQA 184
AAA_13 pfam13166
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 313-410 3.79e-03

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.


Pssm-ID: 463796 [Multi-domain]  Cd Length: 712  Bit Score: 40.04  E-value: 3.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663602 313 LRTLQISYDALKDE---NSKLRRKLNEVQSFSEAQTEMVRTLER-----------------KLEAKMIKE-ESDYHDLES 371
Cdd:pfam13166 337 LDGLRRALEAKRKDpfkSIELDSVDAKIESINDLVASINELIAKhneitdnfeeeknkakkKLRLHLVEEfKSEIDEYKD 416

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1034663602 372 VVQQVEQNLELMTKRAVKAENHVVKLKQEISLLQAQVSN 410
Cdd:pfam13166 417 KYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQLRD 455
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 310-482 1.05e-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: 48.13  E-value: 1.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663602  310 DRHLRTLQISYDALKDENSKLRRKLNEVQSFSEAQTEMVRTLERKLEakMIKEEsdyhdlesvVQQVEQNLELMTKRAVK 389
Cdd:TIGR02168  259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ--ILRER---------LANLERQLEELEAQLEE 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663602  390 AENHVVKLKQEISLLQAQVSNFQRENEALRcGQGASLTVVKQNADVALQNLRVVMNSAQASIKQLVSGAETLNlvAEILK 469
Cdd:TIGR02168  328 LESKLDELAEELAELEEKLEELKEELESLE-AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN--NEIER 404

                          170
                   ....*....|...
gi 1034663602  470 SIDRISEVKDEEE 482
Cdd:TIGR02168  405 LEARLERLEDRRE 417
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
307-482 1.16e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663602 307 SLGDRHLRTLQISYDALKDENSKLRRKLNEvqsfseAQTEMvRTLERKLEAKmiKEEsdyhdlesvVQQVEQNLELMTKR 386
Cdd:COG4372    27 AALSEQLRKALFELDKLQEELEQLREELEQ------AREEL-EQLEEELEQA--RSE---------LEQLEEELEELNEQ 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663602 387 AVKAENHVVKLKQEISLLQAQVSNFQRENEALRcGQGASLTVVKQNADVALQNLRVVMNSAQASIKQLVSGAETL-NLVA 465
Cdd:COG4372    89 LQAAQAELAQAQEELESLQEEAEELQEELEELQ-KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLqEELA 167

                         170
                  ....*....|....*..
gi 1034663602 466 EILKSIDRISEVKDEEE 482
Cdd:COG4372   168 ALEQELQALSEAEAEQA 184
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 321-435 5.46e-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: 42.75  E-value: 5.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663602  321 DALKDE----NSKLRRKLNEVQSFSEAQTEMVRTLERkLEAKMIKEESDYHDLESVVQQVEQNLELMTKRAVKAENHVVK 396
Cdd:TIGR02169  395 EKLKREinelKRELDRLQEELQRLSEELADLNAAIAG-IEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1034663602  397 LKQEISLLQAQVSNFQRENEALRCGQGASLTVVKQNADV 435
Cdd:TIGR02169  474 LKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV 512
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 339-471 2.40e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 2.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663602 339 SFSEAQTEMVRTLERKLEA--KMIKE-ESDYHDLESVVQQVEQNLELMTKRAVKAENHVVKLKQEISLLQAQVSNFQREN 415
Cdd:COG4942    13 LAAAAQADAAAEAEAELEQlqQEIAElEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034663602 416 EALRcgqgASLTvvKQNADVALQNLRVVMNSAQASIKQLVSGAETLNLV--AEILKSI 471
Cdd:COG4942    93 AELR----AELE--AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVrrLQYLKYL 144
AAA_13 pfam13166
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 313-410 3.79e-03

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.


Pssm-ID: 463796 [Multi-domain]  Cd Length: 712  Bit Score: 40.04  E-value: 3.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663602 313 LRTLQISYDALKDE---NSKLRRKLNEVQSFSEAQTEMVRTLER-----------------KLEAKMIKE-ESDYHDLES 371
Cdd:pfam13166 337 LDGLRRALEAKRKDpfkSIELDSVDAKIESINDLVASINELIAKhneitdnfeeeknkakkKLRLHLVEEfKSEIDEYKD 416

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1034663602 372 VVQQVEQNLELMTKRAVKAENHVVKLKQEISLLQAQVSN 410
Cdd:pfam13166 417 KYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQLRD 455
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
313-484 4.02e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.50  E-value: 4.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663602 313 LRTLQISYDALKDENSKLRRKLNEVQ-SFSEAQTEMVRTLER---------KLEAKMIKEESDYHDLESVVQQVEQNLEL 382
Cdd:COG4372    61 LEQLEEELEQARSELEQLEEELEELNeQLQAAQAELAQAQEEleslqeeaeELQEELEELQKERQDLEQQRKQLEAQIAE 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663602 383 MTKRAVKAENHVVKLKQEISLLQAQVSNFQRENEALRcgQGASLTVVKQNADVALQNLrVVMNSAQASIKQLVSGAETLN 462
Cdd:COG4372   141 LQSEIAEREEELKELEEQLESLQEELAALEQELQALS--EAEAEQALDELLKEANRNA-EKEEELAEAEKLIESLPRELA 217

                         170       180
                  ....*....|....*....|..
gi 1034663602 463 LVAEILKSIDRISEVKDEEEDS 484
Cdd:COG4372   218 EELLEAKDSLEAKLGLALSALL 239
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 356-462 5.93e-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: 5.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663602 356 EAKMIKEESDyhDLESVVQQVEQNLELMTKRAVKAENhvvklkqeisllqaqvsNFQREnealrcgqgasltVVKQNADV 435
Cdd:pfam07926   9 EIKRLKEEAA--DAEAQLQKLQEDLEKQAEIAREAQQ-----------------NYERE-------------LVLHAEDI 56

                          90       100
                  ....*....|....*....|....*...
gi 1034663602 436 -ALQNLRVVMNSAQASIKQLVSGAETLN 462
Cdd:pfam07926  57 kALQALREELNELKAEIAELKAEAESAK 84
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 306-414 8.94e-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: 37.57  E-value: 8.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663602 306 ESLGDRHLRTLQISYDALKDENSKLRRKLNEVQSFSEAQTEMVRTLERKLEakmikeesdyhdLESVVQQVEQNLELMTK 385
Cdd:pfam15619  98 LRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLE------------LENKSFRRQLAAEKKKH 165

                          90       100
                  ....*....|....*....|....*....
gi 1034663602 386 RAVKAEnhVVKLKQEISLLQAQVSNFQRE 414
Cdd:pfam15619 166 KEAQEE--VKILQEEIERLQQKLKEKERE 192
 
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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