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Conserved domains on  [gi|325974489|ref|NP_001013153|]
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endosome-associated-trafficking regulator 1 [Rattus norvegicus]

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 ...
 251-373 1.69e-04

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: 44.28  E-value: 1.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325974489   251 AAHEESLGDRHLRTLQLSYEALKDENSKLRRKLSEVQSFSETQTEMVRTLERKLE---AKMIKEESDFHDLESVVQQVEQ 327
Cdd:TIGR02168  251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQilrERLANLERQLEELEAQLEELES 330

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 325974489   328 NLELMTKRAVKAENHVMKLKQEVNLLQAQLSNFKRENEALRSGQGA 373
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 251-373 1.69e-04

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: 44.28  E-value: 1.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325974489   251 AAHEESLGDRHLRTLQLSYEALKDENSKLRRKLSEVQSFSETQTEMVRTLERKLE---AKMIKEESDFHDLESVVQQVEQ 327
Cdd:TIGR02168  251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQilrERLANLERQLEELEAQLEELES 330

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 325974489   328 NLELMTKRAVKAENHVMKLKQEVNLLQAQLSNFKRENEALRSGQGA 373
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
 259-363 2.97e-04

Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442818 [Multi-domain]  Cd Length: 125  Bit Score: 40.61  E-value: 2.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325974489 259 DRHLRTLQLSYEALKDENSKLRRKLS----EVQSFSETQTEMVRTLerkleaKMIKEESdfhdlESVVQQVEQNLELMTK 334
Cdd:COG3599   26 DEFLDEVAEDYERLIRENKELKEKLEeleeELEEYRELEETLQKTL------VVAQETA-----EEVKENAEKEAELIIK 94

                         90       100       110
                 ....*....|....*....|....*....|
gi 325974489 335 RA-VKAENHVMKLKQEVNLLQAQLSNFKRE 363
Cdd:COG3599   95 EAeLEAEKIIEEAQEKARKIVREIEELKRQ 124
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 252-357 5.01e-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: 5.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325974489  252 AHEESLGDRHLRTLQLSYEALKDENSKLRRKLSEVQSFSETQTEMVRTLERKLEakmikeesdfhdLESVVQQVEQNLEL 331
Cdd:pfam15619  95 AELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLE------------LENKSFRRQLAAEK 162

                          90       100
                  ....*....|....*....|....*.
gi 325974489  332 MTKRAVKAEnhVMKLKQEVNLLQAQL 357
Cdd:pfam15619 163 KKHKEAQEE--VKILQEEIERLQQKL 186
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 251-373 1.69e-04

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: 44.28  E-value: 1.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325974489   251 AAHEESLGDRHLRTLQLSYEALKDENSKLRRKLSEVQSFSETQTEMVRTLERKLE---AKMIKEESDFHDLESVVQQVEQ 327
Cdd:TIGR02168  251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQilrERLANLERQLEELEAQLEELES 330

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 325974489   328 NLELMTKRAVKAENHVMKLKQEVNLLQAQLSNFKRENEALRSGQGA 373
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
 259-363 2.97e-04

Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442818 [Multi-domain]  Cd Length: 125  Bit Score: 40.61  E-value: 2.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325974489 259 DRHLRTLQLSYEALKDENSKLRRKLS----EVQSFSETQTEMVRTLerkleaKMIKEESdfhdlESVVQQVEQNLELMTK 334
Cdd:COG3599   26 DEFLDEVAEDYERLIRENKELKEKLEeleeELEEYRELEETLQKTL------VVAQETA-----EEVKENAEKEAELIIK 94

                         90       100       110
                 ....*....|....*....|....*....|
gi 325974489 335 RA-VKAENHVMKLKQEVNLLQAQLSNFKRE 363
Cdd:COG3599   95 EAeLEAEKIIEEAQEKARKIVREIEELKRQ 124
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
256-432 3.37e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 3.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325974489 256 SLGDRHLRTLQLSYEALKDENSKLRRKLSEvqsfseTQTEMvrtleRKLEAKMIKEESDFHDLESVVQQVEQNLELMTKR 335
Cdd:COG4372   27 AALSEQLRKALFELDKLQEELEQLREELEQ------AREEL-----EQLEEELEQARSELEQLEEELEELNEQLQAAQAE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325974489 336 AVKAENHVMKLKQEVNLLQAQLSNFKRENEALRS------GQGASLTVVKQNTDVALQNLHVVMNSAHASIKQL------ 403
Cdd:COG4372   96 LAQAQEELESLQEEAEELQEELEELQKERQDLEQqrkqleAQIAELQSEIAEREEELKELEEQLESLQEELAALeqelqa 175

                        170       180
                 ....*....|....*....|....*....
gi 325974489 404 VSGAETLNLVAEILKSIDRITEVKDEADS 432
Cdd:COG4372  176 LSEAEAEQALDELLKEANRNAEKEEELAE 204
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 270-384 1.13e-03

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: 41.59  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325974489   270 EALKDENSKLRRKLSEVQSFSETQTEMVRTLERKL---EAKMIKEESDFHDLESVVQQVEQNLELMTKRAVKAENHVMKL 346
Cdd:TIGR02169  395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIagiEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 325974489   347 KQEVNLLQAQLSNFKRENEALRSGQGASLTVVKQNTDV 384
Cdd:TIGR02169  475 KEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV 512
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
259-365 1.31e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325974489 259 DRHLRTLQLSYEALKDENSKLRRKLSEVQSFSETQTEMVRTLERKLEAKMIKEESDFHDLESVVQQVEQNLELMTKRAVK 338
Cdd:COG4717  138 EAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217

                         90       100
                 ....*....|....*....|....*..
gi 325974489 339 AENHVMKLKQEVNLLQAQLSNFKRENE 365
Cdd:COG4717  218 AQEELEELEEELEQLENELEAAALEER 244
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 252-357 5.01e-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: 5.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325974489  252 AHEESLGDRHLRTLQLSYEALKDENSKLRRKLSEVQSFSETQTEMVRTLERKLEakmikeesdfhdLESVVQQVEQNLEL 331
Cdd:pfam15619  95 AELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLE------------LENKSFRRQLAAEK 162

                          90       100
                  ....*....|....*....|....*.
gi 325974489  332 MTKRAVKAEnhVMKLKQEVNLLQAQL 357
Cdd:pfam15619 163 KKHKEAQEE--VKILQEEIERLQQKL 186
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 259-430 5.94e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 39.03  E-value: 5.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325974489  259 DRHLRTLQLSYEALKDENSKLRRKLSEVQSFSETQT------EMVRTLERklEAKMIKEES-----DFHDLESVVQQVE- 326
Cdd:pfam10174 516 DSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRtnpeinDRIRLLEQ--EVARYKEESgkaqaEVERLLGILREVEn 593

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325974489  327 ---------QNLELMTKRAVKAEN-HVMKLK---QEVNLLQAQL--SNFKRENEALRSGQG-------ASLTVVKQNTDV 384
Cdd:pfam10174 594 ekndkdkkiAELESLTLRQMKEQNkKVANIKhgqQEMKKKGAQLleEARRREDNLADNSQQlqleelmGALEKTRQELDA 673

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 325974489  385 ALQNLHVVMNSAHASIKQLVsgaetlNLVAEILKSIDRITEVKDEA 430
Cdd:pfam10174 674 TKARLSSTQQSLAEKDGHLT------NLRAERRKQLEEILEMKQEA 713
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 251-358 7.05e-03

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 36.91  E-value: 7.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325974489  251 AAHEESLGDRHLRT------LQLSYEALKDENSKLRRKLSEVQSFSETQTEMVRTLERKLeaKMIKEEsdFHDLESVVQQ 324
Cdd:pfam11559  51 LEFRESLNETIRTLeaeierLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKL--KNEKEE--LQRLKNALQQ 126

                          90       100       110
                  ....*....|....*....|....*....|....
gi 325974489  325 veqnlelmtkRAVKAENHVMKLKQEVNLLQAQLS 358
Cdd:pfam11559 127 ----------IKTQFAHEVKKRDREIEKLKERLA 150
Rabaptin pfam03528
Rabaptin;
270-358 8.80e-03

Rabaptin;


Pssm-ID: 367545 [Multi-domain]  Cd Length: 486  Bit Score: 38.16  E-value: 8.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325974489  270 EALKDENSKLRRKLSEVQSfsetqtemvrtlERKLEAKMIKEESDFHDLESVVQQVEQNLELMTKRAVKAENHVMKLK-- 347
Cdd:pfam03528 140 ESAEREIADLRRRLSEGQE------------EENLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKELEas 207

                          90
                  ....*....|....
gi 325974489  348 --QEVN-LLQAQLS 358
Cdd:pfam03528 208 kmKELNhYLEAEKS 221
 
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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