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Conserved domains on  [gi|55925267|ref|NP_001007365|]
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coatomer subunit epsilon [Danio rerio]

Protein Classification

coatomer subunit epsilon( domain architecture ID 12057363)

coatomer subunit epsilon, a component of the coatomer complex, which is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins

CATH:  1.25.40.10
Gene Ontology:  GO:0015031|GO:0005198|GO:0006888
PubMed:  20579721
SCOP:  4001344

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Coatomer_E pfam04733
Coatomer epsilon subunit; This family represents the epsilon subunit of the coatomer complex, ...
9-297 4.41e-141

Coatomer epsilon subunit; This family represents the epsilon subunit of the coatomer complex, which is involved in the regulation of intracellular protein trafficking between the endoplasmic reticulum and the Golgi complex.


:

Pssm-ID: 398419 [Multi-domain]  Cd Length: 288  Bit Score: 399.16  E-value: 4.41e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925267     9 DELFDVKNAFYIGSYQHCINEAQkVKTSGPEKESEKNIFLYRAYIAQRKYGVVLDDIKPSSTEELQAVRMFAEYLSSEGK 88
Cdd:pfam04733   1 DELFNVRNYFYLGNYQKAINESD-VTSLSEEALVERDVYMYRSYLALGSYQIVISEIKESAATPLQAVRLLAEYLNSPSR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925267    89 RDAIVADLDKKISKSVDVSNTTFLLMAASIYLHEMNTDAALRTLHQGESLECMAMTVQILLKLDRVDMARKELKKMQDQD 168
Cdd:pfam04733  80 KESILASLKEWVADSHIGSNSTLRLLAAIIFIHEGDFDDALKHLHKGENLEAMALNVQILLKMHRIDLAEQQLKKMQQID 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925267   169 EDATLTQLATAWVNLAIGGEKLQDAFYIFQEMSDKYSPTLLLLNGQAASHMAQNKWDEAESVLQDALDKDSGHPETLINL 248
Cdd:pfam04733 160 EDATLTQLANAWVKLAVGGEKIQDAYYIFQEFSEKYDSTPLLLNGQAVCCMCLGRYEEAESLLKEALDKDAKDPETLINL 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 55925267   249 IVLTQHMGKPFEVTNRYLSQLKDAHKSHPFIKDYLAKKNEFDRLVMQYA 297
Cdd:pfam04733 240 VVCALHLGKPAEVSNRNLSQLKLSHPTHPLVKDLNEKEAEFDRAVQQFA 288
 
Name Accession Description Interval E-value
Coatomer_E pfam04733
Coatomer epsilon subunit; This family represents the epsilon subunit of the coatomer complex, ...
9-297 4.41e-141

Coatomer epsilon subunit; This family represents the epsilon subunit of the coatomer complex, which is involved in the regulation of intracellular protein trafficking between the endoplasmic reticulum and the Golgi complex.


Pssm-ID: 398419 [Multi-domain]  Cd Length: 288  Bit Score: 399.16  E-value: 4.41e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925267     9 DELFDVKNAFYIGSYQHCINEAQkVKTSGPEKESEKNIFLYRAYIAQRKYGVVLDDIKPSSTEELQAVRMFAEYLSSEGK 88
Cdd:pfam04733   1 DELFNVRNYFYLGNYQKAINESD-VTSLSEEALVERDVYMYRSYLALGSYQIVISEIKESAATPLQAVRLLAEYLNSPSR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925267    89 RDAIVADLDKKISKSVDVSNTTFLLMAASIYLHEMNTDAALRTLHQGESLECMAMTVQILLKLDRVDMARKELKKMQDQD 168
Cdd:pfam04733  80 KESILASLKEWVADSHIGSNSTLRLLAAIIFIHEGDFDDALKHLHKGENLEAMALNVQILLKMHRIDLAEQQLKKMQQID 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925267   169 EDATLTQLATAWVNLAIGGEKLQDAFYIFQEMSDKYSPTLLLLNGQAASHMAQNKWDEAESVLQDALDKDSGHPETLINL 248
Cdd:pfam04733 160 EDATLTQLANAWVKLAVGGEKIQDAYYIFQEFSEKYDSTPLLLNGQAVCCMCLGRYEEAESLLKEALDKDAKDPETLINL 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 55925267   249 IVLTQHMGKPFEVTNRYLSQLKDAHKSHPFIKDYLAKKNEFDRLVMQYA 297
Cdd:pfam04733 240 VVCALHLGKPAEVSNRNLSQLKLSHPTHPLVKDLNEKEAEFDRAVQQFA 288
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
146-277 6.81e-06

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 44.80  E-value: 6.81e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925267 146 QILLKLDRVDMARKELKKMQDQDEDATLTQLATAWVNLAIGgeKLQDAFYIFQEMSDKYSPTLLLLNGQAASHMAQNKWD 225
Cdd:COG4783  12 QALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLG--DLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYD 89
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 55925267 226 EAESVLQDALDKDSGHPETLINLIVLTQHMGKPFEvtnrYLSQLKDAHKSHP 277
Cdd:COG4783  90 EALALLEKALKLDPEHPEAYLRLARAYRALGRPDE----AIAALEKALELDP 137
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
95-284 3.94e-05

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 45.07  E-value: 3.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925267    95 DLDKKISKSVDVSNT-----TFLLMAASIYLHEMNTDAALRTLH-----QGESLECMAMTVQILLKLDRVDMARKELKKM 164
Cdd:TIGR02917 582 QLKKALAILNEAADAapdspEAWLMLGRAQLAAGDLNKAVSSFKkllalQPDSALALLLLADAYAVMKNYAKAITSLKRA 661
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925267   165 QDQDEDATLTQLATAwvNLAIGGEKLQDAFYIFQEMSDKYSPTLLLLNGQAASHMAQNKWDEAESVLQDALdKDSGHPET 244
Cdd:TIGR02917 662 LELKPDNTEAQIGLA--QLLLAAKRTESAKKIAKSLQKQHPKAALGFELEGDLYLRQKDYPAAIQAYRKAL-KRAPSSQN 738
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 55925267   245 LINLIVLTQHMGKPFEVTNRYLSQLKDaHKSHPFIKDYLA 284
Cdd:TIGR02917 739 AIKLHRALLASGNTAEAVKTLEAWLKT-HPNDAVLRTALA 777
 
Name Accession Description Interval E-value
Coatomer_E pfam04733
Coatomer epsilon subunit; This family represents the epsilon subunit of the coatomer complex, ...
9-297 4.41e-141

Coatomer epsilon subunit; This family represents the epsilon subunit of the coatomer complex, which is involved in the regulation of intracellular protein trafficking between the endoplasmic reticulum and the Golgi complex.


Pssm-ID: 398419 [Multi-domain]  Cd Length: 288  Bit Score: 399.16  E-value: 4.41e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925267     9 DELFDVKNAFYIGSYQHCINEAQkVKTSGPEKESEKNIFLYRAYIAQRKYGVVLDDIKPSSTEELQAVRMFAEYLSSEGK 88
Cdd:pfam04733   1 DELFNVRNYFYLGNYQKAINESD-VTSLSEEALVERDVYMYRSYLALGSYQIVISEIKESAATPLQAVRLLAEYLNSPSR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925267    89 RDAIVADLDKKISKSVDVSNTTFLLMAASIYLHEMNTDAALRTLHQGESLECMAMTVQILLKLDRVDMARKELKKMQDQD 168
Cdd:pfam04733  80 KESILASLKEWVADSHIGSNSTLRLLAAIIFIHEGDFDDALKHLHKGENLEAMALNVQILLKMHRIDLAEQQLKKMQQID 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925267   169 EDATLTQLATAWVNLAIGGEKLQDAFYIFQEMSDKYSPTLLLLNGQAASHMAQNKWDEAESVLQDALDKDSGHPETLINL 248
Cdd:pfam04733 160 EDATLTQLANAWVKLAVGGEKIQDAYYIFQEFSEKYDSTPLLLNGQAVCCMCLGRYEEAESLLKEALDKDAKDPETLINL 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 55925267   249 IVLTQHMGKPFEVTNRYLSQLKDAHKSHPFIKDYLAKKNEFDRLVMQYA 297
Cdd:pfam04733 240 VVCALHLGKPAEVSNRNLSQLKLSHPTHPLVKDLNEKEAEFDRAVQQFA 288
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
146-277 6.81e-06

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 44.80  E-value: 6.81e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925267 146 QILLKLDRVDMARKELKKMQDQDEDATLTQLATAWVNLAIGgeKLQDAFYIFQEMSDKYSPTLLLLNGQAASHMAQNKWD 225
Cdd:COG4783  12 QALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLG--DLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYD 89
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 55925267 226 EAESVLQDALDKDSGHPETLINLIVLTQHMGKPFEvtnrYLSQLKDAHKSHP 277
Cdd:COG4783  90 EALALLEKALKLDPEHPEAYLRLARAYRALGRPDE----AIAALEKALELDP 137
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
146-285 3.31e-05

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 44.72  E-value: 3.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925267 146 QILLKLDRVDMARKELKKMQDQDEDATLTQLATAwvNLAIGGEKLQDAFYIFQEMSDKYSPTLLLLNGQAASHMAQNKWD 225
Cdd:COG2956  16 LNYLLNGQPDKAIDLLEEALELDPETVEAHLALG--NLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLD 93
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925267 226 EAESVLQDALDKDSGHPETLINLIVLTQHMGKpFEVTNRYLSQLKDAHKSHPFIKDYLAK 285
Cdd:COG2956  94 RAEELLEKLLELDPDDAEALRLLAEIYEQEGD-WEKAIEVLERLLKLGPENAHAYCELAE 152
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
95-284 3.94e-05

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 45.07  E-value: 3.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925267    95 DLDKKISKSVDVSNT-----TFLLMAASIYLHEMNTDAALRTLH-----QGESLECMAMTVQILLKLDRVDMARKELKKM 164
Cdd:TIGR02917 582 QLKKALAILNEAADAapdspEAWLMLGRAQLAAGDLNKAVSSFKkllalQPDSALALLLLADAYAVMKNYAKAITSLKRA 661
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925267   165 QDQDEDATLTQLATAwvNLAIGGEKLQDAFYIFQEMSDKYSPTLLLLNGQAASHMAQNKWDEAESVLQDALdKDSGHPET 244
Cdd:TIGR02917 662 LELKPDNTEAQIGLA--QLLLAAKRTESAKKIAKSLQKQHPKAALGFELEGDLYLRQKDYPAAIQAYRKAL-KRAPSSQN 738
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 55925267   245 LINLIVLTQHMGKPFEVTNRYLSQLKDaHKSHPFIKDYLA 284
Cdd:TIGR02917 739 AIKLHRALLASGNTAEAVKTLEAWLKT-HPNDAVLRTALA 777
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
104-293 7.58e-05

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 43.56  E-value: 7.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925267 104 VDVSNTTFLLMAASIYLHEMNTDAALRTLHQ-----GESLECMAMTVQILLKLDRVDMARKELKKMQDQDEDATltQLAT 178
Cdd:COG2956  37 LDPETVEAHLALGNLYRRRGEYDRAIRIHQKllerdPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDA--EALR 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925267 179 AWVNLAIGGEKLQDAFYIFQEMSDKYSPTLLLLNGQAASHMAQNKWDEAESVLQDALDKDSGHPETLINLIVLTQHMGKP 258
Cdd:COG2956 115 LLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDY 194
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 55925267 259 ---FEVTNRYLSQLKDAHKSHPFIKDYLAKKNEFDRLV 293
Cdd:COG2956 195 eeaIAALERALEQDPDYLPALPRLAELYEKLGDPEEAL 232
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
112-257 1.67e-03

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 39.98  E-value: 1.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925267 112 LLMAASIYLHEMNTDAALRTLHQGESLECMAMTVQILLKLDRVDMARKELKKMQDQDEDatltqLATAWVNLA---IGGE 188
Cdd:COG3914  52 AEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALNPD-----NAEALFNLGnllLALG 126
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55925267 189 KLQDAFYIFQ---EMSDKYSPTLLLLngqAASHMAQNKWDEAESVLQDALDKDSGHPETLINLIVLTQHMGK 257
Cdd:COG3914 127 RLEEALAALRralALNPDFAEAYLNL---GEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGR 195
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
108-238 6.53e-03

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 37.40  E-value: 6.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925267 108 NTTFLLMAASIYLHEMNTDAALRTLHQG-----ESLECMAMTVQILLKLDRVDMARKELKKMQDQDEDATLTQLATAWVN 182
Cdd:COG2956 143 NAHAYCELAELYLEQGDYDEAIEALEKAlkldpDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELY 222
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 55925267 183 LAIGgeKLQDAFYIFQEMSDKYsPTLLLLNGQAASHMAQNKWDEAESVLQDALDKD 238
Cdd:COG2956 223 EKLG--DPEEALELLRKALELD-PSDDLLLALADLLERKEGLEAALALLERQLRRH 275
 
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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