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Conserved domains on  [gi|19920832|ref|NP_609037|]
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coat protein (coatomer) epsilon [Drosophila melanogaster]

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, ...
12-296 1.65e-149

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: 420.73  E-value: 1.65e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920832    12 SVLFDARNEYYIGNFMGSIN--FVLPEQGTAGPELLSYMYLSYLAIDSGRIVASDIKEGNSTPLQALRLVHEAFEQPSRT 89
Cdd:pfam04733   1 DELFNVRNYFYLGNYQKAINesDVTSLSEEALVERDVYMYRSYLALGSYQIVISEIKESAATPLQAVRLLAEYLNSPSRK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920832    90 EELLEKLTDKVAGEEDETN-IWHLATAIVYCHDGQFENALKILHGSTNLESMALSVQCLLRLQRVDLAKQLVAKMQEISD 168
Cdd:pfam04733  81 ESILASLKEWVADSHIGSNsTLRLLAAIIFIHEGDFDDALKHLHKGENLEAMALNVQILLKMHRIDLAEQQLKKMQQIDE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920832   169 DATLTQLAQAWVALAQGTEQMQDAFHIYQEFCEKFKPTPALLNGQAVVHLGLERYEEADSVLRESLLKKHNDYDTLINLM 248
Cdd:pfam04733 161 DATLTQLANAWVKLAVGGEKIQDAYYIFQEFSEKYDSTPLLLNGQAVCCMCLGRYEEAESLLKEALDKDAKDPETLINLV 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 19920832   249 VHAHLTGKPTEAITRNLEQLRQFYPKSDFVTDLDKKSAEFDRLCLQYD 296
Cdd:pfam04733 241 VCALHLGKPAEVSNRNLSQLKLSHPTHPLVKDLNEKEAEFDRAVQQFA 288
 
Name Accession Description Interval E-value
Coatomer_E pfam04733
Coatomer epsilon subunit; This family represents the epsilon subunit of the coatomer complex, ...
12-296 1.65e-149

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: 420.73  E-value: 1.65e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920832    12 SVLFDARNEYYIGNFMGSIN--FVLPEQGTAGPELLSYMYLSYLAIDSGRIVASDIKEGNSTPLQALRLVHEAFEQPSRT 89
Cdd:pfam04733   1 DELFNVRNYFYLGNYQKAINesDVTSLSEEALVERDVYMYRSYLALGSYQIVISEIKESAATPLQAVRLLAEYLNSPSRK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920832    90 EELLEKLTDKVAGEEDETN-IWHLATAIVYCHDGQFENALKILHGSTNLESMALSVQCLLRLQRVDLAKQLVAKMQEISD 168
Cdd:pfam04733  81 ESILASLKEWVADSHIGSNsTLRLLAAIIFIHEGDFDDALKHLHKGENLEAMALNVQILLKMHRIDLAEQQLKKMQQIDE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920832   169 DATLTQLAQAWVALAQGTEQMQDAFHIYQEFCEKFKPTPALLNGQAVVHLGLERYEEADSVLRESLLKKHNDYDTLINLM 248
Cdd:pfam04733 161 DATLTQLANAWVKLAVGGEKIQDAYYIFQEFSEKYDSTPLLLNGQAVCCMCLGRYEEAESLLKEALDKDAKDPETLINLV 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 19920832   249 VHAHLTGKPTEAITRNLEQLRQFYPKSDFVTDLDKKSAEFDRLCLQYD 296
Cdd:pfam04733 241 VCALHLGKPAEVSNRNLSQLKLSHPTHPLVKDLNEKEAEFDRAVQQFA 288
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
73-270 9.25e-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: 43.18  E-value: 9.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920832  73 LQALRLVHEAFEQPSRTEELLEKLTDKvaGEEDETNIWHLATaiVYCHDGQFENALKILHGSTNLESMALSVQCLL---- 148
Cdd:COG2956  79 LLELAQDYLKAGLLDRAEELLEKLLEL--DPDDAEALRLLAE--IYEQEGDWEKAIEVLERLLKLGPENAHAYCELaely 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920832 149 -RLQRVDLAKQLVAKMQEISDDATLTQLAQAWVALAQGteQMQDAFHIYQEFCEKFKPTPALLNGQAVVHLGLERYEEAD 227
Cdd:COG2956 155 lEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQG--DYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEAL 232
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 19920832 228 SVLREsLLKKHNDYDTLINLMVHAHLTGKPTEAITRNLEQLRQ 270
Cdd:COG2956 233 ELLRK-ALELDPSDDLLLALADLLERKEGLEAALALLERQLRR 274
 
Name Accession Description Interval E-value
Coatomer_E pfam04733
Coatomer epsilon subunit; This family represents the epsilon subunit of the coatomer complex, ...
12-296 1.65e-149

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: 420.73  E-value: 1.65e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920832    12 SVLFDARNEYYIGNFMGSIN--FVLPEQGTAGPELLSYMYLSYLAIDSGRIVASDIKEGNSTPLQALRLVHEAFEQPSRT 89
Cdd:pfam04733   1 DELFNVRNYFYLGNYQKAINesDVTSLSEEALVERDVYMYRSYLALGSYQIVISEIKESAATPLQAVRLLAEYLNSPSRK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920832    90 EELLEKLTDKVAGEEDETN-IWHLATAIVYCHDGQFENALKILHGSTNLESMALSVQCLLRLQRVDLAKQLVAKMQEISD 168
Cdd:pfam04733  81 ESILASLKEWVADSHIGSNsTLRLLAAIIFIHEGDFDDALKHLHKGENLEAMALNVQILLKMHRIDLAEQQLKKMQQIDE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920832   169 DATLTQLAQAWVALAQGTEQMQDAFHIYQEFCEKFKPTPALLNGQAVVHLGLERYEEADSVLRESLLKKHNDYDTLINLM 248
Cdd:pfam04733 161 DATLTQLANAWVKLAVGGEKIQDAYYIFQEFSEKYDSTPLLLNGQAVCCMCLGRYEEAESLLKEALDKDAKDPETLINLV 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 19920832   249 VHAHLTGKPTEAITRNLEQLRQFYPKSDFVTDLDKKSAEFDRLCLQYD 296
Cdd:pfam04733 241 VCALHLGKPAEVSNRNLSQLKLSHPTHPLVKDLNEKEAEFDRAVQQFA 288
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
73-270 9.25e-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: 43.18  E-value: 9.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920832  73 LQALRLVHEAFEQPSRTEELLEKLTDKvaGEEDETNIWHLATaiVYCHDGQFENALKILHGSTNLESMALSVQCLL---- 148
Cdd:COG2956  79 LLELAQDYLKAGLLDRAEELLEKLLEL--DPDDAEALRLLAE--IYEQEGDWEKAIEVLERLLKLGPENAHAYCELaely 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920832 149 -RLQRVDLAKQLVAKMQEISDDATLTQLAQAWVALAQGteQMQDAFHIYQEFCEKFKPTPALLNGQAVVHLGLERYEEAD 227
Cdd:COG2956 155 lEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQG--DYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEAL 232
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 19920832 228 SVLREsLLKKHNDYDTLINLMVHAHLTGKPTEAITRNLEQLRQ 270
Cdd:COG2956 233 ELLRK-ALELDPSDDLLLALADLLERKEGLEAALALLERQLRR 274
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
145-275 2.24e-04

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: 40.56  E-value: 2.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920832 145 QCLLRLQRVDLAKQLVAKMQEISDDATLTQLAQAWVALAQGteQMQDAFHIYQEFCEKFKPTPALLNGQAVVHLGLERYE 224
Cdd:COG4783  12 QALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLG--DLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYD 89
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 19920832 225 EADSVLRESLLKKHNDYDTLINLMVHAHLTGKPTEAITRnLEQLRQFYPKS 275
Cdd:COG4783  90 EALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAA-LEKALELDPDD 139
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
154-276 3.71e-04

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 39.60  E-value: 3.71e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920832 154 DLAKQLVAKMQEISDDAtltqlaQAWVALAQ---GTEQMQDAFHIYQEFCEKFKPTPALLNGQAVVHLGLERYEEADSVL 230
Cdd:COG4235   1 EAIARLRQALAANPNDA------EGWLLLGRaylRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELL 74
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 19920832 231 RESLLKKHNDYDTLINLMVHAHLTGKPTEAITRnLEQLRQFYPKSD 276
Cdd:COG4235  75 ERALALDPDNPEALYLLGLAAFQQGDYAEAIAA-WQKLLALLPADA 119
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
125-273 1.10e-03

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 40.36  E-value: 1.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920832 125 ENALKILHGSTNLESMALSVQCLLRLQRVDLAKQLVAKMQEISDDATLTQLAQAWVALA-QGTEQMQDAFHIYQEFCEKF 203
Cdd:COG3914  29 AAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLlQALGRYEEALALYRRALALN 108
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920832 204 KPTPALLNGQAVVHLGLERYEEADSVLRESLLKKHNDYDTLINLMVHAHLTGKPTEAItRNLEQLRQFYP 273
Cdd:COG3914 109 PDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAI-AALRRALELDP 177
HemYx COG3071
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to ...
85-275 2.87e-03

Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to protoporphyrinogen oxidase HemY) [Function unknown];


Pssm-ID: 442305 [Multi-domain]  Cd Length: 323  Bit Score: 38.74  E-value: 2.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920832  85 QPSRTEELLEKLTDKVAGEEDETNI----WHLAtaivychDGQFENALKILH-----GSTNLESMALSVQCLLRLQR--- 152
Cdd:COG3071  65 DYERRDEYLAQALELAPEAELAVLLtraeLLLD-------QGQAEQALATLEalragAPRHPQVLRLLLQAYRQLGDwee 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920832 153 -VDLAKQLvAKMQEISDDATLTQLAQAWVALAQGTEQMQDAFH-IYQEFCEKFKPTPALLNGQAVVHLGLERYEEADSVL 230
Cdd:COG3071 138 lLELLPAL-RKHKALSAEEAQALERRAYLGLLRQAARDAEALKaLWKALPRAERRDPELAAAYARALIALGDHDEAERLL 216
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 19920832 231 RESLlkKHNDYDTLINLMVHAHLtGKPTEAITRnLEQLRQFYPKS 275
Cdd:COG3071 217 REAL--KRQWDPRLVRLYGRLQG-GDPAKQLKR-AEKWLKKHPND 257
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
62-237 6.06e-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: 37.79  E-value: 6.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920832  62 ASDIKEGNSTPLQALRLVHEAFEQPSRTEELLEKLTDKVAGEEDetniWHLATAIVYCHDGQFENALKIL-----HGSTN 136
Cdd:COG2956 102 LLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAH----AYCELAELYLEQGDYDEAIEALekalkLDPDC 177
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920832 137 LESMALSVQCLLRLQRVDLAKQLVAKMQEISDDATLTQLAQAWVALAQGteQMQDAFHIYQEFCEKfKPTPALLNGQAVV 216
Cdd:COG2956 178 ARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLG--DPEEALELLRKALEL-DPSDDLLLALADL 254
                       170       180
                ....*....|....*....|.
gi 19920832 217 HLGLERYEEADSVLRESLLKK 237
Cdd:COG2956 255 LERKEGLEAALALLERQLRRH 275
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
84-278 7.38e-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: 7.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920832  84 EQPSRTEELLEKLTdKVAGEEDETniwHLATAIVYCHDGQFENALKIL-----HGSTNLESMALSVQCLLRLQRVDLAKQ 158
Cdd:COG2956  22 GQPDKAIDLLEEAL-ELDPETVEA---HLALGNLYRRRGEYDRAIRIHqklleRDPDRAEALLELAQDYLKAGLLDRAEE 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920832 159 LVAKMQEISDDATltQLAQAWVALAQGTEQMQDAFHIYQEFCEKFKPTPALLNGQAVVHLGLERYEEADSVLRESLLKKH 238
Cdd:COG2956  98 LLEKLLELDPDDA--EALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDP 175
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 19920832 239 NDYDTLINLMVHAHLTGKPTEAItRNLEQLRQFYPKSDFV 278
Cdd:COG2956 176 DCARALLLLAELYLEQGDYEEAI-AALERALEQDPDYLPA 214
 
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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