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Conserved domains on  [gi|2006390164|ref|XP_039945788|]
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Golgi membrane protein 1 [Hirundo rustica]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
18-278 2.98e-06

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


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.99  E-value: 2.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390164  18 MAALVACIIVLGFNYWIANSRSMDLQGRVMDLEGKVRRAAAERGAVEQKKNEFQGELEKQRQQIDkiqslhsfQMENANR 97
Cdd:COG4942     1 MRKLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA--------ALARRIR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390164  98 AHQEEKAILVSNITVNDRLIQSLREHLKDLQTEYGKlQLDVYSFQKNQTNLQRKFS----YDLSQCINQMKELKEQCEER 173
Cdd:COG4942    73 ALEQELAALEAELAELEKEIAELRAELEAQKEELAE-LLRALYRLGRQPPLALLLSpedfLDAVRRLQYLKYLAPARREQ 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390164 174 IDELTKKSSGIPQIKEykgfTEDSQVDTPLPALKQAGFKQDDLEQEKKS-EDIPKAVPTVRKTDLEQAEERTDSLTDIRK 252
Cdd:COG4942   152 AEELRADLAELAALRA----ELEAERAELEALLAELEEERAALEALKAErQKLLARLEKELAELAAELAELQQEAEELEA 227
                         250       260
                  ....*....|....*....|....*.
gi 2006390164 253 QGRKAEEEQLSSQLDKPQESLKAAAG 278
Cdd:COG4942   228 LIARLEAEAAAAAERTPAAGFAALKG 253
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
18-278 2.98e-06

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: 48.99  E-value: 2.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390164  18 MAALVACIIVLGFNYWIANSRSMDLQGRVMDLEGKVRRAAAERGAVEQKKNEFQGELEKQRQQIDkiqslhsfQMENANR 97
Cdd:COG4942     1 MRKLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA--------ALARRIR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390164  98 AHQEEKAILVSNITVNDRLIQSLREHLKDLQTEYGKlQLDVYSFQKNQTNLQRKFS----YDLSQCINQMKELKEQCEER 173
Cdd:COG4942    73 ALEQELAALEAELAELEKEIAELRAELEAQKEELAE-LLRALYRLGRQPPLALLLSpedfLDAVRRLQYLKYLAPARREQ 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390164 174 IDELTKKSSGIPQIKEykgfTEDSQVDTPLPALKQAGFKQDDLEQEKKS-EDIPKAVPTVRKTDLEQAEERTDSLTDIRK 252
Cdd:COG4942   152 AEELRADLAELAALRA----ELEAERAELEALLAELEEERAALEALKAErQKLLARLEKELAELAAELAELQQEAEELEA 227
                         250       260
                  ....*....|....*....|....*.
gi 2006390164 253 QGRKAEEEQLSSQLDKPQESLKAAAG 278
Cdd:COG4942   228 LIARLEAEAAAAAERTPAAGFAALKG 253
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
41-267 9.68e-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: 41.59  E-value: 9.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390164   41 DLQGRVMDLEGKVRRAAAERGAVEQKKNEFQGELEKQRQQIDKIQSlhsfqmENANRahQEEKAILVSNITVNDRLIQSL 120
Cdd:TIGR02169  312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTE------EYAEL--KEELEDLRAELEEVDKEFAET 383
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390164  121 REHLKDLQTEYGKLQLDVYSFQKNQTNLQ---RKFSYDLSQCINQMK-------ELKEQCEERIDELTKKSSGIPQIKEY 190
Cdd:TIGR02169  384 RDELKDYREKLEKLKREINELKRELDRLQeelQRLSEELADLNAAIAgieakinELEEEKEDKALEIKKQEWKLEQLAAD 463
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006390164  191 KGFTEDSqvdtpLPALKQagfKQDDLEQEKKSedipkavptvRKTDLEQAEERTDSLTDiRKQGRKAEEEQLSSQLD 267
Cdd:TIGR02169  464 LSKYEQE-----LYDLKE---EYDRVEKELSK----------LQRELAEAEAQARASEE-RVRGGRAVEEVLKASIQ 521
sdhA PRK08641
succinate dehydrogenase flavoprotein subunit; Reviewed
70-146 7.45e-03

succinate dehydrogenase flavoprotein subunit; Reviewed


Pssm-ID: 236319 [Multi-domain]  Cd Length: 589  Bit Score: 38.42  E-value: 7.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390164  70 FQGELEKQRQQIDKIQSLHsfQMENANRAHQEEKAILVSNITV---NDRLIQSLrEHLKDLQTEYGKLQLDVYSFQKNQT 146
Cdd:PRK08641  425 FEQALKQEQEKFDNILSMD--GTENAYVLHKELGEWMTDNVTVvreNDKLLETD-EKIQELMERYKRISVNDTSRWSNQG 501
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
18-278 2.98e-06

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: 48.99  E-value: 2.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390164  18 MAALVACIIVLGFNYWIANSRSMDLQGRVMDLEGKVRRAAAERGAVEQKKNEFQGELEKQRQQIDkiqslhsfQMENANR 97
Cdd:COG4942     1 MRKLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA--------ALARRIR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390164  98 AHQEEKAILVSNITVNDRLIQSLREHLKDLQTEYGKlQLDVYSFQKNQTNLQRKFS----YDLSQCINQMKELKEQCEER 173
Cdd:COG4942    73 ALEQELAALEAELAELEKEIAELRAELEAQKEELAE-LLRALYRLGRQPPLALLLSpedfLDAVRRLQYLKYLAPARREQ 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390164 174 IDELTKKSSGIPQIKEykgfTEDSQVDTPLPALKQAGFKQDDLEQEKKS-EDIPKAVPTVRKTDLEQAEERTDSLTDIRK 252
Cdd:COG4942   152 AEELRADLAELAALRA----ELEAERAELEALLAELEEERAALEALKAErQKLLARLEKELAELAAELAELQQEAEELEA 227
                         250       260
                  ....*....|....*....|....*.
gi 2006390164 253 QGRKAEEEQLSSQLDKPQESLKAAAG 278
Cdd:COG4942   228 LIARLEAEAAAAAERTPAAGFAALKG 253
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
41-267 9.68e-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: 41.59  E-value: 9.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390164   41 DLQGRVMDLEGKVRRAAAERGAVEQKKNEFQGELEKQRQQIDKIQSlhsfqmENANRahQEEKAILVSNITVNDRLIQSL 120
Cdd:TIGR02169  312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTE------EYAEL--KEELEDLRAELEEVDKEFAET 383
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390164  121 REHLKDLQTEYGKLQLDVYSFQKNQTNLQ---RKFSYDLSQCINQMK-------ELKEQCEERIDELTKKSSGIPQIKEY 190
Cdd:TIGR02169  384 RDELKDYREKLEKLKREINELKRELDRLQeelQRLSEELADLNAAIAgieakinELEEEKEDKALEIKKQEWKLEQLAAD 463
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006390164  191 KGFTEDSqvdtpLPALKQagfKQDDLEQEKKSedipkavptvRKTDLEQAEERTDSLTDiRKQGRKAEEEQLSSQLD 267
Cdd:TIGR02169  464 LSKYEQE-----LYDLKE---EYDRVEKELSK----------LQRELAEAEAQARASEE-RVRGGRAVEEVLKASIQ 521
sdhA PRK08641
succinate dehydrogenase flavoprotein subunit; Reviewed
70-146 7.45e-03

succinate dehydrogenase flavoprotein subunit; Reviewed


Pssm-ID: 236319 [Multi-domain]  Cd Length: 589  Bit Score: 38.42  E-value: 7.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006390164  70 FQGELEKQRQQIDKIQSLHsfQMENANRAHQEEKAILVSNITV---NDRLIQSLrEHLKDLQTEYGKLQLDVYSFQKNQT 146
Cdd:PRK08641  425 FEQALKQEQEKFDNILSMD--GTENAYVLHKELGEWMTDNVTVvreNDKLLETD-EKIQELMERYKRISVNDTSRWSNQG 501
 
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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