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Conserved domains on  [gi|2069553499|ref|XP_042326778|]
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conserved oligomeric Golgi complex subunit 5 [Sceloporus undulatus]

Protein Classification

conserved oligomeric Golgi complex subunit 5( domain architecture ID 10564031)

conserved oligomeric Golgi complex subunit 5 (COG5) is a component of the conserved oligomeric Golgi complex (COG), and is required for normal Golgi function

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG5 pfam10392
Golgi transport complex subunit 5; The COG complex, the peripheral membrane oligomeric protein ...
66-188 3.29e-36

Golgi transport complex subunit 5; The COG complex, the peripheral membrane oligomeric protein complex involved in intra-Golgi protein trafficking, consists of eight subunits arranged in two lobes bridged by Cog1. Cog5 is in the smaller, B lobe, bound in with Cog6-8, and is itself bound to Cog1 as well as, strongly, to Cog7.


:

Pssm-ID: 192566  Cd Length: 132  Bit Score: 133.20  E-value: 3.29e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069553499  66 DFLREDFDVKAYTSQSIHQA--------VIAEQLAKLAQGISQLDKELHLQVVARHEDLLAQATGIESLEGVLQMMQTRI 137
Cdd:pfam10392   2 AFLDPDFDPKSFANALLLATnnnddtplDLSTPLKRLNYDIQELDRRIRTLITSNHLELLSHLSSIKSASSILSTLKSSL 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2069553499 138 SALQSTVDRIRAKIVDPYNKIVSRTEQLARLQAACDLLRRIIRILYLSKRL 188
Cdd:pfam10392  82 EYLSASYERLKSDVLEPYERALKLQSALKRLHQTTDLLRALLRFLHLSRQL 132
 
Name Accession Description Interval E-value
COG5 pfam10392
Golgi transport complex subunit 5; The COG complex, the peripheral membrane oligomeric protein ...
66-188 3.29e-36

Golgi transport complex subunit 5; The COG complex, the peripheral membrane oligomeric protein complex involved in intra-Golgi protein trafficking, consists of eight subunits arranged in two lobes bridged by Cog1. Cog5 is in the smaller, B lobe, bound in with Cog6-8, and is itself bound to Cog1 as well as, strongly, to Cog7.


Pssm-ID: 192566  Cd Length: 132  Bit Score: 133.20  E-value: 3.29e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069553499  66 DFLREDFDVKAYTSQSIHQA--------VIAEQLAKLAQGISQLDKELHLQVVARHEDLLAQATGIESLEGVLQMMQTRI 137
Cdd:pfam10392   2 AFLDPDFDPKSFANALLLATnnnddtplDLSTPLKRLNYDIQELDRRIRTLITSNHLELLSHLSSIKSASSILSTLKSSL 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2069553499 138 SALQSTVDRIRAKIVDPYNKIVSRTEQLARLQAACDLLRRIIRILYLSKRL 188
Cdd:pfam10392  82 EYLSASYERLKSDVLEPYERALKLQSALKRLHQTTDLLRALLRFLHLSRQL 132
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
88-248 1.00e-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: 42.44  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069553499  88 AEQLAKLAQGISQLDKELhlqvvARHEDLLAQATG-IESLEGVLQMMQTRISALQSTVDRIRAKIVDPYNKIVSRTEQLA 166
Cdd:COG4942    19 ADAAAEAEAELEQLQQEI-----AELEKELAALKKeEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069553499 167 RLQAA----CDLLRRIIRILYLSKRLQG-QLQGGSREITKAAQSLNELDYLSQGiDLSGIEVIENDLLFIARARLEVENQ 241
Cdd:COG4942    94 ELRAEleaqKEELAELLRALYRLGRQPPlALLLSPEDFLDAVRRLQYLKYLAPA-RREQAEELRADLAELAALRAELEAE 172

                  ....*..
gi 2069553499 242 AKRLLEQ 248
Cdd:COG4942   173 RAELEAL 179
 
Name Accession Description Interval E-value
COG5 pfam10392
Golgi transport complex subunit 5; The COG complex, the peripheral membrane oligomeric protein ...
66-188 3.29e-36

Golgi transport complex subunit 5; The COG complex, the peripheral membrane oligomeric protein complex involved in intra-Golgi protein trafficking, consists of eight subunits arranged in two lobes bridged by Cog1. Cog5 is in the smaller, B lobe, bound in with Cog6-8, and is itself bound to Cog1 as well as, strongly, to Cog7.


Pssm-ID: 192566  Cd Length: 132  Bit Score: 133.20  E-value: 3.29e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069553499  66 DFLREDFDVKAYTSQSIHQA--------VIAEQLAKLAQGISQLDKELHLQVVARHEDLLAQATGIESLEGVLQMMQTRI 137
Cdd:pfam10392   2 AFLDPDFDPKSFANALLLATnnnddtplDLSTPLKRLNYDIQELDRRIRTLITSNHLELLSHLSSIKSASSILSTLKSSL 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2069553499 138 SALQSTVDRIRAKIVDPYNKIVSRTEQLARLQAACDLLRRIIRILYLSKRL 188
Cdd:pfam10392  82 EYLSASYERLKSDVLEPYERALKLQSALKRLHQTTDLLRALLRFLHLSRQL 132
Vps51 pfam08700
Vps51/Vps67; This family includes a presumed domain found in a number of components of ...
70-149 7.11e-13

Vps51/Vps67; This family includes a presumed domain found in a number of components of vesicular transport. The VFT tethering complex (also known as GARP complex, Golgi associated retrograde protein complex, Vps53 tethering complex) is a conserved eukaryotic docking complex which is involved recycling of proteins from endosomes to the late Golgi. Vps51 (also known as Vps67) is a subunit of VFT and interacts with the SNARE Tlg1. Cog1_N is the N-terminus of the Cog1 subunit of the eight-unit Conserved Oligomeric Golgi (COG) complex that participates in retrograde vesicular transport and is required to maintain normal Golgi structure and function. The subunits are located in two lobes and Cog1 serves to bind the two lobes together probably via the highly conserved N-terminal domain of approximately 85 residues.


Pssm-ID: 462568  Cd Length: 86  Bit Score: 64.99  E-value: 7.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069553499  70 EDFDVKAYTSQSIHQAVIAE---QLAKLAQGISQLDKELHLQVVARHEDLLAQATGIESLEGVLQMMQTRISALQSTVDR 146
Cdd:pfam08700   4 PSFDADRYVSELLSKATLEEllqFESSLRSEIERLDSELKQLVYDNYRDLIKAADTISKMKSEMEQLSQKLSELKQALSK 83

                  ...
gi 2069553499 147 IRA 149
Cdd:pfam08700  84 IAS 86
COG2 pfam06148
COG (conserved oligomeric Golgi) complex component, COG2; The COG complex comprises eight ...
66-181 6.18e-04

COG (conserved oligomeric Golgi) complex component, COG2; The COG complex comprises eight proteins COG1-8. The COG complex plays critical roles in Golgi structure and function. The proposed function of the complex is to mediate the initial physical contact between transport vesicles and their membrane targets. A comparable role in tethering vesicles has been suggested for at least six additional large multisubunit complexes, including the exocyst, a complex that mediates trafficking to the plasma membrane. COG2 structure reveals a six-helix bundle with few conserved surface features but a general resemblance to recently determined crystal structures of four different exocyst subunits. These bundles inCOG2 may act as platforms for interaction with other trafficing proteins including SNAREs (soluble N-ethylmaleimide factor attachment protein receptors) and Rabs.


Pssm-ID: 399271  Cd Length: 133  Bit Score: 40.71  E-value: 6.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069553499  66 DFLREDFDVKAYTSQSIHQAVIAEQLAKLAQGISQLDKELhLQVVAR-HEDLLAQATGIESLEGVLQMMQTRISALQSTV 144
Cdd:pfam06148   7 EFLAPDFDPDAFVSELRHHVPLESLRRDLRAYLKLLRREL-LELVNEdYADFVSLSTNLVGLDEKLNEVEVPLLALRKEV 85
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2069553499 145 DRIRAKIVDPYNKIVSRTEQLARLQAACDLLRRIIRI 181
Cdd:pfam06148  86 ESVRDELEARLEEVEQKLEERKALREKRESLKLLLDY 122
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
88-248 1.00e-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: 42.44  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069553499  88 AEQLAKLAQGISQLDKELhlqvvARHEDLLAQATG-IESLEGVLQMMQTRISALQSTVDRIRAKIVDPYNKIVSRTEQLA 166
Cdd:COG4942    19 ADAAAEAEAELEQLQQEI-----AELEKELAALKKeEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069553499 167 RLQAA----CDLLRRIIRILYLSKRLQG-QLQGGSREITKAAQSLNELDYLSQGiDLSGIEVIENDLLFIARARLEVENQ 241
Cdd:COG4942    94 ELRAEleaqKEELAELLRALYRLGRQPPlALLLSPEDFLDAVRRLQYLKYLAPA-RREQAEELRADLAELAALRAELEAE 172

                  ....*..
gi 2069553499 242 AKRLLEQ 248
Cdd:COG4942   173 RAELEAL 179
 
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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