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Conserved domains on  [gi|1353105|sp|P48563|]
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RecName: Full=Protein MON2

Protein Classification

MON2 family protein( domain architecture ID 11241880)

MON2 family protein may play a role in regulating membrane trafficking of cargo proteins, and may not have guanine nucleotide exchange (GEF) activity

CATH:  1.10.1000.11
Gene Ontology:  GO:0006895|GO:0015031
PubMed:  16219684
SCOP:  4001318

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
DCB pfam16213
dimerization and cyclophilin-binding domain of Mon2; DCB is the N-terminal domain of Mon2- and ...
8-176 3.39e-58

dimerization and cyclophilin-binding domain of Mon2; DCB is the N-terminal domain of Mon2- and GIG1-like proteins from metazoa. Mon2 and BIG1 like proteins play an important role in the cytoplasm-to-vacuole transport pathway and are required for Golgi homeostasis.


:

Pssm-ID: 465072 [Multi-domain]  Cd Length: 172  Bit Score: 198.25  E-value: 3.39e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353105       8 FDSMQRQLEAELRSLSSESKRRNSTIRHASDKSIEILKRVHSFEE-----LERHPDFALPFVLACQSRNAKMTTLAMQCL 82
Cdd:pfam16213    2 GSKLLEALQSDLRTLSSEAKRKYPPVKEASEKGILRLRTVHSSSPlmqnlLSASEDILKPFVLACETKNPKLVQIALGCL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353105      83 QGLSTVPSIPRSRLSEILDAFIEATHLAMEIQLKVLQVVPIFFKTYGkFIYGPLCKKLLLCCSNLLhvPNKAPVVVGTAS 162
Cdd:pfam16213   82 QKLISHDAISQSAAPYILDTLWMLMELGSEIELKVLQTVLLLITTNS-VIHGDTLAKALVLCFRLH--FSKDPTVQNTAS 158
                          170
                   ....*....|....
gi 1353105     163 ATLQQLIDEIFDRL 176
Cdd:pfam16213  159 ATLRQLVSVVFERV 172
Sec7_N pfam12783
Guanine nucleotide exchange factor in Golgi transport N-terminal; The full-length Sec7 ...
202-362 1.97e-37

Guanine nucleotide exchange factor in Golgi transport N-terminal; The full-length Sec7 functions proximally in the secretory pathway as a protein binding scaffold for the coat protein complexes COPII-COPI. The COPII-COPI-protein switch is necessary for maturation of the vesicular-tubular cluster, VTC, intermediate compartments for Golgi compartment biogenesis. This N-terminal domain however does not appear to be binding either of the COP or the ARF.


:

Pssm-ID: 463703  Cd Length: 154  Bit Score: 138.40  E-value: 1.97e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353105     202 YRYDANKLFDNICSLneisSNGAVSDEEMLLDIGDIPIDYGLEILESILKNSQKNLLECQDLQYLLRVKAIPLLLRCISS 281
Cdd:pfam12783    1 AAKDAFLVFRDLCKL----SNGKPLSKSDPKSHAERSKLFSLELIESILENHGDVFLKHPELLQLLKQYLCPSLLRNLSS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353105     282 SrHFSTAVRSCRCLKLLIRKeYLSILELELEVILSLLIHGIsVESNLSGWQRVLSLELFKDLSQDPEIVNTLYMDYDNYP 361
Cdd:pfam12783   77 S-SFPVFVRSLRIFLLLLRR-FRSHLKLEIEVFLSLLILPL-LESDSSLWQKALVLEVLRRLCSDPQLLVEIYLNYDCDL 153

                   .
gi 1353105     362 D 362
Cdd:pfam12783  154 G 154
Mon2_C super family cl24700
C-terminal region of Mon2 protein; Mon2 proteins are found from fungi to plants, to human and ...
936-1161 6.14e-12

C-terminal region of Mon2 protein; Mon2 proteins are found from fungi to plants, to human and is a scaffold protein involved in multiple aspects of endo membrane trafficking. This C-terminal region is essential for Mon2 activity.


The actual alignment was detected with superfamily member pfam16206:

Pssm-ID: 465066  Cd Length: 827  Bit Score: 70.92  E-value: 6.14e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353105     936 DFLQSLPMSVIKFVIDTLVNFVSQKRNLNISFSSISQFWLVGDYLRVRFNPETLNLSDEKRRSLSEKINNQKLIEIITSS 1015
Cdd:pfam16206    2 DFLPTMPCRCLPICIDTAAKFGLHNQELNISLTAIGLLWNISDFFFQRGEIIEKELNKEDAAMQKQAEDKAILLNRPEFP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353105    1016 SSHDWELYNGLWIYLLKNLINCTNDDRVEVKNGAVQTFFRIIDSHSVCF--PPWDLIFLEVIEPLL--TKEWST----EE 1087
Cdd:pfam16206   82 ATVKMPPFDCLWLCLYAKLGELCVDLRPAVRKSAGQTLFSTIGAHGSLLnhPTWHALIWKVLFNLLdnVRALSSsadkEK 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353105    1088 LENETDFINV-----------------TLQGLIKLYPEHFKDFKNNTTCAKEWSMLLDFLKRLLSSTSNNTKNAVILNYQ 1150
Cdd:pfam16206  162 IDAGGGNILIhhsrdtaekqwaetqvlTLAGVARIFNTKRELLQMLGDFERAWDLILDFIQNAALSKNGEVSLAALKSFQ 241
                          250
                   ....*....|.
gi 1353105    1151 TLLKEIITIED 1161
Cdd:pfam16206  242 EILQHNSPTED 252
 
Name Accession Description Interval E-value
DCB pfam16213
dimerization and cyclophilin-binding domain of Mon2; DCB is the N-terminal domain of Mon2- and ...
8-176 3.39e-58

dimerization and cyclophilin-binding domain of Mon2; DCB is the N-terminal domain of Mon2- and GIG1-like proteins from metazoa. Mon2 and BIG1 like proteins play an important role in the cytoplasm-to-vacuole transport pathway and are required for Golgi homeostasis.


Pssm-ID: 465072 [Multi-domain]  Cd Length: 172  Bit Score: 198.25  E-value: 3.39e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353105       8 FDSMQRQLEAELRSLSSESKRRNSTIRHASDKSIEILKRVHSFEE-----LERHPDFALPFVLACQSRNAKMTTLAMQCL 82
Cdd:pfam16213    2 GSKLLEALQSDLRTLSSEAKRKYPPVKEASEKGILRLRTVHSSSPlmqnlLSASEDILKPFVLACETKNPKLVQIALGCL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353105      83 QGLSTVPSIPRSRLSEILDAFIEATHLAMEIQLKVLQVVPIFFKTYGkFIYGPLCKKLLLCCSNLLhvPNKAPVVVGTAS 162
Cdd:pfam16213   82 QKLISHDAISQSAAPYILDTLWMLMELGSEIELKVLQTVLLLITTNS-VIHGDTLAKALVLCFRLH--FSKDPTVQNTAS 158
                          170
                   ....*....|....
gi 1353105     163 ATLQQLIDEIFDRL 176
Cdd:pfam16213  159 ATLRQLVSVVFERV 172
Sec7_N pfam12783
Guanine nucleotide exchange factor in Golgi transport N-terminal; The full-length Sec7 ...
202-362 1.97e-37

Guanine nucleotide exchange factor in Golgi transport N-terminal; The full-length Sec7 functions proximally in the secretory pathway as a protein binding scaffold for the coat protein complexes COPII-COPI. The COPII-COPI-protein switch is necessary for maturation of the vesicular-tubular cluster, VTC, intermediate compartments for Golgi compartment biogenesis. This N-terminal domain however does not appear to be binding either of the COP or the ARF.


Pssm-ID: 463703  Cd Length: 154  Bit Score: 138.40  E-value: 1.97e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353105     202 YRYDANKLFDNICSLneisSNGAVSDEEMLLDIGDIPIDYGLEILESILKNSQKNLLECQDLQYLLRVKAIPLLLRCISS 281
Cdd:pfam12783    1 AAKDAFLVFRDLCKL----SNGKPLSKSDPKSHAERSKLFSLELIESILENHGDVFLKHPELLQLLKQYLCPSLLRNLSS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353105     282 SrHFSTAVRSCRCLKLLIRKeYLSILELELEVILSLLIHGIsVESNLSGWQRVLSLELFKDLSQDPEIVNTLYMDYDNYP 361
Cdd:pfam12783   77 S-SFPVFVRSLRIFLLLLRR-FRSHLKLEIEVFLSLLILPL-LESDSSLWQKALVLEVLRRLCSDPQLLVEIYLNYDCDL 153

                   .
gi 1353105     362 D 362
Cdd:pfam12783  154 G 154
Mon2_C pfam16206
C-terminal region of Mon2 protein; Mon2 proteins are found from fungi to plants, to human and ...
936-1161 6.14e-12

C-terminal region of Mon2 protein; Mon2 proteins are found from fungi to plants, to human and is a scaffold protein involved in multiple aspects of endo membrane trafficking. This C-terminal region is essential for Mon2 activity.


Pssm-ID: 465066  Cd Length: 827  Bit Score: 70.92  E-value: 6.14e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353105     936 DFLQSLPMSVIKFVIDTLVNFVSQKRNLNISFSSISQFWLVGDYLRVRFNPETLNLSDEKRRSLSEKINNQKLIEIITSS 1015
Cdd:pfam16206    2 DFLPTMPCRCLPICIDTAAKFGLHNQELNISLTAIGLLWNISDFFFQRGEIIEKELNKEDAAMQKQAEDKAILLNRPEFP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353105    1016 SSHDWELYNGLWIYLLKNLINCTNDDRVEVKNGAVQTFFRIIDSHSVCF--PPWDLIFLEVIEPLL--TKEWST----EE 1087
Cdd:pfam16206   82 ATVKMPPFDCLWLCLYAKLGELCVDLRPAVRKSAGQTLFSTIGAHGSLLnhPTWHALIWKVLFNLLdnVRALSSsadkEK 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353105    1088 LENETDFINV-----------------TLQGLIKLYPEHFKDFKNNTTCAKEWSMLLDFLKRLLSSTSNNTKNAVILNYQ 1150
Cdd:pfam16206  162 IDAGGGNILIhhsrdtaekqwaetqvlTLAGVARIFNTKRELLQMLGDFERAWDLILDFIQNAALSKNGEVSLAALKSFQ 241
                          250
                   ....*....|.
gi 1353105    1151 TLLKEIITIED 1161
Cdd:pfam16206  242 EILQHNSPTED 252
 
Name Accession Description Interval E-value
DCB pfam16213
dimerization and cyclophilin-binding domain of Mon2; DCB is the N-terminal domain of Mon2- and ...
8-176 3.39e-58

dimerization and cyclophilin-binding domain of Mon2; DCB is the N-terminal domain of Mon2- and GIG1-like proteins from metazoa. Mon2 and BIG1 like proteins play an important role in the cytoplasm-to-vacuole transport pathway and are required for Golgi homeostasis.


Pssm-ID: 465072 [Multi-domain]  Cd Length: 172  Bit Score: 198.25  E-value: 3.39e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353105       8 FDSMQRQLEAELRSLSSESKRRNSTIRHASDKSIEILKRVHSFEE-----LERHPDFALPFVLACQSRNAKMTTLAMQCL 82
Cdd:pfam16213    2 GSKLLEALQSDLRTLSSEAKRKYPPVKEASEKGILRLRTVHSSSPlmqnlLSASEDILKPFVLACETKNPKLVQIALGCL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353105      83 QGLSTVPSIPRSRLSEILDAFIEATHLAMEIQLKVLQVVPIFFKTYGkFIYGPLCKKLLLCCSNLLhvPNKAPVVVGTAS 162
Cdd:pfam16213   82 QKLISHDAISQSAAPYILDTLWMLMELGSEIELKVLQTVLLLITTNS-VIHGDTLAKALVLCFRLH--FSKDPTVQNTAS 158
                          170
                   ....*....|....
gi 1353105     163 ATLQQLIDEIFDRL 176
Cdd:pfam16213  159 ATLRQLVSVVFERV 172
Sec7_N pfam12783
Guanine nucleotide exchange factor in Golgi transport N-terminal; The full-length Sec7 ...
202-362 1.97e-37

Guanine nucleotide exchange factor in Golgi transport N-terminal; The full-length Sec7 functions proximally in the secretory pathway as a protein binding scaffold for the coat protein complexes COPII-COPI. The COPII-COPI-protein switch is necessary for maturation of the vesicular-tubular cluster, VTC, intermediate compartments for Golgi compartment biogenesis. This N-terminal domain however does not appear to be binding either of the COP or the ARF.


Pssm-ID: 463703  Cd Length: 154  Bit Score: 138.40  E-value: 1.97e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353105     202 YRYDANKLFDNICSLneisSNGAVSDEEMLLDIGDIPIDYGLEILESILKNSQKNLLECQDLQYLLRVKAIPLLLRCISS 281
Cdd:pfam12783    1 AAKDAFLVFRDLCKL----SNGKPLSKSDPKSHAERSKLFSLELIESILENHGDVFLKHPELLQLLKQYLCPSLLRNLSS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353105     282 SrHFSTAVRSCRCLKLLIRKeYLSILELELEVILSLLIHGIsVESNLSGWQRVLSLELFKDLSQDPEIVNTLYMDYDNYP 361
Cdd:pfam12783   77 S-SFPVFVRSLRIFLLLLRR-FRSHLKLEIEVFLSLLILPL-LESDSSLWQKALVLEVLRRLCSDPQLLVEIYLNYDCDL 153

                   .
gi 1353105     362 D 362
Cdd:pfam12783  154 G 154
Mon2_C pfam16206
C-terminal region of Mon2 protein; Mon2 proteins are found from fungi to plants, to human and ...
936-1161 6.14e-12

C-terminal region of Mon2 protein; Mon2 proteins are found from fungi to plants, to human and is a scaffold protein involved in multiple aspects of endo membrane trafficking. This C-terminal region is essential for Mon2 activity.


Pssm-ID: 465066  Cd Length: 827  Bit Score: 70.92  E-value: 6.14e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353105     936 DFLQSLPMSVIKFVIDTLVNFVSQKRNLNISFSSISQFWLVGDYLRVRFNPETLNLSDEKRRSLSEKINNQKLIEIITSS 1015
Cdd:pfam16206    2 DFLPTMPCRCLPICIDTAAKFGLHNQELNISLTAIGLLWNISDFFFQRGEIIEKELNKEDAAMQKQAEDKAILLNRPEFP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353105    1016 SSHDWELYNGLWIYLLKNLINCTNDDRVEVKNGAVQTFFRIIDSHSVCF--PPWDLIFLEVIEPLL--TKEWST----EE 1087
Cdd:pfam16206   82 ATVKMPPFDCLWLCLYAKLGELCVDLRPAVRKSAGQTLFSTIGAHGSLLnhPTWHALIWKVLFNLLdnVRALSSsadkEK 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353105    1088 LENETDFINV-----------------TLQGLIKLYPEHFKDFKNNTTCAKEWSMLLDFLKRLLSSTSNNTKNAVILNYQ 1150
Cdd:pfam16206  162 IDAGGGNILIhhsrdtaekqwaetqvlTLAGVARIFNTKRELLQMLGDFERAWDLILDFIQNAALSKNGEVSLAALKSFQ 241
                          250
                   ....*....|.
gi 1353105    1151 TLLKEIITIED 1161
Cdd:pfam16206  242 EILQHNSPTED 252
 
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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