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Conserved domains on  [gi|5032055|ref|NP_005610|]
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reticulon-2 isoform A [Homo sapiens]

Protein Classification

reticulon family protein( domain architecture ID 10493657)

reticulon family protein associates with the endoplasmic reticulum (ER) through a C-terminal di-lysine ER retention motif; such as mammalian RTN4/Nogo, a developmental neurite growth regulatory factor with a role as a negative regulator of axon-axon adhesion and growth, and as a facilitator of neurite branching

Gene Ontology:  GO:0005789|GO:0005783
PubMed:  12832288

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Reticulon pfam02453
Reticulon; Reticulon, also know as neuroendocrine-specific protein (NSP), is a protein of ...
 345-509 4.02e-40

Reticulon; Reticulon, also know as neuroendocrine-specific protein (NSP), is a protein of unknown function which associates with the endoplasmic reticulum. This family represents the C-terminal domain of the three reticulon isoforms and their homologs.


:

Pssm-ID: 460562 [Multi-domain]  Cd Length: 157  Bit Score: 142.62  E-value: 4.02e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032055    345 VADLLYWKDTRTSGVVFTGLMVSLL--CLLHFSIVSVAAHLALLLLCGTISLRVYRKVLQAVhrgdgANPFQayldvDLT 422
Cdd:pfam02453   1 VADLLLWRNPKKSGGVFGGATALWLlfEVLGYSLLSLVSKLLLLLLLVLFLWAEYAGKLNRP-----PPPIP-----ELE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032055    423 LTREQTERLSHQITSRVVSAATQLRHFFLVEDLVDSLKLALLFYILTFVGAIFNGLTLLILGVIGLFTIPLLYRQHQAQI 502
Cdd:pfam02453  71 LSEETVRELADSLRVLINFALSELRRIALGEDLKLFLKVAVVLWILSYVGSLFSFLTLLYIGVVLAFTVPLLYEKYEDEI 150


                  ....*..
gi 5032055    503 DQYVGLV 509
Cdd:pfam02453 151 DAYVEKA 157
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 58-227 5.75e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 5.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032055     58 TPRELTFSYIAFDGVVGSGG--RRDSTAR--------RPRPQGRSVSEP---RDQHPQPSLGDSLESIPSlSQSPEPGRR 124
Cdd:PHA03247 2841 PPPGPPPPSLPLGGSVAPGGdvRRRPPSRspaakpaaPARPPVRRLARPavsRSTESFALPPDQPERPPQ-PQAPPPPQP 2919

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032055    125 GDPDTAPPSERPLEDLRLRLDhlgwvargtgsgedsstsssTPLEDEEPQEPNRLETGEAGEELDLRLRLAQPSSPEVLT 204
Cdd:PHA03247 2920 QPQPPPPPQPQPPPPPPPRPQ--------------------PPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRV 2979

                         170       180
                  ....*....|....*....|...
gi 5032055    205 PQLSPGSGTPQAGTPSPSRSRDS 227
Cdd:PHA03247 2980 PQPAPSREAPASSTPPLTGHSLS 3002
 
Name Accession Description Interval E-value
Reticulon pfam02453
Reticulon; Reticulon, also know as neuroendocrine-specific protein (NSP), is a protein of ...
 345-509 4.02e-40

Reticulon; Reticulon, also know as neuroendocrine-specific protein (NSP), is a protein of unknown function which associates with the endoplasmic reticulum. This family represents the C-terminal domain of the three reticulon isoforms and their homologs.


Pssm-ID: 460562 [Multi-domain]  Cd Length: 157  Bit Score: 142.62  E-value: 4.02e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032055    345 VADLLYWKDTRTSGVVFTGLMVSLL--CLLHFSIVSVAAHLALLLLCGTISLRVYRKVLQAVhrgdgANPFQayldvDLT 422
Cdd:pfam02453   1 VADLLLWRNPKKSGGVFGGATALWLlfEVLGYSLLSLVSKLLLLLLLVLFLWAEYAGKLNRP-----PPPIP-----ELE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032055    423 LTREQTERLSHQITSRVVSAATQLRHFFLVEDLVDSLKLALLFYILTFVGAIFNGLTLLILGVIGLFTIPLLYRQHQAQI 502
Cdd:pfam02453  71 LSEETVRELADSLRVLINFALSELRRIALGEDLKLFLKVAVVLWILSYVGSLFSFLTLLYIGVVLAFTVPLLYEKYEDEI 150


                  ....*..
gi 5032055    503 DQYVGLV 509
Cdd:pfam02453 151 DAYVEKA 157
ABC_6TM_LmrA_like cd18551
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...
 434-521 1.44e-03

Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349995 [Multi-domain]  Cd Length: 289  Bit Score: 40.88  E-value: 1.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032055  434 QITSRVVSAATQLRHfFLVEDLVDslklaLLFYILTFVGAIF---------NGLTLLILGVIGLFTIPLL------YRQH 498
Cdd:cd18551  94 DLVSRVTNDTTLLRE-LITSGLPQ-----LVTGVLTVVGAVVlmflldwvlTLVTLAVVPLAFLIILPLGrrirkaSKRA 167

                        90       100
                ....*....|....*....|...
gi 5032055  499 QAQidqyVGLVTNQLSHIKAKIR 521
Cdd:cd18551 168 QDA----LGELSAALERALSAIR 186
PHA03247 PHA03247
large tegument protein UL36; Provisional
 58-227 5.75e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 5.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032055     58 TPRELTFSYIAFDGVVGSGG--RRDSTAR--------RPRPQGRSVSEP---RDQHPQPSLGDSLESIPSlSQSPEPGRR 124
Cdd:PHA03247 2841 PPPGPPPPSLPLGGSVAPGGdvRRRPPSRspaakpaaPARPPVRRLARPavsRSTESFALPPDQPERPPQ-PQAPPPPQP 2919

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032055    125 GDPDTAPPSERPLEDLRLRLDhlgwvargtgsgedsstsssTPLEDEEPQEPNRLETGEAGEELDLRLRLAQPSSPEVLT 204
Cdd:PHA03247 2920 QPQPPPPPQPQPPPPPPPRPQ--------------------PPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRV 2979

                         170       180
                  ....*....|....*....|...
gi 5032055    205 PQLSPGSGTPQAGTPSPSRSRDS 227
Cdd:PHA03247 2980 PQPAPSREAPASSTPPLTGHSLS 3002
 
Name Accession Description Interval E-value
Reticulon pfam02453
Reticulon; Reticulon, also know as neuroendocrine-specific protein (NSP), is a protein of ...
 345-509 4.02e-40

Reticulon; Reticulon, also know as neuroendocrine-specific protein (NSP), is a protein of unknown function which associates with the endoplasmic reticulum. This family represents the C-terminal domain of the three reticulon isoforms and their homologs.


Pssm-ID: 460562 [Multi-domain]  Cd Length: 157  Bit Score: 142.62  E-value: 4.02e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032055    345 VADLLYWKDTRTSGVVFTGLMVSLL--CLLHFSIVSVAAHLALLLLCGTISLRVYRKVLQAVhrgdgANPFQayldvDLT 422
Cdd:pfam02453   1 VADLLLWRNPKKSGGVFGGATALWLlfEVLGYSLLSLVSKLLLLLLLVLFLWAEYAGKLNRP-----PPPIP-----ELE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032055    423 LTREQTERLSHQITSRVVSAATQLRHFFLVEDLVDSLKLALLFYILTFVGAIFNGLTLLILGVIGLFTIPLLYRQHQAQI 502
Cdd:pfam02453  71 LSEETVRELADSLRVLINFALSELRRIALGEDLKLFLKVAVVLWILSYVGSLFSFLTLLYIGVVLAFTVPLLYEKYEDEI 150


                  ....*..
gi 5032055    503 DQYVGLV 509
Cdd:pfam02453 151 DAYVEKA 157
ABC_6TM_LmrA_like cd18551
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...
 434-521 1.44e-03

Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349995 [Multi-domain]  Cd Length: 289  Bit Score: 40.88  E-value: 1.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032055  434 QITSRVVSAATQLRHfFLVEDLVDslklaLLFYILTFVGAIF---------NGLTLLILGVIGLFTIPLL------YRQH 498
Cdd:cd18551  94 DLVSRVTNDTTLLRE-LITSGLPQ-----LVTGVLTVVGAVVlmflldwvlTLVTLAVVPLAFLIILPLGrrirkaSKRA 167

                        90       100
                ....*....|....*....|...
gi 5032055  499 QAQidqyVGLVTNQLSHIKAKIR 521
Cdd:cd18551 168 QDA----LGELSAALERALSAIR 186
PHA03247 PHA03247
large tegument protein UL36; Provisional
 58-227 5.75e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 5.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032055     58 TPRELTFSYIAFDGVVGSGG--RRDSTAR--------RPRPQGRSVSEP---RDQHPQPSLGDSLESIPSlSQSPEPGRR 124
Cdd:PHA03247 2841 PPPGPPPPSLPLGGSVAPGGdvRRRPPSRspaakpaaPARPPVRRLARPavsRSTESFALPPDQPERPPQ-PQAPPPPQP 2919

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5032055    125 GDPDTAPPSERPLEDLRLRLDhlgwvargtgsgedsstsssTPLEDEEPQEPNRLETGEAGEELDLRLRLAQPSSPEVLT 204
Cdd:PHA03247 2920 QPQPPPPPQPQPPPPPPPRPQ--------------------PPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRV 2979

                         170       180
                  ....*....|....*....|...
gi 5032055    205 PQLSPGSGTPQAGTPSPSRSRDS 227
Cdd:PHA03247 2980 PQPAPSREAPASSTPPLTGHSLS 3002
 
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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