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Conserved domains on  [gi|17999541|ref|NP_060676|]
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vacuolar protein sorting-associated protein 35 [Homo sapiens]

Protein Classification

vacuolar protein sorting-associated protein 35( domain architecture ID 10508273)

vacuolar protein sorting-associated protein 35 (Vps35) is involved in protein trafficking

CATH:  1.25.40.660
Gene Ontology:  GO:0042147|GO:0015031|GO:0030906
SCOP:  4004058

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
Vps35 pfam03635
Vacuolar protein sorting-associated protein 35; Vacuolar protein sorting-associated protein ...
15-752 0e+00

Vacuolar protein sorting-associated protein 35; Vacuolar protein sorting-associated protein (Vps) 35 is one of around 50 proteins involved in protein trafficking. In particular, Vps35 assembles into a retromer complex with at least four other proteins Vps5, Vps17, Vps26 and Vps29. Vps35 contains a central region of weaker sequence similarity, thought to indicate the presence of at least three domains.


:

Pssm-ID: 427414  Cd Length: 733  Bit Score: 1155.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17999541    15 LLDEAIQAVKVQSFQMKRCLDKNKLMDALKHASNMLGELRTSMLSPKSYYELYMAISDELHYLEVYLTDEFAKGRK-VAD 93
Cdd:pfam03635   1 LLEEALSVVKQQSFLMKRCLDNGKLMDALKHASTMLSELRTSSLSPKQYYELYMAVFDELRHLSDYLLDEHKKGRHhLAD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17999541    94 LYELVQYAGNIIPRLYLLITVGVVYVKSFPQSRKDILKDLVEMCRGVQHPLRGLFLRNYLLQCTRNILPDEGEPtDEETT 173
Cdd:pfam03635  81 LYELVQYAGNIVPRLYLMITVGSVYIKSKDAPAKEILKDLVEMCRGVQHPIRGLFLRYYLSQMTKDLLPDGGSE-YEGPG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17999541   174 GDISDSMDFVLLNFAEMNKLWVRMQHQGHSRDREKRERERQELRILVGTNLVRLSQLEGVNVERYKQIVLTGILEQVVNC 253
Cdd:pfam03635 160 GTLNDSIDFILTNFIEMNKLWVRLQHQGHSREREKREKERKELKILVGSNLVRLSQLEGVDLEIYKETILPRILEQIVQC 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17999541   254 RDALAQEYLMECIIQVFPDEFHLQTLNPFLRACAELHQNVNVKNIIIALIDRLALFAHREDgPGIPADIKLFDIFSQQVA 333
Cdd:pfam03635 240 RDVLAQEYLMDVIIQVFPDEFHLATLDILLSATLQLNPDVNIKEIVISLIDRLANYAERDS-SGIPEDVDLFEVFWDQLV 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17999541   334 TVIQSRQDMPSEDVVSLQVSLINLAMKCYPDRVDYVDKVLETTVEIFNKLNLEHIATSSAVSKELTRLLKIPVDTYNNIL 413
Cdd:pfam03635 319 KLIEARPDLPLEDILALLVSLLNLSLKCYPDRLDYVDQVLKFAAEKLSEAGGEDDLHSPEAQKQLLKLLLLPIDSYKSIL 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17999541   414 TVLKLKHFHPLFEYFDYESRKSMSCYVLSNVLDYNTEIVSQDQVDSIMNLVSTLIQDQPDQPVEDPDPEDFADEQSLVGR 493
Cdd:pfam03635 399 TLLKLPNYPPLLSLLPYSTRKSIALEILDNILENETKISTPEQVDGLLELISPLIKDQDDQPETEEDEEEFAEEQELVAR 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17999541   494 FIHLLRSEDPDQQYLILNTARKHFGAGGNQRIRFTLPPLVFAAYQLAFRYK----ENSKVDDKWEKKCQKIFSFAHQTIS 569
Cdd:pfam03635 479 LVHLIRNDDPDTQFEILQTARKHFLKGGPKRIKYTYPPLIFAALKLARRLKalkaREHSKDDKWDKKIKKIFKFIHQTIS 558
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17999541   570 ALI-KAELAELPLRLFLQGALAAGEIGFENhetVAYEFMSQAFSLYEDEISDSKAQLAAITLIIGTFERMKCFSEENHEP 648
Cdd:pfam03635 559 ALYnKAEEAELALKLFLQAALVADQLGLEE---IAYEFFTQAFTIYEESISDSKAQFQALTLIIGTLQKTRSFSEENYDT 635
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17999541   649 LRTQCALAASKLLKKPDQGRAVSTCAHLFWSGrntdknGEELHGGKRVMECLKKALKIANQCMDPSLQVQLFIEILNRYI 728
Cdd:pfam03635 636 LITKCTLYASKLLKKPDQCRAVYLCSHLWWST------EKLYRDGKRVLECLQKALRIADSCMDNAVSLQLFVEILNRYL 709
                         730       740
                  ....*....|....*....|....
gi 17999541   729 YFYEKENDAVTIQVLNQLIQKIRE 752
Cdd:pfam03635 710 YFFEKGNEEVTVKYINGLIELIKE 733
 
Name Accession Description Interval E-value
Vps35 pfam03635
Vacuolar protein sorting-associated protein 35; Vacuolar protein sorting-associated protein ...
15-752 0e+00

Vacuolar protein sorting-associated protein 35; Vacuolar protein sorting-associated protein (Vps) 35 is one of around 50 proteins involved in protein trafficking. In particular, Vps35 assembles into a retromer complex with at least four other proteins Vps5, Vps17, Vps26 and Vps29. Vps35 contains a central region of weaker sequence similarity, thought to indicate the presence of at least three domains.


Pssm-ID: 427414  Cd Length: 733  Bit Score: 1155.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17999541    15 LLDEAIQAVKVQSFQMKRCLDKNKLMDALKHASNMLGELRTSMLSPKSYYELYMAISDELHYLEVYLTDEFAKGRK-VAD 93
Cdd:pfam03635   1 LLEEALSVVKQQSFLMKRCLDNGKLMDALKHASTMLSELRTSSLSPKQYYELYMAVFDELRHLSDYLLDEHKKGRHhLAD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17999541    94 LYELVQYAGNIIPRLYLLITVGVVYVKSFPQSRKDILKDLVEMCRGVQHPLRGLFLRNYLLQCTRNILPDEGEPtDEETT 173
Cdd:pfam03635  81 LYELVQYAGNIVPRLYLMITVGSVYIKSKDAPAKEILKDLVEMCRGVQHPIRGLFLRYYLSQMTKDLLPDGGSE-YEGPG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17999541   174 GDISDSMDFVLLNFAEMNKLWVRMQHQGHSRDREKRERERQELRILVGTNLVRLSQLEGVNVERYKQIVLTGILEQVVNC 253
Cdd:pfam03635 160 GTLNDSIDFILTNFIEMNKLWVRLQHQGHSREREKREKERKELKILVGSNLVRLSQLEGVDLEIYKETILPRILEQIVQC 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17999541   254 RDALAQEYLMECIIQVFPDEFHLQTLNPFLRACAELHQNVNVKNIIIALIDRLALFAHREDgPGIPADIKLFDIFSQQVA 333
Cdd:pfam03635 240 RDVLAQEYLMDVIIQVFPDEFHLATLDILLSATLQLNPDVNIKEIVISLIDRLANYAERDS-SGIPEDVDLFEVFWDQLV 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17999541   334 TVIQSRQDMPSEDVVSLQVSLINLAMKCYPDRVDYVDKVLETTVEIFNKLNLEHIATSSAVSKELTRLLKIPVDTYNNIL 413
Cdd:pfam03635 319 KLIEARPDLPLEDILALLVSLLNLSLKCYPDRLDYVDQVLKFAAEKLSEAGGEDDLHSPEAQKQLLKLLLLPIDSYKSIL 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17999541   414 TVLKLKHFHPLFEYFDYESRKSMSCYVLSNVLDYNTEIVSQDQVDSIMNLVSTLIQDQPDQPVEDPDPEDFADEQSLVGR 493
Cdd:pfam03635 399 TLLKLPNYPPLLSLLPYSTRKSIALEILDNILENETKISTPEQVDGLLELISPLIKDQDDQPETEEDEEEFAEEQELVAR 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17999541   494 FIHLLRSEDPDQQYLILNTARKHFGAGGNQRIRFTLPPLVFAAYQLAFRYK----ENSKVDDKWEKKCQKIFSFAHQTIS 569
Cdd:pfam03635 479 LVHLIRNDDPDTQFEILQTARKHFLKGGPKRIKYTYPPLIFAALKLARRLKalkaREHSKDDKWDKKIKKIFKFIHQTIS 558
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17999541   570 ALI-KAELAELPLRLFLQGALAAGEIGFENhetVAYEFMSQAFSLYEDEISDSKAQLAAITLIIGTFERMKCFSEENHEP 648
Cdd:pfam03635 559 ALYnKAEEAELALKLFLQAALVADQLGLEE---IAYEFFTQAFTIYEESISDSKAQFQALTLIIGTLQKTRSFSEENYDT 635
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17999541   649 LRTQCALAASKLLKKPDQGRAVSTCAHLFWSGrntdknGEELHGGKRVMECLKKALKIANQCMDPSLQVQLFIEILNRYI 728
Cdd:pfam03635 636 LITKCTLYASKLLKKPDQCRAVYLCSHLWWST------EKLYRDGKRVLECLQKALRIADSCMDNAVSLQLFVEILNRYL 709
                         730       740
                  ....*....|....*....|....
gi 17999541   729 YFYEKENDAVTIQVLNQLIQKIRE 752
Cdd:pfam03635 710 YFFEKGNEEVTVKYINGLIELIKE 733
14-3-3 cd08774
14-3-3 domain; 14-3-3 domain is an essential part of 14-3-3 proteins, a ubiquitous class of ...
694-766 7.08e-03

14-3-3 domain; 14-3-3 domain is an essential part of 14-3-3 proteins, a ubiquitous class of regulatory, phosphoserine/threonine-binding proteins found in all eukaryotic cells, including yeast, protozoa and mammalian cells. 14-3-3 proteins play important roles in many biological processes that are regulated by phosphorylation, including cell cycle regulation, cell proliferation, protein trafficking, metabolic regulation and apoptosis. More than 300 binding partners of the 14-3-3 domain have been identified in all subcellular compartments and include transcription factors, signaling molecules, tumor suppressors, biosynthetic enzymes, cytoskeletal proteins and apoptosis factors. 14-3-3 binding can alter the conformation, localization, stability, phosphorylation state, activity as well as molecular interactions of a target protein. They function only as dimers, some preferring strictly homodimeric interaction, while others form heterodimers. Binding of the 14-3-3 domain to its target occurs in a phosphospecific manner where it binds to one of two consensus sequences of their target proteins; RSXpSXP (mode-1) and RXXXpSXP (mode-2). In some instances, 14-3-3 domain containing proteins are involved in regulation and signaling of a number of cellular processes in phosphorylation-independent manner. Many organisms express multiple isoforms: there are seven mammalian 14-3-3 family members (beta, gamma, eta, theta, epsilon, sigma, zeta), each encoded by a distinct gene, while plants contain up to 13 isoforms. The flexible C-terminal segment of 14-3-3 isoforms shows the highest sequence variability and may significantly contribute to individual isoform uniqueness by playing an important regulatory role by occupying the ligand binding groove and blocking the binding of inappropriate ligands in a distinct manner. Elevated amounts of 14-3-3 proteins are found in the cerebrospinal fluid of patients with Creutzfeldt-Jakob disease. In protozoa, like Plasmodium or Cryptosporidium parvum 14-3-3 proteins play an important role in key steps of parasite development.


Pssm-ID: 206755  Cd Length: 225  Bit Score: 38.71  E-value: 7.08e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17999541 694 KRVMECLKKALKIANQCMDPSLQVQLFIeILNRYIYFYEKENDAVT-IQVLNQLIQKIREDLPNL--ESSEETEQI 766
Cdd:cd08774 142 EKAKKAYQEALEIAKKLLPPTHPIRLGL-ALNFSVFYYEILNDPEEaCKLAKKAFDEAIAELDTLseESYKDSTLI 216
 
Name Accession Description Interval E-value
Vps35 pfam03635
Vacuolar protein sorting-associated protein 35; Vacuolar protein sorting-associated protein ...
15-752 0e+00

Vacuolar protein sorting-associated protein 35; Vacuolar protein sorting-associated protein (Vps) 35 is one of around 50 proteins involved in protein trafficking. In particular, Vps35 assembles into a retromer complex with at least four other proteins Vps5, Vps17, Vps26 and Vps29. Vps35 contains a central region of weaker sequence similarity, thought to indicate the presence of at least three domains.


Pssm-ID: 427414  Cd Length: 733  Bit Score: 1155.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17999541    15 LLDEAIQAVKVQSFQMKRCLDKNKLMDALKHASNMLGELRTSMLSPKSYYELYMAISDELHYLEVYLTDEFAKGRK-VAD 93
Cdd:pfam03635   1 LLEEALSVVKQQSFLMKRCLDNGKLMDALKHASTMLSELRTSSLSPKQYYELYMAVFDELRHLSDYLLDEHKKGRHhLAD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17999541    94 LYELVQYAGNIIPRLYLLITVGVVYVKSFPQSRKDILKDLVEMCRGVQHPLRGLFLRNYLLQCTRNILPDEGEPtDEETT 173
Cdd:pfam03635  81 LYELVQYAGNIVPRLYLMITVGSVYIKSKDAPAKEILKDLVEMCRGVQHPIRGLFLRYYLSQMTKDLLPDGGSE-YEGPG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17999541   174 GDISDSMDFVLLNFAEMNKLWVRMQHQGHSRDREKRERERQELRILVGTNLVRLSQLEGVNVERYKQIVLTGILEQVVNC 253
Cdd:pfam03635 160 GTLNDSIDFILTNFIEMNKLWVRLQHQGHSREREKREKERKELKILVGSNLVRLSQLEGVDLEIYKETILPRILEQIVQC 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17999541   254 RDALAQEYLMECIIQVFPDEFHLQTLNPFLRACAELHQNVNVKNIIIALIDRLALFAHREDgPGIPADIKLFDIFSQQVA 333
Cdd:pfam03635 240 RDVLAQEYLMDVIIQVFPDEFHLATLDILLSATLQLNPDVNIKEIVISLIDRLANYAERDS-SGIPEDVDLFEVFWDQLV 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17999541   334 TVIQSRQDMPSEDVVSLQVSLINLAMKCYPDRVDYVDKVLETTVEIFNKLNLEHIATSSAVSKELTRLLKIPVDTYNNIL 413
Cdd:pfam03635 319 KLIEARPDLPLEDILALLVSLLNLSLKCYPDRLDYVDQVLKFAAEKLSEAGGEDDLHSPEAQKQLLKLLLLPIDSYKSIL 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17999541   414 TVLKLKHFHPLFEYFDYESRKSMSCYVLSNVLDYNTEIVSQDQVDSIMNLVSTLIQDQPDQPVEDPDPEDFADEQSLVGR 493
Cdd:pfam03635 399 TLLKLPNYPPLLSLLPYSTRKSIALEILDNILENETKISTPEQVDGLLELISPLIKDQDDQPETEEDEEEFAEEQELVAR 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17999541   494 FIHLLRSEDPDQQYLILNTARKHFGAGGNQRIRFTLPPLVFAAYQLAFRYK----ENSKVDDKWEKKCQKIFSFAHQTIS 569
Cdd:pfam03635 479 LVHLIRNDDPDTQFEILQTARKHFLKGGPKRIKYTYPPLIFAALKLARRLKalkaREHSKDDKWDKKIKKIFKFIHQTIS 558
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17999541   570 ALI-KAELAELPLRLFLQGALAAGEIGFENhetVAYEFMSQAFSLYEDEISDSKAQLAAITLIIGTFERMKCFSEENHEP 648
Cdd:pfam03635 559 ALYnKAEEAELALKLFLQAALVADQLGLEE---IAYEFFTQAFTIYEESISDSKAQFQALTLIIGTLQKTRSFSEENYDT 635
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17999541   649 LRTQCALAASKLLKKPDQGRAVSTCAHLFWSGrntdknGEELHGGKRVMECLKKALKIANQCMDPSLQVQLFIEILNRYI 728
Cdd:pfam03635 636 LITKCTLYASKLLKKPDQCRAVYLCSHLWWST------EKLYRDGKRVLECLQKALRIADSCMDNAVSLQLFVEILNRYL 709
                         730       740
                  ....*....|....*....|....
gi 17999541   729 YFYEKENDAVTIQVLNQLIQKIRE 752
Cdd:pfam03635 710 YFFEKGNEEVTVKYINGLIELIKE 733
14-3-3 cd08774
14-3-3 domain; 14-3-3 domain is an essential part of 14-3-3 proteins, a ubiquitous class of ...
694-766 7.08e-03

14-3-3 domain; 14-3-3 domain is an essential part of 14-3-3 proteins, a ubiquitous class of regulatory, phosphoserine/threonine-binding proteins found in all eukaryotic cells, including yeast, protozoa and mammalian cells. 14-3-3 proteins play important roles in many biological processes that are regulated by phosphorylation, including cell cycle regulation, cell proliferation, protein trafficking, metabolic regulation and apoptosis. More than 300 binding partners of the 14-3-3 domain have been identified in all subcellular compartments and include transcription factors, signaling molecules, tumor suppressors, biosynthetic enzymes, cytoskeletal proteins and apoptosis factors. 14-3-3 binding can alter the conformation, localization, stability, phosphorylation state, activity as well as molecular interactions of a target protein. They function only as dimers, some preferring strictly homodimeric interaction, while others form heterodimers. Binding of the 14-3-3 domain to its target occurs in a phosphospecific manner where it binds to one of two consensus sequences of their target proteins; RSXpSXP (mode-1) and RXXXpSXP (mode-2). In some instances, 14-3-3 domain containing proteins are involved in regulation and signaling of a number of cellular processes in phosphorylation-independent manner. Many organisms express multiple isoforms: there are seven mammalian 14-3-3 family members (beta, gamma, eta, theta, epsilon, sigma, zeta), each encoded by a distinct gene, while plants contain up to 13 isoforms. The flexible C-terminal segment of 14-3-3 isoforms shows the highest sequence variability and may significantly contribute to individual isoform uniqueness by playing an important regulatory role by occupying the ligand binding groove and blocking the binding of inappropriate ligands in a distinct manner. Elevated amounts of 14-3-3 proteins are found in the cerebrospinal fluid of patients with Creutzfeldt-Jakob disease. In protozoa, like Plasmodium or Cryptosporidium parvum 14-3-3 proteins play an important role in key steps of parasite development.


Pssm-ID: 206755  Cd Length: 225  Bit Score: 38.71  E-value: 7.08e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17999541 694 KRVMECLKKALKIANQCMDPSLQVQLFIeILNRYIYFYEKENDAVT-IQVLNQLIQKIREDLPNL--ESSEETEQI 766
Cdd:cd08774 142 EKAKKAYQEALEIAKKLLPPTHPIRLGL-ALNFSVFYYEILNDPEEaCKLAKKAFDEAIAELDTLseESYKDSTLI 216
 
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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