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Conserved domains on  [gi|402908269|ref|XP_003916874|]
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PREDICTED: vacuolar protein sorting-associated protein 35 isoform 1 [Papio anubis]

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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 ...
14-754 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: 252074  Cd Length: 749  Bit Score: 1118.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402908269   14 KLLDEAIQAVKVQSFQMKRCLDKNKLMDALKHASNMLGELRTSMLSPKSYYELYMAISDELHYLEVYLTDEFAKGRKVAD 93
Cdd:pfam03635   1 KLLEEAIAVVKQQSFLMKRCLDQGKLMDALKHASNMLSELRTSSLSPKQYYELYMKVFDELQYLSTYLVDEHPKGHHLAD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402908269   94 LYELVQYAGNIIPRLYLLITVGVVYVKSFPQSRKDILKDLVEMCRGVQHPLRGLFLRNYLLQCTRNILPDEGEPtDEETT 173
Cdd:pfam03635  81 LYELVQYAGNIVPRLYLLITVGSVYIKSKDAPAKEILKDMVEMCRGVQHPTRGLFLRYYLSQRTKDKLPDTGSY-EEGGG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402908269  174 GDISDSMDFVLLNFAEMNKLWVRMQHQGHSRDREKRERERQELRILVGTNLVRLSQLEGVNVERYKQIVLTGILEQVVNC 253
Cdd:pfam03635 160 GTVQDSIEFLLTNFIEMNKLWVRLQHQGPSREREKREKERKELRILVGSNLVRLSQLEGVDLEMYKETILPRILEQVVNC 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402908269  254 RDALAQEYLMECIIQVFPDEFHLQTLNPFLRACAELHQNVNVKNIIIALIDRLALFAHREDGP------------GIPAD 321
Cdd:pfam03635 240 RDVLAQEYLLEVIIQVFPDEFHLATLDTLLSACLQLNPGVDVKKILITLMDRLAAYAERSNEGvaevesrkeeelEAPED 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402908269  322 IKLFDIFSQQVATVIQSRQDMPSEDVVSLQVSLINLAMKCYPDRVDYVDKVLETTVEIFNKLnLEHIATSSAVSKELTRL 401
Cdd:pfam03635 320 VDLFEVFWNQLVKLIKARPDLPLQDIIALLVSLLNLTLKCYPDRLDYVDQVLGFAVEKVSNY-LGAKLNSSEIEQEIVRL 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402908269  402 LKIPVDTYNNILTVLKLKHFHPLFEYFDYESRKSMSCYVLSNVLDYNTEIVSQEQVDSIMNLVSTLIQDQPDQPVED-PD 480
Cdd:pfam03635 399 LLAPISTYKNILTALELPNYQPLLSSLDYSTRKSVALAIIDNILKNNTLITTLDDVERLFELISPLIKDQPDQPSDElDE 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402908269  481 PEDFADEQSLVGRFIHLLRSEDPDQQYLILNTARKHFGAGGNQRIRFTLPPLVFAAYQLAFRYKENSKVDDKWEKKCQKI 560
Cdd:pfam03635 479 TEEFAEEQEKVARLIHLIRSDDVEKQFKILNTVRKHLGKGGPERIRYTLPTLVFAALRLARRLKSQEKKDDKWDAKIKKI 558
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402908269  561 FSFAHQTISALIK-AELAELPLRLFLQGALAAGEIGFENhetVAYEFMSQAFSLYEDEISDSKAQLAAITLIIGTFERMK 639
Cdd:pfam03635 559 FKFIHSTISILYNvAPAAELALKLYLQCAIVADQCGLEE---IAYEFFTQAFTIYEESISDSKAQFQAIVLIISTLQRTR 635
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402908269  640 CFSEENHEPLRTQCALAASKLLKKPDQGRAVSTCAHLFWSGrNTDKNGEELHGGKRVMECLKKALKIANQCMDPSLQVQL 719
Cdd:pfam03635 636 SLPEENYETLATKLALYASKLLKKPDQCRAVYLCSHLFWAT-ELPSTGEFYRDGKRVLECLQKALRIADSCMDNSQSVQL 714
                         730       740       750
                  ....*....|....*....|....*....|....*
gi 402908269  720 FIEILNRYIYFYEKENDAVTIQVLNQLIQKIREDL 754
Cdd:pfam03635 715 FVEILNRYLYYFEKGNTHVTVKYINGLIELIQENL 749
 
Name Accession Description Interval E-value
Vps35 pfam03635
Vacuolar protein sorting-associated protein 35; Vacuolar protein sorting-associated protein ...
14-754 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: 252074  Cd Length: 749  Bit Score: 1118.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402908269   14 KLLDEAIQAVKVQSFQMKRCLDKNKLMDALKHASNMLGELRTSMLSPKSYYELYMAISDELHYLEVYLTDEFAKGRKVAD 93
Cdd:pfam03635   1 KLLEEAIAVVKQQSFLMKRCLDQGKLMDALKHASNMLSELRTSSLSPKQYYELYMKVFDELQYLSTYLVDEHPKGHHLAD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402908269   94 LYELVQYAGNIIPRLYLLITVGVVYVKSFPQSRKDILKDLVEMCRGVQHPLRGLFLRNYLLQCTRNILPDEGEPtDEETT 173
Cdd:pfam03635  81 LYELVQYAGNIVPRLYLLITVGSVYIKSKDAPAKEILKDMVEMCRGVQHPTRGLFLRYYLSQRTKDKLPDTGSY-EEGGG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402908269  174 GDISDSMDFVLLNFAEMNKLWVRMQHQGHSRDREKRERERQELRILVGTNLVRLSQLEGVNVERYKQIVLTGILEQVVNC 253
Cdd:pfam03635 160 GTVQDSIEFLLTNFIEMNKLWVRLQHQGPSREREKREKERKELRILVGSNLVRLSQLEGVDLEMYKETILPRILEQVVNC 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402908269  254 RDALAQEYLMECIIQVFPDEFHLQTLNPFLRACAELHQNVNVKNIIIALIDRLALFAHREDGP------------GIPAD 321
Cdd:pfam03635 240 RDVLAQEYLLEVIIQVFPDEFHLATLDTLLSACLQLNPGVDVKKILITLMDRLAAYAERSNEGvaevesrkeeelEAPED 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402908269  322 IKLFDIFSQQVATVIQSRQDMPSEDVVSLQVSLINLAMKCYPDRVDYVDKVLETTVEIFNKLnLEHIATSSAVSKELTRL 401
Cdd:pfam03635 320 VDLFEVFWNQLVKLIKARPDLPLQDIIALLVSLLNLTLKCYPDRLDYVDQVLGFAVEKVSNY-LGAKLNSSEIEQEIVRL 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402908269  402 LKIPVDTYNNILTVLKLKHFHPLFEYFDYESRKSMSCYVLSNVLDYNTEIVSQEQVDSIMNLVSTLIQDQPDQPVED-PD 480
Cdd:pfam03635 399 LLAPISTYKNILTALELPNYQPLLSSLDYSTRKSVALAIIDNILKNNTLITTLDDVERLFELISPLIKDQPDQPSDElDE 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402908269  481 PEDFADEQSLVGRFIHLLRSEDPDQQYLILNTARKHFGAGGNQRIRFTLPPLVFAAYQLAFRYKENSKVDDKWEKKCQKI 560
Cdd:pfam03635 479 TEEFAEEQEKVARLIHLIRSDDVEKQFKILNTVRKHLGKGGPERIRYTLPTLVFAALRLARRLKSQEKKDDKWDAKIKKI 558
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402908269  561 FSFAHQTISALIK-AELAELPLRLFLQGALAAGEIGFENhetVAYEFMSQAFSLYEDEISDSKAQLAAITLIIGTFERMK 639
Cdd:pfam03635 559 FKFIHSTISILYNvAPAAELALKLYLQCAIVADQCGLEE---IAYEFFTQAFTIYEESISDSKAQFQAIVLIISTLQRTR 635
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402908269  640 CFSEENHEPLRTQCALAASKLLKKPDQGRAVSTCAHLFWSGrNTDKNGEELHGGKRVMECLKKALKIANQCMDPSLQVQL 719
Cdd:pfam03635 636 SLPEENYETLATKLALYASKLLKKPDQCRAVYLCSHLFWAT-ELPSTGEFYRDGKRVLECLQKALRIADSCMDNSQSVQL 714
                         730       740       750
                  ....*....|....*....|....*....|....*
gi 402908269  720 FIEILNRYIYFYEKENDAVTIQVLNQLIQKIREDL 754
Cdd:pfam03635 715 FVEILNRYLYYFEKGNTHVTVKYINGLIELIQENL 749
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 2.74e-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: 2.74e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 402908269 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 ...
14-754 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: 252074  Cd Length: 749  Bit Score: 1118.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402908269   14 KLLDEAIQAVKVQSFQMKRCLDKNKLMDALKHASNMLGELRTSMLSPKSYYELYMAISDELHYLEVYLTDEFAKGRKVAD 93
Cdd:pfam03635   1 KLLEEAIAVVKQQSFLMKRCLDQGKLMDALKHASNMLSELRTSSLSPKQYYELYMKVFDELQYLSTYLVDEHPKGHHLAD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402908269   94 LYELVQYAGNIIPRLYLLITVGVVYVKSFPQSRKDILKDLVEMCRGVQHPLRGLFLRNYLLQCTRNILPDEGEPtDEETT 173
Cdd:pfam03635  81 LYELVQYAGNIVPRLYLLITVGSVYIKSKDAPAKEILKDMVEMCRGVQHPTRGLFLRYYLSQRTKDKLPDTGSY-EEGGG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402908269  174 GDISDSMDFVLLNFAEMNKLWVRMQHQGHSRDREKRERERQELRILVGTNLVRLSQLEGVNVERYKQIVLTGILEQVVNC 253
Cdd:pfam03635 160 GTVQDSIEFLLTNFIEMNKLWVRLQHQGPSREREKREKERKELRILVGSNLVRLSQLEGVDLEMYKETILPRILEQVVNC 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402908269  254 RDALAQEYLMECIIQVFPDEFHLQTLNPFLRACAELHQNVNVKNIIIALIDRLALFAHREDGP------------GIPAD 321
Cdd:pfam03635 240 RDVLAQEYLLEVIIQVFPDEFHLATLDTLLSACLQLNPGVDVKKILITLMDRLAAYAERSNEGvaevesrkeeelEAPED 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402908269  322 IKLFDIFSQQVATVIQSRQDMPSEDVVSLQVSLINLAMKCYPDRVDYVDKVLETTVEIFNKLnLEHIATSSAVSKELTRL 401
Cdd:pfam03635 320 VDLFEVFWNQLVKLIKARPDLPLQDIIALLVSLLNLTLKCYPDRLDYVDQVLGFAVEKVSNY-LGAKLNSSEIEQEIVRL 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402908269  402 LKIPVDTYNNILTVLKLKHFHPLFEYFDYESRKSMSCYVLSNVLDYNTEIVSQEQVDSIMNLVSTLIQDQPDQPVED-PD 480
Cdd:pfam03635 399 LLAPISTYKNILTALELPNYQPLLSSLDYSTRKSVALAIIDNILKNNTLITTLDDVERLFELISPLIKDQPDQPSDElDE 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402908269  481 PEDFADEQSLVGRFIHLLRSEDPDQQYLILNTARKHFGAGGNQRIRFTLPPLVFAAYQLAFRYKENSKVDDKWEKKCQKI 560
Cdd:pfam03635 479 TEEFAEEQEKVARLIHLIRSDDVEKQFKILNTVRKHLGKGGPERIRYTLPTLVFAALRLARRLKSQEKKDDKWDAKIKKI 558
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402908269  561 FSFAHQTISALIK-AELAELPLRLFLQGALAAGEIGFENhetVAYEFMSQAFSLYEDEISDSKAQLAAITLIIGTFERMK 639
Cdd:pfam03635 559 FKFIHSTISILYNvAPAAELALKLYLQCAIVADQCGLEE---IAYEFFTQAFTIYEESISDSKAQFQAIVLIISTLQRTR 635
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402908269  640 CFSEENHEPLRTQCALAASKLLKKPDQGRAVSTCAHLFWSGrNTDKNGEELHGGKRVMECLKKALKIANQCMDPSLQVQL 719
Cdd:pfam03635 636 SLPEENYETLATKLALYASKLLKKPDQCRAVYLCSHLFWAT-ELPSTGEFYRDGKRVLECLQKALRIADSCMDNSQSVQL 714
                         730       740       750
                  ....*....|....*....|....*....|....*
gi 402908269  720 FIEILNRYIYFYEKENDAVTIQVLNQLIQKIREDL 754
Cdd:pfam03635 715 FVEILNRYLYYFEKGNTHVTVKYINGLIELIQENL 749
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 2.74e-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: 2.74e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 402908269 694 KRVMECLKKALKIANQCMDPSLQVQLFIeILNRYIYFYEKENDAVT-IQVLNQLIQKIREDLPNL--ESSEETEQI 766
Cdd:cd08774  142 EKAKKAYQEALEIAKKLLPPTHPIRLGL-ALNFSVFYYEILNDPEEaCKLAKKAFDEAIAELDTLseESYKDSTLI 216
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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