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Conserved domains on  [gi|21755195|dbj|BAC04637|]
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unnamed protein product [Homo sapiens]

Protein Classification

PX domain-containing protein( domain architecture ID 572)

PX (Phox Homology) domain-containing protein may bind phosphoinositides and may function in targeting proteins to membranes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PX_domain super family cl02563
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
 1-53 2.03e-29

The Phox Homology domain, a phosphoinositide binding module; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases, other PIs such as PI4P or PI(3,4)P2, among others, are the preferred substrates. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction, as in the cases of p40phox, p47phox, and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs, which play important roles in endosomal sorting.


The actual alignment was detected with superfamily member cd07301:

Pssm-ID: 470617  Cd Length: 112  Bit Score: 104.50  E-value: 2.03e-29
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 21755195   1 MAAISFPRKRLRRNFTAETIARRSRAFEQFLGHLQAVPELRHAPDLQDFFVLP 53
Cdd:cd07301  60 MAGVSFPRKRLRKNFTAETIAKRSRAFEQFLCHLHSLPELRASPAFLEFFYLR 112
Spy super family cl27809
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 34-164 2.20e-04

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


The actual alignment was detected with superfamily member COG3914:

Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 41.13  E-value: 2.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21755195  34 LQAVPELRHAPDLQDFFVLPELRRAQSLTCTGLYREALALWANAWQLQaqlgtpsgPDRPLlTLAGLAVCHQELEDPGEA 113
Cdd:COG3914  61 ALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALN--------PDNAE-ALFNLGNLLLALGRLEEA 131

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 21755195 114 RACCEKALQLLGDkslhpllapFLEAHVRLSWRLGLDKRQSEArLQALQEA 164
Cdd:COG3914 132 LAALRRALALNPD---------FAEAYLNLGEALRRLGRLEEA-IAALRRA 172
 
Name Accession Description Interval E-value
PX_SNX21 cd07301
The phosphoinositide binding Phox Homology domain of Sorting Nexin 21; The PX domain is a ...
 1-53 2.03e-29

The phosphoinositide binding Phox Homology domain of Sorting Nexin 21; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX21, also called SNX-L, is distinctly and highly-expressed in fetal liver and may be involved in protein sorting and degradation during embryonic liver development.


Pssm-ID: 132834  Cd Length: 112  Bit Score: 104.50  E-value: 2.03e-29
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 21755195   1 MAAISFPRKRLRRNFTAETIARRSRAFEQFLGHLQAVPELRHAPDLQDFFVLP 53
Cdd:cd07301  60 MAGVSFPRKRLRKNFTAETIAKRSRAFEQFLCHLHSLPELRASPAFLEFFYLR 112
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 34-164 2.20e-04

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 41.13  E-value: 2.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21755195  34 LQAVPELRHAPDLQDFFVLPELRRAQSLTCTGLYREALALWANAWQLQaqlgtpsgPDRPLlTLAGLAVCHQELEDPGEA 113
Cdd:COG3914  61 ALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALN--------PDNAE-ALFNLGNLLLALGRLEEA 131

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 21755195 114 RACCEKALQLLGDkslhpllapFLEAHVRLSWRLGLDKRQSEArLQALQEA 164
Cdd:COG3914 132 LAALRRALALNPD---------FAEAYLNLGEALRRLGRLEEA-IAALRRA 172
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 6-50 2.90e-04

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 37.99  E-value: 2.90e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 21755195     6 FPRKRLRRNFTAETIARRSRAFEQFLGHLQAVPELRHAPDLQDFF 50
Cdd:pfam00787  37 LPPKRWLGRYNEEFIEKRRKGLEQYLQRLLQHPELRNSEVLLEFL 81
 
Name Accession Description Interval E-value
PX_SNX21 cd07301
The phosphoinositide binding Phox Homology domain of Sorting Nexin 21; The PX domain is a ...
 1-53 2.03e-29

The phosphoinositide binding Phox Homology domain of Sorting Nexin 21; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX21, also called SNX-L, is distinctly and highly-expressed in fetal liver and may be involved in protein sorting and degradation during embryonic liver development.


Pssm-ID: 132834  Cd Length: 112  Bit Score: 104.50  E-value: 2.03e-29
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 21755195   1 MAAISFPRKRLRRNFTAETIARRSRAFEQFLGHLQAVPELRHAPDLQDFFVLP 53
Cdd:cd07301  60 MAGVSFPRKRLRKNFTAETIAKRSRAFEQFLCHLHSLPELRASPAFLEFFYLR 112
PX_SNX20_21_like cd07279
The phosphoinositide binding Phox Homology domain of Sorting Nexins 20 and 21; The PX domain ...
 1-53 5.85e-24

The phosphoinositide binding Phox Homology domain of Sorting Nexins 20 and 21; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. This subfamily consists of SNX20, SNX21, and similar proteins. SNX20 interacts with P-Selectin glycoprotein ligand-1 (PSGL-1), a surface-expressed mucin that acts as a ligand for the selectin family of adhesion proteins. It may function in the sorting and cycling of PSGL-1 into endosomes. SNX21, also called SNX-L, is distinctly and highly-expressed in fetal liver and may be involved in protein sorting and degradation during embryonic liver development.


Pssm-ID: 132812  Cd Length: 112  Bit Score: 90.46  E-value: 5.85e-24
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 21755195   1 MAAISFPRKRLRRNFTAETIARRSRAFEQFLGHLQAVPELRHAPDLQDFFVLP 53
Cdd:cd07279  60 MAKVSFPRKVLMGNFSSELIAERSRAFEQFLGHILSIPNLRDSKAFLDFLQGP 112
PX_SNX20 cd07300
The phosphoinositide binding Phox Homology domain of Sorting Nexin 20; The PX domain is a ...
 1-55 1.13e-09

The phosphoinositide binding Phox Homology domain of Sorting Nexin 20; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX20 interacts with P-Selectin glycoprotein ligand-1 (PSGL-1), a surface-expressed mucin that acts as a ligand for the selectin family of adhesion proteins. The PX domain of SNX20 binds PIs and targets the SNX20/PSGL-1 complex to endosomes. SNX20 may function in the sorting and cycling of PSGL-1 into endosomes.


Pssm-ID: 132833  Cd Length: 114  Bit Score: 53.67  E-value: 1.13e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21755195   1 MAAISFPRKRLRRNFTAETIARRSRAFEQFLGHLQAVPELRHAPDLQDFFVLPEL 55
Cdd:cd07300  60 LEDVVFPKKKLTGNFSEEIIAERRVALRDYLTLLYSLRFVRRSQAFQDFLTHPEL 114
PX_domain cd06093
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
 5-50 1.99e-05

The Phox Homology domain, a phosphoinositide binding module; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases, other PIs such as PI4P or PI(3,4)P2, among others, are the preferred substrates. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction, as in the cases of p40phox, p47phox, and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs, which play important roles in endosomal sorting.


Pssm-ID: 132768 [Multi-domain]  Cd Length: 106  Bit Score: 41.96  E-value: 1.99e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 21755195   5 SFPRKRLRRNFTAETIARRSRAFEQFLGHLQAVPELRHAPDLQDFF 50
Cdd:cd06093  59 PLPPKKLFGNLDPEFIEERRKQLEQYLQSLLNHPELRNSEELKEFL 104
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 34-164 2.20e-04

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 41.13  E-value: 2.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21755195  34 LQAVPELRHAPDLQDFFVLPELRRAQSLTCTGLYREALALWANAWQLQaqlgtpsgPDRPLlTLAGLAVCHQELEDPGEA 113
Cdd:COG3914  61 ALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALN--------PDNAE-ALFNLGNLLLALGRLEEA 131

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 21755195 114 RACCEKALQLLGDkslhpllapFLEAHVRLSWRLGLDKRQSEArLQALQEA 164
Cdd:COG3914 132 LAALRRALALNPD---------FAEAYLNLGEALRRLGRLEEA-IAALRRA 172
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 6-50 2.90e-04

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 37.99  E-value: 2.90e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 21755195     6 FPRKRLRRNFTAETIARRSRAFEQFLGHLQAVPELRHAPDLQDFF 50
Cdd:pfam00787  37 LPPKRWLGRYNEEFIEKRRKGLEQYLQRLLQHPELRNSEVLLEFL 81
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 19-123 2.86e-03

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 37.67  E-value: 2.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21755195  19 TIARRSRAFEQFLGHLQAVpeLRHAPDlqdfFVLPELRRAQSLTCTGLYREALALWANAWQLQaqlgtpsgPDRPLLtLA 98
Cdd:COG3914 120 NLLLALGRLEEALAALRRA--LALNPD----FAEAYLNLGEALRRLGRLEEAIAALRRALELD--------PDNAEA-LN 184

                        90       100
                ....*....|....*....|....*
gi 21755195  99 GLAVCHQELEDPGEARACCEKALQL 123
Cdd:COG3914 185 NLGNALQDLGRLEEAIAAYRRALEL 209
PX_SNX15_like cd06881
The phosphoinositide binding Phox Homology domain of Sorting Nexin 15-like proteins; The PX ...
 6-51 3.46e-03

The phosphoinositide binding Phox Homology domain of Sorting Nexin 15-like proteins; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Members of this subfamily have similarity to sorting nexin 15 (SNX15), which contains an N-terminal PX domain and a C-terminal Microtubule Interacting and Trafficking (MIT) domain. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNX15 plays a role in protein trafficking processes in the endocytic pathway and the trans-Golgi network. The PX domain of SNX15 interacts with the PDGF receptor and is responsible for the membrane association of the protein. Other members of this subfamily contain an additional C-terminal kinase domain, similar to human RPK118, which binds sphingosine kinase and the antioxidant peroxiredoxin-3 (PRDX3). RPK118 may be involved in the transport of proteins such as PRDX3 from the cytoplasm to its site of function in the mitochondria.


Pssm-ID: 132791  Cd Length: 117  Bit Score: 35.76  E-value: 3.46e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 21755195   6 FPRKRLRRNFTAETIARRSRAFEQFLGHLQAVPELRHAPDLQDFFV 51
Cdd:cd06881  70 FPKGKYFGRFDAAVIEERRQAILELLDFVGNHPALYQSSAFQQFFE 115
 
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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