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Conserved domains on  [gi|1443034972|ref|XP_025880804|]
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uncharacterized protein LOC4327520 [Oryza sativa Japonica Group]

Protein Classification

ChanN-like and RETICULATA-like domain-containing protein( domain architecture ID 10915071)

protein containing domains PX_domain, BAR_SNX, ChanN-like, and RETICULATA-like

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RETICULATA-like pfam11891
Protein RETICULATA-related; This entry represents RETICULATA and related proteins from plants. ...
 1134-1317 4.76e-74

Protein RETICULATA-related; This entry represents RETICULATA and related proteins from plants. Arabidopsis RETICULATA protein is involved in differential development of bundle sheath and mesophyll cell chloroplasts.


:

Pssm-ID: 432167  Cd Length: 177  Bit Score: 243.64  E-value: 4.76e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972 1134 ERLLADPKFLHRLAIEEGISITTTLIAQYEKRKGRFLEEIDYVLTDTIRGSVVDFFTVWLPAPTISLLSLGDNGSGesle 1213
Cdd:pfam11891    1 ERLLADPSFLFKLLIEEAIGVGASLLAEYEKRGERFWNELDLVFADVVVGSVVNFALVWLLAPTRSYGSTSAFAGA---- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972 1214 lLKGLLGSLPDNAFQKGIMGQSWNTNQRFASVLMGGIKLAGVGFISSIGAGVASDVLYAARRVLRPstSVETARRRTPIW 1293
Cdd:pfam11891   77 -LQNLLGSLPNNAFEKSYPGREFTLQQRIAAFFYKGAELAAVGFAAGLVGTGLSNALIALRKKMDP--SFEPSVKVPPVV 153

                          170       180
                   ....*....|....*....|....
gi 1443034972 1294 KSATVYSCFLGTSANLRYQVIAGL 1317
Cdd:pfam11891  154 KNALGYGAFMGVSSNLRYQILAGL 177
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 340-568 3.39e-58

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


:

Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 200.27  E-value: 3.39e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  340 ETDAKFVMHKAKLEYFEQHLTTASQQVEALLKAYDDLKATTGQLGMTFIKLAKFEKEqdtcNSQRKRAVDMSNFANAVIN 419
Cdd:cd07596      1 EEDQEFEEAKDYILKLEEQLKKLSKQAQRLVKRRRELGSALGEFGKALIKLAKCEEE----VGGELGEALSKLGKAAEEL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  420 MSRSQTKLNAKIEIHLGTIYEYLETMTSVRNAFTDRANALLRVQSLSGDLFLLHTQAAKLESVSSrgmgqerLRYQKIEE 499
Cdd:cd07596     77 SSLSEAQANQELVKLLEPLKEYLRYCQAVKETLDDRADALLTLQSLKKDLASKKAQLEKLKAAPG-------IKPAKVEE 149

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443034972  500 LKETIRKTEDAKGNARQEYELIKENNMNEIIRFNKEKRHGLVEMLKGFVRNQVSYSEHISSIWTKVAEE 568
Cdd:cd07596    150 LEEELEEAESALEEARKRYEEISERLKEELKRFHEERARDLKAALKEFARLQVQYAEKIAEAWESLLPE 218
Cofac_haem_bdg pfam04187
Haem-binding uptake, Tiki superfamily, ChaN; This is a family of putative bacterial ...
 808-1027 4.88e-52

Haem-binding uptake, Tiki superfamily, ChaN; This is a family of putative bacterial lipoproteins necessary for the uptake of haem-iron. The structure of UniProtKB:Q0PBW2, PDB:2g5g, comprises a large parallel beta-sheet with flanking alpha-helices and a smaller domain consisting of alpha-helices. Two cofacial haem groups (~3.5 Angstom apart with an inter-iron distance of 4.4 Angstrom) bind in a pocket formed by a dimer of two ChaN monomers.


:

Pssm-ID: 461215  Cd Length: 211  Bit Score: 182.08  E-value: 4.88e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  808 WEKLMAARVVYLGEAElvPDRDDRVLELEVVRKLAARCAeagRSISLALEAFPCNLQEQLNQFMDRRIDGNNLRLYT--- 884
Cdd:pfam04187    1 LARLADADVVLLGEQH--DNPDHHRLQLEILKALHARAR---PALALGLEMFERDQQPALDRYLAGEIDEAELLEELdwq 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  885 SHWaPERWQEYEPLLNYCRDNGVKLVACGTPLEVSRTVQAEGIRGLSKA-QRKLYAPPAGsgfiSGFTSISGRSLIDKIS 963
Cdd:pfam04187   76 RRW-PNDWALYRPLVEFARENGLPLVALNVPRELVRKVAREGLESLDPLpERARVSLPPL----PDPPSEAYRARLLAVF 150

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443034972  964 AIH--GSPFGPSSYLSAQARVVDDYTMSQKIMKEITNGypSGMLVVVTGSSHVIYgsrGIGVPARI 1027
Cdd:pfam04187  151 GGHhcGALPGESLERFVEAQVLWDATMAESIAQALKPN--PRKVVVIAGSGHVRY---GLGIPARL 211
PX_domain super family cl02563
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
 156-275 1.45e-48

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 cd06865:

Pssm-ID: 470617  Cd Length: 120  Bit Score: 168.75  E-value: 1.45e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  156 QITVSEPKKHAEPAAgaagVIPGSGSYFSYLITTRAA----DGGLFRVRRRFRDVVALADRLAAAYRGLFVPARPDKSIV 231
Cdd:cd06865      1 KITVSDPKKEQEPSR----VPLGGPPYISYKVTTRTNipsyTHGEFTVRRRFRDVVALADRLAEAYRGAFVPPRPDKSVV 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1443034972  232 EGQVMQRHEFVNQRCAALQRYLGRLAAHPTIGRSAELHDFLTEP 275
Cdd:cd06865     77 ESQVMQSAEFIEQRRVALEKYLNRLAAHPVIGLSDELRVFLTLQ 120
 
Name Accession Description Interval E-value
RETICULATA-like pfam11891
Protein RETICULATA-related; This entry represents RETICULATA and related proteins from plants. ...
 1134-1317 4.76e-74

Protein RETICULATA-related; This entry represents RETICULATA and related proteins from plants. Arabidopsis RETICULATA protein is involved in differential development of bundle sheath and mesophyll cell chloroplasts.


Pssm-ID: 432167  Cd Length: 177  Bit Score: 243.64  E-value: 4.76e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972 1134 ERLLADPKFLHRLAIEEGISITTTLIAQYEKRKGRFLEEIDYVLTDTIRGSVVDFFTVWLPAPTISLLSLGDNGSGesle 1213
Cdd:pfam11891    1 ERLLADPSFLFKLLIEEAIGVGASLLAEYEKRGERFWNELDLVFADVVVGSVVNFALVWLLAPTRSYGSTSAFAGA---- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972 1214 lLKGLLGSLPDNAFQKGIMGQSWNTNQRFASVLMGGIKLAGVGFISSIGAGVASDVLYAARRVLRPstSVETARRRTPIW 1293
Cdd:pfam11891   77 -LQNLLGSLPNNAFEKSYPGREFTLQQRIAAFFYKGAELAAVGFAAGLVGTGLSNALIALRKKMDP--SFEPSVKVPPVV 153

                          170       180
                   ....*....|....*....|....
gi 1443034972 1294 KSATVYSCFLGTSANLRYQVIAGL 1317
Cdd:pfam11891  154 KNALGYGAFMGVSSNLRYQILAGL 177
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 340-568 3.39e-58

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 200.27  E-value: 3.39e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  340 ETDAKFVMHKAKLEYFEQHLTTASQQVEALLKAYDDLKATTGQLGMTFIKLAKFEKEqdtcNSQRKRAVDMSNFANAVIN 419
Cdd:cd07596      1 EEDQEFEEAKDYILKLEEQLKKLSKQAQRLVKRRRELGSALGEFGKALIKLAKCEEE----VGGELGEALSKLGKAAEEL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  420 MSRSQTKLNAKIEIHLGTIYEYLETMTSVRNAFTDRANALLRVQSLSGDLFLLHTQAAKLESVSSrgmgqerLRYQKIEE 499
Cdd:cd07596     77 SSLSEAQANQELVKLLEPLKEYLRYCQAVKETLDDRADALLTLQSLKKDLASKKAQLEKLKAAPG-------IKPAKVEE 149

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443034972  500 LKETIRKTEDAKGNARQEYELIKENNMNEIIRFNKEKRHGLVEMLKGFVRNQVSYSEHISSIWTKVAEE 568
Cdd:cd07596    150 LEEELEEAESALEEARKRYEEISERLKEELKRFHEERARDLKAALKEFARLQVQYAEKIAEAWESLLPE 218
Cofac_haem_bdg pfam04187
Haem-binding uptake, Tiki superfamily, ChaN; This is a family of putative bacterial ...
 808-1027 4.88e-52

Haem-binding uptake, Tiki superfamily, ChaN; This is a family of putative bacterial lipoproteins necessary for the uptake of haem-iron. The structure of UniProtKB:Q0PBW2, PDB:2g5g, comprises a large parallel beta-sheet with flanking alpha-helices and a smaller domain consisting of alpha-helices. Two cofacial haem groups (~3.5 Angstom apart with an inter-iron distance of 4.4 Angstrom) bind in a pocket formed by a dimer of two ChaN monomers.


Pssm-ID: 461215  Cd Length: 211  Bit Score: 182.08  E-value: 4.88e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  808 WEKLMAARVVYLGEAElvPDRDDRVLELEVVRKLAARCAeagRSISLALEAFPCNLQEQLNQFMDRRIDGNNLRLYT--- 884
Cdd:pfam04187    1 LARLADADVVLLGEQH--DNPDHHRLQLEILKALHARAR---PALALGLEMFERDQQPALDRYLAGEIDEAELLEELdwq 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  885 SHWaPERWQEYEPLLNYCRDNGVKLVACGTPLEVSRTVQAEGIRGLSKA-QRKLYAPPAGsgfiSGFTSISGRSLIDKIS 963
Cdd:pfam04187   76 RRW-PNDWALYRPLVEFARENGLPLVALNVPRELVRKVAREGLESLDPLpERARVSLPPL----PDPPSEAYRARLLAVF 150

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443034972  964 AIH--GSPFGPSSYLSAQARVVDDYTMSQKIMKEITNGypSGMLVVVTGSSHVIYgsrGIGVPARI 1027
Cdd:pfam04187  151 GGHhcGALPGESLERFVEAQVLWDATMAESIAQALKPN--PRKVVVIAGSGHVRY---GLGIPARL 211
PX_SNX_like cd06865
The phosphoinositide binding Phox Homology domain of SNX-like proteins; The PX domain is a ...
 156-275 1.45e-48

The phosphoinositide binding Phox Homology domain of SNX-like proteins; 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. This subfamily is composed of uncharacterized proteins, predominantly from plants, with similarity to sorting nexins. A few members show a similar domain architecture as a subfamily of sorting nexins, containing a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. The PX-BAR structural unit is known to determine specific membrane localization.


Pssm-ID: 132775  Cd Length: 120  Bit Score: 168.75  E-value: 1.45e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  156 QITVSEPKKHAEPAAgaagVIPGSGSYFSYLITTRAA----DGGLFRVRRRFRDVVALADRLAAAYRGLFVPARPDKSIV 231
Cdd:cd06865      1 KITVSDPKKEQEPSR----VPLGGPPYISYKVTTRTNipsyTHGEFTVRRRFRDVVALADRLAEAYRGAFVPPRPDKSVV 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1443034972  232 EGQVMQRHEFVNQRCAALQRYLGRLAAHPTIGRSAELHDFLTEP 275
Cdd:cd06865     77 ESQVMQSAEFIEQRRVALEKYLNRLAAHPVIGLSDELRVFLTLQ 120
ChanN-like cd14727
ChaN is an iron-regulated, heme-binding protein; This family represents a domain found in ChaN, ...
 815-1027 4.15e-28

ChaN is an iron-regulated, heme-binding protein; This family represents a domain found in ChaN, a heme-binding/iron-regulated lipoprotein from Campylobacter jejuni. ChaN, possibly involved in the uptake of heme-iron, contains a pair of cofacial heme groups situated between two ChaN monomers. A single tyrosine residue contacts the heme-bound iron atom while the heme-binding regions of each monomer also have contacts to the heme in the complementary monomer. ChaN presumably associates with an outer membrane-associated receptor, ChaR. Campylobacter jejuni is an important cause of food-borne illness, and is dependent on iron uptake from the host. ChaN like proteins are related to the Tiki/TraB like family of proteases. Proteins containing this domain also include protein reticulata-related from Arabidopsis which may play a role in leaf development.


Pssm-ID: 350609  Cd Length: 211  Bit Score: 113.46  E-value: 4.15e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  815 RVVYLGEAElvPDRDDRVLELEVVRKLAARcaeaGRSISLALEAFPCNLQEQLNQFMDRRIDGNNLRL--YTSHWaPERW 892
Cdd:cd14727      1 DVVLLGEVH--DNPAHHRLQLELLRALAAR----GPRLALGLEMFERDQQPVLDEYLAGEISEEELELldWARGW-PNYF 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  893 QEYEPLLNYCRDNGVKLVACGTPLEVSRTVQAEGIRGLSKAQRKLYAPPAgsgfisGFTSISGRSLIDKISAIHGSPFGP 972
Cdd:cd14727     74 TLYRPLFEFARENGLPVVALNVPREYVRKVAREGLESLDEEERALLPLDI------DLPDPAYRARLEAVFGGHCGGLPE 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1443034972  973 SSYLS-AQARVVDDYTMSQKIMKEITNgYPSGMLVVVTGSSHVIYgsrGIGVPARI 1027
Cdd:cd14727    148 EMFENfVEAQALWDATMAESIAEALKA-NPGGPVVVIAGSGHVRY---GLGIPARL 199
PhuW COG3016
Putative heme-binding protein PhuW [General function prediction only];
809-1062 2.53e-24

Putative heme-binding protein PhuW [General function prediction only];


Pssm-ID: 442253  Cd Length: 287  Bit Score: 104.65  E-value: 2.53e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  809 EKLMAARVVYLGeaELVPDRDDRVLELEVVRKLAARcaeaGRSISLALEAFPCNLQEQLNQFMDRRIDGNNLR---LYTS 885
Cdd:COG3016     48 AELADADVVLLG--EKHDNPAHHRLQLELLQALHAQ----GPQLALGMEMFERDQQPALDRYLAGEISEAELLeaaEWDR 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  886 HWaPERWQEYEPLLNYCRDNGVKLVACGTPLEVSRTVQAEGIRGLSKAQRKLYAPPAgsgfisgFTSISG-RSLIDKISA 964
Cdd:COG3016    122 GW-PNYWELYRPLVEFAKEHGLPLLALNLPRELVRKVAREGLEALPPEERAYLPLDI-------DLPDPAyRALLAEIMG 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  965 IHG--SPFGPSSYLSAQArvVDDYTMSQKIMKEITNgYPSGMLVVVTGSSHVIYgsrGIGVPARIsKKMQKKKQVVVLLN 1042
Cdd:COG3016    194 GHGalPEEQLERFVAAQQ--LWDATMAESIAAALKA-HPGRPVVLIAGSGHVRY---GLGVPLRL-ARRLPGLKVVVLLP 266

                          250       260
                   ....*....|....*....|
gi 1443034972 1043 PERQGIRREGEIPVADFLWY 1062
Cdd:COG3016    267 VEQGEPEELDPAGIADYVWF 286
Vps5 pfam09325
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is ...
 339-536 5.64e-11

Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is the C terminal dimerization domain.


Pssm-ID: 430527 [Multi-domain]  Cd Length: 236  Bit Score: 64.22  E-value: 5.64e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  339 EETDAKFVMHKAKLEYFEQHLTTASQQVEALLKAYDDLKATTGQLGMTFIKLAKFEKEQDTCNSqrkravdMSNFANAVI 418
Cdd:pfam09325   20 NEPDEWFIDKKQYIDSLESQLKKLYKALELLVSQRKELASATGEFAKSLASLASLELSTGLSRA-------LSQLAEVEE 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  419 NMSRSQTKLNAKIEIHLG-TIYEYLETMTSVRNAFTDRANALLRVQSLSGDLFLLHTQAAKLEsvssrgmGQERLRYQKI 497
Cdd:pfam09325   93 RIKELLERQALQDVLTLGeTIDEYLRLIGSVKAVFNQRVKAWQSWQNAEQELSKKKEQLEKLL-------RANKSQNDKL 165

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1443034972  498 EELKETIRKTEDAKGNARQEYELIKENNMNEIIRFNKEK 536
Cdd:pfam09325  166 QQAKKEVEELERRVQQAEKEFEDISELIKKELERFELER 204
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 209-275 2.33e-07

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 49.55  E-value: 2.33e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443034972  209 LADRLAAAYRGLFVPARPDKSIVeGQVMQrhEFVNQRCAALQRYLGRLAAHPTIGRSAELHDFLTEP 275
Cdd:pfam00787   21 LHKKLLRKFPSVIIPPLPPKRWL-GRYNE--EFIEKRRKGLEQYLQRLLQHPELRNSEVLLEFLESD 84
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
 152-568 3.52e-07

Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only];


Pssm-ID: 227680 [Multi-domain]  Cd Length: 524  Bit Score: 54.80  E-value: 3.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  152 PEFVQITVSEPKKHAEPaagaagvIPGSGSYFSYLITTRAADGGLFRVRRRFRDVV-------ALADRLAAAYRGLFVPA 224
Cdd:COG5391    128 DYFISSTVSNPQSLTLL-------VDSRDKHTSYEIITVTNLPSFQLRESRPLVVRrrysdfeSLHSILIKLLPLCAIPP 200

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  225 RPDKSIVEGQVMQR--HEFVNQRCAALQRYLGRLAAHPTIGRSAELHDFLTEPSGIPTSAgESPRSDPALSaamsaaavt 302
Cdd:COG5391    201 LPSKKSNSEYYGDRfsDEFIEERRQSLQNFLRRVSTHPLLSNYKNSKSWESHSTLLSSFI-ENRKSVPTPL--------- 270

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  303 aptapakpgrdifgmFKDLKQTVANGLVAVRPPPVEEETDAKFVMHK--------AKLEYFEQHLTTASQQVEALLKAYD 374
Cdd:COG5391    271 ---------------SLDLTSTTQELDMERKELNESTSKAIHNILSIfslfekilIQLESEEESLTRLLESLNNLLLLVL 335

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  375 DlkattgQLGMTFIKLAKFEkeqdtcnsqrkravdmsnfaNAVINMS--RSQTKLNAKIEIH---LGTIYEYLETMTSVR 449
Cdd:COG5391    336 N------FSGVFAKRLEQNQ--------------------NSILNEGvvQAETLRSSLKELLtqlQDEIKSRESLILTDS 389

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  450 NAFTDRANALLRVQSLSGDlfLLHTQAAKLESVS--------------SRGMGQERLRYQKIEELKETIRKTEDAKGNAR 515
Cdd:COG5391    390 NLEKLTDQNLEDVEELSRS--LRKNSSQRAVVSQqpegltsfsklsykLRDFVQEKSRSKSIESLQQDKEKLEEQLAIAE 467

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1443034972  516 QEYELIKENNMNEIIRFNKEKRHGLVEMLKGFVRNQVSYSEHISSIWTKVAEE 568
Cdd:COG5391    468 KDAQEINEELKNELKFFFSVRNSDLEKILKSVADSHIEWAEENLEIWKSVKEQ 520
 
Name Accession Description Interval E-value
RETICULATA-like pfam11891
Protein RETICULATA-related; This entry represents RETICULATA and related proteins from plants. ...
 1134-1317 4.76e-74

Protein RETICULATA-related; This entry represents RETICULATA and related proteins from plants. Arabidopsis RETICULATA protein is involved in differential development of bundle sheath and mesophyll cell chloroplasts.


Pssm-ID: 432167  Cd Length: 177  Bit Score: 243.64  E-value: 4.76e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972 1134 ERLLADPKFLHRLAIEEGISITTTLIAQYEKRKGRFLEEIDYVLTDTIRGSVVDFFTVWLPAPTISLLSLGDNGSGesle 1213
Cdd:pfam11891    1 ERLLADPSFLFKLLIEEAIGVGASLLAEYEKRGERFWNELDLVFADVVVGSVVNFALVWLLAPTRSYGSTSAFAGA---- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972 1214 lLKGLLGSLPDNAFQKGIMGQSWNTNQRFASVLMGGIKLAGVGFISSIGAGVASDVLYAARRVLRPstSVETARRRTPIW 1293
Cdd:pfam11891   77 -LQNLLGSLPNNAFEKSYPGREFTLQQRIAAFFYKGAELAAVGFAAGLVGTGLSNALIALRKKMDP--SFEPSVKVPPVV 153

                          170       180
                   ....*....|....*....|....
gi 1443034972 1294 KSATVYSCFLGTSANLRYQVIAGL 1317
Cdd:pfam11891  154 KNALGYGAFMGVSSNLRYQILAGL 177
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 340-568 3.39e-58

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 200.27  E-value: 3.39e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  340 ETDAKFVMHKAKLEYFEQHLTTASQQVEALLKAYDDLKATTGQLGMTFIKLAKFEKEqdtcNSQRKRAVDMSNFANAVIN 419
Cdd:cd07596      1 EEDQEFEEAKDYILKLEEQLKKLSKQAQRLVKRRRELGSALGEFGKALIKLAKCEEE----VGGELGEALSKLGKAAEEL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  420 MSRSQTKLNAKIEIHLGTIYEYLETMTSVRNAFTDRANALLRVQSLSGDLFLLHTQAAKLESVSSrgmgqerLRYQKIEE 499
Cdd:cd07596     77 SSLSEAQANQELVKLLEPLKEYLRYCQAVKETLDDRADALLTLQSLKKDLASKKAQLEKLKAAPG-------IKPAKVEE 149

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443034972  500 LKETIRKTEDAKGNARQEYELIKENNMNEIIRFNKEKRHGLVEMLKGFVRNQVSYSEHISSIWTKVAEE 568
Cdd:cd07596    150 LEEELEEAESALEEARKRYEEISERLKEELKRFHEERARDLKAALKEFARLQVQYAEKIAEAWESLLPE 218
Cofac_haem_bdg pfam04187
Haem-binding uptake, Tiki superfamily, ChaN; This is a family of putative bacterial ...
 808-1027 4.88e-52

Haem-binding uptake, Tiki superfamily, ChaN; This is a family of putative bacterial lipoproteins necessary for the uptake of haem-iron. The structure of UniProtKB:Q0PBW2, PDB:2g5g, comprises a large parallel beta-sheet with flanking alpha-helices and a smaller domain consisting of alpha-helices. Two cofacial haem groups (~3.5 Angstom apart with an inter-iron distance of 4.4 Angstrom) bind in a pocket formed by a dimer of two ChaN monomers.


Pssm-ID: 461215  Cd Length: 211  Bit Score: 182.08  E-value: 4.88e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  808 WEKLMAARVVYLGEAElvPDRDDRVLELEVVRKLAARCAeagRSISLALEAFPCNLQEQLNQFMDRRIDGNNLRLYT--- 884
Cdd:pfam04187    1 LARLADADVVLLGEQH--DNPDHHRLQLEILKALHARAR---PALALGLEMFERDQQPALDRYLAGEIDEAELLEELdwq 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  885 SHWaPERWQEYEPLLNYCRDNGVKLVACGTPLEVSRTVQAEGIRGLSKA-QRKLYAPPAGsgfiSGFTSISGRSLIDKIS 963
Cdd:pfam04187   76 RRW-PNDWALYRPLVEFARENGLPLVALNVPRELVRKVAREGLESLDPLpERARVSLPPL----PDPPSEAYRARLLAVF 150

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443034972  964 AIH--GSPFGPSSYLSAQARVVDDYTMSQKIMKEITNGypSGMLVVVTGSSHVIYgsrGIGVPARI 1027
Cdd:pfam04187  151 GGHhcGALPGESLERFVEAQVLWDATMAESIAQALKPN--PRKVVVIAGSGHVRY---GLGIPARL 211
PX_SNX_like cd06865
The phosphoinositide binding Phox Homology domain of SNX-like proteins; The PX domain is a ...
 156-275 1.45e-48

The phosphoinositide binding Phox Homology domain of SNX-like proteins; 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. This subfamily is composed of uncharacterized proteins, predominantly from plants, with similarity to sorting nexins. A few members show a similar domain architecture as a subfamily of sorting nexins, containing a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. The PX-BAR structural unit is known to determine specific membrane localization.


Pssm-ID: 132775  Cd Length: 120  Bit Score: 168.75  E-value: 1.45e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  156 QITVSEPKKHAEPAAgaagVIPGSGSYFSYLITTRAA----DGGLFRVRRRFRDVVALADRLAAAYRGLFVPARPDKSIV 231
Cdd:cd06865      1 KITVSDPKKEQEPSR----VPLGGPPYISYKVTTRTNipsyTHGEFTVRRRFRDVVALADRLAEAYRGAFVPPRPDKSVV 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1443034972  232 EGQVMQRHEFVNQRCAALQRYLGRLAAHPTIGRSAELHDFLTEP 275
Cdd:cd06865     77 ESQVMQSAEFIEQRRVALEKYLNRLAAHPVIGLSDELRVFLTLQ 120
ChanN-like cd14727
ChaN is an iron-regulated, heme-binding protein; This family represents a domain found in ChaN, ...
 815-1027 4.15e-28

ChaN is an iron-regulated, heme-binding protein; This family represents a domain found in ChaN, a heme-binding/iron-regulated lipoprotein from Campylobacter jejuni. ChaN, possibly involved in the uptake of heme-iron, contains a pair of cofacial heme groups situated between two ChaN monomers. A single tyrosine residue contacts the heme-bound iron atom while the heme-binding regions of each monomer also have contacts to the heme in the complementary monomer. ChaN presumably associates with an outer membrane-associated receptor, ChaR. Campylobacter jejuni is an important cause of food-borne illness, and is dependent on iron uptake from the host. ChaN like proteins are related to the Tiki/TraB like family of proteases. Proteins containing this domain also include protein reticulata-related from Arabidopsis which may play a role in leaf development.


Pssm-ID: 350609  Cd Length: 211  Bit Score: 113.46  E-value: 4.15e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  815 RVVYLGEAElvPDRDDRVLELEVVRKLAARcaeaGRSISLALEAFPCNLQEQLNQFMDRRIDGNNLRL--YTSHWaPERW 892
Cdd:cd14727      1 DVVLLGEVH--DNPAHHRLQLELLRALAAR----GPRLALGLEMFERDQQPVLDEYLAGEISEEELELldWARGW-PNYF 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  893 QEYEPLLNYCRDNGVKLVACGTPLEVSRTVQAEGIRGLSKAQRKLYAPPAgsgfisGFTSISGRSLIDKISAIHGSPFGP 972
Cdd:cd14727     74 TLYRPLFEFARENGLPVVALNVPREYVRKVAREGLESLDEEERALLPLDI------DLPDPAYRARLEAVFGGHCGGLPE 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1443034972  973 SSYLS-AQARVVDDYTMSQKIMKEITNgYPSGMLVVVTGSSHVIYgsrGIGVPARI 1027
Cdd:cd14727    148 EMFENfVEAQALWDATMAESIAEALKA-NPGGPVVVIAGSGHVRY---GLGIPARL 199
PhuW COG3016
Putative heme-binding protein PhuW [General function prediction only];
809-1062 2.53e-24

Putative heme-binding protein PhuW [General function prediction only];


Pssm-ID: 442253  Cd Length: 287  Bit Score: 104.65  E-value: 2.53e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  809 EKLMAARVVYLGeaELVPDRDDRVLELEVVRKLAARcaeaGRSISLALEAFPCNLQEQLNQFMDRRIDGNNLR---LYTS 885
Cdd:COG3016     48 AELADADVVLLG--EKHDNPAHHRLQLELLQALHAQ----GPQLALGMEMFERDQQPALDRYLAGEISEAELLeaaEWDR 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  886 HWaPERWQEYEPLLNYCRDNGVKLVACGTPLEVSRTVQAEGIRGLSKAQRKLYAPPAgsgfisgFTSISG-RSLIDKISA 964
Cdd:COG3016    122 GW-PNYWELYRPLVEFAKEHGLPLLALNLPRELVRKVAREGLEALPPEERAYLPLDI-------DLPDPAyRALLAEIMG 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  965 IHG--SPFGPSSYLSAQArvVDDYTMSQKIMKEITNgYPSGMLVVVTGSSHVIYgsrGIGVPARIsKKMQKKKQVVVLLN 1042
Cdd:COG3016    194 GHGalPEEQLERFVAAQQ--LWDATMAESIAAALKA-HPGRPVVLIAGSGHVRY---GLGVPLRL-ARRLPGLKVVVLLP 266

                          250       260
                   ....*....|....*....|
gi 1443034972 1043 PERQGIRREGEIPVADFLWY 1062
Cdd:COG3016    267 VEQGEPEELDPAGIADYVWF 286
PX_SNX1_2_like cd06859
The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is ...
 156-273 2.78e-13

The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; 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 SNX1, SNX2, and similar proteins. They harbor a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. Both domains have been shown to determine the specific membrane-targeting of SNX1. SNX1 and SNX2 are components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures effcient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex.


Pssm-ID: 132769 [Multi-domain]  Cd Length: 114  Bit Score: 67.60  E-value: 2.78e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  156 QITVSEPKKHAEpaagaagvipGSGSYFSYLITTRAADGGLFRVRRRFR----DVVALADRLAAAYRGLFVPARPDKSIV 231
Cdd:cd06859      2 EISVTDPVKVGD----------GMSAYVVYRVTTKTNLPDFKKSEFSVLrrysDFLWLYERLVEKYPGRIVPPPPEKQAV 71

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1443034972  232 eGQVMQRHEFVNQRCAALQRYLGRLAAHPTIGRSAELHDFLT 273
Cdd:cd06859     72 -GRFKVKFEFIEKRRAALERFLRRIAAHPVLRKDPDFRLFLE 112
PX_SNX7_30_like cd06860
The phosphoinositide binding Phox Homology domain of Sorting Nexins 7 and 30; The PX domain is ...
 156-273 1.20e-12

The phosphoinositide binding Phox Homology domain of Sorting Nexins 7 and 30; 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. This subfamily consists of SNX7, SNX30, and similar proteins. They harbor a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to the sorting nexins SNX1-2, SNX4-6, SNX8, and SNX32. Both domains have been shown to determine the specific membrane-targeting of SNX1. The specific function of the sorting nexins in this subfamily has yet to be elucidated.


Pssm-ID: 132770  Cd Length: 116  Bit Score: 65.82  E-value: 1.20e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  156 QITVSEPKKHAEPAagaagvipgsGSYFSYLITTRAA----DGGLFRVRRRFRDVVALADRLAAAYRGLFVPARPDKSIV 231
Cdd:cd06860      2 FITVDNPEKHVTTL----------ETYITYRVTTKTTrsefDSSEYSVRRRYQDFLWLRQKLEESHPTHIIPPLPEKHSV 71

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1443034972  232 EGQVmQRH--EFVNQRCAALQRYLGRLAAHPTIGRSAELHDFLT 273
Cdd:cd06860     72 KGLL-DRFspEFVATRMRALHKFLNRIVEHPVLSFNEHLKVFLT 114
BAR_Vps5p cd07627
The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are ...
 340-536 4.07e-12

The Bin/Amphiphysin/Rvs (BAR) domain of yeast Sorting Nexin Vps5p; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. Vsp5p is the yeast counterpart of human SNX1 and is part of the retromer complex, which functions in the endosome-to-Golgi retrieval of vacuolar protein sorting receptor Vps10p, the Golgi-resident membrane protein A-ALP, and endopeptidase Kex2. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153311 [Multi-domain]  Cd Length: 216  Bit Score: 66.94  E-value: 4.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  340 ETDAKFVMHKAKLEYFEQHLTTASQQVEALLKAYDDLKATTGQLGMTFIKLAKFEKEQDTCNSqrkravdMSNFANAVIN 419
Cdd:cd07627      1 EPDEWFIEKKQYLDSLESQLKQLYKSLELVSSQRKELASATEEFAETLEALSSLELSKSLSDL-------LAALAEVQKR 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  420 MSRSQTKLNAKIEIHLG-TIYEYLETMTSVRNAFTDRANALLRVQSLSGDLFLLHTQAAKLESVSSrgMGQERLRYQKiE 498
Cdd:cd07627     74 IKESLERQALQDVLTLGvTLDEYIRSIGSVRAAFAQRQKLWQYWQSAESELSKKKAQLEKLKRQGK--TQQEKLNSLL-S 150

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1443034972  499 ELKETIRKTEDAKgnarQEYELIKENNMNEIIRFNKEK 536
Cdd:cd07627    151 ELEEAERRASELK----KEFEEVSELIKSELERFERER 184
Vps5 pfam09325
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is ...
 339-536 5.64e-11

Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is the C terminal dimerization domain.


Pssm-ID: 430527 [Multi-domain]  Cd Length: 236  Bit Score: 64.22  E-value: 5.64e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  339 EETDAKFVMHKAKLEYFEQHLTTASQQVEALLKAYDDLKATTGQLGMTFIKLAKFEKEQDTCNSqrkravdMSNFANAVI 418
Cdd:pfam09325   20 NEPDEWFIDKKQYIDSLESQLKKLYKALELLVSQRKELASATGEFAKSLASLASLELSTGLSRA-------LSQLAEVEE 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  419 NMSRSQTKLNAKIEIHLG-TIYEYLETMTSVRNAFTDRANALLRVQSLSGDLFLLHTQAAKLEsvssrgmGQERLRYQKI 497
Cdd:pfam09325   93 RIKELLERQALQDVLTLGeTIDEYLRLIGSVKAVFNQRVKAWQSWQNAEQELSKKKEQLEKLL-------RANKSQNDKL 165

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1443034972  498 EELKETIRKTEDAKGNARQEYELIKENNMNEIIRFNKEK 536
Cdd:pfam09325  166 QQAKKEVEELERRVQQAEKEFEDISELIKKELERFELER 204
PX_SNX2 cd07282
The phosphoinositide binding Phox Homology domain of Sorting Nexin 2; The PX domain is a ...
 155-272 8.59e-10

The phosphoinositide binding Phox Homology domain of Sorting Nexin 2; 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. SNX2 is a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures efficient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. Similar to SNX1, SNX2 contains a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. The PX domain of SNX2 preferentially binds phosphatidylinositol-3-phosphate (PI3P), but not PI(3,4,5)P3. Studies on mice deficient with SNX1 and/or SNX2 suggest that they provide an essential function in embryogenesis and are functionally redundant.


Pssm-ID: 132815  Cd Length: 124  Bit Score: 58.14  E-value: 8.59e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  155 VQITVSEPKKhaepaagaagVIPGSGSYFSYLITTRAADGGLFRVRRRFRDVVA----LADRLAAAYR--GLFVPARPDK 228
Cdd:cd07282      1 IEIGVSDPEK----------VGDGMNAYMAYRVTTKTSLSMFSRSEFSVRRRFSdflgLHSKLASKYLhvGYIVPPAPEK 70

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1443034972  229 SIVE-------GQVMQRHEFVNQRCAALQRYLGRLAAHPTIGRSAELHDFL 272
Cdd:cd07282     71 SIVGmtkvkvgKEDSSSTEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFL 121
PX_Atg24p cd06863
The phosphoinositide binding Phox Homology domain of yeast Atg24p, an autophagic degradation ...
 156-275 2.13e-09

The phosphoinositide binding Phox Homology domain of yeast Atg24p, an autophagic degradation protein; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. The yeast Atg24p is a sorting nexin (SNX) which is involved in membrane fusion events at the vacuolar surface during pexophagy. This is facilitated via binding of Atg24p to phosphatidylinositol 3-phosphate (PI3P) through its PX 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. 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.


Pssm-ID: 132773  Cd Length: 118  Bit Score: 56.53  E-value: 2.13e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  156 QITVSEPKKHAEPaagaagvipGSGSYFSYLITTRAADGGLFRVRRRFRDV----VALADRLAAAYRGLFVPARPDKSIV 231
Cdd:cd06863      2 ECLVSDPQKELDG---------SSDTYISYLITTKTNLPSFSRKEFKVRRRysdfVFLHECLSNDFPACVVPPLPDKHRL 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1443034972  232 EGQVMQR--HEFVNQRCAALQRYLGRLAAHPTIGRSAELHDFLTEP 275
Cdd:cd06863     73 EYITGDRfsPEFITRRAQSLQRFLRRISLHPVLSQSKILHQFLESS 118
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 209-275 2.33e-07

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 49.55  E-value: 2.33e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443034972  209 LADRLAAAYRGLFVPARPDKSIVeGQVMQrhEFVNQRCAALQRYLGRLAAHPTIGRSAELHDFLTEP 275
Cdd:pfam00787   21 LHKKLLRKFPSVIIPPLPPKRWL-GRYNE--EFIEKRRKGLEQYLQRLLQHPELRNSEVLLEFLESD 84
PX_domain cd06093
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
 208-273 2.49e-07

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: 50.43  E-value: 2.49e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443034972  208 ALADRLAAAYRGLFVPARPDKSIVegqVMQRHEFVNQRCAALQRYLGRLAAHPTIGRSAELHDFLT 273
Cdd:cd06093     43 ELHEKLKKKFPGVILPPLPPKKLF---GNLDPEFIEERRKQLEQYLQSLLNHPELRNSEELKEFLE 105
PX_SNX7 cd07284
The phosphoinositide binding Phox Homology domain of Sorting Nexin 7; The PX domain is a ...
 157-273 2.87e-07

The phosphoinositide binding Phox Homology domain of Sorting Nexin 7; 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. SNX7 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to the sorting nexins SNX1-2, SNX4-6, SNX8, SNX30, and SNX32. Both domains have been shown to determine the specific membrane-targeting of SNX1. The specific function of SNX7 has yet to be elucidated.


Pssm-ID: 132817  Cd Length: 116  Bit Score: 50.36  E-value: 2.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  157 ITVSEPKKHaepaagaagvIPGSGSYFSYLITTRAA----DGGLFRVRRRFRDVVALADRLAAAYRGLFVPARPDKSIVE 232
Cdd:cd07284      3 ITVDEPESH----------VTAIETFITYRVMTKTSrsefDSSEFEVRRRYQDFLWLKGRLEEAHPTLIIPPLPEKFVMK 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1443034972  233 GQVMQ-RHEFVNQRCAALQRYLGRLAAHPTIGRSAELHDFLT 273
Cdd:cd07284     73 GMVERfNEDFIETRRKALHKFLNRIADHPTLTFNEDFKIFLT 114
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
 152-568 3.52e-07

Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only];


Pssm-ID: 227680 [Multi-domain]  Cd Length: 524  Bit Score: 54.80  E-value: 3.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  152 PEFVQITVSEPKKHAEPaagaagvIPGSGSYFSYLITTRAADGGLFRVRRRFRDVV-------ALADRLAAAYRGLFVPA 224
Cdd:COG5391    128 DYFISSTVSNPQSLTLL-------VDSRDKHTSYEIITVTNLPSFQLRESRPLVVRrrysdfeSLHSILIKLLPLCAIPP 200

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  225 RPDKSIVEGQVMQR--HEFVNQRCAALQRYLGRLAAHPTIGRSAELHDFLTEPSGIPTSAgESPRSDPALSaamsaaavt 302
Cdd:COG5391    201 LPSKKSNSEYYGDRfsDEFIEERRQSLQNFLRRVSTHPLLSNYKNSKSWESHSTLLSSFI-ENRKSVPTPL--------- 270

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  303 aptapakpgrdifgmFKDLKQTVANGLVAVRPPPVEEETDAKFVMHK--------AKLEYFEQHLTTASQQVEALLKAYD 374
Cdd:COG5391    271 ---------------SLDLTSTTQELDMERKELNESTSKAIHNILSIfslfekilIQLESEEESLTRLLESLNNLLLLVL 335

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  375 DlkattgQLGMTFIKLAKFEkeqdtcnsqrkravdmsnfaNAVINMS--RSQTKLNAKIEIH---LGTIYEYLETMTSVR 449
Cdd:COG5391    336 N------FSGVFAKRLEQNQ--------------------NSILNEGvvQAETLRSSLKELLtqlQDEIKSRESLILTDS 389

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  450 NAFTDRANALLRVQSLSGDlfLLHTQAAKLESVS--------------SRGMGQERLRYQKIEELKETIRKTEDAKGNAR 515
Cdd:COG5391    390 NLEKLTDQNLEDVEELSRS--LRKNSSQRAVVSQqpegltsfsklsykLRDFVQEKSRSKSIESLQQDKEKLEEQLAIAE 467

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1443034972  516 QEYELIKENNMNEIIRFNKEKRHGLVEMLKGFVRNQVSYSEHISSIWTKVAEE 568
Cdd:COG5391    468 KDAQEINEELKNELKFFFSVRNSDLEKILKSVADSHIEWAEENLEIWKSVKEQ 520
PX_SNX9_18_like cd06862
The phosphoinositide binding Phox Homology domain of Sorting Nexins 9 and 18; The PX domain is ...
 209-276 2.56e-06

The phosphoinositide binding Phox Homology domain of Sorting Nexins 9 and 18; 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 SNX9, SNX18, and similar proteins. They contain an N-terminal Src Homology 3 (SH3) domain, a PX domain, and a C-terminal Bin/Amphiphysin/Rvs (BAR) domain. SNX9 is localized to plasma membrane endocytic sites and acts primarily in clathrin-mediated endocytosis, while SNX18 is localized to peripheral endosomal structures, and acts in a trafficking pathway that is clathrin-independent but relies on AP-1 and PACS1.


Pssm-ID: 132772  Cd Length: 125  Bit Score: 48.08  E-value: 2.56e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  209 LADRLAAAYRGLFVPARPDKsivegQVMQRHE--FVNQRCAALQRYLGRLAAHPTIGRSAELHDFLTEPS 276
Cdd:cd06862     44 LYERLVEKYSCIAIPPLPEK-----QVTGRFEedFIEKRRERLELWMNRLARHPVLSQSEVFRHFLTCTD 108
PX_SNX4 cd06864
The phosphoinositide binding Phox Homology domain of Sorting Nexin 4; The PX domain is a ...
 155-274 5.19e-06

The phosphoinositide binding Phox Homology domain of Sorting Nexin 4; 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. SNX4 is involved in recycling traffic from the sorting endosome (post-Golgi endosome) back to the late Golgi. It shows a similar domain architecture as SNX1-2, among others, containing a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. SNX4 is implicated in the regulation of plasma membrane receptor trafficking and interacts with receptors for EGF, insulin, platelet-derived growth factor and the long form of the leptin receptor.


Pssm-ID: 132774  Cd Length: 129  Bit Score: 47.36  E-value: 5.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  155 VQITVSEPKKHAEPAAgaagvIPGSGSYFSYLITTRAADGGLFRVRRRFRDV--------VALADRLAAAYRGLFVPARP 226
Cdd:cd06864      1 MEITVTEAEKRTGGSA-----MNLKETYTVYLIETKIVEHESEEGLSKKLSSlwrrysefELLRNYLVVTYPYVIVPPLP 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1443034972  227 DKsivegQVMQRH----------EFVNQRCAALQRYLGRLAAHPTIGRSAELHDFLTE 274
Cdd:cd06864     76 EK-----RAMFMWqklssdtfdpDFVERRRAGLENFLLRVAGHPELCQDKIFLEFLTH 128
PX_SNX1 cd07281
The phosphoinositide binding Phox Homology domain of Sorting Nexin 1; The PX domain is a ...
 219-272 2.82e-05

The phosphoinositide binding Phox Homology domain of Sorting Nexin 1; 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. SNX1 is both membrane associated and a cytosolic protein that exists as a tetramer in protein complexes. It can associate reversibly with membranes of the endosomal compartment, thereby coating these vesicles. SNX1 is a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures efficient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. SNX1 contains a Bin/Amphiphysin/Rvs (BAR) domain C-terminal to the PX domain. The PX domain of SNX1 specifically binds phosphatidylinositol-3-phosphate (PI3P) and PI(3,5)P2, while the BAR domain detects membrane curvature. Both domains help determine the specific membrane-targeting of SNX1, which is localized to a microdomain in early endosomes where it regulates cation-independent mannose-6-phosphate receptor retrieval to the trans Golgi network.


Pssm-ID: 132814  Cd Length: 124  Bit Score: 45.05  E-value: 2.82e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1443034972  219 GLFVPARPDKSI-------VEGQVMQRHEFVNQRCAALQRYLGRLAAHPTIGRSAELHDFL 272
Cdd:cd07281     61 GFIVPPPPEKSLigmtkvkVGKEDSSSAEFLERRRAALERYLQRIVSHPSLLQDPDVREFL 121
BAR_SNX4 cd07622
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 4; BAR domains are dimerization, lipid ...
 318-567 3.59e-04

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 4; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX4 is involved in recycling traffic from the sorting endosome (post-Golgi endosome) back to the late Golgi. It is also implicated in the regulation of plasma membrane receptor trafficking and interacts with receptors for EGF, insulin, platelet-derived growth factor and leptin. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153306  Cd Length: 201  Bit Score: 43.14  E-value: 3.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  318 FKDLK------QTVANGLVAVRPPPVEEEtdakFVMHKAKLEYfeqhlttasqqveallkayddlkattgqlGMTFIKLA 391
Cdd:cd07622     16 FEDLKnysdelQTNLNNLLKVRARLAERL----YGVYKIHANY-----------------------------GRVFSEWS 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  392 KFEKE-----QDTCNsqrkravDMSNFANAVINMSRSQtklnakiEIHLGTIYEYLetmtsvrnAFTDRANALLRVQSLs 466
Cdd:cd07622     63 AIEKEmgdglQKAGH-------YMDSYAASIDNGLEDE-------ELIADQLKEYL--------FFADSLRAVCKKHEL- 119

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  467 gdlflLHTQAAKLESVSSRGMGQerlryqkieelketirkTEDAKGNARQEYELIKENNMNEIIRFNKEKRHGLVEMLKG 546
Cdd:cd07622    120 -----LQYDLEKAEDALANKKQQ-----------------GEEAVKEAKDELNEFVKKALEDVERFKKQKVRDLKEILIS 177

                          250       260
                   ....*....|....*....|.
gi 1443034972  547 FVRNQVSYSEHISSIWTKVAE 567
Cdd:cd07622    178 YAKLQIKLAKKGLQTWTNIKE 198
PX_SNX30 cd07283
The phosphoinositide binding Phox Homology domain of Sorting Nexin 30; The PX domain is a ...
 157-273 1.33e-03

The phosphoinositide binding Phox Homology domain of Sorting Nexin 30; 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. SNX30 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to the sorting nexins SNX1-2, SNX4-8, and SNX32. Both domains have been shown to determine the specific membrane-targeting of SNX1. The specific function of SNX30 has yet to be elucidated.


Pssm-ID: 132816  Cd Length: 116  Bit Score: 40.07  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443034972  157 ITVSEPKKHaepaagaagvIPGSGSYFSYLITTRAADGGLFRVRRRFRDVVA----LADRLAAAYRGLFVPARPDKSIVE 232
Cdd:cd07283      3 VTVDDPKKH----------VCTMETYITYRVTTKTTRTEFDLPEYSVRRRYQdfdwLRNKLEESQPTHLIPPLPEKFVVK 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1443034972  233 GQVMQ-RHEFVNQRCAALQRYLGRLAAHPTIGRSAELHDFLT 273
Cdd:cd07283     73 GVVDRfSEEFVETRRKALDKFLKRIADHPVLSFNEHFNVFLT 114
PX_SNX8_Mvp1p_like cd06866
The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; The PX ...
 222-275 2.41e-03

The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; 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. SNX8 and the yeast counterpart Mvp1p are involved in sorting and delivery of late-Golgi proteins, such as carboxypeptidase Y, to vacuoles.


Pssm-ID: 132776  Cd Length: 105  Bit Score: 38.75  E-value: 2.41e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1443034972  222 VPARPDKSIveGQVMQRhEFVNQRCAALQRYLGRLAAHPTIGRSAELHDFLTEP 275
Cdd:cd06866     55 VPALPPKRI--GGSADR-EFLEARRRGLSRFLNLVARHPVLSEDELVRTFLTEP 105
 
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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