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Conserved domains on  [gi|767987833|ref|XP_011521040|]
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sorting nexin-29 isoform X2 [Homo sapiens]

Protein Classification

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List of domain hits

 Name Accession Description Interval E-value
RUN_SNX29 cd17689
RUN domain found in sorting nexin-29 (SNX29) and similar proteins; SNX29, also called RUN ...
 26-188 1.50e-96

RUN domain found in sorting nexin-29 (SNX29) and similar proteins; SNX29, also called RUN domain-containing protein 2A (RUNDC2A), belongs to the sorting nexin family. Sorting nexins are a large group of proteins that are localized in the cytoplasm and have the potential for membrane association either through their lipid-binding PX domain, a phospholipid-binding motif, or through protein-protein interactions with membrane-associated protein complexes. Some sorting nexin family members have been shown to facilitate protein sorting. This model contains the RUN domain of SNX29.


:

Pssm-ID: 439051  Cd Length: 166  Bit Score: 299.15  E-value: 1.50e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833  26 RLLDAVKQCQIRFGGRKEIASDSDSRVTCLCAQFEAVLQHGLKRSRGLALTAAAIKQA---AGFASKTETEPVFWYYVKE 102
Cdd:cd17689    1 RLLDAVKQCQIRFGGKTELATESDSRVSCLCAQLEAVLQHGLKTSRSPNLVSSAVTQVsglAGSLGSAETEPTFWPFVKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833 103 VLNKHELQRFYSLRHIASDVGRGRAWLRCALNEHSLERYLHMLLADRCRLSTFYEDWSFVMDEERSSMLPTMAAGLNSIL 182
Cdd:cd17689   81 HLTKHELERFELLKNIWTDIGRGRAWLRSALNEHSLERYLHILLSNENLLRQYYEDWAFLRDEERSSMLPNMAAGLGSIL 160


                 ....*.
gi 767987833 183 FAINID 188
Cdd:cd17689  161 FALSID 166
PX_RUN cd07277
The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX ...
 668-820 5.93e-72

The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX and RUN domains; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized proteins containing an N-terminal RUN domain and a C-terminal PX domain. PX domain harboring proteins 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. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction. The RUN domain is found in GTPases in the Rap and Rab families and may play a role in Ras-like signaling pathways.


:

Pssm-ID: 132810  Cd Length: 118  Bit Score: 231.85  E-value: 5.93e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833 668 INVWIPSVFLRGKAANAFHVYQVYIRIKDDEWNIYRRYTEFRSLHHKLQNKYPQVRAYNFPPKKAIGNKpppspawmtaa 747
Cdd:cd07277    1 INVWIPSVFLRGKGSDAHHVYQVYIRIRDDEWNVYRRYSEFYELHKKLKKKFPVVRSFDFPPKKAIGNK----------- 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767987833 748 asllasllpalpplnlqvtsevtssqDAKFVEERRKQLQNYLRSVMNKVIQMVPEFAASPKKETLIQLMPFFV 820
Cdd:cd07277   70 --------------------------DAKFVEERRKRLQVYLRRVVNTLIQTSPELTACPSKETLIKLLPFFG 116
ZIP_TSC22D-like super family cl40461
leucine zipper found in the TSC22 domain leucine zipper transcription factors, c-Myc-binding ...
 514-548 5.43e-04

leucine zipper found in the TSC22 domain leucine zipper transcription factors, c-Myc-binding protein, and similar proteins; The family includes TGF-beta-stimulated clone-22 domain (TSC22D) leucine zipper transcription factors, TSC22D1-4, as well as c-Myc-binding protein (MycBP). TSC22D proteins have diverse physiological functions, including cell growth, development, homeostasis, and immune regulation. MycBP, also called associate of Myc 1 (AMY-1), is a novel c-Myc binding protein that may control the transcriptional activity of Myc. It stimulates the activation of E box-dependent transcription by Myc. Members of this family contain a conserved leucine zipper (ZIP) domain. Its first helix is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. In the bZIP family of transcription factors, the leucine zipper acts as a dimerization domain and the upstream basic region as a DNA-binding domain. However, DNA-binding capability of TSC22D family proteins is not obvious, due to the lack of the basic region found in the original bZIP DNA-binding domains. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.


The actual alignment was detected with superfamily member cd21936:

Pssm-ID: 424092  Cd Length: 49  Bit Score: 38.32  E-value: 5.43e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 767987833 514 ALRQEVDTLKRKVAEQEERqgmkVQALARENEVLK 548
Cdd:cd21936   12 AVREEVDVLKEQIAELEER----ISQLERENSLLR 42
 
Name Accession Description Interval E-value
RUN_SNX29 cd17689
RUN domain found in sorting nexin-29 (SNX29) and similar proteins; SNX29, also called RUN ...
 26-188 1.50e-96

RUN domain found in sorting nexin-29 (SNX29) and similar proteins; SNX29, also called RUN domain-containing protein 2A (RUNDC2A), belongs to the sorting nexin family. Sorting nexins are a large group of proteins that are localized in the cytoplasm and have the potential for membrane association either through their lipid-binding PX domain, a phospholipid-binding motif, or through protein-protein interactions with membrane-associated protein complexes. Some sorting nexin family members have been shown to facilitate protein sorting. This model contains the RUN domain of SNX29.


Pssm-ID: 439051  Cd Length: 166  Bit Score: 299.15  E-value: 1.50e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833  26 RLLDAVKQCQIRFGGRKEIASDSDSRVTCLCAQFEAVLQHGLKRSRGLALTAAAIKQA---AGFASKTETEPVFWYYVKE 102
Cdd:cd17689    1 RLLDAVKQCQIRFGGKTELATESDSRVSCLCAQLEAVLQHGLKTSRSPNLVSSAVTQVsglAGSLGSAETEPTFWPFVKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833 103 VLNKHELQRFYSLRHIASDVGRGRAWLRCALNEHSLERYLHMLLADRCRLSTFYEDWSFVMDEERSSMLPTMAAGLNSIL 182
Cdd:cd17689   81 HLTKHELERFELLKNIWTDIGRGRAWLRSALNEHSLERYLHILLSNENLLRQYYEDWAFLRDEERSSMLPNMAAGLGSIL 160


                 ....*.
gi 767987833 183 FAINID 188
Cdd:cd17689  161 FALSID 166
PX_RUN cd07277
The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX ...
 668-820 5.93e-72

The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX and RUN domains; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized proteins containing an N-terminal RUN domain and a C-terminal PX domain. PX domain harboring proteins 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. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction. The RUN domain is found in GTPases in the Rap and Rab families and may play a role in Ras-like signaling pathways.


Pssm-ID: 132810  Cd Length: 118  Bit Score: 231.85  E-value: 5.93e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833 668 INVWIPSVFLRGKAANAFHVYQVYIRIKDDEWNIYRRYTEFRSLHHKLQNKYPQVRAYNFPPKKAIGNKpppspawmtaa 747
Cdd:cd07277    1 INVWIPSVFLRGKGSDAHHVYQVYIRIRDDEWNVYRRYSEFYELHKKLKKKFPVVRSFDFPPKKAIGNK----------- 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767987833 748 asllasllpalpplnlqvtsevtssqDAKFVEERRKQLQNYLRSVMNKVIQMVPEFAASPKKETLIQLMPFFV 820
Cdd:cd07277   70 --------------------------DAKFVEERRKRLQVYLRRVVNTLIQTSPELTACPSKETLIKLLPFFG 116
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
 54-189 1.79e-33

RUN domain; This domain is present in several proteins that are linked to the functions of GTPases in the Rap and Rab families. They could hence play important roles in multiple Ras-like GTPase signalling pathways. The domain is comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases.


Pssm-ID: 460679  Cd Length: 134  Bit Score: 125.47  E-value: 1.79e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833   54 CLCAQFEAVLQHGLKRSRGLALTAAAIKQaagfasktetEPVFWYYVKEV-----LNKHELQRFYSLRHIAS---DVGRG 125
Cdd:pfam02759   1 QLCAALEALLSHGLKRSSLLILRAAGLLP----------ERSFWALLERVgklvpPAEELLSSVQELEQIHTpysPDGRG 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767987833  126 RAWLRCALNEHSLERYLHMLLADRCRLSTFYEDWSFVMDEERSSMLPTMAAGLNSILFAINIDN 189
Cdd:pfam02759  71 RAWIRLALNEKLLDQWLKLLLSNKELLSEYYEPWALLADPEFGEILLGLLVGLSALDFNLCLKL 134
RUN smart00593
domain involved in Ras-like GTPase signaling;
125-188 5.41e-21

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 87.28  E-value: 5.41e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767987833   125 GRAWLRCALNEHSLERYLHMLLADRCRLSTFYEDWSFVMDEERSSMLPTMAAGLNSILFAINID 188
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRDPEEGEQLLGLLVGLSALDFNLPVD 64
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 698-807 1.46e-12

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 63.80  E-value: 1.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833  698 EWNIYRRYTEFRSLHHKLQNKYPQVRAYNFPPKKAIGNKpppspawmtaaasllasllpalpplnlqvtsevtssqDAKF 777
Cdd:pfam00787   8 EWSVRRRYSDFVELHKKLLRKFPSVIIPPLPPKRWLGRY-------------------------------------NEEF 50

                          90       100       110
                  ....*....|....*....|....*....|
gi 767987833  778 VEERRKQLQNYLRSVMNkviqmVPEFAASP 807
Cdd:pfam00787  51 IEKRRKGLEQYLQRLLQ-----HPELRNSE 75
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
 683-794 4.14e-12

PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function present in phox proteins, PLD isoforms, a PI3K isoform.


Pssm-ID: 214610  Cd Length: 105  Bit Score: 63.13  E-value: 4.14e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833   683 NAFHVYQVYIRIKDDEWNIYRRYTEFRSLHHKLQNKYPQVRAYNFPPKKAIGNKPppspawmtaaasllasllpalppln 762
Cdd:smart00312  12 HYYYVIEIETKTGLEEWTVSRRYSDFLELHSKLKKHFPRSILPPLPGKKLFGRLN------------------------- 66

                           90       100       110
                   ....*....|....*....|....*....|..
gi 767987833   763 lqvtsevtsSQDAKFVEERRKQLQNYLRSVMN 794
Cdd:smart00312  67 ---------NFSEEFIEKRRRGLEKYLQSLLN 89
ZIP_TSC22D cd21936
leucine zipper domain found in the TSC22 domain family of leucine zipper transcription factors; ...
 514-548 5.43e-04

leucine zipper domain found in the TSC22 domain family of leucine zipper transcription factors; The TGF-beta-stimulated clone-22 domain (TSC22D) family includes TSC22D1-4 and similar proteins. They have diverse physiological functions, including cell growth, development, homeostasis, and immune regulation. All family members contain a conserved leucine zipper (ZIP) domain located at the C-terminus. Its first helix is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. In the bZIP family of transcription factors, the leucine zipper acts as a dimerization domain and the upstream basic region as a DNA-binding domain. However, DNA-binding capability of TSC22D family proteins is not obvious, due to the lack of the basic region found in the original bZIP DNA-binding domains. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.


Pssm-ID: 409276  Cd Length: 49  Bit Score: 38.32  E-value: 5.43e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 767987833 514 ALRQEVDTLKRKVAEQEERqgmkVQALARENEVLK 548
Cdd:cd21936   12 AVREEVDVLKEQIAELEER----ISQLERENSLLR 42
 
Name Accession Description Interval E-value
RUN_SNX29 cd17689
RUN domain found in sorting nexin-29 (SNX29) and similar proteins; SNX29, also called RUN ...
 26-188 1.50e-96

RUN domain found in sorting nexin-29 (SNX29) and similar proteins; SNX29, also called RUN domain-containing protein 2A (RUNDC2A), belongs to the sorting nexin family. Sorting nexins are a large group of proteins that are localized in the cytoplasm and have the potential for membrane association either through their lipid-binding PX domain, a phospholipid-binding motif, or through protein-protein interactions with membrane-associated protein complexes. Some sorting nexin family members have been shown to facilitate protein sorting. This model contains the RUN domain of SNX29.


Pssm-ID: 439051  Cd Length: 166  Bit Score: 299.15  E-value: 1.50e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833  26 RLLDAVKQCQIRFGGRKEIASDSDSRVTCLCAQFEAVLQHGLKRSRGLALTAAAIKQA---AGFASKTETEPVFWYYVKE 102
Cdd:cd17689    1 RLLDAVKQCQIRFGGKTELATESDSRVSCLCAQLEAVLQHGLKTSRSPNLVSSAVTQVsglAGSLGSAETEPTFWPFVKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833 103 VLNKHELQRFYSLRHIASDVGRGRAWLRCALNEHSLERYLHMLLADRCRLSTFYEDWSFVMDEERSSMLPTMAAGLNSIL 182
Cdd:cd17689   81 HLTKHELERFELLKNIWTDIGRGRAWLRSALNEHSLERYLHILLSNENLLRQYYEDWAFLRDEERSSMLPNMAAGLGSIL 160


                 ....*.
gi 767987833 183 FAINID 188
Cdd:cd17689  161 FALSID 166
PX_RUN cd07277
The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX ...
 668-820 5.93e-72

The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX and RUN domains; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized proteins containing an N-terminal RUN domain and a C-terminal PX domain. PX domain harboring proteins 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. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction. The RUN domain is found in GTPases in the Rap and Rab families and may play a role in Ras-like signaling pathways.


Pssm-ID: 132810  Cd Length: 118  Bit Score: 231.85  E-value: 5.93e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833 668 INVWIPSVFLRGKAANAFHVYQVYIRIKDDEWNIYRRYTEFRSLHHKLQNKYPQVRAYNFPPKKAIGNKpppspawmtaa 747
Cdd:cd07277    1 INVWIPSVFLRGKGSDAHHVYQVYIRIRDDEWNVYRRYSEFYELHKKLKKKFPVVRSFDFPPKKAIGNK----------- 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767987833 748 asllasllpalpplnlqvtsevtssqDAKFVEERRKQLQNYLRSVMNKVIQMVPEFAASPKKETLIQLMPFFV 820
Cdd:cd07277   70 --------------------------DAKFVEERRKRLQVYLRRVVNTLIQTSPELTACPSKETLIKLLPFFG 116
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
 54-189 1.79e-33

RUN domain; This domain is present in several proteins that are linked to the functions of GTPases in the Rap and Rab families. They could hence play important roles in multiple Ras-like GTPase signalling pathways. The domain is comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases.


Pssm-ID: 460679  Cd Length: 134  Bit Score: 125.47  E-value: 1.79e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833   54 CLCAQFEAVLQHGLKRSRGLALTAAAIKQaagfasktetEPVFWYYVKEV-----LNKHELQRFYSLRHIAS---DVGRG 125
Cdd:pfam02759   1 QLCAALEALLSHGLKRSSLLILRAAGLLP----------ERSFWALLERVgklvpPAEELLSSVQELEQIHTpysPDGRG 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767987833  126 RAWLRCALNEHSLERYLHMLLADRCRLSTFYEDWSFVMDEERSSMLPTMAAGLNSILFAINIDN 189
Cdd:pfam02759  71 RAWIRLALNEKLLDQWLKLLLSNKELLSEYYEPWALLADPEFGEILLGLLVGLSALDFNLCLKL 134
RUN cd17671
RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new ...
 30-185 2.41e-32

RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new molecule containing SH3 at the carboxyl-terminus), is a less conserved protein motif that comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases. RUN domains are often found in proteins linked particularly to the functions of GTPases in the Rap and Rab families, suggesting the RUN domain may be involved in Rab-mediated membrane trafficking, possibly as a Rab-binding site. RUN domain-containing proteins could hence play important roles in multiple Ras-like GTPase signalling pathways.


Pssm-ID: 439038  Cd Length: 154  Bit Score: 122.92  E-value: 2.41e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833  30 AVKQCQIRFGGRKEIAS-------DSDSRVTCLCAQFEAVLQHGLKRSRGLaltaaaikqaagfasktETEPVFWYYVKE 102
Cdd:cd17671    2 AVKELLESFADNGEADDsaaltltDDDPVVGRLCAALEAILSHGLKPKRFG-----------------GGKVSFWDFLEA 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833 103 VLN-------KHELQRFYSLRHIASDVGRGRAWLRCALNEHSLERYLHMLLADRCRLSTFYEDWSFVMDEERSSMLPTMA 175
Cdd:cd17671   65 LEKllpapslKQAIRDINSLSNVKTDDGRGRAWIRLALNEKSLESYLAALLSDQSLLRKYYEPWALLRDPEEAELFLSLL 144

                        170
                 ....*....|
gi 767987833 176 AGLNSILFAI 185
Cdd:cd17671  145 VGLSSLDFNL 154
RUN_PLEKHM1 cd17679
RUN domain found in pleckstrin homology domain-containing family M member 1 (PLEKHM1) and ...
 23-193 2.37e-28

RUN domain found in pleckstrin homology domain-containing family M member 1 (PLEKHM1) and similar proteins; PLEKHM1, also called PH domain-containing family M member 1, or 162 kDa adapter protein (AP162), may act as a multivalent adapter protein that regulates Rab7-dependent and HOPS complex-dependent fusion events in the endolysosomal system and couples autophagic and the endocytic trafficking pathways. This model represents the RUN domain of PLEKHM1.


Pssm-ID: 439041 [Multi-domain]  Cd Length: 171  Bit Score: 111.91  E-value: 2.37e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833  23 LLERLLDAVKQCQIRFGGRKEIASDSDSRVTCLCAQFEAVLQHGLKRSRglaltaaAIKQAAGFASKTE--TEPVFWYYV 100
Cdd:cd17679    4 LTKELSSSVKELQLEYVSSDEVVTSSDDGANTLCCVLEAIFLHGLKDKF-------ISKVSSVFSGDVDklPEPNFWPLL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833 101 KEVLNKHELQRFYSLRHIASDVGRGRAWLRCALNEHSLERYLHMLLADRCRLSTFYEDWSFVMDEERSSMLPTMAAGLNS 180
Cdd:cd17679   77 LKFSHRDVIDQIEHLSQITTDVGRCRAWIRLALNDGLLESYLEAILKDKSALKSYYNPSAFLRDPEQLDILKSLLQGLES 156

                        170
                 ....*....|...
gi 767987833 181 ILFAINIDNKDLN 193
Cdd:cd17679  157 FQFELPYNSSLLN 169
RUN_PLEKHM2 cd17680
RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and ...
 22-184 2.18e-24

RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and similar proteins; PLEKHM2, also called PH domain-containing family M member 2, or Salmonella-induced filaments A (SifA) and Kinesin-Interacting Protein (SKIP), is the lysosome, melanosome and lytic granule cargo adaptor that controls lysosome positioning using a composite kinesin-1 heavy and light chain-binding domain. In addition to kinesin-1, it also interacts with several Rabs to affect endosomal trafficking. This model represents the RUN domain of PLEKHM2.


Pssm-ID: 439042  Cd Length: 145  Bit Score: 99.62  E-value: 2.18e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833  22 FLLERLLDAVKQCQIRFGGRKEIASDSDSR---VTCLCAQFEAVLQHGLKRSRGLaltaaaikqaagfasktetepvFWY 98
Cdd:cd17680    1 RILRNISEAIKSLQSYSSSQEEEDVLITNEnreLQRLCEALDHALLHGLRRGNRG----------------------YWP 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833  99 YVKEVLNKHELQRFYSLRHIASDVGRGRAWLRCALNEHSLERYLHMLLADRCRLSTFYEDWSFVMDEERSSMLPTMAAGL 178
Cdd:cd17680   59 FVKEFTHKETIKQIENLPNVTTDLGRGRAWLYLALNEGSLESYLRSFLENRKLVKKFYHKHALLRDSQRLELLLTLLSGL 138


                 ....*.
gi 767987833 179 NSILFA 184
Cdd:cd17680  139 EFVQFD 144
PX_KIF16B_SNX23 cd06874
The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The ...
 668-819 3.35e-23

The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; 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. KIF16B, also called sorting nexin 23 (SNX23), is a family-3 kinesin which harbors an N-terminal kinesin motor domain containing ATP and microtubule binding sites, a ForkHead Associated (FHA) domain, and a C-terminal PX domain. The PX domain of KIF16B binds to phosphatidylinositol-3-phosphate (PI3P) in early endosomes and plays a role in the transport of early endosomes to the plus end of microtubules. By regulating early endosome plus end motility, KIF16B modulates the balance between recycling and degradation of receptors. 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: 132784  Cd Length: 127  Bit Score: 95.91  E-value: 3.35e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833 668 INVWIPSVFLRGKAANAFHVYQVYIRIKDDEWNIYRRYTEFRSLHHKLQNKYPQVRAYNFPPKKAIGNKpppspawmtaa 747
Cdd:cd06874    1 IKITIPRYVLRGQGKDEHFEFEVKITVLDETWTVFRRYSRFRELHKTMKLKYPEVAALEFPPKKLFGNK----------- 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767987833 748 asllasllpalpplnlqvtsevtssqDAKFVEERRKQLQNYLRSVMNKVIQ-----MVPEFAASPKKETLIQLMPFF 819
Cdd:cd06874   70 --------------------------SERVAKERRRQLETYLRNFFSVCLKlpacpLYPKVGRTLSKATLCDFSPFF 120
RUN smart00593
domain involved in Ras-like GTPase signaling;
125-188 5.41e-21

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 87.28  E-value: 5.41e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767987833   125 GRAWLRCALNEHSLERYLHMLLADRCRLSTFYEDWSFVMDEERSSMLPTMAAGLNSILFAINID 188
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRDPEEGEQLLGLLVGLSALDFNLPVD 64
PX_domain cd06093
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
 669-794 4.19e-19

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: 83.18  E-value: 4.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833 669 NVWIPSVFLRGKAANAFHVYQVYIRIKD-DEWNIYRRYTEFRSLHHKLQNKYPQVRAYNFPPKKAIGNKpppspawmtaa 747
Cdd:cd06093    1 SVSIPDYEKVKDGGKKYVVYIIEVTTQGgEEWTVYRRYSDFEELHEKLKKKFPGVILPPLPPKKLFGNL----------- 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 767987833 748 asllasllpalpplnlqvtsevtssqDAKFVEERRKQLQNYLRSVMN 794
Cdd:cd06093   70 --------------------------DPEFIEERRKQLEQYLQSLLN 90
RUN_RUNDC3 cd17684
RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 ...
 43-183 9.54e-13

RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 contains two isoforms, RUNDC3A and RUNDC3B. RUNDC3A, also called Rap2-interacting protein 8 (RPIP8), may act as an effector of Rap2A GTPase in neuronal cells. RUNDC3B, also called Rap2-binding protein 9, or Rap2-interacting protein 9 (RPIP-9), contains a RUN domain in its N-terminal region that mediates interaction with Rap2, an important component of the Mitogen-Activated Protein Kinase (MAPK) cascade, which regulates cellular proliferation and differentiation. It also contains characteristic binding sites for MAPK intermediates. Both RUNDC3A and RUNDC3B contain a RUN domain.


Pssm-ID: 439046  Cd Length: 150  Bit Score: 66.65  E-value: 9.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833  43 EIASDSDSRVTCLCAQFEAVLQHGLKrsrglaltaaAIKQAAGfaskTETEPVFWYYVKEVLNK---HELQRFYSLRHIA 119
Cdd:cd17684   20 ETIDDSSEELINFAAILEQILSHRLK----------PVKPWYG----SEEPRTFWDYIRVACKKvpqNCIASIEQMENIK 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767987833 120 SDVGRGRAWLRCALNEHSLERYLHMLLADRCRLSTFYEDWSFVMDEErSSMLPTMAAGLNSILF 183
Cdd:cd17684   86 SPKAKGRAWIRVALMEKRLSEYLSTALKQTRLTRNFYQDGAIMLSED-ATVLCGMLIGLNAIDF 148
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 698-807 1.46e-12

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 63.80  E-value: 1.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833  698 EWNIYRRYTEFRSLHHKLQNKYPQVRAYNFPPKKAIGNKpppspawmtaaasllasllpalpplnlqvtsevtssqDAKF 777
Cdd:pfam00787   8 EWSVRRRYSDFVELHKKLLRKFPSVIIPPLPPKRWLGRY-------------------------------------NEEF 50

                          90       100       110
                  ....*....|....*....|....*....|
gi 767987833  778 VEERRKQLQNYLRSVMNkviqmVPEFAASP 807
Cdd:pfam00787  51 IEKRRKGLEQYLQRLLQ-----HPELRNSE 75
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
 683-794 4.14e-12

PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function present in phox proteins, PLD isoforms, a PI3K isoform.


Pssm-ID: 214610  Cd Length: 105  Bit Score: 63.13  E-value: 4.14e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833   683 NAFHVYQVYIRIKDDEWNIYRRYTEFRSLHHKLQNKYPQVRAYNFPPKKAIGNKPppspawmtaaasllasllpalppln 762
Cdd:smart00312  12 HYYYVIEIETKTGLEEWTVSRRYSDFLELHSKLKKHFPRSILPPLPGKKLFGRLN------------------------- 66

                           90       100       110
                   ....*....|....*....|....*....|..
gi 767987833   763 lqvtsevtsSQDAKFVEERRKQLQNYLRSVMN 794
Cdd:smart00312  67 ---------NFSEEFIEKRRRGLEKYLQSLLN 89
PX_IRAS cd06875
The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor ...
 685-802 5.28e-11

The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor Antisera-Selected; The PX domain is a phosphoinositide binding (PI) module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Imidazoline Receptor Antisera-Selected (IRAS), also called nischarin, contains an N-terminal PX domain, leucine rich repeats, and a predicted coiled coil domain. The PX domain of IRAS binds to phosphatidylinositol-3-phosphate in membranes. Together with the coiled coil domain, it is essential for the localization of IRAS to endosomes. IRAS has been shown to interact with integrin and inhibit cell migration. Its interaction with alpha5 integrin causes a redistribution of the receptor from the cell surface to endosomal structures, suggesting that IRAS may function as a sorting nexin (SNX) which regulates the endosomal trafficking of integrin. 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. 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: 132785  Cd Length: 116  Bit Score: 60.37  E-value: 5.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833 685 FHVYQVYIRIKDDEWNIYRRYTEFRSLHHKLQNKYpQVRAYNFPPKKAIGNKpppSPAwmtaaasllasllpalpplnlq 764
Cdd:cd06875   17 YTVYIIEVKVGSVEWTVKHRYSDFAELHDKLVAEH-KVDKDLLPPKKLIGNK---SPS---------------------- 70

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767987833 765 vtsevtssqdakFVEERRKQLQNYLRSVMNKVIQMVPE 802
Cdd:cd06875   71 ------------FVEKRRKELEIYLQTLLSFFQKTMPR 96
RUN_RUFY1_like cd17681
RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar ...
 55-166 2.29e-10

RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar proteins; This family includes RUN and FYVE domain-containing protein RUFY1, RUFY2, and RUFY3. RUFY1, also called FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homolog of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY2, also called Rab4-interacting protein related, is a novel embryonic factor that is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. RUFY3, also called Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. RUFY1, RUFY2, and RUFY3 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between; this model represents the RUN domain.


Pssm-ID: 439043  Cd Length: 155  Bit Score: 59.89  E-value: 2.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833  55 LCAQFEAVLQHGLKRSRglaltaaaikqaagfaSKTETEPVFWYyVKEVLNKH--ELQRFYS----LRHIASDVGRGRAW 128
Cdd:cd17681   37 FFVILEHVLRHGLKVKK----------------SFLGPNKSFWP-VLEHVEKLvpEANEITAsvrdLPGIKTPLGRARAW 99

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767987833 129 LRCALNEHSLERYLHMLLADRCRLSTFYEDWSFVMDEE 166
Cdd:cd17681  100 LRLALMQKKLADYFRALIENKDLLSEFYEPGALMMSEE 137
RUN_RUNDC3B cd17700
RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN ...
 43-184 4.42e-10

RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN domain-containing protein 3B (RUNDC3B), also called Rap2-binding protein 9, or Rap2-interacting protein 9 (RPIP-9), contains a RUN domain in its N-terminal region that mediates interaction with Rap2, an important component of the Mitogen-Activated Protein Kinase (MAPK) cascade, which regulates cellular proliferation and differentiation. It also contains characteristic binding sites for MAPK intermediates. RUNDC3B contains a RUN domain.


Pssm-ID: 439062  Cd Length: 151  Bit Score: 58.83  E-value: 4.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833  43 EIASDSDSRVTCLCAQFEAVLQHGLKrsrglaltaaaiKQAAGFAskTETEPVFWYYVKEVLNK--HE-LQRFYSLRHIA 119
Cdd:cd17700   20 ETIDDSSPEFVNFAAILEQILSHRLK------------GQVTWFG--YESPRSFWDYIRVACSKvpHNcICSIENMENVS 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767987833 120 SDVGRGRAWLRCALNEHSLERYLHMLLADRCRLSTFYEDWSFVMDEErSSMLPTMAAGLNSILFA 184
Cdd:cd17700   86 SSRAKGRAWIRVALMEKRLSEYISTALRDFKTTRRFYEDGAIVLGEE-ANMLAGMLLGLNAIDFS 149
PX_SNX13 cd06873
The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; The PX domain is a ...
 684-813 1.79e-09

The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; 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. SNX13, also called RGS-PX1, contains an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs. It specifically binds to the stimulatory subunit of the heterotrimeric G protein G(alpha)s, serving as its GTPase activating protein, through the RGS domain. It preferentially binds phosphatidylinositol-3-phosphate (PI3P) through the PX domain and is localized in early endosomes. SNX13 is involved in endosomal sorting of EGFR into multivesicular bodies (MVB) for delivery to the lysosome.


Pssm-ID: 132783  Cd Length: 120  Bit Score: 56.12  E-value: 1.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833 684 AFHVYQVYIRIKDDEWNIYRRYTEFRSLHHKLQNKYPQVRAYNFPPKKAIGNkpppspawmtaaasllasllpalpplnl 763
Cdd:cd06873   26 AISVTRIYPNGQEESWHVYRRYSDFHDLHMRLKEKFPNLSKLSFPGKKTFNN---------------------------- 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767987833 764 qvtsevtssQDAKFVEERRKQLQNYLRSVMNKViqmvpEFAASPKKETLI 813
Cdd:cd06873   78 ---------LDRAFLEKRRKMLNQYLQSLLNPE-----VLDANPGLQEIV 113
PX_MDM1p cd06876
The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a ...
 683-792 2.01e-08

The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a phosphoinositide binding (PI) module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Yeast MDM1p is a filament-like protein localized in punctate structures distributed throughout the cytoplasm. It plays an important role in nuclear and mitochondrial transmission to daughter buds. Members of this subfamily show similar domain architectures as some sorting nexins (SNXs). Some members are similar to SNX19 in that they contain an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some SNXs. Others are similar to SNX13 and SNX14, which also harbor these three domains as well as a regulator of G protein signaling (RGS) domain in between the PXA and PX domains. 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: 132786  Cd Length: 133  Bit Score: 53.47  E-value: 2.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833 683 NAFHVYQVYI-RIKDDE----WNIYRRYTEFRSLHHKLQNKYPQVRAYNFPPKKAIGNKpppspawmtaaasllasllpa 757
Cdd:cd06876   36 KEFVVYLIEVqRLNNDDqssgWVVARRYSEFLELHKYLKKRYPGVLKLDFPQKRKISLK--------------------- 94

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767987833 758 lpplnlqvtsevtsSQDAKFVEERRKQLQNYLRSV 792
Cdd:cd06876   95 --------------YSKTLLVEERRKALEKYLQEL 115
RUN_RUNDC3A cd17699
RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN ...
 47-184 6.64e-08

RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN domain-containing protein 3A (RUNDC3A), also called Rap2-interacting protein 8 (RPIP8), may act as an effector of Rap2A GTPase in neuronal cells. It contains a RUN domain.


Pssm-ID: 439061  Cd Length: 151  Bit Score: 52.72  E-value: 6.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833  47 DSDSRVTCLCAQFEAVLQHGLKrsrglaltaaaikqAAGFASKTETEPVFWYYVKEVLNK---HELQRFYSLRHIASDVG 123
Cdd:cd17699   24 DSSEEFVNFAAILEQILSHRFK--------------GPVSWFSSDGQRGFWDYIRLACSKvpnNCISSIENMENISTSRA 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767987833 124 RGRAWLRCALNEHSLERYLHMLLADRCRLSTFYEDWSFVMDEErSSMLPTMAAGLNSILFA 184
Cdd:cd17699   90 KGRAWIRVALMEKRLSEYIATALRDTRTTRRFYDDGAIMLREE-STVLTGMLIGLSAIDFS 149
RUN_RUFY1 cd17694
RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
 58-181 9.48e-08

RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; RUFY1, also called FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homolog of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY1 contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between; this model represents the RUN domain.


Pssm-ID: 439056  Cd Length: 156  Bit Score: 52.21  E-value: 9.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833  58 QFEAVLQHGLKRsrGLALTAAAIKQAAGFASKTEtepvfwyyVKEVLNKHELQRFYSLRH---IASDVGRGRAWLRCALN 134
Cdd:cd17694   36 QFFVVLEHCLKH--GLKVKKSFIGQNKSFFGPLE--------LVEKLCPEASDIATSARNlpeLKTAVGRGRAWLHLALM 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 767987833 135 EHSLERYLHMLLADRCRLSTFYEDWSFVMDEERSSMLpTMAAGLNSI 181
Cdd:cd17694  106 QKKLADYLKVLIDRKDLLSEFYEPGALMMEEEGAVIV-GLLVGLNVI 151
RUN_RUFY2 cd17695
RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
 122-181 1.04e-07

RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; RUFY2, also called Rab4-interacting protein related, is a novel embryonic factor that contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between. It is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. This model represents the RUN domain of RUFY2.


Pssm-ID: 439057  Cd Length: 156  Bit Score: 52.29  E-value: 1.04e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833 122 VGRGRAWLRCALNEHSLERYLHMLLADRCRLSTFYEDWSFVMDEErSSMLPTMAAGLNSI 181
Cdd:cd17695   93 LGRARAWLRLALMQKKLADYLRCLIIRRDLLSEFYEYHALMMEEE-GAVIVGLLVGLNVI 151
PX_YPT35 cd07280
The phosphoinositide binding Phox Homology domain of the fungal protein YPT35; The PX domain ...
 671-798 1.26e-07

The phosphoinositide binding Phox Homology domain of the fungal protein YPT35; 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. This subfamily is composed of YPT35 proteins from the fungal subkingdom Dikarya. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction. The PX domain of YPT35 binds to phosphatidylinositol 3-phosphate (PI3P). It also serves as a protein interaction domain, binding to members of the Yip1p protein family, which localize to the ER and Golgi. YPT35 is mainly associated with endosomes and together with Yip1p proteins, may be involved in a specific function in the endocytic pathway.


Pssm-ID: 132813  Cd Length: 120  Bit Score: 51.17  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833 671 WIPSVFLRG-------KAANAFHVYQVYIRIKDDEW---NIYRRYTEFRSLHHKLQNKYPQVRAYNFPPkkaignkPPPS 740
Cdd:cd07280    1 HATDVNVGDytivggdTGGGAYVVWKITIETKDLIGssiVAYKRYSEFVQLREALLDEFPRHKRNEIPQ-------LPPK 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767987833 741 PAWmtaaasllasllpalpplnlqvtSEVTSSQDAKFVEERRKQLQNYLRSVM-NKVIQ 798
Cdd:cd07280   74 VPW-----------------------YDSRVNLNKAWLEKRRRGLQYFLNCVLlNPVFG 109
PX_SNARE cd06897
The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain ...
 672-794 2.12e-07

The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; 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. This subfamily is composed of fungal proteins similar to Saccharomyces cerevisiae Vam7p. They contain an N-terminal PX domain and a C-terminal SNARE domain. The SNARE (Soluble NSF attachment protein receptor) family of proteins are integral membrane proteins that serve as key factors for vesicular trafficking. Vam7p is anchored at the vacuolar membrane through the specific interaction of its PX domain with phosphatidylinositol-3-phosphate (PI3P) present in bilayers. It plays an essential role in vacuole fusion. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction.


Pssm-ID: 132807  Cd Length: 108  Bit Score: 49.96  E-value: 2.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833 672 IPSVFLRGKAanaFHVYQVYIRIKDDEWNIYRRYTEFRSLHHKLQNKYPQVRAYNFPPKKaignkpppspaWMTAaasll 751
Cdd:cd06897    5 IPTTSVSPKP---YTVYNIQVRLPLRSYTVSRRYSEFVALHKQLESEVGIEPPYPLPPKS-----------WFLS----- 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767987833 752 asllpalpplnlqvtsevtSSQDAKFVEERRKQLQNYLRSVMN 794
Cdd:cd06897   66 -------------------TSSNPKLVEERRVGLEAFLRALLN 89
RUN_RUBCN cd17686
RUN domain found in Run domain Beclin-1-interacting and cysteine-rich domain-containing ...
 55-171 3.41e-07

RUN domain found in Run domain Beclin-1-interacting and cysteine-rich domain-containing protein (RUBCN) and similar proteins; RUBCN, also called rubicon, or beclin-1 associated RUN domain containing protein (Baron), is part of a Beclin-1-Vps34-containing autophagy complex. It negatively regulates endosome maturation and degradative endocytic trafficking and impairs autophagosome maturation process. It is also an important negative regulator of the innate immune response, enhances viral replication and may play a role in viral immune evasion. This model contains the RUN domain of RUBCN.


Pssm-ID: 439048  Cd Length: 151  Bit Score: 50.73  E-value: 3.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833  55 LCAQFEAVLQHGLKRSRGLaltaaaikqaagfasktETEPVFWYYVKEV--------LNKHELQRFYSLRHIASDVGRgr 126
Cdd:cd17686   24 LCRAVENILQHGLKEFQGL-----------------NKEIDDWEFVQGLrwlqptlaPSIEQQSRSSPSESEVSDKGR-- 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767987833 127 AWLRCALNEHSLERYLHMLLADRCRLSTFYEDWSFVMDEERSSML 171
Cdd:cd17686   85 LWLRQSLQQHCLSSQLQWLVSDKELLRKYYEDEAFLRQEGYATAL 129
PX_SNX2 cd07282
The phosphoinositide binding Phox Homology domain of Sorting Nexin 2; The PX domain is a ...
 679-802 8.58e-07

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: 48.90  E-value: 8.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833 679 GKAANAFHVYQVYIR-----IKDDEWNIYRRYTEFRSLHHKLQNKYPQVrAYNFPPkkaignKPPPSPAWMTaaasllas 753
Cdd:cd07282   12 GDGMNAYMAYRVTTKtslsmFSRSEFSVRRRFSDFLGLHSKLASKYLHV-GYIVPP------APEKSIVGMT-------- 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767987833 754 llpalpplNLQVTSEVTSSQDakFVEERRKQLQNYL-RSVMNKVIQMVPE 802
Cdd:cd07282   77 --------KVKVGKEDSSSTE--FVEKRRAALERYLqRTVKHPTLLQDPD 116
PX_SNX1 cd07281
The phosphoinositide binding Phox Homology domain of Sorting Nexin 1; The PX domain is a ...
 679-794 1.70e-06

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: 47.75  E-value: 1.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833 679 GKAANAFHVYQVYIR-----IKDDEWNIYRRYTEFRSLHHKLQNKYPQvRAYNFPPkkaignkpPPSPAWMtaaasllas 753
Cdd:cd07281   12 GDGMNAYVVYKVTTQtsllmFRSKHFTVKRRFSDFLGLYEKLSEKHSQ-NGFIVPP--------PPEKSLI--------- 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767987833 754 llpalPPLNLQVTSEVTSSqdAKFVEERRKQLQNYLRSVMN 794
Cdd:cd07281   74 -----GMTKVKVGKEDSSS--AEFLERRRAALERYLQRIVS 107
RUN_RUFY4_like cd17682
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil ...
 55-185 2.31e-06

RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil domain-containing protein 1 (FYCO1), and similar proteins; The family includes RUFY4 and FYCO1. RUFY4 acts as a positive regulator that enhances autophagy and lysosome tethering in response to Interleukin-4. It is expressed in a cell-specific manner or under specific immunological conditions associated with IL4 expression such as allergic asthma. FYCO1, also called zinc finger FYVE domain-containing protein 7 (ZFYVE7), is a multidomain autophagy adaptor protein that interacts with kinesin motor proteins and with the autophagosomal membrane components microtubule-associated protein 1 light chain 3 (LC3), Rab7, and phosphatidylinositol 3-phosphate (PI3P), to mediate microtubule plus-end-directed autophagosome transport. Both RUFY4 and FYCO1 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between; this model represents the RUN domain.


Pssm-ID: 439044  Cd Length: 150  Bit Score: 47.99  E-value: 2.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833  55 LCAQFEAVLQHGLKRSRGLALTaaaikqaagfasktetEPVFWYYVKEVLNKHELqRFYSLRHIASDV----------GR 124
Cdd:cd17682   27 FCETLEKILRKGLKEKVSLGGR----------------RKDYWDWLEELLKKLNK-IPKSLSDAVKFVksckkvktnqGR 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767987833 125 GRAWLRCALNEHSLERYLHMLLADRCRLSTFYEDWSFVMDEERSSMLPTMAAGLNSILFAI 185
Cdd:cd17682   90 GRLFIRYALNKKCLHDPVQQLVKNPKLLSDYYSPDSILGNEILSEILLSLLYQLNEINFDL 150
RUN_RUFY3 cd17696
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ...
 118-181 2.40e-06

RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also called Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. This model represents the RUN domain of RUFY3.


Pssm-ID: 439058  Cd Length: 156  Bit Score: 48.45  E-value: 2.40e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767987833 118 IASDVGRGRAWLRCALNEHSLERYLHMLLADRCRLSTFYEDWSFVMDEErSSMLPTMAAGLNSI 181
Cdd:cd17696   89 LKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEE-GAIIAGLLVGLNVI 151
PX_SNX4 cd06864
The phosphoinositide binding Phox Homology domain of Sorting Nexin 4; The PX domain is a ...
 685-792 6.67e-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: 46.21  E-value: 6.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833 685 FHVYQVYIRIKDDEWNI---------YRRYTEFRSLHHKLQNKYPQVRAYNFPPKKAignkpppSPAWmtaaasllasll 755
Cdd:cd06864   23 YTVYLIETKIVEHESEEglskklsslWRRYSEFELLRNYLVVTYPYVIVPPLPEKRA-------MFMW------------ 83

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767987833 756 palpplnlqvtSEVTSSQ-DAKFVEERRKQLQNYLRSV 792
Cdd:cd06864   84 -----------QKLSSDTfDPDFVERRRAGLENFLLRV 110
PX_SNX20_21_like cd07279
The phosphoinositide binding Phox Homology domain of Sorting Nexins 20 and 21; The PX domain ...
 685-735 8.23e-06

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: 45.40  E-value: 8.23e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767987833 685 FHVYQVYIRIKDDEWN----IYRRYTEFRSLHHKLQNKYPQ-VRAYNFPPKKAIGN 735
Cdd:cd07279   18 YVVYQLAVVQTGDPDTqpafIERRYSDFLKLYKALRKQHPQlMAKVSFPRKVLMGN 73
PX_CISK cd06870
The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The ...
 685-740 8.41e-06

The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Cytokine-independent survival kinase (CISK), also called Serum- and Glucocorticoid-induced Kinase 3 (SGK3), plays a role in cell growth and survival. It is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. CISK/SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. N-terminal to a catalytic kinase domain, CISK contains a PX domain which binds highly phosphorylated PIs, directs membrane localization, and regulates the enzyme's activity.


Pssm-ID: 132780  Cd Length: 109  Bit Score: 45.48  E-value: 8.41e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767987833 685 FHVYQVYIRIKDDEWNIYRRYTEFRSLHHKLQNKYPQVrAYNFPPKKAIGNKPPPS 740
Cdd:cd06870   20 FTVYKVVVSVGRSSWFVFRRYAEFDKLYESLKKQFPAS-NLKIPGKRLFGNNFDPD 74
RUN_SGSM1_like cd17687
RUN domain found in small G protein signaling modulators, SGSM1, SGSM2, and similar proteins; ...
 31-183 1.15e-05

RUN domain found in small G protein signaling modulators, SGSM1, SGSM2, and similar proteins; SGSM1, also called RUN and TBC1 domain-containing protein 2 (RUTBC2), interacts with numerous Rab family members, functioning as Rab effector for some, and as GTPase activator for others. It is a Rab9A effector and GTPase-activating protein for Rab36, and links Rab9A function to Rab36 function in the endosomal system. SGSM2, also called RUN and TBC1 domain-containing protein 1 (RUTBC1), is a GTPase-activating protein for Rab32/38, and regulates melanogenic enzyme trafficking in melanocytes. It also acts as a Rab9A effector that activates GTP hydrolysis by Rab32 and Rab33B proteins. This model contains the RUN domain of SGSM1 and SGSM2.


Pssm-ID: 439049  Cd Length: 161  Bit Score: 46.51  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833  31 VKQCQIRFGGRKEIASDSdSRVTCLCAQFEAVLQHGL-KRSRGL---ALTAAAIKQAAgfASKTETEPVFwYYVKEVLNK 106
Cdd:cd17687    3 VKQLMEEAVTRKFIHEDS-SSVTSLCGAVDACLLHGLrKRALGLfrsSSTFSLLQKVA--KSCPPAADIL-RKVQEIENL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833 107 HELQRFYSLRHIASDVGRGRA-------WLRCALNEHSLERYLHMLLAdrcRLSTFYEDWSFVMDEERSSMLPTMAAGLN 179
Cdd:cd17687   79 SENKRSSSSSGSNSSNSHGNSssnrkilWIRIALFEKVLDKIVDYLVE---NASKYYEKEALMADPVDGPLLASLLVGPC 155


                 ....
gi 767987833 180 SILF 183
Cdd:cd17687  156 ALDY 159
PX_SNX16 cd07276
The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; The PX domain is a ...
 685-793 1.26e-05

The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; 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. SNX16 contains a central PX domain followed by a coiled-coil region. SNX16 is localized in early and recycling endosomes through the binding of its PX domain to phosphatidylinositol-3-phosphate (PI3P). It plays a role in epidermal growth factor (EGF) signaling by regulating EGF receptor membrane trafficking.


Pssm-ID: 132809  Cd Length: 110  Bit Score: 45.09  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833 685 FHVYQVYIRIK-DDEWNIYRRYTEFRSLHHKLQNKYPQVRaYNFPPKKAIGNkpppspawmtaaasllasllpalpplnl 763
Cdd:cd07276   20 FTVYKIRVENKvGDSWFVFRRYTDFVRLNDKLKQMFPGFR-LSLPPKRWFKD---------------------------- 70

                         90       100       110
                 ....*....|....*....|....*....|
gi 767987833 764 qvtsevtsSQDAKFVEERRKQLQNYLRSVM 793
Cdd:cd07276   71 --------NFDPDFLEERQLGLQAFVNNIM 92
RUN1_DENND5 cd17677
RUN1 domain found in DENN domain-containing protein 5 (DENND5) and similar proteins; DENND5 ...
 52-171 1.96e-05

RUN1 domain found in DENN domain-containing protein 5 (DENND5) and similar proteins; DENND5 has been characterized as Rab6-interacting protein which is composed of an N-terminal DENN (Differentially Expressed in Normal and Neoplastic cells) domain followed by two RUN (RPIP8 [RaP2-interacting protein 8], UNC-14, and NESCA [new molecule containing SH3 at the carboxyl terminus]) domains flanking a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain. It functions in membrane trafficking at a crossroads between the Golgi and the endosomal system. DENND5 has two isoforms, DENND5A and DENND5B. This model represents the first RUN domain of DENND5.


Pssm-ID: 439039  Cd Length: 183  Bit Score: 46.24  E-value: 1.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833  52 VTCLCAQFEAVLQHGLKRSRGLALTAAAIKqaAGFASKTETEPV---FWYYVKEVLNKHElqrfyslrhIASDVGRGRAW 128
Cdd:cd17677   52 IASLCDLLERIWSHGLQTKQGKSALWSHLL--AYQENEERLKPLpesLLFDMKNVQNMKE---------IKTDVGYARAW 120

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 767987833 129 LRCALNEHSLERYLHMLLADRCRLSTFYEDWSFVM-DEERSSML 171
Cdd:cd17677  121 IRLALEKKLLSKHLKTLLSNQDLLRSLYKRYAFLRcEDEREQFL 164
RUN1_DENND5B cd17691
RUN1 domain found in DENN domain-containing protein 5B (DENND5B) and similar proteins; DENND5B, ...
 107-171 3.41e-05

RUN1 domain found in DENN domain-containing protein 5B (DENND5B) and similar proteins; DENND5B, also called Rab6-interacting protein 1 (Rab6IP1)-like protein, functions in membrane trafficking at a crossroads between the Golgi and the endosomal system. It is composed of an N-terminal DENN (Differentially Expressed in Normal and Neoplastic cells) domain followed by two RUN (RPIP8 [RaP2-interacting protein 8], UNC-14, and NESCA [new molecule containing SH3 at the carboxyl terminus]) domains flanking a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain. This model represents the first RUN domain of DENND5B.


Pssm-ID: 439053 [Multi-domain]  Cd Length: 206  Bit Score: 45.82  E-value: 3.41e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767987833 107 HELQRFYSLRHIASDVGRGRAWLRCALNEHSLERYLHMLLADRCRLSTFYEDWSFVM-DEERSSML 171
Cdd:cd17691  122 QDMRHIQNMSEIKTDVGRARAWIRLSLEKKLLSQHLKQLLSNQALTKKLYKRYAFLRcEEEKEQFL 187
PX_SNX1_2_like cd06859
The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is ...
 679-794 3.67e-05

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: 43.72  E-value: 3.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833 679 GKAANAFHVYQVYIR-----IKDDEWNIYRRYTEFRSLHHKLQNKYPQVRAYNFPPKKAIGnkpppspawmtaaasllas 753
Cdd:cd06859   12 GDGMSAYVVYRVTTKtnlpdFKKSEFSVLRRYSDFLWLYERLVEKYPGRIVPPPPEKQAVG------------------- 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767987833 754 llpalpplnlqvtsevTSSQDAKFVEERRKQLQNYLRSVMN 794
Cdd:cd06859   73 ----------------RFKVKFEFIEKRRAALERFLRRIAA 97
PX_MONaKA cd06871
The phosphoinositide binding Phox Homology domain of Modulator of Na,K-ATPase; The PX domain ...
 695-793 3.76e-05

The phosphoinositide binding Phox Homology domain of Modulator of Na,K-ATPase; 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. MONaKA (Modulator of Na,K-ATPase) binds the plasma membrane ion transporter, Na,K-ATPase, and modulates its enzymatic and ion pump activities. It modulates brain Na,K-ATPase and may be involved in regulating electrical excitability and synaptic transmission. MONaKA contains an N-terminal PX domain and a C-terminal catalytic kinase domain. The PX domain interacts with PIs and plays a role in targeting proteins to PI-enriched membranes.


Pssm-ID: 132781  Cd Length: 120  Bit Score: 43.89  E-value: 3.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833 695 KDDEWNIYRRYTEFRSLHHKLQnkyPQVRAYNFPPKKAIGNkpppspawmtaaasllasllpalpplnlqvtsevtssQD 774
Cdd:cd06871   34 PENSWQVIRRYNDFDLLNASLQ---ISGISLPLPPKKLIGN-------------------------------------MD 73

                         90
                 ....*....|....*....
gi 767987833 775 AKFVEERRKQLQNYLRSVM 793
Cdd:cd06871   74 REFIAERQQGLQNYLNVIL 92
RUN_RUFY4 cd17697
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; ...
 55-183 2.05e-04

RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; RUFY4 acts as a positive regulator that enhances autophagy and lysosome tethering in response to Interleukin-4. It is expressed in a cell-specific manner or under specific immunological conditions associated with IL4 expression such as allergic asthma. RUFY4 belongs to the FUFY protein family which is characterized by the presence of an N-terminal RUN domain and a C-terminal FYVE domain; this model represents the RUN domain of RUFY4.


Pssm-ID: 439059  Cd Length: 150  Bit Score: 42.48  E-value: 2.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833  55 LCAQFEAVLQHGLKRSRGLaltaaaikqaagFASKTEtepvFWYYVKEVLNKHE-----LQRFYSLRHIASDVGRGRAWL 129
Cdd:cd17697   31 LCARLEYLLQFDQKEKKSF------------FGSRKD----YWDFLCLCLNRHRggtegIHFVNSTDKLKTPLGKGRAFI 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767987833 130 RCALNEHSLERYLHMLLADRCRLSTFYEDWS-FVMDEERSSMLPTMAAgLNSILF 183
Cdd:cd17697   95 RYCLVQQQLAESLQLCLLNPELTGEWYYARSpFLSPELRSDILDSLYE-LNGVNF 148
RUN1_DENND5A cd17690
RUN1 domain found in DENN domain-containing protein 5A (DENND5A) and similar proteins; DENND5A, ...
 107-171 3.32e-04

RUN1 domain found in DENN domain-containing protein 5A (DENND5A) and similar proteins; DENND5A, also called Rab6-interacting protein 1 (Rab6IP1), is present predominantly in developing neuronal tissue, and functions in membrane trafficking at a crossroads between the Golgi and the endosomal system. It is composed of an N-terminal DENN (Differentially Expressed in Normal and Neoplastic cells) domain followed by two RUN (RPIP8 [RaP2-interacting protein 8], UNC-14, and NESCA [new molecule containing SH3 at the carboxyl terminus]) domains flanking a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain. This model represents the first RUN domain of DENND5A.


Pssm-ID: 439052 [Multi-domain]  Cd Length: 209  Bit Score: 43.07  E-value: 3.32e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767987833 107 HELQRFYSLRHIASDVGRGRAWLRCALNEHSLERYLHMLLADRCRLSTFYEDWSFVM-DEERSSML 171
Cdd:cd17690  125 QDMRHIQNIGEIKTDVGKARAWVRLSMEKKLLSRHLKQLLSDHELTKKLYKRYAFLRcDDEKEQFL 190
ZIP_TSC22D cd21936
leucine zipper domain found in the TSC22 domain family of leucine zipper transcription factors; ...
 514-548 5.43e-04

leucine zipper domain found in the TSC22 domain family of leucine zipper transcription factors; The TGF-beta-stimulated clone-22 domain (TSC22D) family includes TSC22D1-4 and similar proteins. They have diverse physiological functions, including cell growth, development, homeostasis, and immune regulation. All family members contain a conserved leucine zipper (ZIP) domain located at the C-terminus. Its first helix is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. In the bZIP family of transcription factors, the leucine zipper acts as a dimerization domain and the upstream basic region as a DNA-binding domain. However, DNA-binding capability of TSC22D family proteins is not obvious, due to the lack of the basic region found in the original bZIP DNA-binding domains. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.


Pssm-ID: 409276  Cd Length: 49  Bit Score: 38.32  E-value: 5.43e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 767987833 514 ALRQEVDTLKRKVAEQEERqgmkVQALARENEVLK 548
Cdd:cd21936   12 AVREEVDVLKEQIAELEER----ISQLERENSLLR 42
PX_Vps5p cd06861
The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps5p; The PX domain ...
 679-803 1.58e-03

The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps5p; 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. 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. The PX domain of Vps5p binds phosphatidylinositol-3-phosphate (PI3P). Similar to SNX1, Vps5p contains 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.


Pssm-ID: 132771  Cd Length: 112  Bit Score: 38.87  E-value: 1.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767987833 679 GKAANAFHVYQVYIRIKD-----DEWNIYRRYTEFRSLHHKLQNKYPQVRAYNFPPKKAIGnkpppspawmtaaasllas 753
Cdd:cd06861   12 GDLTSAHTVYTVRTRTTSpnfevSSFSVLRRYRDFRWLYRQLQNNHPGVIVPPPPEKQSVG------------------- 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767987833 754 llpalpplnlqvtsevtsSQDAKFVEERRKQLQNYLRSVMNK-VIQMVPEF 803
Cdd:cd06861   73 ------------------RFDDNFVEQRRAALEKMLRKIANHpVLQKDPDF 105
PX_p40phox cd06882
The phosphoinositide binding Phox Homology domain of the p40phox subunit of NADPH oxidase; The ...
 685-736 8.72e-03

The phosphoinositide binding Phox Homology domain of the p40phox subunit of NADPH oxidase; The PX domain is a phosphoinositide binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. p40phox contains an N-terminal PX domain, a central SH3 domain that binds p47phox, and a C-terminal PB1 domain that interacts with p67phox. It is a cytosolic subunit of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox) which plays a crucial role in the cellular response to bacterial infection. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p40phox positively regulates NADPH oxidase in both phosphatidylinositol-3-phosphate (PI3P)-dependent and PI3P-independent manner. The PX domain is a phospholipid-binding module involved in the membrane targeting of proteins. The p40phox PX domain binds to PI3P, an abundant lipid in phagosomal membranes, playing an important role in the localization of NADPH oxidase. The PX domain of p40phox is also involved in protein-protein interaction.


Pssm-ID: 132792  Cd Length: 123  Bit Score: 37.03  E-value: 8.72e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767987833 685 FHVYQVYIRIKDDE-WNIYRRYTEFRSLHHKLQNKYP---QVRAYN-----FPPKKAIGNK 736
Cdd:cd06882   20 YYVFVIEVKTKGGSkYLIYRRYRQFFALQSKLEERFGpeaGSSAYDctlptLPGKIYVGRK 80
 
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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