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Conserved domains on  [gi|1958660945|ref|XP_038942785|]
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sorting nexin-29 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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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 ...
36-198 2.19e-97

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: 300.69  E-value: 2.19e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945  36 RLLDAVKQCQIRFGGRKEIASDSDSRVTCLCAQFEAVLQHGMKRSRGLALTAAAIKQA---AGFTSKTETEPVFWVYVKE 112
Cdd:cd17689     1 RLLDAVKQCQIRFGGKTELATESDSRVSCLCAQLEAVLQHGLKTSRSPNLVSSAVTQVsglAGSLGSAETEPTFWPFVKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 113 VLSKHELQRFYSLHHITADVGRGRAWLRCALNEHSLERYLHMLLADRTRLSTFYEDWSFVMDEERSSMLPTMAAGLNSIL 192
Cdd:cd17689    81 HLTKHELERFELLKNIWTDIGRGRAWLRSALNEHSLERYLHILLSNENLLRQYYEDWAFLRDEERSSMLPNMAAGLGSIL 160

                  ....*.
gi 1958660945 193 FAINID 198
Cdd:cd17689   161 FALSID 166
PX_RUN cd07277
The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX ...
681-798 1.72e-76

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: 243.41  E-value: 1.72e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 681 INVWIPSVFLRGKAANAYHVYQVYIRIKDDEWNVYRRYTEFRGLHHQLQSAFPQVRAYSFPPKKAIGNKDAKFVEERRKQ 760
Cdd:cd07277     1 INVWIPSVFLRGKGSDAHHVYQVYIRIRDDEWNVYRRYSEFYELHKKLKKKFPVVRSFDFPPKKAIGNKDAKFVEERRKR 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958660945 761 LQSYLRSVMNKVIQMVPEFAANPKKETLVQLVPFFVDI 798
Cdd:cd07277    81 LQVYLRRVVNTLIQTSPELTACPSKETLIKLLPFFGDT 118
Ax_dynein_light super family cl23860
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in ...
485-565 1.04e-03

Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in flagellar and cilia motility. Eukaryotic cilia and flagella are complex organelles consisting of a core structure, the axoneme, which is composed of nine microtubule doublets forming a cylinder that surrounds a pair of central singlet microtubules. This ultra-structural arrangement seems to be one of the most stable micro-tubular assemblies known and is responsible for the flagellar and ciliary movement of a large number of organizms ranging from protozoan to mammals. This light chain interacts directly with the N-terminal half of the heavy chains.


The actual alignment was detected with superfamily member pfam10211:

Pssm-ID: 463000 [Multi-domain]  Cd Length: 187  Bit Score: 41.02  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 485 ESMTVHELRQAIVAMMNRKD------ELEEENGSLRNLLdgemehsAALRQEVDALRRKVTEQQE----RHATKVQALAR 554
Cdd:pfam10211 104 ESSVAFGMRKALQAEQGKAElekkiaDLEEEKEELEKQV-------AELKAKCEAIEKREEERRQaeekKHAEEIAFLKK 176
                          90
                  ....*....|.
gi 1958660945 555 ENEVLKVQLKK 565
Cdd:pfam10211 177 TNQQLKAQLER 187
 
Name Accession Description Interval E-value
RUN_SNX29 cd17689
RUN domain found in sorting nexin-29 (SNX29) and similar proteins; SNX29, also called RUN ...
36-198 2.19e-97

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: 300.69  E-value: 2.19e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945  36 RLLDAVKQCQIRFGGRKEIASDSDSRVTCLCAQFEAVLQHGMKRSRGLALTAAAIKQA---AGFTSKTETEPVFWVYVKE 112
Cdd:cd17689     1 RLLDAVKQCQIRFGGKTELATESDSRVSCLCAQLEAVLQHGLKTSRSPNLVSSAVTQVsglAGSLGSAETEPTFWPFVKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 113 VLSKHELQRFYSLHHITADVGRGRAWLRCALNEHSLERYLHMLLADRTRLSTFYEDWSFVMDEERSSMLPTMAAGLNSIL 192
Cdd:cd17689    81 HLTKHELERFELLKNIWTDIGRGRAWLRSALNEHSLERYLHILLSNENLLRQYYEDWAFLRDEERSSMLPNMAAGLGSIL 160

                  ....*.
gi 1958660945 193 FAINID 198
Cdd:cd17689   161 FALSID 166
PX_RUN cd07277
The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX ...
681-798 1.72e-76

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: 243.41  E-value: 1.72e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 681 INVWIPSVFLRGKAANAYHVYQVYIRIKDDEWNVYRRYTEFRGLHHQLQSAFPQVRAYSFPPKKAIGNKDAKFVEERRKQ 760
Cdd:cd07277     1 INVWIPSVFLRGKGSDAHHVYQVYIRIRDDEWNVYRRYSEFYELHKKLKKKFPVVRSFDFPPKKAIGNKDAKFVEERRKR 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958660945 761 LQSYLRSVMNKVIQMVPEFAANPKKETLVQLVPFFVDI 798
Cdd:cd07277    81 LQVYLRRVVNTLIQTSPELTACPSKETLIKLLPFFGDT 118
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
64-199 1.09e-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: 125.85  E-value: 1.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945  64 CLCAQFEAVLQHGMKRSRGLALTAAAIKQaagftsktetEPVFWVYVKEV-----LSKHELQRFYSL---HHITADVGRG 135
Cdd:pfam02759   1 QLCAALEALLSHGLKRSSLLILRAAGLLP----------ERSFWALLERVgklvpPAEELLSSVQELeqiHTPYSPDGRG 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958660945 136 RAWLRCALNEHSLERYLHMLLADRTRLSTFYEDWSFVMDEERSSMLPTMAAGLNSILFAINIDN 199
Cdd:pfam02759  71 RAWIRLALNEKLLDQWLKLLLSNKELLSEYYEPWALLADPEFGEILLGLLVGLSALDFNLCLKL 134
RUN smart00593
domain involved in Ras-like GTPase signaling;
135-198 3.46e-21

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 87.67  E-value: 3.46e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958660945  135 GRAWLRCALNEHSLERYLHMLLADRTRLSTFYEDWSFVMDEERSSMLPTMAAGLNSILFAINID 198
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRDPEEGEQLLGLLVGLSALDFNLPVD 64
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
711-780 4.22e-19

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 82.29  E-value: 4.22e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958660945 711 EWNVYRRYTEFRGLHHQLQSAFPQVRAYSFPPKKAIGNKDAKFVEERRKQLQSYLRSVMN-KVIQMVPEFA 780
Cdd:pfam00787   8 EWSVRRRYSDFVELHKKLLRKFPSVIIPPLPPKRWLGRYNEEFIEKRRKGLEQYLQRLLQhPELRNSEVLL 78
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
696-770 1.37e-17

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: 78.92  E-value: 1.37e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958660945  696 NAYHVYQVYIRIKDDEWNVYRRYTEFRGLHHQLQSAFPQVRAYSFPPKKAIG---NKDAKFVEERRKQLQSYLRSVMN 770
Cdd:smart00312  12 HYYYVIEIETKTGLEEWTVSRRYSDFLELHSKLKKHFPRSILPPLPGKKLFGrlnNFSEEFIEKRRRGLEKYLQSLLN 89
Ax_dynein_light pfam10211
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in ...
485-565 1.04e-03

Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in flagellar and cilia motility. Eukaryotic cilia and flagella are complex organelles consisting of a core structure, the axoneme, which is composed of nine microtubule doublets forming a cylinder that surrounds a pair of central singlet microtubules. This ultra-structural arrangement seems to be one of the most stable micro-tubular assemblies known and is responsible for the flagellar and ciliary movement of a large number of organizms ranging from protozoan to mammals. This light chain interacts directly with the N-terminal half of the heavy chains.


Pssm-ID: 463000 [Multi-domain]  Cd Length: 187  Bit Score: 41.02  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 485 ESMTVHELRQAIVAMMNRKD------ELEEENGSLRNLLdgemehsAALRQEVDALRRKVTEQQE----RHATKVQALAR 554
Cdd:pfam10211 104 ESSVAFGMRKALQAEQGKAElekkiaDLEEEKEELEKQV-------AELKAKCEAIEKREEERRQaeekKHAEEIAFLKK 176
                          90
                  ....*....|.
gi 1958660945 555 ENEVLKVQLKK 565
Cdd:pfam10211 177 TNQQLKAQLER 187
 
Name Accession Description Interval E-value
RUN_SNX29 cd17689
RUN domain found in sorting nexin-29 (SNX29) and similar proteins; SNX29, also called RUN ...
36-198 2.19e-97

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: 300.69  E-value: 2.19e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945  36 RLLDAVKQCQIRFGGRKEIASDSDSRVTCLCAQFEAVLQHGMKRSRGLALTAAAIKQA---AGFTSKTETEPVFWVYVKE 112
Cdd:cd17689     1 RLLDAVKQCQIRFGGKTELATESDSRVSCLCAQLEAVLQHGLKTSRSPNLVSSAVTQVsglAGSLGSAETEPTFWPFVKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 113 VLSKHELQRFYSLHHITADVGRGRAWLRCALNEHSLERYLHMLLADRTRLSTFYEDWSFVMDEERSSMLPTMAAGLNSIL 192
Cdd:cd17689    81 HLTKHELERFELLKNIWTDIGRGRAWLRSALNEHSLERYLHILLSNENLLRQYYEDWAFLRDEERSSMLPNMAAGLGSIL 160

                  ....*.
gi 1958660945 193 FAINID 198
Cdd:cd17689   161 FALSID 166
PX_RUN cd07277
The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX ...
681-798 1.72e-76

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: 243.41  E-value: 1.72e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 681 INVWIPSVFLRGKAANAYHVYQVYIRIKDDEWNVYRRYTEFRGLHHQLQSAFPQVRAYSFPPKKAIGNKDAKFVEERRKQ 760
Cdd:cd07277     1 INVWIPSVFLRGKGSDAHHVYQVYIRIRDDEWNVYRRYSEFYELHKKLKKKFPVVRSFDFPPKKAIGNKDAKFVEERRKR 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958660945 761 LQSYLRSVMNKVIQMVPEFAANPKKETLVQLVPFFVDI 798
Cdd:cd07277    81 LQVYLRRVVNTLIQTSPELTACPSKETLIKLLPFFGDT 118
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
64-199 1.09e-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: 125.85  E-value: 1.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945  64 CLCAQFEAVLQHGMKRSRGLALTAAAIKQaagftsktetEPVFWVYVKEV-----LSKHELQRFYSL---HHITADVGRG 135
Cdd:pfam02759   1 QLCAALEALLSHGLKRSSLLILRAAGLLP----------ERSFWALLERVgklvpPAEELLSSVQELeqiHTPYSPDGRG 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958660945 136 RAWLRCALNEHSLERYLHMLLADRTRLSTFYEDWSFVMDEERSSMLPTMAAGLNSILFAINIDN 199
Cdd:pfam02759  71 RAWIRLALNEKLLDQWLKLLLSNKELLSEYYEPWALLADPEFGEILLGLLVGLSALDFNLCLKL 134
RUN cd17671
RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new ...
40-195 5.10e-31

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: 119.07  E-value: 5.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945  40 AVKQCQIRFGGRKEIAS-------DSDSRVTCLCAQFEAVLQHGMKRSRGLaltaaaikqaagftsktETEPVFWVYVKE 112
Cdd:cd17671     2 AVKELLESFADNGEADDsaaltltDDDPVVGRLCAALEAILSHGLKPKRFG-----------------GGKVSFWDFLEA 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 113 VL-------SKHELQRFYSLHHITADVGRGRAWLRCALNEHSLERYLHMLLADRTRLSTFYEDWSFVMDEERSSMLPTMA 185
Cdd:cd17671    65 LEkllpapsLKQAIRDINSLSNVKTDDGRGRAWIRLALNEKSLESYLAALLSDQSLLRKYYEPWALLRDPEEAELFLSLL 144
                         170
                  ....*....|
gi 1958660945 186 AGLNSILFAI 195
Cdd:cd17671   145 VGLSSLDFNL 154
RUN_PLEKHM1 cd17679
RUN domain found in pleckstrin homology domain-containing family M member 1 (PLEKHM1) and ...
33-203 3.76e-29

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: 114.23  E-value: 3.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945  33 LLERLLDAVKQCQIRFGGRKEIASDSDSRVTCLCAQFEAVLQHGMKRSRglaltaaaIKQAAGFTSKTET---EPVFWVY 109
Cdd:cd17679     4 LTKELSSSVKELQLEYVSSDEVVTSSDDGANTLCCVLEAIFLHGLKDKF--------ISKVSSVFSGDVDklpEPNFWPL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 110 VKEVLSKHELQRFYSLHHITADVGRGRAWLRCALNEHSLERYLHMLLADRTRLSTFYEDWSFVMDEERSSMLPTMAAGLN 189
Cdd:cd17679    76 LLKFSHRDVIDQIEHLSQITTDVGRCRAWIRLALNDGLLESYLEAILKDKSALKSYYNPSAFLRDPEQLDILKSLLQGLE 155
                         170
                  ....*....|....
gi 1958660945 190 SILFAINIDNKDLN 203
Cdd:cd17679   156 SFQFELPYNSSLLN 169
PX_KIF16B_SNX23 cd06874
The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The ...
681-795 7.57e-29

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: 111.70  E-value: 7.57e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 681 INVWIPSVFLRGKAANAYHVYQVYIRIKDDEWNVYRRYTEFRGLHHQLQSAFPQVRAYSFPPKKAIGNKDAKFVEERRKQ 760
Cdd:cd06874     1 IKITIPRYVLRGQGKDEHFEFEVKITVLDETWTVFRRYSRFRELHKTMKLKYPEVAALEFPPKKLFGNKSERVAKERRRQ 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958660945 761 LQSYLRSVMNKVIQ-----MVPEFAANPKKETLVQLVPFF 795
Cdd:cd06874    81 LETYLRNFFSVCLKlpacpLYPKVGRTLSKATLCDFSPFF 120
PX_domain cd06093
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
682-770 3.21e-25

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: 100.51  E-value: 3.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 682 NVWIPSVFLRGKAANAYHVYQVYIRIKD-DEWNVYRRYTEFRGLHHQLQSAFPQVRAYSFPPKKAIGNKDAKFVEERRKQ 760
Cdd:cd06093     1 SVSIPDYEKVKDGGKKYVVYIIEVTTQGgEEWTVYRRYSDFEELHEKLKKKFPGVILPPLPPKKLFGNLDPEFIEERRKQ 80
                          90
                  ....*....|
gi 1958660945 761 LQSYLRSVMN 770
Cdd:cd06093    81 LEQYLQSLLN 90
RUN_PLEKHM2 cd17680
RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and ...
32-194 7.22e-23

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: 95.39  E-value: 7.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945  32 FLLERLLDAVKQCQIRFGGRKEIASDSDSR---VTCLCAQFEAVLQHGMKRSRGLaltaaaikqaagftsktetepvFWV 108
Cdd:cd17680     1 RILRNISEAIKSLQSYSSSQEEEDVLITNEnreLQRLCEALDHALLHGLRRGNRG----------------------YWP 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 109 YVKEVLSKHELQRFYSLHHITADVGRGRAWLRCALNEHSLERYLHMLLADRTRLSTFYEDWSFVMDEERSSMLPTMAAGL 188
Cdd:cd17680    59 FVKEFTHKETIKQIENLPNVTTDLGRGRAWLYLALNEGSLESYLRSFLENRKLVKKFYHKHALLRDSQRLELLLTLLSGL 138

                  ....*.
gi 1958660945 189 NSILFA 194
Cdd:cd17680   139 EFVQFD 144
RUN smart00593
domain involved in Ras-like GTPase signaling;
135-198 3.46e-21

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 87.67  E-value: 3.46e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958660945  135 GRAWLRCALNEHSLERYLHMLLADRTRLSTFYEDWSFVMDEERSSMLPTMAAGLNSILFAINID 198
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRDPEEGEQLLGLLVGLSALDFNLPVD 64
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
711-780 4.22e-19

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 82.29  E-value: 4.22e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958660945 711 EWNVYRRYTEFRGLHHQLQSAFPQVRAYSFPPKKAIGNKDAKFVEERRKQLQSYLRSVMN-KVIQMVPEFA 780
Cdd:pfam00787   8 EWSVRRRYSDFVELHKKLLRKFPSVIIPPLPPKRWLGRYNEEFIEKRRKGLEQYLQRLLQhPELRNSEVLL 78
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
696-770 1.37e-17

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: 78.92  E-value: 1.37e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958660945  696 NAYHVYQVYIRIKDDEWNVYRRYTEFRGLHHQLQSAFPQVRAYSFPPKKAIG---NKDAKFVEERRKQLQSYLRSVMN 770
Cdd:smart00312  12 HYYYVIEIETKTGLEEWTVSRRYSDFLELHSKLKKHFPRSILPPLPGKKLFGrlnNFSEEFIEKRRRGLEKYLQSLLN 89
PX_SNX13 cd06873
The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; The PX domain is a ...
697-789 1.99e-16

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: 76.15  E-value: 1.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 697 AYHVYQVYIRIKDDEWNVYRRYTEFRGLHHQLQSAFPQVRAYSFPPKKAIGNKDAKFVEERRKQLQSYLRSVMNKViqmv 776
Cdd:cd06873    26 AISVTRIYPNGQEESWHVYRRYSDFHDLHMRLKEKFPNLSKLSFPGKKTFNNLDRAFLEKRRKMLNQYLQSLLNPE---- 101
                          90
                  ....*....|...
gi 1958660945 777 pEFAANPKKETLV 789
Cdd:cd06873   102 -VLDANPGLQEIV 113
PX_SNARE cd06897
The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain ...
685-770 1.07e-15

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: 73.46  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 685 IPSVFLRGKAanaYHVYQVYIRIKDDEWNVYRRYTEFRGLHHQLQSAFPQVRAYSFPPKKAI--GNKDAKFVEERRKQLQ 762
Cdd:cd06897     5 IPTTSVSPKP---YTVYNIQVRLPLRSYTVSRRYSEFVALHKQLESEVGIEPPYPLPPKSWFlsTSSNPKLVEERRVGLE 81

                  ....*...
gi 1958660945 763 SYLRSVMN 770
Cdd:cd06897    82 AFLRALLN 89
PX_IRAS cd06875
The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor ...
696-778 3.73e-15

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: 72.31  E-value: 3.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 696 NAYHVYQVYIRIKDDEWNVYRRYTEFRGLHHQLqsafpqVRAYS-----FPPKKAIGNKDAKFVEERRKQLQSYLRSVMN 770
Cdd:cd06875    15 EGYTVYIIEVKVGSVEWTVKHRYSDFAELHDKL------VAEHKvdkdlLPPKKLIGNKSPSFVEKRRKELEIYLQTLLS 88

                  ....*...
gi 1958660945 771 KVIQMVPE 778
Cdd:cd06875    89 FFQKTMPR 96
PX_MDM1p cd06876
The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a ...
712-768 8.74e-13

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: 66.18  E-value: 8.74e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958660945 712 WNVYRRYTEFRGLHHQLQSAFPQVRAYSFPPKKAIGNKDAK--FVEERRKQLQSYLRSV 768
Cdd:cd06876    57 WVVARRYSEFLELHKYLKKRYPGVLKLDFPQKRKISLKYSKtlLVEERRKALEKYLQEL 115
PX_SNX16 cd07276
The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; The PX domain is a ...
700-769 8.07e-12

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: 62.43  E-value: 8.07e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958660945 700 VYQVYIRIK-DDEWNVYRRYTEFRGLHHQLQSAFPQVRaYSFPPKKAIG-NKDAKFVEERRKQLQSYLRSVM 769
Cdd:cd07276    22 VYKIRVENKvGDSWFVFRRYTDFVRLNDKLKQMFPGFR-LSLPPKRWFKdNFDPDFLEERQLGLQAFVNNIM 92
RUN_RUNDC3 cd17684
RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 ...
53-193 1.07e-11

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: 63.57  E-value: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945  53 EIASDSDSRVTCLCAQFEAVLQHGMKrsrglaltaaAIKQAAGftskTETEPVFWVYVKEVLSK---HELQRFYSLHHIT 129
Cdd:cd17684    20 ETIDDSSEELINFAAILEQILSHRLK----------PVKPWYG----SEEPRTFWDYIRVACKKvpqNCIASIEQMENIK 85
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958660945 130 ADVGRGRAWLRCALNEHSLERYLHMLLADRTRLSTFYEDWSFVMDEErSSMLPTMAAGLNSILF 193
Cdd:cd17684    86 SPKAKGRAWIRVALMEKRLSEYLSTALKQTRLTRNFYQDGAIMLSED-ATVLCGMLIGLNAIDF 148
PX_MONaKA cd06871
The phosphoinositide binding Phox Homology domain of Modulator of Na,K-ATPase; The PX domain ...
708-769 1.66e-11

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: 61.99  E-value: 1.66e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958660945 708 KDDEWNVYRRYTEFRGLHHQLQSAfpqVRAYSFPPKKAIGNKDAKFVEERRKQLQSYLRSVM 769
Cdd:cd06871    34 PENSWQVIRRYNDFDLLNASLQIS---GISLPLPPKKLIGNMDREFIAERQQGLQNYLNVIL 92
PX_SNX1_2_like cd06859
The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is ...
692-770 8.07e-11

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: 59.90  E-value: 8.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 692 GKAANAYHVYQVYIR-----IKDDEWNVYRRYTEFRGLHHQLQSAFPQVRAYSFPPKKAIGNKDAK--FVEERRKQLQSY 764
Cdd:cd06859    12 GDGMSAYVVYRVTTKtnlpdFKKSEFSVLRRYSDFLWLYERLVEKYPGRIVPPPPEKQAVGRFKVKfeFIEKRRAALERF 91

                  ....*.
gi 1958660945 765 LRSVMN 770
Cdd:cd06859    92 LRRIAA 97
PX_Vps5p cd06861
The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps5p; The PX domain ...
692-779 8.34e-11

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: 59.67  E-value: 8.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 692 GKAANAYHVYQVYIRIKD-----DEWNVYRRYTEFRGLHHQLQSAFPQVRAYSFPPKKAIGNKDAKFVEERRKQLQSYLR 766
Cdd:cd06861    12 GDLTSAHTVYTVRTRTTSpnfevSSFSVLRRYRDFRWLYRQLQNNHPGVIVPPPPEKQSVGRFDDNFVEQRRAALEKMLR 91
                          90
                  ....*....|....
gi 1958660945 767 SVMNK-VIQMVPEF 779
Cdd:cd06861    92 KIANHpVLQKDPDF 105
PX_CISK cd06870
The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The ...
698-781 5.09e-10

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: 57.42  E-value: 5.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 698 YHVYQVYIRIKDDEWNVYRRYTEFRGLHHQLQSAFPQVrAYSFPPKKAIGNK-DAKFVEERRKQLQSYLRSVM--NKVIQ 774
Cdd:cd06870    20 FTVYKVVVSVGRSSWFVFRRYAEFDKLYESLKKQFPAS-NLKIPGKRLFGNNfDPDFIKQRRAGLDEFIQRLVsdPKLLN 98

                  ....*..
gi 1958660945 775 MvPEFAA 781
Cdd:cd06870    99 H-PDVRA 104
RUN_RUNDC3B cd17700
RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN ...
53-194 6.28e-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: 58.44  E-value: 6.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945  53 EIASDSDSRVTCLCAQFEAVLQHGMKrsrglaltaaaiKQAAGFtsKTETEPVFWVYVKEVLSK--HE-LQRFYSLHHIT 129
Cdd:cd17700    20 ETIDDSSPEFVNFAAILEQILSHRLK------------GQVTWF--GYESPRSFWDYIRVACSKvpHNcICSIENMENVS 85
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958660945 130 ADVGRGRAWLRCALNEHSLERYLHMLLADRTRLSTFYEDWSFVMDEErSSMLPTMAAGLNSILFA 194
Cdd:cd17700    86 SSRAKGRAWIRVALMEKRLSEYISTALRDFKTTRRFYEDGAIVLGEE-ANMLAGMLLGLNAIDFS 149
RUN_RUFY1_like cd17681
RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar ...
65-176 1.17e-09

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: 57.58  E-value: 1.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945  65 LCAQFEAVLQHGMKRSRglaltaaaikqaagftSKTETEPVFWvYVKEVLSKH--ELQRFYS----LHHITADVGRGRAW 138
Cdd:cd17681    37 FFVILEHVLRHGLKVKK----------------SFLGPNKSFW-PVLEHVEKLvpEANEITAsvrdLPGIKTPLGRARAW 99
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958660945 139 LRCALNEHSLERYLHMLLADRTRLSTFYEDWSFVMDEE 176
Cdd:cd17681   100 LRLALMQKKLADYFRALIENKDLLSEFYEPGALMMSEE 137
PX_SNX20_21_like cd07279
The phosphoinositide binding Phox Homology domain of Sorting Nexins 20 and 21; The PX domain ...
698-766 1.38e-09

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: 56.18  E-value: 1.38e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958660945 698 YHVYQVYIRIKDDEWN----VYRRYTEFRGLHHQLQSAFPQ-VRAYSFPPKKAIGNKDAKFVEERRKQLQSYLR 766
Cdd:cd07279    18 YVVYQLAVVQTGDPDTqpafIERRYSDFLKLYKALRKQHPQlMAKVSFPRKVLMGNFSSELIAERSRAFEQFLG 91
PX_PI3K_C2 cd06883
The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases; The ...
696-770 2.70e-09

The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. The Phosphoinositide 3-Kinase (PI3K) family of enzymes catalyzes the phosphorylation of the 3-hydroxyl group of the inositol ring of phosphatidylinositol. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They are also involved in the regulation of clathrin-mediated membrane trafficking as well as ATP-dependent priming of neurosecretory granule exocytosis. PI3Ks are divided into three main classes (I, II, and III) based on their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PI as a substrate to produce PI3P, but can also phosphorylate PI4P to produce PI(3,4)P2. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a PX domain, and a second C2 domain at the C-terminus. Class II PI3Ks include three vertebrate isoforms (alpha, beta, and gamma), the Drosophila PI3K_68D, and similar proteins.


Pssm-ID: 132793  Cd Length: 109  Bit Score: 55.44  E-value: 2.70e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958660945 696 NAYHVY--QVYIRIKDDEWNVYRRYTEFRGLHHQLQSAFPQVRAYSFPPKKAIGNKDAKFVEERRK-QLQSYLRSVMN 770
Cdd:cd06883    14 EKYYIYvvKVTRENQTEPSFVFRTFEEFQELHNKLSLLFPSLKLPSFPARVVLGRSHIKQVAERRKiELNSYLKSLFN 91
PX_YPT35 cd07280
The phosphoinositide binding Phox Homology domain of the fungal protein YPT35; The PX domain ...
684-774 4.89e-09

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: 55.03  E-value: 4.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 684 WIPSVFLRG-------KAANAYHVYQVYIRIKDDEW---NVYRRYTEFRGLHHQLQSAFPQVRAYSFP--PKKAIG---- 747
Cdd:cd07280     1 HATDVNVGDytivggdTGGGAYVVWKITIETKDLIGssiVAYKRYSEFVQLREALLDEFPRHKRNEIPqlPPKVPWydsr 80
                          90       100
                  ....*....|....*....|....*....
gi 1958660945 748 -NKDAKFVEERRKQLQSYLRSVM-NKVIQ 774
Cdd:cd07280    81 vNLNKAWLEKRRRGLQYFLNCVLlNPVFG 109
PX_SNX4 cd06864
The phosphoinositide binding Phox Homology domain of Sorting Nexin 4; The PX domain is a ...
698-768 6.53e-09

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: 54.68  E-value: 6.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 698 YHVYQVYIRIKDDEW---------NVYRRYTEFRGLHHQLQSAFPQVRAYSFPPKKA--------IGNKDAKFVEERRKQ 760
Cdd:cd06864    23 YTVYLIETKIVEHESeeglskklsSLWRRYSEFELLRNYLVVTYPYVIVPPLPEKRAmfmwqklsSDTFDPDFVERRRAG 102

                  ....*...
gi 1958660945 761 LQSYLRSV 768
Cdd:cd06864   103 LENFLLRV 110
PX_SNX8_Mvp1p_like cd06866
The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; The PX ...
698-770 1.60e-08

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: 53.00  E-value: 1.60e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958660945 698 YHVYQVYIRIKDDEwnVYRRYTEFRGLHHQLQSAFPQVRAYSFPPKKAIGNKDAKFVEERRKQLQSYLRSVMN 770
Cdd:cd06866    18 HVEYEVSSKRFKST--VYRRYSDFVWLHEYLLKRYPYRMVPALPPKRIGGSADREFLEARRRGLSRFLNLVAR 88
RUN_RUNDC3A cd17699
RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN ...
57-194 1.74e-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: 54.26  E-value: 1.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945  57 DSDSRVTCLCAQFEAVLQHGMKrsrglaltaaaikqAAGFTSKTETEPVFWVYVKEVLSK---HELQRFYSLHHITADVG 133
Cdd:cd17699    24 DSSEEFVNFAAILEQILSHRFK--------------GPVSWFSSDGQRGFWDYIRLACSKvpnNCISSIENMENISTSRA 89
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958660945 134 RGRAWLRCALNEHSLERYLHMLLADRTRLSTFYEDWSFVMDEErSSMLPTMAAGLNSILFA 194
Cdd:cd17699    90 KGRAWIRVALMEKRLSEYIATALRDTRTTRRFYDDGAIMLREE-STVLTGMLIGLSAIDFS 149
PX_SNX2 cd07282
The phosphoinositide binding Phox Homology domain of Sorting Nexin 2; The PX domain is a ...
692-778 2.84e-08

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: 53.14  E-value: 2.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 692 GKAANAYHVYQVYIR-----IKDDEWNVYRRYTEFRGLHHQLQSAFPQVrAYSFPP----------KKAIGNKDA---KF 753
Cdd:cd07282    12 GDGMNAYMAYRVTTKtslsmFSRSEFSVRRRFSDFLGLHSKLASKYLHV-GYIVPPapeksivgmtKVKVGKEDSsstEF 90
                          90       100
                  ....*....|....*....|....*.
gi 1958660945 754 VEERRKQLQSYL-RSVMNKVIQMVPE 778
Cdd:cd07282    91 VEKRRAALERYLqRTVKHPTLLQDPD 116
RUN_RUFY2 cd17695
RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
132-191 4.29e-08

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: 53.44  E-value: 4.29e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 132 VGRGRAWLRCALNEHSLERYLHMLLADRTRLSTFYEDWSFVMDEErSSMLPTMAAGLNSI 191
Cdd:cd17695    93 LGRARAWLRLALMQKKLADYLRCLIIRRDLLSEFYEYHALMMEEE-GAVIVGLLVGLNVI 151
RUN_RUBCN cd17686
RUN domain found in Run domain Beclin-1-interacting and cysteine-rich domain-containing ...
65-181 9.75e-08

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: 51.89  E-value: 9.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945  65 LCAQFEAVLQHGMKRSRGLaltaaaikqaagftsktETEPVFWVYVKEV--------LSKHELQRFYSLHHITADVGRgr 136
Cdd:cd17686    24 LCRAVENILQHGLKEFQGL-----------------NKEIDDWEFVQGLrwlqptlaPSIEQQSRSSPSESEVSDKGR-- 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1958660945 137 AWLRCALNEHSLERYLHMLLADRTRLSTFYEDWSFVMDEERSSML 181
Cdd:cd17686    85 LWLRQSLQQHCLSSQLQWLVSDKELLRKYYEDEAFLRQEGYATAL 129
RUN_RUFY1 cd17694
RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
68-191 3.60e-07

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: 50.67  E-value: 3.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945  68 QFEAVLQHGMKRsrGLALTAAAIKQAAGFTSKTEtepvfwvyVKEVLSKHELQRFYS---LHHITADVGRGRAWLRCALN 144
Cdd:cd17694    36 QFFVVLEHCLKH--GLKVKKSFIGQNKSFFGPLE--------LVEKLCPEASDIATSarnLPELKTAVGRGRAWLHLALM 105
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1958660945 145 EHSLERYLHMLLADRTRLSTFYEDWSFVMDEERSSMLpTMAAGLNSI 191
Cdd:cd17694   106 QKKLADYLKVLIDRKDLLSEFYEPGALMMEEEGAVIV-GLLVGLNVI 151
PX_PI3K_C2_alpha cd07289
The phosphoinositide binding Phox Homology Domain of the Alpha Isoform of Class II ...
687-770 4.19e-07

The phosphoinositide binding Phox Homology Domain of the Alpha Isoform of Class II Phosphoinositide 3-Kinases; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. The Phosphoinositide 3-Kinase (PI3K) family of enzymes catalyzes the phosphorylation of the 3-hydroxyl group of the inositol ring of phosphatidylinositol. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. PI3Ks are divided into three main classes (I, II, and III) based on their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PI as a substrate to produce PI3P, but can also phosphorylate PI4P to produce PI(3,4)P2. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a PX domain, and a second C2 domain at the C-terminus. The class II alpha isoform, PI3K-C2alpha, plays key roles in clathrin assembly and clathrin-mediated membrane trafficking, insulin signaling, vascular smooth muscle contraction, and the priming of neurosecretory granule exocytosis. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction.


Pssm-ID: 132822  Cd Length: 109  Bit Score: 49.16  E-value: 4.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 687 SVFLRGKAANAYHVYQVYIRI----KDDEWNVYRRYTEFRGLHHQLQSAFPQVRAYSFPPKKAIGNKDAKFVEERRK-QL 761
Cdd:cd07289     3 SVFTYHKRYNPDKHYIYVVRIlregQIEPSFVFRTFDEFQELHNKLSILFPLWKLPGFPNKMVLGRTHIKDVAAKRKvEL 82

                  ....*....
gi 1958660945 762 QSYLRSVMN 770
Cdd:cd07289    83 NSYIQSLMN 91
PX_SNX25 cd06878
The phosphoinositide binding Phox Homology domain of Sorting Nexin 25; The PX domain is a ...
712-769 4.29e-07

The phosphoinositide binding Phox Homology domain of Sorting Nexin 25; 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. The function of SNX25 is not yet known. It has been found in exosomes from human malignant pleural effusions. SNX25 shows the same domain architecture as SNX13 and SNX14, containing 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.


Pssm-ID: 132788  Cd Length: 127  Bit Score: 49.68  E-value: 4.29e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 712 WNVYRRYTEFRGLHHQLQSAFPQVRAYSFP--PKKAIGNKDAKFVEERRKQLQSYLRSVM 769
Cdd:cd06878    50 WVVTRKLSEFHDLHRKLKECSSWLKKVELPslSKKWFKSIDKKFLDKSKNQLQKYLQFIL 109
PX_SNX1 cd07281
The phosphoinositide binding Phox Homology domain of Sorting Nexin 1; The PX domain is a ...
692-770 4.97e-07

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: 49.29  E-value: 4.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 692 GKAANAYHVYQVYIR-----IKDDEWNVYRRYTEFRGLHHQLQSAFPQvRAYSFPP----------KKAIGNKD---AKF 753
Cdd:cd07281    12 GDGMNAYVVYKVTTQtsllmFRSKHFTVKRRFSDFLGLYEKLSEKHSQ-NGFIVPPppeksligmtKVKVGKEDsssAEF 90
                          90
                  ....*....|....*..
gi 1958660945 754 VEERRKQLQSYLRSVMN 770
Cdd:cd07281    91 LERRRAALERYLQRIVS 107
PX_SNX19_like_plant cd06872
The phosphoinositide binding Phox Homology domain of uncharacterized SNX19-like plant proteins; ...
701-780 6.03e-07

The phosphoinositide binding Phox Homology domain of uncharacterized SNX19-like plant proteins; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized plant proteins containing an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some sorting nexins (SNXs). This is the same domain architecture found in SNX19. SNX13 and SNX14 also contain these three domains but also contain 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. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction.


Pssm-ID: 132782  Cd Length: 107  Bit Score: 48.67  E-value: 6.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 701 YQVY-IRIKDDE---WNVYRRYTEFRGLHHQLQSaFPQVrAYSFPPKKAIGNK-DAKFVEERRKQLQSYLRSVMnkVIQM 775
Cdd:cd06872    18 FAVYsVAVTDNEnetWVVKRRFRNFETLHRRLKE-VPKY-NLELPPKRFLSSSlDGAFIEERCKLLDKYLKDLL--VIEK 93

                  ....*
gi 1958660945 776 VPEFA 780
Cdd:cd06872    94 VAESH 98
PX_SNX10 cd06898
The phosphoinositide binding Phox Homology domain of Sorting Nexin 10; The PX domain is a ...
713-769 6.16e-07

The phosphoinositide binding Phox Homology domain of Sorting Nexin 10; 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. SNX10 may be involved in the regulation of endosome homeostasis. Its expression induces the formation of giant vacuoles in mammalian cells.


Pssm-ID: 132808  Cd Length: 113  Bit Score: 48.87  E-value: 6.16e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958660945 713 NVYRRYTEFRGLHHQLQSAFPQVRAYSFPPKKAIGN-KDAKFVEERRKQLQSYLRSVM 769
Cdd:cd06898    38 CVRRRYSEFVWLRNRLQKNALLIQLPSLPPKNLFGRfNNEGFIEERQQGLQDFLEKVL 95
RUN_RUFY3 cd17696
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ...
132-191 1.20e-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: 49.22  E-value: 1.20e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 132 VGRGRAWLRCALNEHSLERYLHMLLADRTRLSTFYEDWSFVMDEErSSMLPTMAAGLNSI 191
Cdd:cd17696    93 VGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMMEEE-GAIIAGLLVGLNVI 151
RUN_RUFY4_like cd17682
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil ...
65-195 1.61e-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: 48.38  E-value: 1.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945  65 LCAQFEAVLQHGMKRSRGLaltaaaikqaagFTSKTEtepvFWVYVKEVLSKHELqRFYSLHHITADV----------GR 134
Cdd:cd17682    27 FCETLEKILRKGLKEKVSL------------GGRRKD----YWDWLEELLKKLNK-IPKSLSDAVKFVksckkvktnqGR 89
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958660945 135 GRAWLRCALNEHSLERYLHMLLADRTRLSTFYEDWSFVMDEERSSMLPTMAAGLNSILFAI 195
Cdd:cd17682    90 GRLFIRYALNKKCLHDPVQQLVKNPKLLSDYYSPDSILGNEILSEILLSLLYQLNEINFDL 150
PX_SNX17_31 cd06885
The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain ...
685-768 3.59e-06

The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Members of this subfamily include sorting nexin 17 (SNX17), SNX31, and similar proteins. They contain an N-terminal PX domain followed by a truncated FERM (4.1, ezrin, radixin, and moesin) domain and a unique C-terminal region. 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. SNX17 is known to regulate the trafficking and processing of a number of proteins. It binds some members of the low-density lipoprotein receptor (LDLR) family such as LDLR, VLDLR, ApoER2, and others, regulating their endocytosis. It also binds P-selectin and may regulate its lysosomal degradation. SNX17 is highly expressed in neurons. It binds amyloid precursor protein (APP) and may be involved in its intracellular trafficking and processing to amyloid beta peptide, which plays a central role in the pathogenesis of Alzheimer's disease. The biological function of SNX31 is unknown.


Pssm-ID: 132795  Cd Length: 104  Bit Score: 46.17  E-value: 3.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 685 IP-SVFLRGKAANAYHVYQVYIRikddewNVYR---RYTEFRGLHHQLQSAFPQVRAYSFPPKKaIGNKDAKFVEERRKQ 760
Cdd:cd06885     4 IPdTQELSDEGGSTYVAYNIHIN------GVLHcsvRYSQLHGLNEQLKKEFGNRKLPPFPPKK-LLPLTPAQLEERRLQ 76

                  ....*...
gi 1958660945 761 LQSYLRSV 768
Cdd:cd06885    77 LEKYLQAV 84
PX_SNX14 cd06877
The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; The PX domain is a ...
682-771 4.80e-06

The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; 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. SNX14 may be involved in recruiting other proteins to the membrane via protein-protein and protein-ligand interaction. It is expressed in the embryonic nervous system of mice, and is co-expressed in the motoneurons and the anterior pituary with Islet-1. SNX14 shows a similar domain architecture as SNX13, containing 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.


Pssm-ID: 132787  Cd Length: 119  Bit Score: 46.22  E-value: 4.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 682 NVWIPSVFLRGKAANAYHVYqVYI--------RIKDDE---WNVYRRYTEFRGLHHQLQSAFPQVRAYSFPPKKAIGNKD 750
Cdd:cd06877     4 RVSIPYVEMRRDPSNGERIY-VFCieverndrRAKGHEpqhWSVLRRYNEFYVLESKLTEFHGEFPDAPLPSRRIFGPKS 82
                          90       100
                  ....*....|....*....|.
gi 1958660945 751 AKFVEERRKQLQSYLRSVMNK 771
Cdd:cd06877    83 YEFLESKREIFEEFLQKLLQK 103
PX_SNX15_like cd06881
The phosphoinositide binding Phox Homology domain of Sorting Nexin 15-like proteins; The PX ...
714-796 7.03e-06

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


Pssm-ID: 132791  Cd Length: 117  Bit Score: 45.77  E-value: 7.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 714 VYRRYTEFRGLHHQLQS---------AFPQvraysFPPKKAIGNKDAKFVEERRKQLQSYLrsvmnkviqmvpEFAAN-P 783
Cdd:cd06881    40 VWKRYSDFKKLHRELSRlhkqlylsgSFPP-----FPKGKYFGRFDAAVIEERRQAILELL------------DFVGNhP 102
                          90
                  ....*....|...
gi 1958660945 784 KKETLVQLVPFFV 796
Cdd:cd06881   103 ALYQSSAFQQFFE 115
PX_SNX15 cd07288
The phosphoinositide binding Phox Homology domain of Sorting Nexin 15; The PX domain is a ...
693-797 3.30e-05

The phosphoinositide binding Phox Homology domain of Sorting Nexin 15; 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. SNX15 contains an N-terminal PX domain and a C-terminal Microtubule Interacting and Trafficking (MIT) domain. It plays a role in protein trafficking processes in the endocytic pathway and the trans-Golgi network. The PX domain of SNX15 interacts with the PDGF receptor and is responsible for the membrane association of the protein.


Pssm-ID: 132821  Cd Length: 118  Bit Score: 43.80  E-value: 3.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 693 KAANAYHVYQVYIRIKD----DEWNVYRRYTEFRGLHHQL----------QSAFPqvraySFPPKKAIGNKDAKFVEERR 758
Cdd:cd07288    15 KGYTEYKVTAQFISKKQpedvKEVVVWKRYSDLKKLHGELaythrnlfrrQEEFP-----PFPRAQVFGRFEAAVIEERR 89
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958660945 759 KQLQSYLRSVMNkviqmVPEFAANPkketlvQLVPFFVD 797
Cdd:cd07288    90 NAAEAMLLFTVN-----IPALYNSP------QLKEFFRD 117
RUN1_DENND5B cd17691
RUN1 domain found in DENN domain-containing protein 5B (DENND5B) and similar proteins; DENND5B, ...
117-181 3.57e-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: 3.57e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958660945 117 HELQRFYSLHHITADVGRGRAWLRCALNEHSLERYLHMLLADRTRLSTFYEDWSFVM-DEERSSML 181
Cdd:cd17691   122 QDMRHIQNMSEIKTDVGRARAWIRLSLEKKLLSQHLKQLLSNQALTKKLYKRYAFLRcEEEKEQFL 187
PX_SNX20 cd07300
The phosphoinositide binding Phox Homology domain of Sorting Nexin 20; The PX domain is a ...
685-766 5.16e-05

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


Pssm-ID: 132833  Cd Length: 114  Bit Score: 43.27  E-value: 5.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 685 IPSVFLRGKAANAYHVYQVYIrIKDDEWN-----VYRRYTEFRGLHHQLQSAF-PQVRAYSFPPKKAIGNKDAKFVEERR 758
Cdd:cd07300     5 IPSARIIEQTISKHVVYQIIV-IQTGSFDcnkvvIERRYSDFLKLHQELLSDFsEELEDVVFPKKKLTGNFSEEIIAERR 83

                  ....*...
gi 1958660945 759 KQLQSYLR 766
Cdd:cd07300    84 VALRDYLT 91
PX_SNX22 cd06880
The phosphoinositide binding Phox Homology domain of Sorting Nexin 22; The PX domain is a ...
681-779 6.63e-05

The phosphoinositide binding Phox Homology domain of Sorting Nexin 22; 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. SNX22 may be involved in recruiting other proteins to the membrane via protein-protein and protein-ligand interaction. The biological function of SNX22 is not yet known.


Pssm-ID: 132790  Cd Length: 110  Bit Score: 43.03  E-value: 6.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 681 INVWIPSVFL-RGKAANAYHVYQVYIRIKDDEWNVYRRYTEFRGLHHQLQSAFpqvRAYSFPPKKaIGNKDAKFVEERRK 759
Cdd:cd06880     1 IEVSIPSYRLeVDESEKPYTVFTIEVLVNGRRHTVEKRYSEFHALHKKLKKSI---KTPDFPPKR-VRNWNPKVLEQRRQ 76
                          90       100
                  ....*....|....*....|..
gi 1958660945 760 QLQSYLRSVM--NKVIQMVPEF 779
Cdd:cd06880    77 GLEAYLQGLLkiNELPKQLLDF 98
RUN1_DENND5 cd17677
RUN1 domain found in DENN domain-containing protein 5 (DENND5) and similar proteins; DENND5 ...
128-181 7.74e-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: 44.31  E-value: 7.74e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958660945 128 ITADVGRGRAWLRCALNEHSLERYLHMLLADRTRLSTFYEDWSFVM-DEERSSML 181
Cdd:cd17677   110 IKTDVGYARAWIRLALEKKLLSKHLKTLLSNQDLLRSLYKRYAFLRcEDEREQFL 164
PX_p40phox cd06882
The phosphoinositide binding Phox Homology domain of the p40phox subunit of NADPH oxidase; The ...
698-770 1.35e-04

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: 42.42  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 698 YHVYQVYIRIKDDE-WNVYRRYTEFRGLHHQLQSAFP---QVRAY-----SFPPKKAIGNKdAKFVEERRKQLQSYLRSV 768
Cdd:cd06882    20 YYVFVIEVKTKGGSkYLIYRRYRQFFALQSKLEERFGpeaGSSAYdctlpTLPGKIYVGRK-AEIAERRIPLLNRYMKEL 98

                  ..
gi 1958660945 769 MN 770
Cdd:cd06882    99 LS 100
PX_PI3K_C2_68D cd06884
The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases ...
698-780 1.50e-04

The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases similar to the Drosophila PI3K_68D protein; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. The Phosphoinositide 3-Kinase (PI3K) family of enzymes catalyzes the phosphorylation of the 3-hydroxyl group of the inositol ring of phosphatidylinositol. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. PI3Ks are divided into three main classes (I, II, and III) based on their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PI as a substrate to produce PI3P, but can also phosphorylate PI4P to produce PI(3,4)P2. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a PX domain, and a second C2 domain at the C-terminus. PI3K_68D is a novel PI3K which is widely expressed throughout the Drosophila life cycle. In vitro, it has been shown to phosphorylate PI and PI4P. It is involved in signaling pathways that affect pattern formation of Drosophila wings.


Pssm-ID: 132794  Cd Length: 111  Bit Score: 42.02  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 698 YHVYQVYI--RIKDDEWNVYRRYTEFRGLHHQLQSAFPQVRAYSFPPKKAIGNKDAKFVEERRKQ-LQSYLRSVMnkviQ 774
Cdd:cd06884    18 YYVYVVEVtrENQASPQHVFRTYKEFLELYQKLCRKFPLAKLHPLSTGSHVGRSNIKSVAEKRKQdIQQFLNSLF----K 93

                  ....*.
gi 1958660945 775 MVPEFA 780
Cdd:cd06884    94 MAEEVS 99
PX_UP1_plant cd06879
The phosphoinositide binding Phox Homology domain of uncharacterized plant proteins; The PX ...
714-772 1.62e-04

The phosphoinositide binding Phox Homology domain of uncharacterized plant proteins; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized fungal proteins containing a 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.


Pssm-ID: 132789  Cd Length: 138  Bit Score: 42.32  E-value: 1.62e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958660945 714 VYRRYTEFRGLHHQLQSAFPQVRAYSFPPKKAIGNKDAKFVEERRKQLQSYLRSVMNKV 772
Cdd:cd06879    65 VLRRFNDFLKLHTDLKKLFPKKKLPAAPPKGLLRMKNRALLEERRHSLEEWMGKLLSDI 123
RUN1_DENND5A cd17690
RUN1 domain found in DENN domain-containing protein 5A (DENND5A) and similar proteins; DENND5A, ...
117-181 1.84e-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: 43.46  E-value: 1.84e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958660945 117 HELQRFYSLHHITADVGRGRAWLRCALNEHSLERYLHMLLADRTRLSTFYEDWSFVM-DEERSSML 181
Cdd:cd17690   125 QDMRHIQNIGEIKTDVGKARAWVRLSMEKKLLSRHLKQLLSDHELTKKLYKRYAFLRcDDEKEQFL 190
PX_PI3K_C2_beta cd07290
The phosphoinositide binding Phox Homology Domain of the Beta Isoform of Class II ...
714-780 2.24e-04

The phosphoinositide binding Phox Homology Domain of the Beta Isoform of Class II Phosphoinositide 3-Kinases; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. The Phosphoinositide 3-Kinase (PI3K) family of enzymes catalyzes the phosphorylation of the 3-hydroxyl group of the inositol ring of phosphatidylinositol. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. PI3Ks are divided into three main classes (I, II, and III) based on their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PI as a substrate to produce PI3P, but can also phosphorylate PI4P to produce PI(3,4)P2. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a PX domain, and a second C2 domain at the C-terminus. The class II beta isoform, PI3K-C2beta, contributes to the migration and survival of cancer cells. It regulates Rac activity and impacts membrane ruffling, cell motility, and cadherin-mediated cell-cell adhesion. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction.


Pssm-ID: 132823  Cd Length: 109  Bit Score: 41.45  E-value: 2.24e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958660945 714 VYRRYTEFRGLHHQLQSAFPQVRAYSFPPKKAIGNKDAKFVEERRK-QLQSYLRSVMNKviqmVPEFA 780
Cdd:cd07290    34 VQRTFEEFQELHNKLRLLFPSSKLPSFPSRFVIGRSRGEAVAERRKeELNGYIWHLIHA----PPEVA 97
RUN_SGSM1_like cd17687
RUN domain found in small G protein signaling modulators, SGSM1, SGSM2, and similar proteins; ...
41-193 2.76e-04

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: 42.27  E-value: 2.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945  41 VKQCQIRFGGRKEIASDSdSRVTCLCAQFEAVLQHGM-KRSRGL---ALTAAAIKQAAgfTSKTETEPVFwVYVKEVLSK 116
Cdd:cd17687     3 VKQLMEEAVTRKFIHEDS-SSVTSLCGAVDACLLHGLrKRALGLfrsSSTFSLLQKVA--KSCPPAADIL-RKVQEIENL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 117 HELQRFYSLH-------HITADVGRGRAWLRCALNEHSLERYLHMLLadrTRLSTFYEDWSFVMDEERSSMLPTMAAGLN 189
Cdd:cd17687    79 SENKRSSSSSgsnssnsHGNSSSNRKILWIRIALFEKVLDKIVDYLV---ENASKYYEKEALMADPVDGPLLASLLVGPC 155

                  ....
gi 1958660945 190 SILF 193
Cdd:cd17687   156 ALDY 159
PX_SNX19 cd06893
The phosphoinositide binding Phox Homology domain of Sorting Nexin 19; The PX domain is a ...
714-766 2.83e-04

The phosphoinositide binding Phox Homology domain of Sorting Nexin 19; 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. SNX19 contains an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some SNXs. These domains are also found in SNX13 and SNX14, which also contain a regulator of G protein signaling (RGS) domain in between the PXA and PX domains. SNX19 interacts with IA-2, a major autoantigen found in type-1 diabetes. It inhibits the conversion of phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2] to PI(3,4,5)P3, which leads in the decrease of protein phosphorylation in the Akt signaling pathway, resulting in apoptosis. SNX19 may also be implicated in coronary heart disease and thyroid oncocytic tumors.


Pssm-ID: 132803 [Multi-domain]  Cd Length: 132  Bit Score: 41.76  E-value: 2.83e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958660945 714 VYRRYTEFRGLHHQLQ------SAFPQVRAYSFPPKKAIGNKDAKFVEERRKQLQSYLR 766
Cdd:cd06893    53 VNRRFREFLTLQTRLEenpkfrKIMNVKGPPKRLFDLPFGNMDKDKIEARRGLLETFLR 111
PX_UP2_fungi cd06869
The phosphoinositide binding Phox Homology domain of uncharacterized fungal proteins; The PX ...
699-780 2.89e-04

The phosphoinositide binding Phox Homology domain of uncharacterized fungal proteins; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized fungal proteins containing a 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.


Pssm-ID: 132779  Cd Length: 119  Bit Score: 41.11  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 699 HVYQVYIRIKDDEWN-----VYRRYTEFRGLHHQLQSAFPQVRAYSFPPKKaignkdaKFVEER-RKQLQSYLRSVMNkv 772
Cdd:cd06869    32 HHYEFIIRVRREGEEyrtiyVARRYSDFKKLHHDLKKEFPGKKLPKLPHKD-------KLPREKlRLSLRQYLRSLLK-- 102

                  ....*...
gi 1958660945 773 iqmVPEFA 780
Cdd:cd06869   103 ---DPEVA 107
PX_SNX_like cd06865
The phosphoinositide binding Phox Homology domain of SNX-like proteins; The PX domain is a ...
694-768 4.74e-04

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: 40.87  E-value: 4.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 694 AANAYHVYQVYIRIKD-----DEWNVYRRYTEFRGLHHQLQSAFPqvrAYSFPPK------KAIGNKDAKFVEERRKQLQ 762
Cdd:cd06865    19 GGPPYISYKVTTRTNIpsythGEFTVRRRFRDVVALADRLAEAYR---GAFVPPRpdksvvESQVMQSAEFIEQRRVALE 95

                  ....*.
gi 1958660945 763 SYLRSV 768
Cdd:cd06865    96 KYLNRL 101
RUN_RUFY4 cd17697
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; ...
65-193 5.43e-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: 41.32  E-value: 5.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945  65 LCAQFEAVLQHGMKRSRGLaltaaaikqaagFTSKTEtepvFWVYVKEVLSKHE-----LQRFYSLHHITADVGRGRAWL 139
Cdd:cd17697    31 LCARLEYLLQFDQKEKKSF------------FGSRKD----YWDFLCLCLNRHRggtegIHFVNSTDKLKTPLGKGRAFI 94
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958660945 140 RCALNEHSLERYLHMLLADRTRLSTFYEDWS-FVMDEERSSMLPTMAAgLNSILF 193
Cdd:cd17697    95 RYCLVQQQLAESLQLCLLNPELTGEWYYARSpFLSPELRSDILDSLYE-LNGVNF 148
PX_SNX41_42 cd06867
The phosphoinositide binding Phox Homology domain of fungal Sorting Nexins 41 and 42; The PX ...
701-766 6.00e-04

The phosphoinositide binding Phox Homology domain of fungal Sorting Nexins 41 and 42; 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. SNX41 and SNX42 (also called Atg20p) form dimers with SNX4, and are required in protein recycling from the sorting endosome (post-Golgi endosome) back to the late Golgi in yeast.


Pssm-ID: 132777  Cd Length: 112  Bit Score: 40.31  E-value: 6.00e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958660945 701 YQVY-IRIKDDEwnVYRRYTEFRGLHHQLQSAFPQVRAYSFPPKKAIGN---------KDAKFVEERRKQLQSYLR 766
Cdd:cd06867    18 YIVYvIRLGGSE--VKRRYSEFESLRKNLTRLYPTLIIPPIPEKHSLKDyakkpskakNDAKIIERRKRMLQRFLN 91
PX_SNX18 cd07286
The phosphoinositide binding Phox Homology domain of Sorting Nexin 18; The PX domain is a ...
714-761 9.35e-04

The phosphoinositide binding Phox Homology domain of Sorting Nexin 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. SNX18, like SNX9, contains an N-terminal Src Homology 3 (SH3) domain, a PX domain, and a C-terminal Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature. The PX-BAR structural unit helps determine specific membrane localization. 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: 132819  Cd Length: 127  Bit Score: 40.04  E-value: 9.35e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958660945 714 VYRRYTEFRGLHHQLQSAFPQVRAYSFPPKKAIGNKDAKFVEERRKQL 761
Cdd:cd07286    34 VHRRYKHFDWLYARLAEKFPVISVPHIPEKQATGRFEEDFISKRRKGL 81
PX_SNX9_18_like cd06862
The phosphoinositide binding Phox Homology domain of Sorting Nexins 9 and 18; The PX domain is ...
714-774 1.01e-03

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: 39.99  E-value: 1.01e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958660945 714 VYRRYTEFRGLHHQLQSAFPQVRAYSFPPKKAIGNKDAKFVEERRKQLQSYlrsvMNKVIQ 774
Cdd:cd06862    34 VSRRYKHFDWLYERLVEKYSCIAIPPLPEKQVTGRFEEDFIEKRRERLELW----MNRLAR 90
Ax_dynein_light pfam10211
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in ...
485-565 1.04e-03

Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in flagellar and cilia motility. Eukaryotic cilia and flagella are complex organelles consisting of a core structure, the axoneme, which is composed of nine microtubule doublets forming a cylinder that surrounds a pair of central singlet microtubules. This ultra-structural arrangement seems to be one of the most stable micro-tubular assemblies known and is responsible for the flagellar and ciliary movement of a large number of organizms ranging from protozoan to mammals. This light chain interacts directly with the N-terminal half of the heavy chains.


Pssm-ID: 463000 [Multi-domain]  Cd Length: 187  Bit Score: 41.02  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660945 485 ESMTVHELRQAIVAMMNRKD------ELEEENGSLRNLLdgemehsAALRQEVDALRRKVTEQQE----RHATKVQALAR 554
Cdd:pfam10211 104 ESSVAFGMRKALQAEQGKAElekkiaDLEEEKEELEKQV-------AELKAKCEAIEKREEERRQaeekKHAEEIAFLKK 176
                          90
                  ....*....|.
gi 1958660945 555 ENEVLKVQLKK 565
Cdd:pfam10211 177 TNQQLKAQLER 187
PX_SNX21 cd07301
The phosphoinositide binding Phox Homology domain of Sorting Nexin 21; The PX domain is a ...
716-783 2.34e-03

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


Pssm-ID: 132834  Cd Length: 112  Bit Score: 38.63  E-value: 2.34e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958660945 716 RRYTEFRGLHHQLQSAFP-QVRAYSFPPKKAIGNKDAKFVEERRKQLQSYLRSVmnkviQMVPEFAANP 783
Cdd:cd07301    40 RRYSDFERLHRRLRRLFGgEMAGVSFPRKRLRKNFTAETIAKRSRAFEQFLCHL-----HSLPELRASP 103
 
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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