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Conserved domains on  [gi|659128673|ref|XP_008464317|]
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AP-3 complex subunit mu isoform X1 [Cucumis melo]

Protein Classification

AP-3 complex subunit mu( domain architecture ID 13000765)

AP-3 complex subunit mu is part of the AP-3 complex that is associated with the Golgi region as well as more peripheral structures

Gene Ontology:  GO:0006886

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AP-3_Mu3_Cterm cd09252
C-terminal domain of medium Mu3 subunit in adaptor protein (AP) complex AP-3; AP complexes ...
167-414 2.33e-111

C-terminal domain of medium Mu3 subunit in adaptor protein (AP) complex AP-3; AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This family corresponds to the C-terminal domain of heterotetrameric adaptor protein complex 3 (AP-3) medium mu3 subunit, which includes two closely related homologs, mu3A (P47A, encoded by ap3m1) and mu1B (P47B, encoded by ap3m2). Mu3A is ubiquitously expressed, but mu3B is specifically expressed in neurons and neuroendocrine cells. AP-3 is particularly important for targeting integral membrane proteins to lysosomes and lysome-related organelles at trans-Golgi network (TGN) and/or endosomes, such as the yeast vacuole, fly pigment granules and mammalian melanosomes, platelet dense bodies and the secretory lysosomes of cytotoxic T lymphocytes. Unlike AP-1 and AP-2, which function in conjunction with clathrin which is a scaffolding protein participating in the formation of coated vesicles, the nature of the outer shell of AP-3 containing coats remains to be elucidated. Membrane-anchored cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-3 mu3 subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic residue-binding.


:

Pssm-ID: 271160  Cd Length: 251  Bit Score: 326.85  E-value: 2.33e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 167 VPWRTTDPKYAKNEVNVDLVEEMDAILNRDGHLIKCEIYGEVQVNSHLSGLPDLTLSFTNPSILDDVRFHPCVRFRPWES 246
Cdd:cd09252    1 VPWRRAGVKYTNNEIYFDVVEEIDAIVDKSGKPVSGEVRGEIDCNSRLSGMPDLLLSFNNPRLLDDPSFHPCVRYSRWES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 247 HQILSFVPPDGQFKLVSYRVR--KLKNTPIYVKPQFTSDAGTCRVSVLVGIRRDPGKPIDSIDVQFQLPSCVLSADLTSN 324
Cdd:cd09252   81 ERVLSFIPPDGKFTLMSYRVDlnSLVSLPVYVKPQISFSGSSGRFEITVGSRQNLGKSIENVVVEIPLPKGVKSLRLTAS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 325 YGTVNILSN-KICSWTIGKMPKDKTPSMSGTLTLESGLQQLHVFPTVQVRFKIMGVVLSGLQVDKLDVKNLPNHPYKGFR 403
Cdd:cd09252  161 HGSFSFDSStKTLVWNIGKLTPGKTPTLRGSVSLSSGLEAPSESPSISVQFKIPGYTPSGLKVDSLDIYNEKYKPFKGVK 240
                        250
                 ....*....|.
gi 659128673 404 ALTRAGQFEVR 414
Cdd:cd09252  241 YITKAGKYQVR 251
AP3_Mu_N cd14837
AP-3 complex subunit mu N-terminal domain; AP-3 complex mu subunit is part of the ...
3-142 1.87e-63

AP-3 complex subunit mu N-terminal domain; AP-3 complex mu subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large delta-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. AP-3 binds the coat protein clathrin and the phospholipid PI(3)P and it is localized in the endosome. The mu subunit is comprised of an N-terminal longin domain followed by a C-terminal domain which is involved in the binding of the Y-X-X-Phi sorting signal.


:

Pssm-ID: 341441  Cd Length: 139  Bit Score: 200.44  E-value: 1.87e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673   3 QCIFLLSDSGEIMLEKQLTGhRVDRSICVWFWEQSLSQGDSFKLQPVIASPTHYLFQVVRAGITFLACTQVEMPPLMGIE 82
Cdd:cd14837    1 DSLFILNKSGEVILEKHWRG-RIPRSVLDPFNEALTKPSRPEDVPPVIYTPPYYLFHILRNNLYFLAVVTSEVPPLLVIE 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673  83 FLCRVADVLTDYLGELNEDLVKDNFVIVYELLDEMIDNGFPLTTEPNILREIIAPPNLVS 142
Cdd:cd14837   80 FLHRIVDVLEDYFGSLSESTIKENFVVVYQLLEEMLDNGFPLTTEPNALKELVPPPSLLN 139
 
Name Accession Description Interval E-value
AP-3_Mu3_Cterm cd09252
C-terminal domain of medium Mu3 subunit in adaptor protein (AP) complex AP-3; AP complexes ...
167-414 2.33e-111

C-terminal domain of medium Mu3 subunit in adaptor protein (AP) complex AP-3; AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This family corresponds to the C-terminal domain of heterotetrameric adaptor protein complex 3 (AP-3) medium mu3 subunit, which includes two closely related homologs, mu3A (P47A, encoded by ap3m1) and mu1B (P47B, encoded by ap3m2). Mu3A is ubiquitously expressed, but mu3B is specifically expressed in neurons and neuroendocrine cells. AP-3 is particularly important for targeting integral membrane proteins to lysosomes and lysome-related organelles at trans-Golgi network (TGN) and/or endosomes, such as the yeast vacuole, fly pigment granules and mammalian melanosomes, platelet dense bodies and the secretory lysosomes of cytotoxic T lymphocytes. Unlike AP-1 and AP-2, which function in conjunction with clathrin which is a scaffolding protein participating in the formation of coated vesicles, the nature of the outer shell of AP-3 containing coats remains to be elucidated. Membrane-anchored cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-3 mu3 subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic residue-binding.


Pssm-ID: 271160  Cd Length: 251  Bit Score: 326.85  E-value: 2.33e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 167 VPWRTTDPKYAKNEVNVDLVEEMDAILNRDGHLIKCEIYGEVQVNSHLSGLPDLTLSFTNPSILDDVRFHPCVRFRPWES 246
Cdd:cd09252    1 VPWRRAGVKYTNNEIYFDVVEEIDAIVDKSGKPVSGEVRGEIDCNSRLSGMPDLLLSFNNPRLLDDPSFHPCVRYSRWES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 247 HQILSFVPPDGQFKLVSYRVR--KLKNTPIYVKPQFTSDAGTCRVSVLVGIRRDPGKPIDSIDVQFQLPSCVLSADLTSN 324
Cdd:cd09252   81 ERVLSFIPPDGKFTLMSYRVDlnSLVSLPVYVKPQISFSGSSGRFEITVGSRQNLGKSIENVVVEIPLPKGVKSLRLTAS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 325 YGTVNILSN-KICSWTIGKMPKDKTPSMSGTLTLESGLQQLHVFPTVQVRFKIMGVVLSGLQVDKLDVKNLPNHPYKGFR 403
Cdd:cd09252  161 HGSFSFDSStKTLVWNIGKLTPGKTPTLRGSVSLSSGLEAPSESPSISVQFKIPGYTPSGLKVDSLDIYNEKYKPFKGVK 240
                        250
                 ....*....|.
gi 659128673 404 ALTRAGQFEVR 414
Cdd:cd09252  241 YITKAGKYQVR 251
Adap_comp_sub pfam00928
Adaptor complexes medium subunit family; This family also contains members which are coatomer ...
167-414 1.37e-80

Adaptor complexes medium subunit family; This family also contains members which are coatomer subunits.


Pssm-ID: 395742  Cd Length: 259  Bit Score: 248.76  E-value: 1.37e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673  167 VPWRTTDPKYAKNEVNVDLVEEMDAILNRDGHLIKCEIYGEVQVNSHLSGLPDLTLSFTNP---SILDDVRFHPCVRFRP 243
Cdd:pfam00928   1 VPWRPPGIKYKKNEVFLDVIERVSVIVDKDGGLLNSEVQGTIDLKCFLSGMPELRLGLNDKlllIELDDVSFHQCVNLDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673  244 WESHQILSFVPPDGQFKLVSYRV-RKLKNTPIYVKPQFTSDAGTCRVSVLVGIRRDPGKPI--DSIDVQFQLPSCVLSAD 320
Cdd:pfam00928  81 FESERVISFIPPDGEFELMRYRLsTNEVKLPFTVKPIVSVSGDEGRVEIEVKLRSDFPKKLtaENVVISIPVPKEASSPV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673  321 LTSNYGTVNILS-NKICSWTIGKMPKDKTPSMSGTLTLESGLQQLHVFP---TVQVRFKIMGVVLSGLQVDKLDVKNLPN 396
Cdd:pfam00928 161 LRVSDGKAKYDPeENALEWSIKKIPGGNESSLSGELELSVESSSDDEFPsdpPISVEFSIPMFTASGLKVRYLKVEEENY 240
                         250
                  ....*....|....*...
gi 659128673  397 HPYKGFRALTRAGQFEVR 414
Cdd:pfam00928 241 KPYKWVRYVTQSGSYSIR 258
AP3_Mu_N cd14837
AP-3 complex subunit mu N-terminal domain; AP-3 complex mu subunit is part of the ...
3-142 1.87e-63

AP-3 complex subunit mu N-terminal domain; AP-3 complex mu subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large delta-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. AP-3 binds the coat protein clathrin and the phospholipid PI(3)P and it is localized in the endosome. The mu subunit is comprised of an N-terminal longin domain followed by a C-terminal domain which is involved in the binding of the Y-X-X-Phi sorting signal.


Pssm-ID: 341441  Cd Length: 139  Bit Score: 200.44  E-value: 1.87e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673   3 QCIFLLSDSGEIMLEKQLTGhRVDRSICVWFWEQSLSQGDSFKLQPVIASPTHYLFQVVRAGITFLACTQVEMPPLMGIE 82
Cdd:cd14837    1 DSLFILNKSGEVILEKHWRG-RIPRSVLDPFNEALTKPSRPEDVPPVIYTPPYYLFHILRNNLYFLAVVTSEVPPLLVIE 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673  83 FLCRVADVLTDYLGELNEDLVKDNFVIVYELLDEMIDNGFPLTTEPNILREIIAPPNLVS 142
Cdd:cd14837   80 FLHRIVDVLEDYFGSLSESTIKENFVVVYQLLEEMLDNGFPLTTEPNALKELVPPPSLLN 139
 
Name Accession Description Interval E-value
AP-3_Mu3_Cterm cd09252
C-terminal domain of medium Mu3 subunit in adaptor protein (AP) complex AP-3; AP complexes ...
167-414 2.33e-111

C-terminal domain of medium Mu3 subunit in adaptor protein (AP) complex AP-3; AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This family corresponds to the C-terminal domain of heterotetrameric adaptor protein complex 3 (AP-3) medium mu3 subunit, which includes two closely related homologs, mu3A (P47A, encoded by ap3m1) and mu1B (P47B, encoded by ap3m2). Mu3A is ubiquitously expressed, but mu3B is specifically expressed in neurons and neuroendocrine cells. AP-3 is particularly important for targeting integral membrane proteins to lysosomes and lysome-related organelles at trans-Golgi network (TGN) and/or endosomes, such as the yeast vacuole, fly pigment granules and mammalian melanosomes, platelet dense bodies and the secretory lysosomes of cytotoxic T lymphocytes. Unlike AP-1 and AP-2, which function in conjunction with clathrin which is a scaffolding protein participating in the formation of coated vesicles, the nature of the outer shell of AP-3 containing coats remains to be elucidated. Membrane-anchored cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-3 mu3 subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic residue-binding.


Pssm-ID: 271160  Cd Length: 251  Bit Score: 326.85  E-value: 2.33e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 167 VPWRTTDPKYAKNEVNVDLVEEMDAILNRDGHLIKCEIYGEVQVNSHLSGLPDLTLSFTNPSILDDVRFHPCVRFRPWES 246
Cdd:cd09252    1 VPWRRAGVKYTNNEIYFDVVEEIDAIVDKSGKPVSGEVRGEIDCNSRLSGMPDLLLSFNNPRLLDDPSFHPCVRYSRWES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 247 HQILSFVPPDGQFKLVSYRVR--KLKNTPIYVKPQFTSDAGTCRVSVLVGIRRDPGKPIDSIDVQFQLPSCVLSADLTSN 324
Cdd:cd09252   81 ERVLSFIPPDGKFTLMSYRVDlnSLVSLPVYVKPQISFSGSSGRFEITVGSRQNLGKSIENVVVEIPLPKGVKSLRLTAS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 325 YGTVNILSN-KICSWTIGKMPKDKTPSMSGTLTLESGLQQLHVFPTVQVRFKIMGVVLSGLQVDKLDVKNLPNHPYKGFR 403
Cdd:cd09252  161 HGSFSFDSStKTLVWNIGKLTPGKTPTLRGSVSLSSGLEAPSESPSISVQFKIPGYTPSGLKVDSLDIYNEKYKPFKGVK 240
                        250
                 ....*....|.
gi 659128673 404 ALTRAGQFEVR 414
Cdd:cd09252  241 YITKAGKYQVR 251
Adap_comp_sub pfam00928
Adaptor complexes medium subunit family; This family also contains members which are coatomer ...
167-414 1.37e-80

Adaptor complexes medium subunit family; This family also contains members which are coatomer subunits.


Pssm-ID: 395742  Cd Length: 259  Bit Score: 248.76  E-value: 1.37e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673  167 VPWRTTDPKYAKNEVNVDLVEEMDAILNRDGHLIKCEIYGEVQVNSHLSGLPDLTLSFTNP---SILDDVRFHPCVRFRP 243
Cdd:pfam00928   1 VPWRPPGIKYKKNEVFLDVIERVSVIVDKDGGLLNSEVQGTIDLKCFLSGMPELRLGLNDKlllIELDDVSFHQCVNLDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673  244 WESHQILSFVPPDGQFKLVSYRV-RKLKNTPIYVKPQFTSDAGTCRVSVLVGIRRDPGKPI--DSIDVQFQLPSCVLSAD 320
Cdd:pfam00928  81 FESERVISFIPPDGEFELMRYRLsTNEVKLPFTVKPIVSVSGDEGRVEIEVKLRSDFPKKLtaENVVISIPVPKEASSPV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673  321 LTSNYGTVNILS-NKICSWTIGKMPKDKTPSMSGTLTLESGLQQLHVFP---TVQVRFKIMGVVLSGLQVDKLDVKNLPN 396
Cdd:pfam00928 161 LRVSDGKAKYDPeENALEWSIKKIPGGNESSLSGELELSVESSSDDEFPsdpPISVEFSIPMFTASGLKVRYLKVEEENY 240
                         250
                  ....*....|....*...
gi 659128673  397 HPYKGFRALTRAGQFEVR 414
Cdd:pfam00928 241 KPYKWVRYVTQSGSYSIR 258
AP-3_Mu3B_Cterm cd09261
C-terminal domain of medium Mu3B subunit in neuron-specific adaptor protein (AP) complex AP-3; ...
167-415 4.13e-73

C-terminal domain of medium Mu3B subunit in neuron-specific adaptor protein (AP) complex AP-3; AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This subfamily corresponds to the C-terminal domain of heterotetrameric adaptor protein complex 3 (AP-3) medium mu3B subunit encoded by ap3m2 gene. Mu3B is specifically expressed in neurons and neuroendocrine cells. Neuron-specific AP-3 appears to be involved in synaptic vesicle biogenesis from endosomes in neurons and plays an important role in synaptic transmission in the central nervous system. Unlike AP-1 and AP-2, which function in conjunction with clathrin which is a scaffolding protein participating in the formation of coated vesicles, the nature of the outer shell of neuron-specific AP-3 containing coats remains to be elucidated. Membrane-anchored cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-3 mu3B subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic residue-binding.


Pssm-ID: 211372  Cd Length: 254  Bit Score: 229.54  E-value: 4.13e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 167 VPWRTTDPKYAKNEVNVDLVEEMDAILNRDGHLIKCEIYGEVQVNSHLSGLPDLTLSFTNPSILDDVRFHPCVRFRPWES 246
Cdd:cd09261    1 VPWRRTGVKYTNNEAYFDVIEEIDAIIDKSGSTITAEIQGVIDACVKLTGMPDLTLSFMNPRLLDDVSFHPCVRFKRWES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 247 HQILSFVPPDGQFKLVSYRV--RKLKNTPIYVKP--QFTSDAGTCRVSVLVGIRRDPGKPIDSIDVQFQLPSCVLSADLT 322
Cdd:cd09261   81 ERILSFIPPDGNFRLLSYHVsaQNLVAIPVYVKHniSFREGSSLGRFEITLGPKQTMGKTVEGVTVTSQMPKGVLNMSLT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 323 SNYGTVNILS-NKICSWTIGKMPKDKTPSMSGTLTLESGLQQLHVFPTVQVRFKIMGVVLSGLQVDKLDVKNLPNHPYKG 401
Cdd:cd09261  161 PSQGTYTFDPvTKLLSWDVGKINPQKLPSLKGSMSLQAGASKPDENPTINLQFKIQQLAISGLKVNRLDMYGEKYKPFKG 240
                        250
                 ....*....|....
gi 659128673 402 FRALTRAGQFEVRS 415
Cdd:cd09261  241 IKYMTKAGKFQVRT 254
AP-3_Mu3A_Cterm cd09260
C-terminal domain of medium Mu3A subunit in ubiquitously expressed adaptor protein (AP) ...
167-415 1.38e-70

C-terminal domain of medium Mu3A subunit in ubiquitously expressed adaptor protein (AP) complex AP-3; AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This subfamily corresponds to the C-terminal domain of heterotetrameric adaptor protein complex 3 (AP-3) medium mu3A subunit encoded by ap3m1gene. Mu3A is ubiquitously expressed in all mammalian tissues and cells. It appears to be localized to the trans-Golgi network (TGN) and/or endosomes and participates in trafficking to the vacuole/lysosome in yeast, flies, and mammals. Unlike AP-1 and AP-2, which function in conjunction with clathrin which is a scaffolding protein participating in the formation of coated vesicles, the nature of the outer shell of ubiquitous AP-3 containing coats remains to be elucidated. Membrane-anchored cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-3 mu3A subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic residue-binding.


Pssm-ID: 211371  Cd Length: 254  Bit Score: 223.06  E-value: 1.38e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 167 VPWRTTDPKYAKNEVNVDLVEEMDAILNRDGHLIKCEIYGEVQVNSHLSGLPDLTLSFTNPSILDDVRFHPCVRFRPWES 246
Cdd:cd09260    1 IPWRRAGVKYTNNEAYFDVVEEIDAIIDKSGSTVFAEIQGVIDACIKLSGMPDLSLSFMNPRLLDDVSFHPCIRFKRWES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 247 HQILSFVPPDGQFKLVSYRV--RKLKNTPIYVKPQ--FTSDAGTCRVSVLVGIRRDPGKPIDSIDVQFQLPSCVLSADLT 322
Cdd:cd09260   81 ERVLSFIPPDGNFRLISYRVssQNLVAIPVYVKHNisFKENSSCGRFDITIGPKQNMGKTIEGITVTVHMPKVVLNMNLT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 323 SNYGTVNILS-NKICSWTIGKMPKDKTPSMSGTLTLESGLQQLHVFPTVQVRFKIMGVVLSGLQVDKLDVKNLPNHPYKG 401
Cdd:cd09260  161 PTQGSYTFDPvTKVLAWDVGKITPQKLPSLKGLVNLQSGAPKPEENPSLNIQFKIQQLAISGLKVNRLDMYGEKYKPFKG 240
                        250
                 ....*....|....
gi 659128673 402 FRALTRAGQFEVRS 415
Cdd:cd09260  241 VKYITKAGKFQVRT 254
AP3_Mu_N cd14837
AP-3 complex subunit mu N-terminal domain; AP-3 complex mu subunit is part of the ...
3-142 1.87e-63

AP-3 complex subunit mu N-terminal domain; AP-3 complex mu subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large delta-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. AP-3 binds the coat protein clathrin and the phospholipid PI(3)P and it is localized in the endosome. The mu subunit is comprised of an N-terminal longin domain followed by a C-terminal domain which is involved in the binding of the Y-X-X-Phi sorting signal.


Pssm-ID: 341441  Cd Length: 139  Bit Score: 200.44  E-value: 1.87e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673   3 QCIFLLSDSGEIMLEKQLTGhRVDRSICVWFWEQSLSQGDSFKLQPVIASPTHYLFQVVRAGITFLACTQVEMPPLMGIE 82
Cdd:cd14837    1 DSLFILNKSGEVILEKHWRG-RIPRSVLDPFNEALTKPSRPEDVPPVIYTPPYYLFHILRNNLYFLAVVTSEVPPLLVIE 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673  83 FLCRVADVLTDYLGELNEDLVKDNFVIVYELLDEMIDNGFPLTTEPNILREIIAPPNLVS 142
Cdd:cd14837   80 FLHRIVDVLEDYFGSLSESTIKENFVVVYQLLEEMLDNGFPLTTEPNALKELVPPPSLLN 139
AP_MHD_Cterm cd07954
C-terminal domain of adaptor protein (AP) complexes medium mu subunits and its homologs (MHD); ...
180-414 2.58e-46

C-terminal domain of adaptor protein (AP) complexes medium mu subunits and its homologs (MHD); This family corresponds to the C-terminal domain of heterotetrameric AP complexes medium mu subunits and its homologs existing in monomeric stonins, delta-subunit of the heteroheptameric coat protein I (delta-COPI), a protein encoded by a pro-death gene referred as MuD (also known as MUDENG, mu-2 related death-inducing gene), an endocytic adaptor syp1, the mammalian FCH domain only proteins (FCHo1/2), SH3-containing GRB2-like protein 3-interacting protein 1 (SGIP1), and related proteins. AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. Stonins have been characterized as clathrin-dependent AP-2 mu chain related factors and may act as cargo-specific sorting adaptors in endocytosis. Coat protein complex I (COPI)-coated vesicles function in the early secretory pathway. They mediate the retrograde transport from the Golgi to the ER, and intra-Golgi transport. MuD is distantly related to the C-terminal domain of mu2 subunit of AP-2. It is able to induce cell death by itself and plays an important role in cell death in various tissues. Syp1 represents a novel type of endocytic adaptor protein that participates in endocytosis, promotes vesicle tabulation, and contributes to cell polarity and stress responses. It shares the same domain architecture with its two ubiquitously expressed mammalian counterparts, FCHo1/2, which represent key initial proteins ultimately controlling cellular nutrient uptake, receptor regulation, and synaptic vesicle retrieval. They bind specifically to the plasma membrane and recruit the scaffold proteins eps15 and intersectin, which subsequently engage the adaptor complex AP2 and clathrin, leading to coated vesicle formation. Another mammalian neuronal-specific protein SGIP1 does have a C-terminal MHD and has been classified into this family as well. It is an endophilin-interacting protein that plays an obligatory role in the regulation of energy homeostasis. It is also involved in clathrin-mediated endocytosis by interacting with phospholipids and eps15.


Pssm-ID: 271157  Cd Length: 245  Bit Score: 159.49  E-value: 2.58e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 180 EVNVDLVEEMDAILNRDGHLIKCEIYGEVQVNSHLSGLPDLTLSFTNPSI---LDDVRFHPCVRFRPWESHQILSFVPPD 256
Cdd:cd07954    1 EVFLDVVEKVNLLISKDGSLLNSEVQGEIALKSFLSGMPEIRLGLNNPDVgikLDDVSFHPCVRLKRFESERVISFIPPD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 257 GQFKLVSYR-VRKLKNTPIYVKPQFTSDAGTCRVSVLVGIRRDPGKPIDSIDVQFQLPSCVLSADLTSNYGTVNILS-NK 334
Cdd:cd07954   81 GEFELMSYRtVEPWSILPITIFPVVSEEGSQLEVVITLKLSESLQLTAENVEVHIPLPSGVTSLKSKPSDGQAKFDPeKN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 335 ICSWTIGKMP-KDKTPSMSGTLTLESGLQQLHV-FPTVQVRFKIMGVVLSGLQVDKLDV--KNLPNH-PYKGFRALTRAG 409
Cdd:cd07954  161 ALVWRIKRIPvGGKEQSLSAHVELGSLAHECPEeAPPVSVSFEIPETTGSGIQVRSLQVfdEKNPGHdPIKWVRYITHTG 240

                 ....*
gi 659128673 410 QFEVR 414
Cdd:cd07954  241 KYVAR 245
AP-1_Mu1_Cterm cd09250
C-terminal domain of medium Mu1 subunit in clathrin-associated adaptor protein (AP) complex ...
167-414 2.83e-35

C-terminal domain of medium Mu1 subunit in clathrin-associated adaptor protein (AP) complex AP-1; AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This family corresponds to the C-terminal domain of heterotetrameric clathrin-associated adaptor protein complex 1 (AP-1) medium mu1 subunit, which includes two closely related homologs, mu1A (encoded by ap1m1) and mu1B (encoded by ap1m2). Mu1A is ubiquitously expressed, but mu1B is expressed exclusively in polarized epithelial cells. AP-1 has been implicated in bi-directional transport between the trans-Golgi network (TGN) and endosomes. It plays an essential role in the formation of clathrin-coated vesicles (CCVs) from the trans-Golgi network (TGN). Epithelial cell-specific AP-1 is also involved in sorting to the basolateral surface of polarized epithelial cells. Recruitment of AP-1 to the TGN membrane is regulated by a small GTPase, ADP-ribosylation factor 1 (ARF1). Phosphorylation/dephosphorylation events can also regulate the function of AP-1. The membrane-anchored cargo molecules can be linked to the outer lattice of CCVs by AP-1. Those cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-1 mu1 subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic residue-binding.


Pssm-ID: 271158  Cd Length: 272  Bit Score: 131.19  E-value: 2.83e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 167 VPWRTTDPKYAKNEVNVDLVEEMDAILNRDGHLIKCEIYGEVQVNSHLSGLPDLTLSF--------------TNPSILDD 232
Cdd:cd09250    4 VSWRPEGIKYKKNEVFLDVIESVNLLVDLNGQVLRSEIVGAIKMRSYLSGMPELKLGLndkvlfeatgrsskGKAVELED 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 233 VRFHPCVRFRPWESHQILSFVPPDGQFKLVSYRVRKLKNTPIYVKPQFTSDAGTcRVSVLVGI-----RRDPGK------ 301
Cdd:cd09250   84 VKFHQCVRLSRFENDRTISFIPPDGEFELMSYRLSTQVKPLIWVEPTVERHSRS-RVEIMVKAktqfkRRSTANnveiri 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 302 --PIDSIDVQFQlpscvlsadltSNYGTV--NILSNKICsWTIGKMPKDKTPSMSGTLTL----ESGLQQLHVFPTVQVR 373
Cdd:cd09250  163 pvPPDADSPRFK-----------CSAGSVvyAPEKDALL-WKIKSFPGGKEFSMRAEFGLpsieSEEEQGTEKKAPIQVK 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 659128673 374 FKIMGVVLSGLQVDKLDVKNLPNhpYKGF---RALTRAGQFEVR 414
Cdd:cd09250  231 FEIPYFTVSGLQVRYLKIIEKSG--YQALpwvRYITQSGDYYIR 272
AP_Mu_N cd14828
AP complex subunit mu N-terminal domain; AP complex mu subunits are part of the ...
4-135 2.01e-31

AP complex subunit mu N-terminal domain; AP complex mu subunits are part of the heterotetrameric adaptor protein (AP) complex which consists of one large subunit (alpha-, gamma-, delta- or epsilon), one beta-, one mu-, and one sigma-subunit. In general, AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In most cases the coat protein is clathrin (AP1 and AP2 complex), but some of the other members of the AP complex family are associated with nonclathrin coats. The mu subunit is comprised of an N-terminal longin domain followed by a C-terminal domain which is involved in the binding of the Y-X-X-Phi sorting signal.


Pssm-ID: 341432  Cd Length: 136  Bit Score: 116.53  E-value: 2.01e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673   4 CIFLLSDSGEIMLEKQLTGHRVDRSICVWFWE--QSLSQGDSfklQPVIASPTHYLFQVVRAGITFLACTQVEMPPLMGI 81
Cdd:cd14828    2 CLYILDENLEPLISRNYRADINLQSVVQDFFKayKKLNPEER---PPIISSNGWNFIYIKRDDLYFVSVTQTNVNLMSVL 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 659128673  82 EFLCRVADVLTDYLGE--LNEDLVKDNFVIVYELLDEMIDNGFPLTTEPNILREII 135
Cdd:cd14828   79 VFLDQFYDLLKDYFGVkkLDKNSIIDNFVLIYELIDESIDFGIIQLTDYNILKDYI 134
AP-2_Mu2_Cterm cd09251
C-terminal domain of medium Mu2 subunit in ubiquitously expressed clathrin-associated adaptor ...
176-414 4.43e-31

C-terminal domain of medium Mu2 subunit in ubiquitously expressed clathrin-associated adaptor protein (AP) complex AP-2; AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, -2, -3, and -4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This family corresponds to the C-terminal domain of heterotetrameric clathrin-associated adaptor protein complex 2 (AP-2) medium mu2 subunit. Mu2 is ubiquitously expressed in mammals. In higher eukaryotes, AP-2 plays a critical role in clathrin-mediated endocytosis from the plasma membrane in different cells. The membrane-anchored cargo molecules can be linked to the outer lattice of CCVs by AP-2. Those cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-2 mu2 subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic residue-binding. Since the Y-X-X-Phi binding site is buried in the core structure of AP-2, a phosphorylation induced conformational change is required when the cargo molecules binds to AP-2. In addition, the C-terminal domain of mu2 subunit has been shown to bind other molecules. For instance, it can bind phosphoinositides, in particular PI[4,5]P2, which might be involved in the recognition process of the tyrosine-based signals. It can also interact with synaptotagmins, a family of important modulators of calcium-dependent neurosecretion within the synaptic vesicle (SV) membrane. Since many of the other endocytic adaptors responsible for biogenesis of synaptic vesicles exist, in the absence of AP-2, clathrin-mediated endocytosis can still occur. However, the cells may not survive in the complete absence of clathrin as well as AP-2.


Pssm-ID: 271159  Cd Length: 263  Bit Score: 119.62  E-value: 4.43e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 176 YAKNEVNVDLVEEMDAILNRDGHLIKCEIYGEVQVNSHLSGLPDLTLSF------------------TNPSI-LDDVRFH 236
Cdd:cd09251    1 YRKNEVFLDVVESVNLLMSPQGQVLRADVDGVIVMKTYLSGMPECKFGLndklvlesegkeksgsksGKGSVeLDDCTFH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 237 PCVRFRPWESHQILSFVPPDGQFKLVSYRVRKLKNTPIYVKPQFTsDAGTCRVSVLVGIRR--DPGKPIDSIDVQFQLPS 314
Cdd:cd09251   81 QCVRLSKFDSERSISFIPPDGEFELMRYRVTENINLPFRVIPLVK-EVGRTKLEYKVKIKSnfPPKLLATNVVVRIPVPK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 315 CVLSADLTSNYGTVNILSNKIC-SWTIGKMPKDKTPSMSGTLTLESGLQQLHVF--PTVQVRFKIMGVVLSGLQVDKLDV 391
Cdd:cd09251  160 NTAKVTINVSKGKAKYDPEENAiVWKIKKFAGMTESTLSAEVELLSTTSKKKKWsrPPISMDFEVPMFTASGLRVRYLKV 239
                        250       260
                 ....*....|....*....|....
gi 659128673 392 KNLPNH-PYKGFRALTRAGQFEVR 414
Cdd:cd09251  240 FEKSNYkTVKWVRYITRAGSYEIR 263
AP-1_Mu1B_Cterm cd09259
C-terminal domain of medium Mu1B subunit in epithelial cell-specific clathrin-associated ...
167-414 1.57e-30

C-terminal domain of medium Mu1B subunit in epithelial cell-specific clathrin-associated adaptor protein (AP) complex AP-1; AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from different AP complexes exhibits similarity with each other. This subfamily corresponds to the C-terminal domain of heterotetrameric clathrin-associated adaptor protein complex 1 (AP-1) medium mu1B subunit encoded by ap1m2 gene exclusively expressed in polarized epithelial cells. Epithelial cell-specific AP-1 is used to sort proteins to the basolateral plasma membrane, which involves the formation of clathrin-coated vesicles (CCVs) from the trans-Golgi network (TGN). Recruitment of AP-1 to the TGN membrane is regulated by a small GTPase, ADP-ribosylation factor 1 (ARF1). The phosphorylation/dephosphorylation events can also regulate the function of AP-1. The membrane-anchored cargo molecules can be linked to the outer lattice of CCVs by AP-1. Those cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-1 mu1B subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic reside-binding. Besides, AP-1 mu1B subunit mediates the basolateral recycling of low-density lipoprotein receptor (LDLR) and transferrin receptor (TfR) from the sorting endosomes, where the basolateral sorting signal does not belong to the tyrosine-based signals. Thus, the binding site in mu1B subunit of AP-1 for the signals of LDLR and TfR might be distinct from that for YXXPhi signals.


Pssm-ID: 271167  Cd Length: 268  Bit Score: 118.20  E-value: 1.57e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 167 VPWRTTDPKYAKNEVNVDLVEEMDAILNRDGHLIKCEIYGEVQVNSHLSGLPDLTLSFT------------NPSI-LDDV 233
Cdd:cd09259    4 VSWRSEGIKYKKNEVFIDVIESVNVLVNANGSVLSSEIVGCIKLKVFLSGMPELRLGLNdrvlfeltgrdkNKTVeLEDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 234 RFHPCVRFRPWESHQILSFVPPDGQFKLVSYRVRKLKNTPIYVKPQFTSDAGTcRVSVLVGIRRDPGKP--IDSIDVQFQ 311
Cdd:cd09259   84 KFHQCVRLSRFENDRTISFIPPDGDFELMSYRLNTQVKPLIWIESVIEKFSHS-RVEIMVKAKGQFKKQsvANNVEIRVP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 312 LPSCVLSADLTSNYGTVNILSNK-ICSWTIGKMPKDKTPSMSGTLTLES-GLQQLHVFPTVQVRFKIMGVVLSGLQVDKL 389
Cdd:cd09259  163 VPSDADSPKFKTSVGSAKYVPEKnVVVWSIKSFPGGKEYLMRAHFGLPSvENEELEGKPPITVKFEIPYFTVSGIQVRYM 242
                        250       260
                 ....*....|....*....|....*...
gi 659128673 390 DVknLPNHPYKGF---RALTRAGQFEVR 414
Cdd:cd09259  243 KI--IEKSGYQALpwvRYITQSGDYQLR 268
AP-1_Mu1A_Cterm cd09258
C-terminal domain of medium Mu1A subunit in ubiquitously expressed clathrin-associated adaptor ...
167-415 1.18e-28

C-terminal domain of medium Mu1A subunit in ubiquitously expressed clathrin-associated adaptor protein (AP) complex AP-1; AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This subfamily corresponds to the C-terminal domain of heterotetrameric clathrin-associated adaptor protein complex 1 (AP-1) medium mu1A subunit encoded by ap1m1 gene, which is ubiquitously expressed in all mammalian tissues and cells. AP-1 has been implicated in bidirectional transport between the trans-Golgi network (TGN) and endosomes. It is involved in the formation of clathrin-coated vesicles (CCVs) from the trans-Golgi network (TGN). The ubiquitous AP-1 is recruited to the TGN membrane, as well as to immature secretory granules. Recruitment of AP-1 to the TGN membrane is regulated by a small GTPase, ADP-ribosylation factor 1 (ARF1). Phosphorylation/dephosphorylation events can also regulate the function of AP-1. The membrane-anchored cargo molecules can be linked to the outer lattice of CCVs by AP-1. Those cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-1 mu1A subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic residue-binding.


Pssm-ID: 271166  Cd Length: 270  Bit Score: 113.05  E-value: 1.18e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 167 VPWRTTDPKYAKNEVNVDLVEEMDAILNRDGHLIKCEIYGEVQVNSHLSGLPDLTLSFTNPSI-------------LDDV 233
Cdd:cd09258    5 VSWRSEGIKYRKNEVFLDVIESVNLLVSANGNVLRSEIVGSIKMRVYLSGMPELRLGLNDKVLfentgrgksksveLEDV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 234 RFHPCVRFRPWESHQILSFVPPDGQFKLVSYRVRKLKNTPIYVKPQFTSDAGTcRVSVLVGI-----RRDPGkpiDSIDV 308
Cdd:cd09258   85 KFHQCVRLSRFENDRTISFIPPDGEFELMSYRLNTHVKPLIWIESVIERHSHS-RVEYMIKAksqfkRRSTA---NNVEI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 309 QFQLPSCVLSADLTSNYGTVNILSNKIC-SWTIGKMPKDKTPSMSGTLTLESGL-QQLHVFPTVQVRFKIMGVVLSGLQV 386
Cdd:cd09258  161 HIPVPNDADSPKFKTTVGSVKYVPENSEiVWSIKSFPGGKEYLMRAHFGLPSVEsEEKEGRPPISVKFEIPYFTTSGIQV 240
                        250       260       270
                 ....*....|....*....|....*....|..
gi 659128673 387 DKLdvKNLPNHPYKGF---RALTRAGQFEVRS 415
Cdd:cd09258  241 RYL--KIIEKSGYQALpwvRYITQNGDYQLRT 270
AP-4_Mu4_Cterm cd09253
C-terminal domain of medium Mu4 subunit in adaptor protein (AP) complex AP-4; AP complexes ...
178-414 1.73e-27

C-terminal domain of medium Mu4 subunit in adaptor protein (AP) complex AP-4; AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This family corresponds to the C-terminal domain of heterotetrameric adaptor protein complex 4 (AP-4) medium mu4 subunit. AP-4 plays a role in signal-mediated trafficking of integral membrane proteins in mammalian cells. Unlike other AP complexes, AP-4 is found only in mammals and plants. It is believed to be part of a nonclathrin coat, since it might function independently of clathrin, a scaffolding protein participating in the formation of coated vesicles. Recruitment of AP-4 to the trans-Golgi network (TGN) membrane is regulated by a small GTPase, ADP-ribosylation factor 1 (ARF1) or a related protein. Membrane-anchored cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. One of the most important sorting signals binding to mu subunits of AP complexes are tyrosine-based endocytotic signals, which are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. However, AP-4 does not bind most canonical tyrosine-based signals except for two naturally occurring ones from the lysosomal membrane proteins CD63 and LAMP-2a. It binds YX [FYL][FL]E motif, where X can be any residue, from the cytosolic tails of amyloid precursor protein (APP) family members in a distinct way.


Pssm-ID: 271161  Cd Length: 271  Bit Score: 109.97  E-value: 1.73e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 178 KNEVNVDLVEEMDAILNRDGHLIKCEIYGEVQVNSHLSGLPDLTLSFT------------NPS--ILDDVRFHPCVRFRP 243
Cdd:cd09253   10 RNEIFVDVLERLSVVFNANGQVLNSEIDGSIQMKSYLPGNPELRLALNedlvigkrenraYYSavVLDDCNFHESVDLEE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 244 WESHQILSFVPPDGQFKLVSYRVRKLKNTPIYVKPQFTSDAGTcRVSVLVGIRRD--PGKPIDSIDVQFQLPSCVLSADL 321
Cdd:cd09253   90 FESDRTLSLTPPDGEFTLMNYRISGEFKPPFRVFPSVEETSPY-KLELVLKLRADfpPKSTATNVVVRIPLPKGTTSVSC 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 322 TSNYGTVN-----ILSNKICSWTIGKMPKDKTPSMSGTLTLeSGLQQLHV---FPTVQVRFKIMGVVLSGLQVDKLDV-- 391
Cdd:cd09253  169 ELGSGASGqsaeyKEKEKLVLWNIKKFPGGTELTLRAKITL-SSPVSSSVrkeIGPISLSFEIPMYNVSGLQVRYLRIle 247
                        250       260
                 ....*....|....*....|...
gi 659128673 392 KNLPNHPYKGFRALTRAGQFEVR 414
Cdd:cd09253  248 RSSSYNPHRWVRYVTQSSSYVCR 270
AP1_Mu_N cd14835
AP-1 complex subunit mu N-terminal domain; AP-1 complex mu subunit is part of the ...
42-135 2.66e-24

AP-1 complex subunit mu N-terminal domain; AP-1 complex mu subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large gamma-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In the case of AP-1 the coat protein is clathrin. AP-1 binds the phospholipid PI(4)P which plays a role in its localisation to the trans-Golgi network (TGN)/endosome. The mu subunit is comprised of an N-terminal longin domain followed by a C-terminal domain which is involved in the binding of the Y-X-X-Phi sorting signal.


Pssm-ID: 341439  Cd Length: 139  Bit Score: 97.23  E-value: 2.66e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673  42 DSFKLQPVIASP-THYLFqVVRAGITFLACTQVEMPPLMGIEFLCRVADVLTDYLGELNEDLVKDNFVIVYELLDEMIDN 120
Cdd:cd14835   39 EEGNLTPILTDGgVTYIY-IKHNNLYLLAVTKKNANAAMVLSFLYKLVEVFKEYFKELEEESIRDNFVIIYELLDEMMDF 117
                         90
                 ....*....|....*
gi 659128673 121 GFPLTTEPNILREII 135
Cdd:cd14835  118 GYPQTTESKILQEYI 132
AP4_Mu_N cd14838
AP-4 complex subunit mu N-terminal domain; AP-4 complex mu subunit is part of the ...
55-135 8.41e-23

AP-4 complex subunit mu N-terminal domain; AP-4 complex mu subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large epsilon-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. AP-4 does not bind the coat protein clathrin, it is associated with nonclathrin coats. Its phospholipid binding partner is unknown and it is localized in the trans-Golgi network (TGN). The mu subunit is comprised of an N-terminal longin domain followed by a C-terminal domain which is involved in the binding of the Y-X-X-Phi sorting signal.


Pssm-ID: 341442  Cd Length: 137  Bit Score: 93.38  E-value: 8.41e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673  55 HYLFqVVRAGITFLACTQVEMPPLMGIEFLCRVADVLTDYLGELNEDLVKDNFVIVYELLDEMIDNGFPLTTEPNILREI 134
Cdd:cd14838   51 NYLH-VKRNGLYFVATTRFNVSPSYVLELLNRIAKLIKDYCGVLNEESIRKNFVLIYELLDEILDFGYPQTTSTEQLKSF 129

                 .
gi 659128673 135 I 135
Cdd:cd14838  130 V 130
AP2_Mu_N cd14836
AP-2 complex subunit mu N-terminal domain; AP-2 complex mu subunit is part of the ...
1-135 1.36e-19

AP-2 complex subunit mu N-terminal domain; AP-2 complex mu subunit is part of the heterotetrameric adaptor protein (AP)-2 complex which consists of one large alpha-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In the case of AP-2 the coat protein is clathrin. AP-2 binds the phospholipid PI(4,5)P2 which is important for its localisation to the plasma membrane. The mu subunit is comprised of an N-terminal longin domain followed by a C-terminal domain which is involved in the binding of the Y-X-X-Phi sorting signal.


Pssm-ID: 341440  Cd Length: 140  Bit Score: 84.50  E-value: 1.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673   1 MLQCIFLLSDSGEIMLEKQLTgHRVDRSIcvwfweqslsqGDSFKLQpVIASPTHYL----------FQVVRAG-ITFLA 69
Cdd:cd14836    1 MISALFIYNLKGDVLISRTYR-DDVKRSV-----------ADAFRVQ-VINAKEQVRspvltigstsFFHVRHGnLYLVA 67
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 659128673  70 CTQVEMPPLMGIEFLCRVADVLTDYLGELNEDLVKDNFVIVYELLDEMIDNGFPLTTEPNILREII 135
Cdd:cd14836   68 VTRSNVNAAMVFEFLYKLVQLFKSYFGKFNEDSIKNNFVLIYELLDEILDFGYPQNTEPEALKTYI 133
AP_MuD_MHD cd09256
Mu-homology domain (MHD) of a adaptor protein (AP) encoded by mu-2 related death-inducing gene, ...
203-387 3.58e-14

Mu-homology domain (MHD) of a adaptor protein (AP) encoded by mu-2 related death-inducing gene, MuD (also known as MUDENG); This family corresponds to the MHD found in a protein encoded by MuD (also known as Adapter-related protein complex 5 subunit mu-1), which is distantly related to the C-terminal domain of the mu2 subunit of AP complexes that participates in clathrin-mediated endocytosis. MuD is evolutionary conserved from mammals to amphibians. It is able to induce cell death by itself and plays an important role in cell death in various tissues.


Pssm-ID: 271164  Cd Length: 276  Bit Score: 72.42  E-value: 3.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 203 EIYGEVQVNSHLSGLPDLTLSFTNPSI--LDDVRFHPCVR-----FRPWESHQILSFVPPDGQFKLVSYRVRKLKNTPIY 275
Cdd:cd09256   37 SVFGEVRCKAELEGLPEVTVSLSVPANspLQAIIVHPCVQspesgMLAFSGPYKIRFSPPLGNFVLCRYQSQSVPVPPIL 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 276 VKPQFTSDAGTCRVSVLVGIRRDPGKPIDSIDVQFQLP--SCVLSADLTSNYGTVNILSNK-ICSWTIG-KMPKDKTPSM 351
Cdd:cd09256  117 GFYQMKGDEKHVKFLIQLKLHESVKNSFEYCEVHIPFPnrGLIKHVSATPSNGQLEVSKEKrRLVWNIGqKFPKSLEATL 196
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 659128673 352 SGTLTLESgLQQLHVFPT----------VQVRFKIMGVVLSGLQVD 387
Cdd:cd09256  197 SGTVNFGS-ESNRRADPEdpfcvglnayVKLFFKISDYTLSGCSID 241
AP-like_stonins_MHD cd09255
Mu homology domain (MHD) of adaptor-like proteins (AP-like), stonins; A small family of ...
175-315 6.04e-11

Mu homology domain (MHD) of adaptor-like proteins (AP-like), stonins; A small family of proteins named stonins has been characterized as clathrin-dependent AP-2 mu2 chain related factors, which may act as cargo-specific sorting adaptors in endocytosis. Stonins include stonin 1 and stonin 2, which are only mammalian homologs of Drosophila stoned B, a presynaptic protein implicated in neurotransmission and synaptic vesicle (SV) recycling. They are conserved from C. elegans to humans, but are not found in prokaryotes or yeasts. This family corresponds to the mu homology domain of stonins, which is distantly related to the C-terminal domain of mu chains among AP complexes. Due to the low degree of sequence conservation of the corresponding binding site, the mu homology domain of stonins is unable to recognize tyrosine-based endocytic sorting signals. To data, little is known about the localization and function of stonin 1. Stonin 2, also known as stoned B, acts as an AP-2-dependent synaptotagmin-specific sorting adaptors for SV endocytosis. Stoned A is not a stonin. It is structurally unrelated to the adaptins and does not appear to have mammalian homologs. It is not included in this family.


Pssm-ID: 271163 [Multi-domain]  Cd Length: 315  Bit Score: 63.20  E-value: 6.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 175 KYAKNEVNVDLVEEMDAILNRDGHLIKCEIYGEVQVNSHLSGLPDLTLSFTNPSI---------------------LDDV 233
Cdd:cd09255    7 TYREDEITVDVTDEFHGKVTKTGEIKKLGVTVQIHILSFVTGDPECVLGLNDLEVegrevvrrqdimpsstdqwikLHNC 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 234 RFHPCVRFRPWESHQILSFVPPDG-QFKLVSYRVR-KLKNTPIYVK------PQFTSDAGTCRVSVLVGiRRDPGK-PID 304
Cdd:cd09255   87 EFHSCVDVEEFEQSRSIKFHPLDAcRFELMRFRTRyNKKNLPLTLKsvvsvkGAHVELRADVRMSGYHS-RNPLAQvPCE 165
                        170
                 ....*....|.
gi 659128673 305 SIDVQFQLPSC 315
Cdd:cd09255  166 NIMIRFPVPES 176
AP_longin-like cd14823
Longin-like domains of AP complex subunits; AP complex sigma subunits are part of the ...
78-133 6.90e-11

Longin-like domains of AP complex subunits; AP complex sigma subunits are part of the heterotetrameric adaptor protein (AP) complex which consists of one large subunit (alpha-, gamma-, delta- or epsilon), one beta-, one mu-, and one sigma-subunit. In general, AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In most cases the coat protein is clathrin (AP1 and AP2 complex), but some of the other members of the AP complex family are associated with nonclathrin coats. The sigma subunit is comprised of a single longin domain and plays a role in binding dileucine-based sorting signals.


Pssm-ID: 341427  Cd Length: 131  Bit Score: 59.45  E-value: 6.90e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 659128673  78 LMGIEFLCRVADVLTDYLGELNEDLVKDNFVIVYELLDEMIDNGFPLTTEPNILRE 133
Cdd:cd14823   75 LLLLEVLNCLVDVLSEYFRKVEERAILENFEGLYFALDEIVDGGYIQETDPKQVVH 130
AP_muniscins_like_MHD cd09257
Mu-homology domain (MHD) of muniscins adaptor proteins (AP) and similar proteins; This family ...
180-395 1.64e-07

Mu-homology domain (MHD) of muniscins adaptor proteins (AP) and similar proteins; This family corresponds to the MHD found in muniscins, a novel family of endocytic adaptor proteins. The term, muniscins, has been assigned to name the MHD of proteins with both EFC/F-BAR domain and MHD. These two domains are responsible for the membrane-tubulation activity associated with transmembrane cargo proteins. Members in this family include an endocytic adaptor Syp1, the mammalian FCH domain only proteins (FCHo1/2), SH3-containing GRB2-like protein 3-interacting protein 1 (SGIP1), and related uncharacterized proteins. Syp1 is a poorly characterized yeast protein with multiple biological functions. Syp1 contains an N-terminal EFC/F-BAR domain that induces membrane tabulation, a proline-rich domain (PRD) in the middle region, and a C-terminal MHD that can directly binds to the endocytic adaptor/scaffold protein Ede1 or a transmembrane stress sensor cargo protein Mid2. Thus, Syp1 represents a novel type of endocytic adaptor protein that participates in endocytosis, promotes vesicle tabulation, and contributes to cell polarity and stress response. Syp1 shares the same domain architecture with its two ubiquitously expressed mammalian counterparts, the membrane-sculpting F-BAR domain-containing Fer/Cip4 homology domain-only proteins 1 and 2 (FCHo1/2). FCHo1/2 represent key initial proteins ultimately controlling cellular nutrient uptake, receptor regulation, and synaptic vesicle retrieval. They are required for plasma membrane clathrin-coated vesicle (CCV) budding and marked sites of CCV formation. They bind specifically to the plasma membrane and recruit the scaffold proteins eps15 and intersectin, which subsequently engage the adaptor complex AP2 and clathrin, leading to coated vesicle formation. Another mammalian neuronal-specific protein, neuronal-specific transcript Scr homology 3 (SH3)-domain growth factor receptor-bound 2 (GRB2)-like (endophilin) interacting protein 1 [SGIP1] does not contain EFC/F-BAR domain, but does have a PRD and a C-terminal MHD and has been classified into this family as well. SGIP1 is an endophilin-interacting protein that plays an obligatory role in the regulation of energy homeostasis. It is also involved in clathrin-mediated endocytosis by interacting with phospholipids and eps15.


Pssm-ID: 271165  Cd Length: 244  Bit Score: 51.99  E-value: 1.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 180 EVNVDLVEEMDAILnRDGHLIKCEIYGEVQVNSHLSGLPD----LTLSFTNPSILDDVRFHP-CVRFRPWESHQ---ILS 251
Cdd:cd09257    1 GVKAALTEELNAEF-KGSSLQSVGVEGEVQLAVPSSDAKPkpapFNLRLNDASSLEKAAPNVaFLNSVPSGSSPgefLVN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 252 FVPPDG---QFKLVSYRVR-KLKNTPIYVKPQFTSDAGTCRVsvLVGIRRDPGKPIDSIDVQF--QLPSCVLSADLTSNY 325
Cdd:cd09257   80 TKAIRAsevGSPILKYSCSsKLRPVPLRVQTVWRCESHQTSV--MLQYVSNPSLPGPLQDVTVivNVPPGAGENLKSSPG 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 659128673 326 GTVNiLSNKICSWTIGKMPKDKTP-SMSGTLTLESGLQQLHVFPTVQVRFKIMGVVLSGLQVDKLDVKNLP 395
Cdd:cd09257  158 AVWN-EEKRRLTWKLPELGVNGEGgELRARFQIDAGQTAEKVPFPVLVRCLSEGSTLSGLGLEVVALEEEW 227
AP_stonin-2_MHD cd09263
Mu homology domain (MHD) of adaptor-like protein (AP-like), stonin-2; A small family of ...
176-314 1.13e-04

Mu homology domain (MHD) of adaptor-like protein (AP-like), stonin-2; A small family of proteins named stonins has been characterized as clathrin-dependent AP-2 mu2 chain related factors, which may act as cargo-specific sorting adaptors in endocytosis. Stonins include stonin 1 and stonin 2, which are the only mammalian homologs of Drosophila stoned B, a presynaptic protein implicated in neurotransmission and synaptic vesicle (SV) recycling. They are conserved from C. elegans to humans, but are not found in prokaryotes or yeasts. This family corresponds to the mu homology domain of stonin 2, which is distantly related to the C-terminal domain of mu chains among AP complexes. Due to the low degree of sequence conservation of the corresponding binding site, the mu homology domain of stonin-2 is unable to recognize tyrosine-based endocytic sorting signals. It acts as an AP-2-dependent synaptotagmin-specific sorting adaptor for SV endocytosis.


Pssm-ID: 271169  Cd Length: 318  Bit Score: 43.85  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 176 YAKNEVNVDLVEEMDAILNR-DGHLIKCEIYGEVQVNSHLSGLPDLTLSFTNPSI---------------------LDDV 233
Cdd:cd09263    8 YTEEEITVDVRDEFYGILSKgDSRILQHLVLTRINMLSFLSGLAECRLGLNDILIkgneivsrqdimpttttkwikLRDC 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659128673 234 RFHPCVRFRPWESHQILSFVPPDG-QFKLVSYR-VRKLKNTPiyvkpqFTSDAGTC------------RVSVLVGIRRDP 299
Cdd:cd09263   88 RFHECVDEDEFNNSRAILFNPLDAcRFELMRFRtVFAEKTLP------FTLRTAASvngaevevqswlVMSTGFSSNRDP 161
                        170
                 ....*....|....*..
gi 659128673 300 --GKPIDSIDVQFQLPS 314
Cdd:cd09263  162 ltQVPCENVMIRYPVPE 178
 
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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