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Conserved domains on  [gi|3165391|dbj|BAA28603|]
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Supl15h [Mus musculus]

Protein Classification

2A43 family protein( domain architecture ID 11490013)

2A43 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
2A43 TIGR00951
Lysosomal Cystine Transporter; [Transport and binding proteins, Amino acids, peptides and ...
40-236 4.95e-70

Lysosomal Cystine Transporter; [Transport and binding proteins, Amino acids, peptides and amines]


:

Pssm-ID: 130026 [Multi-domain]  Cd Length: 220  Bit Score: 214.33  E-value: 4.95e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3165391     40 ILLSKGLGLGIVAGSLLVKLPQVFKLLGAKSAEGLSLQSVMLELVALTGTVVY--------SITNNFPFSSWG---EALF 108
Cdd:TIGR00951   1 ILLSQILGWGYVAAWSISFYPQIIKNWRRKSAEGLSFDFVMLNLVGFTAYVIFnflqlycwSITNEFPLSSPGvtqNDVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3165391    109 LTLQTVAICFLVMHYRGETVKG-------------VAFLACYAMVLLALLSPVTPLAVVTLLQASNVPAVVVGKLLlQAA 175
Cdd:TIGR00951  81 FTLHAILICFIVLHQCGDYERGwqrvsnpwilrilVALLACFATLLVALLSPITPLAFVTMLSYIKVAVTLVKYFP-QAA 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3165391    176 TNYRNGHTGQLSAITVFMLFGGSLARIFTSVQETGDPLMAGVFVVSSLCNGLIAAQVLFYW 236
Cdd:TIGR00951 160 TNYHNKSTGQLSIITVFLDFTGLLQRIFQSVNETGDPLKAGLFVVSSLFNGLFAAQVFFYW 220
 
Name Accession Description Interval E-value
2A43 TIGR00951
Lysosomal Cystine Transporter; [Transport and binding proteins, Amino acids, peptides and ...
40-236 4.95e-70

Lysosomal Cystine Transporter; [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 130026 [Multi-domain]  Cd Length: 220  Bit Score: 214.33  E-value: 4.95e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3165391     40 ILLSKGLGLGIVAGSLLVKLPQVFKLLGAKSAEGLSLQSVMLELVALTGTVVY--------SITNNFPFSSWG---EALF 108
Cdd:TIGR00951   1 ILLSQILGWGYVAAWSISFYPQIIKNWRRKSAEGLSFDFVMLNLVGFTAYVIFnflqlycwSITNEFPLSSPGvtqNDVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3165391    109 LTLQTVAICFLVMHYRGETVKG-------------VAFLACYAMVLLALLSPVTPLAVVTLLQASNVPAVVVGKLLlQAA 175
Cdd:TIGR00951  81 FTLHAILICFIVLHQCGDYERGwqrvsnpwilrilVALLACFATLLVALLSPITPLAFVTMLSYIKVAVTLVKYFP-QAA 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3165391    176 TNYRNGHTGQLSAITVFMLFGGSLARIFTSVQETGDPLMAGVFVVSSLCNGLIAAQVLFYW 236
Cdd:TIGR00951 160 TNYHNKSTGQLSIITVFLDFTGLLQRIFQSVNETGDPLKAGLFVVSSLFNGLFAAQVFFYW 220
PQ-loop pfam04193
PQ loop repeat; Members of this family are all membrane bound proteins possessing a pair of ...
42-101 1.23e-09

PQ loop repeat; Members of this family are all membrane bound proteins possessing a pair of repeats each spanning two transmembrane helices connected by a loop. The PQ motif found on loop 2 is critical for the localization of cystinosin to lysosomes. However, the PQ motif appears not to be a general lysosome-targeting motif. It is thought likely to possess a more general function. Most probably this involves a glutamine residue. Family members are membrane transporters since two members, cystinosin and PQLC2, transport cystine and cationic amino acids, respectively, across the lysosomal membrane. The 2nd PQ-loop of cystinosin hosts the substrate-coupled H+ binding site underlying its H+ symport mechanism, suggesting that PQ-loop repeats have functional significance. It is thus likely that PQ-loop-containing proteins act as a family of membrane transporters. Some transport cystine and cationic amino acids, respectively, across the lysosomal membrane. Others transport lysine and or arginine across the lysosomal membrane in order to maintain the acidic homoeostasis.


Pssm-ID: 461220 [Multi-domain]  Cd Length: 61  Bit Score: 52.89  E-value: 1.23e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 3165391     42 LSKGLGLGIVAGSLLVKLPQVFKLLGAKSAEGLSLQSVMLELVALTGTVVYSITNNFPFS 101
Cdd:pfam04193   1 LSNVLGYISLVLWLVSYLPQIIKNYKRKSTEGLSILFLLLWLLGDIFYLLYLILNGFPPS 60
CTNS smart00679
Repeated motif present between transmembrane helices in cystinosin, yeast ERS1p, ...
168-199 3.01e-04

Repeated motif present between transmembrane helices in cystinosin, yeast ERS1p, mannose-P-dolichol utilization defect 1, and other hypothetical proteins; Function unknown, but likely to be associated with the glycosylation machinery.


Pssm-ID: 128923 [Multi-domain]  Cd Length: 32  Bit Score: 37.05  E-value: 3.01e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 3165391     168 GKLLLQAATNYRNGHTGQLSAITVFMLFGGSL 199
Cdd:smart00679   1 VSLLPQIIKNYRRKSTEGLSILFVLLWLLGDI 32
 
Name Accession Description Interval E-value
2A43 TIGR00951
Lysosomal Cystine Transporter; [Transport and binding proteins, Amino acids, peptides and ...
40-236 4.95e-70

Lysosomal Cystine Transporter; [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 130026 [Multi-domain]  Cd Length: 220  Bit Score: 214.33  E-value: 4.95e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3165391     40 ILLSKGLGLGIVAGSLLVKLPQVFKLLGAKSAEGLSLQSVMLELVALTGTVVY--------SITNNFPFSSWG---EALF 108
Cdd:TIGR00951   1 ILLSQILGWGYVAAWSISFYPQIIKNWRRKSAEGLSFDFVMLNLVGFTAYVIFnflqlycwSITNEFPLSSPGvtqNDVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3165391    109 LTLQTVAICFLVMHYRGETVKG-------------VAFLACYAMVLLALLSPVTPLAVVTLLQASNVPAVVVGKLLlQAA 175
Cdd:TIGR00951  81 FTLHAILICFIVLHQCGDYERGwqrvsnpwilrilVALLACFATLLVALLSPITPLAFVTMLSYIKVAVTLVKYFP-QAA 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3165391    176 TNYRNGHTGQLSAITVFMLFGGSLARIFTSVQETGDPLMAGVFVVSSLCNGLIAAQVLFYW 236
Cdd:TIGR00951 160 TNYHNKSTGQLSIITVFLDFTGLLQRIFQSVNETGDPLKAGLFVVSSLFNGLFAAQVFFYW 220
PQ-loop pfam04193
PQ loop repeat; Members of this family are all membrane bound proteins possessing a pair of ...
42-101 1.23e-09

PQ loop repeat; Members of this family are all membrane bound proteins possessing a pair of repeats each spanning two transmembrane helices connected by a loop. The PQ motif found on loop 2 is critical for the localization of cystinosin to lysosomes. However, the PQ motif appears not to be a general lysosome-targeting motif. It is thought likely to possess a more general function. Most probably this involves a glutamine residue. Family members are membrane transporters since two members, cystinosin and PQLC2, transport cystine and cationic amino acids, respectively, across the lysosomal membrane. The 2nd PQ-loop of cystinosin hosts the substrate-coupled H+ binding site underlying its H+ symport mechanism, suggesting that PQ-loop repeats have functional significance. It is thus likely that PQ-loop-containing proteins act as a family of membrane transporters. Some transport cystine and cationic amino acids, respectively, across the lysosomal membrane. Others transport lysine and or arginine across the lysosomal membrane in order to maintain the acidic homoeostasis.


Pssm-ID: 461220 [Multi-domain]  Cd Length: 61  Bit Score: 52.89  E-value: 1.23e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 3165391     42 LSKGLGLGIVAGSLLVKLPQVFKLLGAKSAEGLSLQSVMLELVALTGTVVYSITNNFPFS 101
Cdd:pfam04193   1 LSNVLGYISLVLWLVSYLPQIIKNYKRKSTEGLSILFLLLWLLGDIFYLLYLILNGFPPS 60
CTNS smart00679
Repeated motif present between transmembrane helices in cystinosin, yeast ERS1p, ...
168-199 3.01e-04

Repeated motif present between transmembrane helices in cystinosin, yeast ERS1p, mannose-P-dolichol utilization defect 1, and other hypothetical proteins; Function unknown, but likely to be associated with the glycosylation machinery.


Pssm-ID: 128923 [Multi-domain]  Cd Length: 32  Bit Score: 37.05  E-value: 3.01e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 3165391     168 GKLLLQAATNYRNGHTGQLSAITVFMLFGGSL 199
Cdd:smart00679   1 VSLLPQIIKNYRRKSTEGLSILFVLLWLLGDI 32
CTNS smart00679
Repeated motif present between transmembrane helices in cystinosin, yeast ERS1p, ...
56-87 1.41e-03

Repeated motif present between transmembrane helices in cystinosin, yeast ERS1p, mannose-P-dolichol utilization defect 1, and other hypothetical proteins; Function unknown, but likely to be associated with the glycosylation machinery.


Pssm-ID: 128923 [Multi-domain]  Cd Length: 32  Bit Score: 35.12  E-value: 1.41e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 3165391      56 LVKLPQVFKLLGAKSAEGLSLQSVMLELVALT 87
Cdd:smart00679   1 VSLLPQIIKNYRRKSTEGLSILFVLLWLLGDI 32
 
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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