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Conserved domains on  [gi|17532373|ref|NP_495704|]
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Cystinosin homolog [Caenorhabditis elegans]

Protein Classification

cystinosin/MPDU1 family protein( domain architecture ID 11490013)

cystinosin/MPDU1 family protein similar to homo sapiens mannose-P-dolichol utilization defect 1, a cystinosin homolog that required for normal utilization of mannose-dolichol phosphate (Dol-P-Man) in the synthesis of N-linked and O-linked oligosaccharides and GPI anchors

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 ...
127-359 3.67e-90

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


:

Pssm-ID: 130026 [Multi-domain]  Cd Length: 220  Bit Score: 271.34  E-value: 3.67e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532373   127 ILIQIVGWTYFFAWSISFYPQMYLNFKRKSVVGLNFDFLSLNLVGFCAYAIFNLLMYYNSHVKNEYNIVNPRspppVLLN 206
Cdd:TIGR00951   2 LLSQILGWGYVAAWSISFYPQIIKNWRRKSAEGLSFDFVMLNLVGFTAYVIFNFLQLYCWSITNEFPLSSPG----VTQN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532373   207 DVVFAVHAFLACFITILQCLFYERDNQSVSSKCIALMIVLISFGFCSAAATVLRKIQLLSFVTSLSYIKMAVTCCKYFPQ 286
Cdd:TIGR00951  78 DVFFTLHAILICFIVLHQCGDYERGWQRVSNPWILRILVALLACFATLLVALLSPITPLAFVTMLSYIKVAVTLVKYFPQ 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17532373   287 AYFNYTRKSTVGWSIGNIMLDFTGgtldILQMILQAVNVNdwsafyANPVKFGLGFVSIFFDIIFMVQHYVLY 359
Cdd:TIGR00951 158 AATNYHNKSTGQLSIITVFLDFTG----LLQRIFQSVNET------GDPLKAGLFVVSSLFNGLFAAQVFFYW 220
 
Name Accession Description Interval E-value
2A43 TIGR00951
Lysosomal Cystine Transporter; [Transport and binding proteins, Amino acids, peptides and ...
127-359 3.67e-90

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


Pssm-ID: 130026 [Multi-domain]  Cd Length: 220  Bit Score: 271.34  E-value: 3.67e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532373   127 ILIQIVGWTYFFAWSISFYPQMYLNFKRKSVVGLNFDFLSLNLVGFCAYAIFNLLMYYNSHVKNEYNIVNPRspppVLLN 206
Cdd:TIGR00951   2 LLSQILGWGYVAAWSISFYPQIIKNWRRKSAEGLSFDFVMLNLVGFTAYVIFNFLQLYCWSITNEFPLSSPG----VTQN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532373   207 DVVFAVHAFLACFITILQCLFYERDNQSVSSKCIALMIVLISFGFCSAAATVLRKIQLLSFVTSLSYIKMAVTCCKYFPQ 286
Cdd:TIGR00951  78 DVFFTLHAILICFIVLHQCGDYERGWQRVSNPWILRILVALLACFATLLVALLSPITPLAFVTMLSYIKVAVTLVKYFPQ 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17532373   287 AYFNYTRKSTVGWSIGNIMLDFTGgtldILQMILQAVNVNdwsafyANPVKFGLGFVSIFFDIIFMVQHYVLY 359
Cdd:TIGR00951 158 AATNYHNKSTGQLSIITVFLDFTG----LLQRIFQSVNET------GDPLKAGLFVVSSLFNGLFAAQVFFYW 220
PQ-loop pfam04193
PQ loop repeat; Members of this family are all membrane bound proteins possessing a pair of ...
128-185 2.88e-15

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: 69.84  E-value: 2.88e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 17532373   128 LIQIVGWTYFFAWSISFYPQMYLNFKRKSVVGLNFDFLSLNLVGFCAYAIFNLLMYYN 185
Cdd:pfam04193   1 LSNVLGYISLVLWLVSYLPQIIKNYKRKSTEGLSILFLLLWLLGDIFYLLYLILNGFP 58
CTNS smart00679
Repeated motif present between transmembrane helices in cystinosin, yeast ERS1p, ...
142-172 3.22e-05

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: 40.51  E-value: 3.22e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 17532373    142 ISFYPQMYLNFKRKSVVGLNFDFLSLNLVGF 172
Cdd:smart00679   1 VSLLPQIIKNYRRKSTEGLSILFVLLWLLGD 31
 
Name Accession Description Interval E-value
2A43 TIGR00951
Lysosomal Cystine Transporter; [Transport and binding proteins, Amino acids, peptides and ...
127-359 3.67e-90

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


Pssm-ID: 130026 [Multi-domain]  Cd Length: 220  Bit Score: 271.34  E-value: 3.67e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532373   127 ILIQIVGWTYFFAWSISFYPQMYLNFKRKSVVGLNFDFLSLNLVGFCAYAIFNLLMYYNSHVKNEYNIVNPRspppVLLN 206
Cdd:TIGR00951   2 LLSQILGWGYVAAWSISFYPQIIKNWRRKSAEGLSFDFVMLNLVGFTAYVIFNFLQLYCWSITNEFPLSSPG----VTQN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17532373   207 DVVFAVHAFLACFITILQCLFYERDNQSVSSKCIALMIVLISFGFCSAAATVLRKIQLLSFVTSLSYIKMAVTCCKYFPQ 286
Cdd:TIGR00951  78 DVFFTLHAILICFIVLHQCGDYERGWQRVSNPWILRILVALLACFATLLVALLSPITPLAFVTMLSYIKVAVTLVKYFPQ 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17532373   287 AYFNYTRKSTVGWSIGNIMLDFTGgtldILQMILQAVNVNdwsafyANPVKFGLGFVSIFFDIIFMVQHYVLY 359
Cdd:TIGR00951 158 AATNYHNKSTGQLSIITVFLDFTG----LLQRIFQSVNET------GDPLKAGLFVVSSLFNGLFAAQVFFYW 220
PQ-loop pfam04193
PQ loop repeat; Members of this family are all membrane bound proteins possessing a pair of ...
128-185 2.88e-15

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: 69.84  E-value: 2.88e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 17532373   128 LIQIVGWTYFFAWSISFYPQMYLNFKRKSVVGLNFDFLSLNLVGFCAYAIFNLLMYYN 185
Cdd:pfam04193   1 LSNVLGYISLVLWLVSYLPQIIKNYKRKSTEGLSILFLLLWLLGDIFYLLYLILNGFP 58
PQ-loop pfam04193
PQ loop repeat; Members of this family are all membrane bound proteins possessing a pair of ...
271-327 1.97e-11

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: 59.05  E-value: 1.97e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17532373   271 LSYIKMAVTCCKYFPQAYFNYTRKSTVGWSIGNIMLDFTGGTLDILQMILQAVNVND 327
Cdd:pfam04193   5 LGYISLVLWLVSYLPQIIKNYKRKSTEGLSILFLLLWLLGDIFYLLYLILNGFPPSL 61
CTNS smart00679
Repeated motif present between transmembrane helices in cystinosin, yeast ERS1p, ...
142-172 3.22e-05

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: 40.51  E-value: 3.22e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 17532373    142 ISFYPQMYLNFKRKSVVGLNFDFLSLNLVGF 172
Cdd:smart00679   1 VSLLPQIIKNYRRKSTEGLSILFVLLWLLGD 31
CTNS smart00679
Repeated motif present between transmembrane helices in cystinosin, yeast ERS1p, ...
282-312 5.98e-05

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: 39.74  E-value: 5.98e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 17532373    282 KYFPQAYFNYTRKSTVGWSIGNIMLDFTGGT 312
Cdd:smart00679   2 SLLPQIIKNYRRKSTEGLSILFVLLWLLGDI 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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