NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1561760624|gb|QAT80715|]
View 

hemoglobin linker chain, partial [Auchenoplax crinita]

Protein Classification

LDL receptor domain-containing protein( domain architecture ID 10060319)

Low Density Lipoprotein (LDL) receptor class A domain is a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; similar to Bos taurus CD320 antigen; Low Density Lipoprotein (LDL) receptor class A domain is a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; similar to Bos taurus CD320 antigen; Low Density Lipoprotein (LDL) receptor class A domain is a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; similar to Caenorhabditis elegans LDL receptor repeat-containing protein egg-2

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
hemoglobin_linker_C super family cl17028
Globular domain of extracellular hemoglobin linker; This family of hemoglobin linker chains is ...
 175-274 1.01e-18

Globular domain of extracellular hemoglobin linker; This family of hemoglobin linker chains is restricted to annelid worms, and participates in the formation of the large erythrocruorin respiratory complex. Via its N-terminal coiled-coil segment (not included in this model), the molecule forms trimers, which are part of a scaffold organizing the overall complex architecture; the latter encompasses 36 linkers and 144 hemoglobins in total. This C-terminal globular domain is involved in trimerization, and also interacts with globins and other C-terminal globular linker domains of neighboring trimers. The structure resembles that of nitrophorins and lipocalins.


The actual alignment was detected with superfamily member cd11673:

Pssm-ID: 327373  Cd Length: 120  Bit Score: 79.72  E-value: 1.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561760624 175 GCAKRRISEFQVTIRKVVTNEYIASRPRIEASILATSQAGGRSSQEYFTVKGDWDSSHQTLVLRPPEESDPVGLICEFDG 254
Cdd:cd11673    15 HCTKRRPKHMDIHITSVKRYSFFPSRPKVKATVVIESTKDGDEQTSSLQVKGFYSFGSRRLILLPPDGLDGLGFVCDFDG 94

                          90       100
                  ....*....|....*....|
gi 1561760624 255 VDDDHCDGAYYNVHTREKCG 274
Cdd:cd11673    95 GDNDRCKGHIVREASGDVCA 114
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 117-152 2.85e-05

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 40.27  E-value: 2.85e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1561760624 117 CSDSEhFACedGSGRCISRLLVCDKIKDCNNGADED 152
Cdd:cd00112     1 CPPNE-FRC--ANGRCIPSSWVCDGEDDCGDGSDEE 33
 
Name Accession Description Interval E-value
hemoglobin_linker_C cd11673
Globular domain of extracellular hemoglobin linker; This family of hemoglobin linker chains is ...
 175-274 1.01e-18

Globular domain of extracellular hemoglobin linker; This family of hemoglobin linker chains is restricted to annelid worms, and participates in the formation of the large erythrocruorin respiratory complex. Via its N-terminal coiled-coil segment (not included in this model), the molecule forms trimers, which are part of a scaffold organizing the overall complex architecture; the latter encompasses 36 linkers and 144 hemoglobins in total. This C-terminal globular domain is involved in trimerization, and also interacts with globins and other C-terminal globular linker domains of neighboring trimers. The structure resembles that of nitrophorins and lipocalins.


Pssm-ID: 212563  Cd Length: 120  Bit Score: 79.72  E-value: 1.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561760624 175 GCAKRRISEFQVTIRKVVTNEYIASRPRIEASILATSQAGGRSSQEYFTVKGDWDSSHQTLVLRPPEESDPVGLICEFDG 254
Cdd:cd11673    15 HCTKRRPKHMDIHITSVKRYSFFPSRPKVKATVVIESTKDGDEQTSSLQVKGFYSFGSRRLILLPPDGLDGLGFVCDFDG 94

                          90       100
                  ....*....|....*....|
gi 1561760624 255 VDDDHCDGAYYNVHTREKCG 274
Cdd:cd11673    95 GDNDRCKGHIVREASGDVCA 114
Eryth_link_C pfam16915
Annelid erythrocruorin linker subunit C-terminus; This domain is found in linker subunits of ...
 158-274 9.33e-18

Annelid erythrocruorin linker subunit C-terminus; This domain is found in linker subunits of the erythrocruorin respiratory complex in annelid worms.


Pssm-ID: 319001  Cd Length: 120  Bit Score: 77.39  E-value: 9.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561760624 158 PPQSGVRFEAHVTPHdaGCAKRRISEFQVTIRKVVTNEYIASRPRIEASILATSQAGGRSSQEYFTVKGDWDSSHQTLVL 237
Cdd:pfam16915   1 PTPAGSSFIGDLNWD--HCTKRRPKHMDIHITSVKRSSFFPSRPWVKATVDLESHQDGHEQTSTLPVDGFYNFGSRRLIL 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1561760624 238 RPPEEsDPVGLICEFDGVDDDHCDGAYYNVHTREKCG 274
Cdd:pfam16915  79 LPPEG-DGLGLVCSFDGGDDDRCKGHIVRESSLDVCA 114
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 117-152 2.85e-05

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 40.27  E-value: 2.85e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1561760624 117 CSDSEhFACedGSGRCISRLLVCDKIKDCNNGADED 152
Cdd:cd00112     1 CPPNE-FRC--ANGRCIPSSWVCDGEDDCGDGSDEE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 117-151 4.92e-05

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 39.54  E-value: 4.92e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1561760624  117 CSDSEHFACedGSGRCISRLLVCDKIKDCNNGADE 151
Cdd:smart00192   1 TCPPGEFQC--DNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
116-151 2.48e-03

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 34.92  E-value: 2.48e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1561760624 116 QCSDSEhFACedGSGRCISRLLVCDKIKDCNNGADE 151
Cdd:pfam00057   2 TCSPNE-FQC--GSGECIPRSWVCDGDPDCGDGSDE 34
 
Name Accession Description Interval E-value
hemoglobin_linker_C cd11673
Globular domain of extracellular hemoglobin linker; This family of hemoglobin linker chains is ...
 175-274 1.01e-18

Globular domain of extracellular hemoglobin linker; This family of hemoglobin linker chains is restricted to annelid worms, and participates in the formation of the large erythrocruorin respiratory complex. Via its N-terminal coiled-coil segment (not included in this model), the molecule forms trimers, which are part of a scaffold organizing the overall complex architecture; the latter encompasses 36 linkers and 144 hemoglobins in total. This C-terminal globular domain is involved in trimerization, and also interacts with globins and other C-terminal globular linker domains of neighboring trimers. The structure resembles that of nitrophorins and lipocalins.


Pssm-ID: 212563  Cd Length: 120  Bit Score: 79.72  E-value: 1.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561760624 175 GCAKRRISEFQVTIRKVVTNEYIASRPRIEASILATSQAGGRSSQEYFTVKGDWDSSHQTLVLRPPEESDPVGLICEFDG 254
Cdd:cd11673    15 HCTKRRPKHMDIHITSVKRYSFFPSRPKVKATVVIESTKDGDEQTSSLQVKGFYSFGSRRLILLPPDGLDGLGFVCDFDG 94

                          90       100
                  ....*....|....*....|
gi 1561760624 255 VDDDHCDGAYYNVHTREKCG 274
Cdd:cd11673    95 GDNDRCKGHIVREASGDVCA 114
Eryth_link_C pfam16915
Annelid erythrocruorin linker subunit C-terminus; This domain is found in linker subunits of ...
 158-274 9.33e-18

Annelid erythrocruorin linker subunit C-terminus; This domain is found in linker subunits of the erythrocruorin respiratory complex in annelid worms.


Pssm-ID: 319001  Cd Length: 120  Bit Score: 77.39  E-value: 9.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561760624 158 PPQSGVRFEAHVTPHdaGCAKRRISEFQVTIRKVVTNEYIASRPRIEASILATSQAGGRSSQEYFTVKGDWDSSHQTLVL 237
Cdd:pfam16915   1 PTPAGSSFIGDLNWD--HCTKRRPKHMDIHITSVKRSSFFPSRPWVKATVDLESHQDGHEQTSTLPVDGFYNFGSRRLIL 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1561760624 238 RPPEEsDPVGLICEFDGVDDDHCDGAYYNVHTREKCG 274
Cdd:pfam16915  79 LPPEG-DGLGLVCSFDGGDDDRCKGHIVRESSLDVCA 114
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 117-152 2.85e-05

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 40.27  E-value: 2.85e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1561760624 117 CSDSEhFACedGSGRCISRLLVCDKIKDCNNGADED 152
Cdd:cd00112     1 CPPNE-FRC--ANGRCIPSSWVCDGEDDCGDGSDEE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 117-151 4.92e-05

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 39.54  E-value: 4.92e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1561760624  117 CSDSEHFACedGSGRCISRLLVCDKIKDCNNGADE 151
Cdd:smart00192   1 TCPPGEFQC--DNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
116-151 2.48e-03

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 34.92  E-value: 2.48e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1561760624 116 QCSDSEhFACedGSGRCISRLLVCDKIKDCNNGADE 151
Cdd:pfam00057   2 TCSPNE-FQC--GSGECIPRSWVCDGDPDCGDGSDE 34
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH