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Conserved domains on  [gi|296278246|ref|NP_001171710|]
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integral membrane protein DGCR2/IDD isoform 4 precursor [Homo sapiens]

Protein Classification

LDLa and CLECT_DGCR2_like domain-containing protein( domain architecture ID 10060062)

protein containing domains LDLa, CLECT_DGCR2_like, VWC, and PHA03247

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CLECT_DGCR2_like cd03599
C-type lectin-like domain (CTLD) of the type found in DGCR2, an integral membrane protein ...
 112-264 1.83e-113

C-type lectin-like domain (CTLD) of the type found in DGCR2, an integral membrane protein deleted in DiGeorge Syndrome (DGS); CLECT_DGCR2_like: C-type lectin-like domain (CTLD) of the type found in DGCR2, an integral membrane protein deleted in DiGeorge Syndrome (DGS). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DGS is also known velo-cardio-facial syndrome (VCFS). DGS is a genetic abnormality that results in malformations of the heart, face, and limbs and is associated with schizophrenia and depressive disorders. DGCR2 is a candidate for involvement in the pathogenesis of DGS since the DGCR2 gene lies within the minimal DGS critical region (MDGRC) of 22q11, which when deleted gives rise to DGS, and the DGCR2 gene is in close proximity to the balanced translocation breakpoint in a DGS patient having a balanced translocation.


:

Pssm-ID: 153069  Cd Length: 153  Bit Score: 333.42  E-value: 1.83e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278246 112 CPTGWHHYEGTASCYRVYLSGENYWDAAQTCQRLNGSLATFSTDQELRFVLAQEWDQPERSFGWKDQRKLWVGYQYVITG 191
Cdd:cd03599    1 CPSGWHHYEGTASCYKVYLSGENYWDAVQTCQKVNGSLATFTTDQELQFILAQEWDFDERVFGRKDQCKFWVGYQYVITN 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296278246 192 RNRSLEGRWEVAFKGSSEVFLPPDPIFASAMSENDNVFCAQLQCFHFPTLRHHDLHSWHAESCYEKSSFLCKR 264
Cdd:cd03599   81 RNHSLEGRWEVAYKGSMEVFLPPEPIFATGMSTNDNVFCAQLQCFQIPSLRERGLHSWHAENCYEKSSFLCKR 153
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 30-66 1.94e-09

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: 52.98  E-value: 1.94e-09
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 296278246  30 CNPGQFACRSGtiQCIPLPWQCDGWATCEDESDEANC 66
Cdd:cd00112    1 CPPNEFRCANG--RCIPSSWVCDGEDDCGDGSDEENC 35
VWC smart00214
von Willebrand factor (vWF) type C domain;
268-326 5.53e-09

von Willebrand factor (vWF) type C domain;


:

Pssm-ID: 214564  Cd Length: 59  Bit Score: 52.52  E-value: 5.53e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296278246   268 CVDIKDNVVDEGFYFtpkgDDPCLSCTCHGGEPEMCVAALCERPQGCQQYR--KDPKECCK 326
Cdd:smart00214   1 CVHNGRVYNDGETWK----PDPCQICTCLDGTTVLCDPVECPPPPDCPNPErvKPPGECCP 57
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 425-534 6.85e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.54  E-value: 6.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278246  425 DPPPPYTAYKYPDIGQPDDPPPPYEAS-------IHPDSVFYDPADDDAFEPVEVSLP----APGDGGSEGALLRRLEQP 493
Cdd:PHA03247 2607 DPRGPAPPSPLPPDTHAPDPPPPSPSPaanepdpHPPPTVPPPERPRDDPAPGRVSRPrrarRLGRAAQASSPPQRPRRR 2686

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 296278246  494 -LPTAGASLADLEDSADSSSallvPPDPAQSGSTPAAEALPG 534
Cdd:PHA03247 2687 aARPTVGSLTSLADPPPPPP----TPEPAPHALVSATPLPPG 2724
 
Name Accession Description Interval E-value
CLECT_DGCR2_like cd03599
C-type lectin-like domain (CTLD) of the type found in DGCR2, an integral membrane protein ...
 112-264 1.83e-113

C-type lectin-like domain (CTLD) of the type found in DGCR2, an integral membrane protein deleted in DiGeorge Syndrome (DGS); CLECT_DGCR2_like: C-type lectin-like domain (CTLD) of the type found in DGCR2, an integral membrane protein deleted in DiGeorge Syndrome (DGS). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DGS is also known velo-cardio-facial syndrome (VCFS). DGS is a genetic abnormality that results in malformations of the heart, face, and limbs and is associated with schizophrenia and depressive disorders. DGCR2 is a candidate for involvement in the pathogenesis of DGS since the DGCR2 gene lies within the minimal DGS critical region (MDGRC) of 22q11, which when deleted gives rise to DGS, and the DGCR2 gene is in close proximity to the balanced translocation breakpoint in a DGS patient having a balanced translocation.


Pssm-ID: 153069  Cd Length: 153  Bit Score: 333.42  E-value: 1.83e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278246 112 CPTGWHHYEGTASCYRVYLSGENYWDAAQTCQRLNGSLATFSTDQELRFVLAQEWDQPERSFGWKDQRKLWVGYQYVITG 191
Cdd:cd03599    1 CPSGWHHYEGTASCYKVYLSGENYWDAVQTCQKVNGSLATFTTDQELQFILAQEWDFDERVFGRKDQCKFWVGYQYVITN 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296278246 192 RNRSLEGRWEVAFKGSSEVFLPPDPIFASAMSENDNVFCAQLQCFHFPTLRHHDLHSWHAESCYEKSSFLCKR 264
Cdd:cd03599   81 RNHSLEGRWEVAYKGSMEVFLPPEPIFATGMSTNDNVFCAQLQCFQIPSLRERGLHSWHAENCYEKSSFLCKR 153
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 112-263 2.68e-14

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 69.55  E-value: 2.68e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278246   112 CPTGWHHYEGtaSCYRVYLSGENYWDAAQTCQRLNGSLATFSTDQELRFVLAQEWDQPERSFgwkdqrkLWVGYQYvitg 191
Cdd:smart00034   1 CPSGWISYGG--KCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDY-------YWIGLSD---- 67

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296278246   192 RNRSLEGRWEVafkGSSEV-FLPPDPIFASAMSENdnvfCAQLqcfhfptlrHHDLHSWHAESCYEKSSFLCK 263
Cdd:smart00034  68 PDSNGSWQWSD---GSGPVsYSNWAPGEPNNSSGD----CVVL---------STSGGKWNDVSCTSKLPFVCE 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 133-264 1.72e-13

Lectin C-type domain; This family includes both long and short form C-type


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 66.73  E-value: 1.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278246  133 ENYWDAAQTCQRLNGSLATFSTDQELRFVLAQEWDQPErsfgwkdqrKLWVGYQYvitgRNRSLEGRWEVAFKGSSEVFL 212
Cdd:pfam00059   2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNK---------YFWIGLTD----RKNEGTWKWVDGSPVNYTNWA 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 296278246  213 PPDPifasamSENDNVFCAQLqcfhfptlrHHDLHSWHAESCYEKSSFLCKR 264
Cdd:pfam00059  69 PEPN------NNGENEDCVEL---------SSSSGKWNDENCNSKNPFVCEK 105
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 30-66 1.94e-09

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: 52.98  E-value: 1.94e-09
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 296278246  30 CNPGQFACRSGtiQCIPLPWQCDGWATCEDESDEANC 66
Cdd:cd00112    1 CPPNEFRCANG--RCIPSSWVCDGEDDCGDGSDEENC 35
VWC smart00214
von Willebrand factor (vWF) type C domain;
268-326 5.53e-09

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 52.52  E-value: 5.53e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296278246   268 CVDIKDNVVDEGFYFtpkgDDPCLSCTCHGGEPEMCVAALCERPQGCQQYR--KDPKECCK 326
Cdd:smart00214   1 CVHNGRVYNDGETWK----PDPCQICTCLDGTTVLCDPVECPPPPDCPNPErvKPPGECCP 57
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 29-63 1.91e-08

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: 49.94  E-value: 1.91e-08
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 296278246    29 RCNPGQFACRSGtiQCIPLPWQCDGWATCEDESDE 63
Cdd:smart00192   1 TCPPGEFQCDNG--RCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
29-66 1.02e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 48.01  E-value: 1.02e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 296278246   29 RCNPGQFACRSGtiQCIPLPWQCDGWATCEDESDEANC 66
Cdd:pfam00057   2 TCSPNEFQCGSG--ECIPRSWVCDGDPDCGDGSDEENC 37
PHA03247 PHA03247
large tegument protein UL36; Provisional
 425-534 6.85e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.54  E-value: 6.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278246  425 DPPPPYTAYKYPDIGQPDDPPPPYEAS-------IHPDSVFYDPADDDAFEPVEVSLP----APGDGGSEGALLRRLEQP 493
Cdd:PHA03247 2607 DPRGPAPPSPLPPDTHAPDPPPPSPSPaanepdpHPPPTVPPPERPRDDPAPGRVSRPrrarRLGRAAQASSPPQRPRRR 2686

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 296278246  494 -LPTAGASLADLEDSADSSSallvPPDPAQSGSTPAAEALPG 534
Cdd:PHA03247 2687 aARPTVGSLTSLADPPPPPP----TPEPAPHALVSATPLPPG 2724
 
Name Accession Description Interval E-value
CLECT_DGCR2_like cd03599
C-type lectin-like domain (CTLD) of the type found in DGCR2, an integral membrane protein ...
 112-264 1.83e-113

C-type lectin-like domain (CTLD) of the type found in DGCR2, an integral membrane protein deleted in DiGeorge Syndrome (DGS); CLECT_DGCR2_like: C-type lectin-like domain (CTLD) of the type found in DGCR2, an integral membrane protein deleted in DiGeorge Syndrome (DGS). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DGS is also known velo-cardio-facial syndrome (VCFS). DGS is a genetic abnormality that results in malformations of the heart, face, and limbs and is associated with schizophrenia and depressive disorders. DGCR2 is a candidate for involvement in the pathogenesis of DGS since the DGCR2 gene lies within the minimal DGS critical region (MDGRC) of 22q11, which when deleted gives rise to DGS, and the DGCR2 gene is in close proximity to the balanced translocation breakpoint in a DGS patient having a balanced translocation.


Pssm-ID: 153069  Cd Length: 153  Bit Score: 333.42  E-value: 1.83e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278246 112 CPTGWHHYEGTASCYRVYLSGENYWDAAQTCQRLNGSLATFSTDQELRFVLAQEWDQPERSFGWKDQRKLWVGYQYVITG 191
Cdd:cd03599    1 CPSGWHHYEGTASCYKVYLSGENYWDAVQTCQKVNGSLATFTTDQELQFILAQEWDFDERVFGRKDQCKFWVGYQYVITN 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296278246 192 RNRSLEGRWEVAFKGSSEVFLPPDPIFASAMSENDNVFCAQLQCFHFPTLRHHDLHSWHAESCYEKSSFLCKR 264
Cdd:cd03599   81 RNHSLEGRWEVAYKGSMEVFLPPEPIFATGMSTNDNVFCAQLQCFQIPSLRERGLHSWHAENCYEKSSFLCKR 153
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 112-263 2.68e-14

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 69.55  E-value: 2.68e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278246   112 CPTGWHHYEGtaSCYRVYLSGENYWDAAQTCQRLNGSLATFSTDQELRFVLAQEWDQPERSFgwkdqrkLWVGYQYvitg 191
Cdd:smart00034   1 CPSGWISYGG--KCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDY-------YWIGLSD---- 67

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296278246   192 RNRSLEGRWEVafkGSSEV-FLPPDPIFASAMSENdnvfCAQLqcfhfptlrHHDLHSWHAESCYEKSSFLCK 263
Cdd:smart00034  68 PDSNGSWQWSD---GSGPVsYSNWAPGEPNNSSGD----CVVL---------STSGGKWNDVSCTSKLPFVCE 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 133-264 1.72e-13

Lectin C-type domain; This family includes both long and short form C-type


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 66.73  E-value: 1.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278246  133 ENYWDAAQTCQRLNGSLATFSTDQELRFVLAQEWDQPErsfgwkdqrKLWVGYQYvitgRNRSLEGRWEVAFKGSSEVFL 212
Cdd:pfam00059   2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNK---------YFWIGLTD----RKNEGTWKWVDGSPVNYTNWA 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 296278246  213 PPDPifasamSENDNVFCAQLqcfhfptlrHHDLHSWHAESCYEKSSFLCKR 264
Cdd:pfam00059  69 PEPN------NNGENEDCVEL---------SSSSGKWNDENCNSKNPFVCEK 105
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 124-264 7.75e-13

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 65.33  E-value: 7.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278246 124 SCYRVYLSGENYWDAAQTCQRLNGSLATFSTDQELRFVLAQEWDQPERSFgwkdqrklWVGyqyvitGRNRSLEGRWEVA 203
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDV--------WIG------LNDLSSEGTWKWS 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296278246 204 FKGSSEVFLPPDPIFASAMSENDnvfCAQlqcfhfptLRHHDLHSWHAESCYEKSSFLCKR 264
Cdd:cd00037   67 DGSPLVDYTNWAPGEPNPGGSED---CVV--------LSSSSDGKWNDVSCSSKLPFICEK 116
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 30-66 1.94e-09

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: 52.98  E-value: 1.94e-09
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 296278246  30 CNPGQFACRSGtiQCIPLPWQCDGWATCEDESDEANC 66
Cdd:cd00112    1 CPPNEFRCANG--RCIPSSWVCDGEDDCGDGSDEENC 35
VWC smart00214
von Willebrand factor (vWF) type C domain;
268-326 5.53e-09

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 52.52  E-value: 5.53e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296278246   268 CVDIKDNVVDEGFYFtpkgDDPCLSCTCHGGEPEMCVAALCERPQGCQQYR--KDPKECCK 326
Cdd:smart00214   1 CVHNGRVYNDGETWK----PDPCQICTCLDGTTVLCDPVECPPPPDCPNPErvKPPGECCP 57
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 29-63 1.91e-08

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: 49.94  E-value: 1.91e-08
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 296278246    29 RCNPGQFACRSGtiQCIPLPWQCDGWATCEDESDE 63
Cdd:smart00192   1 TCPPGEFQCDNG--RCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
29-66 1.02e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 48.01  E-value: 1.02e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 296278246   29 RCNPGQFACRSGtiQCIPLPWQCDGWATCEDESDEANC 66
Cdd:pfam00057   2 TCSPNEFQCGSG--ECIPRSWVCDGDPDCGDGSDEENC 37
CLECT_attractin_like cd03597
C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and ...
 112-234 3.04e-07

C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and attractin-like protein (ALP); CLECT_attractin_like: C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and attractin-like protein (ALP). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Mouse AtrN (the product of the mahogany gene) has been shown to bind Agouti protein and to function in agouti-induced pigmentation and obesity. Mutations in AtrN have also been shown to cause spongiform encephalopathy and hypomyelination in rats and hamsters. The cytoplasmic region of mouse ALP has been shown to binds to melanocortin receptor (MCR4). Signaling through MCR4 plays a role in appetite suppression. Attractin may have therapeutic potential in the treatment of obesity. Human attractin (hAtrN) has been shown to be expressed on activated T cells and released extracellularly. The circulating serum attractin induces the spreading of monocytes that become the focus of the clustering of non-proliferating T cells.


Pssm-ID: 153067  Cd Length: 129  Bit Score: 49.50  E-value: 3.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278246 112 CPTGWHHYegTASCYRVYLSGENYWDAAQTCQRLNGSLATFSTDQELRFVLaqewDQPERSFGWKDQRKLWVGYQYVitg 191
Cdd:cd03597    1 CGEGWHLV--GNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVL----KELQKHQMTKQKLTPWVGLRKI--- 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 296278246 192 rNRSLEGrWE--VAFKGSSEVFLPPDPifasamseNDNVFCAQLQ 234
Cdd:cd03597   72 -NVSYWC-WEdmSPFTNTTLQWLPGEP--------SDAGFCGYLE 106
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 112-264 7.74e-04

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.


Pssm-ID: 153063  Cd Length: 116  Bit Score: 39.24  E-value: 7.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278246 112 CPTGWHHYEGtaSCYrvYLS-GENYW-DAAQTCQRLNGSLATFSTDQELRFVLAQewdqpersfgwKDQRKLWVGYQYVI 189
Cdd:cd03593    1 CPKDWICYGN--KCY--YFSmEKKTWnESKEACSSKNSSLLKIDDEEELEFLQSQ-----------IGSSSYWIGLSREK 65

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296278246 190 TGRnrslEGRWEvafKGSsevflPPDPIFASAMSENDNvFCAQlqcfhfptlrhhdLHSW--HAESCYEKSSFLCKR 264
Cdd:cd03593   66 SEK----PWKWI---DGS-----PLNNLFNIRGSTKSG-NCAY-------------LSSTgiYSEDCSTKKRWICEK 116
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 112-191 1.21e-03

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.


Pssm-ID: 153060 [Multi-domain]  Cd Length: 126  Bit Score: 39.21  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278246 112 CPTGWHHYEGtaSCYRVYLSGENYWDAAQTCQRLNGSLATFSTDQELRFV--LAQEWD---------QPERSFGWKDQRK 180
Cdd:cd03590    1 CPTNWKSFQS--SCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFIskILSGNRsywiglsdeETEGEWKWVDGTP 78

                         90
                 ....*....|.
gi 296278246 181 LWVGYQYVITG 191
Cdd:cd03590   79 LNSSKTFWHPG 89
PHA03247 PHA03247
large tegument protein UL36; Provisional
 425-534 6.85e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.54  E-value: 6.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278246  425 DPPPPYTAYKYPDIGQPDDPPPPYEAS-------IHPDSVFYDPADDDAFEPVEVSLP----APGDGGSEGALLRRLEQP 493
Cdd:PHA03247 2607 DPRGPAPPSPLPPDTHAPDPPPPSPSPaanepdpHPPPTVPPPERPRDDPAPGRVSRPrrarRLGRAAQASSPPQRPRRR 2686

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 296278246  494 -LPTAGASLADLEDSADSSSallvPPDPAQSGSTPAAEALPG 534
Cdd:PHA03247 2687 aARPTVGSLTSLADPPPPPP----TPEPAPHALVSATPLPPG 2724
 
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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