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Conserved domains on  [gi|2024341832|ref|XP_004937824|]
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transmembrane protease serine 6 isoform X3 [Gallus gallus]

Protein Classification

neuropilin and tolloid-like protein; serine protease( domain architecture ID 10475862)

neuropilin and tolloid-like protein is a CUB and LDLa (low-density lipoprotein receptor class A) domain-containing protein similar to Homo sapiens neuropilin and tolloid-like protein 1 involved in the development and/or maintenance of neuronal circuitry| trypsin-like serine protease catalyzes the cleavage of specific peptide bonds in protein substrates using an active site serine as the nucleophile; contains C-terminal DNA polymerase III subunits gamma and tau

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
553-785 2.81e-100

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


:

Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 309.59  E-value: 2.81e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024341832 553 IIGGANSVEGEWPWQASLQVR-GRHICGGTLIADRWVVSAAHCFQDerlASPSVWTIYLGKYFQNTTSHTEVSFKVIRLF 631
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS---SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024341832 632 LHPYYEEDSHDYDVALLQLDHPVIISPFIQPICLPATSHLFEPGLHCWITGWGALKEGGHISNILQKVDVQIIQQDICSE 711
Cdd:cd00190    78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024341832 712 AYHY--MISPRMLCAGYNKGKKDACQGDSGGPLACEEPsGRWFLAGLVSWGMGCGLPNYYGVYTRITQVLGWMNQT 785
Cdd:cd00190   158 AYSYggTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
62-158 3.46e-12

SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed function of regulating or binding carbohydrate side chains. Recently a proteolytic activity has been shown for a SEA domain.


:

Pssm-ID: 460188  Cd Length: 100  Bit Score: 63.03  E-value: 3.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024341832  62 HFYSGSLQVLNRRYFSELGQVESRAFWLESAKLQNMLKDLIHSTELGRYYNSSTVYAF--GEGALTFFFWFTLQIPESQQ 139
Cdd:pfam01390   1 QYYTGSFKITNLQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLrpDGGSVVVDVVLVFRFPSTEP 80
                          90
                  ....*....|....*....
gi 2024341832 140 KEMTAERVNAVLHQELTTS 158
Cdd:pfam01390  81 ALDREKLIEEILRQTLNNT 99
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
311-426 2.90e-09

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


:

Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 55.50  E-value: 2.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024341832 311 CGVNITLREglelQGKISTPHYPSYYSPNTQCTWHMSVPSlDYGVTLWFDAYALSRQKQ---------DLPCTQGQWIiq 381
Cdd:cd00041     1 CGGTLTAST----SGTISSPNYPNNYPNNLNCVWTIEAPP-GYRIRLTFEDFDLESSPNcsydyleiyDGPSTSSPLL-- 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2024341832 382 nRRLCGLRTLQAYaeripVTSSADIAITFTSQISLTGPGVQAAYS 426
Cdd:cd00041    74 -GRFCGSTLPPPI-----ISSGNSLTVRFRSDSSVTGRGFKATYS 112
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
468-501 4.61e-07

Low-density lipoprotein receptor domain class A;


:

Pssm-ID: 395011  Cd Length: 37  Bit Score: 46.86  E-value: 4.61e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2024341832 468 PAKFQCQeDSTCIEFSRVCNQQRDCVNGSDEEQC 501
Cdd:pfam00057   5 PNEFQCG-SGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
435-465 6.19e-06

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: 43.35  E-value: 6.19e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2024341832 435 PREFLCSvNGLCVPA---CDGIKDCPNGLDERNC 465
Cdd:cd00112     3 PNEFRCA-NGRCIPSswvCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
507-542 1.12e-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: 42.58  E-value: 1.12e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2024341832 507 CSPFTHRCDDGTCVKKpNPLCDATVDCKDLSDEKHC 542
Cdd:cd00112     1 CPPNEFRCANGRCIPS-SWVCDGEDDCGDGSDEENC 35
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
553-785 2.81e-100

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 309.59  E-value: 2.81e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024341832 553 IIGGANSVEGEWPWQASLQVR-GRHICGGTLIADRWVVSAAHCFQDerlASPSVWTIYLGKYFQNTTSHTEVSFKVIRLF 631
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS---SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024341832 632 LHPYYEEDSHDYDVALLQLDHPVIISPFIQPICLPATSHLFEPGLHCWITGWGALKEGGHISNILQKVDVQIIQQDICSE 711
Cdd:cd00190    78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024341832 712 AYHY--MISPRMLCAGYNKGKKDACQGDSGGPLACEEPsGRWFLAGLVSWGMGCGLPNYYGVYTRITQVLGWMNQT 785
Cdd:cd00190   158 AYSYggTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
552-781 2.54e-94

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 293.82  E-value: 2.54e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024341832  552 RIIGGANSVEGEWPWQASLQVRG-RHICGGTLIADRWVVSAAHCFQDerlASPSVWTIYLGKYFQNTTSHTEVsFKVIRL 630
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRG---SDPSNIRVRLGSHDLSSGEEGQV-IKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024341832  631 FLHPYYEEDSHDYDVALLQLDHPVIISPFIQPICLPATSHLFEPGLHCWITGWGALKEG-GHISNILQKVDVQIIQQDIC 709
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024341832  710 SEAYHYM--ISPRMLCAGYNKGKKDACQGDSGGPLACEepSGRWFLAGLVSWGMGCGLPNYYGVYTRITQVLGW 781
Cdd:smart00020 157 RRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228
Trypsin pfam00089
Trypsin;
553-782 6.28e-77

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 247.74  E-value: 6.28e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024341832 553 IIGGANSVEGEWPWQASLQVR-GRHICGGTLIADRWVVSAAHCFqderlASPSVWTIYLGKYFQNTTSHTEVSFKVIRLF 631
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCV-----SGASDVKVVLGAHNIVLREGGEQKFDVEKII 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024341832 632 LHPYYEEDSHDYDVALLQLDHPVIISPFIQPICLPATSHLFEPGLHCWITGWGALKEGGHiSNILQKVDVQIIQQDICSE 711
Cdd:pfam00089  76 VHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024341832 712 AYHYMISPRMLCAGYnkGKKDACQGDSGGPLACEEPsgrwFLAGLVSWGMGCGLPNYYGVYTRITQVLGWM 782
Cdd:pfam00089 155 AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
544-786 2.85e-73

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 239.55  E-value: 2.85e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024341832 544 CGLQAPLSRIIGGANSVEGEWPWQASLQVRG---RHICGGTLIADRWVVSAAHCFQDErlaSPSVWTIYLGKYFQNTTSH 620
Cdd:COG5640    22 APAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGD---GPSDLRVVIGSTDLSTSGG 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024341832 621 TEVsfKVIRLFLHPYYEEDSHDYDVALLQLDHPViisPFIQPICLPATSHLFEPGLHCWITGWGALKEG-GHISNILQKV 699
Cdd:COG5640    99 TVV--KVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTLRKA 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024341832 700 DVQIIQQDICSeAYHYMISPRMLCAGYNKGKKDACQGDSGGPLAcEEPSGRWFLAGLVSWGMGCGLPNYYGVYTRITQVL 779
Cdd:COG5640   174 DVPVVSDATCA-AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYR 251

                  ....*..
gi 2024341832 780 GWMNQTM 786
Cdd:COG5640   252 DWIKSTA 258
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
62-158 3.46e-12

SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed function of regulating or binding carbohydrate side chains. Recently a proteolytic activity has been shown for a SEA domain.


Pssm-ID: 460188  Cd Length: 100  Bit Score: 63.03  E-value: 3.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024341832  62 HFYSGSLQVLNRRYFSELGQVESRAFWLESAKLQNMLKDLIHSTELGRYYNSSTVYAF--GEGALTFFFWFTLQIPESQQ 139
Cdd:pfam01390   1 QYYTGSFKITNLQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLrpDGGSVVVDVVLVFRFPSTEP 80
                          90
                  ....*....|....*....
gi 2024341832 140 KEMTAERVNAVLHQELTTS 158
Cdd:pfam01390  81 ALDREKLIEEILRQTLNNT 99
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
311-426 2.90e-09

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 55.50  E-value: 2.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024341832 311 CGVNITLREglelQGKISTPHYPSYYSPNTQCTWHMSVPSlDYGVTLWFDAYALSRQKQ---------DLPCTQGQWIiq 381
Cdd:cd00041     1 CGGTLTAST----SGTISSPNYPNNYPNNLNCVWTIEAPP-GYRIRLTFEDFDLESSPNcsydyleiyDGPSTSSPLL-- 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2024341832 382 nRRLCGLRTLQAYaeripVTSSADIAITFTSQISLTGPGVQAAYS 426
Cdd:cd00041    74 -GRFCGSTLPPPI-----ISSGNSLTVRFRSDSSVTGRGFKATYS 112
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
468-501 4.61e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 46.86  E-value: 4.61e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2024341832 468 PAKFQCQeDSTCIEFSRVCNQQRDCVNGSDEEQC 501
Cdd:pfam00057   5 PNEFQCG-SGECIPRSWVCDGDPDCGDGSDEENC 37
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
325-425 2.89e-06

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 46.61  E-value: 2.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024341832  325 GKISTPHYPSYYSPNTQCTWHMSVPSlDYGVTLWFDAYALSRQKQ---------DLPCTQGQWIiqnRRLCGLRTLqaya 395
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPP-GYRIELQFTDFDLESSDNceydyveiyDGPSASSPLL---GRFCGSEAP---- 72
                           90       100       110
                   ....*....|....*....|....*....|
gi 2024341832  396 ERIPVTSSADIAITFTSQISLTGPGVQAAY 425
Cdd:smart00042  73 PPVISSSSNSLTLTFVSDSSVQKRGFSARY 102
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
435-465 6.19e-06

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: 43.35  E-value: 6.19e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2024341832 435 PREFLCSvNGLCVPA---CDGIKDCPNGLDERNC 465
Cdd:cd00112     3 PNEFRCA-NGRCIPSswvCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
507-542 1.12e-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: 42.58  E-value: 1.12e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2024341832 507 CSPFTHRCDDGTCVKKpNPLCDATVDCKDLSDEKHC 542
Cdd:cd00112     1 CPPNEFRCANGRCIPS-SWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
467-501 1.82e-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: 42.19  E-value: 1.82e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2024341832 467 CPA-KFQCQeDSTCIEFSRVCNQQRDCVNGSDEEQC 501
Cdd:cd00112     1 CPPnEFRCA-NGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
505-542 3.01e-05

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 41.47  E-value: 3.01e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2024341832 505 VPCSPFTHRCDDGTCVKKpNPLCDATVDCKDLSDEKHC 542
Cdd:pfam00057   1 STCSPNEFQCGSGECIPR-SWVCDGDPDCGDGSDEENC 37
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
467-498 4.16e-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: 41.08  E-value: 4.16e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2024341832  467 CPA-KFQCQeDSTCIEFSRVCNQQRDCVNGSDE 498
Cdd:smart00192   2 CPPgEFQCD-NGRCIPSSWVCDGVDDCGDGSDE 33
CUB pfam00431
CUB domain;
311-367 5.99e-05

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 43.05  E-value: 5.99e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024341832 311 CGVNITlreglELQGKISTPHYPSYYSPNTQCTWHMSVPSlDYGVTLWFDAYALSRQ 367
Cdd:pfam00431   1 CGGVLT-----DSSGSISSPNYPNPYPPNKDCVWLIRAPP-GFRVKLTFQDFELEDH 51
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
507-539 3.68e-04

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: 38.38  E-value: 3.68e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2024341832  507 CSPFTHRCDDGTCVKKPNpLCDATVDCKDLSDE 539
Cdd:smart00192   2 CPPGEFQCDNGRCIPSSW-VCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
435-462 4.27e-04

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: 38.38  E-value: 4.27e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2024341832  435 PREFLCSvNGLCVPA---CDGIKDCPNGLDE 462
Cdd:smart00192   4 PGEFQCD-NGRCIPSswvCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
435-465 3.88e-03

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 35.69  E-value: 3.88e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2024341832 435 PREFLCSvNGLCVP---ACDGIKDCPNGLDERNC 465
Cdd:pfam00057   5 PNEFQCG-SGECIPrswVCDGDPDCGDGSDEENC 37
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
553-785 2.81e-100

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 309.59  E-value: 2.81e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024341832 553 IIGGANSVEGEWPWQASLQVR-GRHICGGTLIADRWVVSAAHCFQDerlASPSVWTIYLGKYFQNTTSHTEVSFKVIRLF 631
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS---SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024341832 632 LHPYYEEDSHDYDVALLQLDHPVIISPFIQPICLPATSHLFEPGLHCWITGWGALKEGGHISNILQKVDVQIIQQDICSE 711
Cdd:cd00190    78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024341832 712 AYHY--MISPRMLCAGYNKGKKDACQGDSGGPLACEEPsGRWFLAGLVSWGMGCGLPNYYGVYTRITQVLGWMNQT 785
Cdd:cd00190   158 AYSYggTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
552-781 2.54e-94

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 293.82  E-value: 2.54e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024341832  552 RIIGGANSVEGEWPWQASLQVRG-RHICGGTLIADRWVVSAAHCFQDerlASPSVWTIYLGKYFQNTTSHTEVsFKVIRL 630
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRG---SDPSNIRVRLGSHDLSSGEEGQV-IKVSKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024341832  631 FLHPYYEEDSHDYDVALLQLDHPVIISPFIQPICLPATSHLFEPGLHCWITGWGALKEG-GHISNILQKVDVQIIQQDIC 709
Cdd:smart00020  77 IIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATC 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024341832  710 SEAYHYM--ISPRMLCAGYNKGKKDACQGDSGGPLACEepSGRWFLAGLVSWGMGCGLPNYYGVYTRITQVLGW 781
Cdd:smart00020 157 RRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228
Trypsin pfam00089
Trypsin;
553-782 6.28e-77

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 247.74  E-value: 6.28e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024341832 553 IIGGANSVEGEWPWQASLQVR-GRHICGGTLIADRWVVSAAHCFqderlASPSVWTIYLGKYFQNTTSHTEVSFKVIRLF 631
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCV-----SGASDVKVVLGAHNIVLREGGEQKFDVEKII 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024341832 632 LHPYYEEDSHDYDVALLQLDHPVIISPFIQPICLPATSHLFEPGLHCWITGWGALKEGGHiSNILQKVDVQIIQQDICSE 711
Cdd:pfam00089  76 VHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024341832 712 AYHYMISPRMLCAGYnkGKKDACQGDSGGPLACEEPsgrwFLAGLVSWGMGCGLPNYYGVYTRITQVLGWM 782
Cdd:pfam00089 155 AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
544-786 2.85e-73

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 239.55  E-value: 2.85e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024341832 544 CGLQAPLSRIIGGANSVEGEWPWQASLQVRG---RHICGGTLIADRWVVSAAHCFQDErlaSPSVWTIYLGKYFQNTTSH 620
Cdd:COG5640    22 APAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGD---GPSDLRVVIGSTDLSTSGG 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024341832 621 TEVsfKVIRLFLHPYYEEDSHDYDVALLQLDHPViisPFIQPICLPATSHLFEPGLHCWITGWGALKEG-GHISNILQKV 699
Cdd:COG5640    99 TVV--KVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTLRKA 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024341832 700 DVQIIQQDICSeAYHYMISPRMLCAGYNKGKKDACQGDSGGPLAcEEPSGRWFLAGLVSWGMGCGLPNYYGVYTRITQVL 779
Cdd:COG5640   174 DVPVVSDATCA-AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYR 251

                  ....*..
gi 2024341832 780 GWMNQTM 786
Cdd:COG5640   252 DWIKSTA 258
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
573-772 3.41e-13

V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 68.93  E-value: 3.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024341832 573 RGRHICGGTLIADRWVVSAAHCFQD-ERLASPSVWTIYLGkyFQNTtshTEVSFKVIRLFLHPYYEEDSH-DYDVALLQL 650
Cdd:COG3591     9 GGGGVCTGTLIGPNLVLTAGHCVYDgAGGGWATNIVFVPG--YNGG---PYGTATATRFRVPPGWVASGDaGYDYALLRL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024341832 651 DHPVIISPFIQPIclpATSHLFEPGLHCWITGWGalkeGGHISNILQKVDVQIIQQDicSEAYHYMIsprmlcagynkgk 730
Cdd:COG3591    84 DEPLGDTTGWLGL---AFNDAPLAGEPVTIIGYP----GDRPKDLSLDCSGRVTGVQ--GNRLSYDC------------- 141
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2024341832 731 kDACQGDSGGPLACEEpSGRWFLAGLVSWGmGCGLPNyYGVY 772
Cdd:COG3591   142 -DTTGGSSGSPVLDDS-DGGGRVVGVHSAG-GADRAN-TGVR 179
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
62-158 3.46e-12

SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed function of regulating or binding carbohydrate side chains. Recently a proteolytic activity has been shown for a SEA domain.


Pssm-ID: 460188  Cd Length: 100  Bit Score: 63.03  E-value: 3.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024341832  62 HFYSGSLQVLNRRYFSELGQVESRAFWLESAKLQNMLKDLIHSTELGRYYNSSTVYAF--GEGALTFFFWFTLQIPESQQ 139
Cdd:pfam01390   1 QYYTGSFKITNLQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLrpDGGSVVVDVVLVFRFPSTEP 80
                          90
                  ....*....|....*....
gi 2024341832 140 KEMTAERVNAVLHQELTTS 158
Cdd:pfam01390  81 ALDREKLIEEILRQTLNNT 99
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
311-426 2.90e-09

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 55.50  E-value: 2.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024341832 311 CGVNITLREglelQGKISTPHYPSYYSPNTQCTWHMSVPSlDYGVTLWFDAYALSRQKQ---------DLPCTQGQWIiq 381
Cdd:cd00041     1 CGGTLTAST----SGTISSPNYPNNYPNNLNCVWTIEAPP-GYRIRLTFEDFDLESSPNcsydyleiyDGPSTSSPLL-- 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2024341832 382 nRRLCGLRTLQAYaeripVTSSADIAITFTSQISLTGPGVQAAYS 426
Cdd:cd00041    74 -GRFCGSTLPPPI-----ISSGNSLTVRFRSDSSVTGRGFKATYS 112
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
468-501 4.61e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 46.86  E-value: 4.61e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2024341832 468 PAKFQCQeDSTCIEFSRVCNQQRDCVNGSDEEQC 501
Cdd:pfam00057   5 PNEFQCG-SGECIPRSWVCDGDPDCGDGSDEENC 37
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
325-425 2.89e-06

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 46.61  E-value: 2.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024341832  325 GKISTPHYPSYYSPNTQCTWHMSVPSlDYGVTLWFDAYALSRQKQ---------DLPCTQGQWIiqnRRLCGLRTLqaya 395
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPP-GYRIELQFTDFDLESSDNceydyveiyDGPSASSPLL---GRFCGSEAP---- 72
                           90       100       110
                   ....*....|....*....|....*....|
gi 2024341832  396 ERIPVTSSADIAITFTSQISLTGPGVQAAY 425
Cdd:smart00042  73 PPVISSSSNSLTLTFVSDSSVQKRGFSARY 102
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
435-465 6.19e-06

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: 43.35  E-value: 6.19e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2024341832 435 PREFLCSvNGLCVPA---CDGIKDCPNGLDERNC 465
Cdd:cd00112     3 PNEFRCA-NGRCIPSswvCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
507-542 1.12e-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: 42.58  E-value: 1.12e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2024341832 507 CSPFTHRCDDGTCVKKpNPLCDATVDCKDLSDEKHC 542
Cdd:cd00112     1 CPPNEFRCANGRCIPS-SWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
467-501 1.82e-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: 42.19  E-value: 1.82e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2024341832 467 CPA-KFQCQeDSTCIEFSRVCNQQRDCVNGSDEEQC 501
Cdd:cd00112     1 CPPnEFRCA-NGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
505-542 3.01e-05

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 41.47  E-value: 3.01e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2024341832 505 VPCSPFTHRCDDGTCVKKpNPLCDATVDCKDLSDEKHC 542
Cdd:pfam00057   1 STCSPNEFQCGSGECIPR-SWVCDGDPDCGDGSDEENC 37
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
467-498 4.16e-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: 41.08  E-value: 4.16e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2024341832  467 CPA-KFQCQeDSTCIEFSRVCNQQRDCVNGSDE 498
Cdd:smart00192   2 CPPgEFQCD-NGRCIPSSWVCDGVDDCGDGSDE 33
CUB pfam00431
CUB domain;
311-367 5.99e-05

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 43.05  E-value: 5.99e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024341832 311 CGVNITlreglELQGKISTPHYPSYYSPNTQCTWHMSVPSlDYGVTLWFDAYALSRQ 367
Cdd:pfam00431   1 CGGVLT-----DSSGSISSPNYPNPYPPNKDCVWLIRAPP-GFRVKLTFQDFELEDH 51
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
507-539 3.68e-04

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: 38.38  E-value: 3.68e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2024341832  507 CSPFTHRCDDGTCVKKPNpLCDATVDCKDLSDE 539
Cdd:smart00192   2 CPPGEFQCDNGRCIPSSW-VCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
435-462 4.27e-04

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: 38.38  E-value: 4.27e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2024341832  435 PREFLCSvNGLCVPA---CDGIKDCPNGLDE 462
Cdd:smart00192   4 PGEFQCD-NGRCIPSswvCDGVDDCGDGSDE 33
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
564-678 2.17e-03

Domain of unknown function (DUF1986); This domain is found in serine proteases and is predicted to contain disulphide bonds.


Pssm-ID: 286432  Cd Length: 116  Bit Score: 38.68  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024341832 564 WPWQASLQVRGRHICGGTLIADRWVVSAAHCFQDERLASPSVwTIYLGKYfqNTTSHTEVSFKVIrlflhpyYEEDSHDY 643
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYI-SVVLGGA--KTLKSIEGPYEQI-------VRVDCRHD 70
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2024341832 644 ----DVALLQLDHPVIISPFIQPICLPATSHLFEPGLHC 678
Cdd:pfam09342  71 ipesEISLLHLASPASFSNHVLPTFVPETRNENEKDNEC 109
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
435-465 3.88e-03

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 35.69  E-value: 3.88e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2024341832 435 PREFLCSvNGLCVP---ACDGIKDCPNGLDERNC 465
Cdd:pfam00057   5 PNEFQCG-SGECIPrswVCDGDPDCGDGSDEENC 37
 
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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