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Conserved domains on  [gi|16758444|ref|NP_446087|]
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suppressor of tumorigenicity 14 protein [Rattus norvegicus]

Protein Classification

CUB domain-containing protein( domain architecture ID 10475859)

CUB (complement C1r/C1s, Uegf, Bmp1) domain-containing protein

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 ...
615-852 1.13e-95

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: 299.19  E-value: 1.13e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444 615 VVGGTNADEGEWPWQVSLHALGQGHLCGASLISPDWLVSAAHCFQDETIFKYsdhtmwTAFLGLLDQSKRSASGvQEHKL 694
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNY------TVRLGSHDLSSNEGGG-QVIKV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444 695 KRIITHPSFNDFTFDYDIALLELEKPAEYSTVVRPICLPDNTHVFPAGKAIWVTGWGHTKEGGTGALILQKGEIRVINQT 774
Cdd:cd00190  74 KKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444 775 TCEELLPQQ--ITPRMMCVGFLSGGVDSCQGDSGGPLsSVEKDGRIFQAGVVSWGEGCAQRNKPGVYTRIPEVRDWIKEQ 852
Cdd:cd00190 154 ECKRAYSYGgtITDNMLCAGGLEGGKDACQGDSGGPL-VCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
340-444 3.61e-28

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: 109.42  E-value: 3.61e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444 340 CGG-LLSEAQGTFSSPYYPGHYPPNINCTWNIKVPNNRNVKVRFKLFYLvdpnIPVGSCTKDYVEI-NGE--------KF 409
Cdd:cd00041   1 CGGtLTASTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDL----ESSPNCSYDYLEIyDGPstsspllgRF 76
                        90       100       110
                ....*....|....*....|....*....|....*
gi 16758444 410 CGERSQFVVSSNSSKITVHFHSDHSYTDTGFLAEY 444
Cdd:cd00041  77 CGSTLPPPIISSGNSLTVRFRSDSSVTGRGFKATY 111
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
214-332 2.16e-19

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: 84.39  E-value: 2.16e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444 214 CSFALHARgrTVTRFTTPGFPNsPYPAHARCQWVLRGDADSVLSLTFRSFDVAPCDGHDSDLVTVYDSLSPMEPHaVVRL 293
Cdd:cd00041   1 CGGTLTAS--TSGTISSPNYPN-NYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPL-LGRF 76
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 16758444 294 CGTFSPSynlTFLSSQNVFLVTLITNTDRRHPGFEATFF 332
Cdd:cd00041  77 CGSTLPP---PIISSGNSLTVRFRSDSSVTGRGFKATYS 112
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
88-178 3.69e-13

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: 66.11  E-value: 3.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444    88 KVFNGHLRITNENFLDAYENSTSTEFISLASQVKEALKLMYSEVPvLGPYHKKSTVTAFS--EGSVIAYYWSEFsIPPHL 165
Cdd:pfam01390   1 QYYTGSFKITNLQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSS-LRKQYIKSHVLRLRpdGGSVVVDVVLVF-RFPST 78
                          90
                  ....*....|...
gi 16758444   166 EEEVDRAMAVERV 178
Cdd:pfam01390  79 EPALDREKLIEEI 91
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
525-559 4.32e-13

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: 63.76  E-value: 4.32e-13
                        10        20        30
                ....*....|....*....|....*....|....*
gi 16758444 525 CPAGSFKCSNGKCLPQSQQCNGKDDCGDGSDEASC 559
Cdd:cd00112   1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
454-486 1.72e-10

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: 56.45  E-value: 1.72e-10
                        10        20        30
                ....*....|....*....|....*....|...
gi 16758444 454 PGMFMCKTGRCIRKDLRCDGWADCPDYSDERHC 486
Cdd:cd00112   3 PNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
492-523 2.40e-10

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: 56.06  E-value: 2.40e-10
                        10        20        30
                ....*....|....*....|....*....|..
gi 16758444 492 HQFMCKNQFCKPLFWVCDSVNDCGDGSDEEGC 523
Cdd:cd00112   4 NEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
567-602 3.19e-08

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: 49.90  E-value: 3.19e-08
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 16758444 567 CTKYTYRCQNGLCLNKGNpECDGKKDCSDGSDEKNC 602
Cdd:cd00112   1 CPPNEFRCANGRCIPSSW-VCDGEDDCGDGSDEENC 35
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
615-852 1.13e-95

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: 299.19  E-value: 1.13e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444 615 VVGGTNADEGEWPWQVSLHALGQGHLCGASLISPDWLVSAAHCFQDETIFKYsdhtmwTAFLGLLDQSKRSASGvQEHKL 694
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNY------TVRLGSHDLSSNEGGG-QVIKV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444 695 KRIITHPSFNDFTFDYDIALLELEKPAEYSTVVRPICLPDNTHVFPAGKAIWVTGWGHTKEGGTGALILQKGEIRVINQT 774
Cdd:cd00190  74 KKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444 775 TCEELLPQQ--ITPRMMCVGFLSGGVDSCQGDSGGPLsSVEKDGRIFQAGVVSWGEGCAQRNKPGVYTRIPEVRDWIKEQ 852
Cdd:cd00190 154 ECKRAYSYGgtITDNMLCAGGLEGGKDACQGDSGGPL-VCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
614-849 4.74e-93

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: 291.89  E-value: 4.74e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444    614 RVVGGTNADEGEWPWQVSLHALGQGHLCGASLISPDWLVSAAHCFQDetifkySDHTMWTAFLGLLDQSkrSASGVQEHK 693
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRG------SDPSNIRVRLGSHDLS--SGEEGQVIK 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444    694 LKRIITHPSFNDFTFDYDIALLELEKPAEYSTVVRPICLPDNTHVFPAGKAIWVTGWGHTKEG-GTGALILQKGEIRVIN 772
Cdd:smart00020  73 VSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVS 152
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16758444    773 QTTCEELLPQQ--ITPRMMCVGFLSGGVDSCQGDSGGPLssVEKDGRIFQAGVVSWGEGCAQRNKPGVYTRIPEVRDWI 849
Cdd:smart00020 153 NATCRRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPL--VCNDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
612-855 6.37e-74

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 242.63  E-value: 6.37e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444 612 QARVVGGTNADEGEWPWQVSLHALG--QGHLCGASLISPDWLVSAAHCFQDETIFKYsdhtmwTAFLGLLDqskRSASGV 689
Cdd:COG5640  28 APAIVGGTPATVGEYPWMVALQSSNgpSGQFCGGTLIAPRWVLTAAHCVDGDGPSDL------RVVIGSTD---LSTSGG 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444 690 QEHKLKRIITHPSFNDFTFDYDIALLELEKPAeysTVVRPICLPDNTHVFPAGKAIWVTGWGHTKEG-GTGALILQKGEI 768
Cdd:COG5640  99 TVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTLRKADV 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444 769 RVINQTTCEeLLPQQITPRMMCVGFLSGGVDSCQGDSGGPLSsVEKDGRIFQAGVVSWGEGCAQRNKPGVYTRIPEVRDW 848
Cdd:COG5640 176 PVVSDATCA-AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDW 253

                ....*..
gi 16758444 849 IKEQTGV 855
Cdd:COG5640 254 IKSTAGG 260
Trypsin pfam00089
Trypsin;
615-849 2.23e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 228.48  E-value: 2.23e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444   615 VVGGTNADEGEWPWQVSLHALGQGHLCGASLISPDWLVSAAHCFqdetifkySDHTMWTAFLGLLDQSKRSAsGVQEHKL 694
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCV--------SGASDVKVVLGAHNIVLREG-GEQKFDV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444   695 KRIITHPSFNDFTFDYDIALLELEKPAEYSTVVRPICLPDNTHVFPAGKAIWVTGWGHTKEGGTgALILQKGEIRVINQT 774
Cdd:pfam00089  72 EKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRE 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16758444   775 TCEELLPQQITPRMMCVGFlsGGVDSCQGDSGGPLssVEKDGriFQAGVVSWGEGCAQRNKPGVYTRIPEVRDWI 849
Cdd:pfam00089 151 TCRSAYGGTVTDTMICAGA--GGKDACQGDSGGPL--VCSDG--ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
340-444 3.61e-28

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: 109.42  E-value: 3.61e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444 340 CGG-LLSEAQGTFSSPYYPGHYPPNINCTWNIKVPNNRNVKVRFKLFYLvdpnIPVGSCTKDYVEI-NGE--------KF 409
Cdd:cd00041   1 CGGtLTASTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDL----ESSPNCSYDYLEIyDGPstsspllgRF 76
                        90       100       110
                ....*....|....*....|....*....|....*
gi 16758444 410 CGERSQFVVSSNSSKITVHFHSDHSYTDTGFLAEY 444
Cdd:cd00041  77 CGSTLPPPIISSGNSLTVRFRSDSSVTGRGFKATY 111
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
349-444 6.40e-23

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: 93.99  E-value: 6.40e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444    349 GTFSSPYYPGHYPPNINCTWNIKVPNNRNVKVRFKLFYLVDPNipvgSCTKDYVEI-NGE--------KFCG-ERSQFVV 418
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSD----NCEYDYVEIyDGPsasspllgRFCGsEAPPPVI 76
                           90       100
                   ....*....|....*....|....*.
gi 16758444    419 SSNSSKITVHFHSDHSYTDTGFLAEY 444
Cdd:smart00042  77 SSSSNSLTLTFVSDSSVQKRGFSARY 102
CUB pfam00431
CUB domain;
340-444 2.05e-19

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 84.27  E-value: 2.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444   340 CGGLLSEAQGTFSSPYYPGHYPPNINCTWNIKVPNNRNVKVRFKLFYLVDPNipvgSCTKDYVEI---------NGEKFC 410
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHD----ECGYDYVEIrdgpsasspLLGRFC 76
                          90       100       110
                  ....*....|....*....|....*....|....
gi 16758444   411 GERSQFVVSSNSSKITVHFHSDHSYTDTGFLAEY 444
Cdd:pfam00431  77 GSGIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
214-332 2.16e-19

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: 84.39  E-value: 2.16e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444 214 CSFALHARgrTVTRFTTPGFPNsPYPAHARCQWVLRGDADSVLSLTFRSFDVAPCDGHDSDLVTVYDSLSPMEPHaVVRL 293
Cdd:cd00041   1 CGGTLTAS--TSGTISSPNYPN-NYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPL-LGRF 76
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 16758444 294 CGTFSPSynlTFLSSQNVFLVTLITNTDRRHPGFEATFF 332
Cdd:cd00041  77 CGSTLPP---PIISSGNSLTVRFRSDSSVTGRGFKATYS 112
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
227-331 1.99e-14

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: 69.73  E-value: 1.99e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444    227 RFTTPGFPNsPYPAHARCQWVLRGDADSVLSLTFRSFDVAPCDGHDSDLVTVYDSLSPMEPHaVVRLCGTFSPsyNLTFL 306
Cdd:smart00042   2 TITSPNYPQ-SYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPL-LGRFCGSEAP--PPVIS 77
                           90       100
                   ....*....|....*....|....*
gi 16758444    307 SSQNVFLVTLITNTDRRHPGFEATF 331
Cdd:smart00042  78 SSSNSLTLTFVSDSSVQKRGFSARY 102
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
88-178 3.69e-13

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: 66.11  E-value: 3.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444    88 KVFNGHLRITNENFLDAYENSTSTEFISLASQVKEALKLMYSEVPvLGPYHKKSTVTAFS--EGSVIAYYWSEFsIPPHL 165
Cdd:pfam01390   1 QYYTGSFKITNLQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSS-LRKQYIKSHVLRLRpdGGSVVVDVVLVF-RFPST 78
                          90
                  ....*....|...
gi 16758444   166 EEEVDRAMAVERV 178
Cdd:pfam01390  79 EPALDREKLIEEI 91
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
525-559 4.32e-13

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: 63.76  E-value: 4.32e-13
                        10        20        30
                ....*....|....*....|....*....|....*
gi 16758444 525 CPAGSFKCSNGKCLPQSQQCNGKDDCGDGSDEASC 559
Cdd:cd00112   1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
525-556 5.08e-12

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: 60.72  E-value: 5.08e-12
                           10        20        30
                   ....*....|....*....|....*....|..
gi 16758444    525 CPAGSFKCSNGKCLPQSQQCNGKDDCGDGSDE 556
Cdd:smart00192   2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
CUB pfam00431
CUB domain;
227-331 3.01e-11

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 61.16  E-value: 3.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444   227 RFTTPGFPNsPYPAHARCQWVLRGDADSVLSLTFRSFDVAPCDGHDSDLVTVYDSLSPMEPhAVVRLCGTFSPsynLTFL 306
Cdd:pfam00431  11 SISSPNYPN-PYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSP-LLGRFCGSGIP---EDIV 85
                          90       100
                  ....*....|....*....|....*
gi 16758444   307 SSQNVFLVTLITNTDRRHPGFEATF 331
Cdd:pfam00431  86 SSSNQMTIKFVSDASVQKRGFKATY 110
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
454-486 1.72e-10

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: 56.45  E-value: 1.72e-10
                        10        20        30
                ....*....|....*....|....*....|...
gi 16758444 454 PGMFMCKTGRCIRKDLRCDGWADCPDYSDERHC 486
Cdd:cd00112   3 PNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
492-523 2.40e-10

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: 56.06  E-value: 2.40e-10
                        10        20        30
                ....*....|....*....|....*....|..
gi 16758444 492 HQFMCKNQFCKPLFWVCDSVNDCGDGSDEEGC 523
Cdd:cd00112   4 NEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
525-559 9.70e-10

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 54.56  E-value: 9.70e-10
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 16758444   525 CPAGSFKCSNGKCLPQSQQCNGKDDCGDGSDEASC 559
Cdd:pfam00057   3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
487-520 3.18e-09

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: 52.64  E-value: 3.18e-09
                           10        20        30
                   ....*....|....*....|....*....|....
gi 16758444    487 RCNAtHQFMCKNQFCKPLFWVCDSVNDCGDGSDE 520
Cdd:smart00192   1 TCPP-GEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
454-483 8.80e-09

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: 51.48  E-value: 8.80e-09
                           10        20        30
                   ....*....|....*....|....*....|
gi 16758444    454 PGMFMCKTGRCIRKDLRCDGWADCPDYSDE 483
Cdd:smart00192   4 PGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
567-602 3.19e-08

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: 49.90  E-value: 3.19e-08
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 16758444 567 CTKYTYRCQNGLCLNKGNpECDGKKDCSDGSDEKNC 602
Cdd:cd00112   1 CPPNEFRCANGRCIPSSW-VCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
454-486 4.41e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 46.86  E-value: 4.41e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 16758444   454 PGMFMCKTGRCIRKDLRCDGWADCPDYSDERHC 486
Cdd:pfam00057   5 PNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
492-523 1.05e-06

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 45.70  E-value: 1.05e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 16758444   492 HQFMCKNQFCKPLFWVCDSVNDCGDGSDEEGC 523
Cdd:pfam00057   6 NEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
567-599 7.28e-06

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: 43.39  E-value: 7.28e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 16758444    567 CTKYTYRCQNGLCLNKGNpECDGKKDCSDGSDE 599
Cdd:smart00192   2 CPPGEFQCDNGRCIPSSW-VCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
572-602 7.67e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 37.61  E-value: 7.67e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 16758444   572 YRCQNGLCLnKGNPECDGKKDCSDGSDEKNC 602
Cdd:pfam00057   8 FQCGSGECI-PRSWVCDGDPDCGDGSDEENC 37
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
615-852 1.13e-95

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: 299.19  E-value: 1.13e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444 615 VVGGTNADEGEWPWQVSLHALGQGHLCGASLISPDWLVSAAHCFQDETIFKYsdhtmwTAFLGLLDQSKRSASGvQEHKL 694
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNY------TVRLGSHDLSSNEGGG-QVIKV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444 695 KRIITHPSFNDFTFDYDIALLELEKPAEYSTVVRPICLPDNTHVFPAGKAIWVTGWGHTKEGGTGALILQKGEIRVINQT 774
Cdd:cd00190  74 KKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444 775 TCEELLPQQ--ITPRMMCVGFLSGGVDSCQGDSGGPLsSVEKDGRIFQAGVVSWGEGCAQRNKPGVYTRIPEVRDWIKEQ 852
Cdd:cd00190 154 ECKRAYSYGgtITDNMLCAGGLEGGKDACQGDSGGPL-VCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
614-849 4.74e-93

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: 291.89  E-value: 4.74e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444    614 RVVGGTNADEGEWPWQVSLHALGQGHLCGASLISPDWLVSAAHCFQDetifkySDHTMWTAFLGLLDQSkrSASGVQEHK 693
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRG------SDPSNIRVRLGSHDLS--SGEEGQVIK 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444    694 LKRIITHPSFNDFTFDYDIALLELEKPAEYSTVVRPICLPDNTHVFPAGKAIWVTGWGHTKEG-GTGALILQKGEIRVIN 772
Cdd:smart00020  73 VSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVS 152
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16758444    773 QTTCEELLPQQ--ITPRMMCVGFLSGGVDSCQGDSGGPLssVEKDGRIFQAGVVSWGEGCAQRNKPGVYTRIPEVRDWI 849
Cdd:smart00020 153 NATCRRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPL--VCNDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
612-855 6.37e-74

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 242.63  E-value: 6.37e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444 612 QARVVGGTNADEGEWPWQVSLHALG--QGHLCGASLISPDWLVSAAHCFQDETIFKYsdhtmwTAFLGLLDqskRSASGV 689
Cdd:COG5640  28 APAIVGGTPATVGEYPWMVALQSSNgpSGQFCGGTLIAPRWVLTAAHCVDGDGPSDL------RVVIGSTD---LSTSGG 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444 690 QEHKLKRIITHPSFNDFTFDYDIALLELEKPAeysTVVRPICLPDNTHVFPAGKAIWVTGWGHTKEG-GTGALILQKGEI 768
Cdd:COG5640  99 TVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTLRKADV 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444 769 RVINQTTCEeLLPQQITPRMMCVGFLSGGVDSCQGDSGGPLSsVEKDGRIFQAGVVSWGEGCAQRNKPGVYTRIPEVRDW 848
Cdd:COG5640 176 PVVSDATCA-AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDW 253

                ....*..
gi 16758444 849 IKEQTGV 855
Cdd:COG5640 254 IKSTAGG 260
Trypsin pfam00089
Trypsin;
615-849 2.23e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 228.48  E-value: 2.23e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444   615 VVGGTNADEGEWPWQVSLHALGQGHLCGASLISPDWLVSAAHCFqdetifkySDHTMWTAFLGLLDQSKRSAsGVQEHKL 694
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCV--------SGASDVKVVLGAHNIVLREG-GEQKFDV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444   695 KRIITHPSFNDFTFDYDIALLELEKPAEYSTVVRPICLPDNTHVFPAGKAIWVTGWGHTKEGGTgALILQKGEIRVINQT 774
Cdd:pfam00089  72 EKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRE 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16758444   775 TCEELLPQQITPRMMCVGFlsGGVDSCQGDSGGPLssVEKDGriFQAGVVSWGEGCAQRNKPGVYTRIPEVRDWI 849
Cdd:pfam00089 151 TCRSAYGGTVTDTMICAGA--GGKDACQGDSGGPL--VCSDG--ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
340-444 3.61e-28

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: 109.42  E-value: 3.61e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444 340 CGG-LLSEAQGTFSSPYYPGHYPPNINCTWNIKVPNNRNVKVRFKLFYLvdpnIPVGSCTKDYVEI-NGE--------KF 409
Cdd:cd00041   1 CGGtLTASTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDL----ESSPNCSYDYLEIyDGPstsspllgRF 76
                        90       100       110
                ....*....|....*....|....*....|....*
gi 16758444 410 CGERSQFVVSSNSSKITVHFHSDHSYTDTGFLAEY 444
Cdd:cd00041  77 CGSTLPPPIISSGNSLTVRFRSDSSVTGRGFKATY 111
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
349-444 6.40e-23

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: 93.99  E-value: 6.40e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444    349 GTFSSPYYPGHYPPNINCTWNIKVPNNRNVKVRFKLFYLVDPNipvgSCTKDYVEI-NGE--------KFCG-ERSQFVV 418
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSD----NCEYDYVEIyDGPsasspllgRFCGsEAPPPVI 76
                           90       100
                   ....*....|....*....|....*.
gi 16758444    419 SSNSSKITVHFHSDHSYTDTGFLAEY 444
Cdd:smart00042  77 SSSSNSLTLTFVSDSSVQKRGFSARY 102
CUB pfam00431
CUB domain;
340-444 2.05e-19

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 84.27  E-value: 2.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444   340 CGGLLSEAQGTFSSPYYPGHYPPNINCTWNIKVPNNRNVKVRFKLFYLVDPNipvgSCTKDYVEI---------NGEKFC 410
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHD----ECGYDYVEIrdgpsasspLLGRFC 76
                          90       100       110
                  ....*....|....*....|....*....|....
gi 16758444   411 GERSQFVVSSNSSKITVHFHSDHSYTDTGFLAEY 444
Cdd:pfam00431  77 GSGIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
214-332 2.16e-19

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: 84.39  E-value: 2.16e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444 214 CSFALHARgrTVTRFTTPGFPNsPYPAHARCQWVLRGDADSVLSLTFRSFDVAPCDGHDSDLVTVYDSLSPMEPHaVVRL 293
Cdd:cd00041   1 CGGTLTAS--TSGTISSPNYPN-NYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPL-LGRF 76
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 16758444 294 CGTFSPSynlTFLSSQNVFLVTLITNTDRRHPGFEATFF 332
Cdd:cd00041  77 CGSTLPP---PIISSGNSLTVRFRSDSSVTGRGFKATYS 112
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
227-331 1.99e-14

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: 69.73  E-value: 1.99e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444    227 RFTTPGFPNsPYPAHARCQWVLRGDADSVLSLTFRSFDVAPCDGHDSDLVTVYDSLSPMEPHaVVRLCGTFSPsyNLTFL 306
Cdd:smart00042   2 TITSPNYPQ-SYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPL-LGRFCGSEAP--PPVIS 77
                           90       100
                   ....*....|....*....|....*
gi 16758444    307 SSQNVFLVTLITNTDRRHPGFEATF 331
Cdd:smart00042  78 SSSNSLTLTFVSDSSVQKRGFSARY 102
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
88-178 3.69e-13

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: 66.11  E-value: 3.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444    88 KVFNGHLRITNENFLDAYENSTSTEFISLASQVKEALKLMYSEVPvLGPYHKKSTVTAFS--EGSVIAYYWSEFsIPPHL 165
Cdd:pfam01390   1 QYYTGSFKITNLQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSS-LRKQYIKSHVLRLRpdGGSVVVDVVLVF-RFPST 78
                          90
                  ....*....|...
gi 16758444   166 EEEVDRAMAVERV 178
Cdd:pfam01390  79 EPALDREKLIEEI 91
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
525-559 4.32e-13

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: 63.76  E-value: 4.32e-13
                        10        20        30
                ....*....|....*....|....*....|....*
gi 16758444 525 CPAGSFKCSNGKCLPQSQQCNGKDDCGDGSDEASC 559
Cdd:cd00112   1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
525-556 5.08e-12

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: 60.72  E-value: 5.08e-12
                           10        20        30
                   ....*....|....*....|....*....|..
gi 16758444    525 CPAGSFKCSNGKCLPQSQQCNGKDDCGDGSDE 556
Cdd:smart00192   2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
CUB pfam00431
CUB domain;
227-331 3.01e-11

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 61.16  E-value: 3.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444   227 RFTTPGFPNsPYPAHARCQWVLRGDADSVLSLTFRSFDVAPCDGHDSDLVTVYDSLSPMEPhAVVRLCGTFSPsynLTFL 306
Cdd:pfam00431  11 SISSPNYPN-PYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSP-LLGRFCGSGIP---EDIV 85
                          90       100
                  ....*....|....*....|....*
gi 16758444   307 SSQNVFLVTLITNTDRRHPGFEATF 331
Cdd:pfam00431  86 SSSNQMTIKFVSDASVQKRGFKATY 110
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
454-486 1.72e-10

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: 56.45  E-value: 1.72e-10
                        10        20        30
                ....*....|....*....|....*....|...
gi 16758444 454 PGMFMCKTGRCIRKDLRCDGWADCPDYSDERHC 486
Cdd:cd00112   3 PNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
492-523 2.40e-10

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: 56.06  E-value: 2.40e-10
                        10        20        30
                ....*....|....*....|....*....|..
gi 16758444 492 HQFMCKNQFCKPLFWVCDSVNDCGDGSDEEGC 523
Cdd:cd00112   4 NEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
636-827 3.10e-10

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 60.46  E-value: 3.10e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444 636 GQGHLCGASLISPDWLVSAAHCFQDETIFKYsdHTMWTAFLGLLDQSKRSASGVqehklkRIITHPSF-NDFTFDYDIAL 714
Cdd:COG3591   9 GGGGVCTGTLIGPNLVLTAGHCVYDGAGGGW--ATNIVFVPGYNGGPYGTATAT------RFRVPPGWvASGDAGYDYAL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758444 715 LELEKPAeySTVVRPICLPDNTHVfPAGKAIWVTGWGhtkeGGTGALILQKGEIRVINQTTceellpqqitprmmcvGFL 794
Cdd:COG3591  81 LRLDEPL--GDTTGWLGLAFNDAP-LAGEPVTIIGYP----GDRPKDLSLDCSGRVTGVQG----------------NRL 137
                       170       180       190
                ....*....|....*....|....*....|....
gi 16758444 795 SGGVDSCQGDSGGP-LSSVEKDGRIFqaGVVSWG 827
Cdd:COG3591 138 SYDCDTTGGSSGSPvLDDSDGGGRVV--GVHSAG 169
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
525-559 9.70e-10

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 54.56  E-value: 9.70e-10
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 16758444   525 CPAGSFKCSNGKCLPQSQQCNGKDDCGDGSDEASC 559
Cdd:pfam00057   3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
487-520 3.18e-09

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: 52.64  E-value: 3.18e-09
                           10        20        30
                   ....*....|....*....|....*....|....
gi 16758444    487 RCNAtHQFMCKNQFCKPLFWVCDSVNDCGDGSDE 520
Cdd:smart00192   1 TCPP-GEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
454-483 8.80e-09

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: 51.48  E-value: 8.80e-09
                           10        20        30
                   ....*....|....*....|....*....|
gi 16758444    454 PGMFMCKTGRCIRKDLRCDGWADCPDYSDE 483
Cdd:smart00192   4 PGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
567-602 3.19e-08

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: 49.90  E-value: 3.19e-08
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 16758444 567 CTKYTYRCQNGLCLNKGNpECDGKKDCSDGSDEKNC 602
Cdd:cd00112   1 CPPNEFRCANGRCIPSSW-VCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
454-486 4.41e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 46.86  E-value: 4.41e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 16758444   454 PGMFMCKTGRCIRKDLRCDGWADCPDYSDERHC 486
Cdd:pfam00057   5 PNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
492-523 1.05e-06

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 45.70  E-value: 1.05e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 16758444   492 HQFMCKNQFCKPLFWVCDSVNDCGDGSDEEGC 523
Cdd:pfam00057   6 NEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
567-599 7.28e-06

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: 43.39  E-value: 7.28e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 16758444    567 CTKYTYRCQNGLCLNKGNpECDGKKDCSDGSDE 599
Cdd:smart00192   2 CPPGEFQCDNGRCIPSSW-VCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
572-602 7.67e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 37.61  E-value: 7.67e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 16758444   572 YRCQNGLCLnKGNPECDGKKDCSDGSDEKNC 602
Cdd:pfam00057   8 FQCGSGECI-PRSWVCDGDPDCGDGSDEENC 37
PRKCSH-like pfam12999
Glucosidase II beta subunit-like; The sequences found in this family are similar to a region ...
472-526 2.50e-03

Glucosidase II beta subunit-like; The sequences found in this family are similar to a region found in the beta-subunit of glucosidase II, which is also known as protein kinase C substrate 80K-H (PRKCSH). The enzyme catalyzes the sequential removal of two alpha-1,3-linked glucose residues in the second step of N-linked oligosaccharide processing. The beta subunit is required for the solubility and stability of the heterodimeric enzyme, and is involved in retaining the enzyme within the endoplasmic reticulum.


Pssm-ID: 372423 [Multi-domain]  Cd Length: 176  Bit Score: 39.77  E-value: 2.50e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758444   472 DGWADCPDYSDERHCRCNATHQFMCKNQFCKPLFWVCDSVND-------CGDGSDEEGCSCP 526
Cdd:pfam12999  55 DDYCDCPDGSDEPGTNACSNGKFYCANEGFIPGYIPSFKVDDgvcdydiCCDGSDEALGKCP 116
CUB_2 pfam02408
CUB-like domain; This is a family of hypothetical C. elegans proteins. The aligned region has ...
360-429 4.17e-03

CUB-like domain; This is a family of hypothetical C. elegans proteins. The aligned region has no known function nor do any of the proteins which possess it. However, this domain is related to the CUB domain.


Pssm-ID: 280554  Cd Length: 120  Bit Score: 38.13  E-value: 4.17e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16758444   360 YPPNINCTWNIKVPNNRNVKVRFKLFYLVDPNIPVGSCTKDYVEINGEK-----FCGERSQFVVSSNSSKITVHF 429
Cdd:pfam02408  38 IPANQNCSWNINVPKGYYAKVIISAKTNDDSSITVTDSLGNSEYVTDSDnepyfFVSPSFTINLSTGSGSVSFGF 112
 
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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