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Conserved domains on  [gi|7363445|ref|NP_035306|]
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suppressor of tumorigenicity 14 protein homolog [Mus musculus]

Protein Classification

neuropilin and tolloid-like protein; serine protease( domain architecture ID 10475859)

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 ...
 615-852 3.10e-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: 298.04  E-value: 3.10e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445  615 VVGGTNADEGEWPWQVSLHALGQGHLCGASLISPDWLVSAAHCFQDDKNFKYsdytmwTAFLGLLDQSKRSASGvQELKL 694
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNY------TVRLGSHDLSSNEGGG-QVIKV 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445  695 KRIITHPSFNDFTFDYDIALLELEKSVEYSTVVRPICLPDATHVFPAGKAIWVTGWGHTKEGGTGALILQKGEIRVINQT 774
Cdd:cd00190  74 KKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNA 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445  775 TCEDLMPQQ--ITPRMMCVGFLSGGVDSCQGDSGGPLsSAEKDGRMFQAGVVSWGEGCAQRNKPGVYTRLPVVRDWIKEH 852
Cdd:cd00190 154 ECKRAYSYGgtITDNMLCAGGLEGGKDACQGDSGGPL-VCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 340-444 1.33e-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: 110.58  E-value: 1.33e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445  340 CGGFLSDT-QGTFSSPYYPGHYPPNINCTWNIKVPNNRNVKVRFKLFYLVDPNvpvgSCTKDYVEI-NGE--------KY 409
Cdd:cd00041   1 CGGTLTAStSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSP----NCSYDYLEIyDGPstsspllgRF 76

                        90       100       110
                ....*....|....*....|....*....|....*
gi 7363445  410 CGERSQFVVSSNSSKITVHFHSDHSYTDTGFLAEY 444
Cdd:cd00041  77 CGSTLPPPIISSGNSLTVRFRSDSSVTGRGFKATY 111
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 227-332 3.82e-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: 83.62  E-value: 3.82e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445  227 RFTTPGFPNsPYPAHARCQWVLRGDADSVLSLTFRSFDVAPCDEHGSDLVTVYDSLSPMEPHaVVRLCGTFSPSynlTFL 306
Cdd:cd00041  12 TISSPNYPN-NYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPL-LGRFCGSTLPP---PII 86

                        90       100
                ....*....|....*....|....*.
gi 7363445  307 SSQNVFLVTLITNTDRRHPGFEATFF 332
Cdd:cd00041  87 SSGNSLTVRFRSDSSVTGRGFKATYS 112
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 525-559 2.71e-12

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: 61.45  E-value: 2.71e-12
                        10        20        30
                ....*....|....*....|....*....|....*
gi 7363445  525 CPAGSFKCSNGKCLPQSQKCNGKDNCGDGSDEASC 559
Cdd:cd00112   1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
 88-178 4.46e-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: 4.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445     88 KVFNGHLRITNEIFLDAYENSTSTEFISLASQVKEALKLLYNEVPvLGPYHKKSAVTAFS--EGSVIAYYWSEFsIPPHL 165
Cdd:pfam01390   1 QYYTGSFKITNLQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSS-LRKQYIKSHVLRLRpdGGSVVVDVVLVF-RFPST 78

                          90
                  ....*....|...
gi 7363445    166 AEEVDRAMAVERV 178
Cdd:pfam01390  79 EPALDREKLIEEI 91
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 492-523 1.86e-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: 1.86e-10
                        10        20        30
                ....*....|....*....|....*....|..
gi 7363445  492 HQFTCKNQFCKPLFWVCDSVNDCGDGSDEEGC 523
Cdd:cd00112   4 NEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 454-486 4.40e-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: 55.29  E-value: 4.40e-10
                        10        20        30
                ....*....|....*....|....*....|...
gi 7363445  454 PGMFMCKTGRCIRKELRCDGWADCPDYSDERYC 486
Cdd:cd00112   3 PNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 567-602 3.62e-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: 3.62e-08
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 7363445  567 CTKYTYRCQNGLCLSKGNpECDGKTDCSDGSDEKNC 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 3.10e-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: 298.04  E-value: 3.10e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445  615 VVGGTNADEGEWPWQVSLHALGQGHLCGASLISPDWLVSAAHCFQDDKNFKYsdytmwTAFLGLLDQSKRSASGvQELKL 694
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNY------TVRLGSHDLSSNEGGG-QVIKV 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445  695 KRIITHPSFNDFTFDYDIALLELEKSVEYSTVVRPICLPDATHVFPAGKAIWVTGWGHTKEGGTGALILQKGEIRVINQT 774
Cdd:cd00190  74 KKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNA 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445  775 TCEDLMPQQ--ITPRMMCVGFLSGGVDSCQGDSGGPLsSAEKDGRMFQAGVVSWGEGCAQRNKPGVYTRLPVVRDWIKEH 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 1.38e-91

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: 288.04  E-value: 1.38e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445     614 RVVGGTNADEGEWPWQVSLHALGQGHLCGASLISPDWLVSAAHCFQDDKNFKYsdytmwTAFLGLLDQSkrSASGVQELK 693
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNI------RVRLGSHDLS--SGEEGQVIK 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445     694 LKRIITHPSFNDFTFDYDIALLELEKSVEYSTVVRPICLPDATHVFPAGKAIWVTGWGHTKEG-GTGALILQKGEIRVIN 772
Cdd:smart00020  73 VSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVS 152

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7363445     773 QTTCEDLMPQQ--ITPRMMCVGFLSGGVDSCQGDSGGPLSSaeKDGRMFQAGVVSWGEGCAQRNKPGVYTRLPVVRDWI 849
Cdd:smart00020 153 NATCRRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVC--NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 612-855 2.64e-72

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 238.01  E-value: 2.64e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445  612 QARVVGGTNADEGEWPWQVSLHALG--QGHLCGASLISPDWLVSAAHCFQDDKNFKYsdytmwTAFLGLLDqskRSASGV 689
Cdd:COG5640  28 APAIVGGTPATVGEYPWMVALQSSNgpSGQFCGGTLIAPRWVLTAAHCVDGDGPSDL------RVVIGSTD---LSTSGG 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445  690 QELKLKRIITHPSFNDFTFDYDIALLELEKSVeysTVVRPICLPDATHVFPAGKAIWVTGWGHTKEG-GTGALILQKGEI 768
Cdd:COG5640  99 TVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTLRKADV 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445  769 RVINQTTCeDLMPQQITPRMMCVGFLSGGVDSCQGDSGGPLSsAEKDGRMFQAGVVSWGEGCAQRNKPGVYTRLPVVRDW 848
Cdd:COG5640 176 PVVSDATC-AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDW 253


                ....*..
gi 7363445  849 IKEHTGV 855
Cdd:COG5640 254 IKSTAGG 260
Trypsin pfam00089
Trypsin;
615-849 2.49e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 228.48  E-value: 2.49e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445    615 VVGGTNADEGEWPWQVSLHALGQGHLCGASLISPDWLVSAAHCFQDdknfkYSDYTMWtafLGLLDQSKRSAsGVQELKL 694
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSG-----ASDVKVV---LGAHNIVLREG-GEQKFDV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445    695 KRIITHPSFNDFTFDYDIALLELEKSVEYSTVVRPICLPDATHVFPAGKAIWVTGWGHTKEGGTgALILQKGEIRVINQT 774
Cdd:pfam00089  72 EKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRE 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7363445    775 TCEDLMPQQITPRMMCVGFlsGGVDSCQGDSGGPLSSaekdGRMFQAGVVSWGEGCAQRNKPGVYTRLPVVRDWI 849
Cdd:pfam00089 151 TCRSAYGGTVTDTMICAGA--GGKDACQGDSGGPLVC----SDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 340-444 1.33e-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: 110.58  E-value: 1.33e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445  340 CGGFLSDT-QGTFSSPYYPGHYPPNINCTWNIKVPNNRNVKVRFKLFYLVDPNvpvgSCTKDYVEI-NGE--------KY 409
Cdd:cd00041   1 CGGTLTAStSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSP----NCSYDYLEIyDGPstsspllgRF 76

                        90       100       110
                ....*....|....*....|....*....|....*
gi 7363445  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 5.58e-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: 5.58e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445     349 GTFSSPYYPGHYPPNINCTWNIKVPNNRNVKVRFKLFYLVDPNvpvgSCTKDYVEI-NGE--------KYCG-ERSQFVV 418
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSD----NCEYDYVEIyDGPsasspllgRFCGsEAPPPVI 76

                           90       100
                   ....*....|....*....|....*.
gi 7363445     419 SSNSSKITVHFHSDHSYTDTGFLAEY 444
Cdd:smart00042  77 SSSSNSLTLTFVSDSSVQKRGFSARY 102
CUB pfam00431
CUB domain;
340-444 1.47e-19

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 84.65  E-value: 1.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445    340 CGGFLSDTQGTFSSPYYPGHYPPNINCTWNIKVPNNRNVKVRFKLFYLVDPNvpvgSCTKDYVEI---------NGEKYC 410
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHD----ECGYDYVEIrdgpsasspLLGRFC 76

                          90       100       110
                  ....*....|....*....|....*....|....
gi 7363445    411 GERSQFVVSSNSSKITVHFHSDHSYTDTGFLAEY 444
Cdd:pfam00431  77 GSGIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 227-332 3.82e-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: 83.62  E-value: 3.82e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445  227 RFTTPGFPNsPYPAHARCQWVLRGDADSVLSLTFRSFDVAPCDEHGSDLVTVYDSLSPMEPHaVVRLCGTFSPSynlTFL 306
Cdd:cd00041  12 TISSPNYPN-NYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPL-LGRFCGSTLPP---PII 86

                        90       100
                ....*....|....*....|....*.
gi 7363445  307 SSQNVFLVTLITNTDRRHPGFEATFF 332
Cdd:cd00041  87 SSGNSLTVRFRSDSSVTGRGFKATYS 112
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 227-331 3.36e-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: 68.96  E-value: 3.36e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445     227 RFTTPGFPNsPYPAHARCQWVLRGDADSVLSLTFRSFDVAPCDEHGSDLVTVYDSLSPMEPHaVVRLCGTFSPsyNLTFL 306
Cdd:smart00042   2 TITSPNYPQ-SYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPL-LGRFCGSEAP--PPVIS 77

                           90       100
                   ....*....|....*....|....*
gi 7363445     307 SSQNVFLVTLITNTDRRHPGFEATF 331
Cdd:smart00042  78 SSSNSLTLTFVSDSSVQKRGFSARY 102
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 525-559 2.71e-12

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: 61.45  E-value: 2.71e-12
                        10        20        30
                ....*....|....*....|....*....|....*
gi 7363445  525 CPAGSFKCSNGKCLPQSQKCNGKDNCGDGSDEASC 559
Cdd:cd00112   1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
 88-178 4.46e-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: 4.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445     88 KVFNGHLRITNEIFLDAYENSTSTEFISLASQVKEALKLLYNEVPvLGPYHKKSAVTAFS--EGSVIAYYWSEFsIPPHL 165
Cdd:pfam01390   1 QYYTGSFKITNLQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSS-LRKQYIKSHVLRLRpdGGSVVVDVVLVF-RFPST 78

                          90
                  ....*....|...
gi 7363445    166 AEEVDRAMAVERV 178
Cdd:pfam01390  79 EPALDREKLIEEI 91
CUB pfam00431
CUB domain;
227-331 1.29e-11

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 61.93  E-value: 1.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445    227 RFTTPGFPNsPYPAHARCQWVLRGDADSVLSLTFRSFDVAPCDEHGSDLVTVYDSLSPMEPhAVVRLCGTFSPsynLTFL 306
Cdd:pfam00431  11 SISSPNYPN-PYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSP-LLGRFCGSGIP---EDIV 85

                          90       100
                  ....*....|....*....|....*
gi 7363445    307 SSQNVFLVTLITNTDRRHPGFEATF 331
Cdd:pfam00431  86 SSSNQMTIKFVSDASVQKRGFKATY 110
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 525-556 3.06e-11

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: 58.41  E-value: 3.06e-11
                           10        20        30
                   ....*....|....*....|....*....|..
gi 7363445     525 CPAGSFKCSNGKCLPQSQKCNGKDNCGDGSDE 556
Cdd:smart00192   2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 492-523 1.86e-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: 1.86e-10
                        10        20        30
                ....*....|....*....|....*....|..
gi 7363445  492 HQFTCKNQFCKPLFWVCDSVNDCGDGSDEEGC 523
Cdd:cd00112   4 NEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 454-486 4.40e-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: 55.29  E-value: 4.40e-10
                        10        20        30
                ....*....|....*....|....*....|...
gi 7363445  454 PGMFMCKTGRCIRKELRCDGWADCPDYSDERYC 486
Cdd:cd00112   3 PNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 487-520 4.75e-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: 52.25  E-value: 4.75e-09
                           10        20        30
                   ....*....|....*....|....*....|....
gi 7363445     487 RCNAtHQFTCKNQFCKPLFWVCDSVNDCGDGSDE 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 6.62e-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: 51.87  E-value: 6.62e-09
                           10        20        30
                   ....*....|....*....|....*....|
gi 7363445     454 PGMFMCKTGRCIRKELRCDGWADCPDYSDE 483
Cdd:smart00192   4 PGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
525-559 2.27e-08

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 50.32  E-value: 2.27e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 7363445    525 CPAGSFKCSNGKCLPQSQKCNGKDNCGDGSDEASC 559
Cdd:pfam00057   3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 567-602 3.62e-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: 3.62e-08
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 7363445  567 CTKYTYRCQNGLCLSKGNpECDGKTDCSDGSDEKNC 602
Cdd:cd00112   1 CPPNEFRCANGRCIPSSW-VCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
492-523 5.11e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 46.86  E-value: 5.11e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 7363445    492 HQFTCKNQFCKPLFWVCDSVNDCGDGSDEEGC 523
Cdd:pfam00057   6 NEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 567-599 9.13e-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: 43.01  E-value: 9.13e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 7363445     567 CTKYTYRCQNGLCLSKGNpECDGKTDCSDGSDE 599
Cdd:smart00192   2 CPPGEFQCDNGRCIPSSW-VCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
454-486 9.49e-06

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 43.01  E-value: 9.49e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 7363445    454 PGMFMCKTGRCIRKELRCDGWADCPDYSDERYC 486
Cdd:pfam00057   5 PNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
572-602 3.07e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 38.77  E-value: 3.07e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 7363445    572 YRCQNGLCLSkGNPECDGKTDCSDGSDEKNC 602
Cdd:pfam00057   8 FQCGSGECIP-RSWVCDGDPDCGDGSDEENC 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 3.10e-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: 298.04  E-value: 3.10e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445  615 VVGGTNADEGEWPWQVSLHALGQGHLCGASLISPDWLVSAAHCFQDDKNFKYsdytmwTAFLGLLDQSKRSASGvQELKL 694
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNY------TVRLGSHDLSSNEGGG-QVIKV 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445  695 KRIITHPSFNDFTFDYDIALLELEKSVEYSTVVRPICLPDATHVFPAGKAIWVTGWGHTKEGGTGALILQKGEIRVINQT 774
Cdd:cd00190  74 KKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNA 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445  775 TCEDLMPQQ--ITPRMMCVGFLSGGVDSCQGDSGGPLsSAEKDGRMFQAGVVSWGEGCAQRNKPGVYTRLPVVRDWIKEH 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 1.38e-91

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: 288.04  E-value: 1.38e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445     614 RVVGGTNADEGEWPWQVSLHALGQGHLCGASLISPDWLVSAAHCFQDDKNFKYsdytmwTAFLGLLDQSkrSASGVQELK 693
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNI------RVRLGSHDLS--SGEEGQVIK 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445     694 LKRIITHPSFNDFTFDYDIALLELEKSVEYSTVVRPICLPDATHVFPAGKAIWVTGWGHTKEG-GTGALILQKGEIRVIN 772
Cdd:smart00020  73 VSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVS 152

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7363445     773 QTTCEDLMPQQ--ITPRMMCVGFLSGGVDSCQGDSGGPLSSaeKDGRMFQAGVVSWGEGCAQRNKPGVYTRLPVVRDWI 849
Cdd:smart00020 153 NATCRRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVC--NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 612-855 2.64e-72

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 238.01  E-value: 2.64e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445  612 QARVVGGTNADEGEWPWQVSLHALG--QGHLCGASLISPDWLVSAAHCFQDDKNFKYsdytmwTAFLGLLDqskRSASGV 689
Cdd:COG5640  28 APAIVGGTPATVGEYPWMVALQSSNgpSGQFCGGTLIAPRWVLTAAHCVDGDGPSDL------RVVIGSTD---LSTSGG 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445  690 QELKLKRIITHPSFNDFTFDYDIALLELEKSVeysTVVRPICLPDATHVFPAGKAIWVTGWGHTKEG-GTGALILQKGEI 768
Cdd:COG5640  99 TVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTLRKADV 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445  769 RVINQTTCeDLMPQQITPRMMCVGFLSGGVDSCQGDSGGPLSsAEKDGRMFQAGVVSWGEGCAQRNKPGVYTRLPVVRDW 848
Cdd:COG5640 176 PVVSDATC-AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDW 253


                ....*..
gi 7363445  849 IKEHTGV 855
Cdd:COG5640 254 IKSTAGG 260
Trypsin pfam00089
Trypsin;
615-849 2.49e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 228.48  E-value: 2.49e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445    615 VVGGTNADEGEWPWQVSLHALGQGHLCGASLISPDWLVSAAHCFQDdknfkYSDYTMWtafLGLLDQSKRSAsGVQELKL 694
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSG-----ASDVKVV---LGAHNIVLREG-GEQKFDV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445    695 KRIITHPSFNDFTFDYDIALLELEKSVEYSTVVRPICLPDATHVFPAGKAIWVTGWGHTKEGGTgALILQKGEIRVINQT 774
Cdd:pfam00089  72 EKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRE 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7363445    775 TCEDLMPQQITPRMMCVGFlsGGVDSCQGDSGGPLSSaekdGRMFQAGVVSWGEGCAQRNKPGVYTRLPVVRDWI 849
Cdd:pfam00089 151 TCRSAYGGTVTDTMICAGA--GGKDACQGDSGGPLVC----SDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 340-444 1.33e-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: 110.58  E-value: 1.33e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445  340 CGGFLSDT-QGTFSSPYYPGHYPPNINCTWNIKVPNNRNVKVRFKLFYLVDPNvpvgSCTKDYVEI-NGE--------KY 409
Cdd:cd00041   1 CGGTLTAStSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSP----NCSYDYLEIyDGPstsspllgRF 76

                        90       100       110
                ....*....|....*....|....*....|....*
gi 7363445  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 5.58e-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: 5.58e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445     349 GTFSSPYYPGHYPPNINCTWNIKVPNNRNVKVRFKLFYLVDPNvpvgSCTKDYVEI-NGE--------KYCG-ERSQFVV 418
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSD----NCEYDYVEIyDGPsasspllgRFCGsEAPPPVI 76

                           90       100
                   ....*....|....*....|....*.
gi 7363445     419 SSNSSKITVHFHSDHSYTDTGFLAEY 444
Cdd:smart00042  77 SSSSNSLTLTFVSDSSVQKRGFSARY 102
CUB pfam00431
CUB domain;
340-444 1.47e-19

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 84.65  E-value: 1.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445    340 CGGFLSDTQGTFSSPYYPGHYPPNINCTWNIKVPNNRNVKVRFKLFYLVDPNvpvgSCTKDYVEI---------NGEKYC 410
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHD----ECGYDYVEIrdgpsasspLLGRFC 76

                          90       100       110
                  ....*....|....*....|....*....|....
gi 7363445    411 GERSQFVVSSNSSKITVHFHSDHSYTDTGFLAEY 444
Cdd:pfam00431  77 GSGIPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 227-332 3.82e-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: 83.62  E-value: 3.82e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445  227 RFTTPGFPNsPYPAHARCQWVLRGDADSVLSLTFRSFDVAPCDEHGSDLVTVYDSLSPMEPHaVVRLCGTFSPSynlTFL 306
Cdd:cd00041  12 TISSPNYPN-NYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYDGPSTSSPL-LGRFCGSTLPP---PII 86

                        90       100
                ....*....|....*....|....*.
gi 7363445  307 SSQNVFLVTLITNTDRRHPGFEATFF 332
Cdd:cd00041  87 SSGNSLTVRFRSDSSVTGRGFKATYS 112
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 227-331 3.36e-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: 68.96  E-value: 3.36e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445     227 RFTTPGFPNsPYPAHARCQWVLRGDADSVLSLTFRSFDVAPCDEHGSDLVTVYDSLSPMEPHaVVRLCGTFSPsyNLTFL 306
Cdd:smart00042   2 TITSPNYPQ-SYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYDGPSASSPL-LGRFCGSEAP--PPVIS 77

                           90       100
                   ....*....|....*....|....*
gi 7363445     307 SSQNVFLVTLITNTDRRHPGFEATF 331
Cdd:smart00042  78 SSSNSLTLTFVSDSSVQKRGFSARY 102
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 525-559 2.71e-12

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: 61.45  E-value: 2.71e-12
                        10        20        30
                ....*....|....*....|....*....|....*
gi 7363445  525 CPAGSFKCSNGKCLPQSQKCNGKDNCGDGSDEASC 559
Cdd:cd00112   1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
 88-178 4.46e-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: 4.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445     88 KVFNGHLRITNEIFLDAYENSTSTEFISLASQVKEALKLLYNEVPvLGPYHKKSAVTAFS--EGSVIAYYWSEFsIPPHL 165
Cdd:pfam01390   1 QYYTGSFKITNLQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSS-LRKQYIKSHVLRLRpdGGSVVVDVVLVF-RFPST 78

                          90
                  ....*....|...
gi 7363445    166 AEEVDRAMAVERV 178
Cdd:pfam01390  79 EPALDREKLIEEI 91
CUB pfam00431
CUB domain;
227-331 1.29e-11

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 61.93  E-value: 1.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445    227 RFTTPGFPNsPYPAHARCQWVLRGDADSVLSLTFRSFDVAPCDEHGSDLVTVYDSLSPMEPhAVVRLCGTFSPsynLTFL 306
Cdd:pfam00431  11 SISSPNYPN-PYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRDGPSASSP-LLGRFCGSGIP---EDIV 85

                          90       100
                  ....*....|....*....|....*
gi 7363445    307 SSQNVFLVTLITNTDRRHPGFEATF 331
Cdd:pfam00431  86 SSSNQMTIKFVSDASVQKRGFKATY 110
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 525-556 3.06e-11

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: 58.41  E-value: 3.06e-11
                           10        20        30
                   ....*....|....*....|....*....|..
gi 7363445     525 CPAGSFKCSNGKCLPQSQKCNGKDNCGDGSDE 556
Cdd:smart00192   2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 492-523 1.86e-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: 1.86e-10
                        10        20        30
                ....*....|....*....|....*....|..
gi 7363445  492 HQFTCKNQFCKPLFWVCDSVNDCGDGSDEEGC 523
Cdd:cd00112   4 NEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 454-486 4.40e-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: 55.29  E-value: 4.40e-10
                        10        20        30
                ....*....|....*....|....*....|...
gi 7363445  454 PGMFMCKTGRCIRKELRCDGWADCPDYSDERYC 486
Cdd:cd00112   3 PNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 636-827 4.88e-10

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 59.69  E-value: 4.88e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445  636 GQGHLCGASLISPDWLVSAAHCFQDDKNFKYsdYTMWTAFLGLLDQSKRSASGVqelklkRIITHPSF-NDFTFDYDIAL 714
Cdd:COG3591   9 GGGGVCTGTLIGPNLVLTAGHCVYDGAGGGW--ATNIVFVPGYNGGPYGTATAT------RFRVPPGWvASGDAGYDYAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7363445  715 LELEKSVeySTVVRPICLPDATHVfPAGKAIWVTGWGhtkeGGTGALILQKGEIRVINQTTcedlmpqqitprmmcvGFL 794
Cdd:COG3591  81 LRLDEPL--GDTTGWLGLAFNDAP-LAGEPVTIIGYP----GDRPKDLSLDCSGRVTGVQG----------------NRL 137

                       170       180       190
                ....*....|....*....|....*....|...
gi 7363445  795 SGGVDSCQGDSGGPLSSAEkDGRMFQAGVVSWG 827
Cdd:COG3591 138 SYDCDTTGGSSGSPVLDDS-DGGGRVVGVHSAG 169
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 487-520 4.75e-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: 52.25  E-value: 4.75e-09
                           10        20        30
                   ....*....|....*....|....*....|....
gi 7363445     487 RCNAtHQFTCKNQFCKPLFWVCDSVNDCGDGSDE 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 6.62e-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: 51.87  E-value: 6.62e-09
                           10        20        30
                   ....*....|....*....|....*....|
gi 7363445     454 PGMFMCKTGRCIRKELRCDGWADCPDYSDE 483
Cdd:smart00192   4 PGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
525-559 2.27e-08

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 50.32  E-value: 2.27e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 7363445    525 CPAGSFKCSNGKCLPQSQKCNGKDNCGDGSDEASC 559
Cdd:pfam00057   3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 567-602 3.62e-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: 3.62e-08
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 7363445  567 CTKYTYRCQNGLCLSKGNpECDGKTDCSDGSDEKNC 602
Cdd:cd00112   1 CPPNEFRCANGRCIPSSW-VCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
492-523 5.11e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 46.86  E-value: 5.11e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 7363445    492 HQFTCKNQFCKPLFWVCDSVNDCGDGSDEEGC 523
Cdd:pfam00057   6 NEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 567-599 9.13e-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: 43.01  E-value: 9.13e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 7363445     567 CTKYTYRCQNGLCLSKGNpECDGKTDCSDGSDE 599
Cdd:smart00192   2 CPPGEFQCDNGRCIPSSW-VCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
454-486 9.49e-06

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 43.01  E-value: 9.49e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 7363445    454 PGMFMCKTGRCIRKELRCDGWADCPDYSDERYC 486
Cdd:pfam00057   5 PNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
572-602 3.07e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 38.77  E-value: 3.07e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 7363445    572 YRCQNGLCLSkGNPECDGKTDCSDGSDEKNC 602
Cdd:pfam00057   8 FQCGSGECIP-RSWVCDGDPDCGDGSDEENC 37
PRKCSH-like pfam12999
Glucosidase II beta subunit-like; The sequences found in this family are similar to a region ...
 472-526 4.33e-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: 39.00  E-value: 4.33e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7363445    472 DGWADCPDYSDERycRCNATH--QFTCKNQFCKPLFWVCDSVND-------CGDGSDEEGCSCP 526
Cdd:pfam12999  55 DDYCDCPDGSDEP--GTNACSngKFYCANEGFIPGYIPSFKVDDgvcdydiCCDGSDEALGKCP 116
CUB_2 pfam02408
CUB-like domain; This is a family of hypothetical C. elegans proteins. The aligned region has ...
 360-427 6.50e-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: 37.36  E-value: 6.50e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7363445    360 YPPNINCTWNIKVPNNRNVKVRFKLFYLVDPNVPVGSCTKDYVEINGEKYcgerSQFVVSSNSSKITV 427
Cdd:pfam02408  38 IPANQNCSWNINVPKGYYAKVIISAKTNDDSSITVTDSLGNSEYVTDSDN----EPYFFVSPSFTINL 101
 
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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