NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|665410108|ref|NP_001163393|]
View 

tequila, isoform F [Drosophila melanogaster]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 2134-2371 3.37e-90

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: 293.03  E-value: 3.37e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108 2134 VVRGNVAQRGRHPWQATIRTRGrggiSSHWCGAVVISKRHLLTAAHCLYGSPKGAYFVRVGDHYANIAESSEVDSFIENW 2213
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTG----GRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108 2214 YLHENFRKGThMNNDIALVVLKTPLKFSDYVQPICLPDKNAELVEDRKCTISGWGSIKSGVSTPaQVLGSAELPILADHV 2293
Cdd:cd00190    77 IVHPNYNPST-YDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLP-DVLQEVNVPIVSNAE 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665410108 2294 CKQSNVYGSAMSEGMFCAGSMDESVDACEGDSGGPLVCSDDDGETLYGLISWGQHCGFKNRPGVYVRVNHYIDWIYEK 2371
Cdd:cd00190   155 CKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 1969-2067 2.73e-40

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


:

Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 144.79  E-value: 2.73e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108   1969 RLEGGRNSNEGRLEVKHHGVWGSVCDDDFNLKSAQVACNSMGFFGPAKIEKNI-FGNSNGPIWLDQVMCFGNETSIDQCN 2047
Cdd:smart00202    2 RLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAyFGPGSGPIWLDNVRCSGTEASLSDCP 81

                            90       100
                    ....*....|....*....|
gi 665410108   2048 HWNWGEHNCNHTEDVALHCS 2067
Cdd:smart00202   82 HSGWGSHNCSHGEDAGVVCS 101
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 1816-1918 3.48e-36

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


:

Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 133.24  E-value: 3.48e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108   1816 VRLSGGESPNMGRIEVKANGQWGYVCDDKFGLKDADVVCRELGFQMGAQEVRGSSFyapPNQDFNYLMDEVECHGNETKL 1895
Cdd:smart00202    1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYF---GPGSGPIWLDNVRCSGTEASL 77

                            90       100
                    ....*....|....*....|...
gi 665410108   1896 GQCAFKGWGVHNCGVDEVAGVTC 1918
Cdd:smart00202   78 SDCPHSGWGSHNCSHGEDAGVVC 100
ChtBD2 smart00494
Chitin-binding domain type 2;
136-184 6.16e-12

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 62.08  E-value: 6.16e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 665410108    136 PKCQPGVNGLQPHPSDCSKFLNCANGQAFIMDCAPGTAFSPASLVCVHK 184
Cdd:smart00494    1 NECPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 65-115 2.29e-11

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


:

Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 60.89  E-value: 2.29e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 665410108    65 CPPHFTGLVAYPHDCHRYVNCFDGSPTIQTCSPGTLFNDRTQVCDHPSNVV 115
Cdd:pfam01607    1 CAGKEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVV 51
ChtBD2 smart00494
Chitin-binding domain type 2;
608-654 6.43e-11

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 59.38  E-value: 6.43e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 665410108    608 CPPGASGNHAHPFDCTKFLECSNGQTFVKNCGPGTAFSTAKHICDHA 654
Cdd:smart00494    3 CPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 1029-1325 2.91e-10

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


The actual alignment was detected with superfamily member pfam09606:

Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 65.80  E-value: 2.91e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108  1029 GGNQPPGKYQAPyySNGGYPTPSQNNGGYQT-------------------PSQNN--GGYQAPFQNNGGYQPSYQGNGGY 1087
Cdd:pfam09606   92 QGTRPQMMGPMG--PGPGGPMGQQMGGPGTAsnllaslgrpqmpmggagfPSQMSrvGRMQPGGQAGGMMQPSSGQPGSG 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108  1088 TPTYQNPFEGYHQPnqSSYQTNGGYQPPLpphgGYQPPSQTY---------GGFQQPNRTYEDFHNPSQTVGGfQPPYSV 1158
Cdd:pfam09606  170 TPNQMGPNGGPGQG--QAGGMNGGQQGPM----GGQMPPQMGvpgmpgpadAGAQMGQQAQANGGMNPQQMGG-APNQVA 242

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108  1159 KGGYQP-----HNQLNGGYNQPNQSSSFQANGGYQ--------PPSQvnrGYQTSFESNGGYQPPLETNKGHQVPSQING 1225
Cdd:pfam09606  243 MQQQQPqqqgqQSQLGMGINQMQQMPQGVGGGAGQggpgqpmgPPGQ---QPGAMPNVMSIGDQNNYQQQQTRQQQQQQG 319

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108  1226 GYQP---------------RVDGNRGYQPPNELNGGYQPPNELNGAYPAPSQLNGGYQPPLEGNLgyRPLSQQNSGYQPP 1290
Cdd:pfam09606  320 GNHPaahqqqmnqsvgqggQVVALGGLNHLETWNPGNFGGLGANPMQRGQPGMMSSPSPVPGQQV--RQVTPNQFMRQSP 397

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 665410108  1291 QPSTGGYQPPFQSTGSGHYPGQdapyaIPTPLLCP 1325
Cdd:pfam09606  398 QPSVPSPQGPGSQPPQSHPGGM-----IPSPALIP 427
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 942-993 1.01e-08

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


:

Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 53.19  E-value: 1.01e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 665410108   942 CPPQAQGYYLHPFDCTKYIVCWEKQTHIESCPQGEAFSISQQKCVARDKITQ 993
Cdd:pfam01607    1 CAGKEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVVD 52
ChtBD2 smart00494
Chitin-binding domain type 2;
521-567 2.13e-08

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 52.06  E-value: 2.13e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 665410108    521 CPPQAQGLYLHPFDCTKYVRCWNQQTFIESCTPGEIFSFSNQKCVPK 567
Cdd:smart00494    3 CPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
ChtBD2 smart00494
Chitin-binding domain type 2;
709-752 2.81e-06

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 46.28  E-value: 2.81e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 665410108    709 CPSGVNGQFVHPFDQTKFLLCQAGKLAVQSCQSGYVFSISKSIC 752
Cdd:smart00494    3 CPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTC 46
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1924-1957 3.59e-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: 45.32  E-value: 3.59e-06
                            10        20        30
                    ....*....|....*....|....*....|....
gi 665410108   1924 KCPNNYWLCHTSKeCIPPAFVCDNTPDCADKSDE 1957
Cdd:smart00192    1 TCPPGEFQCDNGR-CIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1780-1809 5.41e-06

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


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 44.89  E-value: 5.41e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 665410108 1780 FDCGNGQCLKKEEICDGKKNCPNGKDEANC 1809
Cdd:cd00112     6 FRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
ChtBD2 smart00494
Chitin-binding domain type 2;
284-327 3.30e-05

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 43.20  E-value: 3.30e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 665410108    284 CPVGAVGQFVHPFDQTKFLSCKDGKSAVQNCQPNYVFSISRRYC 327
Cdd:smart00494    3 CPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTC 46
ChtBD2 smart00494
Chitin-binding domain type 2;
1474-1518 5.24e-05

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 42.43  E-value: 5.24e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 665410108   1474 CPEGITGTLPHPRVPTKYLRCGPGQAEMYDCPSQQIFSVSRRVCV 1518
Cdd:smart00494    3 CPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCD 47
ChtBD2 smart00494
Chitin-binding domain type 2;
215-261 1.69e-04

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 41.28  E-value: 1.69e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 665410108    215 CPPGTRGLRPHPHDVHKYLRCgIGVKPQVEQCPRGHIFDGSSSVCVY 261
Cdd:smart00494    3 CPGRGDGLYPHPTDCSKYYQC-SNGRPIVGSCPAGLVFNPATQTCDW 48
ChtBD2 smart00494
Chitin-binding domain type 2;
1324-1369 1.79e-04

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 41.28  E-value: 1.79e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 665410108   1324 CPEKISGLFPNPFDATGYLTCIDGHTLPRQCQPLDVFSVSQGYCLP 1369
Cdd:smart00494    3 CPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
ChtBD2 smart00494
Chitin-binding domain type 2;
864-909 8.57e-03

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 36.27  E-value: 8.57e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 665410108    864 ECPSVLRGNYPYPFHAGHFVNCQNGHLQIVSCPPTALYSLSQRECV 909
Cdd:smart00494    2 ECPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCD 47
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 782-829 9.14e-03

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


:

Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 36.24  E-value: 9.14e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 665410108   782 CPDGTNGLHLYPYDAGKYVRCSDGGKmSIQSCENQMAFSLSQRACRPS 829
Cdd:pfam01607    1 CAGKEDGYYADPGDCSKYYVCSNGEA-VEFTCPNGLVFDPTLGICDYP 47
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 2134-2371 3.37e-90

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: 293.03  E-value: 3.37e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108 2134 VVRGNVAQRGRHPWQATIRTRGrggiSSHWCGAVVISKRHLLTAAHCLYGSPKGAYFVRVGDHYANIAESSEVDSFIENW 2213
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTG----GRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108 2214 YLHENFRKGThMNNDIALVVLKTPLKFSDYVQPICLPDKNAELVEDRKCTISGWGSIKSGVSTPaQVLGSAELPILADHV 2293
Cdd:cd00190    77 IVHPNYNPST-YDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLP-DVLQEVNVPIVSNAE 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665410108 2294 CKQSNVYGSAMSEGMFCAGSMDESVDACEGDSGGPLVCSDDDGETLYGLISWGQHCGFKNRPGVYVRVNHYIDWIYEK 2371
Cdd:cd00190   155 CKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 2133-2368 2.85e-87

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: 284.57  E-value: 2.85e-87
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108   2133 RVVRGNVAQRGRHPWQATIRTRGRggisSHWCGAVVISKRHLLTAAHCLYGSPKGAYFVRVGDHYANIAESSEVDSFIEN 2212
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQYGGG----RHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEGQVIKVSKV 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108   2213 wYLHENFRKGThMNNDIALVVLKTPLKFSDYVQPICLPDKNAELVEDRKCTISGWGSIKSGVSTPAQVLGSAELPILADH 2292
Cdd:smart00020   77 -IIHPNYNPST-YDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNA 154

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665410108   2293 VCKQSNVYGSAMSEGMFCAGSMDESVDACEGDSGGPLVCSDDDGeTLYGLISWGQHCGFKNRPGVYVRVNHYIDWI 2368
Cdd:smart00020  155 TCRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGRW-VLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
2134-2368 1.35e-60

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 207.68  E-value: 1.35e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108  2134 VVRGNVAQRGRHPWQATIRTRGrggiSSHWCGAVVISKRHLLTAAHCLYGSPkgAYFVRVGDHYANIAESSEVDSFIENW 2213
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQLSS----GKHFCGGSLISENWVLTAAHCVSGAS--DVKVVLGAHNIVLREGGEQKFDVEKI 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108  2214 YLHENFRKGTHmNNDIALVVLKTPLKFSDYVQPICLPDKNAELVEDRKCTISGWGSIKSGVstPAQVLGSAELPILADHV 2293
Cdd:pfam00089   75 IVHPNYNPDTL-DNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRET 151

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665410108  2294 CKQSnvYGSAMSEGMFCAGSmdESVDACEGDSGGPLVCSDddgETLYGLISWGQHCGFKNRPGVYVRVNHYIDWI 2368
Cdd:pfam00089  152 CRSA--YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSD---GELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 2133-2374 8.72e-58

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 201.42  E-value: 8.72e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108 2133 RVVRGNVAQRGRHPWQATIRTRGrgGISSHWCGAVVISKRHLLTAAHCLYGSPKGAYFVRVGDHyaNIAESSEVDSFIEN 2212
Cdd:COG5640    30 AIVGGTPATVGEYPWMVALQSSN--GPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGST--DLSTSGGTVVKVAR 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108 2213 WYLHENFRKGThMNNDIALVVLKTPLkfsDYVQPICLPDKNAELVEDRKCTISGWGSIKSGVSTPAQVLGSAELPILADH 2292
Cdd:COG5640   106 IVVHPDYDPAT-PGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSDA 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108 2293 VCkqsNVYGSAMSEGMFCAGSMDESVDACEGDSGGPLVCSDDDGETLYGLISWGQHCGFKNRPGVYVRVNHYIDWIYEKI 2372
Cdd:COG5640   182 TC---AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258


                  ..
gi 665410108 2373 NE 2374
Cdd:COG5640   259 GG 260
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 1969-2067 2.73e-40

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 144.79  E-value: 2.73e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108   1969 RLEGGRNSNEGRLEVKHHGVWGSVCDDDFNLKSAQVACNSMGFFGPAKIEKNI-FGNSNGPIWLDQVMCFGNETSIDQCN 2047
Cdd:smart00202    2 RLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAyFGPGSGPIWLDNVRCSGTEASLSDCP 81

                            90       100
                    ....*....|....*....|
gi 665410108   2048 HWNWGEHNCNHTEDVALHCS 2067
Cdd:smart00202   82 HSGWGSHNCSHGEDAGVVCS 101
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 1816-1918 3.48e-36

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 133.24  E-value: 3.48e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108   1816 VRLSGGESPNMGRIEVKANGQWGYVCDDKFGLKDADVVCRELGFQMGAQEVRGSSFyapPNQDFNYLMDEVECHGNETKL 1895
Cdd:smart00202    1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYF---GPGSGPIWLDNVRCSGTEASL 77

                            90       100
                    ....*....|....*....|...
gi 665410108   1896 GQCAFKGWGVHNCGVDEVAGVTC 1918
Cdd:smart00202   78 SDCPHSGWGSHNCSHGEDAGVVC 100
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 1821-1919 1.19e-34

Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular domains. These domains are found in several extracellular receptors and may be involved in protein-protein interactions.


Pssm-ID: 459844  Cd Length: 98  Bit Score: 128.65  E-value: 1.19e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108  1821 GESPNMGRIEVKANGQWGYVCDDKFGLKDADVVCRELGFQMGAQEVRGSSfYAPPNQDFNYLMDEVECHGNETKLGQCAF 1900
Cdd:pfam00530    1 GSSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGCGGAVSAPSGCS-YFGPGSTGPIWLDDVRCSGNETSLWQCPH 79

                           90
                   ....*....|....*....
gi 665410108  1901 KGWGVHNCGVDEVAGVTCK 1919
Cdd:pfam00530   80 RPWGNHNCSHSEDAGVICS 98
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 1973-2067 7.68e-34

Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular domains. These domains are found in several extracellular receptors and may be involved in protein-protein interactions.


Pssm-ID: 459844  Cd Length: 98  Bit Score: 126.34  E-value: 7.68e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108  1973 GRNSNEGRLEVKHHGVWGSVCDDDFNLKSAQVACNSMGFFGPAKI---EKNIFGNSNGPIWLDQVMCFGNETSIDQCNHW 2049
Cdd:pfam00530    1 GSSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGCGGAVSApsgCSYFGPGSTGPIWLDDVRCSGNETSLWQCPHR 80

                           90
                   ....*....|....*...
gi 665410108  2050 NWGEHNCNHTEDVALHCS 2067
Cdd:pfam00530   81 PWGNHNCSHSEDAGVICS 98
ChtBD2 smart00494
Chitin-binding domain type 2;
136-184 6.16e-12

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 62.08  E-value: 6.16e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 665410108    136 PKCQPGVNGLQPHPSDCSKFLNCANGQAFIMDCAPGTAFSPASLVCVHK 184
Cdd:smart00494    1 NECPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 138-189 1.33e-11

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 61.28  E-value: 1.33e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 665410108   138 CQPGVNGLQPHPSDCSKFLNCANGQAFIMDCAPGTAFSPASLVCVHKD-LAKC 189
Cdd:pfam01607    1 CAGKEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDnVVDC 53
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 65-115 2.29e-11

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 60.89  E-value: 2.29e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 665410108    65 CPPHFTGLVAYPHDCHRYVNCFDGSPTIQTCSPGTLFNDRTQVCDHPSNVV 115
Cdd:pfam01607    1 CAGKEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVV 51
ChtBD2 smart00494
Chitin-binding domain type 2;
608-654 6.43e-11

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 59.38  E-value: 6.43e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 665410108    608 CPPGASGNHAHPFDCTKFLECSNGQTFVKNCGPGTAFSTAKHICDHA 654
Cdd:smart00494    3 CPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 1029-1325 2.91e-10

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 65.80  E-value: 2.91e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108  1029 GGNQPPGKYQAPyySNGGYPTPSQNNGGYQT-------------------PSQNN--GGYQAPFQNNGGYQPSYQGNGGY 1087
Cdd:pfam09606   92 QGTRPQMMGPMG--PGPGGPMGQQMGGPGTAsnllaslgrpqmpmggagfPSQMSrvGRMQPGGQAGGMMQPSSGQPGSG 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108  1088 TPTYQNPFEGYHQPnqSSYQTNGGYQPPLpphgGYQPPSQTY---------GGFQQPNRTYEDFHNPSQTVGGfQPPYSV 1158
Cdd:pfam09606  170 TPNQMGPNGGPGQG--QAGGMNGGQQGPM----GGQMPPQMGvpgmpgpadAGAQMGQQAQANGGMNPQQMGG-APNQVA 242

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108  1159 KGGYQP-----HNQLNGGYNQPNQSSSFQANGGYQ--------PPSQvnrGYQTSFESNGGYQPPLETNKGHQVPSQING 1225
Cdd:pfam09606  243 MQQQQPqqqgqQSQLGMGINQMQQMPQGVGGGAGQggpgqpmgPPGQ---QPGAMPNVMSIGDQNNYQQQQTRQQQQQQG 319

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108  1226 GYQP---------------RVDGNRGYQPPNELNGGYQPPNELNGAYPAPSQLNGGYQPPLEGNLgyRPLSQQNSGYQPP 1290
Cdd:pfam09606  320 GNHPaahqqqmnqsvgqggQVVALGGLNHLETWNPGNFGGLGANPMQRGQPGMMSSPSPVPGQQV--RQVTPNQFMRQSP 397

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 665410108  1291 QPSTGGYQPPFQSTGSGHYPGQdapyaIPTPLLCP 1325
Cdd:pfam09606  398 QPSVPSPQGPGSQPPQSHPGGM-----IPSPALIP 427
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 608-659 5.38e-09

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 53.96  E-value: 5.38e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 665410108   608 CPPGASGNHAHPFDCTKFLECSNGQTFVKNCGPGTAFSTAKHICDHA-NQVDC 659
Cdd:pfam01607    1 CAGKEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPdNVVDC 53
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 942-993 1.01e-08

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 53.19  E-value: 1.01e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 665410108   942 CPPQAQGYYLHPFDCTKYIVCWEKQTHIESCPQGEAFSISQQKCVARDKITQ 993
Cdd:pfam01607    1 CAGKEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVVD 52
ChtBD2 smart00494
Chitin-binding domain type 2;
65-111 1.07e-08

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 53.22  E-value: 1.07e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 665410108     65 CPPHFTGLVAYPHDCHRYVNCFDGSPTIQTCSPGTLFNDRTQVCDHP 111
Cdd:smart00494    3 CPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
ChtBD2 smart00494
Chitin-binding domain type 2;
521-567 2.13e-08

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 52.06  E-value: 2.13e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 665410108    521 CPPQAQGLYLHPFDCTKYVRCWNQQTFIESCTPGEIFSFSNQKCVPK 567
Cdd:smart00494    3 CPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 521-569 3.04e-08

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 52.03  E-value: 3.04e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 665410108   521 CPPQAQGLYLHPFDCTKYVRCWNQQTFIESCTPGEIFSFSNQKCVPKEQ 569
Cdd:pfam01607    1 CAGKEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDN 49
ChtBD2 smart00494
Chitin-binding domain type 2;
942-988 3.68e-08

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 51.68  E-value: 3.68e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 665410108    942 CPPQAQGYYLHPFDCTKYIVCWEKQTHIESCPQGEAFSISQQKCVAR 988
Cdd:smart00494    3 CPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
ChtBD2 smart00494
Chitin-binding domain type 2;
709-752 2.81e-06

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 46.28  E-value: 2.81e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 665410108    709 CPSGVNGQFVHPFDQTKFLLCQAGKLAVQSCQSGYVFSISKSIC 752
Cdd:smart00494    3 CPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTC 46
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1924-1957 3.59e-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: 45.32  E-value: 3.59e-06
                            10        20        30
                    ....*....|....*....|....*....|....
gi 665410108   1924 KCPNNYWLCHTSKeCIPPAFVCDNTPDCADKSDE 1957
Cdd:smart00192    1 TCPPGEFQCDNGR-CIPSSWVCDGVDDCGDGSDE 33
PTZ00395 PTZ00395
Sec24-related protein; Provisional
 1029-1184 4.66e-06

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 52.38  E-value: 4.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108 1029 GGNQPPGKYQAPYYSNGGYPTPSQNNGGYQTPSQNNGGYQAPFQNNGGYQPSYQGNGGYTPT-YQNPfegyhqPNQSSYQ 1107
Cdd:PTZ00395  381 GGPHSNASYNCAAYSNAAQSNAAQSNAGFSNAGYSNPGNSNPGYNNAPNSNTPYNNPPNSNTpYSNP------PNSNPPY 454

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108 1108 TNGGY------QPPL---PPHGGYQPPSQTYGGFQQPNRTYEDFHNPSQTVGGFQPPYSVKGgyqpHNQLNGGYNQPNQS 1178
Cdd:PTZ00395  455 SNLPYsntpysNAPLsnaPPSSAKDHHSAYHAAYQHRAANQPAANLPTANQPAANNFHGAAG----NSVGNPFASRPFGS 530


                  ....*.
gi 665410108 1179 SSFQAN 1184
Cdd:PTZ00395  531 APYGGN 536
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1780-1809 5.41e-06

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


Pssm-ID: 238060  Cd Length: 35  Bit Score: 44.89  E-value: 5.41e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 665410108 1780 FDCGNGQCLKKEEICDGKKNCPNGKDEANC 1809
Cdd:cd00112     6 FRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1925-1957 6.27e-06

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


Pssm-ID: 238060  Cd Length: 35  Bit Score: 44.89  E-value: 6.27e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 665410108 1925 CPNNYWLCHtSKECIPPAFVCDNTPDCADKSDE 1957
Cdd:cd00112     1 CPPNEFRCA-NGRCIPSSWVCDGEDDCGDGSDE 32
ChtBD2 smart00494
Chitin-binding domain type 2;
284-327 3.30e-05

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 43.20  E-value: 3.30e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 665410108    284 CPVGAVGQFVHPFDQTKFLSCKDGKSAVQNCQPNYVFSISRRYC 327
Cdd:smart00494    3 CPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTC 46
ChtBD2 smart00494
Chitin-binding domain type 2;
1474-1518 5.24e-05

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 42.43  E-value: 5.24e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 665410108   1474 CPEGITGTLPHPRVPTKYLRCGPGQAEMYDCPSQQIFSVSRRVCV 1518
Cdd:smart00494    3 CPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCD 47
ChtBD2 smart00494
Chitin-binding domain type 2;
215-261 1.69e-04

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 41.28  E-value: 1.69e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 665410108    215 CPPGTRGLRPHPHDVHKYLRCgIGVKPQVEQCPRGHIFDGSSSVCVY 261
Cdd:smart00494    3 CPGRGDGLYPHPTDCSKYYQC-SNGRPIVGSCPAGLVFNPATQTCDW 48
ChtBD2 smart00494
Chitin-binding domain type 2;
1324-1369 1.79e-04

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 41.28  E-value: 1.79e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 665410108   1324 CPEKISGLFPNPFDATGYLTCIDGHTLPRQCQPLDVFSVSQGYCLP 1369
Cdd:smart00494    3 CPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1780-1806 3.98e-04

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


Pssm-ID: 197566  Cd Length: 33  Bit Score: 39.54  E-value: 3.98e-04
                            10        20
                    ....*....|....*....|....*..
gi 665410108   1780 FDCGNGQCLKKEEICDGKKNCPNGKDE 1806
Cdd:smart00192    7 FQCDNGRCIPSSWVCDGVDDCGDGSDE 33
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 1474-1524 3.58e-03

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 37.39  E-value: 3.58e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 665410108  1474 CPEGITGTLPHPRVPTKYLRCGPGQAEMYDCPSQQIFSVSRRVCVLDDKLS 1524
Cdd:pfam01607    1 CAGKEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVV 51
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 215-261 5.47e-03

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 37.01  E-value: 5.47e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 665410108   215 CPPGTRGLRPHPHDVHKYLRCGIGvKPQVEQCPRGHIFDGSSSVCVY 261
Cdd:pfam01607    1 CAGKEDGYYADPGDCSKYYVCSNG-EAVEFTCPNGLVFDPTLGICDY 46
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1924-1957 6.29e-03

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 36.46  E-value: 6.29e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 665410108  1924 KCPNNYWLCHTSkECIPPAFVCDNTPDCADKSDE 1957
Cdd:pfam00057    2 TCSPNEFQCGSG-ECIPRSWVCDGDPDCGDGSDE 34
ChtBD2 smart00494
Chitin-binding domain type 2;
864-909 8.57e-03

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 36.27  E-value: 8.57e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 665410108    864 ECPSVLRGNYPYPFHAGHFVNCQNGHLQIVSCPPTALYSLSQRECV 909
Cdd:smart00494    2 ECPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCD 47
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 782-829 9.14e-03

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 36.24  E-value: 9.14e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 665410108   782 CPDGTNGLHLYPYDAGKYVRCSDGGKmSIQSCENQMAFSLSQRACRPS 829
Cdd:pfam01607    1 CAGKEDGYYADPGDCSKYYVCSNGEA-VEFTCPNGLVFDPTLGICDYP 47
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 2134-2371 3.37e-90

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: 293.03  E-value: 3.37e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108 2134 VVRGNVAQRGRHPWQATIRTRGrggiSSHWCGAVVISKRHLLTAAHCLYGSPKGAYFVRVGDHYANIAESSEVDSFIENW 2213
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTG----GRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108 2214 YLHENFRKGThMNNDIALVVLKTPLKFSDYVQPICLPDKNAELVEDRKCTISGWGSIKSGVSTPaQVLGSAELPILADHV 2293
Cdd:cd00190    77 IVHPNYNPST-YDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLP-DVLQEVNVPIVSNAE 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665410108 2294 CKQSNVYGSAMSEGMFCAGSMDESVDACEGDSGGPLVCSDDDGETLYGLISWGQHCGFKNRPGVYVRVNHYIDWIYEK 2371
Cdd:cd00190   155 CKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 2133-2368 2.85e-87

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: 284.57  E-value: 2.85e-87
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108   2133 RVVRGNVAQRGRHPWQATIRTRGRggisSHWCGAVVISKRHLLTAAHCLYGSPKGAYFVRVGDHYANIAESSEVDSFIEN 2212
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQYGGG----RHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEGQVIKVSKV 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108   2213 wYLHENFRKGThMNNDIALVVLKTPLKFSDYVQPICLPDKNAELVEDRKCTISGWGSIKSGVSTPAQVLGSAELPILADH 2292
Cdd:smart00020   77 -IIHPNYNPST-YDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNA 154

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665410108   2293 VCKQSNVYGSAMSEGMFCAGSMDESVDACEGDSGGPLVCSDDDGeTLYGLISWGQHCGFKNRPGVYVRVNHYIDWI 2368
Cdd:smart00020  155 TCRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGRW-VLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
2134-2368 1.35e-60

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 207.68  E-value: 1.35e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108  2134 VVRGNVAQRGRHPWQATIRTRGrggiSSHWCGAVVISKRHLLTAAHCLYGSPkgAYFVRVGDHYANIAESSEVDSFIENW 2213
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQLSS----GKHFCGGSLISENWVLTAAHCVSGAS--DVKVVLGAHNIVLREGGEQKFDVEKI 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108  2214 YLHENFRKGTHmNNDIALVVLKTPLKFSDYVQPICLPDKNAELVEDRKCTISGWGSIKSGVstPAQVLGSAELPILADHV 2293
Cdd:pfam00089   75 IVHPNYNPDTL-DNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRET 151

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665410108  2294 CKQSnvYGSAMSEGMFCAGSmdESVDACEGDSGGPLVCSDddgETLYGLISWGQHCGFKNRPGVYVRVNHYIDWI 2368
Cdd:pfam00089  152 CRSA--YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSD---GELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 2133-2374 8.72e-58

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 201.42  E-value: 8.72e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108 2133 RVVRGNVAQRGRHPWQATIRTRGrgGISSHWCGAVVISKRHLLTAAHCLYGSPKGAYFVRVGDHyaNIAESSEVDSFIEN 2212
Cdd:COG5640    30 AIVGGTPATVGEYPWMVALQSSN--GPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGST--DLSTSGGTVVKVAR 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108 2213 WYLHENFRKGThMNNDIALVVLKTPLkfsDYVQPICLPDKNAELVEDRKCTISGWGSIKSGVSTPAQVLGSAELPILADH 2292
Cdd:COG5640   106 IVVHPDYDPAT-PGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSDA 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108 2293 VCkqsNVYGSAMSEGMFCAGSMDESVDACEGDSGGPLVCSDDDGETLYGLISWGQHCGFKNRPGVYVRVNHYIDWIYEKI 2372
Cdd:COG5640   182 TC---AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTA 258


                  ..
gi 665410108 2373 NE 2374
Cdd:COG5640   259 GG 260
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 1969-2067 2.73e-40

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 144.79  E-value: 2.73e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108   1969 RLEGGRNSNEGRLEVKHHGVWGSVCDDDFNLKSAQVACNSMGFFGPAKIEKNI-FGNSNGPIWLDQVMCFGNETSIDQCN 2047
Cdd:smart00202    2 RLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAyFGPGSGPIWLDNVRCSGTEASLSDCP 81

                            90       100
                    ....*....|....*....|
gi 665410108   2048 HWNWGEHNCNHTEDVALHCS 2067
Cdd:smart00202   82 HSGWGSHNCSHGEDAGVVCS 101
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 1816-1918 3.48e-36

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 133.24  E-value: 3.48e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108   1816 VRLSGGESPNMGRIEVKANGQWGYVCDDKFGLKDADVVCRELGFQMGAQEVRGSSFyapPNQDFNYLMDEVECHGNETKL 1895
Cdd:smart00202    1 VRLVGGGSPCEGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGSAYF---GPGSGPIWLDNVRCSGTEASL 77

                            90       100
                    ....*....|....*....|...
gi 665410108   1896 GQCAFKGWGVHNCGVDEVAGVTC 1918
Cdd:smart00202   78 SDCPHSGWGSHNCSHGEDAGVVC 100
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 1821-1919 1.19e-34

Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular domains. These domains are found in several extracellular receptors and may be involved in protein-protein interactions.


Pssm-ID: 459844  Cd Length: 98  Bit Score: 128.65  E-value: 1.19e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108  1821 GESPNMGRIEVKANGQWGYVCDDKFGLKDADVVCRELGFQMGAQEVRGSSfYAPPNQDFNYLMDEVECHGNETKLGQCAF 1900
Cdd:pfam00530    1 GSSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGCGGAVSAPSGCS-YFGPGSTGPIWLDDVRCSGNETSLWQCPH 79

                           90
                   ....*....|....*....
gi 665410108  1901 KGWGVHNCGVDEVAGVTCK 1919
Cdd:pfam00530   80 RPWGNHNCSHSEDAGVICS 98
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 1973-2067 7.68e-34

Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular domains. These domains are found in several extracellular receptors and may be involved in protein-protein interactions.


Pssm-ID: 459844  Cd Length: 98  Bit Score: 126.34  E-value: 7.68e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108  1973 GRNSNEGRLEVKHHGVWGSVCDDDFNLKSAQVACNSMGFFGPAKI---EKNIFGNSNGPIWLDQVMCFGNETSIDQCNHW 2049
Cdd:pfam00530    1 GSSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGCGGAVSApsgCSYFGPGSTGPIWLDDVRCSGNETSLWQCPHR 80

                           90
                   ....*....|....*...
gi 665410108  2050 NWGEHNCNHTEDVALHCS 2067
Cdd:pfam00530   81 PWGNHNCSHSEDAGVICS 98
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 2160-2374 1.70e-13

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 71.25  E-value: 1.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108 2160 SSHWCGAVVISKRHLLTAAHCLYGSPKGAYF--VRVGDHYANIAESSEVdsfIENWYLHENFRKGTHMNNDIALVVLKTP 2237
Cdd:COG3591    10 GGGVCTGTLIGPNLVLTAGHCVYDGAGGGWAtnIVFVPGYNGGPYGTAT---ATRFRVPPGWVASGDAGYDYALLRLDEP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108 2238 LkfSDYVQPICLpDKNAELVEDRKCTISGWGSIKSGVSTpaqvlgsaelpilADHVCKQSNVYGSAMSegMFCagsmdes 2317
Cdd:COG3591    87 L--GDTTGWLGL-AFNDAPLAGEPVTIIGYPGDRPKDLS-------------LDCSGRVTGVQGNRLS--YDC------- 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 665410108 2318 vDACEGDSGGPLVCSDDDGETLYGLISWGqHCGFKNRpGVYVRvNHYIDWIYEKINE 2374
Cdd:COG3591   142 -DTTGGSSGSPVLDDSDGGGRVVGVHSAG-GADRANT-GVRLT-SAIVAALRAWASA 194
ChtBD2 smart00494
Chitin-binding domain type 2;
136-184 6.16e-12

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 62.08  E-value: 6.16e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 665410108    136 PKCQPGVNGLQPHPSDCSKFLNCANGQAFIMDCAPGTAFSPASLVCVHK 184
Cdd:smart00494    1 NECPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 138-189 1.33e-11

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 61.28  E-value: 1.33e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 665410108   138 CQPGVNGLQPHPSDCSKFLNCANGQAFIMDCAPGTAFSPASLVCVHKD-LAKC 189
Cdd:pfam01607    1 CAGKEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDnVVDC 53
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 65-115 2.29e-11

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 60.89  E-value: 2.29e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 665410108    65 CPPHFTGLVAYPHDCHRYVNCFDGSPTIQTCSPGTLFNDRTQVCDHPSNVV 115
Cdd:pfam01607    1 CAGKEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVV 51
ChtBD2 smart00494
Chitin-binding domain type 2;
608-654 6.43e-11

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 59.38  E-value: 6.43e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 665410108    608 CPPGASGNHAHPFDCTKFLECSNGQTFVKNCGPGTAFSTAKHICDHA 654
Cdd:smart00494    3 CPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 1029-1325 2.91e-10

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 65.80  E-value: 2.91e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108  1029 GGNQPPGKYQAPyySNGGYPTPSQNNGGYQT-------------------PSQNN--GGYQAPFQNNGGYQPSYQGNGGY 1087
Cdd:pfam09606   92 QGTRPQMMGPMG--PGPGGPMGQQMGGPGTAsnllaslgrpqmpmggagfPSQMSrvGRMQPGGQAGGMMQPSSGQPGSG 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108  1088 TPTYQNPFEGYHQPnqSSYQTNGGYQPPLpphgGYQPPSQTY---------GGFQQPNRTYEDFHNPSQTVGGfQPPYSV 1158
Cdd:pfam09606  170 TPNQMGPNGGPGQG--QAGGMNGGQQGPM----GGQMPPQMGvpgmpgpadAGAQMGQQAQANGGMNPQQMGG-APNQVA 242

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108  1159 KGGYQP-----HNQLNGGYNQPNQSSSFQANGGYQ--------PPSQvnrGYQTSFESNGGYQPPLETNKGHQVPSQING 1225
Cdd:pfam09606  243 MQQQQPqqqgqQSQLGMGINQMQQMPQGVGGGAGQggpgqpmgPPGQ---QPGAMPNVMSIGDQNNYQQQQTRQQQQQQG 319

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108  1226 GYQP---------------RVDGNRGYQPPNELNGGYQPPNELNGAYPAPSQLNGGYQPPLEGNLgyRPLSQQNSGYQPP 1290
Cdd:pfam09606  320 GNHPaahqqqmnqsvgqggQVVALGGLNHLETWNPGNFGGLGANPMQRGQPGMMSSPSPVPGQQV--RQVTPNQFMRQSP 397

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 665410108  1291 QPSTGGYQPPFQSTGSGHYPGQdapyaIPTPLLCP 1325
Cdd:pfam09606  398 QPSVPSPQGPGSQPPQSHPGGM-----IPSPALIP 427
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 608-659 5.38e-09

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 53.96  E-value: 5.38e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 665410108   608 CPPGASGNHAHPFDCTKFLECSNGQTFVKNCGPGTAFSTAKHICDHA-NQVDC 659
Cdd:pfam01607    1 CAGKEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPdNVVDC 53
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 942-993 1.01e-08

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 53.19  E-value: 1.01e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 665410108   942 CPPQAQGYYLHPFDCTKYIVCWEKQTHIESCPQGEAFSISQQKCVARDKITQ 993
Cdd:pfam01607    1 CAGKEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVVD 52
ChtBD2 smart00494
Chitin-binding domain type 2;
65-111 1.07e-08

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 53.22  E-value: 1.07e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 665410108     65 CPPHFTGLVAYPHDCHRYVNCFDGSPTIQTCSPGTLFNDRTQVCDHP 111
Cdd:smart00494    3 CPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
ChtBD2 smart00494
Chitin-binding domain type 2;
521-567 2.13e-08

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 52.06  E-value: 2.13e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 665410108    521 CPPQAQGLYLHPFDCTKYVRCWNQQTFIESCTPGEIFSFSNQKCVPK 567
Cdd:smart00494    3 CPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 521-569 3.04e-08

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 52.03  E-value: 3.04e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 665410108   521 CPPQAQGLYLHPFDCTKYVRCWNQQTFIESCTPGEIFSFSNQKCVPKEQ 569
Cdd:pfam01607    1 CAGKEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDN 49
ChtBD2 smart00494
Chitin-binding domain type 2;
942-988 3.68e-08

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 51.68  E-value: 3.68e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 665410108    942 CPPQAQGYYLHPFDCTKYIVCWEKQTHIESCPQGEAFSISQQKCVAR 988
Cdd:smart00494    3 CPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
ChtBD2 smart00494
Chitin-binding domain type 2;
709-752 2.81e-06

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 46.28  E-value: 2.81e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 665410108    709 CPSGVNGQFVHPFDQTKFLLCQAGKLAVQSCQSGYVFSISKSIC 752
Cdd:smart00494    3 CPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTC 46
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1924-1957 3.59e-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: 45.32  E-value: 3.59e-06
                            10        20        30
                    ....*....|....*....|....*....|....
gi 665410108   1924 KCPNNYWLCHTSKeCIPPAFVCDNTPDCADKSDE 1957
Cdd:smart00192    1 TCPPGEFQCDNGR-CIPSSWVCDGVDDCGDGSDE 33
PTZ00395 PTZ00395
Sec24-related protein; Provisional
 1029-1184 4.66e-06

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 52.38  E-value: 4.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108 1029 GGNQPPGKYQAPYYSNGGYPTPSQNNGGYQTPSQNNGGYQAPFQNNGGYQPSYQGNGGYTPT-YQNPfegyhqPNQSSYQ 1107
Cdd:PTZ00395  381 GGPHSNASYNCAAYSNAAQSNAAQSNAGFSNAGYSNPGNSNPGYNNAPNSNTPYNNPPNSNTpYSNP------PNSNPPY 454

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108 1108 TNGGY------QPPL---PPHGGYQPPSQTYGGFQQPNRTYEDFHNPSQTVGGFQPPYSVKGgyqpHNQLNGGYNQPNQS 1178
Cdd:PTZ00395  455 SNLPYsntpysNAPLsnaPPSSAKDHHSAYHAAYQHRAANQPAANLPTANQPAANNFHGAAG----NSVGNPFASRPFGS 530


                  ....*.
gi 665410108 1179 SSFQAN 1184
Cdd:PTZ00395  531 APYGGN 536
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1780-1809 5.41e-06

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


Pssm-ID: 238060  Cd Length: 35  Bit Score: 44.89  E-value: 5.41e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 665410108 1780 FDCGNGQCLKKEEICDGKKNCPNGKDEANC 1809
Cdd:cd00112     6 FRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1925-1957 6.27e-06

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


Pssm-ID: 238060  Cd Length: 35  Bit Score: 44.89  E-value: 6.27e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 665410108 1925 CPNNYWLCHtSKECIPPAFVCDNTPDCADKSDE 1957
Cdd:cd00112     1 CPPNEFRCA-NGRCIPSSWVCDGEDDCGDGSDE 32
PTZ00395 PTZ00395
Sec24-related protein; Provisional
 1043-1317 3.04e-05

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 49.69  E-value: 3.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108 1043 SNGGYPTPSQNNGGYQTPSQN-NGGYQAPFQNNGGYQ-PSYQGN---GGytPTYQNPFEgyhQPNQSSYQTNGGYQPPLP 1117
Cdd:PTZ00395  273 AESGYAHHRGSNIASHTPNDNiMHAANNPLNNTNDAQrNAIQGDlvrGA--PNDKNSFD---RGNEKTYQIYGGFHDGSP 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108 1118 PHGGYQPPSQTYGgfqqpnrtyedfhnpSQTVGGF--QPPYSVKGGYQPHNQLNGGYNqpnqsSSFQANGGYQPPSQVNR 1195
Cdd:PTZ00395  348 NAASAGAPFNGLG---------------NQADGGHinQVHPDARGAWAGGPHSNASYN-----CAAYSNAAQSNAAQSNA 407

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108 1196 GYqtsfeSNGGYQPPLETNKGHQVPSQINGGYQPRVDGNRGYQPPNELNGGYQPPNELNGAYPAPSQLNGGYQPPLEGNL 1275
Cdd:PTZ00395  408 GF-----SNAGYSNPGNSNPGYNNAPNSNTPYNNPPNSNTPYSNPPNSNPPYSNLPYSNTPYSNAPLSNAPPSSAKDHHS 482

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 665410108 1276 GYRPLSQQNSGYQPPQPSTGGYQPPFQSTGSGHYPGQDAPYA 1317
Cdd:PTZ00395  483 AYHAAYQHRAANQPAANLPTANQPAANNFHGAAGNSVGNPFA 524
ChtBD2 smart00494
Chitin-binding domain type 2;
284-327 3.30e-05

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 43.20  E-value: 3.30e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 665410108    284 CPVGAVGQFVHPFDQTKFLSCKDGKSAVQNCQPNYVFSISRRYC 327
Cdd:smart00494    3 CPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTC 46
ChtBD2 smart00494
Chitin-binding domain type 2;
1474-1518 5.24e-05

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 42.43  E-value: 5.24e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 665410108   1474 CPEGITGTLPHPRVPTKYLRCGPGQAEMYDCPSQQIFSVSRRVCV 1518
Cdd:smart00494    3 CPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCD 47
ChtBD2 smart00494
Chitin-binding domain type 2;
215-261 1.69e-04

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 41.28  E-value: 1.69e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 665410108    215 CPPGTRGLRPHPHDVHKYLRCgIGVKPQVEQCPRGHIFDGSSSVCVY 261
Cdd:smart00494    3 CPGRGDGLYPHPTDCSKYYQC-SNGRPIVGSCPAGLVFNPATQTCDW 48
ChtBD2 smart00494
Chitin-binding domain type 2;
1324-1369 1.79e-04

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 41.28  E-value: 1.79e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 665410108   1324 CPEKISGLFPNPFDATGYLTCIDGHTLPRQCQPLDVFSVSQGYCLP 1369
Cdd:smart00494    3 CPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1780-1806 3.98e-04

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


Pssm-ID: 197566  Cd Length: 33  Bit Score: 39.54  E-value: 3.98e-04
                            10        20
                    ....*....|....*....|....*..
gi 665410108   1780 FDCGNGQCLKKEEICDGKKNCPNGKDE 1806
Cdd:smart00192    7 FQCDNGRCIPSSWVCDGVDDCGDGSDE 33
CTD pfam12815
Spt5 C-terminal nonapeptide repeat binding Spt4; The C-terminal domain of the transcription ...
 1041-1101 4.25e-04

Spt5 C-terminal nonapeptide repeat binding Spt4; The C-terminal domain of the transcription elongation factor protein Spt5 is necessary for binding to Spt4 to form the functional complex that regulates early transcription elongation by RNA polymerase II. The complex may be involved in pre-mRNA processing through its association with mRNA capping enzymes. This CTD domain carries a regular nonapeptide repeat that can be present in up to 18 copies, as in S. pombe. The repeat has a characteriztic TPA motif.


Pssm-ID: 372327 [Multi-domain]  Cd Length: 71  Bit Score: 40.89  E-value: 4.25e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665410108  1041 YYSNGGYPTPSQNNGGYQTPSQNNGGYQAPFQNNGGYQPSYQGNGGYTPTYQNPFEGYHQP 1101
Cdd:pfam12815    7 YNSAGGSRTPAWGADGSRTPAYGGAGGRTPAYNQGGKTPAWGGAGSRTPAYYGAWGGSRTP 67
PHA03378 PHA03378
EBNA-3B; Provisional
 1190-1325 5.39e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 45.44  E-value: 5.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108 1190 PSQVNRGYQTSFESNGG---YQPPLETNKGHQV----PSQINggYQPRVDGNRGYQPPNELNGGYQPPNELNGAYPAPSQ 1262
Cdd:PHA03378  632 PMRPLRMQPITFNVLVFptpHQPPQVEITPYKPtwtqIGHIP--YQPSPTGANTMLPIQWAPGTMQPPPRAPTPMRPPAA 709

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665410108 1263 LNGGYQPPLEGNLGYRPLSQQNSGYQPPQPSTGGYQPPfQSTGSGHYPGQDAPYAIPTPLLCP 1325
Cdd:PHA03378  710 PPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPP-AAAPGRARPPAAAPGRARPPAAAP 771
PHA03378 PHA03378
EBNA-3B; Provisional
 1177-1335 6.28e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 45.06  E-value: 6.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108 1177 QSSSFQANGG---YQPPSQVNRGYQTSFESNGG--YQPPLETNKGHQVPSQINGGYQPRVDGNRGYQPPNELNGGYQPPN 1251
Cdd:PHA03378  639 QPITFNVLVFptpHQPPQVEITPYKPTWTQIGHipYQPSPTGANTMLPIQWAPGTMQPPPRAPTPMRPPAAPPGRAQRPA 718

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108 1252 ELNGAYPAPSQLNGGYQPPLEGNLGYRPLSQQNSGYQPPQPSTGGYQPPFQSTGSGhyPGQDAPYAIPTPLLCPEKISGL 1331
Cdd:PHA03378  719 AATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAP--TPQPPPQAPPAPQQRPRGAPTP 796


                  ....
gi 665410108 1332 FPNP 1335
Cdd:PHA03378  797 QPPP 800
PTZ00395 PTZ00395
Sec24-related protein; Provisional
 1048-1320 2.15e-03

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 43.53  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108 1048 PTPSQNNGGYQTpSQNNGGYQAPFQNNGGYQPSYQ---------GNGGY---TPTYQN---------PFEGY--HQPNQ- 1103
Cdd:PTZ00395  152 APHAQHNHSGKT-NGDNPPTGGQYHQSGGTSRNHQmmdsnkncpADALFnetNPSGEHkrnsidgdiPSDIYidSQPNEg 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108 1104 -----SSYQTNGGYQPPLPPHGGYQPPSQTYGGFQQPNRTYED----FHNPSQTVGGFQPPYSVKGGyqPHNQLNGgyNQ 1174
Cdd:PTZ00395  231 dvqktNPWQGKQGNSATSPPANENNAVTLSCSNDQQRGASSAAesgyAHHRGSNIASHTPNDNIMHA--ANNPLNN--TN 306

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108 1175 PNQSSSFQAN---GGYQPPSQVNRGYQTSFESNGGYQ--PPLETNKGHQ---VPSQINGGY----QPRVDGNRGYQPPNe 1242
Cdd:PTZ00395  307 DAQRNAIQGDlvrGAPNDKNSFDRGNEKTYQIYGGFHdgSPNAASAGAPfngLGNQADGGHinqvHPDARGAWAGGPHS- 385

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108 1243 lNGGYQPPNELNGAYPAPSQLNGG-----YQPPLEGNLGYRPLSQQNSGY-QPPQPSTGGYQPPFQSTGSGHYPGQDAPY 1316
Cdd:PTZ00395  386 -NASYNCAAYSNAAQSNAAQSNAGfsnagYSNPGNSNPGYNNAPNSNTPYnNPPNSNTPYSNPPNSNPPYSNLPYSNTPY 464


                  ....
gi 665410108 1317 AIPT 1320
Cdd:PTZ00395  465 SNAP 468
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 1474-1524 3.58e-03

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 37.39  E-value: 3.58e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 665410108  1474 CPEGITGTLPHPRVPTKYLRCGPGQAEMYDCPSQQIFSVSRRVCVLDDKLS 1524
Cdd:pfam01607    1 CAGKEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVV 51
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 1032-1193 5.10e-03

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 42.33  E-value: 5.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108  1032 QPPGKYQAPyysngGYPTPSQNNGGYQTPSQNngGYQAPFQNNGGYQPSYQGNGGYTPTYQNPFEGYHQPNQSSYQTNGG 1111
Cdd:pfam09770  214 PAPAPAQPP-----AAPPAQQAQQQQQFPPQI--QQQQQPQQQPQQPQQHPGQGHPVTILQRPQSPQPDPAQPSIQPQAQ 286

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410108  1112 YQPPLPPHGGYQpPSQTyggFQQPNRTyedfhnPSQTVGGFQPPYSVKGGYQPHnqlnggYNQPNQSSSFQANGGYQPPS 1191
Cdd:pfam09770  287 QFHQQPPPVPVQ-PTQI---LQNPNRL------SAARVGYPQNPQPGVQPAPAH------QAHRQQGSFGRQAPIITHPQ 350


                   ..
gi 665410108  1192 QV 1193
Cdd:pfam09770  351 QL 352
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 215-261 5.47e-03

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 37.01  E-value: 5.47e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 665410108   215 CPPGTRGLRPHPHDVHKYLRCGIGvKPQVEQCPRGHIFDGSSSVCVY 261
Cdd:pfam01607    1 CAGKEDGYYADPGDCSKYYVCSNG-EAVEFTCPNGLVFDPTLGICDY 46
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1924-1957 6.29e-03

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 36.46  E-value: 6.29e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 665410108  1924 KCPNNYWLCHTSkECIPPAFVCDNTPDCADKSDE 1957
Cdd:pfam00057    2 TCSPNEFQCGSG-ECIPRSWVCDGDPDCGDGSDE 34
ChtBD2 smart00494
Chitin-binding domain type 2;
864-909 8.57e-03

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 36.27  E-value: 8.57e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 665410108    864 ECPSVLRGNYPYPFHAGHFVNCQNGHLQIVSCPPTALYSLSQRECV 909
Cdd:smart00494    2 ECPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCD 47
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 782-829 9.14e-03

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 36.24  E-value: 9.14e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 665410108   782 CPDGTNGLHLYPYDAGKYVRCSDGGKmSIQSCENQMAFSLSQRACRPS 829
Cdd:pfam01607    1 CAGKEDGYYADPGDCSKYYVCSNGEA-VEFTCPNGLVFDPTLGICDYP 47
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH