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Conserved domains on  [gi|5803080|ref|NP_006761|]
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macrophage receptor MARCO [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 424-519 2.05e-41

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: 144.02  E-value: 2.05e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080     424 VRIVGSSNR--GRAEVYYSGTWGTICDDEWQNSDAIVFCRMLGYSKGRALYK---VGAGTGQIWLDNVQCRGTESTLWSC 498
Cdd:smart00202   1 VRLVGGGSPceGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGsayFGPGSGPIWLDNVRCSGTEASLSDC 80

                           90       100
                   ....*....|....*....|.
gi 5803080     499 TKNSWGHHDCSHEEDAGVECS 519
Cdd:smart00202  81 PHSGWGSHNCSHGEDAGVVCS 101
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 147-396 8.99e-33

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 130.03  E-value: 8.99e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080   147 KGEQGAPGLQGhkgamgmpgapgppgppaEKGAKGAMGRDGATGPSGPQGPPGVKGEAGLQGPQGAPGKQGATGTPGPQG 226
Cdd:NF038329 119 KGEPGPAGPAG------------------PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDG 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080   227 EKGSKGDGgliGPKGETGTKGEKGDLGLPGSKGDRGMKGDAGVMGPPGAQGSKGDfgrpGPPGLAGFPGAKGDQGQPGLQ 306
Cdd:NF038329 181 EAGAKGPA---GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDGPQGPD 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080   307 GVPGPPGAVGHPGAKGEPGSAGSPGRAGLPGSPGSPGATGLKGSKGDTGLQGQQGRKGESGVPGPAGVKGEQGSPGLAGP 386
Cdd:NF038329 254 GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGK 333

                        250
                 ....*....|
gi 5803080   387 KGAPGQAGQK 396
Cdd:NF038329 334 DGQPGKPAPK 343
 
Name Accession Description Interval E-value
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 424-519 2.05e-41

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: 144.02  E-value: 2.05e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080     424 VRIVGSSNR--GRAEVYYSGTWGTICDDEWQNSDAIVFCRMLGYSKGRALYK---VGAGTGQIWLDNVQCRGTESTLWSC 498
Cdd:smart00202   1 VRLVGGGSPceGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGsayFGPGSGPIWLDNVRCSGTEASLSDC 80

                           90       100
                   ....*....|....*....|.
gi 5803080     499 TKNSWGHHDCSHEEDAGVECS 519
Cdd:smart00202  81 PHSGWGSHNCSHGEDAGVVCS 101
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 428-519 3.37e-35

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: 127.11  E-value: 3.37e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080    428 GSSNRGRAEVYYSGTWGTICDDEWQNSDAIVFCRMLGY------SKGRALYKVGaGTGQIWLDNVQCRGTESTLWSCTKN 501
Cdd:pfam00530   2 SSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGCggavsaPSGCSYFGPG-STGPIWLDDVRCSGNETSLWQCPHR 80

                          90
                  ....*....|....*...
gi 5803080    502 SWGHHDCSHEEDAGVECS 519
Cdd:pfam00530  81 PWGNHNCSHSEDAGVICS 98
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 147-396 8.99e-33

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 130.03  E-value: 8.99e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080   147 KGEQGAPGLQGhkgamgmpgapgppgppaEKGAKGAMGRDGATGPSGPQGPPGVKGEAGLQGPQGAPGKQGATGTPGPQG 226
Cdd:NF038329 119 KGEPGPAGPAG------------------PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDG 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080   227 EKGSKGDGgliGPKGETGTKGEKGDLGLPGSKGDRGMKGDAGVMGPPGAQGSKGDfgrpGPPGLAGFPGAKGDQGQPGLQ 306
Cdd:NF038329 181 EAGAKGPA---GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDGPQGPD 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080   307 GVPGPPGAVGHPGAKGEPGSAGSPGRAGLPGSPGSPGATGLKGSKGDTGLQGQQGRKGESGVPGPAGVKGEQGSPGLAGP 386
Cdd:NF038329 254 GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGK 333

                        250
                 ....*....|
gi 5803080   387 KGAPGQAGQK 396
Cdd:NF038329 334 DGQPGKPAPK 343
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
178-403 1.95e-14

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 75.45  E-value: 1.95e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080  178 GAKGAMGRDGATGPsgpqgppgvkgeAGLQGPQGAPGKQGATGTPGPQGEKGSKGDGGLIGPKGETGTKGEKGDLGLPGS 257
Cdd:COG5164  16 GVTTPAGSQGSTKP------------AQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTP 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080  258 KGDRGMKGDAGVMGPPGAQGSKGDFGRPGPPGLAGFPGAKGDQGqPGLQGVPGPPGAVGH----PGAKGEPGSAGSPGRA 333
Cdd:COG5164  84 AQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTT-PPSGGSTTPPGDGGStppgPGSTGPGGSTTPPGDG 162

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080  334 GLPGSPGSPGATGLKGSKGDTGlqgqQGRKGESGVPGPAGVKGEQGSPGLAGPKGAPGQAGQKGDQGVKG 403
Cdd:COG5164 163 GSTTPPGPGGSTTPPDDGGSTT----PPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKT 228
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 337-419 4.79e-12

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 68.01  E-value: 4.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080   337 GSPGSPGATGLKGSKGDTGLQGQQGRKGESGVPGPAGVKGEQGSPGLAGPKGAPGQAGQKGDQGVKGSSGEQGVKGEKGE 416
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196


                 ...
gi 5803080   417 RGE 419
Cdd:NF038329 197 RGE 199
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 283-339 2.24e-10

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 55.96  E-value: 2.24e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 5803080    283 GRPGPPGLAGFPGAKGDQGQPGLQGVPGPPGAVGHPGAKGEPGSAGSPGRAGLPGSP 339
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 207-421 1.07e-06

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 51.15  E-value: 1.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080  207 QGPQGAPGKQGATGTPGPQGEKGSKGDGGLIGPKGETGTKGEKGDLG-------------LPGSKGDRGMKGDAGVMGPP 273
Cdd:cd21118 127 HGAYGSQGGPGVQGHGIPGGTGGPWASGGNYGTNSLGGSVGQGGNGGplnygtnsqgavaQPGYGTVRGNNQNSGCTNPP 206

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080  274 GAqGSKGDFGRPGPPGLAGFPGAKGDQGQPGlqgvpgpPGAVGHPGAKGEPGSAGSPGRAGLPGSPGSPGATGLKGSKGD 353
Cdd:cd21118 207 PS-GSHESFSNSGGSSSSGSSGSQGSHGSNG-------QGSSGSSGGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGSGSG 278

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5803080  354 TGLQGQQGRKGESGVPGPAGVKGEQGSPGLAGPKGAPGQAGQKGDQGVKGSSGEQGVKGEKGERGENS 421
Cdd:cd21118 279 GSSSGGSNGWGGSSSSGGSGGSGGGNKPECNNPGNDVRMAGGGGSQGSKESSGSHGSNGGNGQAEAVG 346
PHA03169 PHA03169
hypothetical protein; Provisional
 203-381 4.15e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 46.12  E-value: 4.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080   203 EAGLQGPQGAPGKQGATGTPGPQGEKGSKGDGGLIGP---KGETGTKGEKGDL------GLPGSKGDRGMKGDAGVMGPP 273
Cdd:PHA03169  59 RAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSgseSVGSPTPSPSGSAeelasgLSPENTSGSSPESPASHSPPP 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080   274 GAQGSKGDfGRPGPPGLAGfpGAKGDQGQPGLQGV------PGPPGAVGHPGAKGEPGSAGSPGRAGLPGSPG-SPGATG 346
Cdd:PHA03169 139 SPPSHPGP-HEPAPPESHN--PSPNQQPSSFLQPShedspeEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPdEPGEPQ 215

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 5803080   347 LKGSKGDTGLQGQQGRKGESGVPGPAGVKGEQGSP 381
Cdd:PHA03169 216 SPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFPGH 250
 
Name Accession Description Interval E-value
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 424-519 2.05e-41

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: 144.02  E-value: 2.05e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080     424 VRIVGSSNR--GRAEVYYSGTWGTICDDEWQNSDAIVFCRMLGYSKGRALYK---VGAGTGQIWLDNVQCRGTESTLWSC 498
Cdd:smart00202   1 VRLVGGGSPceGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGsayFGPGSGPIWLDNVRCSGTEASLSDC 80

                           90       100
                   ....*....|....*....|.
gi 5803080     499 TKNSWGHHDCSHEEDAGVECS 519
Cdd:smart00202  81 PHSGWGSHNCSHGEDAGVVCS 101
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 428-519 3.37e-35

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: 127.11  E-value: 3.37e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080    428 GSSNRGRAEVYYSGTWGTICDDEWQNSDAIVFCRMLGY------SKGRALYKVGaGTGQIWLDNVQCRGTESTLWSCTKN 501
Cdd:pfam00530   2 SSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGCggavsaPSGCSYFGPG-STGPIWLDDVRCSGNETSLWQCPHR 80

                          90
                  ....*....|....*...
gi 5803080    502 SWGHHDCSHEEDAGVECS 519
Cdd:pfam00530  81 PWGNHNCSHSEDAGVICS 98
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 147-396 8.99e-33

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 130.03  E-value: 8.99e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080   147 KGEQGAPGLQGhkgamgmpgapgppgppaEKGAKGAMGRDGATGPSGPQGPPGVKGEAGLQGPQGAPGKQGATGTPGPQG 226
Cdd:NF038329 119 KGEPGPAGPAG------------------PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDG 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080   227 EKGSKGDGgliGPKGETGTKGEKGDLGLPGSKGDRGMKGDAGVMGPPGAQGSKGDfgrpGPPGLAGFPGAKGDQGQPGLQ 306
Cdd:NF038329 181 EAGAKGPA---GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDGPQGPD 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080   307 GVPGPPGAVGHPGAKGEPGSAGSPGRAGLPGSPGSPGATGLKGSKGDTGLQGQQGRKGESGVPGPAGVKGEQGSPGLAGP 386
Cdd:NF038329 254 GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGK 333

                        250
                 ....*....|
gi 5803080   387 KGAPGQAGQK 396
Cdd:NF038329 334 DGQPGKPAPK 343
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
178-403 1.95e-14

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 75.45  E-value: 1.95e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080  178 GAKGAMGRDGATGPsgpqgppgvkgeAGLQGPQGAPGKQGATGTPGPQGEKGSKGDGGLIGPKGETGTKGEKGDLGLPGS 257
Cdd:COG5164  16 GVTTPAGSQGSTKP------------AQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTP 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080  258 KGDRGMKGDAGVMGPPGAQGSKGDFGRPGPPGLAGFPGAKGDQGqPGLQGVPGPPGAVGH----PGAKGEPGSAGSPGRA 333
Cdd:COG5164  84 AQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTT-PPSGGSTTPPGDGGStppgPGSTGPGGSTTPPGDG 162

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080  334 GLPGSPGSPGATGLKGSKGDTGlqgqQGRKGESGVPGPAGVKGEQGSPGLAGPKGAPGQAGQKGDQGVKG 403
Cdd:COG5164 163 GSTTPPGPGGSTTPPDDGGSTT----PPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKT 228
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
148-394 1.02e-13

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 73.53  E-value: 1.02e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080  148 GEQGAPGLQGHKGAMGMPGAPGPPGPPAEKG---AKGAMGRDGATGPSGPQGPPGVKGEAGLQGPQGAPGKQGATGTPGP 224
Cdd:COG5164  16 GVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRpaqNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGN 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080  225 QGEKGSKGDGGLIGPKGETGTKGEKGDLG--LPGSKGDRGMKGDAGVMGP-PGAQGSKGDFGRPGPPGLAGFPGAKGDQG 301
Cdd:COG5164  96 TGGTTPAGDGGATGPPDDGGATGPPDDGGstTPPSGGSTTPPGDGGSTPPgPGSTGPGGSTTPPGDGGSTTPPGPGGSTT 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080  302 QPGLQGVPGPPgavgHPGAKGEPGSAGSPGRAGLPGSPGSPGATGLKGSKGDTGlqGQQGRKGESGVPGPAGVKGEQGSP 381
Cdd:COG5164 176 PPDDGGSTTPP----NKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG--GKTGPKDQRPKTNPIERRGPERPE 249

                       250
                ....*....|...
gi 5803080  382 GLAGPKGAPGQAG 394
Cdd:COG5164 250 AAALPAELTALEA 262
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 337-419 4.79e-12

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 68.01  E-value: 4.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080   337 GSPGSPGATGLKGSKGDTGLQGQQGRKGESGVPGPAGVKGEQGSPGLAGPKGAPGQAGQKGDQGVKGSSGEQGVKGEKGE 416
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196


                 ...
gi 5803080   417 RGE 419
Cdd:NF038329 197 RGE 199
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 283-339 2.24e-10

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 55.96  E-value: 2.24e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 5803080    283 GRPGPPGLAGFPGAKGDQGQPGLQGVPGPPGAVGHPGAKGEPGSAGSPGRAGLPGSP 339
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 292-346 3.44e-09

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 52.88  E-value: 3.44e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 5803080    292 GFPGAKGDQGQPGLQGVPGPPGAVGHPGAKGEPGSAGSPGRAGLPGSPGSPGATG 346
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 277-331 5.61e-09

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 52.11  E-value: 5.61e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 5803080    277 GSKGDFGRPGPPGLAGFPGAKGDQGQPGLQGVPGPPGAVGHPGAKGEPGSAGSPG 331
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 298-352 1.11e-08

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 51.34  E-value: 1.11e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 5803080    298 GDQGQPGLQGVPGPPGAVGHPGAKGEPGSAGSPGRAGLPGSPGSPGATGLKGSKG 352
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 259-315 2.23e-08

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 50.57  E-value: 2.23e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 5803080    259 GDRGMKGDAGVMGPPGAQGSKGDFGRPGPPGLAGFPGAKGDQGQPGLQGVPGPPGAV 315
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 337-393 2.25e-08

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 50.57  E-value: 2.25e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 5803080    337 GSPGSPGATGLKGSKGDTGLQGQQGRKGESGVPGPAGVKGEQGSPGLAGPKGAPGQA 393
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 304-359 2.66e-08

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 50.18  E-value: 2.66e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 5803080    304 GLQGVPGPPGAVGHPGAKGEPGSAGSPGRAGLPGSPGSPGATGLKGSKGDTGLQGQ 359
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 301-355 2.74e-08

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 50.18  E-value: 2.74e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 5803080    301 GQPGLQGVPGPPGAVGHPGAKGEPGSAGSPGRAGLPGSPGSPGATGLKGSKGDTG 355
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 358-413 1.05e-07

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 48.64  E-value: 1.05e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 5803080    358 GQQGRKGESGVPGPAGVKGEQGSPGLAGPKGAPGQAGQKGDQGVKGSSGEQGVKGE 413
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 307-372 1.35e-07

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 48.26  E-value: 1.35e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5803080    307 GVPGPPGAVGHPGAKGEPGSAGSPGRAGLPGSPGSPGAtglkgskgdTGLQGQQGRKGESGVPGPA 372
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGP---------PGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 349-403 6.12e-07

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 46.33  E-value: 6.12e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 5803080    349 GSKGDTGLQGQQGRKGESGVPGPAGVKGEQGSPGLAGPKGAPGQAGQKGDQGVKG 403
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 340-395 6.89e-07

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 46.33  E-value: 6.89e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 5803080    340 GSPGATGLKGSKGDTGLQGQQGRKGESGVPGPAGVKGEQGSPGLAGPKGAPGQAGQ 395
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 247-303 7.09e-07

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 46.33  E-value: 7.09e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 5803080    247 GEKGDLGLPGSKGDRGMKGDAGVMGPPGAQGSKGDFGRPGPPGLAGFPGAKGDQGQP 303
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 364-420 7.98e-07

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.95  E-value: 7.98e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 5803080    364 GESGVPGPAGVKGEQGSPGLAGPKGAPGQAGQKGDQGVKGSSGEQGVKGEKGERGEN 420
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 207-421 1.07e-06

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 51.15  E-value: 1.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080  207 QGPQGAPGKQGATGTPGPQGEKGSKGDGGLIGPKGETGTKGEKGDLG-------------LPGSKGDRGMKGDAGVMGPP 273
Cdd:cd21118 127 HGAYGSQGGPGVQGHGIPGGTGGPWASGGNYGTNSLGGSVGQGGNGGplnygtnsqgavaQPGYGTVRGNNQNSGCTNPP 206

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080  274 GAqGSKGDFGRPGPPGLAGFPGAKGDQGQPGlqgvpgpPGAVGHPGAKGEPGSAGSPGRAGLPGSPGSPGATGLKGSKGD 353
Cdd:cd21118 207 PS-GSHESFSNSGGSSSSGSSGSQGSHGSNG-------QGSSGSSGGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGSGSG 278

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5803080  354 TGLQGQQGRKGESGVPGPAGVKGEQGSPGLAGPKGAPGQAGQKGDQGVKGSSGEQGVKGEKGERGENS 421
Cdd:cd21118 279 GSSSGGSNGWGGSSSSGGSGGSGGGNKPECNNPGNDVRMAGGGGSQGSKESSGSHGSNGGNGQAEAVG 346
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 202-256 1.41e-06

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.18  E-value: 1.41e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 5803080    202 GEAGLQGPQGAPGKQGATGTPGPQGEKGSKGDGGLIGPKGETGTKGEKGDLGLPG 256
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 355-409 2.56e-06

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.79  E-value: 2.56e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 5803080    355 GLQGQQGRKGESGVPGPAGVKGEQGSPGLAGPKGAPGQAGQKGDQGVKGSSGEQG 409
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 238-288 5.91e-06

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.64  E-value: 5.91e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 5803080    238 GPKGETGTKGEKGDLGLPGSKGDRGMKGDAGVMGPPGAQGSKGDFGRPGPP 288
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 361-417 8.33e-06

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.25  E-value: 8.33e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 5803080    361 GRKGESGVPGPAGVKGEQGSPGLAGPKGAPGQAGQKGDQGVKGSSGEQGVKGEKGER 417
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 235-289 3.85e-05

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.33  E-value: 3.85e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 5803080    235 GLIGPKGETGTKGEKGDLGLPGSKGDRGMKGDAGVMGPPGAQGSKGDFGRPGPPG 289
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PHA03169 PHA03169
hypothetical protein; Provisional
 203-381 4.15e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 46.12  E-value: 4.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080   203 EAGLQGPQGAPGKQGATGTPGPQGEKGSKGDGGLIGP---KGETGTKGEKGDL------GLPGSKGDRGMKGDAGVMGPP 273
Cdd:PHA03169  59 RAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSgseSVGSPTPSPSGSAeelasgLSPENTSGSSPESPASHSPPP 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080   274 GAQGSKGDfGRPGPPGLAGfpGAKGDQGQPGLQGV------PGPPGAVGHPGAKGEPGSAGSPGRAGLPGSPG-SPGATG 346
Cdd:PHA03169 139 SPPSHPGP-HEPAPPESHN--PSPNQQPSSFLQPShedspeEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPdEPGEPQ 215

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 5803080   347 LKGSKGDTGLQGQQGRKGESGVPGPAGVKGEQGSP 381
Cdd:PHA03169 216 SPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFPGH 250
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 201-250 6.24e-05

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 6.24e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 5803080    201 KGEAGLQGPQGAPGKQGATGTPGPQGEKGSKGDGGLIGPKGETGTKGEKG 250
Cdd:pfam01391   6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 265-410 1.15e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.98  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080   265 GDAGVMGPPGAQGSKGDFGRPGPPGLAGFPGAKGDQGQPGLQGVPGPPGAVGHPGAKGEPGSAGSPGRAGLP----GSPG 340
Cdd:PRK07764 589 GPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPdasdGGDG 668

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080   341 SPGATGLKGSKGDTGLQGQQGRKGESGVPGPAGVKGEQGSPGLAGPKGAPGQAGQKGDQGVKGSSGEQGV 410
Cdd:PRK07764 669 WPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDP 738
PHA03169 PHA03169
hypothetical protein; Provisional
 203-419 1.85e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 43.81  E-value: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080   203 EAGLQGPQGAPGKQGATGTP---GPQGEKGSKGDGGLIGPKGETGTKGEKGDLGLPGSKGDRGMKGDAGVMGPPGAQGSK 279
Cdd:PHA03169  32 QAGRRRGTAARAAKPAPPAPttsGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSA 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080   280 GDFGRPGPPGLAGFPGAKGDQGQPGlqgvPGPPGAVGHPGAKGEPGSAGspgraglpGSPGSPGATGLKGSKGDTGLQGQ 359
Cdd:PHA03169 112 EELASGLSPENTSGSSPESPASHSP----PPSPPSHPGPHEPAPPESHN--------PSPNQQPSSFLQPSHEDSPEEPE 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5803080   360 QGrkgeSGVPGPAGVKGEQGSPGLAGPKGA-----PGQAGQKGDQGVKGSSGEQGVKGEKGERGE 419
Cdd:PHA03169 180 PP----TSEPEPDSPGPPQSETPTSSPPPQsppdePGEPQSPTPQQAPSPNTQQAVEHEDEPTEP 240
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 227-367 2.84e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 43.52  E-value: 2.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080   227 EKGSKGDGGLIGPKG---ETGTKGEKGDLGLPGSKGDRGMKGDAGVMGPPGAQGSKGDFGRPGP----------PGLAGF 293
Cdd:PRK14959 369 ESLRPSGGGASAPSGsaaEGPASGGAATIPTPGTQGPQGTAPAAGMTPSSAAPATPAPSAAPSPrvpwddappaPPRSGI 448

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5803080   294 PgAKGDQGQPGLQGVPGPPGAVGhpGAKGEPGSAGSPGrAGLPGSPGSPGATglkgskgDTGLQGQQGRKGESG 367
Cdd:PRK14959 449 P-PRPAPRMPEASPVPGAPDSVA--SASDAPPTLGDPS-DTAEHTPSGPRTW-------DGFLEFCQGRNGQGG 511
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 209-403 3.11e-04

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 43.51  E-value: 3.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080  209 PQGAPGKQGATGTPGPQGEKGSKGDGGLigPKGETGTKGEKGD--LGLPGSKGDRGMKGDAGVMGPPGAQGSKGDFGRPG 286
Cdd:COG5180 253 PEMRPPADAKERRRAAIGDTPAAEPPGL--PVLEAGSEPQSDApeAETARPIDVKGVASAPPATRPVRPPGGARDPGTPR 330

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080  287 PP----GLAGFPGAKGDQGQPGlQGVPGPPGAVghPGAKGEPGsAGSPGRAGLPGSPGSPGAtglkgskgdtglQGQQGR 362
Cdd:COG5180 331 PGqpteRPAGVPEAASDAGQPP-SAYPPAEEAV--PGKPLEQG-APRPGSSGGDGAPFQPPN------------GAPQPG 394

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 5803080  363 KGESGVPGPAGVKGEQGSPGLAGPKGAPGQAGQKGDQGVKG 403
Cdd:COG5180 395 LGRRGAPGPPMGAGDLVQAALDGGGRETASLGGAAGGAGQG 435
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 207-404 3.12e-04

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: 43.46  E-value: 3.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080    207 QGPQGAPGKQGATGTPGPQGEKGSKGDGGLIGPKGETGTKGEKGDLGLPGSKgdrgmkgDAGVMGPPG-AQGSKGDFGRP 285
Cdd:pfam09606  58 AQQQQPQGGQGNGGMGGGQQGMPDPINALQNLAGQGTRPQMMGPMGPGPGGP-------MGQQMGGPGtASNLLASLGRP 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080    286 GPP-GLAGFPGAKGD--QGQPGLQGVPGPPGAVGHPGAkgepgsaGSPGRAGLPGSPGSPGATGLKGSKGDTGLQGQQGR 362
Cdd:pfam09606 131 QMPmGGAGFPSQMSRvgRMQPGGQAGGMMQPSSGQPGS-------GTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQ 203

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 5803080    363 KGESGVPGPAgvkgeqgSPGLAGPKGAPGQAGQKGDQGVKGS 404
Cdd:pfam09606 204 MGVPGMPGPA-------DAGAQMGQQAQANGGMNPQQMGGAP 238
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 209-411 1.19e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.51  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080   209 PQGAPGKQGATGTPGPQGEKGSKGDGGLIGPKGETGTKGEKGDLGLPGSKGDRGMK-GDAGVMGPPGAQGSkgdfgrPGP 287
Cdd:PRK07764 617 APAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKaGGAAPAAPPPAPAP------AAP 690

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080   288 PGLAGFPGAKGDQGQPGLQGVPGPPGAVGHPGAKGEPGSAGSPGRAGLPGSPGSPGATGLKGSKGDTGLQGQqgrkgesG 367
Cdd:PRK07764 691 AAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPP-------A 763

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 5803080   368 VPGPAGVKGEQGSPGLAGPKGAPGQAGQKGDQGVKGSSGEQGVK 411
Cdd:PRK07764 764 PAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAEEVAME 807
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 266-395 1.63e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.12  E-value: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080   266 DAGVMGPPGAqgskGDFGRPGPPGLAGFPGAkgdQGQPGLQGVPGPPGAVGHPGAKGEPGSAGSPGRAGLPGSPGSPGAT 345
Cdd:PRK07764 585 EAVVGPAPGA----AGGEGPPAPASSGPPEE---AARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHV 657

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 5803080   346 GLKGSKGDTGlqgqqGRKGESGVPGPAGVKGEQGSPGLAGPKGAPGQAGQ 395
Cdd:PRK07764 658 AVPDASDGGD-----GWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPA 702
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 156-422 4.23e-03

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: 39.99  E-value: 4.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080    156 QGHKGAMGMPGAPGPPGPPAekGAKGAMGRDGATGPSGPQGPPGVKGEA----------GLQGPQGAPGKQGATGTPGPQ 225
Cdd:pfam09606  92 QGTRPQMMGPMGPGPGGPMG--QQMGGPGTASNLLASLGRPQMPMGGAGfpsqmsrvgrMQPGGQAGGMMQPSSGQPGSG 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080    226 GEKGSKGDGGLIGPKGETGTKGEKGDLG--LPGSKGDRGMKG--DAGVMGPPGAQGSKGdfgrPGPPGLAGFPGAKGDQG 301
Cdd:pfam09606 170 TPNQMGPNGGPGQGQAGGMNGGQQGPMGgqMPPQMGVPGMPGpaDAGAQMGQQAQANGG----MNPQQMGGAPNQVAMQQ 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803080    302 QPGLQGV--------PGPPGAVghPGAKGEPGSAGSPGRaGLPGSPGSPGATGLKGSKGDTGL---QGQQGRKGESGVPG 370
Cdd:pfam09606 246 QQPQQQGqqsqlgmgINQMQQM--PQGVGGGAGQGGPGQ-PMGPPGQQPGAMPNVMSIGDQNNyqqQQTRQQQQQQGGNH 322

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 5803080    371 PAGVKGEQGSPGLAG------PKGAPGQAGQKGDQGVKGSSGEQGvkGEKGERGENSV 422
Cdd:pfam09606 323 PAAHQQQMNQSVGQGgqvvalGGLNHLETWNPGNFGGLGANPMQR--GQPGMMSSPSP 378
 
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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