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Conserved domains on  [gi|1145587778|gb|AQN67651|]
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macrophage receptor [Homo sapiens]

Protein Classification

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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 ...
 403-498 1.64e-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: 143.64  E-value: 1.64e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778  403 VRIVGSSNR--GRAEVYYSGTWGTICDDEWQNSDAIVFCRMLGYSKGRALYK---VGAGTGQIWLDNVQCRGTESTLWSC 477
Cdd:smart00202   1 VRLVGGGSPceGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGsayFGPGSGPIWLDNVRCSGTEASLSDC 80

                           90       100
                   ....*....|....*....|.
gi 1145587778  478 TKNSWGHHDCSHEEDAGVECS 498
Cdd:smart00202  81 PHSGWGSHNCSHGEDAGVVCS 101
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 147-388 3.54e-35

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: 136.57  E-value: 3.54e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 147 KGEQGAPGLQGhkgamgmpgapgppgppaEKGAKGAMGRDGATGPSGPQGPPGVKGEAGLQGPQGAPGKQGATGTPGPQG 226
Cdd:NF038329  119 KGEPGPAGPAG------------------PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDG 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 227 EKGSKGDGGLIGPKGETGTKGEKGDLGLPGSKGDRGMKGDAGVMGPPGAQGsKGDFGRPGPPGLAGFPGAKGDQGQPGLQ 306
Cdd:NF038329  181 EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKD 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 307 GVPGPPGAVGHPGAKGEPGSAGSPGRAGLQGQqgrKGESGVPGPAGVKGEQGSPGLAGPKGAPGQAGQKGDQGVKGSSGE 386
Cdd:NF038329  260 GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ---NGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQ 336


                  ..
gi 1145587778 387 QG 388
Cdd:NF038329  337 PG 338
 
Name Accession Description Interval E-value
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 403-498 1.64e-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: 143.64  E-value: 1.64e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778  403 VRIVGSSNR--GRAEVYYSGTWGTICDDEWQNSDAIVFCRMLGYSKGRALYK---VGAGTGQIWLDNVQCRGTESTLWSC 477
Cdd:smart00202   1 VRLVGGGSPceGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGsayFGPGSGPIWLDNVRCSGTEASLSDC 80

                           90       100
                   ....*....|....*....|.
gi 1145587778  478 TKNSWGHHDCSHEEDAGVECS 498
Cdd:smart00202  81 PHSGWGSHNCSHGEDAGVVCS 101
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 407-498 2.68e-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: 2.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 407 GSSNRGRAEVYYSGTWGTICDDEWQNSDAIVFCRMLGY------SKGRALYKVGaGTGQIWLDNVQCRGTESTLWSCTKN 480
Cdd:pfam00530   2 SSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGCggavsaPSGCSYFGPG-STGPIWLDDVRCSGNETSLWQCPHR 80

                          90
                  ....*....|....*...
gi 1145587778 481 SWGHHDCSHEEDAGVECS 498
Cdd:pfam00530  81 PWGNHNCSHSEDAGVICS 98
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 147-388 3.54e-35

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: 136.57  E-value: 3.54e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 147 KGEQGAPGLQGhkgamgmpgapgppgppaEKGAKGAMGRDGATGPSGPQGPPGVKGEAGLQGPQGAPGKQGATGTPGPQG 226
Cdd:NF038329  119 KGEPGPAGPAG------------------PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDG 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 227 EKGSKGDGGLIGPKGETGTKGEKGDLGLPGSKGDRGMKGDAGVMGPPGAQGsKGDFGRPGPPGLAGFPGAKGDQGQPGLQ 306
Cdd:NF038329  181 EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKD 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 307 GVPGPPGAVGHPGAKGEPGSAGSPGRAGLQGQqgrKGESGVPGPAGVKGEQGSPGLAGPKGAPGQAGQKGDQGVKGSSGE 386
Cdd:NF038329  260 GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ---NGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQ 336


                  ..
gi 1145587778 387 QG 388
Cdd:NF038329  337 PG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 147-369 3.44e-31

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: 125.02  E-value: 3.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 147 KGEQGAPGLQGHKGAMGMPGAPGPPGPPAEKGAKGAMGRDGATGPSGPQGPPGVKGEAGLQGPQGAPGKQGATGTPGPQG 226
Cdd:NF038329  125 AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAG 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 227 EKGSKgdgGLIGPKGETGTKGEKGDLGLPGsKGDRGMKGDAGVMGPPGAQGSKGDFGRPGPPGLAGFPGAKGDQGQPGLQ 306
Cdd:NF038329  205 EQGPA---GPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGER 280

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1145587778 307 GVPGPPGAVGHPGAKGEPGSAGSPGRAGLQGQQGRKGESGVPGPAGVKGEQGSPGLAGpKGAP 369
Cdd:NF038329  281 GPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG-KPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 319-398 7.85e-14

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: 73.40  E-value: 7.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 319 GAKGEPGSAGSPGRAGLQGQQGRKGESGVPGPAGVKGEQGSPGLAGPKGAPGQAGQKGDQGVKGSSGEQGVKGEK---GE 395
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKgpqGP 196


                  ...
gi 1145587778 396 RGE 398
Cdd:NF038329  197 RGE 199
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
171-382 3.18e-12

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 68.52  E-value: 3.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 171 P---GPPAEKGAKGAMGRDGATGPSGPQGPPGVKGEAGLQGPQGAPGKQGATGTPGPQGEKGSKGDGGLIGPKGETGTKG 247
Cdd:COG5164    12 SdpgGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTR 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 248 EKGDLG---LPGSKGDRGMKGDAGVMGPPGAQGSKG--DFGRPGPPGLAG-FPGAKGDQGQPGLQGVPGPPGAVGHPGAK 321
Cdd:COG5164    92 PAGNTGgttPAGDGGATGPPDDGGATGPPDDGGSTTppSGGSTTPPGDGGsTPPGPGSTGPGGSTTPPGDGGSTTPPGPG 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1145587778 322 GEPGSAGSPGRAGlqgqQGRKGESGVPGPAGVKGEQGSPGLAGPKGAPGQAGQKGDQGVKG 382
Cdd:COG5164   172 GSTTPPDDGGSTT----PPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKT 228
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 283-338 4.99e-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: 55.19  E-value: 4.99e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1145587778 283 GRPGPPGLAGFPGAKGDQGQPGLQGVPGPPGAVGHPGAKGEPGSAGSPGRAGLQGQ 338
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 207-400 2.80e-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: 49.61  E-value: 2.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 207 QGPQGAPGKQGATGTPGPQGEKGSKGDGGLIGPKGETGTKGEKGDLG-------------LPGSKGDRGMKGDAGVMGPP 273
Cdd:cd21118   127 HGAYGSQGGPGVQGHGIPGGTGGPWASGGNYGTNSLGGSVGQGGNGGplnygtnsqgavaQPGYGTVRGNNQNSGCTNPP 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 274 --GAQGSKGDFGRPGPPGLAGFPGAKGDQGQP-----GLQGVPGPPGAVGHPGAKGEPGSAGSPGRAGLQGQQGRKGESG 346
Cdd:cd21118   207 psGSHESFSNSGGSSSSGSSGSQGSHGSNGQGssgssGGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGSGSGGSSSGGSN 286

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 347 VPGPAGVKGEQGSPGLA------GPKGAPGQAGQKGDQGVKGSSGEQGVKGEKGERGENS 400
Cdd:cd21118   287 GWGGSSSSGGSGGSGGGnkpecnNPGNDVRMAGGGGSQGSKESSGSHGSNGGNGQAEAVG 346
PHA03169 PHA03169
hypothetical protein; Provisional
 203-407 2.21e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 46.89  E-value: 2.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 203 EAGLQGPQGAPGKQGATGTPGPQGEKGSKGDGGLIGP---KGETGTKGEKGDLGLPGSKGDRGMKGDAGVMGPPGAQGSK 279
Cdd:PHA03169   59 RAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSgseSVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPP 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 280 GDFGRPGPpglaGFPGAKGDQGQPGLQGVPGPPGAVGHPGAKGEPGSAGSPGRAGLQGQQGRKGESGVPGPAGVKgEQGS 359
Cdd:PHA03169  139 SPPSHPGP----HEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPD-EPGE 213

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1145587778 360 PGLAGPKGAPGQAGQKGDQGVKGSSGEQgvKGEKGERGENSVSVRIVG 407
Cdd:PHA03169  214 PQSPTPQQAPSPNTQQAVEHEDEPTEPE--REGPPFPGHRSHSYTVVG 259
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 147-258 3.30e-05

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: 46.44  E-value: 3.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 147 KGEQGAPGLQGHKGAMGMPGAPGPPGPPAEKGAKGAMGRDGATGPSGPQGPPGVKGEAGLQGPQGAPGKQGATGTPGPQG 226
Cdd:NF038329  232 DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1145587778 227 EKGSKGDGGLIGPKGETGTKGEKGDLGLPGSK 258
Cdd:NF038329  312 LPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
 
Name Accession Description Interval E-value
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 403-498 1.64e-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: 143.64  E-value: 1.64e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778  403 VRIVGSSNR--GRAEVYYSGTWGTICDDEWQNSDAIVFCRMLGYSKGRALYK---VGAGTGQIWLDNVQCRGTESTLWSC 477
Cdd:smart00202   1 VRLVGGGSPceGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGsayFGPGSGPIWLDNVRCSGTEASLSDC 80

                           90       100
                   ....*....|....*....|.
gi 1145587778  478 TKNSWGHHDCSHEEDAGVECS 498
Cdd:smart00202  81 PHSGWGSHNCSHGEDAGVVCS 101
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 407-498 2.68e-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: 2.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 407 GSSNRGRAEVYYSGTWGTICDDEWQNSDAIVFCRMLGY------SKGRALYKVGaGTGQIWLDNVQCRGTESTLWSCTKN 480
Cdd:pfam00530   2 SSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGCggavsaPSGCSYFGPG-STGPIWLDDVRCSGNETSLWQCPHR 80

                          90
                  ....*....|....*...
gi 1145587778 481 SWGHHDCSHEEDAGVECS 498
Cdd:pfam00530  81 PWGNHNCSHSEDAGVICS 98
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 147-388 3.54e-35

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: 136.57  E-value: 3.54e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 147 KGEQGAPGLQGhkgamgmpgapgppgppaEKGAKGAMGRDGATGPSGPQGPPGVKGEAGLQGPQGAPGKQGATGTPGPQG 226
Cdd:NF038329  119 KGEPGPAGPAG------------------PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDG 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 227 EKGSKGDGGLIGPKGETGTKGEKGDLGLPGSKGDRGMKGDAGVMGPPGAQGsKGDFGRPGPPGLAGFPGAKGDQGQPGLQ 306
Cdd:NF038329  181 EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKD 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 307 GVPGPPGAVGHPGAKGEPGSAGSPGRAGLQGQqgrKGESGVPGPAGVKGEQGSPGLAGPKGAPGQAGQKGDQGVKGSSGE 386
Cdd:NF038329  260 GPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ---NGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQ 336


                  ..
gi 1145587778 387 QG 388
Cdd:NF038329  337 PG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 147-369 3.44e-31

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: 125.02  E-value: 3.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 147 KGEQGAPGLQGHKGAMGMPGAPGPPGPPAEKGAKGAMGRDGATGPSGPQGPPGVKGEAGLQGPQGAPGKQGATGTPGPQG 226
Cdd:NF038329  125 AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAG 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 227 EKGSKgdgGLIGPKGETGTKGEKGDLGLPGsKGDRGMKGDAGVMGPPGAQGSKGDFGRPGPPGLAGFPGAKGDQGQPGLQ 306
Cdd:NF038329  205 EQGPA---GPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGER 280

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1145587778 307 GVPGPPGAVGHPGAKGEPGSAGSPGRAGLQGQQGRKGESGVPGPAGVKGEQGSPGLAGpKGAP 369
Cdd:NF038329  281 GPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG-KPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 319-398 7.85e-14

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: 73.40  E-value: 7.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 319 GAKGEPGSAGSPGRAGLQGQQGRKGESGVPGPAGVKGEQGSPGLAGPKGAPGQAGQKGDQGVKGSSGEQGVKGEK---GE 395
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKgpqGP 196


                  ...
gi 1145587778 396 RGE 398
Cdd:NF038329  197 RGE 199
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
171-382 3.18e-12

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 68.52  E-value: 3.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 171 P---GPPAEKGAKGAMGRDGATGPSGPQGPPGVKGEAGLQGPQGAPGKQGATGTPGPQGEKGSKGDGGLIGPKGETGTKG 247
Cdd:COG5164    12 SdpgGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTR 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 248 EKGDLG---LPGSKGDRGMKGDAGVMGPPGAQGSKG--DFGRPGPPGLAG-FPGAKGDQGQPGLQGVPGPPGAVGHPGAK 321
Cdd:COG5164    92 PAGNTGgttPAGDGGATGPPDDGGATGPPDDGGSTTppSGGSTTPPGDGGsTPPGPGSTGPGGSTTPPGDGGSTTPPGPG 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1145587778 322 GEPGSAGSPGRAGlqgqQGRKGESGVPGPAGVKGEQGSPGLAGPKGAPGQAGQKGDQGVKG 382
Cdd:COG5164   172 GSTTPPDDGGSTT----PPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKT 228
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
148-373 3.71e-11

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 65.05  E-value: 3.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 148 GEQGAPGLQGHKGAMGMPGAPGPPGPPAEKGAKGAMGRDGATGPSGPqgppgvKGEAGLQGPQGAPGKQGATGTPGPQGE 227
Cdd:COG5164    43 GGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGG------TRPAGNTGGTTPAGDGGATGPPDDGGA 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 228 KGSKGDGGLIGPKGETGTKGEKGDLGLPGSKGDRGMKGDAGVMGPPGAQGSKGDFGRPGPPGL--AGFPGAKGDQGQPGL 305
Cdd:COG5164   117 TGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDggSTTPPNKGETGTDIP 196

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1145587778 306 QGVPGPPGAVGHPGAKGEPGSAGSPGRAGlqGQQGRKGESGVPGPAGVKGEQGSPGLAGPKGAPGQAG 373
Cdd:COG5164   197 TGGTPRQGPDGPVKKDDKNGKGNPPDDRG--GKTGPKDQRPKTNPIERRGPERPEAAALPAELTALEA 262
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 283-338 4.99e-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: 55.19  E-value: 4.99e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1145587778 283 GRPGPPGLAGFPGAKGDQGQPGLQGVPGPPGAVGHPGAKGEPGSAGSPGRAGLQGQ 338
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 277-331 1.60e-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: 53.65  E-value: 1.60e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1145587778 277 GSKGDFGRPGPPGLAGFPGAKGDQGQPGLQGVPGPPGAVGHPGAKGEPGSAGSPG 331
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 316-372 2.04e-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: 53.27  E-value: 2.04e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1145587778 316 GHPGAKGEPGSAGSPGRAGLQGQQGRKGESGVPGPAGVKGEQGSPGLAGPKGAPGQA 372
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 253-315 6.23e-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: 6.23e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1145587778 253 GLPGSKGDRGMKGDAGVMGPPGAQGSkgdfgrPGPPGLAGFPGAKGDQGQPGLQGVPGPPGAV 315
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGP------PGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 328-382 9.77e-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: 51.34  E-value: 9.77e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1145587778 328 GSPGRAGLQGQQGRKGESGVPGPAGVKGEQGSPGLAGPKGAPGQAGQKGDQGVKG 382
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 298-352 1.29e-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: 50.96  E-value: 1.29e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1145587778 298 GDQGQPGLQGVPGPPGAVGHPGAKGEPGSAGSPGRAGLQGQQGRKGESGVPGPAG 352
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 292-351 1.58e-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: 50.96  E-value: 1.58e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 292 GFPGAKGDQGQPGLQGVPGPPGAvghPGAKGEPGSAGSPGRAGLQGQQGRKGESGVPGPA 351
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGP---PGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 337-392 3.29e-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: 49.80  E-value: 3.29e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1145587778 337 GQQGRKGESGVPGPAGVKGEQGSPGLAGPKGAPGQAGQKGDQGVKGSSGEQGVKGE 392
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 247-303 2.31e-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: 47.49  E-value: 2.31e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1145587778 247 GEKGDLGLPGSKGDRGMKGDAGVMGPPGAQGSKGDFGRPGPPGLAGFPGAKGDQGQP 303
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 343-399 2.60e-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: 47.49  E-value: 2.60e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1145587778 343 GESGVPGPAGVKGEQGSPGLAGPKGAPGQAGQKGDQGVKGSSGEQGVKGEKGERGEN 399
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 202-256 4.68e-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: 46.72  E-value: 4.68e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1145587778 202 GEAGLQGPQGAPGKQGATGTPGPQGEKGSKGDGGLIGPKGETGTKGEKGDLGLPG 256
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 238-288 2.00e-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: 2.00e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1145587778 238 GPKGETGTKGEKGDLGLPGSKGDRGMKGDAGVMGPPGAQGSKGDFGRPGPP 288
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 207-400 2.80e-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: 49.61  E-value: 2.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 207 QGPQGAPGKQGATGTPGPQGEKGSKGDGGLIGPKGETGTKGEKGDLG-------------LPGSKGDRGMKGDAGVMGPP 273
Cdd:cd21118   127 HGAYGSQGGPGVQGHGIPGGTGGPWASGGNYGTNSLGGSVGQGGNGGplnygtnsqgavaQPGYGTVRGNNQNSGCTNPP 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 274 --GAQGSKGDFGRPGPPGLAGFPGAKGDQGQP-----GLQGVPGPPGAVGHPGAKGEPGSAGSPGRAGLQGQQGRKGESG 346
Cdd:cd21118   207 psGSHESFSNSGGSSSSGSSGSQGSHGSNGQGssgssGGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGSGSGGSSSGGSN 286

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 347 VPGPAGVKGEQGSPGLA------GPKGAPGQAGQKGDQGVKGSSGEQGVKGEKGERGENS 400
Cdd:cd21118   287 GWGGSSSSGGSGGSGGGnkpecnNPGNDVRMAGGGGSQGSKESSGSHGSNGGNGQAEAVG 346
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 340-396 2.90e-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: 44.41  E-value: 2.90e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1145587778 340 GRKGESGVPGPAGVKGEQGSPGLAGPKGAPGQAGQKGDQGVKGSSGEQGVKGEKGER 396
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 235-289 1.42e-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: 42.48  E-value: 1.42e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1145587778 235 GLIGPKGETGTKGEKGDLGLPGSKGDRGMKGDAGVMGPPGAQGSKGDFGRPGPPG 289
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 209-382 1.91e-05

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


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 47.37  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 209 PQGAPGKQGATGTPGPQGEKGSKGDGGLigPKGETGTKGEKGD--LGLPGSKGDRGMKGDAGVMGPPGAQGSKGDFGRPG 286
Cdd:COG5180   253 PEMRPPADAKERRRAAIGDTPAAEPPGL--PVLEAGSEPQSDApeAETARPIDVKGVASAPPATRPVRPPGGARDPGTPR 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 287 PP----GLAGFPGAKGDQGQP------GLQGVPGPPGAVGHPGAkGEPGSAGSPGRAGLQGQQGRKGESGVPGPAGVKGE 356
Cdd:COG5180   331 PGqpteRPAGVPEAASDAGQPpsayppAEEAVPGKPLEQGAPRP-GSSGGDGAPFQPPNGAPQPGLGRRGAPGPPMGAGD 409

                         170       180
                  ....*....|....*....|....*.
gi 1145587778 357 QGSPGLAGPKGAPGQAGQKGDQGVKG 382
Cdd:COG5180   410 LVQAALDGGGRETASLGGAAGGAGQG 435
PHA03169 PHA03169
hypothetical protein; Provisional
 203-407 2.21e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 46.89  E-value: 2.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 203 EAGLQGPQGAPGKQGATGTPGPQGEKGSKGDGGLIGP---KGETGTKGEKGDLGLPGSKGDRGMKGDAGVMGPPGAQGSK 279
Cdd:PHA03169   59 RAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSgseSVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPP 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 280 GDFGRPGPpglaGFPGAKGDQGQPGLQGVPGPPGAVGHPGAKGEPGSAGSPGRAGLQGQQGRKGESGVPGPAGVKgEQGS 359
Cdd:PHA03169  139 SPPSHPGP----HEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPD-EPGE 213

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1145587778 360 PGLAGPKGAPGQAGQKGDQGVKGSSGEQgvKGEKGERGENSVSVRIVG 407
Cdd:PHA03169  214 PQSPTPQQAPSPNTQQAVEHEDEPTEPE--REGPPFPGHRSHSYTVVG 259
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 201-250 2.37e-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: 41.71  E-value: 2.37e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1145587778 201 KGEAGLQGPQGAPGKQGATGTPGPQGEKGSKGDGGLIGPKGETGTKGEKG 250
Cdd:pfam01391   6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 147-258 3.30e-05

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: 46.44  E-value: 3.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 147 KGEQGAPGLQGHKGAMGMPGAPGPPGPPAEKGAKGAMGRDGATGPSGPQGPPGVKGEAGLQGPQGAPGKQGATGTPGPQG 226
Cdd:NF038329  232 DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1145587778 227 EKGSKGDGGLIGPKGETGTKGEKGDLGLPGSK 258
Cdd:NF038329  312 LPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
PHA03169 PHA03169
hypothetical protein; Provisional
 203-398 1.80e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 43.81  E-value: 1.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 203 EAGLQGPQGAPGKQGATGTP---GPQGEKGSKGDGGLIGPKGETGTKGEKGDLGLPGSKGDRGMKGDAGVMGPPGAQGSK 279
Cdd:PHA03169   32 QAGRRRGTAARAAKPAPPAPttsGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSA 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 280 GDFGRPGPPGLAGFPGAKGDQGQPGlqgvPGPPGAVGHPGAKGEPGSAG-SPGRAGLQGQQGRKGES--------GVPGP 350
Cdd:PHA03169  112 EELASGLSPENTSGSSPESPASHSP----PPSPPSHPGPHEPAPPESHNpSPNQQPSSFLQPSHEDSpeepepptSEPEP 187

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1145587778 351 AGVKGEQGSPGLAGPKGA-----PGQAGQKGDQGVKGSSGEQGVKGEKGERGE 398
Cdd:PHA03169  188 DSPGPPQSETPTSSPPPQsppdePGEPQSPTPQQAPSPNTQQAVEHEDEPTEP 240
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 269-388 1.08e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 269 VMGPPGAQGSKGDFGRPGPPGLAGFPGAKGDQGQPGLQGVPGPPGAVGHPGAKGEPGSAGSPGRAGLQGQQGRKGESGVP 348
Cdd:PRK07764  587 VVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGG 666

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1145587778 349 GPAGVKGEQGSPglAGPKGAPGQAGQKGDQGVKGSSGEQG 388
Cdd:PRK07764  667 DGWPAKAGGAAP--AAPPPAPAPAAPAAPAGAAPAQPAPA 704
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 156-403 2.62e-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: 40.38  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 156 QGHKGAMGMPGAPGPPGPPAekgakGAMGRDGATGPSGPQGPPGVKGEAGLQGPQgaPGKQGATGTPGPQGEKGSKGDGG 235
Cdd:pfam09606  92 QGTRPQMMGPMGPGPGGPMG-----QQMGGPGTASNLLASLGRPQMPMGGAGFPS--QMSRVGRMQPGGQAGGMMQPSSG 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 236 LIGPkgetGTKGEKGDLGLPGSKGDRGMKGdaGVMGPPGAQgSKGDFGRPGPPGLAGfPGAKGDQGQPGLQGVPGPPGAV 315
Cdd:pfam09606 165 QPGS----GTPNQMGPNGGPGQGQAGGMNG--GQQGPMGGQ-MPPQMGVPGMPGPAD-AGAQMGQQAQANGGMNPQQMGG 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 316 GHPG---AKGEPGSAGSPGRAGLQGQQGRKGESGVPG--PAGVKGEQG-----SPGLAGPKGAPGQAGQKGDQGVKGSSG 385
Cdd:pfam09606 237 APNQvamQQQQPQQQGQQSQLGMGINQMQQMPQGVGGgaGQGGPGQPMgppgqQPGAMPNVMSIGDQNNYQQQQTRQQQQ 316

                         250
                  ....*....|....*...
gi 1145587778 386 EQGVKGEKGERGENSVSV 403
Cdd:pfam09606 317 QQGGNHPAAHQQQMNQSV 334
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 265-374 2.93e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.35  E-value: 2.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 265 GDAGVMGPPGAQGSKGDFGRPGPPGLAGFPGAKGDQGQPGLQGVPGPPGAVGHPGAKGEPGSAGSPGRAGL----QGQQG 340
Cdd:PRK07764  589 GPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVpdasDGGDG 668

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1145587778 341 RKGESGVPGPAGVKGEQGSPGLAGPKGAPGQAGQ 374
Cdd:PRK07764  669 WPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPA 702
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 227-346 3.59e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 40.05  E-value: 3.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 227 EKGSKGDGGLIGPKG---ETGTKGEKGDLGLPGSKGDRGMKGDAGVMGPPGAQGSKGDFGRPGP----------PGLAGF 293
Cdd:PRK14959  369 ESLRPSGGGASAPSGsaaEGPASGGAATIPTPGTQGPQGTAPAAGMTPSSAAPATPAPSAAPSPrvpwddappaPPRSGI 448

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1145587778 294 PgAKGDQGQPGLQGVPGPPGAVGhpGAKGEPGSAGSPGRAG-------------LQGQQGRKGESG 346
Cdd:PRK14959  449 P-PRPAPRMPEASPVPGAPDSVA--SASDAPPTLGDPSDTAehtpsgprtwdgfLEFCQGRNGQGG 511
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 178-380 4.35e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.58  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 178 GAKGAMGRDGATGPSGPQGPPGVKGEAGLQGPQGAPGKQGATGTPGPQGEkGSKGDGGLIGPKGETGTKGEKGDLGLPGS 257
Cdd:PRK07764  589 GPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAE-ASAAPAPGVAAPEHHPKHVAVPDASDGGD 667

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 258 KGDRGMKGDAGVMGPPGAQGskgdfgrPGPPGLAGFPGAKGDQGQPGLQGVPGPPGAVGHPGAKGEPGSAGSPGRAGLQG 337
Cdd:PRK07764  668 GWPAKAGGAAPAAPPPAPAP-------AAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVP 740

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1145587778 338 QQGRKGESGVPGPAGVKGEQ-GSPGLAGPKGAPGQAGQKGDQGV 380
Cdd:PRK07764  741 LPPEPDDPPDPAGAPAQPPPpPAPAPAAAPAAAPPPSPPSEEEE 784
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 250-415 7.11e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 39.12  E-value: 7.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 250 GDLGLPGSKGDRgmKGD------AGVMGPPGAQGSKGDFGRPGPPGLAGFPGAKGDQGQPGLQGVPGPPGAVGHPGAKGE 323
Cdd:PRK12678   36 KQLGIKGTSGMR--KGEliaaikEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAA 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145587778 324 PGSAGSPGRAGLQGQQGRkgesgvpgPAGVKGEQGSPGLAGPKGAPGQAGQKGDQGVKGSSGEQGVKGEKGERGENSVSV 403
Cdd:PRK12678  114 AAAEAASAPEAAQARERR--------ERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEA 185

                         170
                  ....*....|..
gi 1145587778 404 RIVGSSNRGRAE 415
Cdd:PRK12678  186 ERGERGRREERG 197
 
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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