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Conserved domains on  [gi|1622849489|ref|XP_014965420|]
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macrophage receptor MARCO isoform X1 [Macaca mulatta]

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 2.63e-42

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: 146.33  E-value: 2.63e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489  424 VRIVGSSNR--GRAEVYYGGTWGTICDDEWHNSDATVFCRMLGYSRGRALYK---VGAGTGQIWLDNVQCRGTESTLWSC 498
Cdd:smart00202   1 VRLVGGGSPceGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGsayFGPGSGPIWLDNVRCSGTEASLSDC 80

                           90       100
                   ....*....|....*....|.
gi 1622849489  499 SKNSWGSHDCSHEEDAGVECS 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 ...
 201-419 5.15e-37

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: 141.97  E-value: 5.15e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 201 KGEAGLQGPQGAPGKQGATGTPGPQGEKGSKGDGGLIGPKGEtgtKGDKGDLGLPGSKGDKGMKGDAGVMGPpgaQGSKG 280
Cdd:NF038329  125 AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGP---QGEAGPQGPAGKDGEAGAKGPAGEKGP---QGPRG 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 281 DSGRPGSPGLAGFPGAKGDPGQPGLQGVPGPPGAvGQPGAKGEPGSAGSRGLTGLPGSPGSPGAAGLKGSKGDTGLQGQQ 360
Cdd:NF038329  199 ETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKD 277

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849489 361 GVKGEPGVPGPAGVKGEQGSPGLAGSKGAPGRAGQKGDQGVKGSSGERGVKGEKGETGQ 419
Cdd:NF038329  278 GERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQ 336
 
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 2.63e-42

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: 146.33  E-value: 2.63e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489  424 VRIVGSSNR--GRAEVYYGGTWGTICDDEWHNSDATVFCRMLGYSRGRALYK---VGAGTGQIWLDNVQCRGTESTLWSC 498
Cdd:smart00202   1 VRLVGGGSPceGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGsayFGPGSGPIWLDNVRCSGTEASLSDC 80

                           90       100
                   ....*....|....*....|.
gi 1622849489  499 SKNSWGSHDCSHEEDAGVECS 519
Cdd:smart00202  81 PHSGWGSHNCSHGEDAGVVCS 101
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 201-419 5.15e-37

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: 141.97  E-value: 5.15e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 201 KGEAGLQGPQGAPGKQGATGTPGPQGEKGSKGDGGLIGPKGEtgtKGDKGDLGLPGSKGDKGMKGDAGVMGPpgaQGSKG 280
Cdd:NF038329  125 AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGP---QGEAGPQGPAGKDGEAGAKGPAGEKGP---QGPRG 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 281 DSGRPGSPGLAGFPGAKGDPGQPGLQGVPGPPGAvGQPGAKGEPGSAGSRGLTGLPGSPGSPGAAGLKGSKGDTGLQGQQ 360
Cdd:NF038329  199 ETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKD 277

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849489 361 GVKGEPGVPGPAGVKGEQGSPGLAGSKGAPGRAGQKGDQGVKGSSGERGVKGEKGETGQ 419
Cdd:NF038329  278 GERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQ 336
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 428-519 1.05e-36

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: 130.96  E-value: 1.05e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 428 GSSNRGRAEVYYGGTWGTICDDEWHNSDATVFCRMLGY------SRGRALYKVGaGTGQIWLDNVQCRGTESTLWSCSKN 501
Cdd:pfam00530   2 SSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGCggavsaPSGCSYFGPG-STGPIWLDDVRCSGNETSLWQCPHR 80

                          90
                  ....*....|....*...
gi 1622849489 502 SWGSHDCSHEEDAGVECS 519
Cdd:pfam00530  81 PWGNHNCSHSEDAGVICS 98
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 145-371 2.55e-32

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: 128.87  E-value: 2.55e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 145 GIKGEQGPPGLQGHKGAMGMPGAPGPPGPPAEKGAKGAAGRDGATGPPGPQGPPGVKGEAGLQGPQGAPGKQGATGTPGP 224
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 225 QGEKGSKGDGGLIGPKGETGTKGDKGDLGLPGSKGD--KGMKGDAGVMGPPGAQGSKGDSGRPGSPGLAGFPGAKGDPGQ 302
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849489 303 PGLQGVPGPPGAVGQPGAKGEPGSAGSRGLTGLPGSPGSPGAAGLKGSKgdtGLQGQQGVKGEPGVPGP 371
Cdd:NF038329  277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKD---GLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 238-420 3.76e-32

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: 128.10  E-value: 3.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 238 GPKGETGTKGDKGDLGLPGSKGDKGMKGDAGVMGPPGAQGSKGDSGRPGSPGLAGFPGAKGDPGQPGLQGvpgPPGAVGQ 317
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG---PAGEKGP 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 318 PGAKGEPGSAGSRGLTGLPGSPGSPGAAGLKGSKGDTGlQGQQGVKGEPGvpgPAGVKGEQGSPGLAGSKGAPGRAGQKG 397
Cdd:NF038329  194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPG---PTGEDGPQGPDGPAGKDGPRGDRGEAG 269

                         170       180
                  ....*....|....*....|...
gi 1622849489 398 DQGVKGSSGERGVKGEKGETGQN 420
Cdd:NF038329  270 PDGPDGKDGERGPVGPAGKDGQN 292
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 138-336 2.81e-24

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: 105.37  E-value: 2.81e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 138 TQNPGMFGIKGEQGPPGLQGHKGAMGMPGAPGPPGPPAEKGAKGAAGRDGATGPPGPqgppgvKGEAGLQGPQGAPGKQG 217
Cdd:NF038329  143 TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE------TGPAGEQGPAGPAGPDG 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 218 ATGTPGPQGEKGSKGDG--GLIGPKGETGTKGDKGDLGLP---GSKGDKGMKGDAGVMGPPGAQGSKGDSGRPGSPGLAG 292
Cdd:NF038329  217 EAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGPAgkdGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDG 296

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1622849489 293 FPGAKGDPGQPGLQGVPGPPGAVGQPGAKGEPGSAGSRGLTGLP 336
Cdd:NF038329  297 LPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
178-423 4.44e-13

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 71.21  E-value: 4.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 178 GAKGAAGRDGATGPPGPQGPpgvKGEAGLQGPQGAPGKQGATGTPGPQGEKGSKGDGGLIGPKGETGTKGDkgdlglPGS 257
Cdd:COG5164    16 GVTTPAGSQGSTKPAQNQGS---TRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTP------AQN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 258 KGDKGMKGDAGVMGPPGAQGSKGDSGRPGSPGLAGFPGAKGdPGQPGLQGVPGPPGAV-GQPGAKGEPGSAGSRGLTGLP 336
Cdd:COG5164    87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTT-PPSGGSTTPPGDGGSTpPGPGSTGPGGSTTPPGDGGST 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 337 GSPGSPGAAGLKGSKGDTGlqgqQGVKGEPGVPGPAGVKGEQGSPGLAGSKGAPGRAGQKGDQGVK-GSSGERGVKGEKG 415
Cdd:COG5164   166 TPPGPGGSTTPPDDGGSTT----PPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKtGPKDQRPKTNPIE 241


                  ....*...
gi 1622849489 416 ETGQNAVS 423
Cdd:COG5164   242 RRGPERPE 249
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 268-324 8.11e-11

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: 57.50  E-value: 8.11e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622849489 268 GVMGPPGAQGSKGDSGRPGSPGLAGFPGAKGDPGQPGLQGVPGPPGAVGQPGAKGEP 324
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 353-419 3.65e-07

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: 52.60  E-value: 3.65e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849489 353 DTGLQGQQ--GVKGEPGVPGPAGVKGEQGSPGLAGSKGAPGRAGQKGDQGVKGSSGERGVKGEKGETGQ 419
Cdd:NF038329  107 DEGLQQLKgdGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP 175
PHA03169 PHA03169
hypothetical protein; Provisional
 203-421 5.12e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 45.73  E-value: 5.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 203 EAGLQGPQGAPGKQGATGTP---GPQGEKGSKGDGGLIGPKGETGTKGDKGDLGLPGSKGDKGmKGDAGVMGPpgaQGSK 279
Cdd:PHA03169   32 QAGRRRGTAARAAKPAPPAPttsGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSG-SGSESVGSP---TPSP 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 280 GDSGRPGSPGLAGFPGAKGDPGQPGLQGVPGPPGAVGQPGAKGEPGSAGsrgltglpGSPGSPGAAGLKGSKGDTGLQGQ 359
Cdd:PHA03169  108 SGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHN--------PSPNQQPSSFLQPSHEDSPEEPE 179

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622849489 360 QGvKGEPGVPGPAGVKGEQGSPGLAGSKGA--PGRAGQKGDQGVKGSSGERGVKGEKGETGQNA 421
Cdd:PHA03169  180 PP-TSEPEPDSPGPPQSETPTSSPPPQSPPdePGEPQSPTPQQAPSPNTQQAVEHEDEPTEPER 242
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 207-415 1.47e-04

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: 44.22  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 207 QGPQGAPGKQGATGTPGPQGEKGSKGDGGLIGPKGETGTKGDKGDLG-------------LPGSKGDKGMKGDAGVMGPP 273
Cdd:cd21118   127 HGAYGSQGGPGVQGHGIPGGTGGPWASGGNYGTNSLGGSVGQGGNGGplnygtnsqgavaQPGYGTVRGNNQNSGCTNPP 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 274 --GAQGSKGDSGRPGSPGLAGFPGAKGDPGQpGLQGVPGPPGAVGQPGakGEPGSAGSRGLTGLPGSPGSPGAAGLKGSK 351
Cdd:cd21118   207 psGSHESFSNSGGSSSSGSSGSQGSHGSNGQ-GSSGSSGGQGNGGNNG--SSSSNSGNSGGSNGGSSGNSGSGSGGSSSG 283

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849489 352 GDTGLQGQQGVKGEPGVPGPAGVK--GEQGSPGLAGSKGAPGRAGQKGDQGVKGSSGERGVKGEKG 415
Cdd:cd21118   284 GSNGWGGSSSSGGSGGSGGGNKPEcnNPGNDVRMAGGGGSQGSKESSGSHGSNGGNGQAEAVGGLN 349
 
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 2.63e-42

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: 146.33  E-value: 2.63e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489  424 VRIVGSSNR--GRAEVYYGGTWGTICDDEWHNSDATVFCRMLGYSRGRALYK---VGAGTGQIWLDNVQCRGTESTLWSC 498
Cdd:smart00202   1 VRLVGGGSPceGRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGsayFGPGSGPIWLDNVRCSGTEASLSDC 80

                           90       100
                   ....*....|....*....|.
gi 1622849489  499 SKNSWGSHDCSHEEDAGVECS 519
Cdd:smart00202  81 PHSGWGSHNCSHGEDAGVVCS 101
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 201-419 5.15e-37

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: 141.97  E-value: 5.15e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 201 KGEAGLQGPQGAPGKQGATGTPGPQGEKGSKGDGGLIGPKGEtgtKGDKGDLGLPGSKGDKGMKGDAGVMGPpgaQGSKG 280
Cdd:NF038329  125 AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGP---QGEAGPQGPAGKDGEAGAKGPAGEKGP---QGPRG 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 281 DSGRPGSPGLAGFPGAKGDPGQPGLQGVPGPPGAvGQPGAKGEPGSAGSRGLTGLPGSPGSPGAAGLKGSKGDTGLQGQQ 360
Cdd:NF038329  199 ETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKD 277

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849489 361 GVKGEPGVPGPAGVKGEQGSPGLAGSKGAPGRAGQKGDQGVKGSSGERGVKGEKGETGQ 419
Cdd:NF038329  278 GERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQ 336
SRCR pfam00530
Scavenger receptor cysteine-rich domain; These domains are disulphide rich extracellular ...
 428-519 1.05e-36

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: 130.96  E-value: 1.05e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 428 GSSNRGRAEVYYGGTWGTICDDEWHNSDATVFCRMLGY------SRGRALYKVGaGTGQIWLDNVQCRGTESTLWSCSKN 501
Cdd:pfam00530   2 SSPCEGRVEVYHNGSWGTVCDDGWDLRDAHVVCRQLGCggavsaPSGCSYFGPG-STGPIWLDDVRCSGNETSLWQCPHR 80

                          90
                  ....*....|....*...
gi 1622849489 502 SWGSHDCSHEEDAGVECS 519
Cdd:pfam00530  81 PWGNHNCSHSEDAGVICS 98
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 145-371 2.55e-32

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: 128.87  E-value: 2.55e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 145 GIKGEQGPPGLQGHKGAMGMPGAPGPPGPPAEKGAKGAAGRDGATGPPGPQGPPGVKGEAGLQGPQGAPGKQGATGTPGP 224
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 225 QGEKGSKGDGGLIGPKGETGTKGDKGDLGLPGSKGD--KGMKGDAGVMGPPGAQGSKGDSGRPGSPGLAGFPGAKGDPGQ 302
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK 276

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849489 303 PGLQGVPGPPGAVGQPGAKGEPGSAGSRGLTGLPGSPGSPGAAGLKGSKgdtGLQGQQGVKGEPGVPGP 371
Cdd:NF038329  277 DGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKD---GLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 238-420 3.76e-32

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: 128.10  E-value: 3.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 238 GPKGETGTKGDKGDLGLPGSKGDKGMKGDAGVMGPPGAQGSKGDSGRPGSPGLAGFPGAKGDPGQPGLQGvpgPPGAVGQ 317
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG---PAGEKGP 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 318 PGAKGEPGSAGSRGLTGLPGSPGSPGAAGLKGSKGDTGlQGQQGVKGEPGvpgPAGVKGEQGSPGLAGSKGAPGRAGQKG 397
Cdd:NF038329  194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPG---PTGEDGPQGPDGPAGKDGPRGDRGEAG 269

                         170       180
                  ....*....|....*....|...
gi 1622849489 398 DQGVKGSSGERGVKGEKGETGQN 420
Cdd:NF038329  270 PDGPDGKDGERGPVGPAGKDGQN 292
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 138-336 2.81e-24

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: 105.37  E-value: 2.81e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 138 TQNPGMFGIKGEQGPPGLQGHKGAMGMPGAPGPPGPPAEKGAKGAAGRDGATGPPGPqgppgvKGEAGLQGPQGAPGKQG 217
Cdd:NF038329  143 TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE------TGPAGEQGPAGPAGPDG 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 218 ATGTPGPQGEKGSKGDG--GLIGPKGETGTKGDKGDLGLP---GSKGDKGMKGDAGVMGPPGAQGSKGDSGRPGSPGLAG 292
Cdd:NF038329  217 EAGPAGEDGPAGPAGDGqqGPDGDPGPTGEDGPQGPDGPAgkdGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDG 296

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1622849489 293 FPGAKGDPGQPGLQGVPGPPGAVGQPGAKGEPGSAGSRGLTGLP 336
Cdd:NF038329  297 LPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
178-423 4.44e-13

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 71.21  E-value: 4.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 178 GAKGAAGRDGATGPPGPQGPpgvKGEAGLQGPQGAPGKQGATGTPGPQGEKGSKGDGGLIGPKGETGTKGDkgdlglPGS 257
Cdd:COG5164    16 GVTTPAGSQGSTKPAQNQGS---TRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTP------AQN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 258 KGDKGMKGDAGVMGPPGAQGSKGDSGRPGSPGLAGFPGAKGdPGQPGLQGVPGPPGAV-GQPGAKGEPGSAGSRGLTGLP 336
Cdd:COG5164    87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTT-PPSGGSTTPPGDGGSTpPGPGSTGPGGSTTPPGDGGST 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 337 GSPGSPGAAGLKGSKGDTGlqgqQGVKGEPGVPGPAGVKGEQGSPGLAGSKGAPGRAGQKGDQGVK-GSSGERGVKGEKG 415
Cdd:COG5164   166 TPPGPGGSTTPPDDGGSTT----PPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKtGPKDQRPKTNPIE 241


                  ....*...
gi 1622849489 416 ETGQNAVS 423
Cdd:COG5164   242 RRGPERPE 249
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
148-400 1.73e-12

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 69.67  E-value: 1.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 148 GEQGPPGLQGHKGAMGMPGAPGPPGPPAEKGAKGAAGRD---GATGPPGPQGPPGVKGEAGLQGPQGAPGKQGATGTPGP 224
Cdd:COG5164    16 GVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTtpaGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 225 QGEKGSKGDGGLIGPKGETGTKGDKGDLG--LPGSKGDKGMKGDAGVMGP-PGAQGSKGDSGRPGSPGLAGFPGAKGDPG 301
Cdd:COG5164    96 TGGTTPAGDGGATGPPDDGGATGPPDDGGstTPPSGGSTTPPGDGGSTPPgPGSTGPGGSTTPPGDGGSTTPPGPGGSTT 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 302 QPGLQGVPGPP--GAVGQPGAKGEPGSAGSRGLTGLPGS-------PGSPGAAGLKGSKGDTGLQGQQGVKGEPGVPGPA 372
Cdd:COG5164   176 PPDDGGSTTPPnkGETGTDIPTGGTPRQGPDGPVKKDDKngkgnppDDRGGKTGPKDQRPKTNPIERRGPERPEAAALPA 255

                         250       260
                  ....*....|....*....|....*...
gi 1622849489 373 GVKGEQGSPGLAgskgAPGRAGQKGDQG 400
Cdd:COG5164   256 ELTALEAENRAA----NPEPATKTIPET 279
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 268-324 8.11e-11

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: 57.50  E-value: 8.11e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622849489 268 GVMGPPGAQGSKGDSGRPGSPGLAGFPGAKGDPGQPGLQGVPGPPGAVGQPGAKGEP 324
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 271-327 8.82e-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: 54.42  E-value: 8.82e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622849489 271 GPPGAQGSKGDSGRPGSPGLAGFPGAKGDPGQPGLQGVPGPPGAVGQPGAKGEPGSA 327
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 283-339 1.25e-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: 54.04  E-value: 1.25e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622849489 283 GRPGSPGLAGFPGAKGDPGQPGLQGVPGPPGAVGQPGAKGEPGSAGSRGLTGLPGSP 339
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 292-346 1.48e-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: 1.48e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622849489 292 GFPGAKGDPGQPGLQGVPGPPGAVGQPGAKGEPGSAGSRGLTGLPGSPGSPGAAG 346
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 295-349 6.75e-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: 6.75e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622849489 295 GAKGDPGQPGLQGVPGPPGAVGQPGAKGEPGSAGSRGLTGLPGSPGSPGAAGLKG 349
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 277-331 9.24e-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: 51.73  E-value: 9.24e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622849489 277 GSKGDSGRPGSPGLAGFPGAKGDPGQPGLQGVPGPPGAVGQPGAKGEPGSAGSRG 331
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 298-352 1.04e-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: 1.04e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622849489 298 GDPGQPGLQGVPGPPGAVGQPGAKGEPGSAGSRGLTGLPGSPGSPGAAGLKGSKG 352
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 259-315 1.66e-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: 50.96  E-value: 1.66e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622849489 259 GDKGMKGDAGVMGPPGAQGSKGDSGRPGSPGLAGFPGAKGDPGQPGLQGVPGPPGAV 315
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 307-372 1.98e-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: 1.98e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849489 307 GVPGPPGAVGQPGAKGEPGSAGSRGLTGLPGSPGSPGAAGLKGSKGDtglqgqqgvKGEPGVPGPA 372
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP---------PGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 340-395 6.00e-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: 49.41  E-value: 6.00e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849489 340 GSPGAAGLKGSKGDTGLQGQQGVKGEPGVPGPAGVKGEQGSPGLAGSKGAPGRAGQ 395
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 334-390 6.68e-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: 49.03  E-value: 6.68e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622849489 334 GLPGSPGSPGAAGLKGSKGDTGLQGQQGVKGEPGVPGPAGVKGEQGSPGLAGSKGAP 390
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 322-377 7.30e-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: 49.03  E-value: 7.30e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849489 322 GEPGSAGSRGLTGLPGSPGSPGAAGLKGSKGDTGLQGQQGVKGEPGVPGPAGVKGE 377
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 337-391 1.19e-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: 1.19e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622849489 337 GSPGSPGAAGLKGSKGDTGLQGQQGVKGEPGVPGPAGVKGEQGSPGLAGSKGAPG 391
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 325-381 1.30e-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: 1.30e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622849489 325 GSAGSRGLTGLPGSPGSPGAAGLKGSKGDTGLQGQQGVKGEPGVPGPAGVKGEQGSP 381
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 358-413 2.71e-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: 2.71e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849489 358 GQQGVKGEPGVPGPAGVKGEQGSPGLAGSKGAPGRAGQKGDQGVKGSSGERGVKGE 413
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 353-419 3.65e-07

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: 52.60  E-value: 3.65e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622849489 353 DTGLQGQQ--GVKGEPGVPGPAGVKGEQGSPGLAGSKGAPGRAGQKGDQGVKGSSGERGVKGEKGETGQ 419
Cdd:NF038329  107 DEGLQQLKgdGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP 175
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 331-385 4.02e-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: 4.02e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622849489 331 GLTGLPGSPGSPGAAGLKGSKGDTGLQGQQGVKGEPGVPGPAGVKGEQGSPGLAG 385
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 364-420 5.66e-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: 5.66e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622849489 364 GEPGVPGPAGVKGEQGSPGLAGSKGAPGRAGQKGDQGVKGSSGERGVKGEKGETGQN 420
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 349-403 2.39e-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: 2.39e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622849489 349 GSKGDTGLQGQQGVKGEPGVPGPAGVKGEQGSPGLAGSKGAPGRAGQKGDQGVKG 403
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 361-416 3.99e-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: 44.02  E-value: 3.99e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849489 361 GVKGEPGVPGPAGVKGEQGSPGLAGSKGAPGRAGQKGDQGVKGSSGERGVKGEKGE 416
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 208-262 4.62e-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: 44.02  E-value: 4.62e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622849489 208 GPQGAPGKQGATGTPGPQGEKGSKGDGGLIGPKGETGTKGDKGDLGLPGSKGDKG 262
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 355-409 6.14e-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: 6.14e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622849489 355 GLQGQQGVKGEPGVPGPAGVKGEQGSPGLAGSKGAPGRAGQKGDQGVKGSSGERG 409
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 208-441 8.38e-06

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: 48.47  E-value: 8.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 208 GPQGAPGKQ----GATGTPGPQGEKGSKGDGGLIGPKGETGTKGDKGDLGLPGSKGDKGMKGDAGVMGPPGAQGSKGDSG 283
Cdd:pfam09606 105 GPGGPMGQQmggpGTASNLLASLGRPQMPMGGAGFPSQMSRVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQ 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 284 RPGSPGLAGFPGAKGDPGQPGLQGVPGPPGAVGQ-----PGAKGEPGSAGSRGLTGLPGSPGSPGAAGLKGSKGDTGLQG 358
Cdd:pfam09606 185 AGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQmgqqaQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMGINQM 264

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 359 QQGVKGEPGVpGPAGVKGeQGSPGLAGSKGAPGRAGQKGDQGVKGSSGERGVKGEKGETGQNAVSVRIVGSSNRGRAEVY 438
Cdd:pfam09606 265 QQMPQGVGGG-AGQGGPG-QPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQGGQVVA 342


                  ...
gi 1622849489 439 YGG 441
Cdd:pfam09606 343 LGG 345
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 205-259 1.46e-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: 1.46e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622849489 205 GLQGPQGAPGKQGATGTPGPQGEKGSKGDGGLIGPKGETGTKGDKGDLGLPGSKG 259
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 235-289 1.69e-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: 1.69e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622849489 235 GLIGPKGETGTKGDKGDLGLPGSKGDKGMKGDAGVMGPPGAQGSKGDSGRPGSPG 289
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 238-292 2.06e-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: 42.10  E-value: 2.06e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622849489 238 GPKGETGTKGDKGDLGLPGSKGDKGMKGDAGVMGPPGAQGSKGDSGRPGSPGLAG 292
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PHA03169 PHA03169
hypothetical protein; Provisional
 203-421 5.12e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 45.73  E-value: 5.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 203 EAGLQGPQGAPGKQGATGTP---GPQGEKGSKGDGGLIGPKGETGTKGDKGDLGLPGSKGDKGmKGDAGVMGPpgaQGSK 279
Cdd:PHA03169   32 QAGRRRGTAARAAKPAPPAPttsGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSG-SGSESVGSP---TPSP 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 280 GDSGRPGSPGLAGFPGAKGDPGQPGLQGVPGPPGAVGQPGAKGEPGSAGsrgltglpGSPGSPGAAGLKGSKGDTGLQGQ 359
Cdd:PHA03169  108 SGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHN--------PSPNQQPSSFLQPSHEDSPEEPE 179

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622849489 360 QGvKGEPGVPGPAGVKGEQGSPGLAGSKGA--PGRAGQKGDQGVKGSSGERGVKGEKGETGQNA 421
Cdd:PHA03169  180 PP-TSEPEPDSPGPPQSETPTSSPPPQSPPdePGEPQSPTPQQAPSPNTQQAVEHEDEPTEPER 242
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 202-250 5.88e-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: 40.94  E-value: 5.88e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1622849489 202 GEAGLQGPQGAPGKQGATGTPGPQGEKGSKGDGGLIGPKGETGTKGDKG 250
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 209-413 7.08e-05

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


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 45.44  E-value: 7.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 209 PQGAPGKQGATGTPGPQGEKGSKGDGGLIGPKGETGTKGDKGDLGLPGSKGDKGMKGDAGVMGPPGAQGSKGDSG--RPG 286
Cdd:COG5180   253 PEMRPPADAKERRRAAIGDTPAAEPPGLPVLEAGSEPQSDAPEAETARPIDVKGVASAPPATRPVRPPGGARDPGtpRPG 332

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 287 SPGL--AGFPGAKGDPGQPGLQGVPGPPGAVGQPGAKGEPGSAGSrgltGLPGSPGSPGAaglkgskgdtglQGQQGVKG 364
Cdd:COG5180   333 QPTErpAGVPEAASDAGQPPSAYPPAEEAVPGKPLEQGAPRPGSS----GGDGAPFQPPN------------GAPQPGLG 396

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1622849489 365 EPGVPGPAGVKGEQGSPGLAGSKGAPGRAGQKGDQGVKGsSGERGVKGE 413
Cdd:COG5180   397 RRGAPGPPMGAGDLVQAALDGGGRETASLGGAAGGAGQG-PKADFVPGD 444
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 207-415 1.47e-04

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: 44.22  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 207 QGPQGAPGKQGATGTPGPQGEKGSKGDGGLIGPKGETGTKGDKGDLG-------------LPGSKGDKGMKGDAGVMGPP 273
Cdd:cd21118   127 HGAYGSQGGPGVQGHGIPGGTGGPWASGGNYGTNSLGGSVGQGGNGGplnygtnsqgavaQPGYGTVRGNNQNSGCTNPP 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 274 --GAQGSKGDSGRPGSPGLAGFPGAKGDPGQpGLQGVPGPPGAVGQPGakGEPGSAGSRGLTGLPGSPGSPGAAGLKGSK 351
Cdd:cd21118   207 psGSHESFSNSGGSSSSGSSGSQGSHGSNGQ-GSSGSSGGQGNGGNNG--SSSSNSGNSGGSNGGSSGNSGSGSGGSSSG 283

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849489 352 GDTGLQGQQGVKGEPGVPGPAGVK--GEQGSPGLAGSKGAPGRAGQKGDQGVKGSSGERGVKGEKG 415
Cdd:cd21118   284 GSNGWGGSSSSGGSGGSGGGNKPEcnNPGNDVRMAGGGGSQGSKESSGSHGSNGGNGQAEAVGGLN 349
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 265-410 3.99e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 3.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 265 GDAGVMGPPGAQGSKGDSGRPGSPGLAGFPGAKGDPGQPGLQGVPGPPGAVGQPGAKGEPGSAGSRGLTGLPGSPGSPGA 344
Cdd:PRK07764  589 GPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDG 668

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622849489 345 AGlkGSKGDTGLQGQQGVKGEPGVPGPAGVKGEQGSPGLAGSKGAPGRAGQKGDQGVKGSSGERGV 410
Cdd:PRK07764  669 WP--AKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPS 732
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 269-399 5.62e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.67  E-value: 5.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 269 VMGPPGAQGSKGDSGRPGSPGLAGFPGAKGDPGQPGLQGVPGPPGAVGQPGAKGEPGSAGSRGLTGLPGSPGSPgAAGLK 348
Cdd:PRK07764  587 VVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVP-DASDG 665

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622849489 349 GSKGDTGLQGQQGVKGEPGVPGPAGVKGEQGSPGLAGSKGAPGRAGQKGDQ 399
Cdd:PRK07764  666 GDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADD 716
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 256-353 7.07e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 42.36  E-value: 7.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 256 GSKGDKGMKGDAGVMGPPGAQGSKGDSGRPGSPGLAGFPGAKG-----DPGQPGLQGVPGPPGAVGQPgaKGEPGSAGSR 330
Cdd:PRK14959  383 GSAAEGPASGGAATIPTPGTQGPQGTAPAAGMTPSSAAPATPApsaapSPRVPWDDAPPAPPRSGIPP--RPAPRMPEAS 460

                          90       100
                  ....*....|....*....|...
gi 1622849489 331 GLTGLPGSPGSpgAAGLKGSKGD 353
Cdd:PRK14959  461 PVPGAPDSVAS--ASDAPPTLGD 481
PHA03169 PHA03169
hypothetical protein; Provisional
 203-394 1.09e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 41.49  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 203 EAGLQGPQGAPGKQGATGTPGPQGEKGSKGDGGLIGP---KGETGTKGDKGDLGLPGSKGDKGMKGDAGVMGPPGAQGSK 279
Cdd:PHA03169   59 RAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSgseSVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPP 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 280 GDSGRPGSPGLAGFPGAKGDPGQPGLQGV---------PGPPGAVGQPGAKGEPGSAGSRGLTGLPGSPG-SPGAAGLKG 349
Cdd:PHA03169  139 SPPSHPGPHEPAPPESHNPSPNQQPSSFLqpshedspeEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPdEPGEPQSPT 218

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1622849489 350 SKGDTGLQGQQGVKGEPGVPGPAGVKGEQGSPGL----AGSKGAPGRAG 394
Cdd:PHA03169  219 PQQAPSPNTQQAVEHEDEPTEPEREGPPFPGHRShsytVVGWKPSTRPG 267
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 256-480 1.19e-03

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: 41.52  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 256 GSKGDKGMKGDAGVMGPPGAQGSKGDSGRPGSPGLAGFPGAKGDPGQPGLQGVPGPP-------GAVGQPGAKGEPGSAG 328
Cdd:cd21118   119 NSWQGSGGHGAYGSQGGPGVQGHGIPGGTGGPWASGGNYGTNSLGGSVGQGGNGGPLnygtnsqGAVAQPGYGTVRGNNQ 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 329 SRGLTGLPGSpGSPGAAGLKGSKGDTGLQGQQGVKGEPGvpgpAGVKGEQGSPGLAGSKGAPGRAGQKGDQGVKGSSGER 408
Cdd:cd21118   199 NSGCTNPPPS-GSHESFSNSGGSSSSGSSGSQGSHGSNG----QGSSGSSGGQGNGGNNGSSSSNSGNSGGSNGGSSGNS 273

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622849489 409 GVKGEKGETGQNAVSVRIVGSSNRGRAevyyGGTWGTICDDEWHNSDATVFCRMLGYSRGRALYKVGAGTGQ 480
Cdd:cd21118   274 GSGSGGSSSGGSNGWGGSSSSGGSGGS----GGGNKPECNNPGNDVRMAGGGGSQGSKESSGSHGSNGGNGQ 341
PHA03169 PHA03169
hypothetical protein; Provisional
 202-331 1.22e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 41.11  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622849489 202 GEAGLQGPQGAPGKQGATGTPGPQGEKGskGDGGLIGPKGETGTKGDKGDLGlPGSKGDKGMKGDAGVMGPPG-AQGSKG 280
Cdd:PHA03169   96 GSESVGSPTPSPSGSAEELASGLSPENT--SGSSPESPASHSPPPSPPSHPG-PHEPAPPESHNPSPNQQPSSfLQPSHE 172

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622849489 281 DSGRPGSPGLAGFPGAKGDPGQpGLQGVPGPPGAVGqPGAKGEPGSAGSRG 331
Cdd:PHA03169  173 DSPEEPEPPTSEPEPDSPGPPQ-SETPTSSPPPQSP-PDEPGEPQSPTPQQ 221
 
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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