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Conserved domains on  [gi|260166678|ref|NP_001018041|]
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otolin-1 precursor [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 343-474 1.10e-49

Complement component C1q domain; Globular domain found in many collagens and eponymously in complement C1q. When part of full length proteins these domains form a 'bouquet' due to the multimerization of heterotrimers. The C1q fold is similar to that of tumour necrosis factor.


:

Pssm-ID: 128420  Cd Length: 135  Bit Score: 166.32  E-value: 1.10e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166678   343 TQVPQSAFSALLSKPFPPPNVPIKFDKILSNDQGDYSPVTGKFNCSVPGTYIFSYHVTVRGRPARISLVaRNRKQFKS-R 421
Cdd:smart00110   3 KAQPRSAFSVIRSNRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLM-KNGIQVMStY 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 260166678   422 ETLYGQQVDQASLLLILKLSAGDQVWLEVSKDWNGLYVGPEDDSIFSGFLLYP 474
Cdd:smart00110  82 DEYQKGLYDVASGGALLQLRQGDQVWLELPDEKNGLYAGEYVDSTFSGFLLFP 134
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 118-368 3.66e-39

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: 147.36  E-value: 3.66e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166678 118 GQKGEPGKMGKQGPKGETGDTGSPGHPGTTGPQGPKGQKGEKGLKGDRGDQGAGGIPGYPGKPGEQGALGPKGDKGTIGP 197
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166678 198 AGTKGQKGSKGElcgNGTKGEKGDPGASGAHGFIGEPGAKGEKGgvgekgyRGDLGERGEKGQKGEKGMEGEKGSRGDVG 277
Cdd:NF038329 197 RGETGPAGEQGP---AGPAGPDGEAGPAGEDGPAGPAGDGQQGP-------DGDPGPTGEDGPQGPDGPAGKDGPRGDRG 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166678 278 SEGKRGSDGLPGLRGDSGPKGEKGEIGSPGFTGPAGPKGELGSKGVRGPTGKKGSRGVKGSKGEATQVPQSAfsallsKP 357
Cdd:NF038329 267 EAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG------KP 340

                        250
                 ....*....|..
gi 260166678 358 FPP-PNVPIKFD 368
Cdd:NF038329 341 APKtPEVPQKPD 352
 
Name Accession Description Interval E-value
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 343-474 1.10e-49

Complement component C1q domain; Globular domain found in many collagens and eponymously in complement C1q. When part of full length proteins these domains form a 'bouquet' due to the multimerization of heterotrimers. The C1q fold is similar to that of tumour necrosis factor.


Pssm-ID: 128420  Cd Length: 135  Bit Score: 166.32  E-value: 1.10e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166678   343 TQVPQSAFSALLSKPFPPPNVPIKFDKILSNDQGDYSPVTGKFNCSVPGTYIFSYHVTVRGRPARISLVaRNRKQFKS-R 421
Cdd:smart00110   3 KAQPRSAFSVIRSNRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLM-KNGIQVMStY 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 260166678   422 ETLYGQQVDQASLLLILKLSAGDQVWLEVSKDWNGLYVGPEDDSIFSGFLLYP 474
Cdd:smart00110  82 DEYQKGLYDVASGGALLQLRQGDQVWLELPDEKNGLYAGEYVDSTFSGFLLFP 134
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 118-368 3.66e-39

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: 147.36  E-value: 3.66e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166678 118 GQKGEPGKMGKQGPKGETGDTGSPGHPGTTGPQGPKGQKGEKGLKGDRGDQGAGGIPGYPGKPGEQGALGPKGDKGTIGP 197
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166678 198 AGTKGQKGSKGElcgNGTKGEKGDPGASGAHGFIGEPGAKGEKGgvgekgyRGDLGERGEKGQKGEKGMEGEKGSRGDVG 277
Cdd:NF038329 197 RGETGPAGEQGP---AGPAGPDGEAGPAGEDGPAGPAGDGQQGP-------DGDPGPTGEDGPQGPDGPAGKDGPRGDRG 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166678 278 SEGKRGSDGLPGLRGDSGPKGEKGEIGSPGFTGPAGPKGELGSKGVRGPTGKKGSRGVKGSKGEATQVPQSAfsallsKP 357
Cdd:NF038329 267 EAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG------KP 340

                        250
                 ....*....|..
gi 260166678 358 FPP-PNVPIKFD 368
Cdd:NF038329 341 APKtPEVPQKPD 352
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 349-472 1.67e-31

C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement system.


Pssm-ID: 395310 [Multi-domain]  Cd Length: 126  Bit Score: 117.39  E-value: 1.67e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166678  349 AFSALLSKPFPPPN-VPIKFDKILSNDQGDYSPVTGKFNCSVPGTYIFSYHVT-VRGRPARISLVARNRKQFKSRETLYG 426
Cdd:pfam00386   1 AFSAGRTTGLTAPNeQPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITtVDGKSLYVSLVKNGQEVVSFYDQPQK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 260166678  427 QQVDQASLLLILKLSAGDQVWLEVSKDwNGLYVGP-EDDSIFSGFLL 472
Cdd:pfam00386  81 GSLDVASGSVVLELQRGDEVWLQLTGY-NGLYYDGsDTDSTFSGFLL 126
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 117-315 4.85e-27

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: 113.08  E-value: 4.85e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166678 117 TGQKGEPGKMGKQGPKGETGDTGSPGHPGTTGPQGPKGQKGEKGLKGDRGDQGAGGIPGYPGKPGEQG--ALGPKGDKGT 194
Cdd:NF038329 161 KGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpaGDGQQGPDGD 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166678 195 IGPAGTKGQKGSKGELCGNGTKGEKGDPGASGAHGFIGEPGAkgekggvgekgyRGDLGERGEKGQKGEKGMEGEKGSRG 274
Cdd:NF038329 241 PGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGP------------VGPAGKDGQNGKDGLPGKDGKDGQNG 308

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 260166678 275 DVGSEGKRGSDGLPGLRGDSGPKGEKGEIGSPGFTGPAGPK 315
Cdd:NF038329 309 KDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQ 349
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 127-182 5.39e-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: 5.39e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 260166678  127 GKQGPKGETGDTGSPGHPGTTGPQGPKGQKGEKGLKGDRGDQGAGGIPGYPGKPGE 182
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 117-331 7.68e-06

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 48.84  E-value: 7.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166678   117 TGQKGEPGKMGkQGPKGETGDtGSPGHPGTTGPQGPKGQKGEKGLKGDRGDQGAGGIPGYPGKPGEQGALGPKGDKGTIG 196
Cdd:TIGR00927  645 TGEEGERPTEA-EGENGEESG-GEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEHEGETE 722

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166678   197 PAGT----KGQKGSKGELCGNGTKGEkgdpgASGAHGFIGEpGAKGEKGGVGEKGYRGDLGERGEKGQKGEKG-MEGEKG 271
Cdd:TIGR00927  723 AEGTedegEIETGEEGEEVEDEGEGE-----AEGKHEVETE-GDRKETEHEGETEAEGKEDEDEGEIQAGEDGeMKGDEG 796

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 260166678   272 SRGDVGSEGKRGSDGLPGLRGDSGP----KGEKGEIGSPGFTGPAGPKGELGSKGVRGPTGKKG 331
Cdd:TIGR00927  797 AEGKVEHEGETEAGEKDEHEGQSETqaddTEVKDETGEQELNAENQGEAKQDEKGVDGGGGSDG 860
PHA03169 PHA03169
hypothetical protein; Provisional
 127-351 7.33e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 44.96  E-value: 7.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166678 127 GKQGPKGETGDTGSPGHPGTTGPQ------------GPKGQKGEKGLKGDRGDQGAGGipgyPGKPGEQGALGPKGDKGT 194
Cdd:PHA03169  34 GRRRGTAARAAKPAPPAPTTSGPQvravaeqghrqtESDTETAEESRHGEKEERGQGG----PSGSGSESVGSPTPSPSG 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166678 195 IGPAGTKGQKGSKGELCGNGTKGEKGDPGASGAHGFIGEPgakgekggvgekgyrgdlGERGEKGQKGEKGMEGEKGSRG 274
Cdd:PHA03169 110 SAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEP------------------APPESHNPSPNQQPSSFLQPSH 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260166678 275 DVGSEGKRGSDGLPGLRGDSGPKGEKGEIGSPGFTGPAGPKGELGSKGVRGPTGKKGSRGVKGSKGEATQVPQSAFS 351
Cdd:PHA03169 172 EDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFP 248
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 118-350 6.58e-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: 42.29  E-value: 6.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166678 118 GQKGEPGKMGKQGPKGETGDTGSPGHPGTTGPQGPKGQKGEKG-LKGDRGDQGAGGIPGYPGKPG---EQGALGPKgdkg 193
Cdd:cd21118  131 GSQGGPGVQGHGIPGGTGGPWASGGNYGTNSLGGSVGQGGNGGpLNYGTNSQGAVAQPGYGTVRGnnqNSGCTNPP---- 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166678 194 tigPAGTKGQKGSKGELCGNGTKGEKGDPGASGAHGFIGEPGAKGEKGGVGEKGYRGDLGERGEKGQKGEKGMEGEKGSR 273
Cdd:cd21118  207 ---PSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGSGSGGSSSG 283

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260166678 274 GDVGSEGKRGSDGLPGLRGDSGPK--GEKGEIGSPGFTGPAGPKGELGSKGVRGPTGkkGSRGVKGSKGEATQVPQSAF 350
Cdd:cd21118  284 GSNGWGGSSSSGGSGGSGGGNKPEcnNPGNDVRMAGGGGSQGSKESSGSHGSNGGNG--QAEAVGGLNTLNSDASTLPF 360
 
Name Accession Description Interval E-value
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 343-474 1.10e-49

Complement component C1q domain; Globular domain found in many collagens and eponymously in complement C1q. When part of full length proteins these domains form a 'bouquet' due to the multimerization of heterotrimers. The C1q fold is similar to that of tumour necrosis factor.


Pssm-ID: 128420  Cd Length: 135  Bit Score: 166.32  E-value: 1.10e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166678   343 TQVPQSAFSALLSKPFPPPNVPIKFDKILSNDQGDYSPVTGKFNCSVPGTYIFSYHVTVRGRPARISLVaRNRKQFKS-R 421
Cdd:smart00110   3 KAQPRSAFSVIRSNRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLM-KNGIQVMStY 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 260166678   422 ETLYGQQVDQASLLLILKLSAGDQVWLEVSKDWNGLYVGPEDDSIFSGFLLYP 474
Cdd:smart00110  82 DEYQKGLYDVASGGALLQLRQGDQVWLELPDEKNGLYAGEYVDSTFSGFLLFP 134
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 118-368 3.66e-39

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: 147.36  E-value: 3.66e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166678 118 GQKGEPGKMGKQGPKGETGDTGSPGHPGTTGPQGPKGQKGEKGLKGDRGDQGAGGIPGYPGKPGEQGALGPKGDKGTIGP 197
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166678 198 AGTKGQKGSKGElcgNGTKGEKGDPGASGAHGFIGEPGAKGEKGgvgekgyRGDLGERGEKGQKGEKGMEGEKGSRGDVG 277
Cdd:NF038329 197 RGETGPAGEQGP---AGPAGPDGEAGPAGEDGPAGPAGDGQQGP-------DGDPGPTGEDGPQGPDGPAGKDGPRGDRG 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166678 278 SEGKRGSDGLPGLRGDSGPKGEKGEIGSPGFTGPAGPKGELGSKGVRGPTGKKGSRGVKGSKGEATQVPQSAfsallsKP 357
Cdd:NF038329 267 EAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG------KP 340

                        250
                 ....*....|..
gi 260166678 358 FPP-PNVPIKFD 368
Cdd:NF038329 341 APKtPEVPQKPD 352
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 349-472 1.67e-31

C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement system.


Pssm-ID: 395310 [Multi-domain]  Cd Length: 126  Bit Score: 117.39  E-value: 1.67e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166678  349 AFSALLSKPFPPPN-VPIKFDKILSNDQGDYSPVTGKFNCSVPGTYIFSYHVT-VRGRPARISLVARNRKQFKSRETLYG 426
Cdd:pfam00386   1 AFSAGRTTGLTAPNeQPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITtVDGKSLYVSLVKNGQEVVSFYDQPQK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 260166678  427 QQVDQASLLLILKLSAGDQVWLEVSKDwNGLYVGP-EDDSIFSGFLL 472
Cdd:pfam00386  81 GSLDVASGSVVLELQRGDEVWLQLTGY-NGLYYDGsDTDSTFSGFLL 126
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 117-315 4.85e-27

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: 113.08  E-value: 4.85e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166678 117 TGQKGEPGKMGKQGPKGETGDTGSPGHPGTTGPQGPKGQKGEKGLKGDRGDQGAGGIPGYPGKPGEQG--ALGPKGDKGT 194
Cdd:NF038329 161 KGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpaGDGQQGPDGD 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166678 195 IGPAGTKGQKGSKGELCGNGTKGEKGDPGASGAHGFIGEPGAkgekggvgekgyRGDLGERGEKGQKGEKGMEGEKGSRG 274
Cdd:NF038329 241 PGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGP------------VGPAGKDGQNGKDGLPGKDGKDGQNG 308

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 260166678 275 DVGSEGKRGSDGLPGLRGDSGPKGEKGEIGSPGFTGPAGPK 315
Cdd:NF038329 309 KDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQ 349
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 127-182 5.39e-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: 5.39e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 260166678  127 GKQGPKGETGDTGSPGHPGTTGPQGPKGQKGEKGLKGDRGDQGAGGIPGYPGKPGE 182
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 139-193 1.89e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.87  E-value: 1.89e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 260166678  139 GSPGHPGTTGPQGPKGQKGEKGLKGDRGDQGAGGIPGYPGKPGEQGALGPKGDKG 193
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 136-190 2.66e-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: 47.49  E-value: 2.66e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 260166678  136 GDTGSPGHPGTTGPQGPKGQKGEKGLKGDRGDQGAGGIPGYPGKPGEQGALGPKG 190
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 148-203 3.40e-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: 47.10  E-value: 3.40e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 260166678  148 GPQGPKGQKGEKGLKGDRGDQGAGGIPGYPGKPGEQGALGPKGDKGTIGPAGTKGQ 203
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 268-322 4.43e-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: 4.43e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 260166678  268 GEKGSRGDVGSEGKRGSDGLPGLRGDSGPKGEKGEIGSPGFTGPAGPKGELGSKG 322
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 286-342 5.56e-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: 5.56e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 260166678  286 GLPGLRGDSGPKGEKGEIGSPGFTGPAGPKGELGSKGVRGPTGKKGSRGVKGSKGEA 342
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 262-317 6.96e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.95  E-value: 6.96e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 260166678  262 GEKGMEGEKGSRGDVGSEGKRGSDGLPGLRGDSGPKGEKGEIGSPGFTGPAGPKGE 317
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 142-198 7.53e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.95  E-value: 7.53e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 260166678  142 GHPGTTGPQGPKGQKGEKGLKGDRGDQGAGGIPGYPGKPGEQGALGPKGDKGTIGPA 198
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 130-185 9.25e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.95  E-value: 9.25e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 260166678  130 GPKGETGDTGSPGHPGTTGPQGPKGQKGEKGLKGDRGDQGAGGIPGYPGKPGEQGA 185
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 283-337 1.75e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.18  E-value: 1.75e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 260166678  283 GSDGLPGLRGDSGPKGEKGEIGSPGFTGPAGPKGELGSKGVRGPTGKKGSRGVKG 337
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 121-177 1.93e-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: 1.93e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 260166678  121 GEPGKMGKQGPKGETGDTGSPGHPGTTGPQGPKGQKGEKGLKGDRGDQGAGGIPGYP 177
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 124-180 2.05e-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: 2.05e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 260166678  124 GKMGKQGPKGETGDTGSPGHPGTTGPQGPKGQKGEKGLKGDRGDQGAGGIPGYPGKP 180
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 280-334 2.35e-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: 2.35e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 260166678  280 GKRGSDGLPGLRGDSGPKGEKGEIGSPGFTGPAGPKGELGSKGVRGPTGKKGSRG 334
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 253-307 3.12e-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: 3.12e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 260166678  253 GERGEKGQKGEKGMEGEKGSRGDVGSEGKRGSDGLPGLRGDSGPKGEKGEIGSPG 307
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 118-170 4.11e-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: 4.11e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 260166678  118 GQKGEPGKMGKQGPKGETGDTGSPGHPGTTGPQGPKGQKGEKGLKGDRGDQGA 170
Cdd:pfam01391   4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 145-199 6.21e-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: 6.21e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 260166678  145 GTTGPQGPKGQKGEKGLKGDRGDQGAGGIPGYPGKPGEQGALGPKGDKGTIGPAG 199
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 117-331 7.68e-06

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 48.84  E-value: 7.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166678   117 TGQKGEPGKMGkQGPKGETGDtGSPGHPGTTGPQGPKGQKGEKGLKGDRGDQGAGGIPGYPGKPGEQGALGPKGDKGTIG 196
Cdd:TIGR00927  645 TGEEGERPTEA-EGENGEESG-GEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEHEGETE 722

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166678   197 PAGT----KGQKGSKGELCGNGTKGEkgdpgASGAHGFIGEpGAKGEKGGVGEKGYRGDLGERGEKGQKGEKG-MEGEKG 271
Cdd:TIGR00927  723 AEGTedegEIETGEEGEEVEDEGEGE-----AEGKHEVETE-GDRKETEHEGETEAEGKEDEDEGEIQAGEDGeMKGDEG 796

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 260166678   272 SRGDVGSEGKRGSDGLPGLRGDSGP----KGEKGEIGSPGFTGPAGPKGELGSKGVRGPTGKKG 331
Cdd:TIGR00927  797 AEGKVEHEGETEAGEKDEHEGQSETqaddTEVKDETGEQELNAENQGEAKQDEKGVDGGGGSDG 860
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 277-333 2.10e-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: 2.10e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 260166678  277 GSEGKRGSDGLPGLRGDSGPKGEKGEIGSPGFTGPAGPKGELGSKGVRGPTGKKGSR 333
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 117-160 3.30e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.33  E-value: 3.30e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 260166678  117 TGQKGEPGKMGKQGPKGETGDTGSPGHPGTTGPQGPKGQKGEKG 160
Cdd:pfam01391  12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 151-205 4.79e-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: 4.79e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 260166678  151 GPKGQKGEKGLKGDRGDQGAGGIPGYPGKPGEQGALGPKGDKGTIGPAGTKGQKG 205
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 166-227 4.88e-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: 4.88e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260166678  166 GDQGAGGIPGYPGKPGEQGALGPKGDKGTIGPAGTKGQKGSkgelcgNGTKGEKGDPGASGA 227
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGP------PGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 117-165 5.83e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 5.83e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 260166678  117 TGQKGEPGKMGKQGPKGETGDTGSPGHPGTTGPQGPKGQKGEKGLKGDR 165
Cdd:pfam01391   9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 249-299 6.06e-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: 40.55  E-value: 6.06e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 260166678  249 RGDLGERGEKGQKGEKGMEGEKGSRGDVGSEGKRGSDGLPGLRGDSGPKGE 299
Cdd:pfam01391   6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PHA03169 PHA03169
hypothetical protein; Provisional
 127-351 7.33e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 44.96  E-value: 7.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166678 127 GKQGPKGETGDTGSPGHPGTTGPQ------------GPKGQKGEKGLKGDRGDQGAGGipgyPGKPGEQGALGPKGDKGT 194
Cdd:PHA03169  34 GRRRGTAARAAKPAPPAPTTSGPQvravaeqghrqtESDTETAEESRHGEKEERGQGG----PSGSGSESVGSPTPSPSG 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166678 195 IGPAGTKGQKGSKGELCGNGTKGEKGDPGASGAHGFIGEPgakgekggvgekgyrgdlGERGEKGQKGEKGMEGEKGSRG 274
Cdd:PHA03169 110 SAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEP------------------APPESHNPSPNQQPSSFLQPSH 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260166678 275 DVGSEGKRGSDGLPGLRGDSGPKGEKGEIGSPGFTGPAGPKGELGSKGVRGPTGKKGSRGVKGSKGEATQVPQSAFS 351
Cdd:PHA03169 172 EDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFP 248
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 118-350 6.58e-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: 42.29  E-value: 6.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166678 118 GQKGEPGKMGKQGPKGETGDTGSPGHPGTTGPQGPKGQKGEKG-LKGDRGDQGAGGIPGYPGKPG---EQGALGPKgdkg 193
Cdd:cd21118  131 GSQGGPGVQGHGIPGGTGGPWASGGNYGTNSLGGSVGQGGNGGpLNYGTNSQGAVAQPGYGTVRGnnqNSGCTNPP---- 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166678 194 tigPAGTKGQKGSKGELCGNGTKGEKGDPGASGAHGFIGEPGAKGEKGGVGEKGYRGDLGERGEKGQKGEKGMEGEKGSR 273
Cdd:cd21118  207 ---PSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGSGSGGSSSG 283

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260166678 274 GDVGSEGKRGSDGLPGLRGDSGPK--GEKGEIGSPGFTGPAGPKGELGSKGVRGPTGkkGSRGVKGSKGEATQVPQSAF 350
Cdd:cd21118  284 GSNGWGGSSSSGGSGGSGGGNKPEcnNPGNDVRMAGGGGSQGSKESSGSHGSNGGNG--QAEAVGGLNTLNSDASTLPF 360
PHA03169 PHA03169
hypothetical protein; Provisional
 119-291 8.18e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 41.88  E-value: 8.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166678 119 QKGEPGKMGKQGPKGETGDTGSPGHPGTTGPQGPKGQKGEKGLKGDRGDQGAGGIPGYPGKPGEQGAlGPKGDKGTIGPA 198
Cdd:PHA03169  80 RHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGP-HEPAPPESHNPS 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166678 199 GTKGQKGSKGELCGNGTkgEKGDPGASGAHGFIGEPGAKGEKGGVGEKGYRGDLG--ERGEKGQKGEKGMEGEKGSRGDV 276
Cdd:PHA03169 159 PNQQPSSFLQPSHEDSP--EEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPgePQSPTPQQAPSPNTQQAVEHEDE 236

                        170
                 ....*....|....*
gi 260166678 277 GSEGKRGSDGLPGLR 291
Cdd:PHA03169 237 PTEPEREGPPFPGHR 251
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 187-236 5.40e-03

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: 35.16  E-value: 5.40e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 260166678  187 GPKGDKGTIGPAGTKGQKGSKGELCGNGTKGEKGDPGASGAHGFIGEPGA 236
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
 
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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