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Conserved domains on  [gi|17506747|ref|NP_492013|]
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Nematode cuticle collagen N-terminal domain-containing protein [Caenorhabditis elegans]

Protein Classification

cuticular collagen family protein( domain architecture ID 18387949)

cuticular collagen family protein is a structural macromolecule of the extracellular matrix containing triple helix domains that form tight interactions and stabilize supramolecular aggregates

Gene Ontology:  GO:0042302|GO:0005581
PubMed:  1916105|21421911

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 113-270 4.23e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 101.14  E-value: 4.23e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747  113 GQAGQDGQDGNTPSEEYGNSQDGSTSTCPAGPPGEQGPDGAPGEAGRD------GQPGSDGQSGNEGPTGPRGSPGNKGR 186
Cdd:NF038329 135 GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAgakgpaGEKGPQGPRGETGPAGEQGPAGPAGP 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747  187 DGNPGRDGSPGRPGRDGTRGVGQPGSPGQPGSRGPEGPRGQPGNMGRPGEYGDAGPAGQPGNDGEQGPDGVVGIPGE--- 263
Cdd:NF038329 215 DGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQngk 294


                 ....*..
gi 17506747  264 PGLPGSD 270
Cdd:NF038329 295 DGLPGKD 301
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 6-58 6.48e-14

Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is found in the N-terminal region of nematode cuticle collagens. Cuticle is a tough elastic structure secreted by hypodermal cells and is primarily composed of collagen proteins.


:

Pssm-ID: 198156  Cd Length: 53  Bit Score: 64.80  E-value: 6.48e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17506747      6 TILYGCTVFSSVAILAALLFTTFMYNDLYDFHSEVEEELYGFKDIYNDAWFLM 58
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 113-270 4.23e-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: 101.14  E-value: 4.23e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747  113 GQAGQDGQDGNTPSEEYGNSQDGSTSTCPAGPPGEQGPDGAPGEAGRD------GQPGSDGQSGNEGPTGPRGSPGNKGR 186
Cdd:NF038329 135 GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAgakgpaGEKGPQGPRGETGPAGEQGPAGPAGP 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747  187 DGNPGRDGSPGRPGRDGTRGVGQPGSPGQPGSRGPEGPRGQPGNMGRPGEYGDAGPAGQPGNDGEQGPDGVVGIPGE--- 263
Cdd:NF038329 215 DGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQngk 294


                 ....*..
gi 17506747  264 PGLPGSD 270
Cdd:NF038329 295 DGLPGKD 301
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 89-281 6.39e-19

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: 86.50  E-value: 6.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747   89 GAKASNCPRGPPGPPGEPGENGTDGQAGQDGQDG-NTPSEEYGNSQDGSTS-TCPAGPPGEQGPDGAPGEAGRDGQPGSD 166
Cdd:NF038329 189 GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGeDGPAGPAGDGQQGPDGdPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747  167 GQSGNEGPTGPRGSPGNKGRDGNPGRDGSPGRPGRDGTRgvGQPGSPGQPGSRGPEGPRGQPGNMGRPGEYGDAGPAGQp 246
Cdd:NF038329 269 GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQN--GKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP- 345

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 17506747  247 gnDGEQGPDGVVGIPGEPGLPGsdasycQCPDRTP 281
Cdd:NF038329 346 --EVPQKPDTAPHTPKTPQIPG------QSKDVTP 372
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 166-281 1.25e-16

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: 79.56  E-value: 1.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747  166 DGQSGNEGPTGPRGSPGNKGRDGNPGRDGSPGRPGRDGTRGV----------GQPGSPGQPGSRGPEGPRGQPGNMGRPG 235
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGErgekgpagpqGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 17506747  236 EYGDAGPAGQPGNDGEQGPDGVVGIPGEPGLPGSDASYCQCPDRTP 281
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDP 241
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 6-58 6.48e-14

Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is found in the N-terminal region of nematode cuticle collagens. Cuticle is a tough elastic structure secreted by hypodermal cells and is primarily composed of collagen proteins.


Pssm-ID: 198156  Cd Length: 53  Bit Score: 64.80  E-value: 6.48e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17506747      6 TILYGCTVFSSVAILAALLFTTFMYNDLYDFHSEVEEELYGFKDIYNDAWFLM 58
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 9-58 1.55e-12

Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is found in the N-terminal region of nematode cuticle collagens, see pfam01391. Cuticle is a tough elastic structure secreted by hypodermal cells and is primarily composed of collagen proteins.


Pssm-ID: 460226  Cd Length: 50  Bit Score: 60.94  E-value: 1.55e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 17506747     9 YGCTVFSSVAILAALLFTTFMYNDLYDFHSEVEEELYGFKDIYNDAWFLM 58
Cdd:pfam01484   1 YVAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 193-289 3.48e-08

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: 54.14  E-value: 3.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747  193 DGSPGRPGRDGTRGvgQPGSPGQPGSRGPEGPRGQPGNMGRPGEYGDAGPAGQPGNDGEQGPDGVVGIPGEPGLPGSDAS 272
Cdd:NF038329 116 DGEKGEPGPAGPAG--PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193

                         90
                 ....*....|....*..
gi 17506747  273 YCQCPDRTPTVEKTSAG 289
Cdd:NF038329 194 QGPRGETGPAGEQGPAG 210
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 146-200 4.94e-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: 48.64  E-value: 4.94e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 17506747   146 GEQGPDGAPGEAGRDGQPGSDGQSGNEGPTGPRGSPGNKGRDGNPGRDGSPGRPG 200
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PHA03169 PHA03169
hypothetical protein; Provisional
 112-229 4.25e-06

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 47.66  E-value: 4.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747  112 DGQAGQDGQDGNTPSEEYGNSQDGSTSTCPAGP------PGEQGPDGAPGEAGRDGQPGSDGQSGNEGPTGPRGSPGNKG 185
Cdd:PHA03169 107 PSGSAEELASGLSPENTSGSSPESPASHSPPPSppshpgPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPE 186

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 17506747  186 RDGNPGRDGSPGRPGRDGTRGVGQPGSPGQPGSRGPEGPRGQPG 229
Cdd:PHA03169 187 PDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQA 230
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
112-268 1.58e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 43.09  E-value: 1.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747 112 DGQAGQDGQDGNTPSEEYGNSQDGSTSTCPAGPPGEQGPDGAPGEAGRDGQPGSDGQSGNEGPTGPRGSPGNKGRDGNPG 191
Cdd:COG5164   9 TGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQG 88

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17506747 192 RDGSPGRPGRDGTRGVGQPGSPGQPGSRGPEGPRGQPGNMGRPGEYGDAGPAGQ-PGNDGEQGPDGVVGIPGEPGLPG 268
Cdd:COG5164  89 GTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGStPPGPGSTGPGGSTTPPGDGGSTT 166
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 130-272 1.13e-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: 40.37  E-value: 1.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747 130 GNSQDGSTSTCPAGPPGEQGPDGAPGEAGRDGQPGS-DGQSGNEGptgpRGSPGNKGRDGNPGRDGSPGRPGRDGtrgvG 208
Cdd:cd21118 219 GSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSsSSNSGNSG----GSNGGSSGNSGSGSGGSSSGGSNGWG----G 290

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17506747 209 QPGSPGQPGSRGPEGPR-GQPGNMGR-PGEYGDAGPAGQPGNDGEQGPDGVVGIPGEPGLPGSDAS 272
Cdd:cd21118 291 SSSSGGSGGSGGGNKPEcNNPGNDVRmAGGGGSQGSKESSGSHGSNGGNGQAEAVGGLNTLNSDAS 356
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 113-270 4.23e-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: 101.14  E-value: 4.23e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747  113 GQAGQDGQDGNTPSEEYGNSQDGSTSTCPAGPPGEQGPDGAPGEAGRD------GQPGSDGQSGNEGPTGPRGSPGNKGR 186
Cdd:NF038329 135 GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAgakgpaGEKGPQGPRGETGPAGEQGPAGPAGP 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747  187 DGNPGRDGSPGRPGRDGTRGVGQPGSPGQPGSRGPEGPRGQPGNMGRPGEYGDAGPAGQPGNDGEQGPDGVVGIPGE--- 263
Cdd:NF038329 215 DGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQngk 294


                 ....*..
gi 17506747  264 PGLPGSD 270
Cdd:NF038329 295 DGLPGKD 301
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 89-281 6.39e-19

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: 86.50  E-value: 6.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747   89 GAKASNCPRGPPGPPGEPGENGTDGQAGQDGQDG-NTPSEEYGNSQDGSTS-TCPAGPPGEQGPDGAPGEAGRDGQPGSD 166
Cdd:NF038329 189 GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGeDGPAGPAGDGQQGPDGdPGPTGEDGPQGPDGPAGKDGPRGDRGEA 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747  167 GQSGNEGPTGPRGSPGNKGRDGNPGRDGSPGRPGRDGTRgvGQPGSPGQPGSRGPEGPRGQPGNMGRPGEYGDAGPAGQp 246
Cdd:NF038329 269 GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQN--GKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP- 345

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 17506747  247 gnDGEQGPDGVVGIPGEPGLPGsdasycQCPDRTP 281
Cdd:NF038329 346 --EVPQKPDTAPHTPKTPQIPG------QSKDVTP 372
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 166-281 1.25e-16

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: 79.56  E-value: 1.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747  166 DGQSGNEGPTGPRGSPGNKGRDGNPGRDGSPGRPGRDGTRGV----------GQPGSPGQPGSRGPEGPRGQPGNMGRPG 235
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGErgekgpagpqGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 17506747  236 EYGDAGPAGQPGNDGEQGPDGVVGIPGEPGLPGSDASYCQCPDRTP 281
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDP 241
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 6-58 6.48e-14

Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is found in the N-terminal region of nematode cuticle collagens. Cuticle is a tough elastic structure secreted by hypodermal cells and is primarily composed of collagen proteins.


Pssm-ID: 198156  Cd Length: 53  Bit Score: 64.80  E-value: 6.48e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17506747      6 TILYGCTVFSSVAILAALLFTTFMYNDLYDFHSEVEEELYGFKDIYNDAWFLM 58
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 9-58 1.55e-12

Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is found in the N-terminal region of nematode cuticle collagens, see pfam01391. Cuticle is a tough elastic structure secreted by hypodermal cells and is primarily composed of collagen proteins.


Pssm-ID: 460226  Cd Length: 50  Bit Score: 60.94  E-value: 1.55e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 17506747     9 YGCTVFSSVAILAALLFTTFMYNDLYDFHSEVEEELYGFKDIYNDAWFLM 58
Cdd:pfam01484   1 YVAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 193-289 3.48e-08

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: 54.14  E-value: 3.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747  193 DGSPGRPGRDGTRGvgQPGSPGQPGSRGPEGPRGQPGNMGRPGEYGDAGPAGQPGNDGEQGPDGVVGIPGEPGLPGSDAS 272
Cdd:NF038329 116 DGEKGEPGPAGPAG--PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193

                         90
                 ....*....|....*..
gi 17506747  273 YCQCPDRTPTVEKTSAG 289
Cdd:NF038329 194 QGPRGETGPAGEQGPAG 210
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 146-200 4.94e-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: 48.64  E-value: 4.94e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 17506747   146 GEQGPDGAPGEAGRDGQPGSDGQSGNEGPTGPRGSPGNKGRDGNPGRDGSPGRPG 200
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 141-196 8.67e-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: 48.26  E-value: 8.67e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 17506747   141 PAGPPGEQGPDGAPGEAGRDGQPGSDGQSGNEGPTGPRGSPGNKGRDGNPGRDGSP 196
Cdd:pfam01391   2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 211-267 1.22e-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: 1.22e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17506747   211 GSPGQPGSRGPEGPRGQPGNMGRPGEYGDAGPAGQPGNDGEQGPDGVVGIPGEPGLP 267
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 208-264 2.10e-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: 2.10e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17506747   208 GQPGSPGQPGSRGPEGPRGQPGNMGRPGEYGDAGPAGQPGNDGEQGPDGVVGIPGEP 264
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 217-269 1.99e-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: 44.41  E-value: 1.99e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 17506747   217 GSRGPEGPRGQPGNMGRPGEYGDAGPAGQPGNDGEQGPDGVVGIPGEPGLPGS 269
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
PHA03169 PHA03169
hypothetical protein; Provisional
 112-229 4.25e-06

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 47.66  E-value: 4.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747  112 DGQAGQDGQDGNTPSEEYGNSQDGSTSTCPAGP------PGEQGPDGAPGEAGRDGQPGSDGQSGNEGPTGPRGSPGNKG 185
Cdd:PHA03169 107 PSGSAEELASGLSPENTSGSSPESPASHSPPPSppshpgPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPE 186

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 17506747  186 RDGNPGRDGSPGRPGRDGTRGVGQPGSPGQPGSRGPEGPRGQPG 229
Cdd:PHA03169 187 PDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQA 230
PHA03169 PHA03169
hypothetical protein; Provisional
 147-270 8.86e-06

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 46.89  E-value: 8.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747  147 EQGPDGAPGEAGRDGQPGSDGQSGNEGPTGPRGSPGNKGRDGNPGRDGSPGRPGRDGtrGVGQPGSPGQPGSRGPEGPRG 226
Cdd:PHA03169  85 EERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPP--SHPGPHEPAPPESHNPSPNQQ 162

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 17506747  227 QPGNMGRPGEYGDA---GPAGQPGNDGEQGPDGVVGIPGEPGLPGSD 270
Cdd:PHA03169 163 PSSFLQPSHEDSPEepePPTSEPEPDSPGPPQSETPTSSPPPQSPPD 209
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 115-290 1.03e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.90  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747  115 AGQDGQDGNTPSEEYGNSQDGSTSTCPAGPPGEQGPDGAPGEAGrdgQPGSDGQSGNEGPTGPRGSPGNKGRDGNPGRDG 194
Cdd:PRK07764 589 GPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGA---AAAPAEASAAPAPGVAAPEHHPKHVAVPDASDG 665

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747  195 SPGRPGRDGTRG----VGQPGSPGQPGSRGPEGPRGQPGNMGRPGEYGDAGPAGQPGNDGE------QGPDGVVGIPGEP 264
Cdd:PRK07764 666 GDGWPAKAGGAApaapPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQgasapsPAADDPVPLPPEP 745

                        170       180
                 ....*....|....*....|....*..
gi 17506747  265 GL-PGSDASYCQCPDRTPTVEKTSAGG 290
Cdd:PRK07764 746 DDpPDPAGAPAQPPPPPAPAPAAAPAA 772
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 161-216 1.10e-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: 1.10e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17506747   161 GQPGSDGQSGNEGPTGPRGSPGNKGRDGNPGRDGSPGRPGRDGTRG-VGQPGSPGQP 216
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGpPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 220-270 2.28e-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: 2.28e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 17506747   220 GPEGPRGQPGNMGRPGEYGDAGPAGQPGNDGEQGPDGVVGIPGEPGLPGSD 270
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 112-239 4.96e-05

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 44.51  E-value: 4.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747  112 DGQAGQDGQDGNTPSEEygnSQDGSTSTCPAGPPGEQGPDGAPGEAGRDGQPGSDGQSGNEGPTGPRGSPGNKGRDGNP- 190
Cdd:PRK12678 139 RGAARKAGEGGEQPATE---ARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRr 215

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 17506747  191 GRDGSPGRPGRDGTRGVGQPGSPGQPGSRGPEGPRGQPGNMGRPGEYGD 239
Cdd:PRK12678 216 EERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGR 264
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 113-255 8.92e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.82  E-value: 8.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747  113 GQAGQDGQDGNTPSEEYGNSQDGS------TSTCPAGPPGEQGPDGAPGEAGRDGQPGSDGQSGNEGPTGPRGSPGNKGR 186
Cdd:PRK07764 623 APAAPAPAGAAAAPAEASAAPAPGvaapehHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPA 702

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747  187 DGNPGRDGSPGRPGRDGT-RGVGQPGSPGQPGSRGPEGPRGQPGNMGRPGEYGDAGPAGQPGNDGEQGPD 255
Cdd:PRK07764 703 PAPAATPPAGQADDPAAQpPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAA 772
PHA03169 PHA03169
hypothetical protein; Provisional
 112-253 1.24e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 43.04  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747  112 DGQAGQDGQDGNTPSEEYGNSQDGSTSTCPAgppGEQGPDGAPGEAGRDGQPGSDGQSGNEGPTGPRGSPGNKGRDGNPG 191
Cdd:PHA03169  92 PSGSGSESVGSPTPSPSGSAEELASGLSPEN---TSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQ 168

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17506747  192 RDGSPGRPGRDGTRGVGQPGSPGQPGSRGPE--GPRGQPGNmgRPGEYGDAGPAGQPGNDGEQG 253
Cdd:PHA03169 169 PSHEDSPEEPEPPTSEPEPDSPGPPQSETPTssPPPQSPPD--EPGEPQSPTPQQAPSPNTQQA 230
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 96-253 1.44e-04

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 43.35  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747   96 PRGPPGPPGEPGENGTDGQAGQDGQDGNTPSEEYGNSQDGSTSTCPAGPP-------GEQGPDGAPGEAGRDGQPGSDGQ 168
Cdd:PRK12678  77 ARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQarerrerGEAARRGAARKAGEGGEQPATEA 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747  169 SGNEGPTGPRGSPGNKGRDGNPGRDGSPGRPGRDGTRG-VGQPGSPGQPGSRGPEGPR----GQPGNMGRPGEYGDAGPA 243
Cdd:PRK12678 157 RADAAERTEEEERDERRRRGDREDRQAEAERGERGRREeRGRDGDDRDRRDRREQGDRreerGRRDGGDRRGRRRRRDRR 236

                        170
                 ....*....|
gi 17506747  244 GQPGNDGEQG 253
Cdd:PRK12678 237 DARGDDNRED 246
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
112-268 1.58e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 43.09  E-value: 1.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747 112 DGQAGQDGQDGNTPSEEYGNSQDGSTSTCPAGPPGEQGPDGAPGEAGRDGQPGSDGQSGNEGPTGPRGSPGNKGRDGNPG 191
Cdd:COG5164   9 TGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQG 88

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17506747 192 RDGSPGRPGRDGTRGVGQPGSPGQPGSRGPEGPRGQPGNMGRPGEYGDAGPAGQ-PGNDGEQGPDGVVGIPGEPGLPG 268
Cdd:COG5164  89 GTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGStPPGPGSTGPGGSTTPPGDGGSTT 166
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 104-272 3.48e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 3.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747  104 GEPGENGTDGQAGQDGQDGNTPSEEYGNSQDGSTSTCPAGPPGEQGPDGAPGEAGRDGQPGSDGQSGneGPTGPRGSPGN 183
Cdd:PRK07764 638 EASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPA--PAATPPAGQAD 715

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747  184 KGRDGNPGRDGSPGRPGRDGTRGVGQPGSPGQPGSRGPEGPRGQPGNMGRPGEYGDAGPAGQPGNDGEQGPDGVVGIPGE 263
Cdd:PRK07764 716 DPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDD 795


                 ....*....
gi 17506747  264 PGLPGSDAS 272
Cdd:PRK07764 796 EDRRDAEEV 804
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 134-232 8.30e-04

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 40.76  E-value: 8.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747  134 DGSTSTCPAGPPGEQGPDGAPGEagrdgqPGSDGQSGNEGPTGPRGSPGNKGRDGNPgrDGSPGRPGRDGTRGVGQPGSP 213
Cdd:PHA03264 271 SGGSPAPPGDDRPEAKPEPGPVE------DGAPGRETGGEGEGPEPAGRDGAAGGEP--KPGPPRPAPDADRPEGWPSLE 342

                         90       100
                 ....*....|....*....|...
gi 17506747  214 GQ----PGSRGPEGPRGQPGNMG 232
Cdd:PHA03264 343 AItfppPTPATPAVPRARPVIVG 365
DUF4175 pfam13779
Domain of unknown function (DUF4175);
186-233 8.55e-04

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 40.74  E-value: 8.55e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 17506747   186 RDGNPGRDGSPGRPGRDGTRGVGQPGSPGQPGSRGPEGPRGQPGNMGR 233
Cdd:pfam13779 628 RQLQQQGGQQQGQPGQQGQQGQGQQPGQGGQQPGAQMPPQGGAEALGD 675
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 130-272 1.13e-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: 40.37  E-value: 1.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747 130 GNSQDGSTSTCPAGPPGEQGPDGAPGEAGRDGQPGS-DGQSGNEGptgpRGSPGNKGRDGNPGRDGSPGRPGRDGtrgvG 208
Cdd:cd21118 219 GSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSsSSNSGNSG----GSNGGSSGNSGSGSGGSSSGGSNGWG----G 290

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17506747 209 QPGSPGQPGSRGPEGPR-GQPGNMGR-PGEYGDAGPAGQPGNDGEQGPDGVVGIPGEPGLPGSDAS 272
Cdd:cd21118 291 SSSSGGSGGSGGGNKPEcNNPGNDVRmAGGGGSQGSKESSGSHGSNGGNGQAEAVGGLNTLNSDAS 356
PHA03169 PHA03169
hypothetical protein; Provisional
 112-225 1.85e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 39.57  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747  112 DGQAGQDGQDGNTPSEEYGNSQDGSTSTCPAGPPGEQGPDGAPGEAGRDGQPGSDGQSGNEGPTGPRGsPGNKGRDGNPG 191
Cdd:PHA03169 140 PPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSP-PDEPGEPQSPT 218

                         90       100       110
                 ....*....|....*....|....*....|....
gi 17506747  192 RDGSPGRPGRDGTRGVGQPGSPGQPGSrGPEGPR 225
Cdd:PHA03169 219 PQQAPSPNTQQAVEHEDEPTEPEREGP-PFPGHR 251
PHA03378 PHA03378
EBNA-3B; Provisional
 141-254 2.41e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.67  E-value: 2.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747  141 PAGPPGE-QGPDGAPGEAGRDGQPGSDGQSGNEGPTGPRGSPGNKGRDGNPGRDGSPGRPGRdGTRGVGQPGSPGQPGSR 219
Cdd:PHA03378 707 PAAPPGRaQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPA-AAPGAPTPQPPPQAPPA 785

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 17506747  220 GPEGPRGQPGNMGRPgeygDAGPAGQ----PGNDGEQGP 254
Cdd:PHA03378 786 PQQRPRGAPTPQPPP----QAGPTSMqlmpRAAPGQQGP 820
dnaA PRK14086
chromosomal replication initiator protein DnaA;
122-219 2.76e-03

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 39.04  E-value: 2.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747  122 GNTPSEEYGNSQDGSTSTCP-AGPPGEQGPDGAPGEAGRDG------QPGSDGQSGNEGPTG----PRGSPGNKGRDGNP 190
Cdd:PRK14086 173 GFPPRAPYASPASYAPEQERdREPYDAGRPEYDQRRRDYDHprpdwdRPRRDRTDRPEPPPGaghvHRGGPGPPERDDAP 252

                         90       100
                 ....*....|....*....|....*....
gi 17506747  191 GRDGSPGRPGRDGTRGVGQPGsPGQPGSR 219
Cdd:PRK14086 253 VVPIRPSAPGPLAAQPAPAPG-PGEPTAR 280
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 173-271 2.95e-03

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 38.83  E-value: 2.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747  173 GPTGPRGSPGNKGRDGNPGRD-GSPGRPGRDGTRGVGQPG-----SPGQPGSRGPEGPRGQPGNMGRPGEYGDAGPAGQP 246
Cdd:PHA03264 251 GGVVPPYFEESKGYEPPPAPSgGSPAPPGDDRPEAKPEPGpvedgAPGRETGGEGEGPEPAGRDGAAGGEPKPGPPRPAP 330

                         90       100
                 ....*....|....*....|....*
gi 17506747  247 GNDGEQGPDGVVGIPGEPGLPGSDA 271
Cdd:PHA03264 331 DADRPEGWPSLEAITFPPPTPATPA 355
PTZ00146 PTZ00146
fibrillarin; Provisional
 191-244 4.49e-03

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 38.18  E-value: 4.49e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 17506747  191 GRDGSPGRPGRDGTRGVGQPGSPGQPGSRGPEGPRGQPGNMGRPGEYGDAGPAG 244
Cdd:PTZ00146   3 GGGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGGGGPGK 56
PTZ00146 PTZ00146
fibrillarin; Provisional
 183-235 5.93e-03

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 37.79  E-value: 5.93e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 17506747  183 NKGRDGNPGRDGSPGRPGRDGTRGVGQPGSPGQPGSRGPEGPRGQPGNMGRPG 235
Cdd:PTZ00146   1 GMGGGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGGGG 53
PHA03169 PHA03169
hypothetical protein; Provisional
 179-290 9.46e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 37.26  E-value: 9.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506747  179 GSPGNKGRDGNPGRDGSPGRPGRDGTRGvgqpGSPGQPGSRGPEGPRGQPGNMGRPGEYGDAGPA--GQPGNDGEQGPDG 256
Cdd:PHA03169  90 GGPSGSGSESVGSPTPSPSGSAEELASG----LSPENTSGSSPESPASHSPPPSPPSHPGPHEPAppESHNPSPNQQPSS 165

                         90       100       110
                 ....*....|....*....|....*....|....
gi 17506747  257 VVGIPGEPGLPGSDASYCQCPDRTPTVEKTSAGG 290
Cdd:PHA03169 166 FLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPT 199
PTZ00146 PTZ00146
fibrillarin; Provisional
 164-215 9.80e-03

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 37.02  E-value: 9.80e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17506747  164 GSDGQSGNEGPTGPRGSPGNKGRDGNPGRDGSPGRPGRDGTRGVGQPGSPGQ 215
Cdd:PTZ00146   5 GFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGGGGPGK 56
 
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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