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Conserved domains on  [gi|17569903|ref|NP_508386|]
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Nematode cuticle collagen N-terminal domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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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 ...
 105-281 1.29e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 113.08  E-value: 1.29e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  105 PAGPKGESGSAGEPGTDGTDGTPGKDGADGSneqtASQAGDLCTACPAGPPGVAGYKGKRGPRGEKGDKGAPGNAGRDGA 184
Cdd:NF038329 124 PAGPAGPAGEQGPRGDRGETGPAGPAGPPGP----QGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  185 PGDDGPEGDHGHPGPMGPAGEKGTSGADGKGfAKGAPGPKGPTGMDGLAGDEGLPGERGEDGSAGAQGETGPQGPQGEKG 264
Cdd:NF038329 200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPA-GDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG 278

                        170
                 ....*....|....*..
gi 17569903  265 PDGFPGLPGSAGASGED 281
Cdd:NF038329 279 ERGPVGPAGKDGQNGKD 295
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 13-63 7.13e-07

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: 45.92  E-value: 7.13e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 17569903     13 VSFAVILSGSAFLIMVTATPVLFYTMGDMTAQLETAKTGFEETSNVLWKEL 63
Cdd:smart01088   3 AYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
PRK07764 super family cl35613
DNA polymerase III subunits gamma and tau; Validated
 171-396 8.69e-04

DNA polymerase III subunits gamma and tau; Validated


The actual alignment was detected with superfamily member PRK07764:

Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.51  E-value: 8.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  171 GDKGAPGNAGRDGAPGDDGPEGDHGHP----GPMGPAGEKGTSGADGKGFAKGAPGPKGPTGMDGLAGDEGLPGERGEDG 246
Cdd:PRK07764 589 GPAPGAAGGEGPPAPASSGPPEEAARPaapaAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDG 668

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  247 SAGAQGETGPQGPQGEKGPDGFPGLPGSAGASGEDAAYCPCPSRKGDIAGGGGGGYAAAPGTEFEGSPVESDPAKLSADI 326
Cdd:PRK07764 669 WPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDP 748

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  327 PAPSPISDVSAEGAGAPVSDASGEGPADSATEGEGAPAggapkGDTTYPTKNRARFTARQRAVSRIRRTF 396
Cdd:PRK07764 749 PDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMA-----EDDAPSMDDEDRRDAEEVAMELLEEEL 813
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 105-281 1.29e-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: 1.29e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  105 PAGPKGESGSAGEPGTDGTDGTPGKDGADGSneqtASQAGDLCTACPAGPPGVAGYKGKRGPRGEKGDKGAPGNAGRDGA 184
Cdd:NF038329 124 PAGPAGPAGEQGPRGDRGETGPAGPAGPPGP----QGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  185 PGDDGPEGDHGHPGPMGPAGEKGTSGADGKGfAKGAPGPKGPTGMDGLAGDEGLPGERGEDGSAGAQGETGPQGPQGEKG 264
Cdd:NF038329 200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPA-GDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG 278

                        170
                 ....*....|....*..
gi 17569903  265 PDGFPGLPGSAGASGED 281
Cdd:NF038329 279 ERGPVGPAGKDGQNGKD 295
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 79-264 7.96e-25

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 105.37  E-value: 7.96e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903   79 EGGAAGEGSPAATAPEASPVKiddscPAGPKGESGSAGEPGTDGTDGTPGKDGADGSNEQT--ASQAGDLCTACPAGPPG 156
Cdd:NF038329 154 PQGERGEKGPAGPQGEAGPQG-----PAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAgpAGPDGEAGPAGEDGPAG 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  157 VAGyKGKRGPRGEKGDKGAPGNAGRDGAPGDDGPEGDHGHPGPMGP---AGEKGTSGADGKGFAKGAPGPKGPTGMDGLA 233
Cdd:NF038329 229 PAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPdgkDGERGPVGPAGKDGQNGKDGLPGKDGKDGQN 307

                        170       180       190
                 ....*....|....*....|....*....|.
gi 17569903  234 GDEGLPGERGEDGSAGAQGETGPQGPQGEKG 264
Cdd:NF038329 308 GKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 81-293 9.65e-25

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: 104.99  E-value: 9.65e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903   81 GAAGEGSPAATAPEASPV-KIDDSCPAGPKGESGSAGEPGTDGTDGTPGKDGADGSNEQTASQ--AGDLCTACPAGPPGV 157
Cdd:NF038329 138 GDRGETGPAGPAGPPGPQgERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETgpAGEQGPAGPAGPDGE 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  158 AGYKGKRGP-----RGEKGDKGAPGNAGRDGAPGDDGPEGDHGHPGPMGPAGEKGTSGADGKGfakgapGPKGPTGMDGL 232
Cdd:NF038329 218 AGPAGEDGPagpagDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGER------GPVGPAGKDGQ 291

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17569903  233 AGDEGLPGERGEDGSAGAQGETGPQGPQGEKGPDGFPGLPGSAGASGEDAAYCPCPSRKGD 293
Cdd:NF038329 292 NGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPD 352
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 151-283 8.61e-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: 102.29  E-value: 8.61e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  151 PAGPPGVAGYKGKRGPRGEKGDKGAPGNAGRDGAPGDDGPEGDHGHPGPMGPAGEKGTSGADGKGFAKGAPGPKGPTGMD 230
Cdd:NF038329 124 PAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPA 203

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 17569903  231 GLAGDEGLPGERGEDGSAGAQGETGP-----QGPQGEKGPDGFPGLPGSAGASGEDAA 283
Cdd:NF038329 204 GEQGPAGPAGPDGEAGPAGEDGPAGPagdgqQGPDGDPGPTGEDGPQGPDGPAGKDGP 261
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 156-276 3.42e-18

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: 85.73  E-value: 3.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  156 GVAGYKGKRGPRGEKGDKGAPGNAGRDGAPGDDGPEGDHGHPGPMGPAGEKGTSGadgkgfAKGAPGPKGPTGMDGLAGD 235
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG------PQGPAGKDGEAGAKGPAGE 190

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 17569903  236 EGLPGERGEDGSAGAQGETGPQGPQGEKGPDGFPGLPGSAG 276
Cdd:NF038329 191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG 231
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 191-286 1.49e-13

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: 71.86  E-value: 1.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  191 EGDHGHPGPMGPAGEKGTSGADGKGFAKGAPGPKGPTGMDGLAGDEGLPGERGEDGSAGAQGETGPQGPQGEKGPDGFPG 270
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                         90
                 ....*....|....*.
gi 17569903  271 LPGSAGASGEDAAYCP 286
Cdd:NF038329 196 PRGETGPAGEQGPAGP 211
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 13-63 7.13e-07

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: 45.92  E-value: 7.13e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 17569903     13 VSFAVILSGSAFLIMVTATPVLFYTMGDMTAQLETAKTGFEETSNVLWKEL 63
Cdd:smart01088   3 AYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
PHA03169 PHA03169
hypothetical protein; Provisional
 65-270 9.15e-06

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 47.27  E-value: 9.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903   65 TNESHRRVARQTYKEGGAAGEGSPAATAPEASPVKiddscpAGPKGESGSAGEPGTDGTDGTPGKDGADGSNEQTASQAG 144
Cdd:PHA03169  75 TAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSG------SAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHE 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  145 DlctacpaGPPGVAGYKGKRGPRGEKGDKGAPGNAGRDGAPGDDGPEGDHGHPGPMGPAGEKGTSGADGKGFAKGAPGPK 224
Cdd:PHA03169 149 P-------APPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQ 221

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 17569903  225 GPTGMDGLAGDEGLPGERGEDGSAGAQGETGPQGPQGEKGPDGFPG 270
Cdd:PHA03169 222 APSPNTQQAVEHEDEPTEPEREGPPFPGHRSHSYTVVGWKPSTRPG 267
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 159-214 3.58e-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: 3.58e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 17569903   159 GYKGKRGPRGEKGDKGAPGNAGRDGAPGDDGPEGDHGHPGPMGPAGEKGTSGADGK 214
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 171-396 8.69e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.51  E-value: 8.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  171 GDKGAPGNAGRDGAPGDDGPEGDHGHP----GPMGPAGEKGTSGADGKGFAKGAPGPKGPTGMDGLAGDEGLPGERGEDG 246
Cdd:PRK07764 589 GPAPGAAGGEGPPAPASSGPPEEAARPaapaAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDG 668

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  247 SAGAQGETGPQGPQGEKGPDGFPGLPGSAGASGEDAAYCPCPSRKGDIAGGGGGGYAAAPGTEFEGSPVESDPAKLSADI 326
Cdd:PRK07764 669 WPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDP 748

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  327 PAPSPISDVSAEGAGAPVSDASGEGPADSATEGEGAPAggapkGDTTYPTKNRARFTARQRAVSRIRRTF 396
Cdd:PRK07764 749 PDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMA-----EDDAPSMDDEDRRDAEEVAMELLEEEL 813
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 79-281 6.04e-03

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


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 38.82  E-value: 6.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903     79 EGGAAGEGSPAATAPEASPVKIDDSCPAGPKGESGSAGEPGTDGTDGTPGKDGADGSNEQTASQAGDLCTACPAGPPGVA 158
Cdd:TIGR00927  670 EGETETKGENESEGEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEA 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903    159 GYKGKRGPRGEKGDKGAPGNAGRDGAPGDDGPEGDHGHPGPMgpageKGTSGADGKGFAKGAPGPKGPTGMDGLAGDEGL 238
Cdd:TIGR00927  750 EGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAGEDGEM-----KGDEGAEGKVEHEGETEAGEKDEHEGQSETQAD 824

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 17569903    239 -PGERGEDGSAGAQGETGPQGPQGEKGPDGFPGLPGSAGASGED 281
Cdd:TIGR00927  825 dTEVKDETGEQELNAENQGEAKQDEKGVDGGGGSDGGDSEEEEE 868
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 105-281 1.29e-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: 1.29e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  105 PAGPKGESGSAGEPGTDGTDGTPGKDGADGSneqtASQAGDLCTACPAGPPGVAGYKGKRGPRGEKGDKGAPGNAGRDGA 184
Cdd:NF038329 124 PAGPAGPAGEQGPRGDRGETGPAGPAGPPGP----QGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  185 PGDDGPEGDHGHPGPMGPAGEKGTSGADGKGfAKGAPGPKGPTGMDGLAGDEGLPGERGEDGSAGAQGETGPQGPQGEKG 264
Cdd:NF038329 200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPA-GDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG 278

                        170
                 ....*....|....*..
gi 17569903  265 PDGFPGLPGSAGASGED 281
Cdd:NF038329 279 ERGPVGPAGKDGQNGKD 295
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 79-264 7.96e-25

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 105.37  E-value: 7.96e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903   79 EGGAAGEGSPAATAPEASPVKiddscPAGPKGESGSAGEPGTDGTDGTPGKDGADGSNEQT--ASQAGDLCTACPAGPPG 156
Cdd:NF038329 154 PQGERGEKGPAGPQGEAGPQG-----PAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAgpAGPDGEAGPAGEDGPAG 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  157 VAGyKGKRGPRGEKGDKGAPGNAGRDGAPGDDGPEGDHGHPGPMGP---AGEKGTSGADGKGFAKGAPGPKGPTGMDGLA 233
Cdd:NF038329 229 PAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPdgkDGERGPVGPAGKDGQNGKDGLPGKDGKDGQN 307

                        170       180       190
                 ....*....|....*....|....*....|.
gi 17569903  234 GDEGLPGERGEDGSAGAQGETGPQGPQGEKG 264
Cdd:NF038329 308 GKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 81-293 9.65e-25

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: 104.99  E-value: 9.65e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903   81 GAAGEGSPAATAPEASPV-KIDDSCPAGPKGESGSAGEPGTDGTDGTPGKDGADGSNEQTASQ--AGDLCTACPAGPPGV 157
Cdd:NF038329 138 GDRGETGPAGPAGPPGPQgERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETgpAGEQGPAGPAGPDGE 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  158 AGYKGKRGP-----RGEKGDKGAPGNAGRDGAPGDDGPEGDHGHPGPMGPAGEKGTSGADGKGfakgapGPKGPTGMDGL 232
Cdd:NF038329 218 AGPAGEDGPagpagDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGER------GPVGPAGKDGQ 291

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17569903  233 AGDEGLPGERGEDGSAGAQGETGPQGPQGEKGPDGFPGLPGSAGASGEDAAYCPCPSRKGD 293
Cdd:NF038329 292 NGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPD 352
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 151-283 8.61e-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: 102.29  E-value: 8.61e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  151 PAGPPGVAGYKGKRGPRGEKGDKGAPGNAGRDGAPGDDGPEGDHGHPGPMGPAGEKGTSGADGKGFAKGAPGPKGPTGMD 230
Cdd:NF038329 124 PAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPA 203

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 17569903  231 GLAGDEGLPGERGEDGSAGAQGETGP-----QGPQGEKGPDGFPGLPGSAGASGEDAA 283
Cdd:NF038329 204 GEQGPAGPAGPDGEAGPAGEDGPAGPagdgqQGPDGDPGPTGEDGPQGPDGPAGKDGP 261
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 156-276 3.42e-18

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: 85.73  E-value: 3.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  156 GVAGYKGKRGPRGEKGDKGAPGNAGRDGAPGDDGPEGDHGHPGPMGPAGEKGTSGadgkgfAKGAPGPKGPTGMDGLAGD 235
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG------PQGPAGKDGEAGAKGPAGE 190

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 17569903  236 EGLPGERGEDGSAGAQGETGPQGPQGEKGPDGFPGLPGSAG 276
Cdd:NF038329 191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG 231
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 191-286 1.49e-13

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: 71.86  E-value: 1.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  191 EGDHGHPGPMGPAGEKGTSGADGKGFAKGAPGPKGPTGMDGLAGDEGLPGERGEDGSAGAQGETGPQGPQGEKGPDGFPG 270
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG 195

                         90
                 ....*....|....*.
gi 17569903  271 LPGSAGASGEDAAYCP 286
Cdd:NF038329 196 PRGETGPAGEQGPAGP 211
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 13-63 7.13e-07

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: 45.92  E-value: 7.13e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 17569903     13 VSFAVILSGSAFLIMVTATPVLFYTMGDMTAQLETAKTGFEETSNVLWKEL 63
Cdd:smart01088   3 AYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
PHA03169 PHA03169
hypothetical protein; Provisional
 65-270 9.15e-06

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 47.27  E-value: 9.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903   65 TNESHRRVARQTYKEGGAAGEGSPAATAPEASPVKiddscpAGPKGESGSAGEPGTDGTDGTPGKDGADGSNEQTASQAG 144
Cdd:PHA03169  75 TAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSG------SAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHE 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  145 DlctacpaGPPGVAGYKGKRGPRGEKGDKGAPGNAGRDGAPGDDGPEGDHGHPGPMGPAGEKGTSGADGKGFAKGAPGPK 224
Cdd:PHA03169 149 P-------APPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQ 221

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 17569903  225 GPTGMDGLAGDEGLPGERGEDGSAGAQGETGPQGPQGEKGPDGFPG 270
Cdd:PHA03169 222 APSPNTQQAVEHEDEPTEPEREGPPFPGHRSHSYTVVGWKPSTRPG 267
PHA03169 PHA03169
hypothetical protein; Provisional
 65-259 1.19e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 47.27  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903   65 TNESHRRVARQtykEGGAAGEGSPAATAPEASPVKIDDSCPAGPKGEsGSAGEPGTDGTDGTPGKDGADGSNEQTASQAG 144
Cdd:PHA03169  52 TTSGPQVRAVA---EQGHRQTESDTETAEESRHGEKEERGQGGPSGS-GSESVGSPTPSPSGSAEELASGLSPENTSGSS 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  145 DLCTACPAGPPGVAGYKGKRGPRGEKGDKGAPGNAGRDGAPGD--------DGPEGDHGHPGPMGPAGEKGTSGADGKGF 216
Cdd:PHA03169 128 PESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPShedspeepEPPTSEPEPDSPGPPQSETPTSSPPPQSP 207

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 17569903  217 AKGAPGPKGPTGMDGLAGDEGLPGERGEDGSAGAQGETGPQGP 259
Cdd:PHA03169 208 PDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFPGH 250
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 159-214 3.58e-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: 3.58e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 17569903   159 GYKGKRGPRGEKGDKGAPGNAGRDGAPGDDGPEGDHGHPGPMGPAGEKGTSGADGK 214
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 231-283 5.97e-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: 5.97e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 17569903   231 GLAGDEGLPGERGEDGSAGAQGETGPQGPQGEKGPDGFPGLPGSAGASGEDAA 283
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 219-277 1.20e-04

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: 39.40  E-value: 1.20e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 17569903   219 GAPGPKGPTGMDGLAgdeGLPGERGEDGSAGAQGETGPQGPQGEKGPDGFPGLPGSAGA 277
Cdd:pfam01391   1 GPPGPPGPPGPPGPP---GPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 79-394 2.27e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903    79 EGGAAGEGSPAATAPEASPVKIDDSCPAGPKGESGSAGEPGTDGTDGTPGKDGADGSNEQTASQAGDLCTACPAGPPGVA 158
Cdd:PHA03307  108 PPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPS 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903   159 GykgkrgprgekGDKGAPGNAGRDGAPGDDGPEGDHGHPGPMGPAGEKGTSGADGKGFAKGAPGPKGPTGMDGlagdegl 238
Cdd:PHA03307  188 S-----------PPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGW------- 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903   239 pGERGEDGSAGAQGETGPQGPQGEKGPDGFPGLPGSAGASGEDAAYCPCPSRKGDiagGGGGGYAAAPGTEFEGSPVESD 318
Cdd:PHA03307  250 -GPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSP---GSGPAPSSPRASSSSSSSRESS 325

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17569903   319 PAKLSADIPAPSPISDVSAEGAGAPVSDASGEGPADSATEGEGAPAGGAPKGDTTYPTKNRARFTARQRAVSRIRR 394
Cdd:PHA03307  326 SSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRR 401
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 42-228 2.54e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 2.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903   42 TAQLETAKTGFEETSNVLWKELVTNESHRRVARQTYKEGGAAGEGSPAATAPEASPVKIDDSCPAGPKGESGSAGEPGTD 121
Cdd:PRK07764 585 EAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASD 664

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  122 GTDGTPGKDGADGSNEQTASQAGDLCTACPAGPPGVAGYKGKRGPRGEKGDKGAPGNAGRDGAPGDDGPEGDHGHPGPMG 201
Cdd:PRK07764 665 GGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPE 744

                        170       180
                 ....*....|....*....|....*..
gi 17569903  202 PAGEKGTSGADGKGFAKGAPGPKGPTG 228
Cdd:PRK07764 745 PDDPPDPAGAPAQPPPPPAPAPAAAPA 771
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 219-272 2.56e-04

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: 38.63  E-value: 2.56e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 17569903   219 GAPGPKGPTGMDGLAGDEGLPGERGEDGSAGAQGETGPQGPQGEKGPDGFPGLP 272
Cdd:pfam01391   4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 151-203 3.61e-04

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: 38.24  E-value: 3.61e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 17569903   151 PAGPPGVAGYKGKRGPRGEKGDKGAPGNAGRDGAPGDDGPEGDHGHPGPMGPA 203
Cdd:pfam01391   5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PHA03169 PHA03169
hypothetical protein; Provisional
 167-356 7.26e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 41.49  E-value: 7.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  167 RGEKGDKGApgnaGRDGAPGDDGPEGDHGHPGPMGPAGEKGTSGADGKGFAKGAPGPKGPTGMDGLAGDEGLPGERGEDG 246
Cdd:PHA03169  81 HGEKEERGQ----GGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHN 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  247 SAGAQGETGPQGPQGEKGPDGFPGLPGSAGASGEDAAYCPCPSRKGDIAGGGGGGYAAAPGTEFEGSPVESDPAKLSADI 326
Cdd:PHA03169 157 PSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDE 236

                        170       180       190
                 ....*....|....*....|....*....|
gi 17569903  327 PAPSPISDVSAEGAGAPVSDASGEGPADSA 356
Cdd:PHA03169 237 PTEPEREGPPFPGHRSHSYTVVGWKPSTRP 266
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 171-396 8.69e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.51  E-value: 8.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  171 GDKGAPGNAGRDGAPGDDGPEGDHGHP----GPMGPAGEKGTSGADGKGFAKGAPGPKGPTGMDGLAGDEGLPGERGEDG 246
Cdd:PRK07764 589 GPAPGAAGGEGPPAPASSGPPEEAARPaapaAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDG 668

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  247 SAGAQGETGPQGPQGEKGPDGFPGLPGSAGASGEDAAYCPCPSRKGDIAGGGGGGYAAAPGTEFEGSPVESDPAKLSADI 326
Cdd:PRK07764 669 WPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDP 748

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  327 PAPSPISDVSAEGAGAPVSDASGEGPADSATEGEGAPAggapkGDTTYPTKNRARFTARQRAVSRIRRTF 396
Cdd:PRK07764 749 PDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMA-----EDDAPSMDDEDRRDAEEVAMELLEEEL 813
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 168-223 1.19e-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: 36.70  E-value: 1.19e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 17569903   168 GEKGDKGAPGNAGRDGAPGDDGPEGDHGHPGPMGPAGEKGTSGADGKGFAKGAPGP 223
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 125-358 1.64e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  125 GTPGKDGADGSNEQTASQAGDLCTACPAGPPgvagykgkrGPRGEKGDKGAPGNAGRDGAPGDDGPEGDHGHPGPMGPAG 204
Cdd:PRK07764 589 GPAPGAAGGEGPPAPASSGPPEEAARPAAPA---------APAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAV 659

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  205 EKGTSGADGKGFAKGAPGPKGPTGMDGLAGDEGLPGERGEDGSAGAQGETGPQGPQGEKGPDGFPGLPGSAGASGEDAAY 284
Cdd:PRK07764 660 PDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPV 739

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17569903  285 CPCPSRKGDIAGGGGGGYAAAPGTEFEGSPVESDPAklsadiPAPSPISDVSAEGAGAPVSDASGEGPADSATE 358
Cdd:PRK07764 740 PLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPP------PSPPSEEEEMAEDDAPSMDDEDRRDAEEVAME 807
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 148-369 5.94e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 38.81  E-value: 5.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  148 TACPAGPPGVAGYKGKRGPRGekgdKGAPGNAGRDGAPgdDGPEGDHGHPGPMGPAGEKGTSGADGKGFAKGAPGPKGPT 227
Cdd:PRK07764 585 EAVVGPAPGAAGGEGPPAPAS----SGPPEEAARPAAP--AAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVA 658

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903  228 GMDGLAGDEGLPGERGEDGSAGAQGETGPQGPQGEKGPDGFPGLPG-SAGASGEDAAYCPCPSRKGDIAGGGGGGYAAAP 306
Cdd:PRK07764 659 VPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPApAATPPAGQADDPAAQPPQAAQGASAPSPAADDP 738

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17569903  307 GTEFEGSPVESDPAKLSADIPAPSPISDVSAEGAGAPVSDAS-GEGPADSATEGEGAPAGGAPK 369
Cdd:PRK07764 739 VPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSeEEEMAEDDAPSMDDEDRRDAE 802
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 79-281 6.04e-03

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


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 38.82  E-value: 6.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903     79 EGGAAGEGSPAATAPEASPVKIDDSCPAGPKGESGSAGEPGTDGTDGTPGKDGADGSNEQTASQAGDLCTACPAGPPGVA 158
Cdd:TIGR00927  670 EGETETKGENESEGEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEA 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569903    159 GYKGKRGPRGEKGDKGAPGNAGRDGAPGDDGPEGDHGHPGPMgpageKGTSGADGKGFAKGAPGPKGPTGMDGLAGDEGL 238
Cdd:TIGR00927  750 EGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAGEDGEM-----KGDEGAEGKVEHEGETEAGEKDEHEGQSETQAD 824

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 17569903    239 -PGERGEDGSAGAQGETGPQGPQGEKGPDGFPGLPGSAGASGED 281
Cdd:TIGR00927  825 dTEVKDETGEQELNAENQGEAKQDEKGVDGGGGSDGGDSEEEEE 868
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 195-248 7.50e-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: 34.39  E-value: 7.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 17569903   195 GHPGPMGPAGEKGTSGADGKGFAKGAPGPKGPTGMDGLAGDEGLPGERGEDGSA 248
Cdd:pfam01391   4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
 
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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