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Conserved domains on  [gi|326676611|ref|XP_001343145|]
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acetylcholinesterase collagenic tail peptide [Danio rerio]

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 ...
 103-247 4.61e-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: 112.69  E-value: 4.61e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326676611 103 GPAGPQGDRGIPGMVGPKGDKGDLGRPGSKGRTGRPGLPGKPGSAGLPGPEGPKGEKGDPGLMGMPGMRGPVGPKGLAGY 182
Cdd:NF038329 129 GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGP 208

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 326676611 183 KGEKGARGDFGPAGP--------KGDKGATGLPGMLGQKGEMGPKGESGVSGKRGPTGRPGKRGKQGADGERG 247
Cdd:NF038329 209 AGPAGPDGEAGPAGEdgpagpagDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281
DUF4215 pfam13948
Domain of unknown function (DUF4215); The function of this family is unknown.
 374-402 3.39e-03

Domain of unknown function (DUF4215); The function of this family is unknown.


:

Pssm-ID: 290659  Cd Length: 47  Bit Score: 35.46  E-value: 3.39e-03
                          10        20
                  ....*....|....*....|....*....
gi 326676611  374 CGDGDVQelNGEECDDGNRVVTDDCIGCK 402
Cdd:pfam13948  21 CGDGIIV--NNEQCDDGNNLQFDGCYQCQ 47
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 103-247 4.61e-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: 112.69  E-value: 4.61e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326676611 103 GPAGPQGDRGIPGMVGPKGDKGDLGRPGSKGRTGRPGLPGKPGSAGLPGPEGPKGEKGDPGLMGMPGMRGPVGPKGLAGY 182
Cdd:NF038329 129 GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGP 208

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 326676611 183 KGEKGARGDFGPAGP--------KGDKGATGLPGMLGQKGEMGPKGESGVSGKRGPTGRPGKRGKQGADGERG 247
Cdd:NF038329 209 AGPAGPDGEAGPAGEdgpagpagDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 110-247 2.96e-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: 104.60  E-value: 2.96e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326676611 110 DRGIPGMVGPKGDKGDLGRPGSKGRTGRPGLPGKPGSAGLPGPEGP-----KGEKGDPGLMGMPGMRGPVGPKGLAGYKG 184
Cdd:NF038329 184 AKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagdgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 326676611 185 EKGARGDFGPAGPKGDKGATGLPGMLGQKGEMGPKGESGVSGKRGPTGRPGKRGKQGADGERG 247
Cdd:NF038329 264 DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDG 326
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 106-247 4.93e-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: 103.83  E-value: 4.93e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326676611 106 GPQGDRGIPGMVGPKGDKGDLGRPGSKGRTGRPGLPGKPGSAGLPGPEGPKGEKGDPGLMGMPGM-----RGPVGPKGLA 180
Cdd:NF038329 165 GPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagdgqQGPDGDPGPT 244

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 326676611 181 GYKGEKGARGDFGPAGPKGDKGATGLPGMLGQKGEMGPKGESGVSGKRGPTGRPGKRGKQGADGERG 247
Cdd:NF038329 245 GEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 110-247 1.88e-22

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: 99.21  E-value: 1.88e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326676611 110 DRGIPGMVGPKGDKGDLGRPGSKGRTGRPGLPGKP-----GSAGLPGPEGPKGEKGDPGLMGMPGMRGPVGPKGLAGYKG 184
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgdgqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 326676611 185 EKGARGDFGPAGPKGDKGATGLPGMLGQKGEMGPKGESGVSGKRGPTGRPGKRGKQGADGERG 247
Cdd:NF038329 276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 139-290 4.39e-22

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: 98.05  E-value: 4.39e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326676611 139 GLPGKPGSAGLPGPEGPKGEKGDPGLMGMPGMRGPVGPKGLAGYKGEKGARGDFGPAGP---KGDKGATGLPgmlGQKGE 215
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPagkDGEAGAKGPA---GEKGP 193

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 326676611 216 MGPKGESGVSGKRGPTGRPGKRGKQGADGERGFSGPVGPIGPPGPRGHPGPPGVPASG----LFVVGEKGEMGLPGPPG 290
Cdd:NF038329 194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGpdgpAGKDGPRGDRGEAGPDG 272
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 142-234 9.81e-15

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: 75.71  E-value: 9.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326676611 142 GKPGSAGLPGPEGPKGEKGDPGLMGMPGMRGPVGPKGLAGYKGEKGARGDFGPAGPKGDKGATGLPGMLGQKGEMGPKGE 221
Cdd:NF038329 248 GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327

                         90
                 ....*....|...
gi 326676611 222 SGVSGKRGPTGRP 234
Cdd:NF038329 328 PGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 169-313 6.09e-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: 70.32  E-value: 6.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326676611 169 GMRGPVGPKGLAGYKGEKGARGDFGPAGPKGDKGATGLPGMLGQKGEMGPKGESGVSGKRGPTGRPGKRGKQGADGERGf 248
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG- 195

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 326676611 249 sgpvgpigppgPRGHPGPPgvpasglfvvGEKGEMGLPGPPGVCDCSFPSLSPASAPLQHRNKYG 313
Cdd:NF038329 196 -----------PRGETGPA----------GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDG 239
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 133-189 1.87e-08

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 50.57  E-value: 1.87e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 326676611  133 GRTGRPGLPGKPGSAGLPGPEGPKGEKGDPGLMGMPGMRGPVGPKGLAGYKGEKGAR 189
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
114-291 5.28e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 45.41  E-value: 5.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326676611 114 PGMVGPKGDKGDLGRPGSKGRTGrpglpgKPGSAGLPGPEGPKGEKGDPGLMGMPGMRGPVGPKGLAGYKGEKGARGDFG 193
Cdd:COG5164    6 PGKTGPSDPGGVTTPAGSQGSTK------PAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326676611 194 PAGPKGDKGATGLPGmlgQKGEMGPKGESGVSGKRGPTGRPGKRGKQGADGergfsgpvgpigpPGPRGHPGPPGVPASG 273
Cdd:COG5164   80 GTTPAQNQGGTRPAG---NTGGTTPAGDGGATGPPDDGGATGPPDDGGSTT-------------PPSGGSTTPPGDGGST 143

                        170
                 ....*....|....*...
gi 326676611 274 LFVVGEKGEMGLPGPPGV 291
Cdd:COG5164  144 PPGPGSTGPGGSTTPPGD 161
DUF4215 pfam13948
Domain of unknown function (DUF4215); The function of this family is unknown.
 374-402 3.39e-03

Domain of unknown function (DUF4215); The function of this family is unknown.


Pssm-ID: 290659  Cd Length: 47  Bit Score: 35.46  E-value: 3.39e-03
                          10        20
                  ....*....|....*....|....*....
gi 326676611  374 CGDGDVQelNGEECDDGNRVVTDDCIGCK 402
Cdd:pfam13948  21 CGDGIIV--NNEQCDDGNNLQFDGCYQCQ 47
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
 374-398 9.53e-03

Myxococcus cysteine-rich repeat; This model represents a sequence region shared between several proteins of Myxococcus xanthus DK 1622 and some eukaryotic proteins that include human pappalysin-1 (SP|Q13219). The region of about 40 amino acids contains several conserved Cys residues presumed to form disulfide bonds. The region appears in up to 13 repeats in Myxococcus.


Pssm-ID: 200169 [Multi-domain]  Cd Length: 38  Bit Score: 33.89  E-value: 9.53e-03
                          10        20
                  ....*....|....*....|....*
gi 326676611  374 CGDGDVQElnGEECDDGNRVVTDDC 398
Cdd:TIGR02232   4 CGDGIIEP--GEECDDGNTTSGDGC 26
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 103-247 4.61e-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: 112.69  E-value: 4.61e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326676611 103 GPAGPQGDRGIPGMVGPKGDKGDLGRPGSKGRTGRPGLPGKPGSAGLPGPEGPKGEKGDPGLMGMPGMRGPVGPKGLAGY 182
Cdd:NF038329 129 GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGP 208

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 326676611 183 KGEKGARGDFGPAGP--------KGDKGATGLPGMLGQKGEMGPKGESGVSGKRGPTGRPGKRGKQGADGERG 247
Cdd:NF038329 209 AGPAGPDGEAGPAGEdgpagpagDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG 281
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 110-247 2.96e-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: 104.60  E-value: 2.96e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326676611 110 DRGIPGMVGPKGDKGDLGRPGSKGRTGRPGLPGKPGSAGLPGPEGP-----KGEKGDPGLMGMPGMRGPVGPKGLAGYKG 184
Cdd:NF038329 184 AKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagdgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 326676611 185 EKGARGDFGPAGPKGDKGATGLPGMLGQKGEMGPKGESGVSGKRGPTGRPGKRGKQGADGERG 247
Cdd:NF038329 264 DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDG 326
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 106-247 4.93e-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: 103.83  E-value: 4.93e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326676611 106 GPQGDRGIPGMVGPKGDKGDLGRPGSKGRTGRPGLPGKPGSAGLPGPEGPKGEKGDPGLMGMPGM-----RGPVGPKGLA 180
Cdd:NF038329 165 GPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagdgqQGPDGDPGPT 244

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 326676611 181 GYKGEKGARGDFGPAGPKGDKGATGLPGMLGQKGEMGPKGESGVSGKRGPTGRPGKRGKQGADGERG 247
Cdd:NF038329 245 GEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 110-247 1.88e-22

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: 99.21  E-value: 1.88e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326676611 110 DRGIPGMVGPKGDKGDLGRPGSKGRTGRPGLPGKP-----GSAGLPGPEGPKGEKGDPGLMGMPGMRGPVGPKGLAGYKG 184
Cdd:NF038329 196 PRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgdgqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 326676611 185 EKGARGDFGPAGPKGDKGATGLPGMLGQKGEMGPKGESGVSGKRGPTGRPGKRGKQGADGERG 247
Cdd:NF038329 276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 139-290 4.39e-22

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: 98.05  E-value: 4.39e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326676611 139 GLPGKPGSAGLPGPEGPKGEKGDPGLMGMPGMRGPVGPKGLAGYKGEKGARGDFGPAGP---KGDKGATGLPgmlGQKGE 215
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPagkDGEAGAKGPA---GEKGP 193

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 326676611 216 MGPKGESGVSGKRGPTGRPGKRGKQGADGERGFSGPVGPIGPPGPRGHPGPPGVPASG----LFVVGEKGEMGLPGPPG 290
Cdd:NF038329 194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGpdgpAGKDGPRGDRGEAGPDG 272
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 142-234 9.81e-15

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: 75.71  E-value: 9.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326676611 142 GKPGSAGLPGPEGPKGEKGDPGLMGMPGMRGPVGPKGLAGYKGEKGARGDFGPAGPKGDKGATGLPGMLGQKGEMGPKGE 221
Cdd:NF038329 248 GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327

                         90
                 ....*....|...
gi 326676611 222 SGVSGKRGPTGRP 234
Cdd:NF038329 328 PGKDGKDGQPGKP 340
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 169-313 6.09e-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: 70.32  E-value: 6.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326676611 169 GMRGPVGPKGLAGYKGEKGARGDFGPAGPKGDKGATGLPGMLGQKGEMGPKGESGVSGKRGPTGRPGKRGKQGADGERGf 248
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQG- 195

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 326676611 249 sgpvgpigppgPRGHPGPPgvpasglfvvGEKGEMGLPGPPGVCDCSFPSLSPASAPLQHRNKYG 313
Cdd:NF038329 196 -----------PRGETGPA----------GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDG 239
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 133-189 1.87e-08

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 50.57  E-value: 1.87e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 326676611  133 GRTGRPGLPGKPGSAGLPGPEGPKGEKGDPGLMGMPGMRGPVGPKGLAGYKGEKGAR 189
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 127-181 2.01e-08

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 50.57  E-value: 2.01e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 326676611  127 GRPGSKGRTGRPGLPGKPGSAGLPGPEGPKGEKGDPGLMGMPGMRGPVGPKGLAG 181
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 166-221 6.70e-08

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 49.03  E-value: 6.70e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 326676611  166 GMPGMRGPVGPKGLAGYKGEKGARGDFGPAGPKGDKGATGLPGMLGQKGEMGPKGE 221
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 142-197 7.40e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.95  E-value: 7.40e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 326676611  142 GKPGSAGLPGPEGPKGEKGDPGLMGMPGMRGPVGPKGLAGYKGEKGARGDFGPAGP 197
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 148-207 1.08e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.56  E-value: 1.08e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 326676611  148 GLPGPEGPKGEKGDPGLmgmPGMRGPVGPKGLAGYKGEKGARGDFGPAGPKGDKGATGLP 207
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGP---PGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 115-163 2.92e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.41  E-value: 2.92e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 326676611  115 GMVGPKGDKGDLGRPGSKGRTGRPGLPGKPGSAGLPGPEGPKGEKGDPG 163
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 193-247 7.64e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.25  E-value: 7.64e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 326676611  193 GPAGPKGDKGATGLPGMLGQKGEMGPKGESGVSGKRGPTGRPGKRGKQGADGERG 247
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 172-228 8.03e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 43.25  E-value: 8.03e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 326676611  172 GPVGPKGLAGYKGEKGARGDFGPAGPKGDKGATGLPGMLGQKGEMGPKGESGVSGKR 228
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 121-176 1.73e-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: 1.73e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 326676611  121 GDKGDLGRPGSKGRTGRPGLPGKPGSAGLPGPEGPKGEKGDPGLMGMPGMRGPVGP 176
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
114-291 5.28e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 45.41  E-value: 5.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326676611 114 PGMVGPKGDKGDLGRPGSKGRTGrpglpgKPGSAGLPGPEGPKGEKGDPGLMGMPGMRGPVGPKGLAGYKGEKGARGDFG 193
Cdd:COG5164    6 PGKTGPSDPGGVTTPAGSQGSTK------PAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326676611 194 PAGPKGDKGATGLPGmlgQKGEMGPKGESGVSGKRGPTGRPGKRGKQGADGergfsgpvgpigpPGPRGHPGPPGVPASG 273
Cdd:COG5164   80 GTTPAQNQGGTRPAG---NTGGTTPAGDGGATGPPDDGGATGPPDDGGSTT-------------PPSGGSTTPPGDGGST 143

                        170
                 ....*....|....*...
gi 326676611 274 LFVVGEKGEMGLPGPPGV 291
Cdd:COG5164  144 PPGPGSTGPGGSTTPPGD 161
DUF4215 pfam13948
Domain of unknown function (DUF4215); The function of this family is unknown.
 374-402 3.39e-03

Domain of unknown function (DUF4215); The function of this family is unknown.


Pssm-ID: 290659  Cd Length: 47  Bit Score: 35.46  E-value: 3.39e-03
                          10        20
                  ....*....|....*....|....*....
gi 326676611  374 CGDGDVQelNGEECDDGNRVVTDDCIGCK 402
Cdd:pfam13948  21 CGDGIIV--NNEQCDDGNNLQFDGCYQCQ 47
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
 374-398 9.53e-03

Myxococcus cysteine-rich repeat; This model represents a sequence region shared between several proteins of Myxococcus xanthus DK 1622 and some eukaryotic proteins that include human pappalysin-1 (SP|Q13219). The region of about 40 amino acids contains several conserved Cys residues presumed to form disulfide bonds. The region appears in up to 13 repeats in Myxococcus.


Pssm-ID: 200169 [Multi-domain]  Cd Length: 38  Bit Score: 33.89  E-value: 9.53e-03
                          10        20
                  ....*....|....*....|....*
gi 326676611  374 CGDGDVQElnGEECDDGNRVVTDDC 398
Cdd:TIGR02232   4 CGDGIIEP--GEECDDGNTTSGDGC 26
 
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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