NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|74199399|dbj|BAE33218|]
View 

unnamed protein product [Mus musculus]

Protein Classification

phage tail protein( domain architecture ID 10507594)

phage tail protein is part of a multi-protein structure that mediates the attachment, digestion and penetration of the cell wall and genome ejection

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Macscav_rec pfam03523
Macrophage scavenger receptor;
125-173 1.68e-23

Macrophage scavenger receptor;


:

Pssm-ID: 460956  Cd Length: 49  Bit Score: 91.75  E-value: 1.68e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 74199399   125 MEERIQSISNSKADLIDTGRFQNFSMATDQRLNDILLQLNSLILSVQEH 173
Cdd:pfam03523   1 MEKRIQYISDSEANLIDSEHFQNFSMTTDQRFNDVLLQLNTLVSSVQEH 49
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 277-338 7.41e-21

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: 84.47  E-value: 7.41e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74199399   277 GPPGPqgekgdRGLTGQTGPPGAPGIRGIPGVKGDRGQIGFPGGRGNPGAPGKPGRSGSPGP 338
Cdd:pfam01391   1 GPPGP------PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
GumC super family cl34566
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
135-259 3.37e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


The actual alignment was detected with superfamily member COG3206:

Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.23  E-value: 3.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199399 135 SKADLIDTGRFQNFSMatdQRLNDILLQLNSLILSVQEHGNSLDAISKSLQSLNMTLLDVQLHTETLHVRVRESTAKQQe 214
Cdd:COG3206 203 QKNGLVDLSEEAKLLL---QQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAE- 278

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 74199399 215 dISKLEERVYKVSAEVQSVKEEQAHVEQEVKQEV-RVLNNITNDLR 259
Cdd:COG3206 279 -LAELSARYTPNHPDVIALRAQIAALRAQLQQEAqRILASLEAELE 323
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 328-350 6.36e-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: 6.36e-03
                          10        20
                  ....*....|....*....|...
gi 74199399   328 GKPGRSGSPGPKGQKGEKGSVGG 350
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGP 23
 
Name Accession Description Interval E-value
Macscav_rec pfam03523
Macrophage scavenger receptor;
125-173 1.68e-23

Macrophage scavenger receptor;


Pssm-ID: 460956  Cd Length: 49  Bit Score: 91.75  E-value: 1.68e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 74199399   125 MEERIQSISNSKADLIDTGRFQNFSMATDQRLNDILLQLNSLILSVQEH 173
Cdd:pfam03523   1 MEKRIQYISDSEANLIDSEHFQNFSMTTDQRFNDVLLQLNTLVSSVQEH 49
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 277-338 7.41e-21

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: 84.47  E-value: 7.41e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74199399   277 GPPGPqgekgdRGLTGQTGPPGAPGIRGIPGVKGDRGQIGFPGGRGNPGAPGKPGRSGSPGP 338
Cdd:pfam01391   1 GPPGP------PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 276-349 8.67e-17

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: 81.10  E-value: 8.67e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74199399  276 QGPPGPQGEKGDRGLTGQTGPPGAPGIRGIPGVKGDRGQIGFPGGRGNPGAPGKPGRSGSPGPKGQKGEKGSVG 349
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 276-349 2.22e-14

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: 73.79  E-value: 2.22e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74199399  276 QGPPGPQGEKGDRGLTGQTGPPGA---PGIRGIPGVKGDRGQIGFPGGRGNPGAPGKPGRSGSPG--PKGQKGEKGSVG 349
Cdd:NF038329 167 QGEAGPQGPAGKDGEAGAKGPAGEkgpQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTG 245
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 276-349 2.52e-14

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: 73.79  E-value: 2.52e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74199399  276 QGPPGPQGEKGDRGLTGQTGPPGAPGIRGIPGVKGDRGQ---IGFPGGRGNPGAPGKPGRSGSPGPKGQKGEKGSVG 349
Cdd:NF038329 131 AGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEagpQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 277-349 1.17e-12

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: 68.39  E-value: 1.17e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74199399  277 GPPGPQGEKGDRGLTGQTGPPGAPGIRGIPGVKGDRGQigfPGGRGNPGAPGKPGRSGSPGPKGQKGEKGSVG 349
Cdd:NF038329 254 GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ---NGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 276-349 3.48e-12

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: 67.24  E-value: 3.48e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74199399  276 QGPPGPQGEKGDRGLTGQTGPPGAPGIRGIPGVKGDRGQIGFPGGRGNPGAPGKPGRSGS---PGPKGQKGEKGSVG 349
Cdd:NF038329 235 QGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKdglPGKDGKDGQNGKDG 311
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 277-346 1.35e-10

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: 62.23  E-value: 1.35e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74199399  277 GPPGPQ---GEKGDRGLTGQTGPPGAPGIRGIPGVKGDRGQIGFPGGRGNPGAPGKPGRSGSPGPKGQKGEKG 346
Cdd:NF038329 266 GEAGPDgpdGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
277-354 7.61e-07

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 50.80  E-value: 7.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199399 277 GPPGPQGEKGDRGLTGQTGPPgAPGIRGIPGVKGDRGQIG----FPGGRGNPGAPGKPGRSGSPGPKGQKGEKGSVGGSR 352
Cdd:COG5164 166 TPPGPGGSTTPPDDGGSTTPP-NKGETGTDIPTGGTPRQGpdgpVKKDDKNGKGNPPDDRGGKTGPKDQRPKTNPIERRG 244


                ..
gi 74199399 353 SV 354
Cdd:COG5164 245 PE 246
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
135-259 3.37e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.23  E-value: 3.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199399 135 SKADLIDTGRFQNFSMatdQRLNDILLQLNSLILSVQEHGNSLDAISKSLQSLNMTLLDVQLHTETLHVRVRESTAKQQe 214
Cdd:COG3206 203 QKNGLVDLSEEAKLLL---QQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAE- 278

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 74199399 215 dISKLEERVYKVSAEVQSVKEEQAHVEQEVKQEV-RVLNNITNDLR 259
Cdd:COG3206 279 -LAELSARYTPNHPDVIALRAQIAALRAQLQQEAqRILASLEAELE 323
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 150-254 4.60e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 38.46  E-value: 4.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199399    150 MATDQRLNDILLQLNSLILSVQEHGNSLDAISKSLQSLNMTLLDVQlhTETLHVRVRESTAKQQEdISKLEERVYKVSAE 229
Cdd:smart00787 164 MKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRA--KEKLKKLLQEIMIKVKK-LEELEEELQELESK 240

                           90       100
                   ....*....|....*....|....*
gi 74199399    230 VQSVKEEQAHVEQEVKQEVRVLNNI 254
Cdd:smart00787 241 IEDLTNKKSELNTEIAEAEKKLEQC 265
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 328-350 6.36e-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: 6.36e-03
                          10        20
                  ....*....|....*....|...
gi 74199399   328 GKPGRSGSPGPKGQKGEKGSVGG 350
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGP 23
PTZ00146 PTZ00146
fibrillarin; Provisional
 283-348 6.45e-03

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 37.79  E-value: 6.45e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74199399  283 GEKGDRGltgqTGPPGAPGIRGipgvKGDRGQIGFPGGRGNPGAPGKPGRSGSPGPKGQKGEKGSV 348
Cdd:PTZ00146   1 GMGGGFG----GGRGGGRGGGG----GGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGGGGPGKVI 58
 
Name Accession Description Interval E-value
Macscav_rec pfam03523
Macrophage scavenger receptor;
125-173 1.68e-23

Macrophage scavenger receptor;


Pssm-ID: 460956  Cd Length: 49  Bit Score: 91.75  E-value: 1.68e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 74199399   125 MEERIQSISNSKADLIDTGRFQNFSMATDQRLNDILLQLNSLILSVQEH 173
Cdd:pfam03523   1 MEKRIQYISDSEANLIDSEHFQNFSMTTDQRFNDVLLQLNTLVSSVQEH 49
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 277-338 7.41e-21

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: 84.47  E-value: 7.41e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74199399   277 GPPGPqgekgdRGLTGQTGPPGAPGIRGIPGVKGDRGQIGFPGGRGNPGAPGKPGRSGSPGP 338
Cdd:pfam01391   1 GPPGP------PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 292-346 6.12e-18

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: 76.76  E-value: 6.12e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 74199399   292 GQTGPPGAPGIRGIPGVKGDRGQIGFPGGRGNPGAPGKPGRSGSPGPKGQKGEKG 346
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 295-349 1.40e-17

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: 75.61  E-value: 1.40e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 74199399   295 GPPGAPGIRGIPGVKGDRGQIGFPGGRGNPGAPGKPGRSGSPGPKGQKGEKGSVG 349
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 276-349 8.67e-17

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: 81.10  E-value: 8.67e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74199399  276 QGPPGPQGEKGDRGLTGQTGPPGAPGIRGIPGVKGDRGQIGFPGGRGNPGAPGKPGRSGSPGPKGQKGEKGSVG 349
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 276-349 2.22e-14

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: 73.79  E-value: 2.22e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74199399  276 QGPPGPQGEKGDRGLTGQTGPPGA---PGIRGIPGVKGDRGQIGFPGGRGNPGAPGKPGRSGSPG--PKGQKGEKGSVG 349
Cdd:NF038329 167 QGEAGPQGPAGKDGEAGAKGPAGEkgpQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTG 245
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 276-349 2.52e-14

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: 73.79  E-value: 2.52e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74199399  276 QGPPGPQGEKGDRGLTGQTGPPGAPGIRGIPGVKGDRGQ---IGFPGGRGNPGAPGKPGRSGSPGPKGQKGEKGSVG 349
Cdd:NF038329 131 AGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEagpQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 277-349 1.17e-12

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: 68.39  E-value: 1.17e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74199399  277 GPPGPQGEKGDRGLTGQTGPPGAPGIRGIPGVKGDRGQigfPGGRGNPGAPGKPGRSGSPGPKGQKGEKGSVG 349
Cdd:NF038329 254 GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQ---NGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 276-349 3.48e-12

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: 67.24  E-value: 3.48e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74199399  276 QGPPGPQGEKGDRGLTGQTGPPGAPGIRGIPGVKGDRGQIGFPGGRGNPGAPGKPGRSGS---PGPKGQKGEKGSVG 349
Cdd:NF038329 235 QGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKdglPGKDGKDGQNGKDG 311
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 276-330 3.65e-11

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 57.89  E-value: 3.65e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 74199399   276 QGPPGPQGEKGDRGLTGQTGPPGAPgirgipgvkgdrgqiGFPGGRGNPGAPGKP 330
Cdd:pfam01391  18 PGPPGPPGPPGPPGEPGPPGPPGPP---------------GPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 277-346 1.35e-10

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: 62.23  E-value: 1.35e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74199399  277 GPPGPQ---GEKGDRGLTGQTGPPGAPGIRGIPGVKGDRGQIGFPGGRGNPGAPGKPGRSGSPGPKGQKGEKG 346
Cdd:NF038329 266 GEAGPDgpdGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
277-354 7.61e-07

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 50.80  E-value: 7.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199399 277 GPPGPQGEKGDRGLTGQTGPPgAPGIRGIPGVKGDRGQIG----FPGGRGNPGAPGKPGRSGSPGPKGQKGEKGSVGGSR 352
Cdd:COG5164 166 TPPGPGGSTTPPDDGGSTTPP-NKGETGTDIPTGGTPRQGpdgpVKKDDKNGKGNPPDDRGGKTGPKDQRPKTNPIERRG 244


                ..
gi 74199399 353 SV 354
Cdd:COG5164 245 PE 246
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
277-352 1.64e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 49.64  E-value: 1.64e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74199399 277 GPPGPQGEKGDRGLTGQTGPPGAPGIRGiPGvkGDRGQIGFPGGRGNPGAPGKPGRSGSPGPKGQKGEKGSVGGSR 352
Cdd:COG5164  10 GPSDPGGVTTPAGSQGSTKPAQNQGSTR-PA--GNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTT 82
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
276-349 2.09e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 49.26  E-value: 2.09e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74199399 276 QGPPGPQGEKGDRGLTGQTGPPGAPGIRGIPGVKGDRGQIGFPGGR---GNPGAPGKPGRSGSPGPKGQKGEKGSVG 349
Cdd:COG5164  36 TRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTtpaQNQGGTRPAGNTGGTTPAGDGGATGPPD 112
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
276-353 1.25e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 46.95  E-value: 1.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199399 276 QGPPGPQGEKGDRGLTGQTGPPGAPGIRGIPGVKGDRGQIGFPGGRGNP---GAPGKPGRSGSPGPKGQKGEKGSV-GGS 351
Cdd:COG5164  54 TTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAgdgGATGPPDDGGATGPPDDGGSTTPPsGGS 133


                ..
gi 74199399 352 RS 353
Cdd:COG5164 134 TT 135
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
135-259 3.37e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.23  E-value: 3.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199399 135 SKADLIDTGRFQNFSMatdQRLNDILLQLNSLILSVQEHGNSLDAISKSLQSLNMTLLDVQLHTETLHVRVRESTAKQQe 214
Cdd:COG3206 203 QKNGLVDLSEEAKLLL---QQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAE- 278

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 74199399 215 dISKLEERVYKVSAEVQSVKEEQAHVEQEVKQEV-RVLNNITNDLR 259
Cdd:COG3206 279 -LAELSARYTPNHPDVIALRAQIAALRAQLQQEAqRILASLEAELE 323
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 150-254 4.60e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 38.46  E-value: 4.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199399    150 MATDQRLNDILLQLNSLILSVQEHGNSLDAISKSLQSLNMTLLDVQlhTETLHVRVRESTAKQQEdISKLEERVYKVSAE 229
Cdd:smart00787 164 MKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRA--KEKLKKLLQEIMIKVKK-LEELEEELQELESK 240

                           90       100
                   ....*....|....*....|....*
gi 74199399    230 VQSVKEEQAHVEQEVKQEVRVLNNI 254
Cdd:smart00787 241 IEDLTNKKSELNTEIAEAEKKLEQC 265
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 328-350 6.36e-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: 6.36e-03
                          10        20
                  ....*....|....*....|...
gi 74199399   328 GKPGRSGSPGPKGQKGEKGSVGG 350
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGP 23
PTZ00146 PTZ00146
fibrillarin; Provisional
 283-348 6.45e-03

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 37.79  E-value: 6.45e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74199399  283 GEKGDRGltgqTGPPGAPGIRGipgvKGDRGQIGFPGGRGNPGAPGKPGRSGSPGPKGQKGEKGSV 348
Cdd:PTZ00146   1 GMGGGFG----GGRGGGRGGGG----GGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGGGGPGKVI 58
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH