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Conserved domains on  [gi|15149946|emb|CAC51021|]
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procollagen type I alpha 1 chain, partial [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 244-480 1.55e-165

Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1 alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.


:

Pssm-ID: 460199  Cd Length: 233  Bit Score: 466.43  E-value: 1.55e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149946   244 RDLEVDTTLKSLSQQIESIISPDGTKKNPARTCRDLKMCHPDWKSGEYWIDPDQGCNQDAIKVYCNMETGETCVNPTESA 323
Cdd:pfam01410   1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFETGETCIYPTKAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149946   324 IPKKNWYTskniKEKKHVWFGEAMTDGFQFEYGSEGSKPEDVNIQLTFLRLMSTEASQNITYHCKNSIAYMDQASGNLKK 403
Cdd:pfam01410  81 IPRKNWWT----KESKHVWFGEFMNGGSQFSYGVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKK 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15149946   404 ALLLQGSNEIEIRAEGNSRFTYSVTEDGCTSHTGAWGKTVIDYKTTKTSRLPIIDIAPMDVGAPNQEFGIEVGPVCF 480
Cdd:pfam01410 157 ALLLQGSNDEEIRAEGNSRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 34-172 3.03e-21

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: 95.74  E-value: 3.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149946   34 GTPGNEGSAGRDGAAGPKGDRGETGPSGTPGAPGPPgaagpigpagktGDRGETGPAGVPGPAGPSGPRGPSGPAGARGD 113
Cdd:NF038329 120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQ------------GERGEKGPAGPQGEAGPQGPAGKDGEAGAKGP 187

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15149946  114 KGETGEAGERGMKGHRGFTGMPGPPGPPGPSGESGPAGASGPA--------GPRGPAGSAGSAGKDG 172
Cdd:NF038329 188 AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgdgqqgpdGDPGPTGEDGPQGPDG 254
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 244-480 1.55e-165

Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1 alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.


Pssm-ID: 460199  Cd Length: 233  Bit Score: 466.43  E-value: 1.55e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149946   244 RDLEVDTTLKSLSQQIESIISPDGTKKNPARTCRDLKMCHPDWKSGEYWIDPDQGCNQDAIKVYCNMETGETCVNPTESA 323
Cdd:pfam01410   1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFETGETCIYPTKAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149946   324 IPKKNWYTskniKEKKHVWFGEAMTDGFQFEYGSEGSKPEDVNIQLTFLRLMSTEASQNITYHCKNSIAYMDQASGNLKK 403
Cdd:pfam01410  81 IPRKNWWT----KESKHVWFGEFMNGGSQFSYGVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKK 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15149946   404 ALLLQGSNEIEIRAEGNSRFTYSVTEDGCTSHTGAWGKTVIDYKTTKTSRLPIIDIAPMDVGAPNQEFGIEVGPVCF 480
Cdd:pfam01410 157 ALLLQGSNDEEIRAEGNSRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 245-481 3.09e-148

Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.


Pssm-ID: 197483  Cd Length: 232  Bit Score: 422.26  E-value: 3.09e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149946    245 DLEVDTTLKSLSQQIESIISPDGTKKNPARTCRDLKMCHPDWKSGEYWIDPDQGCNQDAIKVYCNMETGETCVNPTESAI 324
Cdd:smart00038   1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFETGETCVSPSPSSI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149946    325 PKKNWYTSKNikekKHVWFGEAMTDGFQFEYGsEGSKPEDVNIQLTFLRLMSTEASQNITYHCKNSIAYMDQASGNLKKA 404
Cdd:smart00038  81 PRKTWYSGKS----KHVWFGETMNGGFKFSYG-DSEGPPVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKA 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15149946    405 LLLQGSNEIEIRAEGNSRFTYSVTEDGCTSHTGAWGKTVIDYKTTKTSRLPIIDIAPMDVGAPNQEFGIEVGPVCFL 481
Cdd:smart00038 156 LRLRGSNDVELSAEGNSKFTYEVLEDGCQKRTGKWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 34-172 3.03e-21

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: 95.74  E-value: 3.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149946   34 GTPGNEGSAGRDGAAGPKGDRGETGPSGTPGAPGPPgaagpigpagktGDRGETGPAGVPGPAGPSGPRGPSGPAGARGD 113
Cdd:NF038329 120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQ------------GERGEKGPAGPQGEAGPQGPAGKDGEAGAKGP 187

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15149946  114 KGETGEAGERGMKGHRGFTGMPGPPGPPGPSGESGPAGASGPA--------GPRGPAGSAGSAGKDG 172
Cdd:NF038329 188 AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgdgqqgpdGDPGPTGEDGPQGPDG 254
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1-173 4.12e-19

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 89.58  E-value: 4.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149946    1 GKQGPSGPSGERGPPGPMGPPGLAGPPGEPGREGTPGNEGSAGRDGAAGPKGDRGETGPSGTPGAPGPPGAAGPIGPAGK 80
Cdd:NF038329 135 GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGP 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149946   81 TGDRGETGPAGVPGPAG--PSGPRGPSGPAGARGDKGETGEAGERGMKGHRGFTgmpgppgppgpsGESGPAGASGPAGP 158
Cdd:NF038329 215 DGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA------------GPDGPDGKDGERGP 282

                        170
                 ....*....|....*
gi 15149946  159 RGPAGSAGSAGKDGM 173
Cdd:NF038329 283 VGPAGKDGQNGKDGL 297
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1-172 5.98e-16

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 79.95  E-value: 5.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149946    1 GKQGPSGPSGERGPPGPMGPPGLAGPPGEPGREGTPGNEGSAGRDGAAGPKGDRGETGPSGTPGAPGPPGAAGPIGPAGK 80
Cdd:NF038329 162 GPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDP 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149946   81 --TGDRGETGPAGVPGPAGPSGPRGPSGPAGARGDKGETGEAGERGMKGHRGftgmpgppgppgpsgesgPAGASGPAGP 158
Cdd:NF038329 242 gpTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG------------------KDGLPGKDGK 303

                        170
                 ....*....|....
gi 15149946  159 RGPAGSAGSAGKDG 172
Cdd:NF038329 304 DGQNGKDGLPGKDG 317
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 82-172 7.62e-16

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 79.56  E-value: 7.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149946   82 GDRGETGPAGVPGPAGPSGPRGPSGPAGARGDKGETGEAGERGMKGHRGFTGMPGPPGPPGPSGESGPAGASGPAGPRGP 161
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90
                 ....*....|.
gi 15149946  162 AGSAGSAGKDG 172
Cdd:NF038329 197 RGETGPAGEQG 207
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 100-170 1.39e-08

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 50.96  E-value: 1.39e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15149946   100 GPRGPSGPAGARGDKGETGEAGERGMKGHRGFtgmpgppgppgpsgesgpagaSGPAGPRGPAGSAGSAGK 170
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGE---------------------PGPPGPPGPPGPPGPPGA 50
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 275-312 3.30e-07

fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, describes a conserved domain found in eukaryotic proteins such as fibrinogen beta and gamma chains, fincolin, and angiopoietin. This model describes a small homology domain, about 46 amino acids long, found in the PF00147 homology region of those proteins but also as a much shorter homology domain in bacterial proteins that may lack homology to those proteins, or to each other, outside this region. The signature motif, at the C-terminus of this domain, is YCDxTTDGGGWxLV.


Pssm-ID: 468872 [Multi-domain]  Cd Length: 46  Bit Score: 46.79  E-value: 3.30e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 15149946  275 TCRDLKMCHPDWKSGEYWIDPDQGCNQDAIKVYCNMET 312
Cdd:NF040941   1 SCWEILQAGPSAPSGVYWIDPDGMGGLAPFQVYCDMTT 38
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
34-172 5.83e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 45.41  E-value: 5.83e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149946  34 GTPGNEGSAGRDGAAGPKGDRGETGPSGTPGAPGPPGAAGPIGPAGKTG------DRGETGPAGVPG---PAGPSGPRGP 104
Cdd:COG5164  22 GSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGatgpaqNQGGTTPAQNQGgtrPAGNTGGTTP 101

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15149946 105 SGPAGARGDKGETGEAGERGMKGHRGFTGMPGPPGPPGPSGESGPAGASGPAGPRGPAGSAGSAGKDG 172
Cdd:COG5164 102 AGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPG 169
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 244-480 1.55e-165

Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1 alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.


Pssm-ID: 460199  Cd Length: 233  Bit Score: 466.43  E-value: 1.55e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149946   244 RDLEVDTTLKSLSQQIESIISPDGTKKNPARTCRDLKMCHPDWKSGEYWIDPDQGCNQDAIKVYCNMETGETCVNPTESA 323
Cdd:pfam01410   1 RDEEVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFETGETCIYPTKAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149946   324 IPKKNWYTskniKEKKHVWFGEAMTDGFQFEYGSEGSKPEDVNIQLTFLRLMSTEASQNITYHCKNSIAYMDQASGNLKK 403
Cdd:pfam01410  81 IPRKNWWT----KESKHVWFGEFMNGGSQFSYGVDGVGPSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKK 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15149946   404 ALLLQGSNEIEIRAEGNSRFTYSVTEDGCTSHTGAWGKTVIDYKTTKTSRLPIIDIAPMDVGAPNQEFGIEVGPVCF 480
Cdd:pfam01410 157 ALLLQGSNDEEIRAEGNSRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDIAPMDIGGADQEFGVEVGPVCF 233
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 245-481 3.09e-148

Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.


Pssm-ID: 197483  Cd Length: 232  Bit Score: 422.26  E-value: 3.09e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149946    245 DLEVDTTLKSLSQQIESIISPDGTKKNPARTCRDLKMCHPDWKSGEYWIDPDQGCNQDAIKVYCNMETGETCVNPTESAI 324
Cdd:smart00038   1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFETGETCVSPSPSSI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149946    325 PKKNWYTSKNikekKHVWFGEAMTDGFQFEYGsEGSKPEDVNIQLTFLRLMSTEASQNITYHCKNSIAYMDQASGNLKKA 404
Cdd:smart00038  81 PRKTWYSGKS----KHVWFGETMNGGFKFSYG-DSEGPPVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKA 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15149946    405 LLLQGSNEIEIRAEGNSRFTYSVTEDGCTSHTGAWGKTVIDYKTTKTSRLPIIDIAPMDVGAPNQEFGIEVGPVCFL 481
Cdd:smart00038 156 LRLRGSNDVELSAEGNSKFTYEVLEDGCQKRTGKWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 34-172 3.03e-21

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: 95.74  E-value: 3.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149946   34 GTPGNEGSAGRDGAAGPKGDRGETGPSGTPGAPGPPgaagpigpagktGDRGETGPAGVPGPAGPSGPRGPSGPAGARGD 113
Cdd:NF038329 120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQ------------GERGEKGPAGPQGEAGPQGPAGKDGEAGAKGP 187

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15149946  114 KGETGEAGERGMKGHRGFTGMPGPPGPPGPSGESGPAGASGPA--------GPRGPAGSAGSAGKDG 172
Cdd:NF038329 188 AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgdgqqgpdGDPGPTGEDGPQGPDG 254
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1-173 4.12e-19

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 89.58  E-value: 4.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149946    1 GKQGPSGPSGERGPPGPMGPPGLAGPPGEPGREGTPGNEGSAGRDGAAGPKGDRGETGPSGTPGAPGPPGAAGPIGPAGK 80
Cdd:NF038329 135 GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGP 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149946   81 TGDRGETGPAGVPGPAG--PSGPRGPSGPAGARGDKGETGEAGERGMKGHRGFTgmpgppgppgpsGESGPAGASGPAGP 158
Cdd:NF038329 215 DGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA------------GPDGPDGKDGERGP 282

                        170
                 ....*....|....*
gi 15149946  159 RGPAGSAGSAGKDGM 173
Cdd:NF038329 283 VGPAGKDGQNGKDGL 297
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 1-172 5.98e-16

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 79.95  E-value: 5.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149946    1 GKQGPSGPSGERGPPGPMGPPGLAGPPGEPGREGTPGNEGSAGRDGAAGPKGDRGETGPSGTPGAPGPPGAAGPIGPAGK 80
Cdd:NF038329 162 GPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDP 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149946   81 --TGDRGETGPAGVPGPAGPSGPRGPSGPAGARGDKGETGEAGERGMKGHRGftgmpgppgppgpsgesgPAGASGPAGP 158
Cdd:NF038329 242 gpTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNG------------------KDGLPGKDGK 303

                        170
                 ....*....|....
gi 15149946  159 RGPAGSAGSAGKDG 172
Cdd:NF038329 304 DGQNGKDGLPGKDG 317
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 82-172 7.62e-16

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 79.56  E-value: 7.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149946   82 GDRGETGPAGVPGPAGPSGPRGPSGPAGARGDKGETGEAGERGMKGHRGFTGMPGPPGPPGPSGESGPAGASGPAGPRGP 161
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90
                 ....*....|.
gi 15149946  162 AGSAGSAGKDG 172
Cdd:NF038329 197 RGETGPAGEQG 207
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 100-170 1.39e-08

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 50.96  E-value: 1.39e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15149946   100 GPRGPSGPAGARGDKGETGEAGERGMKGHRGFtgmpgppgppgpsgesgpagaSGPAGPRGPAGSAGSAGK 170
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGE---------------------PGPPGPPGPPGPPGPPGA 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 88-168 1.96e-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: 1.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149946    88 GPAGVPGPAGPSGPRGPSGPAGARGDKGETGEAGERGMKGHrgftgmpgppgppgpsgesgpagaSGPAGPRGPAGSAGS 167
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGP------------------------PGPPGPPGAPGAPGP 56


                  .
gi 15149946   168 A 168
Cdd:pfam01391  57 P 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 40-123 3.14e-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: 49.80  E-value: 3.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149946    40 GSAGRDGAAGPKGDRGETgpsgtpgapgppgaagpigpagktgdrGETGPAGVPGPAGPSGPRGPSGPAGARGDKGETGE 119
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPP---------------------------GPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGA 53


                  ....
gi 15149946   120 AGER 123
Cdd:pfam01391  54 PGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 46-124 1.49e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.87  E-value: 1.49e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15149946    46 GAAGPKGDRGEtgpsgtpgapgppgaagpigpagkTGDRGETGPAGVPGPAGPSGPRGPSGPAGARGDKGETGEAGERG 124
Cdd:pfam01391   1 GPPGPPGPPGP------------------------PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 275-312 3.30e-07

fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, describes a conserved domain found in eukaryotic proteins such as fibrinogen beta and gamma chains, fincolin, and angiopoietin. This model describes a small homology domain, about 46 amino acids long, found in the PF00147 homology region of those proteins but also as a much shorter homology domain in bacterial proteins that may lack homology to those proteins, or to each other, outside this region. The signature motif, at the C-terminus of this domain, is YCDxTTDGGGWxLV.


Pssm-ID: 468872 [Multi-domain]  Cd Length: 46  Bit Score: 46.79  E-value: 3.30e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 15149946  275 TCRDLKMCHPDWKSGEYWIDPDQGCNQDAIKVYCNMET 312
Cdd:NF040941   1 SCWEILQAGPSAPSGVYWIDPDGMGGLAPFQVYCDMTT 38
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
34-172 5.83e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 45.41  E-value: 5.83e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149946  34 GTPGNEGSAGRDGAAGPKGDRGETGPSGTPGAPGPPGAAGPIGPAGKTG------DRGETGPAGVPG---PAGPSGPRGP 104
Cdd:COG5164  22 GSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGatgpaqNQGGTTPAQNQGgtrPAGNTGGTTP 101

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15149946 105 SGPAGARGDKGETGEAGERGMKGHRGFTGMPGPPGPPGPSGESGPAGASGPAGPRGPAGSAGSAGKDG 172
Cdd:COG5164 102 AGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPG 169
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
36-172 7.23e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 38.86  E-value: 7.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149946  36 PGNEGSAGRDGAAGPKGDRGETGPSGTPGAPGPPgaagpigpagktGDRGETGPA---GVPGPAGPSGPRGPSGPAGARG 112
Cdd:COG5164   6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPA------------GNTGGTRPAqnqGSTTPAGNTGGTRPAGNQGATG 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15149946 113 DKGETGEAGERGMKGHRGftgmpgppgPPGPSGESGPAGASGPAGPRGPAGSAGSAGKDG 172
Cdd:COG5164  74 PAQNQGGTTPAQNQGGTR---------PAGNTGGTTPAGDGGATGPPDDGGATGPPDDGG 124
 
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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