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Conserved domains on  [gi|1720409164|ref|XP_030109492|]
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collagen alpha-1(XXVII) chain isoform X7 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COLFI super family cl02436
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 889-1087 2.71e-55

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.


The actual alignment was detected with superfamily member pfam01410:

Pssm-ID: 470578  Cd Length: 233  Bit Score: 191.79  E-value: 2.71e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  889 EIFKTLHYLSNLIQSIKTPLGTKENPARVCRDLMDCEQRMADGTYWVDPNLGCSSDTIEVSCNFTQGgQTCLKPITAS-- 966
Cdd:pfam01410    4 EVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFETG-ETCIYPTKASip 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  967 --------------------KAEF---------AVSRVQMNFLHLLSSEGTQHITIHCLNMTVWQEGPGrSSARQAVRFR 1017
Cdd:pfam01410   83 rknwwtkeskhvwfgefmngGSQFsygvdgvgpSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQAT-GNLKKALLLQ 161

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720409164 1018 AWNGQVFEAGG--QFRPEVSMDGCKVHDGRWHQTLFTFRTQDPQQLPIVSVdnlPPVSSGK---QYRLEVGPACF 1087
Cdd:pfam01410  162 GSNDEEIRAEGnsRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDI---APMDIGGadqEFGVEVGPVCF 233
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 555-780 1.40e-30

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: 126.17  E-value: 1.40e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  555 EKGDQGEDGktegPPGPPGDRGPVGDRGDRGEPGDPGYPGQEGVQGLRGEPGQQGQPGHPGPRGRPGPKGSKGEEGPKGK 634
Cdd:NF038329   118 EKGEPGPAG----PAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  635 PGKAGPSGRRGTQGLQGLPGPRGVVGRQGPEGTAGSDGiPGRDGRPGYQGDQGNDGDPGPVGPAGRRGNPGVAGLPGAQG 714
Cdd:NF038329   194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720409164  715 PPGFKGESGLPGQLGPPGKRGTEGGTGLPGNQGEPGSKGQPGDSGEMGFPGVAGLFGPKGPPGDIG 780
Cdd:NF038329   273 PDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 201-476 7.10e-29

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: 121.17  E-value: 7.10e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  201 LDGSKGEPGDPGRPGPVGEQGLMGFIGLVGEPGIVGEKGDRGvmgppgapgpkgsmghpgtpggignpgepgpwgPPGSR 280
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG---------------------------------ERGEK 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  281 GLPGMRGAKGHRGPRGPDGPAGEQGSKGLKGRVGPRGRPGQPGQQGAAGERGHSGAKGflgipgpsgppgAKGLPGEPGs 360
Cdd:NF038329   162 GPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAG------------PAGEDGPAG- 228

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  361 qgpqgpVGPPGEMGPKGPPGAVGEPGLPGDSGMKGDLGPLGPPGEQGLIGQRGEPGLEGDHGPVGPDGLKGDRGDPGPDG 440
Cdd:NF038329   229 ------PAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG 302

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1720409164  441 EHGEKGQEGLKGEDGSPGPPGITGVPGREGKPGKQG 476
Cdd:NF038329   303 KDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 50-335 8.38e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 90.73  E-value: 8.38e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164   50 GDTGALGPVGYPGPKGMKGLMGGVGEPGLKGDKGEQGVPGVSGDPGFQGDKGshglpglpggrgKPGPLGKAGDKgslgf 129
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG------------EAGPQGPAGKD----- 179

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  130 pgppgpegfpgdiGPPGDNGPEGMKGKPGARGLPGPPGQLGPEGDEGPMGPPGVPGLEGQPGRKGfPGRPGLDGSKGEPG 209
Cdd:NF038329   180 -------------GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTG 245

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  210 DPGRPGPVGEQGLMGFIGLVGEPGIVGEKGDRGvmgppgapgpkgsmghpgtpggignpgepgpwgPPGSRGLPGMRGAK 289
Cdd:NF038329   246 EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG---------------------------------ERGPVGPAGKDGQN 292

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1720409164  290 GHRGPRGPDGPAGEQGSKGLKGRVGPRGRPGQPGQQGAAGERGHSG 335
Cdd:NF038329   293 GKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 17-71 7.71e-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: 35.93  E-value: 7.71e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720409164   17 GFPGDFGERGPPGLDGNPGEIGLPGPPGVLGLIGDTGALGPVGYPGPKGMKGLMG 71
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 889-1087 2.71e-55

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: 191.79  E-value: 2.71e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  889 EIFKTLHYLSNLIQSIKTPLGTKENPARVCRDLMDCEQRMADGTYWVDPNLGCSSDTIEVSCNFTQGgQTCLKPITAS-- 966
Cdd:pfam01410    4 EVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFETG-ETCIYPTKASip 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  967 --------------------KAEF---------AVSRVQMNFLHLLSSEGTQHITIHCLNMTVWQEGPGrSSARQAVRFR 1017
Cdd:pfam01410   83 rknwwtkeskhvwfgefmngGSQFsygvdgvgpSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQAT-GNLKKALLLQ 161

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720409164 1018 AWNGQVFEAGG--QFRPEVSMDGCKVHDGRWHQTLFTFRTQDPQQLPIVSVdnlPPVSSGK---QYRLEVGPACF 1087
Cdd:pfam01410  162 GSNDEEIRAEGnsRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDI---APMDIGGadqEFGVEVGPVCF 233
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 888-1088 2.34e-52

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: 183.44  E-value: 2.34e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164   888 GEIFKTLHYLSNLIQSIKTPLGTKENPARVCRDLMDCEQRMADGTYWVDPNLGCSSDTIEVSCNFTqGGQTCLKPITASK 967
Cdd:smart00038    2 EEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFE-TGETCVSPSPSSI 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164   968 A----------------------EFA--------VSRVQMNFLHLLSSEGTQHITIHCLNMTVWQEgPGRSSARQAVRFR 1017
Cdd:smart00038   81 PrktwysgkskhvwfgetmnggfKFSygdsegppVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMD-EATGNLKKALRLR 159

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720409164  1018 AWNGQVFEAGGQFRP--EVSMDGCKVHDGRWHQTLFTFRTQDPQQLPIVsvdNLPPVSSGKQYR---LEVGPACFL 1088
Cdd:smart00038  160 GSNDVELSAEGNSKFtyEVLEDGCQKRTGKWGKTVIEYRTKKTERLPIV---DIAPSDIGGPDQefgVEIGPVCFS 232
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 555-780 1.40e-30

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: 126.17  E-value: 1.40e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  555 EKGDQGEDGktegPPGPPGDRGPVGDRGDRGEPGDPGYPGQEGVQGLRGEPGQQGQPGHPGPRGRPGPKGSKGEEGPKGK 634
Cdd:NF038329   118 EKGEPGPAG----PAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  635 PGKAGPSGRRGTQGLQGLPGPRGVVGRQGPEGTAGSDGiPGRDGRPGYQGDQGNDGDPGPVGPAGRRGNPGVAGLPGAQG 714
Cdd:NF038329   194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720409164  715 PPGFKGESGLPGQLGPPGKRGTEGGTGLPGNQGEPGSKGQPGDSGEMGFPGVAGLFGPKGPPGDIG 780
Cdd:NF038329   273 PDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 596-826 1.51e-30

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: 126.17  E-value: 1.51e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  596 EGVQGLRGEpGQQGQPGHPGPRGRPGPKGSKGEEGPKGKPGKAGPSGRRGTQGLQGLPGPRGVVGRQGPegtagsdgipg 675
Cdd:NF038329   108 EGLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP----------- 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  676 rdgrPGYQGDQGNDGDPGPVGPAGRRGNPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRGtEGGTGLPGNQGEPGSKGQP 755
Cdd:NF038329   176 ----AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQ 250

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720409164  756 GDSGEMGFPGVAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIIGPPGMLGPSGLPGPKGDRGSRGDLGL 826
Cdd:NF038329   251 GPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ 321
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 410-697 1.29e-29

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: 123.48  E-value: 1.29e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  410 GQRGEPGLEgdhGPVGPDGLKGDRGDPGPDGEHGEKGQEGLKGEDGSPGPPGITGVPGREGKPGKQGEKGQRGAKGAKGH 489
Cdd:NF038329   117 GEKGEPGPA---GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  490 QGYLGEmgipgepgppgtPGPKGSRGTLGPTGAPGRMGAQGEPGLAGYNGhkgitgplgppgpkgekgdqgedgktegpp 569
Cdd:NF038329   194 QGPRGE------------TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG------------------------------ 231

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  570 gppgdrgpvgdRGDRGEPGDPGYPGQEGVQGLRGEPGQQGQpghPGPRGRPGPKGSKGEEGPKGKPGKAGPSGRRGTQGL 649
Cdd:NF038329   232 -----------DGQQGPDGDPGPTGEDGPQGPDGPAGKDGP---RGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGL 297

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1720409164  650 QGLPGPRGVVGRQGPEGTAGSDGIPGRDGRPGYQGDQGNDGDPGPVGP 697
Cdd:NF038329   298 PGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 201-476 7.10e-29

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: 121.17  E-value: 7.10e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  201 LDGSKGEPGDPGRPGPVGEQGLMGFIGLVGEPGIVGEKGDRGvmgppgapgpkgsmghpgtpggignpgepgpwgPPGSR 280
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG---------------------------------ERGEK 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  281 GLPGMRGAKGHRGPRGPDGPAGEQGSKGLKGRVGPRGRPGQPGQQGAAGERGHSGAKGflgipgpsgppgAKGLPGEPGs 360
Cdd:NF038329   162 GPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAG------------PAGEDGPAG- 228

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  361 qgpqgpVGPPGEMGPKGPPGAVGEPGLPGDSGMKGDLGPLGPPGEQGLIGQRGEPGLEGDHGPVGPDGLKGDRGDPGPDG 440
Cdd:NF038329   229 ------PAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG 302

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1720409164  441 EHGEKGQEGLKGEDGSPGPPGITGVPGREGKPGKQG 476
Cdd:NF038329   303 KDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 275-491 3.59e-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: 116.16  E-value: 3.59e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  275 GPPGSRGLPGMRGAKGHRGPRGPDGPAGEQGSKGLKGRVGPRGRPGQPGQQGAAGERGHSGAKGFLGIPGPSGPPGAKGL 354
Cdd:NF038329   126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  355 PGEPGSQGPQGPVGPPGEMGPKGPPGA--VGEPGLPGDSGMKGDLGPLGPPGEQGLIGQRGEPglegdhGPVGPDGLKGD 432
Cdd:NF038329   206 QGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA------GPDGPDGKDGE 279

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720409164  433 RGDPGPDGEHGEKGQEGLKGEDGSPGPPGITGVPGREGKPGKQGEKGQRGAKGAKGHQG 491
Cdd:NF038329   280 RGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 50-335 8.38e-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: 90.73  E-value: 8.38e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164   50 GDTGALGPVGYPGPKGMKGLMGGVGEPGLKGDKGEQGVPGVSGDPGFQGDKGshglpglpggrgKPGPLGKAGDKgslgf 129
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG------------EAGPQGPAGKD----- 179

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  130 pgppgpegfpgdiGPPGDNGPEGMKGKPGARGLPGPPGQLGPEGDEGPMGPPGVPGLEGQPGRKGfPGRPGLDGSKGEPG 209
Cdd:NF038329   180 -------------GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTG 245

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  210 DPGRPGPVGEQGLMGFIGLVGEPGIVGEKGDRGvmgppgapgpkgsmghpgtpggignpgepgpwgPPGSRGLPGMRGAK 289
Cdd:NF038329   246 EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG---------------------------------ERGPVGPAGKDGQN 292

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1720409164  290 GHRGPRGPDGPAGEQGSKGLKGRVGPRGRPGQPGQQGAAGERGHSG 335
Cdd:NF038329   293 GKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 17-216 9.69e-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: 78.02  E-value: 9.69e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164   17 GFPGDFGERGPPGLDGNPGEIGLPGPPGVLGLIGDTGALGPVGYPGPKGMKGLMGGVGEPGLKGD--KGEQGVPGVSGDP 94
Cdd:NF038329   165 GPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagDGQQGPDGDPGPT 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164   95 GFQGDKGSHGLPGLPGGRGKPGPLGKAGDKgslgfpgppgpegfpgdiGPPGDNGPEGMKGKPGARGLPGPPGQLGPEGD 174
Cdd:NF038329   245 GEDGPQGPDGPAGKDGPRGDRGEAGPDGPD------------------GKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQ 306

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1720409164  175 EgpmgppGVPGLEGQPGRKGFPGRPGLDGSKGEPGDPGRPGP 216
Cdd:NF038329   307 N------GKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 727-827 9.16e-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: 9.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  727 QLGPPGKRGTEGGTGLPGNQGEPGSKGQPGDSGEMGFPGVAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIIGPPGML 806
Cdd:NF038329   112 QLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK 191

                           90       100
                   ....*....|....*....|.
gi 1720409164  807 GPSGLPGPKGDRGSRGDLGLQ 827
Cdd:NF038329   192 GPQGPRGETGPAGEQGPAGPA 212
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 284-338 1.97e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.87  E-value: 1.97e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720409164  284 GMRGAKGHRGPRGPDGPAGEQGSKGLKGRVGPRGRPGQPGQQGAAGERGHSGAKG 338
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 600-656 4.71e-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: 4.71e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720409164  600 GLRGEPGQQGQPGHPGPRGRPGPKGSKGEEGPKGKPGKAGPSGRRGTQGLQGLPGPR 656
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
651-825 5.49e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 46.95  E-value: 5.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  651 GLPGPRGVVGRQGPEGTAGSDGIPGRDGRPGYQGDQGNDGDPGPVGPAGRRGNPGVAGLPGAQGPPGFKGESGLPGQLGP 730
Cdd:COG5164     10 GPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGG 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  731 PGKRGTEGGTGLPGNQgepGSKGQPGDSGEMGFPGVAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIIGPPGMLGPSG 810
Cdd:COG5164     90 TRPAGNTGGTTPAGDG---GATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTT 166

                          170
                   ....*....|....*
gi 1720409164  811 LPGPKGDRGSRGDLG 825
Cdd:COG5164    167 PPGPGGSTTPPDDGG 181
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 603-792 3.66e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.59  E-value: 3.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  603 GEPGQQGQPGHPGPRGRPGPKGS---KGEEGPKGKPGKAGPSGRRGTQGLQGLPGPRGVVGRQGPEGTAGSDGIPGRDGR 679
Cdd:PRK07764   590 PAPGAAGGEGPPAPASSGPPEEAarpAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  680 PGYQGDQGNDGDPGPVGPAGRRGNPGVAGLPGAQGPPGfkgesglpgqlgPPGKRGTEGGTGLPGNQGEPGSKGQPGDSG 759
Cdd:PRK07764   670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAA------------TPPAGQADDPAAQPPQAAQGASAPSPAADD 737

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1720409164  760 EMGFPGVAGLF-GPKGPPGDIGFKGIQGPRGPPG 792
Cdd:PRK07764   738 PVPLPPEPDDPpDPAGAPAQPPPPPAPAPAAAPA 771
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
114-329 1.03e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 43.09  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  114 KPGPLGKAGDKGSLGFPGPPGPEGFPGDIGPPGDNGPEGMKGKPGARGLPGPPGQLGPEGDEGPMGPPGVPGLEGQPGRK 193
Cdd:COG5164      8 KTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQ 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  194 GFPGRPGLDGSKGEPGDPGRPGPVGEQGLMGFIGLVG-----EPGIVGEKGDRGVMGPPGAPGPKGSMGHPGTPGGIGNP 268
Cdd:COG5164     88 GGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGsttppSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTP 167

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720409164  269 GEPGPWGPPGSRGLPGMRGAKGHRGPRGPDGPAGEQGSKGLKGRVGPRGRPGQPGQQGAAG 329
Cdd:COG5164    168 PGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKT 228
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 143-217 2.23e-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: 37.09  E-value: 2.23e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720409164  143 GPPGDNGPEGMKGKPGARGLPGPPGQLGPegdegpmgppgvpglegqPGRKGFPGRPGLDGSKGEPGDPGRPGPV 217
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGP------------------PGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 17-71 7.71e-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: 35.93  E-value: 7.71e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720409164   17 GFPGDFGERGPPGLDGNPGEIGLPGPPGVLGLIGDTGALGPVGYPGPKGMKGLMG 71
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 27-101 8.88e-03

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 39.73  E-value: 8.88e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720409164   27 PPGLDGN-PGEIGLPGPPGVLGLIGDTGALGPVGYPG---PKGMKGLMGGVGEPGLKGDKGEQGVPGVSGDPGFQGDKG 101
Cdd:cd05922    277 PPERILEkPGSIGLAIPGGEFEILDDDGTPTPPGEPGeivHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDG 355
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 889-1087 2.71e-55

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: 191.79  E-value: 2.71e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  889 EIFKTLHYLSNLIQSIKTPLGTKENPARVCRDLMDCEQRMADGTYWVDPNLGCSSDTIEVSCNFTQGgQTCLKPITAS-- 966
Cdd:pfam01410    4 EVMATLKSLSQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCTRDAIKVFCNFETG-ETCIYPTKASip 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  967 --------------------KAEF---------AVSRVQMNFLHLLSSEGTQHITIHCLNMTVWQEGPGrSSARQAVRFR 1017
Cdd:pfam01410   83 rknwwtkeskhvwfgefmngGSQFsygvdgvgpSVAAVQLTFLRLLSTEASQNITYHCKNSVAYMDQAT-GNLKKALLLQ 161

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720409164 1018 AWNGQVFEAGG--QFRPEVSMDGCKVHDGRWHQTLFTFRTQDPQQLPIVSVdnlPPVSSGK---QYRLEVGPACF 1087
Cdd:pfam01410  162 GSNDEEIRAEGnsRFTYTVLEDGCTKRTGQWGKTVIEYRTQKVSRLPIVDI---APMDIGGadqEFGVEVGPVCF 233
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
 888-1088 2.34e-52

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: 183.44  E-value: 2.34e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164   888 GEIFKTLHYLSNLIQSIKTPLGTKENPARVCRDLMDCEQRMADGTYWVDPNLGCSSDTIEVSCNFTqGGQTCLKPITASK 967
Cdd:smart00038    2 EEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFE-TGETCVSPSPSSI 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164   968 A----------------------EFA--------VSRVQMNFLHLLSSEGTQHITIHCLNMTVWQEgPGRSSARQAVRFR 1017
Cdd:smart00038   81 PrktwysgkskhvwfgetmnggfKFSygdsegppVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMD-EATGNLKKALRLR 159

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720409164  1018 AWNGQVFEAGGQFRP--EVSMDGCKVHDGRWHQTLFTFRTQDPQQLPIVsvdNLPPVSSGKQYR---LEVGPACFL 1088
Cdd:smart00038  160 GSNDVELSAEGNSKFtyEVLEDGCQKRTGKWGKTVIEYRTKKTERLPIV---DIAPSDIGGPDQefgVEIGPVCFS 232
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 555-780 1.40e-30

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: 126.17  E-value: 1.40e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  555 EKGDQGEDGktegPPGPPGDRGPVGDRGDRGEPGDPGYPGQEGVQGLRGEPGQQGQPGHPGPRGRPGPKGSKGEEGPKGK 634
Cdd:NF038329   118 EKGEPGPAG----PAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  635 PGKAGPSGRRGTQGLQGLPGPRGVVGRQGPEGTAGSDGiPGRDGRPGYQGDQGNDGDPGPVGPAGRRGNPGVAGLPGAQG 714
Cdd:NF038329   194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720409164  715 PPGFKGESGLPGQLGPPGKRGTEGGTGLPGNQGEPGSKGQPGDSGEMGFPGVAGLFGPKGPPGDIG 780
Cdd:NF038329   273 PDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 596-826 1.51e-30

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: 126.17  E-value: 1.51e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  596 EGVQGLRGEpGQQGQPGHPGPRGRPGPKGSKGEEGPKGKPGKAGPSGRRGTQGLQGLPGPRGVVGRQGPegtagsdgipg 675
Cdd:NF038329   108 EGLQQLKGD-GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP----------- 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  676 rdgrPGYQGDQGNDGDPGPVGPAGRRGNPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRGtEGGTGLPGNQGEPGSKGQP 755
Cdd:NF038329   176 ----AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQ 250

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720409164  756 GDSGEMGFPGVAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIIGPPGMLGPSGLPGPKGDRGSRGDLGL 826
Cdd:NF038329   251 GPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ 321
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 410-697 1.29e-29

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: 123.48  E-value: 1.29e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  410 GQRGEPGLEgdhGPVGPDGLKGDRGDPGPDGEHGEKGQEGLKGEDGSPGPPGITGVPGREGKPGKQGEKGQRGAKGAKGH 489
Cdd:NF038329   117 GEKGEPGPA---GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  490 QGYLGEmgipgepgppgtPGPKGSRGTLGPTGAPGRMGAQGEPGLAGYNGhkgitgplgppgpkgekgdqgedgktegpp 569
Cdd:NF038329   194 QGPRGE------------TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG------------------------------ 231

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  570 gppgdrgpvgdRGDRGEPGDPGYPGQEGVQGLRGEPGQQGQpghPGPRGRPGPKGSKGEEGPKGKPGKAGPSGRRGTQGL 649
Cdd:NF038329   232 -----------DGQQGPDGDPGPTGEDGPQGPDGPAGKDGP---RGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGL 297

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1720409164  650 QGLPGPRGVVGRQGPEGTAGSDGIPGRDGRPGYQGDQGNDGDPGPVGP 697
Cdd:NF038329   298 PGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 201-476 7.10e-29

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: 121.17  E-value: 7.10e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  201 LDGSKGEPGDPGRPGPVGEQGLMGFIGLVGEPGIVGEKGDRGvmgppgapgpkgsmghpgtpggignpgepgpwgPPGSR 280
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG---------------------------------ERGEK 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  281 GLPGMRGAKGHRGPRGPDGPAGEQGSKGLKGRVGPRGRPGQPGQQGAAGERGHSGAKGflgipgpsgppgAKGLPGEPGs 360
Cdd:NF038329   162 GPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAG------------PAGEDGPAG- 228

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  361 qgpqgpVGPPGEMGPKGPPGAVGEPGLPGDSGMKGDLGPLGPPGEQGLIGQRGEPGLEGDHGPVGPDGLKGDRGDPGPDG 440
Cdd:NF038329   229 ------PAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG 302

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1720409164  441 EHGEKGQEGLKGEDGSPGPPGITGVPGREGKPGKQG 476
Cdd:NF038329   303 KDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 275-491 3.59e-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: 116.16  E-value: 3.59e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  275 GPPGSRGLPGMRGAKGHRGPRGPDGPAGEQGSKGLKGRVGPRGRPGQPGQQGAAGERGHSGAKGFLGIPGPSGPPGAKGL 354
Cdd:NF038329   126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  355 PGEPGSQGPQGPVGPPGEMGPKGPPGA--VGEPGLPGDSGMKGDLGPLGPPGEQGLIGQRGEPglegdhGPVGPDGLKGD 432
Cdd:NF038329   206 QGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA------GPDGPDGKDGE 279

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720409164  433 RGDPGPDGEHGEKGQEGLKGEDGSPGPPGITGVPGREGKPGKQGEKGQRGAKGAKGHQG 491
Cdd:NF038329   280 RGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 50-335 8.38e-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: 90.73  E-value: 8.38e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164   50 GDTGALGPVGYPGPKGMKGLMGGVGEPGLKGDKGEQGVPGVSGDPGFQGDKGshglpglpggrgKPGPLGKAGDKgslgf 129
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG------------EAGPQGPAGKD----- 179

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  130 pgppgpegfpgdiGPPGDNGPEGMKGKPGARGLPGPPGQLGPEGDEGPMGPPGVPGLEGQPGRKGfPGRPGLDGSKGEPG 209
Cdd:NF038329   180 -------------GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTG 245

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  210 DPGRPGPVGEQGLMGFIGLVGEPGIVGEKGDRGvmgppgapgpkgsmghpgtpggignpgepgpwgPPGSRGLPGMRGAK 289
Cdd:NF038329   246 EDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG---------------------------------ERGPVGPAGKDGQN 292

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1720409164  290 GHRGPRGPDGPAGEQGSKGLKGRVGPRGRPGQPGQQGAAGERGHSG 335
Cdd:NF038329   293 GKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 17-216 9.69e-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: 78.02  E-value: 9.69e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164   17 GFPGDFGERGPPGLDGNPGEIGLPGPPGVLGLIGDTGALGPVGYPGPKGMKGLMGGVGEPGLKGD--KGEQGVPGVSGDP 94
Cdd:NF038329   165 GPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPagDGQQGPDGDPGPT 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164   95 GFQGDKGSHGLPGLPGGRGKPGPLGKAGDKgslgfpgppgpegfpgdiGPPGDNGPEGMKGKPGARGLPGPPGQLGPEGD 174
Cdd:NF038329   245 GEDGPQGPDGPAGKDGPRGDRGEAGPDGPD------------------GKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQ 306

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1720409164  175 EgpmgppGVPGLEGQPGRKGFPGRPGLDGSKGEPGDPGRPGP 216
Cdd:NF038329   307 N------GKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 727-827 9.16e-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: 9.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  727 QLGPPGKRGTEGGTGLPGNQGEPGSKGQPGDSGEMGFPGVAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIIGPPGML 806
Cdd:NF038329   112 QLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK 191

                           90       100
                   ....*....|....*....|.
gi 1720409164  807 GPSGLPGPKGDRGSRGDLGLQ 827
Cdd:NF038329   192 GPQGPRGETGPAGEQGPAGPA 212
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 284-338 1.97e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.87  E-value: 1.97e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720409164  284 GMRGAKGHRGPRGPDGPAGEQGSKGLKGRVGPRGRPGQPGQQGAAGERGHSGAKG 338
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 600-656 4.71e-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: 4.71e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720409164  600 GLRGEPGQQGQPGHPGPRGRPGPKGSKGEEGPKGKPGKAGPSGRRGTQGLQGLPGPR 656
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
651-825 5.49e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 46.95  E-value: 5.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  651 GLPGPRGVVGRQGPEGTAGSDGIPGRDGRPGYQGDQGNDGDPGPVGPAGRRGNPGVAGLPGAQGPPGFKGESGLPGQLGP 730
Cdd:COG5164     10 GPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGG 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  731 PGKRGTEGGTGLPGNQgepGSKGQPGDSGEMGFPGVAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIIGPPGMLGPSG 810
Cdd:COG5164     90 TRPAGNTGGTTPAGDG---GATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTT 166

                          170
                   ....*....|....*
gi 1720409164  811 LPGPKGDRGSRGDLG 825
Cdd:COG5164    167 PPGPGGSTTPPDDGG 181
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 588-642 5.79e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.71  E-value: 5.79e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720409164  588 GDPGYPGQEGVQGLRGEPGQQGQPGHPGPRGRPGPKGSKGEEGPKGKPGKAGPSG 642
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 675-731 8.09e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.33  E-value: 8.09e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720409164  675 GRDGRPGYQGDQGNDGDPGPVGPAGRRGNPGVAGLPGAQGPPGFKGESGLPGQLGPP 731
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 603-657 9.85e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.94  E-value: 9.85e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720409164  603 GEPGQQGQPGHPGPRGRPGPKGSKGEEGPKGKPGKAGPSGRRGTQGLQGLPGPRG 657
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 612-666 1.02e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.94  E-value: 1.02e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720409164  612 GHPGPRGRPGPKGSKGEEGPKGKPGKAGPSGRRGTQGLQGLPGPRGVVGRQGPEG 666
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 609-664 1.16e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.94  E-value: 1.16e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720409164  609 GQPGHPGPRGRPGPKGSKGEEGPKGKPGKAGPSGRRGTQGLQGLPGPRGVVGRQGP 664
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 663-717 1.20e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.94  E-value: 1.20e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720409164  663 GPEGTAGSDGIPGRDGRPGYQGDQGNDGDPGPVGPAGRRGNPGVAGLPGAQGPPG 717
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
669-825 1.41e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 45.79  E-value: 1.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  669 GSDGIPGRDGRPGYQGDQGNDGDPGPVG---PAGRRGNPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRGTEGGTGLPGN 745
Cdd:COG5164      7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGstrPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  746 qgePGSKGQPGDSGEMGFPGVAGLFGPKGPPGDIGFKGIQGPRGPP--GLMGKEGIIGP----PGMLGPSGLPGPKGDRG 819
Cdd:COG5164     87 ---QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPsgGSTTPPGDGGStppgPGSTGPGGSTTPPGDGG 163


                   ....*.
gi 1720409164  820 SRGDLG 825
Cdd:COG5164    164 STTPPG 169
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 422-477 1.47e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 1.47e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720409164  422 GPVGPDGLKGDRGDPGPDGEHGEKGQEGLKGEDGSPGPPGITGVPGREGKPGKQGE 477
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 690-744 1.56e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 1.56e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720409164  690 GDPGPVGPAGRRGNPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRGTEGGTGLPG 744
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 729-783 2.10e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.17  E-value: 2.10e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720409164  729 GPPGKRGTEGGTGLPGNQGEPGSKGQPGDSGEMGFPGVAGLFGPKGPPGDIGFKG 783
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 708-762 2.29e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.17  E-value: 2.29e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720409164  708 GLPGAQGPPGFKGESGLPGQLGPPGKRGTEGGTGLPGNQGEPGSKGQPGDSGEMG 762
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 702-756 2.68e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 2.68e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720409164  702 GNPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRGTEGGTGLPGNQGEPGSKGQPG 756
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 603-792 3.66e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.59  E-value: 3.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  603 GEPGQQGQPGHPGPRGRPGPKGS---KGEEGPKGKPGKAGPSGRRGTQGLQGLPGPRGVVGRQGPEGTAGSDGIPGRDGR 679
Cdd:PRK07764   590 PAPGAAGGEGPPAPASSGPPEEAarpAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  680 PGYQGDQGNDGDPGPVGPAGRRGNPGVAGLPGAQGPPGfkgesglpgqlgPPGKRGTEGGTGLPGNQGEPGSKGQPGDSG 759
Cdd:PRK07764   670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAA------------TPPAGQADDPAAQPPQAAQGASAPSPAADD 737

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1720409164  760 EMGFPGVAGLF-GPKGPPGDIGFKGIQGPRGPPG 792
Cdd:PRK07764   738 PVPLPPEPDDPpDPAGAPAQPPPPPAPAPAAAPA 771
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 582-795 3.85e-04

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 44.61  E-value: 3.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  582 GDRGEPGDPGYPGQEGVQGLRGEPGQQGQPGHPGPrgrpgpkgskgEEGPKGKPGKAGPSGRRGTQGLQGlpGPRGVVGR 661
Cdd:pfam09606  178 GGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGP-----------ADAGAQMGQQAQANGGMNPQQMGG--APNQVAMQ 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  662 QGPEGTAGSDGIPGRDGRPGYQGDQGNDGDPGPVGPAGRRGNPGVAglPGAQGPPGFKGESGLPGQLGPPGKRGTEGGTG 741
Cdd:pfam09606  245 QQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQ--PGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNH 322

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720409164  742 LPGNQGEPGSKGQPGdsGEMGFPGVAGLFGPkGPPGDIGFKGIQGP-RGPPGLMG 795
Cdd:pfam09606  323 PAAHQQQMNQSVGQG--GQVVALGGLNHLET-WNPGNFGGLGANPMqRGQPGMMS 374
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 747-803 4.75e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.01  E-value: 4.75e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720409164  747 GEPGSKGQPGDSGEMGFPGVAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIIGPP 803
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 581-624 6.02e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.01  E-value: 6.02e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1720409164  581 RGDRGEPGDPGYPGQEGVQGLRGEPGQQGQPGHPGPRGRPGPKG 624
Cdd:pfam01391   12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 666-721 6.51e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.63  E-value: 6.51e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720409164  666 GTAGSDGIPGRDGRPGYQGDQGNDGDPGPVGPAGRRGNPGVAGLPGAQGPPGFKGE 721
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 398-460 7.77e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.63  E-value: 7.77e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720409164  398 GPLGPPGEQGLIGQRGEPGlegdhgPVGPDGLKGDRGDPGPDGEHGEKGQEGLKGEDGSPGPP 460
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPG------PPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 627-681 1.02e-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: 38.24  E-value: 1.02e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720409164  627 GEEGPKGKPGKAGPSGRRGTQGLQGLPGPRGVVGRQGPEGTAGSDGIPGRDGRPG 681
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
114-329 1.03e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 43.09  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  114 KPGPLGKAGDKGSLGFPGPPGPEGFPGDIGPPGDNGPEGMKGKPGARGLPGPPGQLGPEGDEGPMGPPGVPGLEGQPGRK 193
Cdd:COG5164      8 KTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQ 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  194 GFPGRPGLDGSKGEPGDPGRPGPVGEQGLMGFIGLVG-----EPGIVGEKGDRGVMGPPGAPGPKGSMGHPGTPGGIGNP 268
Cdd:COG5164     88 GGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGsttppSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTP 167

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720409164  269 GEPGPWGPPGSRGLPGMRGAKGHRGPRGPDGPAGEQGSKGLKGRVGPRGRPGQPGQQGAAG 329
Cdd:COG5164    168 PGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKT 228
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 591-645 1.03e-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: 38.24  E-value: 1.03e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720409164  591 GYPGQEGVQGLRGEPGQQGQPGHPGPRGRPGPKGSKGEEGPKGKPGKAGPSGRRG 645
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 383-438 1.12e-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: 38.24  E-value: 1.12e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720409164  383 GEPGLPGDSGMKGDLGPLGPPGEQGLIGQRGEPGLEGDHGPVGPDGLKGDRGDPGP 438
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 618-672 1.25e-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: 37.86  E-value: 1.25e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720409164  618 GRPGPKGSKGEEGPKGKPGKAGPSGRRGTQGLQGLPGPRGVVGRQGPEGTAGSDG 672
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
419-718 1.27e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 42.71  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  419 GDHGPVGPDGLKGDRGDPGPDGEHGEKGQEGLKGEDGSPGPPGITGVPGREGKPGKQGEKGQRGAKGAKGHQGYLGEMGI 498
Cdd:COG5164      7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  499 PGEPGPPGTPGPKGSRGTLGPTGAPGRMGAQGEPGLAGYNGHKGiTGPLGPPgpkgekGDQGEDGKTEGPPGPPGDRGPV 578
Cdd:COG5164     87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPS-GGSTTPP------GDGGSTPPGPGSTGPGGSTTPP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  579 GDRGDRGEPGDPGYPGQEGVQGlRGEPGQQGQPGHPGPRGRPGPKGSKGEEGPKGKPGKAGPSGRRGtqGLQGLPGPRGV 658
Cdd:COG5164    160 GDGGSTTPPGPGGSTTPPDDGG-STTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG--GKTGPKDQRPK 236

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720409164  659 VGRQGPEGTAGSDGIPGRDGRPGYQGDQ--GNDGDPGPVGPAGRRGNPGVAGLPGAQGPPGF 718
Cdd:COG5164    237 TNPIERRGPERPEAAALPAELTALEAENraANPEPATKTIPETTTVKDLATVLGKKGSDLVT 298
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 639-695 1.39e-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: 37.86  E-value: 1.39e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720409164  639 GPSGRRGTQGLQGLPGPRGVVGRQGPEGTAGSDGIPGRDGRPGYQGDQGNDGDPGPV 695
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 585-777 1.67e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.67  E-value: 1.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  585 GEPGDPGYPGQEGVQGlRGEPGQQGQPGHPG-PRGRPGPKGSkgeegpkgkPGKAGPSGRRGTQGLQGLPGPRGVVGRQG 663
Cdd:PRK07764   590 PAPGAAGGEGPPAPAS-SGPPEEAARPAAPAaPAAPAAPAPA---------GAAAAPAEASAAPAPGVAAPEHHPKHVAV 659

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  664 PEGTAGSDGIPGRDGRPGYQGDQGNDGDPGPVGPAGRRGNPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRGTEGGTGLP 743
Cdd:PRK07764   660 PDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPV 739

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1720409164  744 GNQGEPGSKGQPGDSGEMGfPGVAGLFGPKGPPG 777
Cdd:PRK07764   740 PLPPEPDDPPDPAGAPAQP-PPPPAPAPAAAPAA 772
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 621-675 1.76e-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: 37.47  E-value: 1.76e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720409164  621 GPKGSKGEEGPKGKPGKAGPSGRRGTQGLQGLPGPRGVVGRQGPEGTAGSDGIPG 675
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 581-705 1.89e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 42.20  E-value: 1.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  581 RGDRGEPGDPGYPGQEGVQGLRGEPGQQGQPGHPGPRGRPGPKGSKGEEGPKGKPGKAGPSGRRGTQGLQGlpgPRGVVG 660
Cdd:PRK12678   112 AAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQ---AEAERG 188

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1720409164  661 RQGPEGTAGSDGIPGRDGRPGYQGDQGNDGDPGPVGpaGRRGNPG 705
Cdd:PRK12678   189 ERGRREERGRDGDDRDRRDRREQGDRREERGRRDGG--DRRGRRR 231
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 738-792 2.16e-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: 37.47  E-value: 2.16e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720409164  738 GGTGLPGNQGEPGSKGQPGDSGEMGFPGVAGLFGPKGPPGDIGFKGIQGPRGPPG 792
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 143-217 2.23e-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: 37.09  E-value: 2.23e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720409164  143 GPPGDNGPEGMKGKPGARGLPGPPGQLGPegdegpmgppgvpglegqPGRKGFPGRPGLDGSKGEPGDPGRPGPV 217
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGP------------------PGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 431-486 2.74e-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: 37.09  E-value: 2.74e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720409164  431 GDRGDPGPDGEHGEKGQEGLKGEDGSPGPPGITGVPGREGKPGKQGEKGQRGAKGA 486
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 434-488 4.31e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.32  E-value: 4.31e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720409164  434 GDPGPDGEHGEKGQEGLKGEDGSPGPPGITGVPGREGKPGKQGEKGQRGAKGAKG 488
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 624-680 4.80e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.32  E-value: 4.80e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720409164  624 GSKGEEGPKGKPGKAGPSGRRGTQGLQGLPGPRGVVGRQGPEGTAGSDGIPGRDGRP 680
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
208-472 5.28e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 40.78  E-value: 5.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  208 PGDPGRPGPVGEQGLMGFIGLVGEPGIVGEKGDRGVMGPPGAPGPKGSMGHPGTPGGignpgePGPWGPPGSRGLPGMRG 287
Cdd:COG5164      6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGG------TRPAGNQGATGPAQNQG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  288 AKGHRGPRGPDGPAGEQGSKGlkgRVGPRGRPGQPGQQGAAGERGHSGAKGFLGIPGPSGPPGAKGLPGEPGSQGPQGPV 367
Cdd:COG5164     80 GTTPAQNQGGTRPAGNTGGTT---PAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGST 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  368 GPPGEMGPKGPPGAVGEPGLPGD--SGMKGDLGPLGPPGEQGLIGQRGEPGLEGDHGPVGPDGLKGDR-GDPGPDGEHGE 444
Cdd:COG5164    157 TPPGDGGSTTPPGPGGSTTPPDDggSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRgGKTGPKDQRPK 236

                          250       260
                   ....*....|....*....|....*...
gi 1720409164  445 KGQEGLKGEDGSPGPPGITGVPGREGKP 472
Cdd:COG5164    237 TNPIERRGPERPEAAALPAELTALEAEN 264
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 280-328 5.74e-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: 35.93  E-value: 5.74e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1720409164  280 RGLPGMRGAKGHRGPRGPDGPAGEQGSKGLKGRVGPRGRPGQPGQQGAA 328
Cdd:pfam01391    9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 374-424 5.74e-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: 35.93  E-value: 5.74e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720409164  374 GPKGPPGAVGEPGLPGDSGMKGDLGPLGPPGEQGLIGQRGEPGLEGDHGPV 424
Cdd:pfam01391    7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 648-704 6.33e-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: 35.93  E-value: 6.33e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720409164  648 GLQGLPGPRGVVGRQGPEGTAGSDGIPGRDGRPGYQGDQGNDGDPGPVGPAGRRGNP 704
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 654-710 6.52e-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: 35.93  E-value: 6.52e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720409164  654 GPRGVVGRQGPEGTAGSDGIPGRDGRPGYQGDQGNDGDPGPVGPAGRRGNPGVAGLP 710
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 17-71 7.71e-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: 35.93  E-value: 7.71e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720409164   17 GFPGDFGERGPPGLDGNPGEIGLPGPPGVLGLIGDTGALGPVGYPGPKGMKGLMG 71
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 27-101 8.88e-03

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 39.73  E-value: 8.88e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720409164   27 PPGLDGN-PGEIGLPGPPGVLGLIGDTGALGPVGYPG---PKGMKGLMGGVGEPGLKGDKGEQGVPGVSGDPGFQGDKG 101
Cdd:cd05922    277 PPERILEkPGSIGLAIPGGEFEILDDDGTPTPPGEPGeivHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDG 355
PHA03169 PHA03169
hypothetical protein; Provisional
 555-699 9.85e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 39.57  E-value: 9.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409164  555 EKGDQGEDGKTEGPPGPPGDRGPVGDRGDRGEPGDPGYPGQEGVQGLRGEPGQQGQPGHPGPrGRPGPKGSKGEEGPKGK 634
Cdd:PHA03169    85 EERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGP-HEPAPPESHNPSPNQQP 163

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720409164  635 PGKAGPSGRRGTQ---GLQGLPGPRGVVGRQGPEGTAGSDGIPGRDGRPGYQGDQGNDGDPGPVGPAG 699
Cdd:PHA03169   164 SSFLQPSHEDSPEepePPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAV 231
 
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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