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Conserved domains on  [gi|2564803972|ref|WP_306009337|]
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Gp37-like protein [Bacillus sp. MMSF_3328]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Sipho_Gp37 pfam14594
Siphovirus ReqiPepy6 Gp37-like protein; This family includes numerous phage proteins from ...
 18-342 2.62e-115

Siphovirus ReqiPepy6 Gp37-like protein; This family includes numerous phage proteins from Siphoviruses. The function of this protein is uncertain, but it is related to pfam06605. In Rhodococcus phage ReqiPepy6 this protein is called Gp37.


:

Pssm-ID: 434058  Cd Length: 336  Bit Score: 358.19  E-value: 2.62e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972   18 YTSLQYQPRWHKSGSFQLMIEGRV-NVSAFSKDHLLLFNNDHfKSAIISYAEYEVREDGQEVFVVQGSSLGSWLSQRITV 96
Cdd:pfam14594    2 YSSLTWTRRYSQPGTFELHLPATPeNADLLQEGNLIVLNDTE-KVGIIEHREITTDAEGGETLTVKGRDLKGLLARRIAW 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972   97 PPEGQAYHRLDASVETIMKEYVNLQAVNPVDPKRKITNLVISPDLERGSRTVYQTRFKQLDEELEKLSIASGLGWGIYLD 176
Cdd:pfam14594   81 PPPTAAGDVRSGTAETIMRALVNNNCINPADPARKIPNLTLGESQGRGPTVSKQARYDNLLDELESLCEASGLGFRVRLD 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  177 IENKRFVFDVFEGKDLSVSQSELSPVTFSIEFDNIKTQKYTDSGLGYKNYGYVAGQGEGAERSLVEVGNAEQTGVERYET 256
Cdd:pfam14594  161 LSTKKLIFEVYEGRDRTAGQTLNPPVIFSIEFENLTSQTYTLSAPNYKNVALVAGQGEGADREVVTVVGGEATGLDRREV 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  257 FIDARDIENEAD----------LPSRGEQKLSEFARVRSFENTILPYSSFVYGRDWNLGDIITIQNRKAGITENLRITEI 326
Cdd:pfam14594  241 FVDARDISEEAQtltdtdylaeLKERGKEKLAEYKAIESFESEVNDNGDLRYGRDYDLGDIVTVENKGWGITIDARITEV 320

                          330
                   ....*....|....*.
gi 2564803972  327 KEIYEPGGLNLEATFG 342
Cdd:pfam14594  321 EETYEQGGYTIEPTFG 336
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 412-706 1.53e-32

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: 131.95  E-value: 1.53e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  412 QGPQGIQGPQGPKGDRGV---QGQKGDTGAQGSQGAQGATGPEGPAGPKGDTGPQGIQGAKGDTGPIGPQGPKGATGSQG 488
Cdd:NF038329   125 AGPAGPAGEQGPRGDRGEtgpAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAG 204

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  489 PKGDTGLQGPQGVPGTQGPQGfgleytwdstklgvkredesayqyaeLKGEKGDAGpvgpmgppgssqsyvlferefnss 568
Cdd:NF038329   205 EQGPAGPAGPDGEAGPAGEDG--------------------------PAGPAGDGQ------------------------ 234

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  569 anqtvyswndgyvfpvgihavelyiNGDRQPsqsfkelpggngielladlpddqyllvsakmavvdlQGPQGEKGDTGPR 648
Cdd:NF038329   235 -------------------------QGPDGD------------------------------------PGPTGEDGPQGPD 253

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2564803972  649 GPIGLTGPKGEQGLQGPQGIKGDTGPAGPHGLTGSIGPKGDTGAQGPTGPIGPKGDKG 706
Cdd:NF038329   254 GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 635-821 2.71e-28

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: 119.24  E-value: 2.71e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  635 LQGPQGEKGDTGPRGPIGLTGPKGEQGLQGPQGIKGDTGPAGPHGLTGSIGPKGDTGAQGPTGPIGPKGDKGDsivwRGT 714
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGP----AGE 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  715 YSSSATYSVRDAVAYNGSSYILKALASAGtiptnTAYWDPLSIKGATGSQGPQGIQGAQGLQGETGPQGPIGLTGPKGDK 794
Cdd:NF038329   191 KGPQGPRGETGPAGEQGPAGPAGPDGEAG-----PAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDR 265

                          170       180
                   ....*....|....*....|....*..
gi 2564803972  795 GEKGDIGATGPQGIKGDTGPQGLKGDK 821
Cdd:NF038329   266 GEAGPDGPDGKDGERGPVGPAGKDGQN 292
pyocin_knob cd19958
knob domain of R1 and R2 pyocins and similar domains; The knob domain is present as a tandemly ...
 896-982 7.23e-05

knob domain of R1 and R2 pyocins and similar domains; The knob domain is present as a tandemly repeated structural domain in R-type pyocins, which are high-molecular weight bacteriocins produced by some strains of Pseudomonas aeruginosa to specifically kill other strains of the same species. R-type pyocins are structurally similar to simple contractile tails, such as those of phage P2 and Mu, and they punch a hole in the bacterial envelope to efficiently kill target cells. The second knob domain may contain regions responsible for determining the killing spectrum. Knob-like domains occur in host-recognition and binding proteins of, not only pyocins, but also phages, such as in phage K1F endosialidase (not represented by this model), where it may interact with sialic acid, the cell surface molecule that is recognized during infection.


:

Pssm-ID: 410997 [Multi-domain]  Cd Length: 80  Bit Score: 41.94  E-value: 7.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  896 DITYLGSYVKNADD---THSSYPVGvssmfvrsnegwfSYGTITTIKgySSGGGTLQIYTPYSSSyggdfikiRRW--NY 970
Cdd:cd19958     12 TLTTPGFYYQSANAnatTALNYPVA-------------GAGYLEVYR--YGGGGVTQIYTPYNSG--------RIYvrTR 68

                           90
                   ....*....|..
gi 2564803972  971 NATTWTDWETLI 982
Cdd:cd19958     69 YNGTWSAWKEIA 80
 
Name Accession Description Interval E-value
Sipho_Gp37 pfam14594
Siphovirus ReqiPepy6 Gp37-like protein; This family includes numerous phage proteins from ...
 18-342 2.62e-115

Siphovirus ReqiPepy6 Gp37-like protein; This family includes numerous phage proteins from Siphoviruses. The function of this protein is uncertain, but it is related to pfam06605. In Rhodococcus phage ReqiPepy6 this protein is called Gp37.


Pssm-ID: 434058  Cd Length: 336  Bit Score: 358.19  E-value: 2.62e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972   18 YTSLQYQPRWHKSGSFQLMIEGRV-NVSAFSKDHLLLFNNDHfKSAIISYAEYEVREDGQEVFVVQGSSLGSWLSQRITV 96
Cdd:pfam14594    2 YSSLTWTRRYSQPGTFELHLPATPeNADLLQEGNLIVLNDTE-KVGIIEHREITTDAEGGETLTVKGRDLKGLLARRIAW 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972   97 PPEGQAYHRLDASVETIMKEYVNLQAVNPVDPKRKITNLVISPDLERGSRTVYQTRFKQLDEELEKLSIASGLGWGIYLD 176
Cdd:pfam14594   81 PPPTAAGDVRSGTAETIMRALVNNNCINPADPARKIPNLTLGESQGRGPTVSKQARYDNLLDELESLCEASGLGFRVRLD 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  177 IENKRFVFDVFEGKDLSVSQSELSPVTFSIEFDNIKTQKYTDSGLGYKNYGYVAGQGEGAERSLVEVGNAEQTGVERYET 256
Cdd:pfam14594  161 LSTKKLIFEVYEGRDRTAGQTLNPPVIFSIEFENLTSQTYTLSAPNYKNVALVAGQGEGADREVVTVVGGEATGLDRREV 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  257 FIDARDIENEAD----------LPSRGEQKLSEFARVRSFENTILPYSSFVYGRDWNLGDIITIQNRKAGITENLRITEI 326
Cdd:pfam14594  241 FVDARDISEEAQtltdtdylaeLKERGKEKLAEYKAIESFESEVNDNGDLRYGRDYDLGDIVTVENKGWGITIDARITEV 320

                          330
                   ....*....|....*.
gi 2564803972  327 KEIYEPGGLNLEATFG 342
Cdd:pfam14594  321 EETYEQGGYTIEPTFG 336
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 412-706 1.53e-32

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: 131.95  E-value: 1.53e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  412 QGPQGIQGPQGPKGDRGV---QGQKGDTGAQGSQGAQGATGPEGPAGPKGDTGPQGIQGAKGDTGPIGPQGPKGATGSQG 488
Cdd:NF038329   125 AGPAGPAGEQGPRGDRGEtgpAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAG 204

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  489 PKGDTGLQGPQGVPGTQGPQGfgleytwdstklgvkredesayqyaeLKGEKGDAGpvgpmgppgssqsyvlferefnss 568
Cdd:NF038329   205 EQGPAGPAGPDGEAGPAGEDG--------------------------PAGPAGDGQ------------------------ 234

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  569 anqtvyswndgyvfpvgihavelyiNGDRQPsqsfkelpggngielladlpddqyllvsakmavvdlQGPQGEKGDTGPR 648
Cdd:NF038329   235 -------------------------QGPDGD------------------------------------PGPTGEDGPQGPD 253

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2564803972  649 GPIGLTGPKGEQGLQGPQGIKGDTGPAGPHGLTGSIGPKGDTGAQGPTGPIGPKGDKG 706
Cdd:NF038329   254 GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 635-821 2.71e-28

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: 119.24  E-value: 2.71e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  635 LQGPQGEKGDTGPRGPIGLTGPKGEQGLQGPQGIKGDTGPAGPHGLTGSIGPKGDTGAQGPTGPIGPKGDKGDsivwRGT 714
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGP----AGE 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  715 YSSSATYSVRDAVAYNGSSYILKALASAGtiptnTAYWDPLSIKGATGSQGPQGIQGAQGLQGETGPQGPIGLTGPKGDK 794
Cdd:NF038329   191 KGPQGPRGETGPAGEQGPAGPAGPDGEAG-----PAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDR 265

                          170       180
                   ....*....|....*....|....*..
gi 2564803972  795 GEKGDIGATGPQGIKGDTGPQGLKGDK 821
Cdd:NF038329   266 GEAGPDGPDGKDGERGPVGPAGKDGQN 292
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 636-819 1.50e-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: 116.93  E-value: 1.50e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  636 QGPQGEKGDTGPRGPIGLTGPKGEQGLQGPQGIKGDTGPAGPHGLTGSIGPKGDTGAQGPTGPIGPKGDKGDsivwRGTY 715
Cdd:NF038329   125 AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP----RGET 200

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  716 SSSATYSVRDAVAYNGssyilKALASAGTIPTNTAYWDPLSIKGATGSQGPQGIQGAQGLQGETGPQGPIGLTGPKGDKG 795
Cdd:NF038329   201 GPAGEQGPAGPAGPDG-----EAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                          170       180
                   ....*....|....*....|....
gi 2564803972  796 EKGDIGATGPQGIKGDTGPQGLKG 819
Cdd:NF038329   276 KDGERGPVGPAGKDGQNGKDGLPG 299
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
636-938 2.64e-15

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 80.07  E-value: 2.64e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  636 QGPQGEKGDTGPRGPIGLTGPKGEQGLQGPQGIKGDTGPAGPHGLT------GSIGPKGDTGAQGPTGPIGPKGDKGDSI 709
Cdd:COG5164     18 TTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTrpagnqGATGPAQNQGGTTPAQNQGGTRPAGNTG 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  710 VWRGTYSSSATYSVRDAVAYNGssyilkALASAGTIPTNTAYWDPLSIKGAT----GSQGPQGIQGAQGLQGETGPQGPI 785
Cdd:COG5164     98 GTTPAGDGGATGPPDDGGATGP------PDDGGSTTPPSGGSTTPPGDGGSTppgpGSTGPGGSTTPPGDGGSTTPPGPG 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  786 GLTGPKGDKGEK--GDIGATGPQGIKGDTGPQGLKGDKPAHQWTGTSlrfeNPDGTYGLSVDLKGEKGDKGDTGPQGPEG 863
Cdd:COG5164    172 GSTTPPDDGGSTtpPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKG----NPPDDRGGKTGPKDQRPKTNPIERRGPER 247

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2564803972  864 PPGAAVADSVEwaNVLNRPSNFPPSSHAHSTSDITYLGSYVKNADDTHSSYPVGVSSMFVRSNE-GWFSYGTITTI 938
Cdd:COG5164    248 PEAAALPAELT--ALEAENRAANPEPATKTIPETTTVKDLATVLGKKGSDLVTNLMKKGKGTNInAALDFETAATI 321
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
409-706 8.10e-15

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 78.53  E-value: 8.10e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  409 TNLQGPQGIQGPQGPKGDRGVQGQKGDTGAQGSQGAQGATGPEG------PAGPKGDTGPQGIQGAKGDTGPIGPQGPKG 482
Cdd:COG5164     15 GGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGntggtrPAGNQGATGPAQNQGGTTPAQNQGGTRPAG 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  483 ATGSQGPKGDTGLQGPQGVPGTQGPQGfgleytwdstklgvkredesayqyaelkgekgdagpvgpmgppgssqsyvlfe 562
Cdd:COG5164     95 NTGGTTPAGDGGATGPPDDGGATGPPD----------------------------------------------------- 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  563 refnssanqtvyswNDGYVFPVGIHAVELYINGDRQPSQSFKELPGGNgielladlpddqyllvsakmavvdlQGPQGEK 642
Cdd:COG5164    122 --------------DGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGS-------------------------TTPPGDG 162

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2564803972  643 GDTGPRGPIGLTGPKGEQGLQGPqGIKGDTGPAGPHGLTGSIGPKGDTGAQGPTGPIGPKGDKG 706
Cdd:COG5164    163 GSTTPPGPGGSTTPPDDGGSTTP-PNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG 225
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 412-506 1.14e-12

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 71.47  E-value: 1.14e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  412 QGPQGIQGPQGPKGDRGVQGQKGDTGAQGSQGAQGATGPEGPAGPKGDTGPQGIQGAKGDTGPIGPQGPKGATGSQGPKG 491
Cdd:NF038329   244 TGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323

                           90
                   ....*....|....*
gi 2564803972  492 DTGLQGPQGVPGTQG 506
Cdd:NF038329   324 KDGLPGKDGKDGQPG 338
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 452-507 5.05e-12

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: 61.74  E-value: 5.05e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2564803972  452 GPAGPKGDTGPQGIQGAKGDTGPIGPQGPKGATGSQGPKGDTGLQGPQGVPGTQGP 507
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 762-855 2.41e-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: 63.77  E-value: 2.41e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  762 GSQGPQGIQGAQGLQGETGPQGPIGLTGP---KGDKGEKGDIGATGPQGIKGDTGPQGLKGdkpahqwtgtslrfenPDG 838
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPagpAGPPGPQGERGEKGPAGPQGEAGPQGPAG----------------KDG 180

                           90
                   ....*....|....*..
gi 2564803972  839 TYGLSVDlKGEKGDKGD 855
Cdd:NF038329   181 EAGAKGP-AGEKGPQGP 196
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 765-819 4.93e-09

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: 53.27  E-value: 4.93e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2564803972  765 GPQGIQGAQGLQGETGPQGPIGLTGPKGDKGEKGDIGATGPQGIKGDTGPQGLKG 819
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 767-855 1.50e-08

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: 58.38  E-value: 1.50e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  767 QGIQGAQGlQGETGPQGPIGLTGPKGDKGEKGDIGATGPQGIKGDTGPQGLKGDKPAHQWTGtslrfenPDGTYGLSVDl 846
Cdd:NF038329   108 EGLQQLKG-DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG-------EAGPQGPAGK- 178


                   ....*....
gi 2564803972  847 KGEKGDKGD 855
Cdd:NF038329   179 DGEAGAKGP 187
pyocin_knob cd19958
knob domain of R1 and R2 pyocins and similar domains; The knob domain is present as a tandemly ...
 896-982 7.23e-05

knob domain of R1 and R2 pyocins and similar domains; The knob domain is present as a tandemly repeated structural domain in R-type pyocins, which are high-molecular weight bacteriocins produced by some strains of Pseudomonas aeruginosa to specifically kill other strains of the same species. R-type pyocins are structurally similar to simple contractile tails, such as those of phage P2 and Mu, and they punch a hole in the bacterial envelope to efficiently kill target cells. The second knob domain may contain regions responsible for determining the killing spectrum. Knob-like domains occur in host-recognition and binding proteins of, not only pyocins, but also phages, such as in phage K1F endosialidase (not represented by this model), where it may interact with sialic acid, the cell surface molecule that is recognized during infection.


Pssm-ID: 410997 [Multi-domain]  Cd Length: 80  Bit Score: 41.94  E-value: 7.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  896 DITYLGSYVKNADD---THSSYPVGvssmfvrsnegwfSYGTITTIKgySSGGGTLQIYTPYSSSyggdfikiRRW--NY 970
Cdd:cd19958     12 TLTTPGFYYQSANAnatTALNYPVA-------------GAGYLEVYR--YGGGGVTQIYTPYNSG--------RIYvrTR 68

                           90
                   ....*....|..
gi 2564803972  971 NATTWTDWETLI 982
Cdd:cd19958     69 YNGTWSAWKEIA 80
PHA03169 PHA03169
hypothetical protein; Provisional
 377-509 1.63e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 45.35  E-value: 1.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  377 DGLNGSDGIGLEYQWNGTSlGVRREDEASFAYTNLQGPQGIQGPQGPKGDRGvQGQKGDTGAQGSQGAQGATGPEGPAGP 456
Cdd:PHA03169    92 PSGSGSESVGSPTPSPSGS-AEELASGLSPENTSGSSPESPASHSPPPSPPS-HPGPHEPAPPESHNPSPNQQPSSFLQP 169

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2564803972  457 KGDTGPQGIQGAKGDTGPIGPQGPKGATGSQGPKGDTGLQGPqGVPGTQGPQG 509
Cdd:PHA03169   170 SHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEP-GEPQSPTPQQ 221
 
Name Accession Description Interval E-value
Sipho_Gp37 pfam14594
Siphovirus ReqiPepy6 Gp37-like protein; This family includes numerous phage proteins from ...
 18-342 2.62e-115

Siphovirus ReqiPepy6 Gp37-like protein; This family includes numerous phage proteins from Siphoviruses. The function of this protein is uncertain, but it is related to pfam06605. In Rhodococcus phage ReqiPepy6 this protein is called Gp37.


Pssm-ID: 434058  Cd Length: 336  Bit Score: 358.19  E-value: 2.62e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972   18 YTSLQYQPRWHKSGSFQLMIEGRV-NVSAFSKDHLLLFNNDHfKSAIISYAEYEVREDGQEVFVVQGSSLGSWLSQRITV 96
Cdd:pfam14594    2 YSSLTWTRRYSQPGTFELHLPATPeNADLLQEGNLIVLNDTE-KVGIIEHREITTDAEGGETLTVKGRDLKGLLARRIAW 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972   97 PPEGQAYHRLDASVETIMKEYVNLQAVNPVDPKRKITNLVISPDLERGSRTVYQTRFKQLDEELEKLSIASGLGWGIYLD 176
Cdd:pfam14594   81 PPPTAAGDVRSGTAETIMRALVNNNCINPADPARKIPNLTLGESQGRGPTVSKQARYDNLLDELESLCEASGLGFRVRLD 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  177 IENKRFVFDVFEGKDLSVSQSELSPVTFSIEFDNIKTQKYTDSGLGYKNYGYVAGQGEGAERSLVEVGNAEQTGVERYET 256
Cdd:pfam14594  161 LSTKKLIFEVYEGRDRTAGQTLNPPVIFSIEFENLTSQTYTLSAPNYKNVALVAGQGEGADREVVTVVGGEATGLDRREV 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  257 FIDARDIENEAD----------LPSRGEQKLSEFARVRSFENTILPYSSFVYGRDWNLGDIITIQNRKAGITENLRITEI 326
Cdd:pfam14594  241 FVDARDISEEAQtltdtdylaeLKERGKEKLAEYKAIESFESEVNDNGDLRYGRDYDLGDIVTVENKGWGITIDARITEV 320

                          330
                   ....*....|....*.
gi 2564803972  327 KEIYEPGGLNLEATFG 342
Cdd:pfam14594  321 EETYEQGGYTIEPTFG 336
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 412-706 1.53e-32

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: 131.95  E-value: 1.53e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  412 QGPQGIQGPQGPKGDRGV---QGQKGDTGAQGSQGAQGATGPEGPAGPKGDTGPQGIQGAKGDTGPIGPQGPKGATGSQG 488
Cdd:NF038329   125 AGPAGPAGEQGPRGDRGEtgpAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAG 204

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  489 PKGDTGLQGPQGVPGTQGPQGfgleytwdstklgvkredesayqyaeLKGEKGDAGpvgpmgppgssqsyvlferefnss 568
Cdd:NF038329   205 EQGPAGPAGPDGEAGPAGEDG--------------------------PAGPAGDGQ------------------------ 234

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  569 anqtvyswndgyvfpvgihavelyiNGDRQPsqsfkelpggngielladlpddqyllvsakmavvdlQGPQGEKGDTGPR 648
Cdd:NF038329   235 -------------------------QGPDGD------------------------------------PGPTGEDGPQGPD 253

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2564803972  649 GPIGLTGPKGEQGLQGPQGIKGDTGPAGPHGLTGSIGPKGDTGAQGPTGPIGPKGDKG 706
Cdd:NF038329   254 GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 635-821 2.71e-28

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: 119.24  E-value: 2.71e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  635 LQGPQGEKGDTGPRGPIGLTGPKGEQGLQGPQGIKGDTGPAGPHGLTGSIGPKGDTGAQGPTGPIGPKGDKGDsivwRGT 714
Cdd:NF038329   115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGP----AGE 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  715 YSSSATYSVRDAVAYNGSSYILKALASAGtiptnTAYWDPLSIKGATGSQGPQGIQGAQGLQGETGPQGPIGLTGPKGDK 794
Cdd:NF038329   191 KGPQGPRGETGPAGEQGPAGPAGPDGEAG-----PAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDR 265

                          170       180
                   ....*....|....*....|....*..
gi 2564803972  795 GEKGDIGATGPQGIKGDTGPQGLKGDK 821
Cdd:NF038329   266 GEAGPDGPDGKDGERGPVGPAGKDGQN 292
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 636-819 1.50e-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: 116.93  E-value: 1.50e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  636 QGPQGEKGDTGPRGPIGLTGPKGEQGLQGPQGIKGDTGPAGPHGLTGSIGPKGDTGAQGPTGPIGPKGDKGDsivwRGTY 715
Cdd:NF038329   125 AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP----RGET 200

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  716 SSSATYSVRDAVAYNGssyilKALASAGTIPTNTAYWDPLSIKGATGSQGPQGIQGAQGLQGETGPQGPIGLTGPKGDKG 795
Cdd:NF038329   201 GPAGEQGPAGPAGPDG-----EAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                          170       180
                   ....*....|....*....|....
gi 2564803972  796 EKGDIGATGPQGIKGDTGPQGLKG 819
Cdd:NF038329   276 KDGERGPVGPAGKDGQNGKDGLPG 299
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
636-938 2.64e-15

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 80.07  E-value: 2.64e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  636 QGPQGEKGDTGPRGPIGLTGPKGEQGLQGPQGIKGDTGPAGPHGLT------GSIGPKGDTGAQGPTGPIGPKGDKGDSI 709
Cdd:COG5164     18 TTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTrpagnqGATGPAQNQGGTTPAQNQGGTRPAGNTG 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  710 VWRGTYSSSATYSVRDAVAYNGssyilkALASAGTIPTNTAYWDPLSIKGAT----GSQGPQGIQGAQGLQGETGPQGPI 785
Cdd:COG5164     98 GTTPAGDGGATGPPDDGGATGP------PDDGGSTTPPSGGSTTPPGDGGSTppgpGSTGPGGSTTPPGDGGSTTPPGPG 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  786 GLTGPKGDKGEK--GDIGATGPQGIKGDTGPQGLKGDKPAHQWTGTSlrfeNPDGTYGLSVDLKGEKGDKGDTGPQGPEG 863
Cdd:COG5164    172 GSTTPPDDGGSTtpPNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKG----NPPDDRGGKTGPKDQRPKTNPIERRGPER 247

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2564803972  864 PPGAAVADSVEwaNVLNRPSNFPPSSHAHSTSDITYLGSYVKNADDTHSSYPVGVSSMFVRSNE-GWFSYGTITTI 938
Cdd:COG5164    248 PEAAALPAELT--ALEAENRAANPEPATKTIPETTTVKDLATVLGKKGSDLVTNLMKKGKGTNInAALDFETAATI 321
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
409-706 8.10e-15

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 78.53  E-value: 8.10e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  409 TNLQGPQGIQGPQGPKGDRGVQGQKGDTGAQGSQGAQGATGPEG------PAGPKGDTGPQGIQGAKGDTGPIGPQGPKG 482
Cdd:COG5164     15 GGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGntggtrPAGNQGATGPAQNQGGTTPAQNQGGTRPAG 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  483 ATGSQGPKGDTGLQGPQGVPGTQGPQGfgleytwdstklgvkredesayqyaelkgekgdagpvgpmgppgssqsyvlfe 562
Cdd:COG5164     95 NTGGTTPAGDGGATGPPDDGGATGPPD----------------------------------------------------- 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  563 refnssanqtvyswNDGYVFPVGIHAVELYINGDRQPSQSFKELPGGNgielladlpddqyllvsakmavvdlQGPQGEK 642
Cdd:COG5164    122 --------------DGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGS-------------------------TTPPGDG 162

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2564803972  643 GDTGPRGPIGLTGPKGEQGLQGPqGIKGDTGPAGPHGLTGSIGPKGDTGAQGPTGPIGPKGDKG 706
Cdd:COG5164    163 GSTTPPGPGGSTTPPDDGGSTTP-PNKGETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRG 225
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
635-828 1.90e-13

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 73.91  E-value: 1.90e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  635 LQGPQGekgdTGPRGPIGLTGPKGEQGLQGPQGIKGDTGPAGPhglTGSIGPKGDTGAQGPTGPIGPKGDKGDSIVWRGT 714
Cdd:COG5164      3 LYGPGK----TGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGN---TGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPA 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  715 YSSSATYSVRDA----VAYNGSSYILKALASAGTIPTNTAYWDPLSIKGAT-----GSQGPQGI-------QGAQGLQGE 778
Cdd:COG5164     76 QNQGGTTPAQNQggtrPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTtppsgGSTTPPGDggstppgPGSTGPGGS 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2564803972  779 TGPQGPIGLTGPKGDKGEKGDIGATGPQGI--KGDTGPQGLKGDKPAHQWTG 828
Cdd:COG5164    156 TTPPGDGGSTTPPGPGGSTTPPDDGGSTTPpnKGETGTDIPTGGTPRQGPDG 207
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 412-506 1.14e-12

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 71.47  E-value: 1.14e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  412 QGPQGIQGPQGPKGDRGVQGQKGDTGAQGSQGAQGATGPEGPAGPKGDTGPQGIQGAKGDTGPIGPQGPKGATGSQGPKG 491
Cdd:NF038329   244 TGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPG 323

                           90
                   ....*....|....*
gi 2564803972  492 DTGLQGPQGVPGTQG 506
Cdd:NF038329   324 KDGLPGKDGKDGQPG 338
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 452-507 5.05e-12

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: 61.74  E-value: 5.05e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2564803972  452 GPAGPKGDTGPQGIQGAKGDTGPIGPQGPKGATGSQGPKGDTGLQGPQGVPGTQGP 507
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 443-498 5.96e-12

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: 61.36  E-value: 5.96e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2564803972  443 GAQGATGPEGPAGPKGDTGPQGIQGAKGDTGPIGPQGPKGATGSQGPKGDTGLQGP 498
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 646-703 1.37e-11

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 60.20  E-value: 1.37e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2564803972  646 GPRGPIGLTGPKGEQGLQGPQGIKGDTGPAGPhglTGSIGPKGDTGAQGPTGPIGPKG 703
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGE---PGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 446-503 1.48e-11

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 60.20  E-value: 1.48e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2564803972  446 GATGPEGPAGPKGDTGPQGIQGAKGDTGPigpQGPKGATGSQGPKGDTGLQGPQGVPG 503
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGP---PGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 419-474 1.93e-11

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 59.81  E-value: 1.93e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2564803972  419 GPQGPKGDRGVQGQKGDTGAQGSQGAQGATGPEGPAGPKGDTGPQGIQGAKGDTGP 474
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 413-470 4.17e-11

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 59.04  E-value: 4.17e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2564803972  413 GPQGIQGPQGPKGDRGvqgQKGDTGAQGSQGAQGATGPEGPAGPKGDTGPQGIQGAKG 470
Cdd:pfam01391    1 GPPGPPGPPGPPGPPG---PPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 440-494 6.47e-11

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 58.66  E-value: 6.47e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2564803972  440 GSQGAQGATGPEGPAGPKGDTGPQGIQGAKGDTGPIGPQGPKGATGSQGPKGDTG 494
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 437-491 7.72e-11

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 58.27  E-value: 7.72e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2564803972  437 GAQGSQGAQGATGPEGPAGPKGDTGPQGIQGAKGDTGPIGPQGPKGATGSQGPKG 491
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 428-483 1.69e-10

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 57.12  E-value: 1.69e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2564803972  428 GVQGQKGDTGAQGSQGAQGATGPEGPAGPKGDTGPQGIQGAKGDTGPIGPQGPKGA 483
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 422-480 1.72e-10

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 57.12  E-value: 1.72e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2564803972  422 GPKGDRGVQGQKGDTGAQGSQGAQGATGPEGPAGPkgdTGPQGIQGAKGDTGPIGPQGP 480
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGP---PGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 762-855 2.41e-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: 63.77  E-value: 2.41e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  762 GSQGPQGIQGAQGLQGETGPQGPIGLTGP---KGDKGEKGDIGATGPQGIKGDTGPQGLKGdkpahqwtgtslrfenPDG 838
Cdd:NF038329   117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPagpAGPPGPQGERGEKGPAGPQGEAGPQGPAG----------------KDG 180

                           90
                   ....*....|....*..
gi 2564803972  839 TYGLSVDlKGEKGDKGD 855
Cdd:NF038329   181 EAGAKGP-AGEKGPQGP 196
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 431-485 4.95e-10

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: 55.96  E-value: 4.95e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2564803972  431 GQKGDTGAQGSQGAQGATGPEGPAGPKGDTGPQGIQGAKGDTGPIGPQGPKGATG 485
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 413-462 8.90e-10

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: 55.19  E-value: 8.90e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2564803972  413 GPQGIQGPQGPKGDRGVQGQKGDTGAQGSQGAQGATGPEGPAGPKGDTGP 462
Cdd:pfam01391    7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 455-509 8.99e-10

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: 55.19  E-value: 8.99e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2564803972  455 GPKGDTGPQGIQGAKGDTGPIGPQGPKGATGSQGPKGDTGLQGPQGVPGTQGPQG 509
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 411-464 1.23e-09

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: 54.81  E-value: 1.23e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2564803972  411 LQGPQGIQGPQGPKGDRGVQGQKGDTGAQGSQGAQGATGPEGPAGPKGDTGPQG 464
Cdd:pfam01391    2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 765-819 4.93e-09

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: 53.27  E-value: 4.93e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2564803972  765 GPQGIQGAQGLQGETGPQGPIGLTGPKGDKGEKGDIGATGPQGIKGDTGPQGLKG 819
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 767-855 1.50e-08

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: 58.38  E-value: 1.50e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  767 QGIQGAQGlQGETGPQGPIGLTGPKGDKGEKGDIGATGPQGIKGDTGPQGLKGDKPAHQWTGtslrfenPDGTYGLSVDl 846
Cdd:NF038329   108 EGLQQLKG-DGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG-------EAGPQGPAGK- 178


                   ....*....
gi 2564803972  847 KGEKGDKGD 855
Cdd:NF038329   179 DGEAGAKGP 187
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 637-688 1.55e-08

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 51.73  E-value: 1.55e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2564803972  637 GPQGEKGDTGPRGPIGLTGPKGEQGLQGPQGIKGDTGPAGPhglTGSIGPKG 688
Cdd:pfam01391    7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP---PGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 464-510 2.90e-08

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 50.96  E-value: 2.90e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2564803972  464 GIQGAKGDTGPIGPQGPKGATGSQGPKGDTGLQGPQGVPGTQGPQGF 510
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP 47
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 759-814 3.64e-08

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 50.57  E-value: 3.64e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2564803972  759 GATGSQGPQGIQGAQGLQGETGPQGPIGLTGPKGDKGEKGDIGATGPQGIKGDTGP 814
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 768-821 9.41e-08

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 49.41  E-value: 9.41e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2564803972  768 GIQGAQGLQGETGPQGPIGLTGPKGDKGEKGDIGATGPQGIKGDTGPQGLKGDK 821
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 658-706 1.52e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 49.03  E-value: 1.52e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2564803972  658 GEQGLQGPQGIKGDTGPAGPHGLTGSIGPKGDTGAQGPTGPIGPKGDKG 706
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 636-675 1.13e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 46.33  E-value: 1.13e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2564803972  636 QGPQGEKGDTGPRGPIGLTGPKGEQGLQGPQGIKGDTGPA 675
Cdd:pfam01391   18 PGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 758-805 2.06e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.56  E-value: 2.06e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2564803972  758 KGATGSQGPQGIQGAQGLQGETGPQGPIGLTGPK---GDKGEKGDIGATGP 805
Cdd:pfam01391    6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPgppGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 637-677 5.79e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.41  E-value: 5.79e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2564803972  637 GPQGEKGDTGPRGPIGLTGPKGEQGLQGPQGIKGDTGPAGP 677
Cdd:pfam01391   16 GPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 412-450 1.03e-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: 43.64  E-value: 1.03e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2564803972  412 QGPQGIQGPQGPKGDRGVQGQKGDTGAQGSQGAQGATGP 450
Cdd:pfam01391   18 PGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
pyocin_knob cd19958
knob domain of R1 and R2 pyocins and similar domains; The knob domain is present as a tandemly ...
 896-982 7.23e-05

knob domain of R1 and R2 pyocins and similar domains; The knob domain is present as a tandemly repeated structural domain in R-type pyocins, which are high-molecular weight bacteriocins produced by some strains of Pseudomonas aeruginosa to specifically kill other strains of the same species. R-type pyocins are structurally similar to simple contractile tails, such as those of phage P2 and Mu, and they punch a hole in the bacterial envelope to efficiently kill target cells. The second knob domain may contain regions responsible for determining the killing spectrum. Knob-like domains occur in host-recognition and binding proteins of, not only pyocins, but also phages, such as in phage K1F endosialidase (not represented by this model), where it may interact with sialic acid, the cell surface molecule that is recognized during infection.


Pssm-ID: 410997 [Multi-domain]  Cd Length: 80  Bit Score: 41.94  E-value: 7.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  896 DITYLGSYVKNADD---THSSYPVGvssmfvrsnegwfSYGTITTIKgySSGGGTLQIYTPYSSSyggdfikiRRW--NY 970
Cdd:cd19958     12 TLTTPGFYYQSANAnatTALNYPVA-------------GAGYLEVYR--YGGGGVTQIYTPYNSG--------RIYvrTR 68

                           90
                   ....*....|..
gi 2564803972  971 NATTWTDWETLI 982
Cdd:cd19958     69 YNGTWSAWKEIA 80
PHA03169 PHA03169
hypothetical protein; Provisional
 377-509 1.63e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 45.35  E-value: 1.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  377 DGLNGSDGIGLEYQWNGTSlGVRREDEASFAYTNLQGPQGIQGPQGPKGDRGvQGQKGDTGAQGSQGAQGATGPEGPAGP 456
Cdd:PHA03169    92 PSGSGSESVGSPTPSPSGS-AEELASGLSPENTSGSSPESPASHSPPPSPPS-HPGPHEPAPPESHNPSPNQQPSSFLQP 169

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2564803972  457 KGDTGPQGIQGAKGDTGPIGPQGPKGATGSQGPKGDTGLQGPqGVPGTQGPQG 509
Cdd:PHA03169   170 SHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEP-GEPQSPTPQQ 221
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 414-508 2.58e-04

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 42.72  E-value: 2.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  414 PQGIQGPQGPKGDRGvQGQKGDTGAQGSQGAQGATGPEGPAGPKGDTGPQGIQGAKGDTGPIGPQGPKGATGSQGPKGDT 493
Cdd:pfam15240   50 PPGGFPPQPPASDDP-PGPPPPGGPQQPPPQGGKQKPQGPPPQGGPRPPPGKPQGPPPQGGNQQQGPPPPGKPQGPPPQG 128

                           90
                   ....*....|....*
gi 2564803972  494 GLQGPQGVPgTQGPQ 508
Cdd:pfam15240  129 GGPPPQGGN-QQGPP 142
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 679-784 9.62e-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: 35.55  E-value: 9.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564803972  679 GLTGSIGPKGDTGAQGPTGPIGPKGDKGDSivwrgtysssatysvrdavayngssyilkalasagtiptntaywdplsik 758
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPP-------------------------------------------------- 30

                           90       100
                   ....*....|....*....|....*.
gi 2564803972  759 GATGSQGPQGIQGAQGLQGETGPQGP 784
Cdd:pfam01391   31 GEPGPPGPPGPPGPPGPPGAPGAPGP 56
 
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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