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Conserved domains on  [gi|28204656|gb|AAN87341|]
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collagen type XXVII proalpha 1 chain [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 ...
1646-1844 4.34e-57

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: 321934  Cd Length: 230  Bit Score: 197.54  E-value: 4.34e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1646 EIFKTLHYLSNLIQSIKTPLGTKENPARVCRDLMDCEQRMADGTYWVDPNLGCSSDTIEVSCNFTQGgQTCLKPITAS-- 1723
Cdd:pfam01410    1 EVFASLKSLNQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCAKDAIKVFCNFETG-ETCIYPDPASip 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1724 ---------------------KAEF--------AVSRVQMNFLHLLSSEGTQHITIHCLNMTVWQEgPGRSSARQAVRFR 1774
Cdd:pfam01410   80 rknwwtkenkkhvwfgefmngGSQFsyvddsgpAVGVVQLTFLRLLSTEASQNITYHCKNSVAYMD-QATGNLKKALRLL 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28204656   1775 AWNGQVFEAGG--QFRPEVSMDGCKVHDGRWHQTLFTFRTQDPQQLPIVsvdNLPPVSSGK---QYRLEVGPACF 1844
Cdd:pfam01410  159 GSNDEELRAEGnsRFTYTVLEDGCSKRTGQWGKTVIEYRTQKTSRLPIV---DIAPMDIGGadqEFGVEVGPVCF 230
LamG super family cl22861
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
43-221 1.90e-13

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


The actual alignment was detected with superfamily member smart00210:

Pssm-ID: 354964  Cd Length: 184  Bit Score: 70.46  E-value: 1.90e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656      43 DVDVLQRLGL-----SWTKAGGGRSPTPpgvipfpsGFIFTQRAKLQAPTANVLPTTLGRELALVLSLCSHRVNHAFLFA 117
Cdd:smart00210    1 GQDLLQVFDLpslsfAIRQVVGPEPGSP--------AYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFA 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656     118 IRSRKHKLQLGLQFLPGRTIIHL------GPRQSVAF-DLDVHDGRWHHLALELRGRTVTMVTACGQHRVpVPLPSRRDS 190
Cdd:smart00210   73 IYDAQNVRQFGLEVDGRANTLLLryqgvdGKQHTVSFrNLPLADGQWHKLALSVSGSSATLYVDCNEIDS-RPLDRPGQP 151
                           170       180       190
                    ....*....|....*....|....*....|.
gi 28204656     191 MLDPQGSFLLGKVNPRAVQFEGALCQFSIHP 221
Cdd:smart00210  152 PIDTDGIEVRGAQAADRKPFQGDLQQLKIVC 182
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
269-567 4.72e-07

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


The actual alignment was detected with superfamily member pfam05109:

Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 54.92  E-value: 4.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656    269 GLGNLTRTPATLGArPVSRALAVTVAramptkPVRSVRPDVSERSCSQTPLSPAKQSARKTPSPSSSASLANSTRVYRPA 348
Cdd:pfam05109  447 GLPSSTHVPTNLTA-PASTGPTVSTA------DVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPN 519
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656    349 AAQPR-QITTTSPTKRSPTKPSVSPLSVTPMKSPHATQKTgvPSFTKPVP----PT-QKPAPFTSYLAPS-KASSPTVrp 421
Cdd:pfam05109  520 ATSPTpAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPT--PAVTTPTPnatiPTlGKTSPTSAVTTPTpNATSPTV-- 595
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656    422 vqktfmtprppvpspqplrPTTGLSKKFTNPTVAKSkSKTTSWASKPVLARSSVpKTLQQTVLSQSPVSY-LGSQTLAPA 500
Cdd:pfam05109  596 -------------------GETSPQANTTNHTLGGT-SSTPVVTSPPKNATSAV-TTGQHNITSSSTSSMsLRPSSISET 654
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28204656    501 LPPLGVGNPRTMPPTRDSAlTPAGSKKFTGRETSKKTRQKSSPRKPEPlSPGKSARDASP--RDLTTKP 567
Cdd:pfam05109  655 LSPSTSDNSTSHMPLLTSA-HPTGGENITQVTPASTSTHHVSTSSPAP-RPGTTSQASGPgnSSTSTKP 721
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
679-737 4.40e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 45.56  E-value: 4.40e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 28204656    679 GLPGLSGNPGPLGRKGHKGHPGAAGHPGEQGQPGPEGSPGAKGYPGRQGFPGPVGDPGP 737
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
709-768 1.14e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 44.40  E-value: 1.14e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656    709 GQPGPEGSPGAKGYPGRQGFPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKR 768
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1367-1424 1.32e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 44.02  E-value: 1.32e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 28204656   1367 GQPGHPGPRGRPGPKGSKGEEGPKGKPGKAGPSGRRGTQGLQGLPGPRGVVGRQGPEG 1424
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
745-801 1.70e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 43.63  E-value: 1.70e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 28204656    745 GLPGLFGLPGSDGERGLPGVPGKRGEMGRPGFPGDFGERGPPGLDGNPGEIGLPGPP 801
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1430-1489 2.13e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 43.63  E-value: 2.13e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1430 GIPGRDGRPGYQGDQGNDGDPGPVGPAGRRGNPGVAGLPGAQGPPGFKGESGLPGQLGPP 1489
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1159-1218 6.48e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 42.09  E-value: 6.48e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1159 GPPGEQGLIGQRGEPGLEGDHGPVGPDGLKGDRGDPGPDGEHGEKGQEGLKGEDGSPGPP 1218
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1463-1520 8.20e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 41.71  E-value: 8.20e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 28204656   1463 GVAGLPGAQGPPGFKGESGLPGQLGPPGKRGTEGGTGLPGNQGEPGSKGQPGDSGEMG 1520
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1038-1096 9.59e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 41.71  E-value: 9.59e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 28204656   1038 RGLPGMRGAKGHRGPRGPDGPAGEQGSKGLKgrvGPRGRPGQPGQQGAAGERGHSGAKG 1096
Cdd:pfam01391    3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGPP---GPPGPPGPPGPPGPPGPPGAPGAPG 58
Glutenin_hmw super family cl26620
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
1198-1550 1.55e-04

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


The actual alignment was detected with superfamily member pfam03157:

Pssm-ID: 281191 [Multi-domain]  Cd Length: 772  Bit Score: 46.67  E-value: 1.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1198 GEHGEKGQEGLKGEDGSPG--PPGITGVPGREGKPGkQGEKGQRGAKGAKGHQGYLGEMGipgepgppgtpgpkgSRGTL 1275
Cdd:pfam03157  124 GQQPGQGQQGRQPGQGQPGyyPTSSQLQPGQLQQPA-QGQQGQQPGQGQQGQQPGQGQQP---------------GQGQQ 187
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1276 GPTGAPGRMGAQGEPGLAGYNGHKGITGPLGPPGPKGEKGDQGEDGKTEGPPGPPGDRGPVGDRGDRGEPGDPGYP---- 1351
Cdd:pfam03157  188 GQQPGQGQQPGQGQQGQQLGQGQQGYYPTSLQQSGQGQPGYYPTSLQQLGQGQSGYYPTSPQQPGQGQQPGQLQQPaqgq 267
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1352 ----GQEGVQGLRGEPGQQGQPGHPGPRGRPGPKGSKGEEGPKGKPGKAGPSGRRGTQGLQGLPGPRGVVGRQGPEGTAG 1427
Cdd:pfam03157  268 qpeqGQQGQQPGQGQQGQQPGQGQQPGQGQPGYYPTSPQQSGQGQPGYYPTSSQQPTQSQQPGQGQQGQQVGQGQQAQQP 347
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1428 SDGIPGRDGRPGYQGD---QGNDGDPGPVGPAGRRGNPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRGTEGGTGLPGNQ 1504
Cdd:pfam03157  348 GQGQQPGQGQPGYYPTsplQSGQGQPGYYLTSPQQSGQGQQPGQLQQSAQGQKGQQPGQGQQPGQGQQGQQPGQGQQGQQ 427
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 28204656   1505 GEPGSKG----QPGDSGEMGFPGVAGLFGpKGPPGDIGFKGIQGPRGPPG 1550
Cdd:pfam03157  428 PGQGQPGyyptSPQQSGQGQQPGQWQQPG-QGQPGYYPTSPLQPGQGQPG 476
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
904-975 1.78e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 38.24  E-value: 1.78e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28204656    904 GDNGPEGMKGKPGARGLPGPPGQLGPEGDEgpmgppgvpgleGQPGRKGFPGRPGLDGSKGEPGDPGRPGPV 975
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPP------------GPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
784-842 4.72e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 37.08  E-value: 4.72e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 28204656    784 GPPGLDGNPGEIGLPGPPGVLGLIGDTGALGPVGYPGPKGMKGLMGGVGEPGLKGDKGE 842
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1130-1184 5.63e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 36.70  E-value: 5.63e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28204656   1130 EMGPKGPPGAVGEPGLPGDSGMKGDLGPLGPPGEQGLIGQRGEPGLEGDHGPVGP 1184
Cdd:pfam01391    5 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
1646-1844 4.34e-57

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: 307527  Cd Length: 230  Bit Score: 197.54  E-value: 4.34e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1646 EIFKTLHYLSNLIQSIKTPLGTKENPARVCRDLMDCEQRMADGTYWVDPNLGCSSDTIEVSCNFTQGgQTCLKPITAS-- 1723
Cdd:pfam01410    1 EVFASLKSLNQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCAKDAIKVFCNFETG-ETCIYPDPASip 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1724 ---------------------KAEF--------AVSRVQMNFLHLLSSEGTQHITIHCLNMTVWQEgPGRSSARQAVRFR 1774
Cdd:pfam01410   80 rknwwtkenkkhvwfgefmngGSQFsyvddsgpAVGVVQLTFLRLLSTEASQNITYHCKNSVAYMD-QATGNLKKALRLL 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28204656   1775 AWNGQVFEAGG--QFRPEVSMDGCKVHDGRWHQTLFTFRTQDPQQLPIVsvdNLPPVSSGK---QYRLEVGPACF 1844
Cdd:pfam01410  159 GSNDEELRAEGnsRFTYTVLEDGCSKRTGQWGKTVIEYRTQKTSRLPIV---DIAPMDIGGadqEFGVEVGPVCF 230
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
1645-1845 3.44e-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: 3.44e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656    1645 GEIFKTLHYLSNLIQSIKTPLGTKENPARVCRDLMDCEQRMADGTYWVDPNLGCSSDTIEVSCNFTqGGQTCLKPITASK 1724
Cdd:smart00038    2 EEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFE-TGETCVSPSPSSI 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656    1725 A----------------------EFA--------VSRVQMNFLHLLSSEGTQHITIHCLNMTVWQEgPGRSSARQAVRFR 1774
Cdd:smart00038   81 PrktwysgkskhvwfgetmnggfKFSygdsegppVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMD-EATGNLKKALRLR 159
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28204656    1775 AWNGQVFEAGGQFRP--EVSMDGCKVHDGRWHQTLFTFRTQDPQQLPIVsvdNLPPVSSGKQYR---LEVGPACFL 1845
Cdd:smart00038  160 GSNDVELSAEGNSKFtyEVLEDGCQKRTGKWGKTVIEYRTKKTERLPIV---DIAPSDIGGPDQefgVEIGPVCFS 232
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
43-221 1.90e-13

Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin


Pssm-ID: 214560  Cd Length: 184  Bit Score: 70.46  E-value: 1.90e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656      43 DVDVLQRLGL-----SWTKAGGGRSPTPpgvipfpsGFIFTQRAKLQAPTANVLPTTLGRELALVLSLCSHRVNHAFLFA 117
Cdd:smart00210    1 GQDLLQVFDLpslsfAIRQVVGPEPGSP--------AYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFA 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656     118 IRSRKHKLQLGLQFLPGRTIIHL------GPRQSVAF-DLDVHDGRWHHLALELRGRTVTMVTACGQHRVpVPLPSRRDS 190
Cdd:smart00210   73 IYDAQNVRQFGLEVDGRANTLLLryqgvdGKQHTVSFrNLPLADGQWHKLALSVSGSSATLYVDCNEIDS-RPLDRPGQP 151
                           170       180       190
                    ....*....|....*....|....*....|.
gi 28204656     191 MLDPQGSFLLGKVNPRAVQFEGALCQFSIHP 221
Cdd:smart00210  152 PIDTDGIEVRGAQAADRKPFQGDLQQLKIVC 182
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
269-567 4.72e-07

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 54.92  E-value: 4.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656    269 GLGNLTRTPATLGArPVSRALAVTVAramptkPVRSVRPDVSERSCSQTPLSPAKQSARKTPSPSSSASLANSTRVYRPA 348
Cdd:pfam05109  447 GLPSSTHVPTNLTA-PASTGPTVSTA------DVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPN 519
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656    349 AAQPR-QITTTSPTKRSPTKPSVSPLSVTPMKSPHATQKTgvPSFTKPVP----PT-QKPAPFTSYLAPS-KASSPTVrp 421
Cdd:pfam05109  520 ATSPTpAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPT--PAVTTPTPnatiPTlGKTSPTSAVTTPTpNATSPTV-- 595
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656    422 vqktfmtprppvpspqplrPTTGLSKKFTNPTVAKSkSKTTSWASKPVLARSSVpKTLQQTVLSQSPVSY-LGSQTLAPA 500
Cdd:pfam05109  596 -------------------GETSPQANTTNHTLGGT-SSTPVVTSPPKNATSAV-TTGQHNITSSSTSSMsLRPSSISET 654
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28204656    501 LPPLGVGNPRTMPPTRDSAlTPAGSKKFTGRETSKKTRQKSSPRKPEPlSPGKSARDASP--RDLTTKP 567
Cdd:pfam05109  655 LSPSTSDNSTSHMPLLTSA-HPTGGENITQVTPASTSTHHVSTSSPAP-RPGTTSQASGPgnSSTSTKP 721
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
679-737 4.40e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 45.56  E-value: 4.40e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 28204656    679 GLPGLSGNPGPLGRKGHKGHPGAAGHPGEQGQPGPEGSPGAKGYPGRQGFPGPVGDPGP 737
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
709-768 1.14e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 44.40  E-value: 1.14e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656    709 GQPGPEGSPGAKGYPGRQGFPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKR 768
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1367-1424 1.32e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 44.02  E-value: 1.32e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 28204656   1367 GQPGHPGPRGRPGPKGSKGEEGPKGKPGKAGPSGRRGTQGLQGLPGPRGVVGRQGPEG 1424
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
745-801 1.70e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 43.63  E-value: 1.70e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 28204656    745 GLPGLFGLPGSDGERGLPGVPGKRGEMGRPGFPGDFGERGPPGLDGNPGEIGLPGPP 801
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1430-1489 2.13e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 43.63  E-value: 2.13e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1430 GIPGRDGRPGYQGDQGNDGDPGPVGPAGRRGNPGVAGLPGAQGPPGFKGESGLPGQLGPP 1489
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1159-1218 6.48e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 42.09  E-value: 6.48e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1159 GPPGEQGLIGQRGEPGLEGDHGPVGPDGLKGDRGDPGPDGEHGEKGQEGLKGEDGSPGPP 1218
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1463-1520 8.20e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 41.71  E-value: 8.20e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 28204656   1463 GVAGLPGAQGPPGFKGESGLPGQLGPPGKRGTEGGTGLPGNQGEPGSKGQPGDSGEMG 1520
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
318-577 8.38e-05

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 47.23  E-value: 8.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   318 PLSPAKQSARKTPSPSSSASLANSTRVYRPAAAQP-RQITTTSPTKRSPTKP---SVSPLS-------VTPMKSPHATQK 386
Cdd:PLN03209  312 PLTPMEELLAKIPSQRVPPKESDAADGPKPVPTKPvTPEAPSPPIEEEPPQPkavVPRPLSpytayedLKPPTSPIPTPP 391
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   387 TGVPSFTKPVPPTQKPAPFTSYLAPSKASS---PTVRPVQKTFMTPRPPVPSPQPLRPTTGLSKK---FTNPTVAKSKSK 460
Cdd:PLN03209  392 SSSPASSKSVDAVAKPAEPDVVPSPGSASNvpeVEPAQVEAKKTRPLSPYARYEDLKPPTSPSPTaptGVSPSVSSTSSV 471
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   461 TTSWASKPVLARSSvpKTLQQTVLSQSPVSYLGSQTLAPALPPLGVGNPRTMPPTRDSALTPAGSkkfTGRETSKKTRQK 540
Cdd:PLN03209  472 PAVPDTAPATAATD--AAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEVVKVGN---SAPPTALADEQH 546
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 28204656   541 SSPRKPEPLSPGKSARDASPrdlttkPSRPsTPALVL 577
Cdd:PLN03209  547 HAQPKPRPLSPYTMYEDLKP------PTSP-TPSPVL 576
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1038-1096 9.59e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 41.71  E-value: 9.59e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 28204656   1038 RGLPGMRGAKGHRGPRGPDGPAGEQGSKGLKgrvGPRGRPGQPGQQGAAGERGHSGAKG 1096
Cdd:pfam01391    3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGPP---GPPGPPGPPGPPGPPGPPGAPGAPG 58
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
1198-1550 1.55e-04

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 281191 [Multi-domain]  Cd Length: 772  Bit Score: 46.67  E-value: 1.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1198 GEHGEKGQEGLKGEDGSPG--PPGITGVPGREGKPGkQGEKGQRGAKGAKGHQGYLGEMGipgepgppgtpgpkgSRGTL 1275
Cdd:pfam03157  124 GQQPGQGQQGRQPGQGQPGyyPTSSQLQPGQLQQPA-QGQQGQQPGQGQQGQQPGQGQQP---------------GQGQQ 187
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1276 GPTGAPGRMGAQGEPGLAGYNGHKGITGPLGPPGPKGEKGDQGEDGKTEGPPGPPGDRGPVGDRGDRGEPGDPGYP---- 1351
Cdd:pfam03157  188 GQQPGQGQQPGQGQQGQQLGQGQQGYYPTSLQQSGQGQPGYYPTSLQQLGQGQSGYYPTSPQQPGQGQQPGQLQQPaqgq 267
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1352 ----GQEGVQGLRGEPGQQGQPGHPGPRGRPGPKGSKGEEGPKGKPGKAGPSGRRGTQGLQGLPGPRGVVGRQGPEGTAG 1427
Cdd:pfam03157  268 qpeqGQQGQQPGQGQQGQQPGQGQQPGQGQPGYYPTSPQQSGQGQPGYYPTSSQQPTQSQQPGQGQQGQQVGQGQQAQQP 347
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1428 SDGIPGRDGRPGYQGD---QGNDGDPGPVGPAGRRGNPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRGTEGGTGLPGNQ 1504
Cdd:pfam03157  348 GQGQQPGQGQPGYYPTsplQSGQGQPGYYLTSPQQSGQGQQPGQLQQSAQGQKGQQPGQGQQPGQGQQGQQPGQGQQGQQ 427
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 28204656   1505 GEPGSKG----QPGDSGEMGFPGVAGLFGpKGPPGDIGFKGIQGPRGPPG 1550
Cdd:pfam03157  428 PGQGQPGyyptSPQQSGQGQQPGQWQQPG-QGQPGYYPTSPLQPGQGQPG 476
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
124-205 6.51e-04

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058  Cd Length: 151  Bit Score: 42.02  E-value: 6.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656  124 KLQLGLQFLPGRTIIHLGPRqsvafdldVHDGRWHHLALELRGRTVTMVTACGQHrVPVPLPsRRDSMLDPQGSFLLGKV 203
Cdd:cd00110   57 RLVLRYDLGSGSLVLSSKTP--------LNDGQWHSVSVERNGRSVTLSVDGERV-VESGSP-GGSALLNLDGPLYLGGL 126

                 ..
gi 28204656  204 NP 205
Cdd:cd00110  127 PE 128
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1361-1550 6.58e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.59  E-value: 6.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656  1361 GEPGQQGQPGHPGPRGRPGPKGS---KGEEGPKGKPGKAGPSGRRGTQGLQGLPGPRGVVGRQGPEGTAGSDGIPGRDGR 1437
Cdd:PRK07764  590 PAPGAAGGEGPPAPASSGPPEEAarpAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656  1438 PGYQGDQGNDGDPGPVGPAGRRGNPGVAGLPGAQGPPGfkgesglpgqlgPPGKRGTEGGTGLPGNQGEPGSKGQPGDSG 1517
Cdd:PRK07764  670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAA------------TPPAGQADDPAAQPPQAAQGASAPSPAADD 737
                         170       180       190
                  ....*....|....*....|....*....|....
gi 28204656  1518 EMGFPGVAGLF-GPKGPPGDIGFKGIQGPRGPPG 1550
Cdd:PRK07764  738 PVPLPPEPDDPpDPAGAPAQPPPPPAPAPAAAPA 771
PHA03169 PHA03169
hypothetical protein; Provisional
1074-1235 1.57e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 42.65  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656  1074 RGRPGQPGQQGAAGErGHSGAKGFLGIPGPSGPPGAKGLPGEPGSqgpqgpvgPPGEMGPKGPPGAVGEPGLPGDsGMKG 1153
Cdd:PHA03169   81 HGEKEERGQGGPSGS-GSESVGSPTPSPSGSAEELASGLSPENTS--------GSSPESPASHSPPPSPPSHPGP-HEPA 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656  1154 DLGPLGPPGEQGLIGQRGEPGLEGDHGPVGPDGLKGDRGDPGPDGEHGEKGQEGLKG--EDGSPGPPGITGVPGREGKPG 1231
Cdd:PHA03169  151 PPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPpdEPGEPQSPTPQQAPSPNTQQA 230

                  ....
gi 28204656  1232 KQGE 1235
Cdd:PHA03169  231 VEHE 234
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
904-975 1.78e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 38.24  E-value: 1.78e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28204656    904 GDNGPEGMKGKPGARGLPGPPGQLGPEGDEgpmgppgvpgleGQPGRKGFPGRPGLDGSKGEPGDPGRPGPV 975
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPP------------GPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
141-205 2.69e-03

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 308045  Cd Length: 126  Bit Score: 39.34  E-value: 2.69e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28204656    141 GPRQSVAFDLDVHDGRWHHLALELRGRTVTMVTaCGQHRVPVPLPSRRDsMLDPQGSFLLGKVNP 205
Cdd:pfam02210   39 GPVSLLSSGKPLNDGQWHRVRVSRNGRTLTLSV-DGQTVVSALPPGESL-LLNLNGPLYLGGLPP 101
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
784-842 4.72e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 37.08  E-value: 4.72e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 28204656    784 GPPGLDGNPGEIGLPGPPGVLGLIGDTGALGPVGYPGPKGMKGLMGGVGEPGLKGDKGE 842
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1130-1184 5.63e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 36.70  E-value: 5.63e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28204656   1130 EMGPKGPPGAVGEPGLPGDSGMKGDLGPLGPPGEQGLIGQRGEPGLEGDHGPVGP 1184
Cdd:pfam01391    5 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
1646-1844 4.34e-57

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: 307527  Cd Length: 230  Bit Score: 197.54  E-value: 4.34e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1646 EIFKTLHYLSNLIQSIKTPLGTKENPARVCRDLMDCEQRMADGTYWVDPNLGCSSDTIEVSCNFTQGgQTCLKPITAS-- 1723
Cdd:pfam01410    1 EVFASLKSLNQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCAKDAIKVFCNFETG-ETCIYPDPASip 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1724 ---------------------KAEF--------AVSRVQMNFLHLLSSEGTQHITIHCLNMTVWQEgPGRSSARQAVRFR 1774
Cdd:pfam01410   80 rknwwtkenkkhvwfgefmngGSQFsyvddsgpAVGVVQLTFLRLLSTEASQNITYHCKNSVAYMD-QATGNLKKALRLL 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28204656   1775 AWNGQVFEAGG--QFRPEVSMDGCKVHDGRWHQTLFTFRTQDPQQLPIVsvdNLPPVSSGK---QYRLEVGPACF 1844
Cdd:pfam01410  159 GSNDEELRAEGnsRFTYTVLEDGCSKRTGQWGKTVIEYRTQKTSRLPIV---DIAPMDIGGadqEFGVEVGPVCF 230
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
1645-1845 3.44e-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: 3.44e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656    1645 GEIFKTLHYLSNLIQSIKTPLGTKENPARVCRDLMDCEQRMADGTYWVDPNLGCSSDTIEVSCNFTqGGQTCLKPITASK 1724
Cdd:smart00038    2 EEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFE-TGETCVSPSPSSI 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656    1725 A----------------------EFA--------VSRVQMNFLHLLSSEGTQHITIHCLNMTVWQEgPGRSSARQAVRFR 1774
Cdd:smart00038   81 PrktwysgkskhvwfgetmnggfKFSygdsegppVGVVQLTFLRLLSTEAHQNITYHCKNSVAYMD-EATGNLKKALRLR 159
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28204656    1775 AWNGQVFEAGGQFRP--EVSMDGCKVHDGRWHQTLFTFRTQDPQQLPIVsvdNLPPVSSGKQYR---LEVGPACFL 1845
Cdd:smart00038  160 GSNDVELSAEGNSKFtyEVLEDGCQKRTGKWGKTVIEYRTKKTERLPIV---DIAPSDIGGPDQefgVEIGPVCFS 232
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
43-221 1.90e-13

Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin


Pssm-ID: 214560  Cd Length: 184  Bit Score: 70.46  E-value: 1.90e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656      43 DVDVLQRLGL-----SWTKAGGGRSPTPpgvipfpsGFIFTQRAKLQAPTANVLPTTLGRELALVLSLCSHRVNHAFLFA 117
Cdd:smart00210    1 GQDLLQVFDLpslsfAIRQVVGPEPGSP--------AYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFA 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656     118 IRSRKHKLQLGLQFLPGRTIIHL------GPRQSVAF-DLDVHDGRWHHLALELRGRTVTMVTACGQHRVpVPLPSRRDS 190
Cdd:smart00210   73 IYDAQNVRQFGLEVDGRANTLLLryqgvdGKQHTVSFrNLPLADGQWHKLALSVSGSSATLYVDCNEIDS-RPLDRPGQP 151
                           170       180       190
                    ....*....|....*....|....*....|.
gi 28204656     191 MLDPQGSFLLGKVNPRAVQFEGALCQFSIHP 221
Cdd:smart00210  152 PIDTDGIEVRGAQAADRKPFQGDLQQLKIVC 182
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
269-567 4.72e-07

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 54.92  E-value: 4.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656    269 GLGNLTRTPATLGArPVSRALAVTVAramptkPVRSVRPDVSERSCSQTPLSPAKQSARKTPSPSSSASLANSTRVYRPA 348
Cdd:pfam05109  447 GLPSSTHVPTNLTA-PASTGPTVSTA------DVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPN 519
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656    349 AAQPR-QITTTSPTKRSPTKPSVSPLSVTPMKSPHATQKTgvPSFTKPVP----PT-QKPAPFTSYLAPS-KASSPTVrp 421
Cdd:pfam05109  520 ATSPTpAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPT--PAVTTPTPnatiPTlGKTSPTSAVTTPTpNATSPTV-- 595
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656    422 vqktfmtprppvpspqplrPTTGLSKKFTNPTVAKSkSKTTSWASKPVLARSSVpKTLQQTVLSQSPVSY-LGSQTLAPA 500
Cdd:pfam05109  596 -------------------GETSPQANTTNHTLGGT-SSTPVVTSPPKNATSAV-TTGQHNITSSSTSSMsLRPSSISET 654
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28204656    501 LPPLGVGNPRTMPPTRDSAlTPAGSKKFTGRETSKKTRQKSSPRKPEPlSPGKSARDASP--RDLTTKP 567
Cdd:pfam05109  655 LSPSTSDNSTSHMPLLTSA-HPTGGENITQVTPASTSTHHVSTSSPAP-RPGTTSQASGPgnSSTSTKP 721
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
679-737 4.40e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 45.56  E-value: 4.40e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 28204656    679 GLPGLSGNPGPLGRKGHKGHPGAAGHPGEQGQPGPEGSPGAKGYPGRQGFPGPVGDPGP 737
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
709-768 1.14e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 44.40  E-value: 1.14e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656    709 GQPGPEGSPGAKGYPGRQGFPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKR 768
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1367-1424 1.32e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 44.02  E-value: 1.32e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 28204656   1367 GQPGHPGPRGRPGPKGSKGEEGPKGKPGKAGPSGRRGTQGLQGLPGPRGVVGRQGPEG 1424
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
745-801 1.70e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 43.63  E-value: 1.70e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 28204656    745 GLPGLFGLPGSDGERGLPGVPGKRGEMGRPGFPGDFGERGPPGLDGNPGEIGLPGPP 801
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1430-1489 2.13e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 43.63  E-value: 2.13e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1430 GIPGRDGRPGYQGDQGNDGDPGPVGPAGRRGNPGVAGLPGAQGPPGFKGESGLPGQLGPP 1489
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
673-732 2.42e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 43.25  E-value: 2.42e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656    673 GAKGNMGLPGLSGNPGPLGRKGHKGHPGAAGHPGEQGQPGPEGSPGAKGYPGRQGFPGPV 732
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1355-1414 3.04e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 43.25  E-value: 3.04e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1355 GVQGLRGEPGQQGQPGHPGPRGRPGPKGSKGEEGPKGKPGKAGPSGRRGTQGLQGLPGPR 1414
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1358-1415 3.42e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 42.86  E-value: 3.42e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 28204656   1358 GLRGEPGQQGQPGHPGPRGRPGPKGSKGEEGPKGKPGKAGPSGRRGTQGLQGLPGPRG 1415
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
691-748 4.55e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 42.48  E-value: 4.55e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 28204656    691 GRKGHKGHPGAAGHPGEQGQPGPEGSPGAKGYPGRQGFPGPVGDPGPKGSRGYIGLPG 748
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1364-1422 5.07e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 42.48  E-value: 5.07e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 28204656   1364 GQQGQPGHPGPRGRPGPKGSKGEEGPKGKPGKAGPSGRRGTQGLQGLPGPRGVVGRQGP 1422
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1418-1475 5.12e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 42.48  E-value: 5.12e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 28204656   1418 GRQGPEGTAGSDGIPGRDGRPGYQGDQGNDGDPGPVGPAGRRGNPGVAGLPGAQGPPG 1475
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1457-1514 5.81e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 42.09  E-value: 5.81e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 28204656   1457 GRRGNPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRGTEGGTGLPGNQGEPGSKGQPG 1514
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1159-1218 6.48e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 42.09  E-value: 6.48e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1159 GPPGEQGLIGQRGEPGLEGDHGPVGPDGLKGDRGDPGPDGEHGEKGQEGLKGEDGSPGPP 1218
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1448-1507 7.65e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 42.09  E-value: 7.65e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1448 GDPGPVGPAGRRGNPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRGTEGGTGLPGNQGEP 1507
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1463-1520 8.20e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 41.71  E-value: 8.20e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 28204656   1463 GVAGLPGAQGPPGFKGESGLPGQLGPPGKRGTEGGTGLPGNQGEPGSKGQPGDSGEMG 1520
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
318-577 8.38e-05

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 47.23  E-value: 8.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   318 PLSPAKQSARKTPSPSSSASLANSTRVYRPAAAQP-RQITTTSPTKRSPTKP---SVSPLS-------VTPMKSPHATQK 386
Cdd:PLN03209  312 PLTPMEELLAKIPSQRVPPKESDAADGPKPVPTKPvTPEAPSPPIEEEPPQPkavVPRPLSpytayedLKPPTSPIPTPP 391
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   387 TGVPSFTKPVPPTQKPAPFTSYLAPSKASS---PTVRPVQKTFMTPRPPVPSPQPLRPTTGLSKK---FTNPTVAKSKSK 460
Cdd:PLN03209  392 SSSPASSKSVDAVAKPAEPDVVPSPGSASNvpeVEPAQVEAKKTRPLSPYARYEDLKPPTSPSPTaptGVSPSVSSTSSV 471
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   461 TTSWASKPVLARSSvpKTLQQTVLSQSPVSYLGSQTLAPALPPLGVGNPRTMPPTRDSALTPAGSkkfTGRETSKKTRQK 540
Cdd:PLN03209  472 PAVPDTAPATAATD--AAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEVVKVGN---SAPPTALADEQH 546
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 28204656   541 SSPRKPEPLSPGKSARDASPrdlttkPSRPsTPALVL 577
Cdd:PLN03209  547 HAQPKPRPLSPYTMYEDLKP------PTSP-TPSPVL 576
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1038-1096 9.59e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 41.71  E-value: 9.59e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 28204656   1038 RGLPGMRGAKGHRGPRGPDGPAGEQGSKGLKgrvGPRGRPGQPGQQGAAGERGHSGAKG 1096
Cdd:pfam01391    3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGPP---GPPGPPGPPGPPGPPGPPGAPGAPG 58
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1421-1479 9.98e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 41.71  E-value: 9.98e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 28204656   1421 GPEGTAGSDGIPGRDGRPGYQGDQGNDGDPGPVGPAGRRGNPGVAGLPGAQGPPGFKGE 1479
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
751-802 1.09e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 41.32  E-value: 1.09e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 28204656    751 GLPGSDGERGLPGVPGKRGEMGRPGFPGDFGERGPPGLDGNPGEIGLPGPPG 802
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPG 52
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1177-1235 1.12e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 41.32  E-value: 1.12e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 28204656   1177 GDHGPVGPDGLKGDRGDPGPDGEHGEKGQEGLKGEDGSPGPPGITGVPGREGKPGKQGE 1235
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1373-1430 1.19e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 41.32  E-value: 1.19e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 28204656   1373 GPRGRPGPKGSKGEEGPKGKPGKAGPSGRRGTQGLQGLPGPRGVVGRQGPEGTAGSDG 1430
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1346-1403 1.24e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 41.32  E-value: 1.24e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 28204656   1346 GDPGYPGQEGVQGLRGEPGQQGQPGHPGPRGRPGPKGSKGEEGPKGKPGKAGPSGRRG 1403
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
1198-1550 1.55e-04

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 281191 [Multi-domain]  Cd Length: 772  Bit Score: 46.67  E-value: 1.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1198 GEHGEKGQEGLKGEDGSPG--PPGITGVPGREGKPGkQGEKGQRGAKGAKGHQGYLGEMGipgepgppgtpgpkgSRGTL 1275
Cdd:pfam03157  124 GQQPGQGQQGRQPGQGQPGyyPTSSQLQPGQLQQPA-QGQQGQQPGQGQQGQQPGQGQQP---------------GQGQQ 187
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1276 GPTGAPGRMGAQGEPGLAGYNGHKGITGPLGPPGPKGEKGDQGEDGKTEGPPGPPGDRGPVGDRGDRGEPGDPGYP---- 1351
Cdd:pfam03157  188 GQQPGQGQQPGQGQQGQQLGQGQQGYYPTSLQQSGQGQPGYYPTSLQQLGQGQSGYYPTSPQQPGQGQQPGQLQQPaqgq 267
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1352 ----GQEGVQGLRGEPGQQGQPGHPGPRGRPGPKGSKGEEGPKGKPGKAGPSGRRGTQGLQGLPGPRGVVGRQGPEGTAG 1427
Cdd:pfam03157  268 qpeqGQQGQQPGQGQQGQQPGQGQQPGQGQPGYYPTSPQQSGQGQPGYYPTSSQQPTQSQQPGQGQQGQQVGQGQQAQQP 347
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1428 SDGIPGRDGRPGYQGD---QGNDGDPGPVGPAGRRGNPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRGTEGGTGLPGNQ 1504
Cdd:pfam03157  348 GQGQQPGQGQPGYYPTsplQSGQGQPGYYLTSPQQSGQGQQPGQLQQSAQGQKGQQPGQGQQPGQGQQGQQPGQGQQGQQ 427
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 28204656   1505 GEPGSKG----QPGDSGEMGFPGVAGLFGpKGPPGDIGFKGIQGPRGPPG 1550
Cdd:pfam03157  428 PGQGQPGyyptSPQQSGQGQQPGQWQQPG-QGQPGYYPTSPLQPGQGQPG 476
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
685-742 1.57e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 40.94  E-value: 1.57e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 28204656    685 GNPGPLGRKGHKGHPGAAGHPGEQGQPGPEGSPGAKGYPGRQGFPGPVGDPGPKGSRG 742
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1484-1541 1.80e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 40.94  E-value: 1.80e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 28204656   1484 GQLGPPGKRGTEGGTGLPGNQGEPGSKGQPGDSGEMGFPGVAGLFGPKGPPGDIGFKG 1541
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1376-1433 1.91e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 40.94  E-value: 1.91e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 28204656   1376 GRPGPKGSKGEEGPKGKPGKAGPSGRRGTQGLQGLPGPRGVVGRQGPEGTAGSDGIPG 1433
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1394-1453 3.28e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 40.17  E-value: 3.28e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1394 GKAGPSGRRGTQGLQGLPGPRGVVGRQGPEGTAGSDGIPGRDGRPGYQGDQGNDGDPGPV 1453
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1162-1219 4.15e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 39.78  E-value: 4.15e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 28204656   1162 GEQGLIGQRGEPGLEGDHGPVGPDGLKGDRGDPGPDGEHGEKGQEGLKGEDGSPGPPG 1219
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1168-1225 4.53e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 39.78  E-value: 4.53e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 28204656   1168 GQRGEPGLEGDHGPVGPDGLKGDRGDPGPDGEHGEKGQEGLKGEDGSPGPPGITGVPG 1225
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1502-1561 4.58e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 39.78  E-value: 4.58e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1502 GNQGEPGSKGQPGDSGEMGFPGVAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIIGPP 1561
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1379-1438 5.41e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 39.39  E-value: 5.41e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1379 GPKGSKGEEGPKGKPGKAGPSGRRGTQGLQGLPGPRGVVGRQGPEGTAGSDGIPGRDGRP 1438
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1466-1523 5.52e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 39.39  E-value: 5.52e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 28204656   1466 GLPGAQGPPGFKGESGLPGQLGPPGKRGTEGGTGLPGNQGEPGSKGQPGDSGEMGFPG 1523
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
760-819 6.09e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 39.39  E-value: 6.09e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656    760 GLPGVPGKRGEMGRPGFPGDFGERGPPGLDGNPGEIGLPGPPGVLGLIGDTGALGPVGYP 819
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
124-205 6.51e-04

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058  Cd Length: 151  Bit Score: 42.02  E-value: 6.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656  124 KLQLGLQFLPGRTIIHLGPRqsvafdldVHDGRWHHLALELRGRTVTMVTACGQHrVPVPLPsRRDSMLDPQGSFLLGKV 203
Cdd:cd00110   57 RLVLRYDLGSGSLVLSSKTP--------LNDGQWHSVSVERNGRSVTLSVDGERV-VESGSP-GGSALLNLDGPLYLGGL 126

                 ..
gi 28204656  204 NP 205
Cdd:cd00110  127 PE 128
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1361-1550 6.58e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.59  E-value: 6.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656  1361 GEPGQQGQPGHPGPRGRPGPKGS---KGEEGPKGKPGKAGPSGRRGTQGLQGLPGPRGVVGRQGPEGTAGSDGIPGRDGR 1437
Cdd:PRK07764  590 PAPGAAGGEGPPAPASSGPPEEAarpAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656  1438 PGYQGDQGNDGDPGPVGPAGRRGNPGVAGLPGAQGPPGfkgesglpgqlgPPGKRGTEGGTGLPGNQGEPGSKGQPGDSG 1517
Cdd:PRK07764  670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAA------------TPPAGQADDPAAQPPQAAQGASAPSPAADD 737
                         170       180       190
                  ....*....|....*....|....*....|....
gi 28204656  1518 EMGFPGVAGLF-GPKGPPGDIGFKGIQGPRGPPG 1550
Cdd:PRK07764  738 PVPLPPEPDDPpDPAGAPAQPPPPPAPAPAAAPA 771
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1487-1549 6.85e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 39.39  E-value: 6.85e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28204656   1487 GPPGKRGTEGGTGLPGNQGEPGSKGQPGDSGEMGFPGVAglfGPKGPPGDIGFKGIQGPRGPP 1549
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPP---GPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
772-829 7.27e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 39.01  E-value: 7.27e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 28204656    772 GRPGFPGDFGERGPPGLDGNPGEIGLPGPPGVLGLIGDTGALGPVGYPGPKGMKGLMG 829
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1180-1239 7.79e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 39.01  E-value: 7.79e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1180 GPVGPDGLKGDRGDPGPDGEHGEKGQEGLKGEDGSPGPPGITGVPGREGKPGKQGEKGQR 1239
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1183-1241 9.77e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 39.01  E-value: 9.77e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 28204656   1183 GPDGLKGDRGDPGPDGEHGEKGQEGLKGEDGSPGPPGITGVPGREGKPGKQGEKGQRGA 1241
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1340-1382 9.96e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 38.62  E-value: 9.96e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 28204656   1340 GDRGEPGDPGYPGQEGVQGLRGEPGQQGQPGHPGPRGRPGPKG 1382
Cdd:pfam01391   16 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1409-1468 1.11e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 38.62  E-value: 1.11e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1409 GLPGPRGVVGRQGPEGTAGSDGIPGRDGRPGYQGDQGNDGDPGPVGPAGRRGNPGVAGLP 1468
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
PRK12678 PRK12678
transcription termination factor Rho; Provisional
1283-1463 1.23e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 43.35  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656  1283 RMGAQGEPGLAGYNGHKGITGPLGPPGPKGEKGDQGEDGKTEGPPGPPGDRGPVGDRGDRGEPGDPGYPGQEGVQglRGE 1362
Cdd:PRK12678   58 ARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRE--RGE 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656  1363 PGQQGQPGHPGPRGRPGPKGSKGEEGPKGKPGKAGPSGRRGTQGLQGlpgPRGVVGRQGPEGTAGSDGIPGRDGRPGYQG 1442
Cdd:PRK12678  136 AARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQ---AEAERGERGRREERGRDGDDRDRRDRREQG 212
                         170       180
                  ....*....|....*....|.
gi 28204656  1443 DQGNDGDPGPVGpaGRRGNPG 1463
Cdd:PRK12678  213 DRREERGRRDGG--DRRGRRR 231
PHA03169 PHA03169
hypothetical protein; Provisional
1338-1481 1.28e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 43.04  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656  1338 DRGDRGEPGDPGyPGQEGVQGLRGEPGQQGQPGHPGPRGRPGPKGSKGEEGPKGKPGKAGPSGRRGTQGLQGLPgprgvv 1417
Cdd:PHA03169   98 ESVGSPTPSPSG-SAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPS------ 170
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28204656  1418 GRQGPEGTAGSDGIPGRDGRPGYQGDQGNDGDPGPVGPAgrrgNPGVAGLPGAQGPPGFKGESG 1481
Cdd:PHA03169  171 HEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPD----EPGEPQSPTPQQAPSPNTQQA 230
PHA03169 PHA03169
hypothetical protein; Provisional
1313-1452 1.31e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 43.04  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656  1313 EKGDQGEDGKTEGPPGPPGDRGPVGDRGDRGEPGDPGYPGQEGVQGLRGEPGQQGQPGHPGPrGRPGPKGSKGEEGPKGK 1392
Cdd:PHA03169   85 EERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGP-HEPAPPESHNPSPNQQP 163
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28204656  1393 PGKAGPSGRRGTQ---GLQGLPGPRGVVGRQGPEGTAGSDGIPGRDgRPGYQGDQGNDGDPGP 1452
Cdd:PHA03169  164 SSFLQPSHEDSPEepePPTSEPEPDSPGPPQSETPTSSPPPQSPPD-EPGEPQSPTPQQAPSP 225
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
1145-1533 1.40e-03

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: 43.46  E-value: 1.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1145 LPGDSGMKGDLGPLGPPGEQGLIGQRGEPGLEGD--HGPVGPDGLKGDRGDPGPDGEHGEKGQEGlkgedGSPGPPGITG 1222
Cdd:pfam09606   89 LAGQGTRPQMMGPMGPGPGGPMGQQMGGPGTASNllASLGRPQMPMGGAGFPSQMSRVGRMQPGG-----QAGGMMQPSS 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1223 VPGREGKPGKQGEKGQRGAKGAKGHQGylgemgIPGEPGPPGTPGPKGSRGTLGPTGAPGRMGAQgepglAGYNGHKGIT 1302
Cdd:pfam09606  164 GQPGSGTPNQMGPNGGPGQGQAGGMNG------GQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQ-----AQANGGMNPQ 232
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1303 GPLGPPGPKGEKGDQGEDGKTEGPPGPPGDRGPVGDRGDRGEPGDpGYPGqegvQGLRGEPGQQGQPGHPGPRGRPGPKG 1382
Cdd:pfam09606  233 QMGGAPNQVAMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQ-GGPG----QPMGPPGQQPGAMPNVMSIGDQNNYQ 307
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1383 SKGEEGPKGKPGKAGPSGRRGTQGLQGLPGPR-GVVGRQGPEGTAGSDGIPGRDGRPGYQGDQGNDGDPGPVGPAGRRGN 1461
Cdd:pfam09606  308 QQQTRQQQQQQGGNHPAAHQQQMNQSVGQGGQvVALGGLNHLETWNPGNFGGLGANPMQRGQPGMMSSPSPVPGQQVRQV 387
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28204656   1462 PGVAGLPGAQ-------GPPGFKGESGLPGQLGPPGKRGTEGGTGLPGNQGEPGSKGQPGDSGEMGFPGVAGLFGPKGP 1533
Cdd:pfam09606  388 TPNQFMRQSPqpsvpspQGPGSQPPQSHPGGMIPSPALIPSPSPQMSQQPAQQRTIGQDSPGGSLNTPGQSAVNSPLNP 466
PHA03169 PHA03169
hypothetical protein; Provisional
1074-1235 1.57e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 42.65  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656  1074 RGRPGQPGQQGAAGErGHSGAKGFLGIPGPSGPPGAKGLPGEPGSqgpqgpvgPPGEMGPKGPPGAVGEPGLPGDsGMKG 1153
Cdd:PHA03169   81 HGEKEERGQGGPSGS-GSESVGSPTPSPSGSAEELASGLSPENTS--------GSSPESPASHSPPPSPPSHPGP-HEPA 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656  1154 DLGPLGPPGEQGLIGQRGEPGLEGDHGPVGPDGLKGDRGDPGPDGEHGEKGQEGLKG--EDGSPGPPGITGVPGREGKPG 1231
Cdd:PHA03169  151 PPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPpdEPGEPQSPTPQQAPSPNTQQA 230

                  ....
gi 28204656  1232 KQGE 1235
Cdd:PHA03169  231 VEHE 234
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1370-1427 1.61e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 38.24  E-value: 1.61e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 28204656   1370 GHPGPRGRPGPKGSKGEEGPKGKPGKAGPSGRRGTQGLQGLPGPRGVVGRQGPEGTAG 1427
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1436-1493 1.68e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 38.24  E-value: 1.68e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 28204656   1436 GRPGYQGDQGNDGDPGPVGPAGRRGNPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRG 1493
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
PHA03247 PHA03247
large tegument protein UL36; Provisional
301-573 1.73e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   301 PVRSVRPDVSERSCSQTPLSPAKQSARKTPSPSSSASLANSTRVYRP--AAAQPRQITTTSPT---KRSPTKPSVSPLS- 374
Cdd:PHA03247 2618 PPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPrrARRLGRAAQASSPPqrpRRRAARPTVGSLTs 2697
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   375 --------VTPMKSPHATQkTGVPSFTKPV-------PPTQKPAPFTSYLAPSKASSPTVRPVQKTFMTPRPPVPSPQpl 439
Cdd:PHA03247 2698 ladpppppPTPEPAPHALV-SATPLPPGPAaarqaspALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAA-- 2774
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   440 rPTTGLSKKFTNPTVAKSKSKTTSWASKPVLARSSVPKTLQQTVL--SQSPVSYL----GSQTLAPALPPLGVGNPRTM- 512
Cdd:PHA03247 2775 -PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALppAASPAGPLppptSAQPTAPPPPPGPPPPSLPLg 2853
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28204656   513 ------------PPTRDSALTPAGSKKFTGRETSKKTRQKSS------PRKPEPLSPGKSARDASPRDLTTKPSRPSTP 573
Cdd:PHA03247 2854 gsvapggdvrrrPPSRSPAAKPAAPARPPVRRLARPAVSRSTesfalpPDQPERPPQPQAPPPPQPQPQPPPPPQPQPP 2932
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
904-975 1.78e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 38.24  E-value: 1.78e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28204656    904 GDNGPEGMKGKPGARGLPGPPGQLGPEGDEgpmgppgvpgleGQPGRKGFPGRPGLDGSKGEPGDPGRPGPV 975
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPP------------GPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
715-774 1.96e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 37.85  E-value: 1.96e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656    715 GSPGAKGYPGRQGFPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKRGEMGRP 774
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
363-573 2.22e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 42.75  E-value: 2.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   363 RSPTKPsVSPLSVTPMKSPHATQKTGVP-SFTKPVPPTQKPAPftsyLAPSKASSPTVRPVQKTFMTPRPPVPSPQPLRP 441
Cdd:PTZ00449  595 KKPKRP-RSAQRPTRPKSPKLPELLDIPkSPKRPESPKSPKRP----PPPQRPSSPERPEGPKIIKSPKPPKSPKPPFDP 669
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   442 TtgLSKKFTNpTVAKSKSKTTSWASKPVLARSSvpKTLQQTVLSQSPVSYLGSQTLAPALPPLGVGNPRTmPPTRDSALT 521
Cdd:PTZ00449  670 K--FKEKFYD-DYLDAAAKSKETKTTVVLDESF--ESILKETLPETPGTPFTTPRPLPPKLPRDEEFPFE-PIGDPDAEQ 743
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 28204656   522 PAGSKKFTGREtSKKTRQKSSPrkPEPLSPGKSARDASPRDLTTKPSRPSTP 573
Cdd:PTZ00449  744 PDDIEFFTPPE-EERTFFHETP--ADTPLPDILAEEFKEEDIHAETGEPDEA 792
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
141-205 2.69e-03

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 308045  Cd Length: 126  Bit Score: 39.34  E-value: 2.69e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28204656    141 GPRQSVAFDLDVHDGRWHHLALELRGRTVTMVTaCGQHRVPVPLPSRRDsMLDPQGSFLLGKVNP 205
Cdd:pfam02210   39 GPVSLLSSGKPLNDGQWHRVRVSRNGRTLTLSV-DGQTVVSALPPGESL-LLNLNGPLYLGGLPP 101
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1343-1535 2.89e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 2.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656  1343 GEPGDPGYPGQEGVQGlRGEPGQQGQPGHPG-PRGRPGPKGSkgeegpkgkPGKAGPSGRRGTQGLQGLPGPRGVVGRQG 1421
Cdd:PRK07764  590 PAPGAAGGEGPPAPAS-SGPPEEAARPAAPAaPAAPAAPAPA---------GAAAAPAEASAAPAPGVAAPEHHPKHVAV 659
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656  1422 PEGTAGSDGIPGRDGRPGYQGDQGNDGDPGPVGPAGRRGNPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRGTEGGTGLP 1501
Cdd:PRK07764  660 PDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPV 739
                         170       180       190
                  ....*....|....*....|....*....|....
gi 28204656  1502 GNQGEPGSKGQPGDSGEMGfPGVAGLFGPKGPPG 1535
Cdd:PRK07764  740 PLPPEPDDPPDPAGAPAQP-PPPPAPAPAAAPAA 772
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1037-1089 3.38e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 37.47  E-value: 3.38e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 28204656   1037 SRGLPGMRGAKGHRGPRGPDGPAGEQGSKGLKGRVGPRGRPGQPGQQGAAGER 1089
Cdd:pfam01391    8 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1174-1232 3.76e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 37.08  E-value: 3.76e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 28204656   1174 GLEGDHGPVGPDGLKGDRGDPGPDGEHGEKGQEGLKGEDGSPGPPGITGVPGREGKPGK 1232
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
946-995 3.84e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 37.08  E-value: 3.84e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 28204656    946 GQPGRKGFPGRPGLDGSKGEPGDPGRPGPVGEQGLMGFIGLVGEPGIVGE 995
Cdd:pfam01391   10 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1403-1462 4.54e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 37.08  E-value: 4.54e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28204656   1403 GTQGLQGLPGPRGVVGRQGPEGTAGSDGIPGRDGRPGYQGDQGNDGDPGPVGPAGRRGNP 1462
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
784-842 4.72e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 37.08  E-value: 4.72e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 28204656    784 GPPGLDGNPGEIGLPGPPGVLGLIGDTGALGPVGYPGPKGMKGLMGGVGEPGLKGDKGE 842
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1130-1184 5.63e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 36.70  E-value: 5.63e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28204656   1130 EMGPKGPPGAVGEPGLPGDSGMKGDLGPLGPPGEQGLIGQRGEPGLEGDHGPVGP 1184
Cdd:pfam01391    5 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1132-1182 6.60e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 36.31  E-value: 6.60e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 28204656   1132 GPKGPPGAVGEPGLPGDSGMKGDLGPLGPPGEQGLIGQRGEPGLEGDHGPV 1182
Cdd:pfam01391   10 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
781-838 8.61e-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: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 36.31  E-value: 8.61e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 28204656    781 GERGPPGLDGNPGEIGLPGPPGVLGLIGDTGALGPVGYPGPKGMKGLMGGVGEPGLKG 838
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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