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Conserved domains on  [gi|24251209|gb|AAN41263|]
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collagen XXVII proalpha 1 chain precursor [Homo sapiens]

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 ...
1661-1859 4.07e-58

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: 200.62  E-value: 4.07e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   1661 EIFKTLHYLSNLIQSIKTPLGTKENPARVCRDLMDCEQKMVDGTYWVDPNLGCSSDTIEVSCNFThGGQTCLKPITAS-- 1738
Cdd:pfam01410    1 EVFASLKSLNQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCAKDAIKVFCNFE-TGETCIYPDPASip 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   1739 ---------------------KVEF--------AISRVQMNFLHLLSSEVTQHITIHCLNMTVWQ-EGTGQTpaKQAVRF 1788
Cdd:pfam01410   80 rknwwtkenkkhvwfgefmngGSQFsyvddsgpAVGVVQLTFLRLLSTEASQNITYHCKNSVAYMdQATGNL--KKALRL 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24251209   1789 RAWNGQIFEAGG--QFRPEVSMDGCKVQDGRWHQTLFTFRTQDPQQLPIISVDNLPPASSGKQYRLEVGPACF 1859
Cdd:pfam01410  158 LGSNDEELRAEGnsRFTYTVLEDGCSKRTGQWGKTVIEYRTQKTSRLPIVDIAPMDIGGADQEFGVEVGPVCF 230
PHA03247 super family cl33720
large tegument protein UL36; Provisional
274-605 3.79e-14

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 78.44  E-value: 3.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   274 TATPALGSLPAGRGPRGTVAPATPTKPQRTSPTNPHQHMAVGGPAQTPLLPAklsasnaldpmLPASVGGSTRTPRPAAA 353
Cdd:PHA03247 2636 NEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRA-----------ARPTVGSLTSLADPPPP 2704
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   354 QPSQKITATKIPKSLPTKP-------SAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPaekPI 426
Cdd:PHA03247 2705 PPTPEPAPHALVSATPLPPgpaaarqASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP---PR 2781
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   427 QRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTeakitshASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPAT 506
Cdd:PHA03247 2782 RLTRPAVASLSESRESLPSPWDPADPPAAVLAPA-------AALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGG 2854
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   507 MVPPTSGTS---TPRTAPAVPTPGSAPTGSKKPiGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSPR-QPQP 582
Cdd:PHA03247 2855 SVAPGGDVRrrpPSRSPAAKPAAPARPPVRRLA-RPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQpQPPP 2933
                         330       340
                  ....*....|....*....|...
gi 24251209   583 SQQTTPALVLAPAQFLSSSPRPT 605
Cdd:PHA03247 2934 PPPPRPQPPLAPTTDPAGAGEPS 2956
LamG super family cl22861
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
45-220 5.64e-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: 68.92  E-value: 5.64e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209      45 DVDILQRLGLSWTKAGSPAPPGVIPFQSGFIFTQRARLQAPTGTVIPAALGTELALVLSLCSHRVNHAFLFAVRSQKRKL 124
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEPGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYDAQNVR 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209     125 QLGLQFLPGKTVVHL------GSRRSVAF-DLDMHDGRWHHLALELRGRTVTLVTACGQR-RVPVLLPFHrdPALDPGGS 196
Cdd:smart00210   81 QFGLEVDGRANTLLLryqgvdGKQHTVSFrNLPLADGQWHKLALSVSGSSATLYVDCNEIdSRPLDRPGQ--PPIDTDGI 158
                           170       180
                    ....*....|....*....|....
gi 24251209     197 FLFGKMNPHAVQFEGALCQFSIYP 220
Cdd:smart00210  159 EVRGAQAADRKPFQGDLQQLKIVC 182
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
694-752 1.01e-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: 47.10  E-value: 1.01e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 24251209    694 GLPGLSGNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPVGDPGP 752
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
724-783 1.29e-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: 1.29e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    724 GQPGPEGSPGAKGYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKR 783
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1376-1433 3.52e-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: 3.52e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 24251209   1376 GKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVVG 1433
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1478-1535 5.06e-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: 5.06e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 24251209   1478 GVAGLPGAQGPPGFKGESGLPGQLGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMG 1535
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
832-890 3.61e-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: 3.61e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 24251209    832 GYPGPKGMKGLMGSVGEPGLKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPGP 890
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1517-1575 1.45e-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: 1.45e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 24251209   1517 GNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGP 1575
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1146-1199 2.34e-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: 2.34e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 24251209   1146 MGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGP 1199
Cdd:pfam01391    6 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
916-990 2.69e-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: 2.69e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24251209    916 GPPGDNGPEGMKGKPGARGLPGPRGQLGPEGDegpmgppgapglegqPGRKGFPGRPGLDGVKGEPGDPGRPGPV 990
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGP---------------PGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
760-809 7.71e-03

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


:

Pssm-ID: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 36.31  E-value: 7.71e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 24251209    760 GLPGLFGLPGSDGERGLPGVPGKRGKMGMPGFPGVFGERGPPGLDGNPGE 809
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGA 53
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
1661-1859 4.07e-58

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: 200.62  E-value: 4.07e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   1661 EIFKTLHYLSNLIQSIKTPLGTKENPARVCRDLMDCEQKMVDGTYWVDPNLGCSSDTIEVSCNFThGGQTCLKPITAS-- 1738
Cdd:pfam01410    1 EVFASLKSLNQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCAKDAIKVFCNFE-TGETCIYPDPASip 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   1739 ---------------------KVEF--------AISRVQMNFLHLLSSEVTQHITIHCLNMTVWQ-EGTGQTpaKQAVRF 1788
Cdd:pfam01410   80 rknwwtkenkkhvwfgefmngGSQFsyvddsgpAVGVVQLTFLRLLSTEASQNITYHCKNSVAYMdQATGNL--KKALRL 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24251209   1789 RAWNGQIFEAGG--QFRPEVSMDGCKVQDGRWHQTLFTFRTQDPQQLPIISVDNLPPASSGKQYRLEVGPACF 1859
Cdd:pfam01410  158 LGSNDEELRAEGnsRFTYTVLEDGCSKRTGQWGKTVIEYRTQKTSRLPIVDIAPMDIGGADQEFGVEVGPVCF 230
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
1660-1860 3.21e-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: 183.82  E-value: 3.21e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    1660 GEIFKTLHYLSNLIQSIKTPLGTKENPARVCRDLMDCEQKMVDGTYWVDPNLGCSSDTIEVSCNFThGGQTCLKPITAS- 1738
Cdd:smart00038    2 EEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFE-TGETCVSPSPSSi 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    1739 -----------------------KVEFAISR------VQMNFLHLLSSEVTQHITIHCLNMTVWQ-EGTGQTpaKQAVRF 1788
Cdd:smart00038   81 prktwysgkskhvwfgetmnggfKFSYGDSEgppvgvVQLTFLRLLSTEAHQNITYHCKNSVAYMdEATGNL--KKALRL 158
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24251209    1789 RAWNGQIFEAGGQFRP--EVSMDGCKVQDGRWHQTLFTFRTQDPQQLPIISVDNLPPASSGKQYRLEVGPACFL 1860
Cdd:smart00038  159 RGSNDVELSAEGNSKFtyEVLEDGCQKRTGKWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
PHA03247 PHA03247
large tegument protein UL36; Provisional
274-605 3.79e-14

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 78.44  E-value: 3.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   274 TATPALGSLPAGRGPRGTVAPATPTKPQRTSPTNPHQHMAVGGPAQTPLLPAklsasnaldpmLPASVGGSTRTPRPAAA 353
Cdd:PHA03247 2636 NEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRA-----------ARPTVGSLTSLADPPPP 2704
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   354 QPSQKITATKIPKSLPTKP-------SAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPaekPI 426
Cdd:PHA03247 2705 PPTPEPAPHALVSATPLPPgpaaarqASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP---PR 2781
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   427 QRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTeakitshASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPAT 506
Cdd:PHA03247 2782 RLTRPAVASLSESRESLPSPWDPADPPAAVLAPA-------AALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGG 2854
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   507 MVPPTSGTS---TPRTAPAVPTPGSAPTGSKKPiGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSPR-QPQP 582
Cdd:PHA03247 2855 SVAPGGDVRrrpPSRSPAAKPAAPARPPVRRLA-RPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQpQPPP 2933
                         330       340
                  ....*....|....*....|...
gi 24251209   583 SQQTTPALVLAPAQFLSSSPRPT 605
Cdd:PHA03247 2934 PPPPRPQPPLAPTTDPAGAGEPS 2956
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
45-220 5.64e-13

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 68.92  E-value: 5.64e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209      45 DVDILQRLGLSWTKAGSPAPPGVIPFQSGFIFTQRARLQAPTGTVIPAALGTELALVLSLCSHRVNHAFLFAVRSQKRKL 124
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEPGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYDAQNVR 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209     125 QLGLQFLPGKTVVHL------GSRRSVAF-DLDMHDGRWHHLALELRGRTVTLVTACGQR-RVPVLLPFHrdPALDPGGS 196
Cdd:smart00210   81 QFGLEVDGRANTLLLryqgvdGKQHTVSFrNLPLADGQWHKLALSVSGSSATLYVDCNEIdSRPLDRPGQ--PPIDTDGI 158
                           170       180
                    ....*....|....*....|....
gi 24251209     197 FLFGKMNPHAVQFEGALCQFSIYP 220
Cdd:smart00210  159 EVRGAQAADRKPFQGDLQQLKIVC 182
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
271-626 2.05e-09

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: 62.63  E-value: 2.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    271 NLTTATPA---LGSLPAGRGPRGTVAPATPTKPQRTSPTNphqhmAVGGP---AQTPLLPAKLSASNALDPML-PASVGG 343
Cdd:pfam05109  472 DVTSPTPAgttSGASPVTPSPSPRDNGTESKAPDMTSPTS-----AVTTPtpnATSPTPAVTTPTPNATSPTLgKTSPTS 546
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    344 STRTPRPAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSsftksalpTQKQVPPTSRPVPARVSRPAE 423
Cdd:pfam05109  547 AVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTVGE--------TSPQANTTNHTLGGTSSTPVV 618
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    424 KPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIP---TLA-RTEAKITSH-----ASKPASARTSTHKPPPFTAL----SSS 490
Cdd:pfam05109  619 TSPPKNATSAVTTGQHNITSSSTSSMSLRPSSiseTLSpSTSDNSTSHmplltSAHPTGGENITQVTPASTSThhvsTSS 698
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    491 PAPTPGSTRSTRPP---ATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASkkAGPKSSPRKPVPLRPGKAARDVp 567
Cdd:pfam05109  699 PAPRPGTTSQASGPgnsSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTS--TGGKANSTTGGKHTTGHGARTS- 775
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 24251209    568 lSDLTTRPSPRQPQPSQQTTPALVLAPAQFLSSSPRPTSSGYSIFHLAGSTPFPLLMGP 626
Cdd:pfam05109  776 -TEPTTDYGGDSTTPRTRYNATTYLPPSTSSKLRPRWTFTSPPVTTAQATVPVPPTSQP 833
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
694-752 1.01e-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: 47.10  E-value: 1.01e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 24251209    694 GLPGLSGNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPVGDPGP 752
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
724-783 1.29e-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: 1.29e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    724 GQPGPEGSPGAKGYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKR 783
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1376-1433 3.52e-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: 3.52e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 24251209   1376 GKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVVG 1433
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1478-1535 5.06e-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: 5.06e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 24251209   1478 GVAGLPGAQGPPGFKGESGLPGQLGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMG 1535
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
rad23 TIGR00601
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
460-531 2.75e-04

UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273167 [Multi-domain]  Cd Length: 378  Bit Score: 45.27  E-value: 2.75e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24251209    460 TEAKITSHASKPASARTSTHKPPPFTALSSSPAPTpgstrSTRPPATMVPPTSGTSTPRT-APAVPTPGSAPT 531
Cdd:TIGR00601   80 GTGKVAPPAATPTSAPTPTPSPPASPASGMSAAPA-----SAVEEKSPSEESATATAPESpSTSVPSSGSDAA 147
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
832-890 3.61e-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: 3.61e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 24251209    832 GYPGPKGMKGLMGSVGEPGLKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPGP 890
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
136-204 1.23e-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: 40.50  E-value: 1.23e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24251209    136 VVHLGSRRSVAFDLD--MHDGRWHHLALELRGRTVTLVTaCGQRRVPVLLPfHRDPALDPGGSFLFGKMNP 204
Cdd:pfam02210   33 RYDLGSGPVSLLSSGkpLNDGQWHRVRVSRNGRTLTLSV-DGQTVVSALPP-GESLLLNLNGPLYLGGLPP 101
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1517-1575 1.45e-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: 1.45e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 24251209   1517 GNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGP 1575
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1146-1199 2.34e-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: 2.34e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 24251209   1146 MGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGP 1199
Cdd:pfam01391    6 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
916-990 2.69e-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: 2.69e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24251209    916 GPPGDNGPEGMKGKPGARGLPGPRGQLGPEGDegpmgppgapglegqPGRKGFPGRPGLDGVKGEPGDPGRPGPV 990
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGP---------------PGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
760-809 7.71e-03

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


Pssm-ID: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 36.31  E-value: 7.71e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 24251209    760 GLPGLFGLPGSDGERGLPGVPGKRGKMGMPGFPGVFGERGPPGLDGNPGE 809
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGA 53
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
1661-1859 4.07e-58

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: 200.62  E-value: 4.07e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   1661 EIFKTLHYLSNLIQSIKTPLGTKENPARVCRDLMDCEQKMVDGTYWVDPNLGCSSDTIEVSCNFThGGQTCLKPITAS-- 1738
Cdd:pfam01410    1 EVFASLKSLNQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCAKDAIKVFCNFE-TGETCIYPDPASip 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   1739 ---------------------KVEF--------AISRVQMNFLHLLSSEVTQHITIHCLNMTVWQ-EGTGQTpaKQAVRF 1788
Cdd:pfam01410   80 rknwwtkenkkhvwfgefmngGSQFsyvddsgpAVGVVQLTFLRLLSTEASQNITYHCKNSVAYMdQATGNL--KKALRL 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24251209   1789 RAWNGQIFEAGG--QFRPEVSMDGCKVQDGRWHQTLFTFRTQDPQQLPIISVDNLPPASSGKQYRLEVGPACF 1859
Cdd:pfam01410  158 LGSNDEELRAEGnsRFTYTVLEDGCSKRTGQWGKTVIEYRTQKTSRLPIVDIAPMDIGGADQEFGVEVGPVCF 230
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
1660-1860 3.21e-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: 183.82  E-value: 3.21e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    1660 GEIFKTLHYLSNLIQSIKTPLGTKENPARVCRDLMDCEQKMVDGTYWVDPNLGCSSDTIEVSCNFThGGQTCLKPITAS- 1738
Cdd:smart00038    2 EEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFE-TGETCVSPSPSSi 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    1739 -----------------------KVEFAISR------VQMNFLHLLSSEVTQHITIHCLNMTVWQ-EGTGQTpaKQAVRF 1788
Cdd:smart00038   81 prktwysgkskhvwfgetmnggfKFSYGDSEgppvgvVQLTFLRLLSTEAHQNITYHCKNSVAYMdEATGNL--KKALRL 158
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24251209    1789 RAWNGQIFEAGGQFRP--EVSMDGCKVQDGRWHQTLFTFRTQDPQQLPIISVDNLPPASSGKQYRLEVGPACFL 1860
Cdd:smart00038  159 RGSNDVELSAEGNSKFtyEVLEDGCQKRTGKWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
PHA03247 PHA03247
large tegument protein UL36; Provisional
274-605 3.79e-14

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 78.44  E-value: 3.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   274 TATPALGSLPAGRGPRGTVAPATPTKPQRTSPTNPHQHMAVGGPAQTPLLPAklsasnaldpmLPASVGGSTRTPRPAAA 353
Cdd:PHA03247 2636 NEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRA-----------ARPTVGSLTSLADPPPP 2704
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   354 QPSQKITATKIPKSLPTKP-------SAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPaekPI 426
Cdd:PHA03247 2705 PPTPEPAPHALVSATPLPPgpaaarqASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP---PR 2781
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   427 QRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTeakitshASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPAT 506
Cdd:PHA03247 2782 RLTRPAVASLSESRESLPSPWDPADPPAAVLAPA-------AALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGG 2854
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   507 MVPPTSGTS---TPRTAPAVPTPGSAPTGSKKPiGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSPR-QPQP 582
Cdd:PHA03247 2855 SVAPGGDVRrrpPSRSPAAKPAAPARPPVRRLA-RPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQpQPPP 2933
                         330       340
                  ....*....|....*....|...
gi 24251209   583 SQQTTPALVLAPAQFLSSSPRPT 605
Cdd:PHA03247 2934 PPPPRPQPPLAPTTDPAGAGEPS 2956
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
45-220 5.64e-13

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


Pssm-ID: 214560  Cd Length: 184  Bit Score: 68.92  E-value: 5.64e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209      45 DVDILQRLGLSWTKAGSPAPPGVIPFQSGFIFTQRARLQAPTGTVIPAALGTELALVLSLCSHRVNHAFLFAVRSQKRKL 124
Cdd:smart00210    1 GQDLLQVFDLPSLSFAIRQVVGPEPGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYDAQNVR 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209     125 QLGLQFLPGKTVVHL------GSRRSVAF-DLDMHDGRWHHLALELRGRTVTLVTACGQR-RVPVLLPFHrdPALDPGGS 196
Cdd:smart00210   81 QFGLEVDGRANTLLLryqgvdGKQHTVSFrNLPLADGQWHKLALSVSGSSATLYVDCNEIdSRPLDRPGQ--PPIDTDGI 158
                           170       180
                    ....*....|....*....|....
gi 24251209     197 FLFGKMNPHAVQFEGALCQFSIYP 220
Cdd:smart00210  159 EVRGAQAADRKPFQGDLQQLKIVC 182
PHA03247 PHA03247
large tegument protein UL36; Provisional
275-631 1.22e-12

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 73.43  E-value: 1.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   275 ATPALGSLPAG-RGPRGTVAPATPTKPQRTSPTNPhqhmaVGGPAQTPLLPAKLSASNALDPMLP--ASVGGSTRTPRPA 351
Cdd:PHA03247 2593 PQSARPRAPVDdRGDPRGPAPPSPLPPDTHAPDPP-----PPSPSPAANEPDPHPPPTVPPPERPrdDPAPGRVSRPRRA 2667
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   352 AAQpsQKITATKIPKSLPTKPSAPST--SIVPIKSPHPTQKTAPSSFTksalPTQKQVPPTSRPVPARVSRPAE--KPIQ 427
Cdd:PHA03247 2668 RRL--GRAAQASSPPQRPRRRAARPTvgSLTSLADPPPPPPTPEPAPH----ALVSATPLPPGPAAARQASPALpaAPAP 2741
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   428 RNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTEA-----KITSHASKPASARTSTHKPP--PFTALSSSPAPTPGSTRS 500
Cdd:PHA03247 2742 PAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAagpprRLTRPAVASLSESRESLPSPwdPADPPAAVLAPAAALPPA 2821
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   501 TRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKP-VPLRPGKAARDVPLSDLTTRPSP-- 577
Cdd:PHA03247 2822 ASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPaAPARPPVRRLARPAVSRSTESFAlp 2901
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 24251209   578 -----RQPQPSQQTTPALVLAPAQFLSSSPRPTSSGYSIFHLAgstPFPLLMGPPGPKG 631
Cdd:PHA03247 2902 pdqpeRPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLA---PTTDPAGAGEPSG 2957
PHA03247 PHA03247
large tegument protein UL36; Provisional
283-780 6.76e-12

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 71.12  E-value: 6.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   283 PAGRGPRGTVAPATPTKPQRTSPTNPhqhmAVGGPAQTPLLP-----AKLSASNALDP-------MLPASVGGSTRTPRP 350
Cdd:PHA03247 2498 PGGGGPPDPDAPPAPSRLAPAILPDE----PVGEPVHPRMLTwirglEELASDDAGDPppplppaAPPAAPDRSVPPPRP 2573
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   351 AAAQPSQKITATKIPKSLPTKPSAPSTsivPIKSPHPTQKTAPSSftksalPTQKQVPPTSRPVPARVSRPAEKPiqrnp 430
Cdd:PHA03247 2574 APRPSEPAVTSRARRPDAPPQSARPRA---PVDDRGDPRGPAPPS------PLPPDTHAPDPPPPSPSPAANEPD----- 2639
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   431 GMPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHASKPASARTSTHKPP--PFTALSSSPAPTPGSTRSTRPPATMV 508
Cdd:PHA03247 2640 PHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTvgSLTSLADPPPPPPTPEPAPHALVSAT 2719
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   509 PPTSGTSTPRTA----PAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPVPLR-----PGKAARDVPLSDLT----TRP 575
Cdd:PHA03247 2720 PLPPGPAAARQAspalPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAapaagPPRRLTRPAVASLSesreSLP 2799
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   576 SPRQPQPSqqttPALVLAPAQFLSSSPRPTSsgysifhLAGSTPFPLLMGPPGPKGdcGLPGPPGLPGLPGIPGARGPRG 655
Cdd:PHA03247 2800 SPWDPADP----PAAVLAPAAALPPAASPAG-------PLPPPTSAQPTAPPPPPG--PPPPSLPLGGSVAPGGDVRRRP 2866
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   656 PPGPYGNPGLPGPPGAKGQKGDPGLSPgkahdgAKGDMGLPGLSGNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAK 735
Cdd:PHA03247 2867 PSRSPAAKPAAPARPPVRRLARPAVSR------STESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQ 2940
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 24251209   736 GYPGRQGLPGPVGDPGPKGSRGYIG--LPGLFGLPGSDGERGLPGVP 780
Cdd:PHA03247 2941 PPLAPTTDPAGAGEPSGAVPQPWLGalVPGRVAVPRFRVPQPAPSRE 2987
PHA03247 PHA03247
large tegument protein UL36; Provisional
273-576 1.57e-11

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 69.97  E-value: 1.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   273 TTATPALgSLPAGRGPRGTVAPATPTKPqrTSPTNPHQHMAVGGPAQTPLLPAKLSASNALDPMLPASvGGSTRTPRPAA 352
Cdd:PHA03247 2713 HALVSAT-PLPPGPAAARQASPALPAAP--APPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAA-GPPRRLTRPAV 2788
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   353 AQ-------------PSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPP--------TS 411
Cdd:PHA03247 2789 ASlsesreslpspwdPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPggdvrrrpPS 2868
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   412 RPVPARVSRPAEKPIQRnpgmprpppPSTRPLPPTTSSSKKPIPTLARTEakitshaSKPASARTSTHKPPPFTALSSSP 491
Cdd:PHA03247 2869 RSPAAKPAAPARPPVRR---------LARPAVSRSTESFALPPDQPERPP-------QPQAPPPPQPQPQPPPPPQPQPP 2932
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   492 APTPGstrstRPPATMVPPTSGTSTPRTAPAVPTPgsaPTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDL 571
Cdd:PHA03247 2933 PPPPP-----RPQPPLAPTTDPAGAGEPSGAVPQP---WLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRV 3004

                  ....*
gi 24251209   572 TTRPS 576
Cdd:PHA03247 3005 SSWAS 3009
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
271-626 2.05e-09

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: 62.63  E-value: 2.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    271 NLTTATPA---LGSLPAGRGPRGTVAPATPTKPQRTSPTNphqhmAVGGP---AQTPLLPAKLSASNALDPML-PASVGG 343
Cdd:pfam05109  472 DVTSPTPAgttSGASPVTPSPSPRDNGTESKAPDMTSPTS-----AVTTPtpnATSPTPAVTTPTPNATSPTLgKTSPTS 546
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    344 STRTPRPAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSsftksalpTQKQVPPTSRPVPARVSRPAE 423
Cdd:pfam05109  547 AVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTVGE--------TSPQANTTNHTLGGTSSTPVV 618
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    424 KPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIP---TLA-RTEAKITSH-----ASKPASARTSTHKPPPFTAL----SSS 490
Cdd:pfam05109  619 TSPPKNATSAVTTGQHNITSSSTSSMSLRPSSiseTLSpSTSDNSTSHmplltSAHPTGGENITQVTPASTSThhvsTSS 698
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    491 PAPTPGSTRSTRPP---ATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASkkAGPKSSPRKPVPLRPGKAARDVp 567
Cdd:pfam05109  699 PAPRPGTTSQASGPgnsSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTS--TGGKANSTTGGKHTTGHGARTS- 775
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 24251209    568 lSDLTTRPSPRQPQPSQQTTPALVLAPAQFLSSSPRPTSSGYSIFHLAGSTPFPLLMGP 626
Cdd:pfam05109  776 -TEPTTDYGGDSTTPRTRYNATTYLPPSTSSKLRPRWTFTSPPVTTAQATVPVPPTSQP 833
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
272-607 3.77e-08

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 58.64  E-value: 3.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   272 LTTATPALGSLPAGRGPRGTVAPATPTkpqrtSPTNPHQHMAVGGPAQTPLLPAKLSASNALDPMLPASVGGSTRTPRPA 351
Cdd:PHA03307   50 LAAVTVVAGAAACDRFEPPTGPPPGPG-----TEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPA 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   352 AAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKqVPPTSRPVParvSRPAEKPIQRNPG 431
Cdd:PHA03307  125 SPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSS-PEETARAPS---SPPAEPPPSTPPA 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   432 MPRPPPPSTRPLPPTTSSSkkPIPTLARTEAKITSHASKPASARTSTHK------------PPPFTALSSSPAPTPGSTR 499
Cdd:PHA03307  201 AASPRPPRRSSPISASASS--PAPAPGRSAADDAGASSSDSSSSESSGCgwgpenecplprPAPITLPTRIWEASGWNGP 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   500 STRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKK-----PIGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSdltTR 574
Cdd:PHA03307  279 SSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRAsssssSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSP---SR 355
                         330       340       350
                  ....*....|....*....|....*....|...
gi 24251209   575 PSPRQPQPSQQTTPALVLAPAQFLSSSPRPTSS 607
Cdd:PHA03307  356 PPPPADPSSPRKRPRPSRAPSSPAASAGRPTRR 388
PARM pfam17061
PARM; Human PARM-1 is a mucin-like, androgen-regulated transmembrane protein that is present ...
267-533 2.96e-07

PARM; Human PARM-1 is a mucin-like, androgen-regulated transmembrane protein that is present in most tissues, with high levels in the heart, kidney and placenta. It has been shown to be induced and expressed in prostate after castration and may have a role in cell proliferation and immortalisation in prostate cancer.


Pssm-ID: 319112 [Multi-domain]  Cd Length: 296  Bit Score: 54.07  E-value: 2.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    267 LGLENLTTATPALGSLPAGRGPRGTVAPATPTKPQR--TSPTNphqhmavgGPAQTPLLPAKLSASNALdpmLPASVGGS 344
Cdd:pfam17061    2 LRVQSLPTSAPLPVSLPAKITPPTATWTSSPQNTAAvtASPTS--------GTHNNSVLPVTASAPTSP---LPKNISVE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    345 TRTPRPAAAQPSQKITATKipkslPTKPSAPSTSIVPIKSPHPTQKTAPSSFTkSALPTQKQVPPTSrpvPARVSRPAek 424
Cdd:pfam17061   71 PREEEPTSPASNWEGTNTD-----PSPPGLSPTSGGVHLTPTPEEHSSGTPEA-SVPATGSQSPAES---PTLTSPQA-- 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    425 piqrnpgmprppppstrplpptTSSSKKPIPTLArTEAKITSHASKPASARTSTHKPPPFTALSSsPAPTPGSTRSTRPP 504
Cdd:pfam17061  140 ----------------------PASSPSSLSTSP-PEVSSASVTTNHSSTETSTQPTGAPTTPES-PTEEHSSGHTPTSH 195
                          250       260
                   ....*....|....*....|....*....
gi 24251209    505 ATMVPPTSGTSTPRTAPAVPTPGSAPTGS 533
Cdd:pfam17061  196 ATSEPVPTETTPQTTVPAKVTCELIDTET 224
PRK07003 PRK07003
DNA polymerase III subunits gamma and tau; Validated
277-588 4.14e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 54.86  E-value: 4.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   277 PALGslpAGRGPRGTVAPATPTkpqrtsptnphqhmAVGGPAQTPLLPAKLSASnaldPMLPASVGGSTRTPRPAAAQPS 356
Cdd:PRK07003  360 PAVT---GGGAPGGGVPARVAG--------------AVPAPGARAAAAVGASAV----PAVTAVTGAAGAALAPKAAAAA 418
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   357 QKiTATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPAEKPIQRNpgmprpp 436
Cdd:PRK07003  419 AA-TRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAF------- 490
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   437 ppstrplppttsSSKKPIPTLARTEAKITSHASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTR-----PPATMVPPT 511
Cdd:PRK07003  491 ------------EPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAAraggaAAALDVLRN 558
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   512 SG----TSTPRTAPAVPTPGSAPTGSKKPigseaskkagpkSSPRKPVPLRPGKAARDVPLSDLTTRPSPRQPQPSQQTT 587
Cdd:PRK07003  559 AGmrvsSDRGARAAAAAKPAAAPAAAPKP------------AAPRVAVQVPTPRARAATGDAPPNGAARAEQAAESRGAP 626

                  .
gi 24251209   588 P 588
Cdd:PRK07003  627 P 627
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
694-752 1.01e-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: 47.10  E-value: 1.01e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 24251209    694 GLPGLSGNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPVGDPGP 752
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
PHA03247 PHA03247
large tegument protein UL36; Provisional
275-594 1.03e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.17  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   275 ATPALGSLPAGRG-PRGTVAPATPTKPQR-TSPTNPHQHMAVGGPAQTPLLPAKLSASNALDPMLPASVGGSTRTPRPAA 352
Cdd:PHA03247 2731 ASPALPAAPAPPAvPAGPATPGGPARPARpPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAA 2810
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   353 AQPSqkiTATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSAL---------PTQKQVPPT----SRPVPARVS 419
Cdd:PHA03247 2811 VLAP---AAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVapggdvrrrPPSRSPAAKpaapARPPVRRLA 2887
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   420 RPA------------------EKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLA-RTEAKITSHASKPASARTSTHK 480
Cdd:PHA03247 2888 RPAvsrstesfalppdqperpPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLApTTDPAGAGEPSGAVPQPWLGAL 2967
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   481 PPPFTALSSSPAPTPGSTRSTrpPATMVPPTSGTSTPRTAP----------AVPTPGSAPTGSKKPIGSEASKKAGPKSS 550
Cdd:PHA03247 2968 VPGRVAVPRFRVPQPAPSREA--PASSTPPLTGHSLSRVSSwasslalheeTDPPPVSLKQTLWPPDDTEDSDADSLFDS 3045
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 24251209   551 PRKPVPLRPGKAARDVPLSDLTTRPSPRQPQPSQQTTPALVLAP 594
Cdd:PHA03247 3046 DSERSDLEALDPLPPEPHDPFAHEPDPATPEAGARESPSSQFGP 3089
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
688-747 1.27e-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: 47.10  E-value: 1.27e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    688 GAKGDMGLPGLSGNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPV 747
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
PARM pfam17061
PARM; Human PARM-1 is a mucin-like, androgen-regulated transmembrane protein that is present ...
360-578 1.52e-06

PARM; Human PARM-1 is a mucin-like, androgen-regulated transmembrane protein that is present in most tissues, with high levels in the heart, kidney and placenta. It has been shown to be induced and expressed in prostate after castration and may have a role in cell proliferation and immortalisation in prostate cancer.


Pssm-ID: 319112 [Multi-domain]  Cd Length: 296  Bit Score: 51.76  E-value: 1.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    360 TATKIPKSLPTKpSAPSTSIVPIKSPHPTQKTAPSS---FTKSALPTQKQVPPTsrPVPARVS-RPAEKPIQRNPGMPRP 435
Cdd:pfam17061    9 TSAPLPVSLPAK-ITPPTATWTSSPQNTAAVTASPTsgtHNNSVLPVTASAPTS--PLPKNISvEPREEEPTSPASNWEG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    436 PPPSTRPLPPTTSSSKKPIPTLARTEAKITSHASKPASARTSTHKPPpftALSSSPAPTPG-STRSTRPPAtmVPPTSGT 514
Cdd:pfam17061   86 TNTDPSPPGLSPTSGGVHLTPTPEEHSSGTPEASVPATGSQSPAESP---TLTSPQAPASSpSSLSTSPPE--VSSASVT 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24251209    515 STPRTAPAVPTPGSAPTGSKKPIGSEASKK-------AGPKSSPRKPVPLRPGKAARDVPLSDLTTrPSPR 578
Cdd:pfam17061  161 TNHSSTETSTQPTGAPTTPESPTEEHSSGHtptshatSEPVPTETTPQTTVPAKVTCELIDTETTT-TSPR 230
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
268-614 2.06e-06

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: 52.61  E-value: 2.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    268 GLENLTTATPALGSLPAGRGPRGTvAPAT--PTKPQRTSPTNPHQHMAVGGPAQTPLLPAkLSASNALDPMLPASVGGST 345
Cdd:pfam05109  375 GCENISGAFASNRTFDITVSGLGT-APKTliITRTATNATTTTHKVIFSKAPESTTTSPT-LNTTGFAAPNTTTGLPSST 452
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    346 RTPRPAAAQPSQKITATKIPKSLPTkPSAPSTSIVPIK-SPHPTQKTAPSSFTKSALPTQKQVPPT---SRPVPArVSRP 421
Cdd:pfam05109  453 HVPTNLTAPASTGPTVSTADVTSPT-PAGTTSGASPVTpSPSPRDNGTESKAPDMTSPTSAVTTPTpnaTSPTPA-VTTP 530
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    422 AEKPIQrnpgmprppppstrplppttssskkpiPTLARTEakitshaskPASARTSthkPPPftalsSSPAPTPGSTRST 501
Cdd:pfam05109  531 TPNATS---------------------------PTLGKTS---------PTSAVTT---PTP-----NATSPTPAVTTPT 566
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    502 rPPATMvpPTSGTSTPRTAPAVPTP-GSAPT-GSKKPIGSEASKKAGPKSSprKPVPLRPGKAArdvplsdlTTRPSPRQ 579
Cdd:pfam05109  567 -PNATI--PTLGKTSPTSAVTTPTPnATSPTvGETSPQANTTNHTLGGTSS--TPVVTSPPKNA--------TSAVTTGQ 633
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 24251209    580 PQPSQQTTPALVLAPAQfLSSSPRPTSSGYSIFHL 614
Cdd:pfam05109  634 HNITSSSTSSMSLRPSS-ISETLSPSTSDNSTSHM 667
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
700-757 4.65e-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: 4.65e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 24251209    700 GNPGPPGRKGHKGYPGPAGHPGEQGQPGPEGSPGAKGYPGRQGLPGPVGDPGPKGSRG 757
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
283-622 5.57e-06

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteristic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 335243 [Multi-domain]  Cd Length: 980  Bit Score: 51.17  E-value: 5.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    283 PAGRGPRGTVAPATPTKPQRTSPTNPHQHMAVGGPAQTPLLPAKLSASNALDPMLPASVGGSTRTPR-PAAAQPSQKITA 361
Cdd:pfam03154  173 PVLQCQNGVPSPPPGPQTQVATPAPTPSAPSLPSQVSPPTTQPPLQPLPVASPHTLIQQTPTLHPQRlPSPHPPLQPMPD 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    362 TKiPKSLPTKPSAPSTSIVPIKSPHPTQktAPSSFTKSALP---TQKQVPPTSRP-VPARVSRPAEKPIQRNPGMPRPPP 437
Cdd:pfam03154  253 PP-SQVSPQSAPQPGLHGPMPPMPHSLQ--GPSHLPHPGPPqpfGQGQVPPPPSLqAPHPSQLQHTPPSQSQGPSPQPPR 329
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    438 PSTRPLPPTTSSSKKPIPTLArteakiTSHASKPASARTSTH--KPPPFTALSSSPAPTPG-----STRSTRPPATMVPP 510
Cdd:pfam03154  330 EQPLPPAPLSMPHIKPPPTTP------IPQLPNPQSHKHPPHlsAPSPFPQMPSNLPPPPAlkplsSLPTHHPPSAHPPP 403
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    511 TSGTSTPRTAPAVPtpgsaptgSKKPIGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSPRQPQPS-QQTTPA 589
Cdd:pfam03154  404 LQLMPQSQQLPSPP--------AQPPVLTQSQSHPPKASPHPPTAASHSLPSQSPFPQHSFSPSGSPPVTPPSgPPPSPS 475
                          330       340       350
                   ....*....|....*....|....*....|...
gi 24251209    590 LVLAPAQFLSSSPRPTSSGYSIFHLAGSTPFPL 622
Cdd:pfam03154  476 PSMPGLQPPSSSATSVSSSGPVPAAVSCVLPPV 508
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
350-586 8.38e-06

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 50.31  E-value: 8.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   350 PAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSrPVPARVSRPAEKPIQRN 429
Cdd:PLN03209  324 PSQRVPPKESDAADGPKPVPTKPVTPEAPSPPIEEEPPQPKAVVPRPLSPYTAYEDLKPPTS-PIPTPPSSSPASSKSVD 402
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   430 PGMPRPPPPSTRPLPPTTS-SSKKPIPTLARTEAKITSHA-------------SKPASARTSTHKPPPFTALSSSPAPTP 495
Cdd:PLN03209  403 AVAKPAEPDVVPSPGSASNvPEVEPAQVEAKKTRPLSPYAryedlkpptspspTAPTGVSPSVSSTSSVPAVPDTAPATA 482
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   496 GSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTT-- 573
Cdd:PLN03209  483 ATDAAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEVVKVGNSAPPTALADEQHHAQPKPRPLSPYTMye 562
                         250
                  ....*....|....*
gi 24251209   574 --RPsPRQPQPSQQT 586
Cdd:PLN03209  563 dlKP-PTSPTPSPVL 576
PARM pfam17061
PARM; Human PARM-1 is a mucin-like, androgen-regulated transmembrane protein that is present ...
473-607 9.67e-06

PARM; Human PARM-1 is a mucin-like, androgen-regulated transmembrane protein that is present in most tissues, with high levels in the heart, kidney and placenta. It has been shown to be induced and expressed in prostate after castration and may have a role in cell proliferation and immortalisation in prostate cancer.


Pssm-ID: 319112 [Multi-domain]  Cd Length: 296  Bit Score: 49.45  E-value: 9.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    473 SARTSThkPPPFTALSSSPAPTPGSTRStrPPATMVPPTSGTSTPRTAPAVPTPGSAPTG------SKKPIGSEASKKAG 546
Cdd:pfam17061    6 SLPTSA--PLPVSLPAKITPPTATWTSS--PQNTAAVTASPTSGTHNNSVLPVTASAPTSplpkniSVEPREEEPTSPAS 81
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24251209    547 PKSSPRK-PVPLRPGKAARDVPLSDLTTRPSPRQPQPSQQTTPALVLAPAQFLSSSPRPTSS 607
Cdd:pfam17061   82 NWEGTNTdPSPPGLSPTSGGVHLTPTPEEHSSGTPEASVPATGSQSPAESPTLTSPQAPASS 143
PHA03269 PHA03269
envelope glycoprotein C; Provisional
448-556 1.28e-05

envelope glycoprotein C; Provisional


Pssm-ID: 165527  Cd Length: 566  Bit Score: 49.73  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   448 SSSKKPIPTLARTEAkiTSHASKPASARTS--THKPPPFTALSSS------PAPTPGSTRSTRPPATMVPPTSGTSTPRt 519
Cdd:PHA03269   35 AATQKPDPAPAPHQA--ASRAPDPAVAPTSaaSRKPDLAQAPTPAasekfdPAPAPHQAASRAPDPAVAPQLAAAPKPD- 111
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 24251209   520 aPAVPtPGSAPTgskkpiGSEASKKAGPKSSPRKPVP 556
Cdd:PHA03269  112 -AAEA-FTSAAQ------AHEAPADAGTSAASKKPDP 140
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
724-783 1.29e-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: 1.29e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    724 GQPGPEGSPGAKGYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKR 783
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
AF-4 pfam05110
AF-4 proto-oncoprotein; This family consists of AF4 (Proto-oncogene AF4) and FMR2 (Fragile X E ...
348-588 1.42e-05

AF-4 proto-oncoprotein; This family consists of AF4 (Proto-oncogene AF4) and FMR2 (Fragile X E mental retardation syndrome) nuclear proteins. These proteins have been linked to human diseases such as acute lymphoblastic leukaemia and mental retardation. The family also contains a Drosophila AF4 protein homolog Lilliputian which contains an AT-hook domain. Lilliputian represents a novel pair-rule gene that acts in cytoskeleton regulation, segmentation and morphogenesis in Drosophila.


Pssm-ID: 310000 [Multi-domain]  Cd Length: 1142  Bit Score: 50.10  E-value: 1.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    348 PRPAAAQPSQKiTATK------IPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKsalPTQKQVP-PTSRPVPARVSR 420
Cdd:pfam05110  429 PRPPAPEPEPP-TTNKwqldnwLTKVNQPAVPQESSSETPPSDGHQESKEQSQGKSS---TSGQEHPkDSSEPTPKSSSR 504
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    421 PAEKPiqrnpgmprppppstRPLPPTTSSSKKPIPtlarteakitSHASKPASARTSTHKPPPFTALSSSPAPTPGSTRS 500
Cdd:pfam05110  505 APQKP---------------PEGPHPGKRSRQKSP----------AASSEPSQRRTVGKKQPKKPEKASVEEEPKGGLKV 559
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    501 TRPPatmvPPTSGTSTPRTAPAVPTPGSAPTGSK---KPIGSEASKKAGPKSSPRKPVPLRpgkAARDVPLSDLTTRP-- 575
Cdd:pfam05110  560 ESEP----PPEEKDQSSKDRPKVKTKGRPKSGPRkepKSSPRPASEKKKHKSSHKAPPKSR---EFVETDKSSSDSDSpe 632
                          250
                   ....*....|....
gi 24251209    576 -SPRQPQPSQQTTP 588
Cdd:pfam05110  633 rLPLSPLPQSQTPS 646
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
342-588 2.04e-05

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 49.30  E-value: 2.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   342 GGSTRTPRPAAA-QPSQKITATKIPkSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSR 420
Cdd:PTZ00449  555 GEVGKKPGPAKEhKPSKIPTLSKKP-EFPKDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSP 633
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   421 PAEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPI-PTLA-RTEAKITSHASKPASARTSTHKPPPFTALSSSPAP-TPGS 497
Cdd:PTZ00449  634 KRPPPPQRPSSPERPEGPKIIKSPKPPKSPKPPFdPKFKeKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPeTPGT 713
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   498 TRSTRPPATMVPPT--SGTSTPRTAPAVPTPgSAPTGSKKPIGSEASKKAGPKSSPrkpvplRPGKAARDVPLSDLTTRP 575
Cdd:PTZ00449  714 PFTTPRPLPPKLPRdeEFPFEPIGDPDAEQP-DDIEFFTPPEEERTFFHETPADTP------LPDILAEEFKEEDIHAET 786
                         250       260
                  ....*....|....*....|.
gi 24251209   576 S--------PRQPQPSQQTTP 588
Cdd:PTZ00449  787 GepdeamkrPDSPSEHEDKPP 807
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
273-604 2.57e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteristic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 335243 [Multi-domain]  Cd Length: 980  Bit Score: 49.25  E-value: 2.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    273 TTATPALGSLPAGRGPrgtvaPATPTKPQRTSPTNPHQHMAVGGPAQTPLLPAKLSASNALDPMLPASVGGSTRTPR--- 349
Cdd:pfam03154  195 PAPTPSAPSLPSQVSP-----PTTQPPLQPLPVASPHTLIQQTPTLHPQRLPSPHPPLQPMPDPPSQVSPQSAPQPGlhg 269
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    350 PAAAQPSQKITATKIPKSLPTKPSAPSTSIVP--IKSPHPTQ-KTAPSSFTKSalptQKQVPPTSRPV-PARVSRPAEKP 425
Cdd:pfam03154  270 PMPPMPHSLQGPSHLPHPGPPQPFGQGQVPPPpsLQAPHPSQlQHTPPSQSQG----PSPQPPREQPLpPAPLSMPHIKP 345
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    426 iqrnpgmprppppstrplppttsSSKKPIPTLARTEA-KITSHASKPA---SARTSTHKPPPFTALSSSPAPTPGSTRSt 501
Cdd:pfam03154  346 -----------------------PPTTPIPQLPNPQShKHPPHLSAPSpfpQMPSNLPPPPALKPLSSLPTHHPPSAHP- 401
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    502 rPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSPRQP- 580
Cdd:pfam03154  402 -PPLQLMPQSQQLPSPPAQPPVLTQSQSHPPKASPHPPTAASHSLPSQSPFPQHSFSPSGSPPVTPPSGPPPSPSPSMPg 480
                          330       340
                   ....*....|....*....|....*.
gi 24251209    581 --QPSQQTTPALVLAPAQFLSSSPRP 604
Cdd:pfam03154  481 lqPPSSSATSVSSSGPVPAAVSCVLP 506
PHA03269 PHA03269
envelope glycoprotein C; Provisional
399-531 2.62e-05

envelope glycoprotein C; Provisional


Pssm-ID: 165527  Cd Length: 566  Bit Score: 48.96  E-value: 2.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   399 SALPTQKQVPPTSRPVPARVSRPAEKPIQRnpgmprPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHASKPASARTST 478
Cdd:PHA03269   20 ANLNTNIPIPELHTSAATQKPDPAPAPHQA------ASRAPDPAVAPTSAASRKPDLAQAPTPAASEKFDPAPAPHQAAS 93
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 24251209   479 HKPPPFTALSSSPAPTPG-----STRSTRPPATMVPPTSgTSTPRTAPAVPTPGSAPT 531
Cdd:PHA03269   94 RAPDPAVAPQLAAAPKPDaaeafTSAAQAHEAPADAGTS-AASKKPDPAAHTQHSPPP 150
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
372-554 2.76e-05

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 48.92  E-value: 2.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   372 PSAPSTSIVPIKSP---------HPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPAEKPIQrnpgmprppppstrp 442
Cdd:PTZ00449  511 PEGPEASGLPPKAPgdkegeegeHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKEHKPSKIPTL--------------- 575
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   443 lppttssSKKPiptlarTEAKITSHASKPASARTSTHkppPFTALSSSPAPTPgstrsTRPPATMVPPTSGTSTPRTAPA 522
Cdd:PTZ00449  576 -------SKKP------EFPKDPKHPKDPEEPKKPKR---PRSAQRPTRPKSP-----KLPELLDIPKSPKRPESPKSPK 634
                         170       180       190
                  ....*....|....*....|....*....|..
gi 24251209   523 VPTPGSAPTGSKKPIGSEASKKAGPKSSPRKP 554
Cdd:PTZ00449  635 RPPPPQRPSSPERPEGPKIIKSPKPPKSPKPP 666
KAR9 pfam08580
Yeast cortical protein KAR9; The KAR9 protein in Saccharomyces cerevisiae is a cytoskeletal ...
408-628 3.30e-05

Yeast cortical protein KAR9; The KAR9 protein in Saccharomyces cerevisiae is a cytoskeletal protein required for karyogamy, correct positioning of the mitotic spindle and for orientation of cytoplasmic microtubules. KAR9 localizes at the shmoo tip in mating cells and at the tip of the growing bud in anaphase.


Pssm-ID: 312178  Cd Length: 668  Bit Score: 48.64  E-value: 3.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    408 PPTSRPVPARVSRPAEKPIQRNPGMPRPPPPstrplppttSSSKKPIP--TLARTEAKITSHASKPASARTSTHKPPPFT 485
Cdd:pfam08580  417 PATLSANKTPGSSPASSVIMEPVNGPKSNGS---------SSRRGSSFgsGPRAIVSKLRRESKIPQIASTLTKRKSSIP 487
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    486 ALSSSP-------APTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPVPLR 558
Cdd:pfam08580  488 RLSPTPsntitseTPTPASRPPGRPPPPPPNRPRWNASTNTNDLDVGHNFKPLTPTTPSSPTPSRGSRSPSTPPSPSPLS 567
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    559 PGKAARDVP---------------LSDLTTRPSPRQPQPSQQTTPALVLAPAQFLSSSPRPTSSGYSiFHLAGSTPFPLL 623
Cdd:pfam08580  568 RDKSRSPAPtcrsgsrvsrrrasrKPTRIGSPNSRTSLLDEPPYPKLTLSKGLPRTPRSRQSYAGTS-PSRSVSMFSGLG 646

                   ....*
gi 24251209    624 MGPPG 628
Cdd:pfam08580  647 SHRPG 651
PRK10905 PRK10905
cell division protein DamX; Validated
328-549 3.44e-05

cell division protein DamX; Validated


Pssm-ID: 236792 [Multi-domain]  Cd Length: 328  Bit Score: 48.01  E-value: 3.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   328 SASNALDPMLPASVGGSTRTPRPAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIkSPHPTQKTAPSSFTKSALpTQKQV 407
Cdd:PRK10905   33 SGEKSIDLAGNATDQANGVQPAPGTTSAEQTAGNTQQDVSLPPISSTPTQGQTPV-ATDGQQRVEVQGDLNNAL-TQPQN 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   408 PPTSRPVPARVSRPAE----KPIQRNPGMPRPPPPStrplppttSSSKKPIPTLARTEAKItsHASKPASARTSTHKPPP 483
Cdd:PRK10905  111 QQQLNNVAVNSTLPTEpatvAPVRNGNASRQTAKTQ--------TAERPATTRPARKQAVI--EPKKPQATAKTEPKPVA 180
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24251209   484 FTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKS 549
Cdd:PRK10905  181 QTPKRTEPAAPVASTKAPAATSTPAPKETATTAPVQTASPAQTTATPAAGGKTAGNVGSLKSAPSS 246
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1376-1433 3.52e-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: 3.52e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 24251209   1376 GKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVVG 1433
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
PHA03378 PHA03378
EBNA-3B; Provisional
338-595 3.62e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 48.52  E-value: 3.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   338 PASVGGSTRTPRPAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSfTKSALPTQ---KQVPPTSRPV 414
Cdd:PHA03378  553 PASTEPVHDQLLPAPGLGPLQIQPLTSPTTSQLASSAPSYAQTPWPVPHPSQTPEPPT-TQSHIPETsapRQWPMPLRPI 631
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   415 PARVSR-----------------PAEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKP--IPTLARTEAKITSHASKPASAR 475
Cdd:PHA03378  632 PMRPLRmqpitfnvlvfptphqpPQVEITPYKPTWTQIGHIPYQPSPTGANTMLPIqwAPGTMQPPPRAPTPMRPPAAPP 711
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   476 TSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTpRTAPAVPTPGSAPTgskkpigseaskkagPKSSPRKPV 555
Cdd:PHA03378  712 GRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPG-RARPPAAAPGRARP---------------PAAAPGAPT 775
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 24251209   556 PLRPGKAArDVPLSDLTTRPSPrQPQPSQQTTPALVLAPA 595
Cdd:PHA03378  776 PQPPPQAP-PAPQQRPRGAPTP-QPPPQAGPTSMQLMPRA 813
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
273-595 4.57e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteristic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 335243 [Multi-domain]  Cd Length: 980  Bit Score: 48.48  E-value: 4.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    273 TTATPALGSLPAGRGPRGTVAPATP---------TKPQRTSPTNPHQHMAVGGPAQTPLLPAKLSASNALDPMLPASVGG 343
Cdd:pfam03154  201 APSLPSQVSPPTTQPPLQPLPVASPhtliqqtptLHPQRLPSPHPPLQPMPDPPSQVSPQSAPQPGLHGPMPPMPHSLQG 280
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    344 STRTPRPAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPAE 423
Cdd:pfam03154  281 PSHLPHPGPPQPFGQGQVPPPPSLQAPHPSQLQHTPPSQSQGPSPQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQSH 360
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    424 KPIQRNPGMPRPPPPSTR-------------PLPPTTSSSKKPIPTLARTEAKITSHASKPASARTSTHKPPPftalSSS 490
Cdd:pfam03154  361 KHPPHLSAPSPFPQMPSNlppppalkplsslPTHHPPSAHPPPLQLMPQSQQLPSPPAQPPVLTQSQSHPPKA----SPH 436
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    491 PAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSK-KPIGSEASKKAGPKSSPRKPVPLRPGKAARDVPLS 569
Cdd:pfam03154  437 PPTAASHSLPSQSPFPQHSFSPSGSPPVTPPSGPPPSPSPSMPGlQPPSSSATSVSSSGPVPAAVSCVLPPVQIKEEPLD 516
                          330       340
                   ....*....|....*....|....*.
gi 24251209    570 DLTTRPSPRQPQPSQQTTPALVLAPA 595
Cdd:pfam03154  517 EEEEPESPPPPPRSPSPEPTVVNTPS 542
Retinal pfam15449
Retinal protein; This family of proteins is found in the photoreceptor cells of the retina. ...
273-604 4.89e-05

Retinal protein; This family of proteins is found in the photoreceptor cells of the retina. Mutations of the gene encoding this protein have been associated with retinal disorders such as retinitis pigmentosa and late-onset progressive retinal atrophy. The function of this family of proteins is unknown, but it is likely to be important in the development and function of the retina.


Pssm-ID: 317802 [Multi-domain]  Cd Length: 1292  Bit Score: 48.25  E-value: 4.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    273 TTATPalgSLPAGRGPRGTVAPATPTKPqrTSPTNpHQHMAVGGPAQTPLLPAKLSASNALDPML----------PASVG 342
Cdd:pfam15449  908 STASP---TRPRSTGPGSSKSGCNPRKL--ALDLN-HPPAASHNPEAEGGAQSQAQAEEAASLSKqpqkaipwhhSSHTS 981
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    343 GSTRTPRPAAAQPSQKitatkipkslPTKPSAPSTSivPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPa 422
Cdd:pfam15449  982 GQSRTSEPSLARPTRG----------PHSPEAPRQS--QERSPPLVRKASPTRAHWAPRADRRHPSLPSSHRPAQPSLP- 1048
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    423 ekpiqrnpgmprppppstrplppttSSSKKPIPTLarteakiTSHASKPASARTSThkPPPFTALSSSPA------PTPG 496
Cdd:pfam15449 1049 -------------------------TVQRSPSPPL-------SPAPSPPASPRVLS--PPTSKKRTSPPPqhklpsPPPE 1094
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    497 STRSTRPPATmvPPTSGT--STPRTAPAVPTPGSAPTGSKKPIGSE----ASKKAG------------------PKSSPR 552
Cdd:pfam15449 1095 SPQAQHKLSS--PPTQRTeaSSPSSGPSPSPPTSPSQGPKETRDSEdsqaATAKASgntcsifcpatsslfeakSPFSTA 1172
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 24251209    553 KPVPLRPGKAARDVPLSDLTTRPSPRQPQPSQQTTPALVLAPAQFL---SSSPRP 604
Cdd:pfam15449 1173 HPLPPPEAGGPLGTPAGGWRSSSGPRLRADSQRRMALCALNPQPFVrrtASDRRP 1227
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1478-1535 5.06e-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: 5.06e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 24251209   1478 GVAGLPGAQGPPGFKGESGLPGQLGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMG 1535
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
PRK12323 PRK12323
DNA polymerase III subunits gamma and tau; Provisional
453-629 5.28e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 47.95  E-value: 5.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   453 PIPTLARTEAKITSHASKPASA---RTSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSA 529
Cdd:PRK12323  374 PATAAAAPVAQPAPAAAAPAAAapaPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPA 453
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   530 PTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAArdvplsdlttrpsprQPQPSQQTTPALVLAPAQFLSSSPRPTSSGY 609
Cdd:PRK12323  454 PAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAA---------------APAPADDDPPPWEELPPEFASPAPAQPDAAP 518
                         170       180
                  ....*....|....*....|
gi 24251209   610 SIFHLAgSTPFPLLMGPPGP 629
Cdd:PRK12323  519 AGWVAE-SIPDPATADPDDA 537
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1463-1517 6.53e-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: 6.53e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 24251209   1463 GDPGPMGPAGKRGNPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRGTEGRTGLPG 1517
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1472-1529 7.06e-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: 7.06e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 24251209   1472 GKRGNPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRGTEGRTGLPGNQGEPGSKGQPG 1529
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1361-1418 8.60e-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: 8.60e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 24251209   1361 GDPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRG 1418
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
PRK12323 PRK12323
DNA polymerase III subunits gamma and tau; Provisional
283-529 8.71e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 47.18  E-value: 8.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   283 PAGRGprGTVAPATPTKPQRTSPTNPHQHMAVGGPAQTPLLPAKLSASNALDPMLPASVGGSTRTPRPAAAQPSQKITAT 362
Cdd:PRK12323  365 PGQSG--GGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASAR 442
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   363 KiPKSLPTKPSAPSTSIVPIKSPhPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPAEKPiqrnpgmprppppstrp 442
Cdd:PRK12323  443 G-PGGAPAPAPAPAAAPAAAARP-AAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELP----------------- 503
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   443 lppttssSKKPIPTLARTEAKITSHASKPASARTSTHKPPPFTALSSSP--APTPGSTRSTRPPATMVPPTSGTSTPRTA 520
Cdd:PRK12323  504 -------PEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPaaAPAPRAAAATEPVVAPRPPRASASGLPDM 576

                  ....*....
gi 24251209   521 PAVPTPGSA 529
Cdd:PRK12323  577 FDGDWPALA 585
Spc7_N pfam15402
N-terminus of kinetochore NMS complex subunit Spc7;
448-601 9.03e-05

N-terminus of kinetochore NMS complex subunit Spc7;


Pssm-ID: 317767  Cd Length: 913  Bit Score: 47.43  E-value: 9.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    448 SSSKKPIPtlaRTEAKITSHASKPASA-------RTSTHKPPPFTALSSSPAPTPGSTRSTrPPATMVPPTSGTSTPRTA 520
Cdd:pfam15402  622 SPPKSPVT---FHVAPVASESGSPSLAsvrsrptRQSLGRRESTTPTSKSPQSSPVKNTST-PSKQSTPRVARPSTPAKT 697
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    521 PAVPTPGSAPTGSKKPIGSEaskkagPKSSPRKPVPLRPGKaardvplsdLTTRPSprqpqPSQQTTPALVLAPAQFLSS 600
Cdd:pfam15402  698 PPSSKVGFRSASPKKLFQPE------LQSTASKAKSPGRKS---------LFGQNA-----TTGQSTPSFVLKPHRRRRS 757

                   .
gi 24251209    601 S 601
Cdd:pfam15402  758 S 758
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1382-1439 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 24251209   1382 GQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVVGRQGLEG 1439
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
SAP130_C pfam16014
Histone deacetylase complex subunit SAP130 C-terminus;
322-518 1.16e-04

Histone deacetylase complex subunit SAP130 C-terminus;


Pssm-ID: 318271 [Multi-domain]  Cd Length: 405  Bit Score: 46.48  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    322 LLPAKLSASNAldPMLPASVGGSTRTPRPAAAQPSQKITATKIPkslptkPSAPSTSIVPIKSPHPTQKTA--PSSFTKS 399
Cdd:pfam16014   26 LIPAQPGEATS--PRVDSGIRSTSGSPRPAGAKPKPDIHVAVAP------PVTVAVEALSGQSSDQQTASAlpPSQHPAQ 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    400 ALPTQKQVP-PTSRPVPARVSRPAEKPIqrNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKItshaSKPASARTST 478
Cdd:pfam16014   98 AIPTLLAAAsPPSQPSAALSALPAAMAV--TPPIASMANVVAPPTQPAASSTPACAISSVLPEIKI----KQEAEPMDTS 171
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 24251209    479 HKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPR 518
Cdd:pfam16014  172 QPVPPLTPNSVAPALTSLANNLSVPAGDLLPGASPRKKPR 211
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
317-628 1.21e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteristic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 335243 [Multi-domain]  Cd Length: 980  Bit Score: 46.94  E-value: 1.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    317 PAQTPLL----PAKLSASNALDPMLPASVGGSTRTPRPAA-AQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKT 391
Cdd:pfam03154  162 SAQQQILqtqpPVLQCQNGVPSPPPGPQTQVATPAPTPSApSLPSQVSPPTTQPPLQPLPVASPHTLIQQTPTLHPQRLP 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    392 APSSFTKSALPTQKQVPPTSRPVPARVSR--------------PAEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTL 457
Cdd:pfam03154  242 SPHPPLQPMPDPPSQVSPQSAPQPGLHGPmppmphslqgpshlPHPGPPQPFGQGQVPPPPSLQAPHPSQLQHTPPSQSQ 321
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    458 ARTEAKITSHASKPASARTSTHKPPPFTALSSSPAPtpgstRSTRPPATMVPPTSGTSTPRTAPAVPtpgsaptgSKKPI 537
Cdd:pfam03154  322 GPSPQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNP-----QSHKHPPHLSAPSPFPQMPSNLPPPP--------ALKPL 388
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    538 GSEASKKagPKSSPRKPVPLRPgkaardvplsdlttRPSPRQPQPSQqtTPALVLAPAQFLSSSPRPTSSGysIFHLAGS 617
Cdd:pfam03154  389 SSLPTHH--PPSAHPPPLQLMP--------------QSQQLPSPPAQ--PPVLTQSQSHPPKASPHPPTAA--SHSLPSQ 448
                          330
                   ....*....|.
gi 24251209    618 TPFPLLMGPPG 628
Cdd:pfam03154  449 SPFPQHSFSPS 459
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1379-1436 1.71e-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: 1.71e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 24251209   1379 GQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVVGRQG 1436
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
468-608 1.90e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 46.25  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   468 ASKPASARTSTHKPPPFTALSSSPAPTP--GSTRSTRPPATMVPPtsgtsTPRTAPAVPTPGSAPtgskkpigSEASKKA 545
Cdd:PRK14951  370 AEAAAPAEKKTPARPEAAAPAAAPVAQAaaAPAPAAAPAAAASAP-----AAPPAAAPPAPVAAP--------AAAAPAA 436
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24251209   546 GPKSSPRkPVPLRPGKAARDVP-LSDLTTRPSPRQPQPSQQTTPALVLAPAqflssSPRPTSSG 608
Cdd:PRK14951  437 APAAAPA-AVALAPAPPAQAAPeTVAIPVRVAPEPAVASAAPAPAAAPAAA-----RLTPTEEG 494
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1373-1430 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 24251209   1373 GLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRG 1430
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
335-629 2.20e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteristic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 335243 [Multi-domain]  Cd Length: 980  Bit Score: 46.17  E-value: 2.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    335 PMLPASVGGSTRTPRPAAAQPSQKIT-ATKIPKSLPTKPSAPSTSiVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRP 413
Cdd:pfam03154  147 PSIPSPQDNESDSDSSAQQQILQTQPpVLQCQNGVPSPPPGPQTQ-VATPAPTPSAPSLPSQVSPPTTQPPLQPLPVASP 225
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    414 VPARVSRPAEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPtlaRTEAKITSHASKPASARTSTHKPPPFTALSSSPAP 493
Cdd:pfam03154  226 HTLIQQTPTLHPQRLPSPHPPLQPMPDPPSQVSPQSAPQPGL---HGPMPPMPHSLQGPSHLPHPGPPQPFGQGQVPPPP 302
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    494 TPG----STRSTRPPATMVPPTSgtSTPRTAPAVPTPGSA------PTGSKKPIGSEASKKAGPKSSPRKPVP-----LR 558
Cdd:pfam03154  303 SLQaphpSQLQHTPPSQSQGPSP--QPPREQPLPPAPLSMphikppPTTPIPQLPNPQSHKHPPHLSAPSPFPqmpsnLP 380
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24251209    559 PGKAARdvPLSDLTTRPSPRQPQPSQQTTP---ALVLAPAQFLSSSPRPTSSGYSIFHLAGSTPFPLLMGPPGP 629
Cdd:pfam03154  381 PPPALK--PLSSLPTHHPPSAHPPPLQLMPqsqQLPSPPAQPPVLTQSQSHPPKASPHPPTAASHSLPSQSPFP 452
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1388-1447 2.21e-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: 40.55  E-value: 2.21e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   1388 GPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVVGRQGLEGIAGPDGLP 1447
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
PRK12323 PRK12323
DNA polymerase III subunits gamma and tau; Provisional
338-531 2.31e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 46.02  E-value: 2.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   338 PASVGGSTRTPRPAAAQPSQKITATKIPKSL---PTKPSAPSTSIVPIKSPHPTQKTAPS--SFTKSALPTQKQV----- 407
Cdd:PRK12323  365 PGQSGGGAGPATAAAAPVAQPAPAAAAPAAAapaPAAPPAAPAAAPAAAAAARAVAAAPArrSPAPEALAAARQAsargp 444
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   408 ------PPTSRPVPARVSRPAEKPIQRNPGMpRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHASKPASARTSTHKP 481
Cdd:PRK12323  445 ggapapAPAPAAAPAAAARPAAAGPRPVAAA-AAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVA 523
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 24251209   482 PPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPT 531
Cdd:PRK12323  524 ESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGL 573
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1475-1533 2.34e-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: 40.55  E-value: 2.34e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 24251209   1475 GNPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGE 1533
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1370-1429 2.61e-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: 40.55  E-value: 2.61e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   1370 GVQGLRGKPGQQGQPGHPGPRGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPR 1429
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
rad23 TIGR00601
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
460-531 2.75e-04

UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273167 [Multi-domain]  Cd Length: 378  Bit Score: 45.27  E-value: 2.75e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24251209    460 TEAKITSHASKPASARTSTHKPPPFTALSSSPAPTpgstrSTRPPATMVPPTSGTSTPRT-APAVPTPGSAPT 531
Cdd:TIGR00601   80 GTGKVAPPAATPTSAPTPTPSPPASPASGMSAAPA-----SAVEEKSPSEESATATAPESpSTSVPSSGSDAA 147
SAP130_C pfam16014
Histone deacetylase complex subunit SAP130 C-terminus;
455-585 2.93e-04

Histone deacetylase complex subunit SAP130 C-terminus;


Pssm-ID: 318271 [Multi-domain]  Cd Length: 405  Bit Score: 45.33  E-value: 2.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    455 PTLARTEAKITSHASKP--ASARTSTHKPPPFTALSSSPAPT--PGSTRSTRPPATMVPP----TSGTSTPRTAPAVPTP 526
Cdd:pfam16014   68 PVTVAVEALSGQSSDQQtaSALPPSQHPAQAIPTLLAAASPPsqPSAALSALPAAMAVTPpiasMANVVAPPTQPAASST 147
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24251209    527 GSAPTGSKKP---IGSEA----SKKAGPKSSPRKPVP-LRPGKAARDVPLSDLTTRPSPRQPQPSQQ 585
Cdd:pfam16014  148 PACAISSVLPeikIKQEAepmdTSQPVPPLTPNSVAPaLTSLANNLSVPAGDLLPGASPRKKPRKQQ 214
SOG2 pfam10428
RAM signalling pathway protein; SOG2 proteins in Saccharomyces cerevisiae are involved in cell ...
467-620 3.46e-04

RAM signalling pathway protein; SOG2 proteins in Saccharomyces cerevisiae are involved in cell separation and cytokinesis.


Pssm-ID: 337747  Cd Length: 430  Bit Score: 45.00  E-value: 3.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    467 HASKPASARTSTHKPPPFTALSSSPAPTPGStrSTRPPATMVPPTSGTStPRTAPAVPTPGSAPTGSkkpigseASKKAG 546
Cdd:pfam10428  157 EAVKPLLRAGRTKSPSPSITSGGSPSPPALS--STRSGSSSRTPTPRRR-SRSDTTIPHPGGNLSSP-------APNGAT 226
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24251209    547 PKSSPRKPVPLRPgkaardVPLSDLTTRPSPRQPQPSQQTTPALvlapaqfLSSSPRPTSSGYSIFHLAGSTPF 620
Cdd:pfam10428  227 PISSASSPGAIPR------PLDSSPRSRSSSRSNTLASTSPPSS-------LASTPRSGESFASTSTGSRINPL 287
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
832-890 3.61e-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: 3.61e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 24251209    832 GYPGPKGMKGLMGSVGEPGLKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPGP 890
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
PHA03247 PHA03247
large tegument protein UL36; Provisional
453-632 4.16e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 4.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   453 PIPTLARTE-AKITSHASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAP---------- 521
Cdd:PHA03247  255 PAPPPVVGEgADRAPETARGATGPPPPPEAAAPNGAAAPPDGVWGAALAGAPLALPAPPDPPPPAPAGDAeeeddedgam 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   522 --AVPTP---GSAPTGSKK-------PIGSEASKKAGPKSSPRKPVPLRPGKAARDV-------PLSDLTTRPSPRQPQP 582
Cdd:PHA03247  335 evVSPLPrprQHYPLGFPKrrrptwtPPSSLEDLSAGRHHPKRASLPTRKRRSARHAatpfargPGGDDQTRPAAPVPAS 414
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 24251209   583 SQQTTPALVLAPAQFLSSSPRPTSSGYSifhlAGSTPFPLLMGPPGPKGD 632
Cdd:PHA03247  415 VPTPAPTPVPASAPPPPATPLPSAEPGS----DDGPAPPPERQPPAPATE 460
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1499-1556 5.35e-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: 5.35e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 24251209   1499 GQLGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIGFKG 1556
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
468-582 5.69e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 44.47  E-value: 5.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   468 ASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVP--TPGSAPTGSKKPIGSEASKKA 545
Cdd:PRK07994  358 AFHPAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPlpETTSQLLAARQQLQRAQGATK 437
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 24251209   546 GPKSSPRKPVPLRPGKAARDvPLSDLTTRPSPRQPQP 582
Cdd:PRK07994  438 AKKSEPAAASRARPVNSALE-RLASVRPAPSALEKAP 473
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
733-790 5.85e-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: 5.85e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 24251209    733 GAKGYPGRQGLPGPVGDPGPKGSRGYIGLPGLFGLPGSDGERGLPGVPGKRGKMGMPG 790
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
PRK00708 PRK00708
sec-independent translocase; Provisional
487-589 6.16e-04

sec-independent translocase; Provisional


Pssm-ID: 234818 [Multi-domain]  Cd Length: 209  Bit Score: 42.88  E-value: 6.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   487 LSSSPAPTPGSTRStrPPATMVPPTSGTSTPRTAPAVPTPGSAPtgskKPIGSEASKKAGPKsSPRKPVPLRPGKAARDV 566
Cdd:PRK00708   96 LQKATSMSEPATEN--KPAEVTTPVEPMGLPETPPAVPVPAPAP----AVAAAAAQAAAAPK-APAKPRAKSPRPAAKAA 168
                          90       100
                  ....*....|....*....|...
gi 24251209   567 PlsdlttRPSPRQPQPSQQTTPA 589
Cdd:PRK00708  169 P------KPTETITAKKAKKTAA 185
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1490-1549 6.26e-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: 6.26e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   1490 GFKGESGLPGQLGPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPP 1549
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
PRK12323 PRK12323
DNA polymerase III subunits gamma and tau; Provisional
275-529 6.63e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.48  E-value: 6.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   275 ATPALGSLPAGRGPRgtVAPATPTKPQRTSPTNPHQHMAVGGPAQTPllPAKLSASNALDPMLPASVGGSTRTPRPAAAQ 354
Cdd:PRK12323  379 AAPVAQPAPAAAAPA--AAAPAPAAPPAAPAAAPAAAAAARAVAAAP--ARRSPAPEALAAARQASARGPGGAPAPAPAP 454
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   355 PSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPssftksalptqkQVPPTSRPVPARVSRPAEKPIQrnpgmpr 434
Cdd:PRK12323  455 AAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPAD------------DDPPPWEELPPEFASPAPAQPD------- 515
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   435 ppppstrplppttssskkPIPTLARTEAkITSHASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPP---ATMVPPT 511
Cdd:PRK12323  516 ------------------AAPAGWVAES-IPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPrasASGLPDM 576
                         250
                  ....*....|....*...
gi 24251209   512 SGTSTPRTAPAVPTPGSA 529
Cdd:PRK12323  577 FDGDWPALAARLPVRGLA 594
motB PRK12799
flagellar motor protein MotB; Reviewed
463-606 7.55e-04

flagellar motor protein MotB; Reviewed


Pssm-ID: 183756 [Multi-domain]  Cd Length: 421  Bit Score: 43.94  E-value: 7.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   463 KITSHASKPASArtsthkPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGsapTGSKKPIGSEAS 542
Cdd:PRK12799  292 QIDTHGTVPVAA------VTPSSAVTQSSAITPSSAAIPSPAVIPSSVTTQSATTTQASAVALSS---AGVLPSDVTLPG 362
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24251209   543 KKAGPKSSPRKPVPlRPGKAARDVPLSDLTTRPSPRQPqpsqqtTPALVLAPAQflSSSPRPTS 606
Cdd:PRK12799  363 TVALPAAEPVNMQP-QPMSTTETQQSSTGNITSTANGP------TTSLPAAPAS--NIPVSPTS 417
minC PRK00030
septum formation inhibitor; Provisional
479-612 7.70e-04

septum formation inhibitor; Provisional


Pssm-ID: 178806 [Multi-domain]  Cd Length: 292  Bit Score: 43.53  E-value: 7.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   479 HKPPPF----------TALSSSPAPTPGSTRSTRPPATMVP-PTSGTSTPrtAPAVPTpGSAPTGSKKPIGSEASKKAGP 547
Cdd:PRK00030   73 HNLPPIgvvaeganlqGARDAGLVPVELSTPVARAPQVIDTaPPNDVATP--VPSVPE-ATAEAAAKAGPQDDEADGEQA 149
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24251209   548 KSSPRKPVPLRPGKAARDVPLSdltTRPSPRQPQPSQqttpALVLApaqflssspRPTSSGYSIF 612
Cdd:PRK00030  150 DEAPAHNPESVPTRAARETTEA---NRPTATPPQSSS----ALVIT---------KPLRSGQRVY 198
NPAT_C pfam15712
NPAT C-terminus;
290-552 8.09e-04

NPAT C-terminus;


Pssm-ID: 339523  Cd Length: 677  Bit Score: 44.10  E-value: 8.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    290 GTVAPAT---PTKPQRTSPTNPHQHMAVGgPAQTPLLP---AKLSASnALDPMLPASVG-------GSTRTprpAAAQPS 356
Cdd:pfam15712  136 GNSAPLAsqpPPPQQLQTPPRSNSVFAVN-QAVSPNFSqgsAIIIAS-PVQPVLQGMVGmipvsvvGQNGN---AFSAPS 210
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    357 QKITatkipkSLPTKPSAPSTSIVPIKSPHPTQKtAPSsfTKSALPTQKQVPPTSRPVparvSRPAEKPIQRnpgmprpp 436
Cdd:pfam15712  211 QQVL------HMPLAAPVCNRSIPKLPIPPKSQK-IPG--LRNKPNTGKQVNSLTDSS----SHPVGSRTQR-------- 269
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    437 pPSTRPLPPTTSSSKKPIPTLARTEAKITSHASKPASartSTHKPPPFTALSSSPAPTPGSTRSTRPpatmvpptsgTST 516
Cdd:pfam15712  270 -TENSDKNIATDLGKKLEETTVPFSTESTVPSSKPFE---SHRRVLCFDNLTSPVANTQGSNNKSTS----------QNK 335
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 24251209    517 PRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPR 552
Cdd:pfam15712  336 ERNENSFFSVDSPGASSALSPSTQASKREKEKTLPR 371
KAR9 pfam08580
Yeast cortical protein KAR9; The KAR9 protein in Saccharomyces cerevisiae is a cytoskeletal ...
448-630 8.20e-04

Yeast cortical protein KAR9; The KAR9 protein in Saccharomyces cerevisiae is a cytoskeletal protein required for karyogamy, correct positioning of the mitotic spindle and for orientation of cytoplasmic microtubules. KAR9 localizes at the shmoo tip in mating cells and at the tip of the growing bud in anaphase.


Pssm-ID: 312178  Cd Length: 668  Bit Score: 44.01  E-value: 8.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    448 SSSKKPIptLARTEAKITSHASKPASARTSTHKPPPFTALSSSPA---------PTPGSTRSTRPPATmvpPTSGTSTPR 518
Cdd:pfam08580  421 SANKTPG--SSPASSVIMEPVNGPKSNGSSSRRGSSFGSGPRAIVsklrreskiPQIASTLTKRKSSI---PRLSPTPSN 495
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    519 TAPAV-PTPGSAPTGSKKPigseaskkaGPKSSPRKPVPLRPGKAARDVPLSDLT-TRPSPRQPQPSQ--QTTPALVLAP 594
Cdd:pfam08580  496 TITSEtPTPASRPPGRPPP---------PPPNRPRWNASTNTNDLDVGHNFKPLTpTTPSSPTPSRGSrsPSTPPSPSPL 566
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 24251209    595 AQFLSSSPRPTSSGYSIFHLAGSTPFPLLMGPPGPK 630
Cdd:pfam08580  567 SRDKSRSPAPTCRSGSRVSRRRASRKPTRIGSPNSR 602
DUF4045 pfam13254
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ...
280-588 8.28e-04

Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and eukaryotes, and is typically between 384 and 430 amino acids in length.


Pssm-ID: 338652 [Multi-domain]  Cd Length: 422  Bit Score: 43.63  E-value: 8.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    280 GSLPAGRGprGTVAPATPTKPQRTS-------PTNPHQHMAVGGPAQTPLLPAKLSASNALD-PMLPasvgGSTRTPRPA 351
Cdd:pfam13254   47 GSVAGSSS--SLSSGLSPTKLSREGspestsrPSSSHSEATIVHHSKSEESRGSSRTDEGFVrPALP----RHSRSSSAL 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    352 AAQPSQKITAtkipkSLPTKPSAPSTSIVPiKSPHPTqktaPSSFTKSAL-----PTQKQVPPTSRPvPARVSRPAEKPI 426
Cdd:pfam13254  121 SNTGSEEDSP-----SDPTSPPSPSKTMDP-KRWSPT----KSSWLESALnrpesPKPKAQPSQPQQ-PSWMAELNKIKQ 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    427 QRNPGMPRPPppstrplppttSSSKKPIPTLARTEAKITSHASKP----ASARTSTHKPPPF-----TALSSSPAPTPGS 497
Cdd:pfam13254  190 SRASVDLGRP-----------AAFKEVTPVGLMRSPAPGSHSKSPsvsgISADASPAKESPSeetetTSTDKEQSPIPAN 258
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    498 TRSTRPPATMVPPTSGTST-PRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPrkpvplrPGKAARDVPLSDLTTRPS 576
Cdd:pfam13254  259 SEIPPPSEKELPKDSEEPEaPSKSAEVSTEKKEPDVESSPETPSARKRAPSLLSP-------TSKASSDKPLVARFSPAR 331
                          330
                   ....*....|...
gi 24251209    577 -PRQPQPSQQTTP 588
Cdd:pfam13254  332 dPPSPKPKPQTPP 344
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1502-1564 9.66e-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: 9.66e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24251209   1502 GPPGKRGTEGRTGLPGNQGEPGSKGQPGDSGEMGFPGMAGlfgPKGPPGDIGFKGIQGPRGPP 1564
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPG---PPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
835-894 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 24251209    835 GPKGMKGLMGSVGEPGLKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKPGPLGKV 894
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
136-204 1.23e-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: 40.50  E-value: 1.23e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24251209    136 VVHLGSRRSVAFDLD--MHDGRWHHLALELRGRTVTLVTaCGQRRVPVLLPfHRDPALDPGGSFLFGKMNP 204
Cdd:pfam02210   33 RYDLGSGPVSLLSSGkpLNDGQWHRVRVSRNGRTLTLSV-DGQTVVSALPP-GESLLLNLNGPLYLGGLPP 101
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
284-588 1.41e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 43.45  E-value: 1.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    284 AGRG--PRGTVAPATPTKPQRT------SPTNPHQHMAVGGPAQTPLLPAklSASNALDPMLPAS----VGGSTRTPRPA 351
Cdd:TIGR00927   97 VGRDeaTPSIAMENTPSPPRRTakitptTPKNNYSPTAAGTERVKEDTPA--TPSRALNHYISTSgrqrVKSYTPKPRGE 174
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    352 AAQPSQKITATKIPKSLPT------KPSAPSTSIVPIKS----PHPTQKTAPSSFTKSALPTQ--KQVPPTSRPVPAR-- 417
Cdd:TIGR00927  175 VKSSSPTQTREKVRKYTPSplgrmvNSYAPSTFMTMPRShgitPRTTVKDSEITATYKMLETNpsKRTAGKTTPTPLKgm 254
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    418 -------VSRPAEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHASKPASARTSTHKPPPFTALSSS 490
Cdd:TIGR00927  255 tdntptfLTREVETDLLTSPRSVVEKNTLTTPRRVESNSSTNHWGLVGKNNLTTPQGTVLEHTPATSEGQVTISIMTGSS 334
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    491 PAPTPGSTRSTRppatMVPPTSGTSTP--RTAPA-----VPTPGSAPTGSKKPigseaSKKAGPKSSPRKPVPLRPGKAA 563
Cdd:TIGR00927  335 PAETKASTAAWK----IRNPLSRTSAPavRIASAtfrglEKNPSTAPSTPATP-----RVRAVLTTQVHHCVVVKPAPAV 405
                          330       340
                   ....*....|....*....|....*
gi 24251209    564 RDVPLSDLTTRPSPRQPQPSQQTTP 588
Cdd:TIGR00927  406 PTTPSPSLTTALFPEAPSPSPSALP 430
TALPID3 pfam15324
Hedgehog signalling target; TALPID3 is a family of eukaryotic proteins that are targets for ...
486-632 1.42e-03

Hedgehog signalling target; TALPID3 is a family of eukaryotic proteins that are targets for Hedgehog signalling. Mutations in this gene noticed first in chickens lead to multiple abnormalities of development.


Pssm-ID: 317697 [Multi-domain]  Cd Length: 1241  Bit Score: 43.68  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    486 ALSSSPAPTPGSTRSTRPPAtmVPPTSGTSTPRTAPAVPTPGSAPtgskkpigsEASKKAGPKSSPRKPVPLR------- 558
Cdd:pfam15324  901 ALAETIAIMLGDREAQRPAP--VAPSVPGDASDKETTLPTPVPTP---------QPTPPPSPPSSLKEPSPVKtpdsspc 969
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24251209    559 PGKAARDVPLSDLTTRPSPRQPQPSQQTTPALVLAPAQFLSSSPRPTSSGYSIFHLAGSTPfpllmGPPGPKGD 632
Cdd:pfam15324  970 PSEHDGAFPVKEIPAEKGADGPAVTPVITPTVTPVATPPPAATPSPPLSENSIDKLKSPSP-----ELPKPWED 1038
Herpes_TAF50 pfam03326
Herpesvirus transcription activation factor (transactivator); This family includes EBV BRLF1 ...
304-602 1.44e-03

Herpesvirus transcription activation factor (transactivator); This family includes EBV BRLF1 and similar ORF 50 proteins from other herpesviruses.


Pssm-ID: 308764 [Multi-domain]  Cd Length: 568  Bit Score: 43.15  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    304 SPTNPHQHMAVG-GPAQTPLLPAKLSASNALDPMLPASV---GGSTRTPRPAAAQPSQKITATKIPKSLPTKPSAPSTSI 379
Cdd:pfam03326  234 SPTMPQQALKPGaQSSDTSGVSDTEQSARQTATAEPQRLqapGFSRSTSRPARGQTAQYFLAAQQHGVVSLFPSTATLVP 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    380 VPIKSPHPT------QKTAPSSFT--KSALPTQKQVPPTSRPVPARVSRPA---------EKPIQRNPGMPRPPPPSTRP 442
Cdd:pfam03326  314 IAGSTGVTEvvsyghNSTSPSSTPcpSTAVTEADHQTEPEVPWIATAHQESdqrpigpgpEKPTFLPPVGGKQFFQGLRD 393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    443 LPPTTSSSKKPIPTLARTEAKITSHASkpaSARTSTHKPPpftALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPA 522
Cdd:pfam03326  394 SRSTSFLTAPEATSAISDVFQGTEVCQ---PKRIRALHPP---GSPSANRPLPSSLAPTPTGPVHEPGSSLTPATVPQPL 467
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    523 VPTPGSAPTGSkkpigSEASKKAGPKSSPRKpvplrpgkaaRDVPLSDLTTRPSPRQPQPSQQTTPALVLAPAQFLSSSP 602
Cdd:pfam03326  468 DAAPVATPEAS-----HELQPPDEETPQPLD----------EDQALCGQQDASHPPPRGQLDELTTTLESMTEDLNLDSP 532
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1517-1575 1.45e-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: 1.45e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 24251209   1517 GNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGP 1575
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
452-629 1.66e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 42.99  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   452 KPIPTLART-EAKITSHASKPASARTSTHKP-PPFTALS-----SSPAPTPGSTRSTRPPatmvpPTSGTSTPRTAPAVP 524
Cdd:PLN03209  340 KPVPTKPVTpEAPSPPIEEEPPQPKAVVPRPlSPYTAYEdlkppTSPIPTPPSSSPASSK-----SVDAVAKPAEPDVVP 414
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   525 TPGSAPTGSKKPIGSEASKKAGPKS---------SPRKPVPlrpgKAARDVPLSDLTTRPSPRQPQPSQQTTPALVLAPA 595
Cdd:PLN03209  415 SPGSASNVPEVEPAQVEAKKTRPLSpyaryedlkPPTSPSP----TAPTGVSPSVSSTSSVPAVPDTAPATAATDAAAPP 490
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 24251209   596 qflSSSPRPTSSGYSIFHLAGST-PFPLLMGPPGP 629
Cdd:PLN03209  491 ---PANMRPLSPYAVYDDLKPPTsPSPAAPVGKVA 522
PRK14971 PRK14971
DNA polymerase III subunits gamma and tau; Provisional
456-597 1.85e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 42.84  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   456 TLARTEAKITSHASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPATmvpPTSGTSTPRTAPAVPTPGSAPTGSKK 535
Cdd:PRK14971  363 TQKGDDASGGRGPKQHIKPVFTQPAAAPQPSAAAAASPSPSQSSAAAQPSA---PQSATQPAGTPPTVSVDPPAAVPVNP 439
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24251209   536 PIGSEASKKAGPKSSPRKPVPLRPGKAARdvplsdLTTRPSPRQPQPSQQTTPALVLAPAQF 597
Cdd:PRK14971  440 PSTAPQAVRPAQFKEEKKIPVSKVSSLGP------STLRPIQEKAEQATGNIKEAPTGTQKE 495
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
829-888 1.87e-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: 1.87e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    829 GPIGYPGPKGMKGLMGSVGEPGLKGDKGEQGVPGVSGDPGFQGDKGSQGLPGFPGARGKP 888
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
PRK14954 PRK14954
DNA polymerase III subunits gamma and tau; Provisional
481-546 1.90e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184918 [Multi-domain]  Cd Length: 620  Bit Score: 43.01  E-value: 1.90e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24251209   481 PPPFTALSSSPAPTpGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAG 546
Cdd:PRK14954  396 EPDLPQPDRHPGPA-KPEAPGARPAELPSPASAPTPEQQPPVARSAPLPPSPQASAPRNVASGKPG 460
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1146-1199 2.34e-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: 2.34e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 24251209   1146 MGPKGPPGAVGEPGLPGEAGMKGDLGPLGTPGEQGLIGQRGEPGLEGDSGPMGP 1199
Cdd:pfam01391    6 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
916-990 2.69e-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: 2.69e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24251209    916 GPPGDNGPEGMKGKPGARGLPGPRGQLGPEGDegpmgppgapglegqPGRKGFPGRPGLDGVKGEPGDPGRPGPV 990
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGP---------------PGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
CEP170_C pfam15308
CEP170 C-terminus; This family includes the C-terminus of centrosomal protein of 170 kDa ...
273-605 2.81e-03

CEP170 C-terminus; This family includes the C-terminus of centrosomal protein of 170 kDa (CEP170).


Pssm-ID: 317681  Cd Length: 674  Bit Score: 42.40  E-value: 2.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    273 TTATPALGSLPAGRGPRGTVAPATPTKPQRTSPTNPHQHMAVGGPAQTPLlPAKLSASNALDPMLPASVGGSTRTPRPAA 352
Cdd:pfam15308  115 TASTVSLVSGKNEPKSTQKRRSLSGLQKEKSSSSPSSQDKGSQPSARERL-SEKRRKPRTPDDPGRAEARRRLQSRRGRG 193
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    353 AQPSQKITATKIPKSLPtkpSAPSTSIVpiKSPHPTQkTAPSSFTKsalptqKQVPPTSRPVPARVSRPAEKPIQrnpgm 432
Cdd:pfam15308  194 PRGSLDLTDDDQGSSLP---HSPISDIL--SSDHETS-SRPSHRRK------PLTSPAQKEEQSKSSKTVQKTQQ----- 256
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    433 prppppstrpLPPTTSSSKKPIPT----LAR--------TEAKITSHASkPASARTSTHKPPP----------------- 483
Cdd:pfam15308  257 ----------ALTRSNSLSTPRPTraslLRRarlgdasdTELADTDRGS-VASEVSTTSKPPTerkklsrldilamprkr 325
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    484 ---FTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGS-APTGSKKPIgseasKKAGPKSSPRKPVplrP 559
Cdd:pfam15308  326 agsFTAPSDSEATTARSGFSGRSAETYYALRKGRVSEARAAARKGARArANSASKQPD-----SRTRSGSAKYSPS---S 397
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 24251209    560 GKAARDVPlSDLT---------TRPSPRQ----PQPSQQTTPALVLAPAQFLSSSPRPT 605
Cdd:pfam15308  398 SSRRRQQG-SDYAstseeeygsNRGSPKHkrshPSTATQTPRLGGSAPARPKPPGHRET 455
PRK10905 PRK10905
cell division protein DamX; Validated
500-610 2.86e-03

cell division protein DamX; Validated


Pssm-ID: 236792 [Multi-domain]  Cd Length: 328  Bit Score: 41.85  E-value: 2.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   500 STRP--PATmVPPTSGTSTPRTAPAVPTPGSAPTG----------SKKPigsEASKKAGPKSSPRKPVPLRPGKAARDVP 567
Cdd:PRK10905  121 STLPtePAT-VAPVRNGNASRQTAKTQTAERPATTrparkqaviePKKP---QATAKTEPKPVAQTPKRTEPAAPVASTK 196
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 24251209   568 LSDLTTRPsprQPQPSQQTTPALVLAPAQflsSSPRPTSSGYS 610
Cdd:PRK10905  197 APAATSTP---APKETATTAPVQTASPAQ---TTATPAAGGKT 233
PHA03247 PHA03247
large tegument protein UL36; Provisional
452-560 2.92e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   452 KPIPTLARTEAKITSHASKPASARTSTHKPPPFTAL--SSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSA 529
Cdd:PHA03247  375 PKRASLPTRKRRSARHAATPFARGPGGDDQTRPAAPvpASVPTPAPTPVPASAPPPPATPLPSAEPGSDDGPAPPPERQP 454
                          90       100       110
                  ....*....|....*....|....*....|....
gi 24251209   530 PTGSK---KPIGSEASKKAGPKSSPRKPvPLRPG 560
Cdd:PHA03247  455 PAPATepaPDDPDDATRKALDALRERRP-PEPPG 487
kgd PRK12270
alpha-ketoglutarate decarboxylase; Reviewed
476-564 3.07e-03

alpha-ketoglutarate decarboxylase; Reviewed


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 42.57  E-value: 3.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   476 TSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPV 555
Cdd:PRK12270   39 GSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDEVT 118

                  ....*....
gi 24251209   556 PLRpGKAAR 564
Cdd:PRK12270  119 PLR-GAAAA 126
MIP-T3 pfam10243
Microtubule-binding protein MIP-T3; This protein, which interacts with both microtubules and ...
341-550 3.15e-03

Microtubule-binding protein MIP-T3; This protein, which interacts with both microtubules and TRAF3 (tumor necrosis factor receptor-associated factor 3), is conserved from worms to humans. The N-terminal region is the microtubule binding domain and is well-conserved; the C-terminal 100 residues, also well-conserved, constitute the coiled-coil region which binds to TRAF3. The central region of the protein is rich in lysine and glutamic acid and carries KKE motifs which may also be necessary for tubulin-binding, but this region is the least well-conserved.


Pssm-ID: 313469 [Multi-domain]  Cd Length: 518  Bit Score: 42.15  E-value: 3.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    341 VGGSTRTPRPAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTA--------PSSFTKSALPTQKQVPPT-S 411
Cdd:pfam10243   80 VEKGGSKGPAALTKPAKEPKNRSGTEEEARKEKVKEEKKKKEEKPQSTPKDRkpkeelkePRPPTEKEKEKEKKVKAPrD 159
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    412 RPVPAR------VSRPAEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPI---------------PTLARTEAKITSHASK 470
Cdd:pfam10243  160 REKEKRrdrekaSSAEKKPKKKDSKNKKKDPEREKKKQASGKAVSGKEEerdhneerekeaddgPDPETNTSPPSEHESR 239
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    471 PASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKP-------IGSEASK 543
Cdd:pfam10243  240 RSSEKSRRSSKSEKKPQSNPGQSTSQEQPTDVTSLPRPPTEAKSGRTSLRPPSPRPASARPAPPRVkrknveiVLQDAQG 319

                   ....*..
gi 24251209    544 KAGPKSS 550
Cdd:pfam10243  320 VGKIVSN 326
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
372-633 3.75e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.08  E-value: 3.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   372 PSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPAEKPIQRNPGMPRPPPPSTRPLPPTTSSSK 451
Cdd:PHA03307   63 DRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVG 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   452 KPIPTLARTEAKITSHASKPASARTSTHKPPPFTALSSSPAPTPGStrstrPPATMVPPTSGTSTPRTAPAVPTPGSAPT 531
Cdd:PHA03307  143 SPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSS-----PPAEPPPSTPPAAASPRPPRRSSPISASA 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   532 GSKKPigseaskkAGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSPRQPQPSQQTTPALVLAPAQFLSSSPRPTSSgysi 611
Cdd:PHA03307  218 SSPAP--------APGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPA---- 285
                         250       260
                  ....*....|....*....|..
gi 24251209   612 fhlAGSTPFPLLMGPPGPKGDC 633
Cdd:PHA03307  286 ---SSSSSPRERSPSPSPSSPG 304
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1520-1577 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 24251209   1520 GEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIGFKGIQGPRGPPGLMGKEGIVGPLG 1577
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
Mucin pfam01456
Mucin-like glycoprotein; This family of trypanosomal proteins resemble vertebrate mucins. The ...
461-563 3.96e-03

Mucin-like glycoprotein; This family of trypanosomal proteins resemble vertebrate mucins. The protein consists of three regions. The N and C terminii are conserved between all members of the family, whereas the central region is not well conserved and contains a large number of threonine residues which can be glycosylated. Indirect evidence suggested that these genes might encode the core protein of parasite mucins, glycoproteins that were proposed to be involved in the interaction with, and invasion of, mammalian host cells. This family contains an N-terminal signal peptide.


Pssm-ID: 250634 [Multi-domain]  Cd Length: 143  Bit Score: 39.46  E-value: 3.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    461 EAKITSHASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPT-GSKKPIGS 539
Cdd:pfam01456   33 AAVVEAAEGQSQTTTTTTTTTPPTTTTTTTTTTTTITTTTTKTTTTTTTTTTTTTTTEAPSKNTTTSEAPTtTDTRAPSS 112
                           90       100
                   ....*....|....*....|....
gi 24251209    540 EASKKAGPKSSPRKPVPLRPGKAA 563
Cdd:pfam01456  113 IREIDGSLGSSAWVCAPLLLAVSA 136
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
457-571 3.99e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 41.72  E-value: 3.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   457 LARTEAKITS----HASKPASARTSTHKPPPftALSSSPAPTPGSTRSTRPP-ATMVPPTSGTSTPRTAPAVPTPGSAPT 531
Cdd:PRK14950  353 LAVIEALLVPvpapQPAKPTAAAPSPVRPTP--APSTRPKAAAAANIPPKEPvRETATPPPVPPRPVAPPVPHTPESAPK 430
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 24251209   532 GSKKPIGSEASKKAGPkssprkPVPLRPGKAARDVPLSDL 571
Cdd:PRK14950  431 LTRAAIPVDEKPKYTP------PAPPKEEEKALIADGDVL 464
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1394-1449 4.10e-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: 4.10e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 24251209   1394 GPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVVGRQGLEGIAGPDGLPGR 1449
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGA 56
PHA03379 PHA03379
EBNA-3A; Provisional
283-629 4.23e-03

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 41.97  E-value: 4.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   283 PAGRGPRGTVAPATPTKPQRTSPTNPHqhmavgGPAQTPLLP----AKLSASNALDPMLPASVGGSTRTPRPAAAQPSQK 358
Cdd:PHA03379  411 PTYGTPRPPVEKPRPEVPQSLETATSH------GSAQVPEPPpvhdLEPGPLHDQHSMAPCPVAQLPPGPLQDLEPGDQL 484
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   359 ITATKIPKSLPTKPSAPSTSIVPIKSPHPTQktAPSSFTKSALPTQKQVPPTSRPVPARVSRPAEKPIQRNPGMPRPPPP 438
Cdd:PHA03379  485 PGVVQDGRPACAPVPAPAGPIVRPWEASLSQ--VPGVAFAPVMPQPMPVEPVPVPTVALERPVCPAPPLIAMQGPGETSG 562
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   439 STRPLPPTTSSSKKPIPTLARTEAKITSHASKPASARTSTHKP----PPFTALSSSPAPTpgsTRSTRPPATMVPPTSGT 514
Cdd:PHA03379  563 IVRVRERWRPAPWTPNPPRSPSQMSVRDRLARLRAEAQPYQASvevqPPQLTQVSPQQPM---EYPLEPEQQMFPGSPFS 639
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   515 STPRTAPAVPTPGSAPTGSKKPIGSEASKKA--GPKSSPRKPVPLRPGKAAR--DVPLSD-LTTRPSPRQPQPSQQTTPA 589
Cdd:PHA03379  640 QVADVMRAGGVPAMQPQYFDLPLQQPISQGAplAPLRASMGPVPPVPATQPQyfDIPLTEpINQGASAAHFLPQQPMEGP 719
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 24251209   590 LV----LAPAQFLSSSPRPTSSGYSIFHLAGSTPF----PLLMGPPGP 629
Cdd:PHA03379  720 LVperwMFQGATLSQSVRPGVAQSQYFDLPLTQPInhgaPAAHFLHQP 767
TALPID3 pfam15324
Hedgehog signalling target; TALPID3 is a family of eukaryotic proteins that are targets for ...
339-611 4.25e-03

Hedgehog signalling target; TALPID3 is a family of eukaryotic proteins that are targets for Hedgehog signalling. Mutations in this gene noticed first in chickens lead to multiple abnormalities of development.


Pssm-ID: 317697 [Multi-domain]  Cd Length: 1241  Bit Score: 41.75  E-value: 4.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    339 ASVGGSTRTPRPAAAQPSQKITATKIPKSLPTkpsapstsivPIKSPHPTQKTAPSSFTKSALPTQKqvpPTSRPVParv 418
Cdd:pfam15324  907 AIMLGDREAQRPAPVAPSVPGDASDKETTLPT----------PVPTPQPTPPPSPPSSLKEPSPVKT---PDSSPCP--- 970
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    419 srpaekpiqrnpgmprppppstrplppttssskkpiptlarTEAKITSHaSKPASARTSTHKPppftalSSSPAPTPGST 498
Cdd:pfam15324  971 -----------------------------------------SEHDGAFP-VKEIPAEKGADGP------AVTPVITPTVT 1002
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    499 RSTRPP--ATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEaskkagpKSSPRKPVPLRPG----KAARDVPLSDLT 572
Cdd:pfam15324 1003 PVATPPpaATPSPPLSENSIDKLKSPSPELPKPWEDADLPLEEE-------NPNPFQEEPLHPRavvmSVAKDEEPESLV 1075
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 24251209    573 TRPSPRQPQP-SQQTTPALVLAPAQFLSSSPRPTSSGYSI 611
Cdd:pfam15324 1076 FPASPPEPVPfAPLPLGARVPSPVQSPSSSSSTQESSSSV 1115
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
1355-1397 4.35e-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: 4.35e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 24251209   1355 GDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGHPGPRGWPGPKG 1397
Cdd:pfam01391   16 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPG 58
rad23 TIGR00601
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
469-545 4.95e-03

UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273167 [Multi-domain]  Cd Length: 378  Bit Score: 41.03  E-value: 4.95e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24251209    469 SKPASARTSTHKPPPftalSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKA 545
Cdd:TIGR00601   75 SKPKTGTGKVAPPAA----TPTSAPTPTPSPPASPASGMSAAPASAVEEKSPSEESATATAPESPSTSVPSSGSDAA 147
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
349-512 5.07e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 41.62  E-value: 5.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   349 RPAAAQPSQKITAtkipKSLPTKPSAPStsivPIKSPHPTQKTAPSSftKSALPTQKQVP--PTSRPVPARVSRPAEKPi 426
Cdd:PRK14951  365 KPAAAAEAAAPAE----KKTPARPEAAA----PAAAPVAQAAAAPAP--AAAPAAAASAPaaPPAAAPPAPVAAPAAAA- 433
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   427 qrnpgmprppppstrplppttsssKKPIPTLARTEAKITSHASKPASARTSThkpPPFTALSSSPAPTPGSTRSTRPPAT 506
Cdd:PRK14951  434 ------------------------PAAAPAAAPAAVALAPAPPAQAAPETVA---IPVRVAPEPAVASAAPAPAAAPAAA 486

                  ....*.
gi 24251209   507 MVPPTS 512
Cdd:PRK14951  487 RLTPTE 492
PRK10263 PRK10263
DNA translocase FtsK; Provisional
334-590 5.09e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 41.61  E-value: 5.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   334 DPML-------PASVGGSTRTPRPAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPH---PTQKTAPSSFTKSALPT 403
Cdd:PRK10263  308 DPLLngapitePVAVAAAATTATQSWAAPVEPVTQTPPVASVDVPPAQPTVAWQPVPGPQtgePVIAPAPEGYPQQSQYA 387
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   404 QKQVP---PTSRPVP-------------ARVSRPAEKPIQRNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSH 467
Cdd:PRK10263  388 QPAVQynePLQQPVQpqqpyyapaaeqpAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQT 467
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   468 ASKPASARTSTHKPPPFTALSS-SPAPTPGSTRSTRPP------------------ATMVPPtsgTSTPRTAPAVPTPGS 528
Cdd:PRK10263  468 YQQPAAQEPLYQQPQPVEQQPVvEPEPVVEETKPARPPlyyfeeveekrarereqlAAWYQP---IPEPVKEPEPIKSSL 544
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24251209   529 APTGSKKPIGSEASKKAGPKSSPRKPVPLRPGKAARD-VPLSDLTTRPSPRqPQPSQQTTPAL 590
Cdd:PRK10263  545 KAPSVAAVPPVEAAAAVSPLASGVKKATLATGAAATVaAPVFSLANSGGPR-PQVKEGIGPQL 606
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
1355-1568 5.29e-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: 41.53  E-value: 5.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   1355 GDRGEPGDPGYPGQEGVQGLRGKPGQQGQPGHPGP-RGWPGPKGSKGAEGPKGKQGKAGAPGRRGVQGLQGLPGPRGVvg 1433
Cdd:pfam09606  178 GGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPaDAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQS-- 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   1434 rQGLEGIAGPDGLPGRDGQAGQQgeqgddGDPG-PMGPAGKRgnPGVAGLPGAQGPPGFKGESGLPGQLGPPGKRGTEGR 1512
Cdd:pfam09606  256 -QLGMGINQMQQMPQGVGGGAGQ------GGPGqPMGPPGQQ--PGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAH 326
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 24251209   1513 TGLPGNQGEPGSKGQPGDSGEMGFPGMAGLFGPKGPPGDIgfkgiqgpRGPPGLMG 1568
Cdd:pfam09606  327 QQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGANPMQ--------RGQPGMMS 374
Lamp pfam01299
Lysosome-associated membrane glycoprotein (Lamp);
458-525 6.93e-03

Lysosome-associated membrane glycoprotein (Lamp);


Pssm-ID: 334479  Cd Length: 314  Bit Score: 40.36  E-value: 6.93e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24251209    458 ARTEAKITSHASKPASARTSTHKPppftalssSPAPTPGSTRSTRPPATMVPPTsgTSTPRTAPAVPT 525
Cdd:pfam01299   62 VTTQAYTSNGTTSKQETTCSTDSP--------TTTTATTNTTSTTTPTPTPPTP--TPTPPSSPTVGN 119
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
472-593 7.12e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 40.95  E-value: 7.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   472 ASARTSTHKPPPF------TALSSSPAPTPGSTRSTRPPAtmVPPTSGTST-PRTAPAVPTPGSAPTGSKKPIGSEASKK 544
Cdd:PRK14950  339 FQLRTTSYGQLPLelavieALLVPVPAPQPAKPTAAAPSP--VRPTPAPSTrPKAAAAANIPPKEPVRETATPPPVPPRP 416
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 24251209   545 AGPKSSPRKPVPLRPGKAARDVPLSDLTTRPSPRQPQPSQQTTPALVLA 593
Cdd:PRK14950  417 VAPPVPHTPESAPKLTRAAIPVDEKPKYTPPAPPKEEEKALIADGDVLE 465
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
283-426 7.37e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 40.85  E-value: 7.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   283 PAGRGPRGTVAPATPTKPQRTSPtnphqhmAVGGPAQTPLLPAKLSASNALDPMLPASVGGSTRTPRPAAAQPSQKITAT 362
Cdd:PRK14951  367 AAAAEAAAPAEKKTPARPEAAAP-------AAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPA 439
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24251209   363 KIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSsftksalPTQKQVPPTSRPVPARVSRPAEKPI 426
Cdd:PRK14951  440 AAPAAVALAPAPPAQAAPETVAIPVRVAPEPA-------VASAAPAPAAAPAAARLTPTEEGDV 496
PHA03377 PHA03377
EBNA-3C; Provisional
366-619 7.45e-03

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 41.19  E-value: 7.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   366 KSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPAEKPIQRNPGMPRPPPPSTRPLPP 445
Cdd:PHA03377  447 QSTPERPGPSDQPSVPVEPAHLTPVEHTTVILHQPPQSPPTVAIKPAPPPSRRRRGACVVYDDDIIEVIDVETTEEEESV 526
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   446 TTSSSKKPIPTLARTEAKITSHASKPASARTSTHKPP---PFTALSSSPAPTPGSTRSTRPPAtMVPPTSG--------T 514
Cdd:PHA03377  527 TQPAKPHRKVQDGFQRSGRRQKRATPPKVSPSDRGPPkasPPVMAPPSTGPRVMATPSTGPRD-MAPPSTGprqqakckD 605
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   515 STPRTAPAVPTPGS-APTGSKKPIGSEASK-KAGPKSSPRKPVPLRPGKAARDVPlsDLTTRPSPRQPQPSQQTTPALVL 592
Cdd:PHA03377  606 GPPASGPHEKQPPSsAPRDMAPSVVRMFLReRLLEQSTGPKPKSFWEMRAGRDGS--GIQQEPSSRRQPATQSTPPRPSW 683
                         250       260
                  ....*....|....*....|....*...
gi 24251209   593 APAQF-LSSSPRPTSSGYSIFHLAGSTP 619
Cdd:PHA03377  684 LPSVFvLPSVDAGRAQPSEESHLSSMSP 711
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
760-809 7.71e-03

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


Pssm-ID: 189968 [Multi-domain]  Cd Length: 60  Bit Score: 36.31  E-value: 7.71e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 24251209    760 GLPGLFGLPGSDGERGLPGVPGKRGKMGMPGFPGVFGERGPPGLDGNPGE 809
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGA 53
Treacle pfam03546
Treacher Collins syndrome protein Treacle;
270-596 7.89e-03

Treacher Collins syndrome protein Treacle;


Pssm-ID: 335373 [Multi-domain]  Cd Length: 522  Bit Score: 40.81  E-value: 7.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    270 ENLTTATPALGSLPAGRGP--RGTVAPATPTKPQRTSPTNPHQHMAVGGPAQTPLLPAKLSASNALDPMLPASVGGSTRT 347
Cdd:pfam03546   36 EETPAAKTPLQAKPSGKTPqvRAASAPAKESPRKGAPPVPPGKTGPAAAQAQAGKPEEDSESSSEESDSDGETPAAATLT 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    348 PRPAAAQPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPaeKPIQ 427
Cdd:pfam03546  116 TSPAQVKPLGKNPQVRPASTVTAGPSGKGASPAPPGKAGPAGPLAQVGKGEEDSESSSEESDSEGEAPPAATQA--KPSG 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    428 RNPGMPRPPPPSTRPLPPTTSSSKKPIPTLARTEAKITSHASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPATM 507
Cdd:pfam03546  194 KILQVRPASGPAKGVAAPAPPQKAGPVATQVKAERSKDDSESSEESSDSEEEAPAAATPAQAKPALKTPQTKASPRKGTP 273
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    508 VPPTS--------GTSTPRTAPAVPTPGSA-----PTGSKKP-------IGSEASKKAGPKSSPRKPVPLRPGKAARDVP 567
Cdd:pfam03546  274 ITPTSakgppvrvGTPAPWKAGTVTSPACAsspavARGAQRPeddssssEESESEEETAPAAAVGQAKSVGKGLQGKAAS 353
                          330       340
                   ....*....|....*....|....*....
gi 24251209    568 LSDLTTRPSPRQPQPSQQTTPALVLAPAQ 596
Cdd:pfam03546  354 APTKGPSGQGTAPLPPGKTGPAVAQVKAE 382
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
275-429 8.87e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 40.62  E-value: 8.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   275 ATPALGSLPAGRGPRGTVAPATPTKPQRTSPTNPHQHMavggPAQTPLLPAKLSASNALDPMLP-ASVGGSTRTPRPAAA 353
Cdd:PRK07994  369 EVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASA----PQQAPAVPLPETTSQLLAARQQlQRAQGATKAKKSEPA 444
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   354 QPSQKITATKIPKSLPTKPSAPSTSIVPIKSPHP----TQKTAPSSFTKSALPTQKQVPPTSRPVPARVSRPAEKPIQRN 429
Cdd:PRK07994  445 AASRARPVNSALERLASVRPAPSALEKAPAKKEAyrwkATNPVEVKKEPVATPKALKKALEHEKTPELAAKLAAEAIERD 524
PHA02682 PHA02682
ORF080 virion core protein; Provisional
275-426 9.37e-03

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 39.84  E-value: 9.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   275 ATPALGSLPAGRGPRGTVAPATPTKPQRTSPTNPHQHMAVGGPAQTPLLPAklsasnALDPMLPasvggstrtprPAAAQ 354
Cdd:PHA02682   68 ANSACMQRPSGQSPLAPSPACAAPAPACPACAPAAPAPAVTCPAPAPACPP------ATAPTCP-----------PPAVC 130
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24251209   355 PSQKITATKIPkslptkpsaPSTSIVPIKSPHPTQKTAPssftkSALPT--QKQVPPTSRPV---PARVSRPAEKPI 426
Cdd:PHA02682  131 PAPARPAPACP---------PSTRQCPPAPPLPTPKPAP-----AAKPIflHNQLPPPDYPAascPTIETAPAASPV 193
SOG2 pfam10428
RAM signalling pathway protein; SOG2 proteins in Saccharomyces cerevisiae are involved in cell ...
448-576 9.64e-03

RAM signalling pathway protein; SOG2 proteins in Saccharomyces cerevisiae are involved in cell separation and cytokinesis.


Pssm-ID: 337747  Cd Length: 430  Bit Score: 40.37  E-value: 9.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209    448 SSSKKPIPTLARTEAKITShASKPASARTSTHKPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPG 527
Cdd:pfam10428  166 GRTKSPSPSITSGGSPSPP-ALSSTRSGSSSRTPTPRRRSRSDTTIPHPGGNLSSPAPNGATPISSASSPGAIPRPLDSS 244
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 24251209    528 SAPTGSkkpigseASKKAGPKSSPRKPVPLRPgkAARDVPLSDLTTRPS 576
Cdd:pfam10428  245 PRSRSS-------SRSNTLASTSPPSSLASTP--RSGESFASTSTGSRI 284
PLN02983 PLN02983
biotin carboxyl carrier protein of acetyl-CoA carboxylase
480-539 9.64e-03

biotin carboxyl carrier protein of acetyl-CoA carboxylase


Pssm-ID: 215533 [Multi-domain]  Cd Length: 274  Bit Score: 39.82  E-value: 9.64e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   480 KPPPFTALSSSPAPTPGSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGS 539
Cdd:PLN02983  143 QPPPPAPVVMMQPPPPHAMPPASPPAAQPAPSAPASSPPPTPASPPPAKAPKSSHPPLKS 202
PRK07003 PRK07003
DNA polymerase III subunits gamma and tau; Validated
338-604 9.70e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 40.60  E-value: 9.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   338 PASVGGSTrtprPAAAQPSQkiTATKIPKSLPTKPSAPSTSIVPIKSPHPTQKTAPssftksalptqkqvpPTSRPVPAR 417
Cdd:PRK07003  360 PAVTGGGA----PGGGVPAR--VAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAA---------------LAPKAAAAA 418
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   418 VSRPAEKPIQRnpgmprppppstrplppttssskkpiPTLARTEAKITSHASKPASARTSTHKPPPFTALSSSPAPTP-- 495
Cdd:PRK07003  419 AATRAEAPPAA--------------------------PAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPpa 472
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24251209   496 ------GSTRSTRPPATMVPPTSGTSTPRTAPAVPTPGSAPTGSKKPIGSEASKKAGPKSSPRKPVPLRPGK------AA 563
Cdd:PRK07003  473 dsgsasAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAAraggaaAA 552
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 24251209   564 RDV------PLSDLTTRPSPRQPQPSQQTTPALVLAPAQFLSSSPRP 604
Cdd:PRK07003  553 LDVlrnagmRVSSDRGARAAAAAKPAAAPAAAPKPAAPRVAVQVPTP 599
 
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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