|
Name |
Accession |
Description |
Interval |
E-value |
| 5 |
PHA02596 |
baseplate hub subunit and tail lysozyme; Provisional |
2-600 |
0e+00 |
|
baseplate hub subunit and tail lysozyme; Provisional
Pssm-ID: 222900 [Multi-domain] Cd Length: 576 Bit Score: 1054.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20218971 2 LMFNNSVKWFTGIVENREDPLMLGRVQVRIHGIHPSLSAHGDIQGLPTEDLLWITPVQDITSAAISGIGQSPTGIVEGSM 81
Cdd:PHA02596 1 EMINNNLKWFVGVVEDRMDPLKLGRVRVRVHGIHPAQKAKGDVYGIPTEDLPWMSVIQPITSAAISGIGQSPTGIVEGTH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20218971 82 VFGLALDERYLNCVILGTIAGQYTEKPLTTEGFCDPSGAYPRYIGNDVNILARGGINPETgqttkPDSVYIRDENTGVAV 161
Cdd:PHA02596 81 VYGHFLDKWKQNGLILGTYGGIYREKPNTNEGFSDPTGQYPRYVGNDVNVLARGGEVGYD-----PSSVVIQDANTDVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20218971 162 NPDDEPLDQIPVDDNPDFTIEKMLRGDEGYREKWYLDSEGYPTIGIGHLIIYKKTSDLGIINNELSKLVGREVTNGRLTA 241
Cdd:PHA02596 156 NPDDTPLDEIPPDDNPDFTIEKMLRRDEGIRLKVYWDSEGYPTIGIGHLIIREKTRDMAQINKLLSKQVGREVTGGRITA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20218971 242 EEVSKVFADDIEKTRRDMRKHPRIAPVYNKCNASRRMALENMAFQMGVGGLGKFKNSLAAMLAEEWKQAYDGLRQSVWAN 321
Cdd:PHA02596 236 EEASKLFARDLAKVQRDISRHSKVGPVYNKLNRSRQMALENMAFQMGVGGVAKFKNMLAAMLAGDWKKAYDALRDSLWAN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20218971 322 QTPGRSSRVSKIILTGNLESYGVIAPkkeesisDDPRARLRNAriAAYKTQRAEEEDPEAPFTPQDTRIMFKEPKSSYSA 401
Cdd:PHA02596 316 QTPGRASRVSKIILTGNLESYGVMVP-------DPPGRSLSTI--AAYKTAVATSSDPADPFTPGDTRIMFKEPKSSYSA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20218971 402 RYPYNHVYESESGHIIEIDDTPSHERYHRKHPSGTFEETRPDGTRVEKIEGDDYLIVKQGRKVNVKGNLQVVVEGDAQVY 481
Cdd:PHA02596 387 EYPYNHVMESESGHIQEFDDTPGHERYRRVHPTGTYEEIRPDGTRVVKIVGDDYYIVKQDRNVNVKGNLKVVVEGDAIYY 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20218971 482 YMGNVMQTVDGNVTEFIRGNVNQTVEGTANMHVVGDVTAQLDANLTANVKGNAELMIEGNTTETIKGNYDLTVEGNFNMT 561
Cdd:PHA02596 467 NMGNVLQTIDGNVTIFVRGNVTKTVEGNGTLYVKGNVTVQVDGNLDATVKGNATTLVEGNQTNTVNGNYKLKVEGNFDMT 546
|
570 580 590
....*....|....*....|....*....|....*....
gi 20218971 562 VNGTKSDQVNGDWSrncgasvkdIASGTVKIDGSRIDLG 600
Cdd:PHA02596 547 VGGNWSEQMAGMSS---------IASGTYTIDGSRIDIG 576
|
|
| Gp5_OB |
pfam06714 |
Gp5 N-terminal OB domain; This domain is found at the N terminus of the Gp5 baseplate protein ... |
33-178 |
1.56e-81 |
|
Gp5 N-terminal OB domain; This domain is found at the N terminus of the Gp5 baseplate protein of bacteriophage T4. This domain binds to the Gp27 protein. This domain has the common OB fold.
Pssm-ID: 148361 Cd Length: 144 Bit Score: 252.39 E-value: 1.56e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20218971 33 GIHPSLSAHGDIQGLPTEDLLWITPVQDITSAAISGIGQSPTGIVEGSMVFGLALDERYLNCVILGTIAGQYTEKPLTTE 112
Cdd:pfam06714 1 GIHPEQKVKGDVQGIPTEDLLWMSPMQPITSAAVSGIGQSPTGIVEGTHVYGFFLDKWYQNGVILGTYPGIYKEKPNTNK 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20218971 113 GFCDPSGAYPRYIGNDVNILARGGINPETGQTTkpDSVYIRDENTGVAVNPDDEPLDQIPVDDNPD 178
Cdd:pfam06714 81 GFSDPNGQYPRYVGNDVNVLARGGKDPEVGYGS--SSNVIQDSNTDVAINPDDTPLDEIPPDDNPD 144
|
|
| T4-like_lys |
cd00735 |
bacteriophage T4-like lysozymes; Bacteriophage T4-like lysozymes hydrolyze the beta-1, ... |
180-341 |
4.91e-74 |
|
bacteriophage T4-like lysozymes; Bacteriophage T4-like lysozymes hydrolyze the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) in peptidoglycan heteropolymers of prokaryotic cell walls. Members include a variety of bacteriophages (T4, RB49, RB69, Aeh1), as well as Dictyostelium.
Pssm-ID: 381597 Cd Length: 146 Bit Score: 233.03 E-value: 4.91e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20218971 180 TIEKMLRGDEGYREKWYLDSEGYPTIGIGHLIIYKKTSdlgiinnelsklvgreVTNGRLTAEEVSKVFADDIEKTRRDM 259
Cdd:cd00735 1 TIREMLRQDEGYRLKAYKDTEGYPTIGIGHLIGKKGAS----------------LTNGTITKDEAEALFEQDVDRAVRDM 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20218971 260 RKHPRIAPVYNKCNASRRMALENMAFQMGVGGLGKFKNSLAAMLAEEWKQAYDGLRQSVWANQTPGRSSRVSKIILTGNL 339
Cdd:cd00735 65 LRNPKLAPVYAQLNAARRMALINMAFQMGVGGLAKFKNMLAAIKAGDWEEAADGMLNSLWAKQTPNRANRVSAVMRTGTW 144
|
..
gi 20218971 340 ES 341
Cdd:cd00735 145 AP 146
|
|
| RrrD |
COG3772 |
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis]; |
189-321 |
2.18e-07 |
|
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442986 [Multi-domain] Cd Length: 146 Bit Score: 50.61 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20218971 189 EGYREKWYLDSEGYPTIGIGHLiiykktsdlgiinnelsklvGREVTNG-RLTAEEVSKVFADDIEKTRRDMRKHPRIap 267
Cdd:COG3772 16 EGFRLKAYRDPAGVWTIGYGHT--------------------GKDVKPGdTITEEEAEALLAADLAKAEAAVRRLVKV-- 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 20218971 268 vynKCNASRRMALENMAFQMGVGGLGkfKNSLAAML-AEEWKQAYDGLRQSVWAN 321
Cdd:COG3772 74 ---PLTQNQFDALVSFAYNVGAGAFC--RSTLLRKLnAGDYAGACDELLRWVYAG 123
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| 5 |
PHA02596 |
baseplate hub subunit and tail lysozyme; Provisional |
2-600 |
0e+00 |
|
baseplate hub subunit and tail lysozyme; Provisional
Pssm-ID: 222900 [Multi-domain] Cd Length: 576 Bit Score: 1054.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20218971 2 LMFNNSVKWFTGIVENREDPLMLGRVQVRIHGIHPSLSAHGDIQGLPTEDLLWITPVQDITSAAISGIGQSPTGIVEGSM 81
Cdd:PHA02596 1 EMINNNLKWFVGVVEDRMDPLKLGRVRVRVHGIHPAQKAKGDVYGIPTEDLPWMSVIQPITSAAISGIGQSPTGIVEGTH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20218971 82 VFGLALDERYLNCVILGTIAGQYTEKPLTTEGFCDPSGAYPRYIGNDVNILARGGINPETgqttkPDSVYIRDENTGVAV 161
Cdd:PHA02596 81 VYGHFLDKWKQNGLILGTYGGIYREKPNTNEGFSDPTGQYPRYVGNDVNVLARGGEVGYD-----PSSVVIQDANTDVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20218971 162 NPDDEPLDQIPVDDNPDFTIEKMLRGDEGYREKWYLDSEGYPTIGIGHLIIYKKTSDLGIINNELSKLVGREVTNGRLTA 241
Cdd:PHA02596 156 NPDDTPLDEIPPDDNPDFTIEKMLRRDEGIRLKVYWDSEGYPTIGIGHLIIREKTRDMAQINKLLSKQVGREVTGGRITA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20218971 242 EEVSKVFADDIEKTRRDMRKHPRIAPVYNKCNASRRMALENMAFQMGVGGLGKFKNSLAAMLAEEWKQAYDGLRQSVWAN 321
Cdd:PHA02596 236 EEASKLFARDLAKVQRDISRHSKVGPVYNKLNRSRQMALENMAFQMGVGGVAKFKNMLAAMLAGDWKKAYDALRDSLWAN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20218971 322 QTPGRSSRVSKIILTGNLESYGVIAPkkeesisDDPRARLRNAriAAYKTQRAEEEDPEAPFTPQDTRIMFKEPKSSYSA 401
Cdd:PHA02596 316 QTPGRASRVSKIILTGNLESYGVMVP-------DPPGRSLSTI--AAYKTAVATSSDPADPFTPGDTRIMFKEPKSSYSA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20218971 402 RYPYNHVYESESGHIIEIDDTPSHERYHRKHPSGTFEETRPDGTRVEKIEGDDYLIVKQGRKVNVKGNLQVVVEGDAQVY 481
Cdd:PHA02596 387 EYPYNHVMESESGHIQEFDDTPGHERYRRVHPTGTYEEIRPDGTRVVKIVGDDYYIVKQDRNVNVKGNLKVVVEGDAIYY 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20218971 482 YMGNVMQTVDGNVTEFIRGNVNQTVEGTANMHVVGDVTAQLDANLTANVKGNAELMIEGNTTETIKGNYDLTVEGNFNMT 561
Cdd:PHA02596 467 NMGNVLQTIDGNVTIFVRGNVTKTVEGNGTLYVKGNVTVQVDGNLDATVKGNATTLVEGNQTNTVNGNYKLKVEGNFDMT 546
|
570 580 590
....*....|....*....|....*....|....*....
gi 20218971 562 VNGTKSDQVNGDWSrncgasvkdIASGTVKIDGSRIDLG 600
Cdd:PHA02596 547 VGGNWSEQMAGMSS---------IASGTYTIDGSRIDIG 576
|
|
| Gp5_OB |
pfam06714 |
Gp5 N-terminal OB domain; This domain is found at the N terminus of the Gp5 baseplate protein ... |
33-178 |
1.56e-81 |
|
Gp5 N-terminal OB domain; This domain is found at the N terminus of the Gp5 baseplate protein of bacteriophage T4. This domain binds to the Gp27 protein. This domain has the common OB fold.
Pssm-ID: 148361 Cd Length: 144 Bit Score: 252.39 E-value: 1.56e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20218971 33 GIHPSLSAHGDIQGLPTEDLLWITPVQDITSAAISGIGQSPTGIVEGSMVFGLALDERYLNCVILGTIAGQYTEKPLTTE 112
Cdd:pfam06714 1 GIHPEQKVKGDVQGIPTEDLLWMSPMQPITSAAVSGIGQSPTGIVEGTHVYGFFLDKWYQNGVILGTYPGIYKEKPNTNK 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20218971 113 GFCDPSGAYPRYIGNDVNILARGGINPETGQTTkpDSVYIRDENTGVAVNPDDEPLDQIPVDDNPD 178
Cdd:pfam06714 81 GFSDPNGQYPRYVGNDVNVLARGGKDPEVGYGS--SSNVIQDSNTDVAINPDDTPLDEIPPDDNPD 144
|
|
| T4-like_lys |
cd00735 |
bacteriophage T4-like lysozymes; Bacteriophage T4-like lysozymes hydrolyze the beta-1, ... |
180-341 |
4.91e-74 |
|
bacteriophage T4-like lysozymes; Bacteriophage T4-like lysozymes hydrolyze the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) in peptidoglycan heteropolymers of prokaryotic cell walls. Members include a variety of bacteriophages (T4, RB49, RB69, Aeh1), as well as Dictyostelium.
Pssm-ID: 381597 Cd Length: 146 Bit Score: 233.03 E-value: 4.91e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20218971 180 TIEKMLRGDEGYREKWYLDSEGYPTIGIGHLIIYKKTSdlgiinnelsklvgreVTNGRLTAEEVSKVFADDIEKTRRDM 259
Cdd:cd00735 1 TIREMLRQDEGYRLKAYKDTEGYPTIGIGHLIGKKGAS----------------LTNGTITKDEAEALFEQDVDRAVRDM 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20218971 260 RKHPRIAPVYNKCNASRRMALENMAFQMGVGGLGKFKNSLAAMLAEEWKQAYDGLRQSVWANQTPGRSSRVSKIILTGNL 339
Cdd:cd00735 65 LRNPKLAPVYAQLNAARRMALINMAFQMGVGGLAKFKNMLAAIKAGDWEEAADGMLNSLWAKQTPNRANRVSAVMRTGTW 144
|
..
gi 20218971 340 ES 341
Cdd:cd00735 145 AP 146
|
|
| Phage_lysozyme |
pfam00959 |
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin. |
202-326 |
7.18e-11 |
|
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.
Pssm-ID: 395766 [Multi-domain] Cd Length: 107 Bit Score: 59.29 E-value: 7.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20218971 202 YPTIGIGHliiykKTSDLGiinnelsklvgrevTNGRLTAEEVSKVFADDIEKTRRDMRKHPRIAPVynkcNASRRMALE 281
Cdd:pfam00959 1 YWTIGIGH-----NGKDVS--------------PHPRATKSEAAGRLQIDLDTAERCINQYHKVKDF----NPNQQDALV 57
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 20218971 282 NMAFQMGVGGLGkFKNSLAAMLAEEWKQAYDGLRQSV----WANQTPGR 326
Cdd:pfam00959 58 SLAFNVGCGKRG-FSTLLRAGNIGQWIKACSAIWKSLkagkVYNGLVNR 105
|
|
| lyz_endolysin_autolysin |
cd00737 |
endolysin and autolysin; The dsDNA phages of eubacteria use endolysins or muralytic enzymes in ... |
184-321 |
6.85e-08 |
|
endolysin and autolysin; The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.
Pssm-ID: 381599 [Multi-domain] Cd Length: 136 Bit Score: 51.75 E-value: 6.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20218971 184 MLRGDEGYREKWYLDSEGYPTIGIGHLIIYKKTSDLGIinnelsklvgrevtngrlTAEEVSKVFADDIEKTRRDMRKHP 263
Cdd:cd00737 4 LIKEFEGLRLKAYRDPAGVWTIGYGHTGGVVVKPGDTI------------------TEAQAEALLRQDLARFEAAVNRLV 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 20218971 264 RIAPvynkcNASRRMALENMAFQMGVGGlgkFKNS-LAAML-AEEWKQAYDGLRQSVWAN 321
Cdd:cd00737 66 KVPL-----NQNQFDALVSFAFNVGAGA---FKSStLLRKLnAGDYAGAADEFLRWNKAG 117
|
|
| RrrD |
COG3772 |
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis]; |
189-321 |
2.18e-07 |
|
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442986 [Multi-domain] Cd Length: 146 Bit Score: 50.61 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20218971 189 EGYREKWYLDSEGYPTIGIGHLiiykktsdlgiinnelsklvGREVTNG-RLTAEEVSKVFADDIEKTRRDMRKHPRIap 267
Cdd:COG3772 16 EGFRLKAYRDPAGVWTIGYGHT--------------------GKDVKPGdTITEEEAEALLAADLAKAEAAVRRLVKV-- 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 20218971 268 vynKCNASRRMALENMAFQMGVGGLGkfKNSLAAML-AEEWKQAYDGLRQSVWAN 321
Cdd:COG3772 74 ---PLTQNQFDALVSFAYNVGAGAFC--RSTLLRKLnAGDYAGACDELLRWVYAG 123
|
|
| lyz_P1 |
cd16901 |
P1 lysozyme Lyz-like proteins; Enterobacteria phage P1 lysozyme Lyz is secreted to the ... |
189-310 |
3.25e-05 |
|
P1 lysozyme Lyz-like proteins; Enterobacteria phage P1 lysozyme Lyz is secreted to the Escherichia coli periplasm where it is membrane bound and inactive. Activation involves the release from the membrane, an intramolecular thiol-disulfide isomerization and extensive structural rearrangement of the N-terminal region. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.
Pssm-ID: 381620 [Multi-domain] Cd Length: 140 Bit Score: 44.13 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20218971 189 EGYREKWYLDSEGYPTIGIGHliiykkTSdlGIInnelsklvgrevTNGRLTAEEVSKVFADDIEKTRRdmrkhpriapV 268
Cdd:cd16901 14 EGCRRDPYKCPAGVPTIGIGS------TH--GVK------------PGDRYTDEQAAKRLAKDIKKAER----------C 63
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 20218971 269 YNKCNASRRM------ALENMAFQMGVgglGKFKNS--LAAMLAEEWKQA 310
Cdd:cd16901 64 VNRCFNGVPLpqgefdAYVSFAFNVGC---GAFCKStiYKKLQAGDYAAA 110
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
465-557 |
1.11e-04 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 45.55 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20218971 465 NVKGNLQVVVEGDAQvyymGNVMQTVDGNVTEFIRGNVNQTVEGTANMHVVGDVTAQLDANLTANVKGNAELMIEGNTTE 544
Cdd:PTZ00341 938 HLKEHAEANIEEDAE----ENVEEDAEENVEENVEENVEENVEENVEENVEENVEENVEENVEENVEENIEENVEENVEE 1013
|
90
....*....|...
gi 20218971 545 TIKGNYDLTVEGN 557
Cdd:PTZ00341 1014 NIEENVEEYDEEN 1026
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
458-555 |
1.18e-04 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 45.16 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20218971 458 VKQGRKVNVKGNLQVVVEGDAQvyymGNVMQTVDGNVTEFIRGNVNQTVEGTANMHVVGDVTAQLDANLTANVKGNAELM 537
Cdd:PTZ00341 939 LKEHAEANIEEDAEENVEEDAE----ENVEENVEENVEENVEENVEENVEENVEENVEENVEENVEENIEENVEENVEEN 1014
|
90
....*....|....*...
gi 20218971 538 IEGNTTETIKGNYDLTVE 555
Cdd:PTZ00341 1015 IEENVEEYDEENVEEVEE 1032
|
|
| 34 |
PHA02584 |
long tail fiber, proximal subunit; Provisional |
485-573 |
7.06e-04 |
|
long tail fiber, proximal subunit; Provisional
Pssm-ID: 222890 [Multi-domain] Cd Length: 1229 Bit Score: 42.82 E-value: 7.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20218971 485 NVMQTVDGnvTEFIRGNVNQTVEG----TANMHVVGDVTAQLDANLTANVKGNAELMIEGNTTETIKgnYDLTVEGNFNM 560
Cdd:PHA02584 888 LKLDGLDS--AQFIRRDIDQTVNGsltfTKNTNLSAPLVSSSTATFGGSVTANSTLTTQNTSNGTVV--VVDETSIAFYS 963
|
90
....*....|...
gi 20218971 561 TVNGTKSDQVNGD 573
Cdd:PHA02584 964 QNNTTGNIVFNID 976
|
|
| Gp5_C |
pfam06715 |
Gp5 C-terminal repeat (3 copies); This repeat composes the C-terminal part of the ... |
476-499 |
7.70e-03 |
|
Gp5 C-terminal repeat (3 copies); This repeat composes the C-terminal part of the bacteriophage T4 baseplate protein Gp5. This region of the protein forms a needle like projection from the baseplate that is presumed to puncture the bacterial cell membrane. Structurally three copies of the repeated region trimerize to form a beta solenoid type structure. This family also includes repeats from bacterial Vgr proteins.
Pssm-ID: 310962 [Multi-domain] Cd Length: 24 Bit Score: 34.18 E-value: 7.70e-03
|
|