|
Name |
Accession |
Description |
Interval |
E-value |
| C1Q |
smart00110 |
Complement component C1q domain; Globular domain found in many collagens and eponymously in ... |
524-652 |
9.90e-48 |
|
Complement component C1q domain; Globular domain found in many collagens and eponymously in complement C1q. When part of full length proteins these domains form a 'bouquet' due to the multimerization of heterotrimers. The C1q fold is similar to that of tumour necrosis factor.
Pssm-ID: 128420 Cd Length: 135 Bit Score: 164.01 E-value: 9.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 524 SPVSAFTVATVTPYPPSGTPIKFDQVVYNAEQHYDPETGIFTCHIPGIYYFSYSMHVNGANALVALYKNGDPVMFTYDEY 603
Cdd:smart00110 5 QPRSAFSVIRSNRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQVMSTYDEY 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 61740433 604 NKGFVDQMSGSSVLQLNEQDTVYMQIpDDEANGVFAADNVHCSFSGFLI 652
Cdd:smart00110 85 QKGLYDVASGGALLQLRQGDQVWLEL-PDEKNGLYAGEYVDSTFSGFLL 132
|
|
| C1q |
pfam00386 |
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ... |
528-652 |
8.78e-44 |
|
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement system.
Pssm-ID: 395310 [Multi-domain] Cd Length: 126 Bit Score: 152.82 E-value: 8.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 528 AFTVA-TVTPYPPSGTPIKFDQVVYNAEQHYDPETGIFTCHIPGIYYFSYSMH-VNGANALVALYKNGDPVMFTYDEYNK 605
Cdd:pfam00386 1 AFSAGrTTGLTAPNEQPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITtVDGKSLYVSLVKNGQEVVSFYDQPQK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 61740433 606 GFVDQMSGSSVLQLNEQDTVYMQIPDdeANGVFAAD-NVHCSFSGFLI 652
Cdd:pfam00386 81 GSLDVASGSVVLELQRGDEVWLQLTG--YNGLYYDGsDTDSTFSGFLL 126
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
171-421 |
2.60e-31 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 127.33 E-value: 2.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 171 GLPGQKGEMGVGVQGPAGERGPTGPVGPSGKPGAPG-VGLPGKPGAPGEAGKSGSPGRDGESGPMGPQGQKGQTGAPGvg 249
Cdd:NF038329 109 GLQQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGpAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG-- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 250 ipgKPGENGAPGMPGPTGPKGPQGVSGAPGapgvpgygKPGENGLKGDRGVPGSPGTtGQKGEPGAKGHTGYPGSPGAVG 329
Cdd:NF038329 187 ---PAGEKGPQGPRGETGPAGEQGPAGPAG--------PDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDG 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 330 PAGPQGAKGFPGERGQAGDKGEPGPmgppglKGHKGEQGAQGIEGKQGYPGATGQPGPRGATGAPGAKGELGHTGATGAP 409
Cdd:NF038329 255 PAGKDGPRGDRGEAGPDGPDGKDGE------RGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLP 328
|
250
....*....|..
gi 61740433 410 GTPGSVGPKGHP 421
Cdd:NF038329 329 GKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
106-334 |
2.70e-31 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 126.94 E-value: 2.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 106 GATGAPGLKGDTGAPGLQGPRGMPGPSGSPGPAGisATGKPGPAGLPGAMGPRGEQGFKGHPGIPGLPGQKGEmgvgvQG 185
Cdd:NF038329 129 GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKG--PAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE-----TG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 186 PAGERGPTGPVGPSGKPGAPGVGLPGKPGAPGEAGKSGSPGRDGESGPMGPQGQKGQTGAPgvGIPGKPGENGAPGMPGP 265
Cdd:NF038329 202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR--GDRGEAGPDGPDGKDGE 279
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 266 TGPKGPQGVSGAPGAPGVPGY-GKPGENGLKGDRGVPGSPGTTGQKGEPGAKGHTGYPGSPGAVGPAGPQ 334
Cdd:NF038329 280 RGPVGPAGKDGQNGKDGLPGKdGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQ 349
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
144-386 |
3.08e-30 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 123.86 E-value: 3.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 144 GKPGPAGLPGAMGPRGEQGFKGHPGIPGLPGQKGEMGV----GVQGPAGERGPTGPVGPSGKPGAPGV-GLPGKPGAPGE 218
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPqgerGEKGPAGPQGEAGPQGPAGKDGEAGAkGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 219 AGKSGSPGRDGESGPMGPQGQKGQTGAPGVGIPGKPGENGAPGMPGPTGPKGPQGVSgapgapgvpgyGKPGENGLKGDR 298
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPD-----------GPAGKDGPRGDR 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 299 GVPGSPGTTGQKGEPGAKGHTGYPGSPGAVGPAGPQGAKGFPGERGqagdkgepgpmgppgLKGHKGEQGAQGIEGKQGY 378
Cdd:NF038329 266 GEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG---------------LPGKDGKDGQPGKDGLPGK 330
|
....*...
gi 61740433 379 PGATGQPG 386
Cdd:NF038329 331 DGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
214-436 |
2.50e-25 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 109.22 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 214 GAPGEAGKSGSPGRDGESGPMGPQGQKGQTGAPG-VGIPGKPGENGAPGMPGPTGPKGPQGVSGAPGAPGvpgygKPGEN 292
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGpPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG-----PAGEK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 293 GLKGDRGVPGSPGTTGQKGEPGAKGHTGYPGSPGAVGPAGpQGAKGFPGERGQAGDKGEPGPMGPP------GLKGHKGE 366
Cdd:NF038329 192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAgkdgprGDRGEAGP 270
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 367 QGAQGIEGKQGYPGATGQPGPRGATGAPGAKGELGHTGATGAPGTPGSVGPKGHPGYPGATGEKGEQGAP 436
Cdd:NF038329 271 DGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
109-284 |
1.12e-20 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 95.36 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 109 GAPGLKGDTGAPGLQGPRGMPGPSGSPGPAGISATGKPGPAGLPG------AMGPRGEQGFKGHPGIPGLPGQkgemgvg 182
Cdd:NF038329 198 GETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGptgedgPQGPDGPAGKDGPRGDRGEAGP------- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 183 vQGPAGERGPTGPVGPSGKPGAPG-VGLPGKPGAPGEAGKSGSPGRDGESGPMGPQgqkgqtgapgvGIPGKPGENGAPG 261
Cdd:NF038329 271 -DGPDGKDGERGPVGPAGKDGQNGkDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKD-----------GLPGKDGKDGQPG 338
|
170 180
....*....|....*....|...
gi 61740433 262 MPGPTGPKGPQGVSGAPGAPGVP 284
Cdd:NF038329 339 KPAPKTPEVPQKPDTAPHTPKTP 361
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
258-469 |
3.86e-16 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 81.10 E-value: 3.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 258 GAPGMPGPTGPKGPQGVSGAPGapgvpgygkpgENGLKGDRGVPGSPGTTGQKGEPGAKGHTGYPGSPGAVGPAGPQGAK 337
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRG-----------DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAK 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 338 GFPGERGQAGDKGepgpmgppgLKGHKGEQGAQGIEGKQGYPGATGQPGPRGatgaPGAKGELGHTGATGAPGTPGSVGP 417
Cdd:NF038329 186 GPAGEKGPQGPRG---------ETGPAGEQGPAGPAGPDGEAGPAGEDGPAG----PAGDGQQGPDGDPGPTGEDGPQGP 252
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 61740433 418 KGHPGYPGATGEKGEQGAPGARgpvgpagpggppglkghpgipGAPGPAGLA 469
Cdd:NF038329 253 DGPAGKDGPRGDRGEAGPDGPD---------------------GKDGERGPV 283
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
339-464 |
1.89e-08 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 57.22 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 339 FPGERGQAGDKGEpgpmgppglKGHKGEQGAQGIEGKQGYPGATGQPGPRGATGAPGAKGELGHTGATGAPGTPGSVGPK 418
Cdd:NF038329 115 GDGEKGEPGPAGP---------AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAK 185
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 61740433 419 GHPGYPGATGEKGEQGAPGARGPVGPAGPGGPPGLKGHPGIPGAPG 464
Cdd:NF038329 186 GPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG 231
|
|
| Med15 |
pfam09606 |
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
121-422 |
2.72e-07 |
|
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: 53.86 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 121 GLQGPRGMPGPSGSPGPAGISATGKPGPAGLPGAMGPRGEQGFKGHPGIPGLPGQ---------KGEMGVGVQGPAGerg 191
Cdd:pfam09606 65 GGQGNGGMGGGQQGMPDPINALQNLAGQGTRPQMMGPMGPGPGGPMGQQMGGPGTasnllaslgRPQMPMGGAGFPS--- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 192 PTGPVGPSGKPGAPGVGLPGKPGAPGEAGKSGSPGRDGESGPMGPQGQKGQTGAPGVGipgKPGENGAPGMPGPTGPKGP 271
Cdd:pfam09606 142 QMSRVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQ---MPPQMGVPGMPGPADAGAQ 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 272 QGVSGAPGAPGVPGYGKPGENGLKGDRGVPGSPGTTGQKGEPGAKGHTGYPGSPGAVGPAGPQGAKGFPGER-GQAGDKG 350
Cdd:pfam09606 219 MGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQpGAMPNVM 298
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 61740433 351 EPGPMGPPGLKGHKGEQGAQGIEGKQGYPGATGQPGPRGatGAPGAKGELGHTGatgaPGTPGSVGPKGHPG 422
Cdd:pfam09606 299 SIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQG--GQVVALGGLNHLE----TWNPGNFGGLGANP 364
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
131-284 |
6.99e-07 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 52.68 E-value: 6.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 131 PSGSPGPAGISATGKPGPAGLPGAMGPRGEQGFKGHPGIPGLPGQKGEMGVGVQGPAGERGPTGPVGPSGKPGAPGVGLP 210
Cdd:PRK07764 621 PAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQ 700
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 61740433 211 GKPGAPGEAGKSGSPGRdGESGPMGPQGQKGQTGAPGVGIPGKPGENGAPGMPGPTGPKGPQGVSGAPGAPGVP 284
Cdd:PRK07764 701 PAPAPAATPPAGQADDP-AAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAA 773
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
380-514 |
8.05e-06 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 48.75 E-value: 8.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 380 GATGQPGPRGATGAPGAKGELGHTGATGAPGTPGSVGPKGHPGYPGATGEKGEQGAPGARGPVGPAGPGGPPGLKGHPGI 459
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 61740433 460 PGAPGPAGLAAKGIPGPQGPPGLPGSEGPAGIPGPSGPPGPPGPPGEVIFEKAQG 514
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQG 251
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
266-438 |
8.59e-05 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 45.41 E-value: 8.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 266 TGPKGPQGVSGAPGAPGVPGYGKPGENGLKGDRGVPGSPGTTGQKGEPGAKGHTGYPGSPGAVGPAGPQGAKGFPGERGQ 345
Cdd:COG5164 1 TGLYGPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 346 AGDKGEPGPMGPPGLKGHKGEQGAQGIEGKQGYPGATGQPGPRGATGAPGAKGELGHTGATGAPGTPGSVGPKGHPGYPG 425
Cdd:COG5164 81 TTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPG 160
|
170
....*....|...
gi 61740433 426 ATGEKGEQGAPGA 438
Cdd:COG5164 161 DGGSTTPPGPGGS 173
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
130-196 |
2.36e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 36.70 E-value: 2.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 61740433 130 GPSGSPGPagisatgkPGPAGLPGAMGPRGEQGFKGHPGIPGLPGQKGEMgvGVQGPAGERGPTGPV 196
Cdd:pfam01391 1 GPPGPPGP--------PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPP--GPPGPPGAPGAPGPP 57
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
361-515 |
6.54e-03 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 39.50 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 361 KGHKGEQGAQGIEGKQGYPGATGQPGPRGATGAPGAKGELGHTGATGAPGTPGSVGPKGHPGYPGATGEKGEQGAPGARg 440
Cdd:NF038329 119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPR- 197
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 61740433 441 pvgpagpggppglkghpgipGAPGPAGLAAKGIPgpqgppglpgsegpagipgpsgpPGPPGPPGEVIFEKAQGE 515
Cdd:NF038329 198 --------------------GETGPAGEQGPAGP-----------------------AGPDGEAGPAGEDGPAGP 229
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| C1Q |
smart00110 |
Complement component C1q domain; Globular domain found in many collagens and eponymously in ... |
524-652 |
9.90e-48 |
|
Complement component C1q domain; Globular domain found in many collagens and eponymously in complement C1q. When part of full length proteins these domains form a 'bouquet' due to the multimerization of heterotrimers. The C1q fold is similar to that of tumour necrosis factor.
Pssm-ID: 128420 Cd Length: 135 Bit Score: 164.01 E-value: 9.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 524 SPVSAFTVATVTPYPPSGTPIKFDQVVYNAEQHYDPETGIFTCHIPGIYYFSYSMHVNGANALVALYKNGDPVMFTYDEY 603
Cdd:smart00110 5 QPRSAFSVIRSNRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQVMSTYDEY 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 61740433 604 NKGFVDQMSGSSVLQLNEQDTVYMQIpDDEANGVFAADNVHCSFSGFLI 652
Cdd:smart00110 85 QKGLYDVASGGALLQLRQGDQVWLEL-PDEKNGLYAGEYVDSTFSGFLL 132
|
|
| C1q |
pfam00386 |
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ... |
528-652 |
8.78e-44 |
|
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement system.
Pssm-ID: 395310 [Multi-domain] Cd Length: 126 Bit Score: 152.82 E-value: 8.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 528 AFTVA-TVTPYPPSGTPIKFDQVVYNAEQHYDPETGIFTCHIPGIYYFSYSMH-VNGANALVALYKNGDPVMFTYDEYNK 605
Cdd:pfam00386 1 AFSAGrTTGLTAPNEQPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITtVDGKSLYVSLVKNGQEVVSFYDQPQK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 61740433 606 GFVDQMSGSSVLQLNEQDTVYMQIPDdeANGVFAAD-NVHCSFSGFLI 652
Cdd:pfam00386 81 GSLDVASGSVVLELQRGDEVWLQLTG--YNGLYYDGsDTDSTFSGFLL 126
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
171-421 |
2.60e-31 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 127.33 E-value: 2.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 171 GLPGQKGEMGVGVQGPAGERGPTGPVGPSGKPGAPG-VGLPGKPGAPGEAGKSGSPGRDGESGPMGPQGQKGQTGAPGvg 249
Cdd:NF038329 109 GLQQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGpAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG-- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 250 ipgKPGENGAPGMPGPTGPKGPQGVSGAPGapgvpgygKPGENGLKGDRGVPGSPGTtGQKGEPGAKGHTGYPGSPGAVG 329
Cdd:NF038329 187 ---PAGEKGPQGPRGETGPAGEQGPAGPAG--------PDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDG 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 330 PAGPQGAKGFPGERGQAGDKGEPGPmgppglKGHKGEQGAQGIEGKQGYPGATGQPGPRGATGAPGAKGELGHTGATGAP 409
Cdd:NF038329 255 PAGKDGPRGDRGEAGPDGPDGKDGE------RGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLP 328
|
250
....*....|..
gi 61740433 410 GTPGSVGPKGHP 421
Cdd:NF038329 329 GKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
106-334 |
2.70e-31 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 126.94 E-value: 2.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 106 GATGAPGLKGDTGAPGLQGPRGMPGPSGSPGPAGisATGKPGPAGLPGAMGPRGEQGFKGHPGIPGLPGQKGEmgvgvQG 185
Cdd:NF038329 129 GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKG--PAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE-----TG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 186 PAGERGPTGPVGPSGKPGAPGVGLPGKPGAPGEAGKSGSPGRDGESGPMGPQGQKGQTGAPgvGIPGKPGENGAPGMPGP 265
Cdd:NF038329 202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR--GDRGEAGPDGPDGKDGE 279
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 266 TGPKGPQGVSGAPGAPGVPGY-GKPGENGLKGDRGVPGSPGTTGQKGEPGAKGHTGYPGSPGAVGPAGPQ 334
Cdd:NF038329 280 RGPVGPAGKDGQNGKDGLPGKdGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQ 349
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
144-386 |
3.08e-30 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 123.86 E-value: 3.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 144 GKPGPAGLPGAMGPRGEQGFKGHPGIPGLPGQKGEMGV----GVQGPAGERGPTGPVGPSGKPGAPGV-GLPGKPGAPGE 218
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPqgerGEKGPAGPQGEAGPQGPAGKDGEAGAkGPAGEKGPQGP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 219 AGKSGSPGRDGESGPMGPQGQKGQTGAPGVGIPGKPGENGAPGMPGPTGPKGPQGVSgapgapgvpgyGKPGENGLKGDR 298
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPD-----------GPAGKDGPRGDR 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 299 GVPGSPGTTGQKGEPGAKGHTGYPGSPGAVGPAGPQGAKGFPGERGqagdkgepgpmgppgLKGHKGEQGAQGIEGKQGY 378
Cdd:NF038329 266 GEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG---------------LPGKDGKDGQPGKDGLPGK 330
|
....*...
gi 61740433 379 PGATGQPG 386
Cdd:NF038329 331 DGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
214-436 |
2.50e-25 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 109.22 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 214 GAPGEAGKSGSPGRDGESGPMGPQGQKGQTGAPG-VGIPGKPGENGAPGMPGPTGPKGPQGVSGAPGAPGvpgygKPGEN 292
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGpPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG-----PAGEK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 293 GLKGDRGVPGSPGTTGQKGEPGAKGHTGYPGSPGAVGPAGpQGAKGFPGERGQAGDKGEPGPMGPP------GLKGHKGE 366
Cdd:NF038329 192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAgkdgprGDRGEAGP 270
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 367 QGAQGIEGKQGYPGATGQPGPRGATGAPGAKGELGHTGATGAPGTPGSVGPKGHPGYPGATGEKGEQGAP 436
Cdd:NF038329 271 DGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
109-284 |
1.12e-20 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 95.36 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 109 GAPGLKGDTGAPGLQGPRGMPGPSGSPGPAGISATGKPGPAGLPG------AMGPRGEQGFKGHPGIPGLPGQkgemgvg 182
Cdd:NF038329 198 GETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGptgedgPQGPDGPAGKDGPRGDRGEAGP------- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 183 vQGPAGERGPTGPVGPSGKPGAPG-VGLPGKPGAPGEAGKSGSPGRDGESGPMGPQgqkgqtgapgvGIPGKPGENGAPG 261
Cdd:NF038329 271 -DGPDGKDGERGPVGPAGKDGQNGkDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKD-----------GLPGKDGKDGQPG 338
|
170 180
....*....|....*....|...
gi 61740433 262 MPGPTGPKGPQGVSGAPGAPGVP 284
Cdd:NF038329 339 KPAPKTPEVPQKPDTAPHTPKTP 361
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
258-469 |
3.86e-16 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 81.10 E-value: 3.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 258 GAPGMPGPTGPKGPQGVSGAPGapgvpgygkpgENGLKGDRGVPGSPGTTGQKGEPGAKGHTGYPGSPGAVGPAGPQGAK 337
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRG-----------DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAK 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 338 GFPGERGQAGDKGepgpmgppgLKGHKGEQGAQGIEGKQGYPGATGQPGPRGatgaPGAKGELGHTGATGAPGTPGSVGP 417
Cdd:NF038329 186 GPAGEKGPQGPRG---------ETGPAGEQGPAGPAGPDGEAGPAGEDGPAG----PAGDGQQGPDGDPGPTGEDGPQGP 252
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 61740433 418 KGHPGYPGATGEKGEQGAPGARgpvgpagpggppglkghpgipGAPGPAGLA 469
Cdd:NF038329 253 DGPAGKDGPRGDRGEAGPDGPD---------------------GKDGERGPV 283
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
339-464 |
1.89e-08 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 57.22 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 339 FPGERGQAGDKGEpgpmgppglKGHKGEQGAQGIEGKQGYPGATGQPGPRGATGAPGAKGELGHTGATGAPGTPGSVGPK 418
Cdd:NF038329 115 GDGEKGEPGPAGP---------AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAK 185
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 61740433 419 GHPGYPGATGEKGEQGAPGARGPVGPAGPGGPPGLKGHPGIPGAPG 464
Cdd:NF038329 186 GPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG 231
|
|
| Med15 |
pfam09606 |
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
121-422 |
2.72e-07 |
|
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: 53.86 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 121 GLQGPRGMPGPSGSPGPAGISATGKPGPAGLPGAMGPRGEQGFKGHPGIPGLPGQ---------KGEMGVGVQGPAGerg 191
Cdd:pfam09606 65 GGQGNGGMGGGQQGMPDPINALQNLAGQGTRPQMMGPMGPGPGGPMGQQMGGPGTasnllaslgRPQMPMGGAGFPS--- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 192 PTGPVGPSGKPGAPGVGLPGKPGAPGEAGKSGSPGRDGESGPMGPQGQKGQTGAPGVGipgKPGENGAPGMPGPTGPKGP 271
Cdd:pfam09606 142 QMSRVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQ---MPPQMGVPGMPGPADAGAQ 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 272 QGVSGAPGAPGVPGYGKPGENGLKGDRGVPGSPGTTGQKGEPGAKGHTGYPGSPGAVGPAGPQGAKGFPGER-GQAGDKG 350
Cdd:pfam09606 219 MGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQpGAMPNVM 298
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 61740433 351 EPGPMGPPGLKGHKGEQGAQGIEGKQGYPGATGQPGPRGatGAPGAKGELGHTGatgaPGTPGSVGPKGHPG 422
Cdd:pfam09606 299 SIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQG--GQVVALGGLNHLE----TWNPGNFGGLGANP 364
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
131-284 |
6.99e-07 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 52.68 E-value: 6.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 131 PSGSPGPAGISATGKPGPAGLPGAMGPRGEQGFKGHPGIPGLPGQKGEMGVGVQGPAGERGPTGPVGPSGKPGAPGVGLP 210
Cdd:PRK07764 621 PAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQ 700
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 61740433 211 GKPGAPGEAGKSGSPGRdGESGPMGPQGQKGQTGAPGVGIPGKPGENGAPGMPGPTGPKGPQGVSGAPGAPGVP 284
Cdd:PRK07764 701 PAPAPAATPPAGQADDP-AAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAA 773
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
380-514 |
8.05e-06 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 48.75 E-value: 8.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 380 GATGQPGPRGATGAPGAKGELGHTGATGAPGTPGSVGPKGHPGYPGATGEKGEQGAPGARGPVGPAGPGGPPGLKGHPGI 459
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 61740433 460 PGAPGPAGLAAKGIPGPQGPPGLPGSEGPAGIPGPSGPPGPPGPPGEVIFEKAQG 514
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQG 251
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
374-429 |
1.08e-05 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 43.25 E-value: 1.08e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 61740433 374 GKQGYPGATGQPGPRGATGAPGAKGELGHTGATGAPGTPGSVGPKGHPGYPGATGE 429
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
138-346 |
1.12e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 48.83 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 138 AGISATGKPGPAGLPGAMGPRGEQGFKGHPGIPGLPGQkgemgvgvqgPAGERGPTGPVGPSGKPGAPGVGLPGKPGAP- 216
Cdd:PRK07764 586 AVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAA----------PAAPAPAGAAAAPAEASAAPAPGVAAPEHHPk 655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 217 GEAGKSGSPGRDGESGPMGPQGQKGQTGAP-GVGIPGKPGENGAPGMPGPTGPKGPQGVSGAPGAPGVPGYGkpgeNGLK 295
Cdd:PRK07764 656 HVAVPDASDGGDGWPAKAGGAAPAAPPPAPaPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQG----ASAP 731
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 61740433 296 GDRGVPGSPGTTGQKGEPGAKGHTGYPGSPGAVGPAGPQGAKGFPGERGQA 346
Cdd:PRK07764 732 SPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
181-396 |
1.67e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 48.06 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 181 VGVQGPAGERGPTGPVGPSGKPGAPGVGLPGKPGAPGEAGKSGSPGRDGESGPmgpqgqkgQTGAPGVGIPGKPGENGAP 260
Cdd:PRK07764 586 AVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAE--------ASAAPAPGVAAPEHHPKHV 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 261 GMPGPTGPKGPQGVSGAPGAPGVPGygkpgenglkgdrGVPGSPGTTGQKGEPGAKGHTGYPGSPGAVGPAGPQGAkgfP 340
Cdd:PRK07764 658 AVPDASDGGDGWPAKAGGAAPAAPP-------------PAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQ---P 721
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 61740433 341 GERGQAGDKGEPGPMGPPGLKGHKGEQGAQGIEGKQGYPgaTGQPGPRGATGAPGA 396
Cdd:PRK07764 722 PQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPP--PPAPAPAAAPAAAPP 775
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
248-438 |
2.28e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 47.67 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 248 VGIPGKPGENGAPGMPGPTGPKGPQGVSGAPGAPGVPGYGKPGenGLKGDRGVPGSPGTTGQKGEPGAKGHTGYPGSPGA 327
Cdd:PRK07764 588 VGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPA--GAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDG 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 328 VGPAGPQGAKGFPGERGQAGDKGEPgpmgppglkghkgeQGAQGIEGKQGYPGATGQPGPRGATGAPGAKGELGHTGATG 407
Cdd:PRK07764 666 GDGWPAKAGGAAPAAPPPAPAPAAP--------------AAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAP 731
|
170 180 190
....*....|....*....|....*....|.
gi 61740433 408 APGTPGSVGPKGHPGYPGATGEKGEQGAPGA 438
Cdd:PRK07764 732 SPAADDPVPLPPEPDDPPDPAGAPAQPPPPP 762
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
287-343 |
2.93e-05 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 42.10 E-value: 2.93e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 61740433 287 GKPGENGLKGDRGVPGSPGTTGQKGEPGAKGHTGYPGSPGAVGPAGPQGAKGFPGER 343
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PRK14959 |
PRK14959 |
DNA polymerase III subunits gamma and tau; Provisional |
192-347 |
3.20e-05 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184923 [Multi-domain] Cd Length: 624 Bit Score: 46.98 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 192 PTGPVGPSGKPGAPGVGLPGKPGAPGEAGKSGSPGRDGESGPMGPQGQKGQTGAPGVgipGKPGENGAPGMPGPTGPKGP 271
Cdd:PRK14959 367 PVESLRPSGGGASAPSGSAAEGPASGGAATIPTPGTQGPQGTAPAAGMTPSSAAPAT---PAPSAAPSPRVPWDDAPPAP 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 272 QGVSGAP-GAPGVPGYGKpgenglkgdrgVPGSPGTTGQKGepGAKGHTGYPGSPGAVGPAGPQGAKGF----PGERGQA 346
Cdd:PRK14959 444 PRSGIPPrPAPRMPEASP-----------VPGAPDSVASAS--DAPPTLGDPSDTAEHTPSGPRTWDGFlefcQGRNGQG 510
|
.
gi 61740433 347 G 347
Cdd:PRK14959 511 G 511
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
182-236 |
4.79e-05 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 41.33 E-value: 4.79e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 61740433 182 GVQGPAGERGPTGPVGPSGKPGAPGV-GLPGKPGAPGEAGKSGSPGRDGESGPMGP 236
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPpGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
293-347 |
5.60e-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: 460189 [Multi-domain] Cd Length: 57 Bit Score: 41.33 E-value: 5.60e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 61740433 293 GLKGDRGVPGSPGTTGQKGEPGAKGHTGYPGSPGAVGPAGPQGAKGFPGERGQAG 347
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
266-438 |
8.59e-05 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 45.41 E-value: 8.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 266 TGPKGPQGVSGAPGAPGVPGYGKPGENGLKGDRGVPGSPGTTGQKGEPGAKGHTGYPGSPGAVGPAGPQGAKGFPGERGQ 345
Cdd:COG5164 1 TGLYGPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 346 AGDKGEPGPMGPPGLKGHKGEQGAQGIEGKQGYPGATGQPGPRGATGAPGAKGELGHTGATGAPGTPGSVGPKGHPGYPG 425
Cdd:COG5164 81 TTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPG 160
|
170
....*....|...
gi 61740433 426 ATGEKGEQGAPGA 438
Cdd:COG5164 161 DGGSTTPPGPGGS 173
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
229-284 |
1.90e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 39.78 E-value: 1.90e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 61740433 229 GESGPMGPQGQKGQTGAPG-VGIPGKPGENGAPGMPGPTGPKGPQGVSGAPGAPGVP 284
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGpPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
107-291 |
2.14e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.59 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 107 ATGAPGlkGDTGAPGLQGPRGMPGPSGSPGPAGISATGKPGPAGLPGAMGPRGEQGFKGHPGIPGLPGqkgemgvGVQGP 186
Cdd:PRK07764 617 APAAPA--APAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPP-------PAPAP 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 187 AGERGPTGPVGPSGKPGAPGVGLPGKPGAPGEAGksgspgrdgeSGPMGPQGQKGQTGAPGVGIPGKPGENGAPGMPGPT 266
Cdd:PRK07764 688 AAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQP----------PQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQ 757
|
170 180
....*....|....*....|....*
gi 61740433 267 GPkGPQGVSGAPGAPGVPGYGKPGE 291
Cdd:PRK07764 758 PP-PPPAPAPAAAPAAAPPPSPPSE 781
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
235-285 |
3.77e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 38.63 E-value: 3.77e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 61740433 235 GPQGQKGQTGAPGvgIPGKPGENGAPGMPGPTGPKGPQGVSGAPGAPGVPG 285
Cdd:pfam01391 1 GPPGPPGPPGPPG--PPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
365-421 |
5.33e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 38.24 E-value: 5.33e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 61740433 365 GEQGAQGIEGKQGYPGATGQPGPRGATGAPGAKGELGHTGATGAPGTPGSVGPKGHP 421
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
299-470 |
5.60e-04 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 43.09 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 299 GVPGSPGTTGQKGEPGAKGHTGYPGSPGAVGPAGPQGAKGFPGERGQAGDKGEPGPMGPPGLKGHKGEQGAQGIEGKQGY 378
Cdd:COG5164 7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 379 PGATGQPGPRGATGAPGAKGELGHTGATGAPGTPGSVGPKGhPGYPGATGEKGEQGAPGARGPVGPAGPGGPPGLKGHPG 458
Cdd:COG5164 87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTT-PPSGGSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGST 165
|
170
....*....|..
gi 61740433 459 IPGAPGPAGLAA 470
Cdd:COG5164 166 TPPGPGGSTTPP 177
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
228-436 |
5.78e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 43.05 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 228 DGESGPMGPQGQKGQTGAPGVGIPGKPGengAPGMPGPTGPKGPQGVSGAPG-APGVPGYGKPGENGLKGDRGVPGSP-G 305
Cdd:PRK07764 589 GPAPGAAGGEGPPAPASSGPPEEAARPA---APAAPAAPAAPAPAGAAAAPAeASAAPAPGVAAPEHHPKHVAVPDASdG 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 306 TTGQKGEPGAKGHTGYPGSPGAVGPAGPQGAKGFPGERGQAGdkgepgpmgppglkGHKGEQGAQGIEGKQGYPGATGQP 385
Cdd:PRK07764 666 GDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAA--------------TPPAGQADDPAAQPPQAAQGASAP 731
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 61740433 386 GPRGATGAPGAKGELGHTGATGAPGTPGSVGPKGHPGYPGATGEKGEQGAP 436
Cdd:PRK07764 732 SPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
200-260 |
5.99e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 38.24 E-value: 5.99e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 61740433 200 GKPGAPGvgLPGKPGAPGEAGKSGSPGRDGESGPMGPQGQKGQTGAPgvGIPGKPGENGAP 260
Cdd:pfam01391 1 GPPGPPG--PPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPP--GPPGAPGAPGPP 57
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
107-425 |
7.18e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.85 E-value: 7.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 107 ATGAPGLKGDTGAPGLQGPRGMPGPSGSPGPAGISATGKPGPAGLPGAMGPRGEQGFKGHPG--IPGLPGQKGEMGVGVQ 184
Cdd:PHA03307 119 PTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEetARAPSSPPAEPPPSTP 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 185 GPAGERGPTGPVGPSGKPGAPGVGLPGKPGA--PGEAGKSGSPGRDGESG-------PMGPQGQKGQTGAPGVGIPGKPG 255
Cdd:PHA03307 199 PAAASPRPPRRSSPISASASSPAPAPGRSAAddAGASSSDSSSSESSGCGwgpenecPLPRPAPITLPTRIWEASGWNGP 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 256 ENGAPGMPGPTGPKGPQGVSgAPGAPGVPGYGKPGENGLKGDRGVPGSPGTTGQKGEPGAKGHTGyPGSPGAVGPAGPQG 335
Cdd:PHA03307 279 SSRPGPASSSSSPRERSPSP-SPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVS-PGPSPSRSPSPSRP 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 336 AKGFPGERGQAGDKGEPGPMGPPGLKGHKGEQGAQGIEGKQGYPGATGQPGPRGAT--GAPGAKGELGHTGATGAPGTP- 412
Cdd:PHA03307 357 PPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPrpSPLDAGAASGAFYARYPLLTPs 436
|
330
....*....|...
gi 61740433 413 GSVGPKGHPGYPG 425
Cdd:PHA03307 437 GEPWPGSPPPPPG 449
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
130-196 |
2.36e-03 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 36.70 E-value: 2.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 61740433 130 GPSGSPGPagisatgkPGPAGLPGAMGPRGEQGFKGHPGIPGLPGQKGEMgvGVQGPAGERGPTGPV 196
Cdd:pfam01391 1 GPPGPPGP--------PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPP--GPPGPPGAPGAPGPP 57
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
253-398 |
2.92e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 40.34 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 253 KPGENGAPGMPGPTGPKGPQGVSGAPGAPGVPGYGKPGENGLKGDRGVPGSPGTTGQKGEPGAKGHTGYPGSPGAVGPAG 332
Cdd:PHA03169 80 RHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSP 159
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 61740433 333 PQGAKGFPGERGQAGDKGEPGPMGPPGLKGHKGEQGAQGIEGKQGYPGA--TGQPGPRGATGAPGAKG 398
Cdd:PHA03169 160 NQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPdePGEPQSPTPQQAPSPNT 227
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
218-391 |
4.55e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 39.95 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 218 EAGKSGSPGRDGESGPMGPQGQKGQTGAPGVGIPGKPGENGA-PGMPGPTGPKGPQGVSGAPGAPGVPGYGKPGENGLKG 296
Cdd:PHA03169 77 EESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLsPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHN 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 297 DRGVPGSPGTTGQKGEPGAKGHTGYPGSPGAVGPAGPQGAKGFPGERGQAGDKGEPGPMGPPGLKGHKGEQGAQGIEGKQ 376
Cdd:PHA03169 157 PSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDE 236
|
170
....*....|....*
gi 61740433 377 GYPGATGQPGPRGAT 391
Cdd:PHA03169 237 PTEPEREGPPFPGHR 251
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
121-277 |
5.85e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 39.57 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 121 GLQGPRGMPGPSGSPGPAGISATGKPGPAGLPGAMGPRGEQGFKGHPGIPGLPGQKGemgvgvqGPAGERGPTGPVGPSG 200
Cdd:PHA03169 82 GEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPP-------SPPSHPGPHEPAPPES 154
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 61740433 201 KPGAPGVGLPGKPGAPGEAGKSGSPGRDGESGPMGPQGQKGQTGAPGVGIPGKPGENGAPGMPGPTGPKGPQGVSGA 277
Cdd:PHA03169 155 HNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAV 231
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
108-285 |
6.11e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 39.57 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 108 TGAPGLKGDTGAPGLQGPRGmpGPSGSPGPAGISATGKPGPAGLPGAMGPRGEQGfkghpgipglpGQKGEMGVGVQGPA 187
Cdd:PHA03169 104 TPSPSGSAEELASGLSPENT--SGSSPESPASHSPPPSPPSHPGPHEPAPPESHN-----------PSPNQQPSSFLQPS 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 188 GERGPTGPVGPSGKPgAPGVGLPGKPGAPGEAGKSGSPG-RDGESGPMGPQGQKGQTGAPGVGIPGKPGENGAPGmPGPT 266
Cdd:PHA03169 171 HEDSPEEPEPPTSEP-EPDSPGPPQSETPTSSPPPQSPPdEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREG-PPFP 248
|
170
....*....|....*....
gi 61740433 267 GPKGPQGVSGAPGAPGVPG 285
Cdd:PHA03169 249 GHRSHSYTVVGWKPSTRPG 267
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
361-515 |
6.54e-03 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 39.50 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61740433 361 KGHKGEQGAQGIEGKQGYPGATGQPGPRGATGAPGAKGELGHTGATGAPGTPGSVGPKGHPGYPGATGEKGEQGAPGARg 440
Cdd:NF038329 119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPR- 197
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 61740433 441 pvgpagpggppglkghpgipGAPGPAGLAAKGIPgpqgppglpgsegpagipgpsgpPGPPGPPGEVIFEKAQGE 515
Cdd:NF038329 198 --------------------GETGPAGEQGPAGP-----------------------AGPDGEAGPAGEDGPAGP 229
|
|
| |
