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Conserved domains on  [gi|940372728|emb|CDK24026|]
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phage tail fibre [Escherichia phage P14437]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 193-494 9.76e-37

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 143.12  E-value: 9.76e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 193 RGPRGPQGETGPKGDVGPKGETGPVGPQGPAGPKGERGDVGAQGAVGPAGPRGEKGEQGERGPQGIPGLKGDTGERGPKG 272
Cdd:NF038329 122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 273 DQGDMGPKGEkgdpGGPAGPQGPKGERGEAGPQGPmGARGERGETGPRGEPGPAGPRGERGETGPQGPRGEPGPAgsaan 352
Cdd:NF038329 202 PAGEQGPAGP----AGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD----- 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 353 vadattaqkgivqlssatdsddeakaatpkavkaamdvaneaktkaeeaaagggvpGPKGDKGDSGPAGPAGPRGVQGPK 432
Cdd:NF038329 272 --------------------------------------------------------GPDGKDGERGPVGPAGKDGQNGKD 295

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940372728 433 GDPGPQGPKGDTGAAGAKGEKGATGATGPQGPKGDTGAAGPAGPQGPKG-------DTGAAGPAGPQGP 494
Cdd:NF038329 296 GLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTpevpqkpDTAPHTPKTPQIP 364
Phage_fiber_2 pfam03406
Phage tail fibre repeat; This repeat is found in the tail fibres of phage. For example protein ...
 357-392 5.15e-13

Phage tail fibre repeat; This repeat is found in the tail fibres of phage. For example protein K. The repeats are about 40 residues long.


:

Pssm-ID: 427282 [Multi-domain]  Cd Length: 38  Bit Score: 63.49  E-value: 5.15e-13
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 940372728  357 TTAQKGIVQLSSATDSDDEAKAATPKAVKAAMDVAN 392
Cdd:pfam03406   1 TLTQKGIVQLSSATNSTSETLAATPKAVKTAYDNAN 36
Peptidase_S74 pfam13884
Chaperone of endosialidase; This is the very C-terminal, chaperone, domain of the ...
 600-652 6.41e-11

Chaperone of endosialidase; This is the very C-terminal, chaperone, domain of the bacteriophage protein endosialidase. It releases itself, via the serine-lysine dyad at the N-terminus, from the remainder of the end-tail-spike. Cleavage occurs after the threonine which is the final residue of the End-tail-spike family, pfam12219. The endosialidase protein forms homotrimeric molecules in bacteriophages. The catalytic dyad allows this portion of the molecule to be cleaved from the more N-terminal region such that the latter can fold and bind to polysialic acid in the bacterial outer envelope.


:

Pssm-ID: 404724  Cd Length: 56  Bit Score: 58.03  E-value: 6.41e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 940372728  600 SDKRNKRNLVKLD-NALDRLEALTGYLYeiQY----SADGWQTSVGLIAQDAQKALPE 652
Cdd:pfam13884   1 SDRRLKTNIKPIDeNALDKIEQLEPVSY--DYkdekGEDGARRHIGVIAQEVEEVFPE 56
PRK12678 super family cl36163
transcription termination factor Rho; Provisional
 71-276 1.83e-05

transcription termination factor Rho; Provisional


The actual alignment was detected with superfamily member PRK12678:

Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 47.98  E-value: 1.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728  71 RRLNEDTATKNTQATQSKESAAASAKSASDSAKTATSRAAEAGQKATDATEAATRAVTAAGNAEESSTRAGESEKAAGAD 150
Cdd:PRK12678  77 ARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEA 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 151 AEKARQHAEKARLAQESAGEilkraeaatvsaEEARRMAENARGPRGPQGETGPKGDVGPKGETGPVGPQGPAGPKGERG 230
Cdd:PRK12678 157 RADAAERTEEEERDERRRRG------------DREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGG 224

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 940372728 231 DVGAQGAVGPAGPRGEKGEQGERGPQGIPGLKGDTGERGPKGDQGD 276
Cdd:PRK12678 225 DRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDRD 270
SPT5 super family cl34925
Transcription elongation factor SPT5 [Transcription];
436-559 2.16e-05

Transcription elongation factor SPT5 [Transcription];


The actual alignment was detected with superfamily member COG5164:

Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 47.72  E-value: 2.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 436 GPQGPK--GDTGAAGAKGEKGATGATGPQGPKGDTGAAGPAGPQGPKGDTGAAGPAGPQGPKGDTGAAGPAGAQGPKGDK 513
Cdd:COG5164    2 GLYGPGktGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGT 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 940372728 514 GDPGVAGPAGPAGAPGPKGDKGDPGVAGPAGPEGPQGPKGDTGAPG 559
Cdd:COG5164   82 TPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTT 127
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 193-494 9.76e-37

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: 143.12  E-value: 9.76e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 193 RGPRGPQGETGPKGDVGPKGETGPVGPQGPAGPKGERGDVGAQGAVGPAGPRGEKGEQGERGPQGIPGLKGDTGERGPKG 272
Cdd:NF038329 122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 273 DQGDMGPKGEkgdpGGPAGPQGPKGERGEAGPQGPmGARGERGETGPRGEPGPAGPRGERGETGPQGPRGEPGPAgsaan 352
Cdd:NF038329 202 PAGEQGPAGP----AGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD----- 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 353 vadattaqkgivqlssatdsddeakaatpkavkaamdvaneaktkaeeaaagggvpGPKGDKGDSGPAGPAGPRGVQGPK 432
Cdd:NF038329 272 --------------------------------------------------------GPDGKDGERGPVGPAGKDGQNGKD 295

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940372728 433 GDPGPQGPKGDTGAAGAKGEKGATGATGPQGPKGDTGAAGPAGPQGPKG-------DTGAAGPAGPQGP 494
Cdd:NF038329 296 GLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTpevpqkpDTAPHTPKTPQIP 364
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 194-495 1.43e-35

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: 140.04  E-value: 1.43e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 194 GPRGPQGETGPKGDVGPKGETGPVGPQGPAGPKGERGDVGAQGAVGPAGPRGEKGEQGERGPQGIPGLKGDTGERGPKGD 273
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 274 QGDMGPkgekgdpggpagpqgpkgeRGEAGPQGPMGARGERGETGPRGEPGPAGpRGERGETGPQGPRGEPGPAGSAanv 353
Cdd:NF038329 197 RGETGP-------------------AGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPD--- 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 354 adattaqkgivqlssatdsddeakaatpkavkaamdvaneaktkaeeaaaggGVPGPKGDKGDSGPAGPAGPRGVQGPKG 433
Cdd:NF038329 254 ----------------------------------------------------GPAGKDGPRGDRGEAGPDGPDGKDGERG 281

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 940372728 434 DPGPQGPKGDTGAAGAKGEKGATGATGPQGPKGDTGAAGPAGPQGPKGDTGAAGPAGPQGPK 495
Cdd:NF038329 282 PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 209-551 8.08e-35

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: 137.73  E-value: 8.08e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 209 GPKGETGPVGPQGPAGPKGERGDVGAQGAVGPAGPRGEKGEQGERGPQGipglkgdtgERGPKGDQGDMGPKGEkgdpgg 288
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAG---------PQGEAGPQGPAGKDGE------ 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 289 pagpqgpkgeRGEAGPQGPMGARGERGETGPRGEPGPAGPRGERGETGPQGPRGEPGPAGSaanvadattaqkgivqlss 368
Cdd:NF038329 182 ----------AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD------------------- 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 369 atdsddeakaatpkavkaamdvaneaktkaeeaaagggvpgpkgdkgdsgpaGPAGPRGVQGPKGDPGPQGPKGDTGAAG 448
Cdd:NF038329 233 ----------------------------------------------------GQQGPDGDPGPTGEDGPQGPDGPAGKDG 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 449 AKGEKGATGATGPQGPKGDTGAAGPAGPQGPKGDTGAAGPAGPQGPKGdtgaagpagaqgPKGDKGDPGVAGPAGPAGAP 528
Cdd:NF038329 261 PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG------------KDGLPGKDGKDGQPGKDGLP 328

                        330       340
                 ....*....|....*....|...
gi 940372728 529 GPKGDKGDPGVAGPAGPEGPQGP 551
Cdd:NF038329 329 GKDGKDGQPGKPAPKTPEVPQKP 351
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 300-562 6.36e-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: 123.48  E-value: 6.36e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 300 GEAGPQGPMGARGERGETGPRGEPGPAGPRGERGETGPQGPRGEPGPAGSAAnvadattaqkgivqlssatdSDDEAKAA 379
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG--------------------KDGEAGAK 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 380 TPKavkaamdvaneaktkaeeaaaggGVPGPKGDKGDSGPAGPAGPRGVQGPKGDPGPQGPKGDTGAAGaKGEKGATGAT 459
Cdd:NF038329 186 GPA-----------------------GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDP 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 460 GPQGPKGDTGAAGPAGPQGPKGDTGAAGPAGPQGPKGDTGAAGPAGAQGPKGDKGDPGVAGPAGPAGAPGPKGDKGDPGV 539
Cdd:NF038329 242 GPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ 321

                        250       260
                 ....*....|....*....|...
gi 940372728 540 AGPAGPEGPQGPKGDTGAPGQGT 562
Cdd:NF038329 322 PGKDGLPGKDGKDGQPGKPAPKT 344
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 412-563 2.93e-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: 2.93e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 412 GDKGDSGPAGPAGPRGVQGPKGDPGPQGPKGDTGAAGAKGEKGATGATGPQGPKGDTGAAGPAGPQGPKGDTGAAGPAGP 491
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 940372728 492 QGPKGDTGAAGPAGAQGPKGDKGdPGVAGPAGPAGAPGPKGDKGDPGVAGPAGPEGPQGPKGDTGAPGQGTE 563
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAG-PAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 409-559 1.54e-23

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: 104.22  E-value: 1.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 409 GPKGDKGDSGPAGPAGPRGVQGPKGDPGPQGPKGDTGAAGAKGEKGATGATGPQGPKGDTGAAGPAGPQGPKGDTGAAGP 488
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 940372728 489 AGPQGPKGDTGAAGPAGAQGPKGDKGDPGVAGPAGPAGAPGP--KGDKGDPGVAGPAGPEGPQGPKGDTGAPG 559
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDgdPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
189-498 5.14e-13

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 71.98  E-value: 5.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 189 AENARGPRGPQGETGPKGDVGPKGETGPVGPQGPAGPKGERGDVGAQGAVGPAGPRGEKGEQGERGPQGIPglkGDTGER 268
Cdd:COG5164    5 GPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPA---QNQGGT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 269 GPKGDQGDMGPkgekgdpggpagpqgpkgergeAGPQGPMGARGERGETGPRGEPGPAGPRGERGETGPQGprgepGPAG 348
Cdd:COG5164   82 TPAQNQGGTRP----------------------AGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPS-----GGST 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 349 SAANVADATTAQKGIVQLSSATDSDDEAKAATPKAVKAAMDVANEAKTKAEEAAAGGGVPGPKGDKGDSGPAGPAGPRGv 428
Cdd:COG5164  135 TPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDD- 213

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 940372728 429 QGPKGDPgpqgPKGDTGAAGAKGEKGATGATGPQGPKGDTGAAGPAGPQGPKGDTGAA--GPAGPQGPKGDT 498
Cdd:COG5164  214 KNGKGNP----PDDRGGKTGPKDQRPKTNPIERRGPERPEAAALPAELTALEAENRAAnpEPATKTIPETTT 281
Phage_fiber_2 pfam03406
Phage tail fibre repeat; This repeat is found in the tail fibres of phage. For example protein ...
 357-392 5.15e-13

Phage tail fibre repeat; This repeat is found in the tail fibres of phage. For example protein K. The repeats are about 40 residues long.


Pssm-ID: 427282 [Multi-domain]  Cd Length: 38  Bit Score: 63.49  E-value: 5.15e-13
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 940372728  357 TTAQKGIVQLSSATDSDDEAKAATPKAVKAAMDVAN 392
Cdd:pfam03406   1 TLTQKGIVQLSSATNSTSETLAATPKAVKTAYDNAN 36
Peptidase_S74 pfam13884
Chaperone of endosialidase; This is the very C-terminal, chaperone, domain of the ...
 600-652 6.41e-11

Chaperone of endosialidase; This is the very C-terminal, chaperone, domain of the bacteriophage protein endosialidase. It releases itself, via the serine-lysine dyad at the N-terminus, from the remainder of the end-tail-spike. Cleavage occurs after the threonine which is the final residue of the End-tail-spike family, pfam12219. The endosialidase protein forms homotrimeric molecules in bacteriophages. The catalytic dyad allows this portion of the molecule to be cleaved from the more N-terminal region such that the latter can fold and bind to polysialic acid in the bacterial outer envelope.


Pssm-ID: 404724  Cd Length: 56  Bit Score: 58.03  E-value: 6.41e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 940372728  600 SDKRNKRNLVKLD-NALDRLEALTGYLYeiQY----SADGWQTSVGLIAQDAQKALPE 652
Cdd:pfam13884   1 SDRRLKTNIKPIDeNALDKIEQLEPVSY--DYkdekGEDGARRHIGVIAQEVEEVFPE 56
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 105-340 1.94e-10

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 64.15  E-value: 1.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 105 ATSRAAEAGQKATDA-TEAATRAVTAAGNAEESSTRAGESEKAAGADAEKARQHAEKARLAQESAGEILKRAEAATVSAE 183
Cdd:PRK12678  53 AAIKEARGGGAAAAAaTPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRE 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 184 EARRMAENARGPRGPQGETGPKGDVGPKGETGPVGPQGPAGPKGERGDVGAQGAVGPAGPRGEKGEQGERGPQGIPGLKG 263
Cdd:PRK12678 133 RGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQG 212

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 940372728 264 DTGERGPKGDQGDmgpkGEKGDPGGPAGPQGPKGERGEAGPQGPMGARGERGETGPRGEpgpagPRGERGETGPQGP 340
Cdd:PRK12678 213 DRREERGRRDGGD----RRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFR-----DRDRRGRRGGDGG 280
COG5301 COG5301
Phage-related tail fiber protein [Mobilome: prophages, transposons];
350-404 2.00e-08

Phage-related tail fiber protein [Mobilome: prophages, transposons];


Pssm-ID: 444101 [Multi-domain]  Cd Length: 254  Bit Score: 55.83  E-value: 2.00e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 940372728 350 AANVADATTAQKGIVQLSSATDSDDEAKAATPKAVKAAMDVANEAKTKAEEAAAG 404
Cdd:COG5301  162 SRNHPDATLTEKGFVQLSSATDSNSETLAATPKAVKTAYDLADTAFVAASGNAAG 216
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 298-350 8.98e-08

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 49.03  E-value: 8.98e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 940372728  298 ERGEAGPQGPMGARGERGETGPRGEPGPAGPRGERGETGPQGPRGEPGPAGSA 350
Cdd:pfam01391   2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 71-276 1.83e-05

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 47.98  E-value: 1.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728  71 RRLNEDTATKNTQATQSKESAAASAKSASDSAKTATSRAAEAGQKATDATEAATRAVTAAGNAEESSTRAGESEKAAGAD 150
Cdd:PRK12678  77 ARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEA 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 151 AEKARQHAEKARLAQESAGEilkraeaatvsaEEARRMAENARGPRGPQGETGPKGDVGPKGETGPVGPQGPAGPKGERG 230
Cdd:PRK12678 157 RADAAERTEEEERDERRRRG------------DREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGG 224

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 940372728 231 DVGAQGAVGPAGPRGEKGEQGERGPQGIPGLKGDTGERGPKGDQGD 276
Cdd:PRK12678 225 DRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDRD 270
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
436-559 2.16e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 47.72  E-value: 2.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 436 GPQGPK--GDTGAAGAKGEKGATGATGPQGPKGDTGAAGPAGPQGPKGDTGAAGPAGPQGPKGDTGAAGPAGAQGPKGDK 513
Cdd:COG5164    2 GLYGPGktGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGT 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 940372728 514 GDPGVAGPAGPAGAPGPKGDKGDPGVAGPAGPEGPQGPKGDTGAPG 559
Cdd:COG5164   82 TPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTT 127
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 110-334 2.57e-04

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


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 44.60  E-value: 2.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728   110 AEAGQKATDATEAATRAVTAAG-NAEESSTRA---GESEKAAGADAEKARQHAEKARlaQESAGEILKRAEAATVSAEEA 185
Cdd:TIGR00927  636 AEAEHTGERTGEEGERPTEAEGeNGEESGGEAeqeGETETKGENESEGEIPAERKGE--QEGEGEIEAKEADHKGETEAE 713

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728   186 RRMAENARGPRGP----QGETGPKGDVGPKGETGPVGPQGPAGPKGERGDVGAQGAVGPAGPRGEkgEQGERGPQGIPGL 261
Cdd:TIGR00927  714 EVEHEGETEAEGTedegEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDE--DEGEIQAGEDGEM 791

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940372728   262 KGDTGERGPKGDQGDMGPKGEKGDPGGPAGPQGPKGERGEAGPQ---GPMGARGERGETGPRGEPGPAGPRGERGE 334
Cdd:TIGR00927  792 KGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQelnAENQGEAKQDEKGVDGGGGSDGGDSEEEE 867
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 469-558 7.55e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.16  E-value: 7.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728  469 GAAGPAGPQGPKGDTGAAGPAGPQGPKGDtgaagpagaqgpkgdkgdpgvagpagpagapgpKGDKGDPGVAGPAGPEGP 548
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGP---------------------------------PGEPGPPGPPGPPGPPGP 47

                          90
                  ....*....|
gi 940372728  549 QGPKGDTGAP 558
Cdd:pfam01391  48 PGAPGAPGPP 57
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 193-494 9.76e-37

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: 143.12  E-value: 9.76e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 193 RGPRGPQGETGPKGDVGPKGETGPVGPQGPAGPKGERGDVGAQGAVGPAGPRGEKGEQGERGPQGIPGLKGDTGERGPKG 272
Cdd:NF038329 122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 273 DQGDMGPKGEkgdpGGPAGPQGPKGERGEAGPQGPmGARGERGETGPRGEPGPAGPRGERGETGPQGPRGEPGPAgsaan 352
Cdd:NF038329 202 PAGEQGPAGP----AGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD----- 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 353 vadattaqkgivqlssatdsddeakaatpkavkaamdvaneaktkaeeaaagggvpGPKGDKGDSGPAGPAGPRGVQGPK 432
Cdd:NF038329 272 --------------------------------------------------------GPDGKDGERGPVGPAGKDGQNGKD 295

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940372728 433 GDPGPQGPKGDTGAAGAKGEKGATGATGPQGPKGDTGAAGPAGPQGPKG-------DTGAAGPAGPQGP 494
Cdd:NF038329 296 GLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTpevpqkpDTAPHTPKTPQIP 364
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 194-495 1.43e-35

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: 140.04  E-value: 1.43e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 194 GPRGPQGETGPKGDVGPKGETGPVGPQGPAGPKGERGDVGAQGAVGPAGPRGEKGEQGERGPQGIPGLKGDTGERGPKGD 273
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 274 QGDMGPkgekgdpggpagpqgpkgeRGEAGPQGPMGARGERGETGPRGEPGPAGpRGERGETGPQGPRGEPGPAGSAanv 353
Cdd:NF038329 197 RGETGP-------------------AGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPD--- 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 354 adattaqkgivqlssatdsddeakaatpkavkaamdvaneaktkaeeaaaggGVPGPKGDKGDSGPAGPAGPRGVQGPKG 433
Cdd:NF038329 254 ----------------------------------------------------GPAGKDGPRGDRGEAGPDGPDGKDGERG 281

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 940372728 434 DPGPQGPKGDTGAAGAKGEKGATGATGPQGPKGDTGAAGPAGPQGPKGDTGAAGPAGPQGPK 495
Cdd:NF038329 282 PVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 209-551 8.08e-35

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: 137.73  E-value: 8.08e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 209 GPKGETGPVGPQGPAGPKGERGDVGAQGAVGPAGPRGEKGEQGERGPQGipglkgdtgERGPKGDQGDMGPKGEkgdpgg 288
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAG---------PQGEAGPQGPAGKDGE------ 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 289 pagpqgpkgeRGEAGPQGPMGARGERGETGPRGEPGPAGPRGERGETGPQGPRGEPGPAGSaanvadattaqkgivqlss 368
Cdd:NF038329 182 ----------AGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD------------------- 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 369 atdsddeakaatpkavkaamdvaneaktkaeeaaagggvpgpkgdkgdsgpaGPAGPRGVQGPKGDPGPQGPKGDTGAAG 448
Cdd:NF038329 233 ----------------------------------------------------GQQGPDGDPGPTGEDGPQGPDGPAGKDG 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 449 AKGEKGATGATGPQGPKGDTGAAGPAGPQGPKGDTGAAGPAGPQGPKGdtgaagpagaqgPKGDKGDPGVAGPAGPAGAP 528
Cdd:NF038329 261 PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG------------KDGLPGKDGKDGQPGKDGLP 328

                        330       340
                 ....*....|....*....|...
gi 940372728 529 GPKGDKGDPGVAGPAGPEGPQGP 551
Cdd:NF038329 329 GKDGKDGQPGKPAPKTPEVPQKP 351
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 300-562 6.36e-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: 123.48  E-value: 6.36e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 300 GEAGPQGPMGARGERGETGPRGEPGPAGPRGERGETGPQGPRGEPGPAGSAAnvadattaqkgivqlssatdSDDEAKAA 379
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG--------------------KDGEAGAK 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 380 TPKavkaamdvaneaktkaeeaaaggGVPGPKGDKGDSGPAGPAGPRGVQGPKGDPGPQGPKGDTGAAGaKGEKGATGAT 459
Cdd:NF038329 186 GPA-----------------------GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDP 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 460 GPQGPKGDTGAAGPAGPQGPKGDTGAAGPAGPQGPKGDTGAAGPAGAQGPKGDKGDPGVAGPAGPAGAPGPKGDKGDPGV 539
Cdd:NF038329 242 GPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ 321

                        250       260
                 ....*....|....*....|...
gi 940372728 540 AGPAGPEGPQGPKGDTGAPGQGT 562
Cdd:NF038329 322 PGKDGLPGKDGKDGQPGKPAPKT 344
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 412-563 2.93e-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: 2.93e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 412 GDKGDSGPAGPAGPRGVQGPKGDPGPQGPKGDTGAAGAKGEKGATGATGPQGPKGDTGAAGPAGPQGPKGDTGAAGPAGP 491
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 940372728 492 QGPKGDTGAAGPAGAQGPKGDKGdPGVAGPAGPAGAPGPKGDKGDPGVAGPAGPEGPQGPKGDTGAPGQGTE 563
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAG-PAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 409-559 1.54e-23

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: 104.22  E-value: 1.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 409 GPKGDKGDSGPAGPAGPRGVQGPKGDPGPQGPKGDTGAAGAKGEKGATGATGPQGPKGDTGAAGPAGPQGPKGDTGAAGP 488
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 940372728 489 AGPQGPKGDTGAAGPAGAQGPKGDKGDPGVAGPAGPAGAPGP--KGDKGDPGVAGPAGPEGPQGPKGDTGAPG 559
Cdd:NF038329 197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDgdPGPTGEDGPQGPDGPAGKDGPRGDRGEAG 269
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
189-498 5.14e-13

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 71.98  E-value: 5.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 189 AENARGPRGPQGETGPKGDVGPKGETGPVGPQGPAGPKGERGDVGAQGAVGPAGPRGEKGEQGERGPQGIPglkGDTGER 268
Cdd:COG5164    5 GPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPA---QNQGGT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 269 GPKGDQGDMGPkgekgdpggpagpqgpkgergeAGPQGPMGARGERGETGPRGEPGPAGPRGERGETGPQGprgepGPAG 348
Cdd:COG5164   82 TPAQNQGGTRP----------------------AGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPS-----GGST 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 349 SAANVADATTAQKGIVQLSSATDSDDEAKAATPKAVKAAMDVANEAKTKAEEAAAGGGVPGPKGDKGDSGPAGPAGPRGv 428
Cdd:COG5164  135 TPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDD- 213

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 940372728 429 QGPKGDPgpqgPKGDTGAAGAKGEKGATGATGPQGPKGDTGAAGPAGPQGPKGDTGAA--GPAGPQGPKGDT 498
Cdd:COG5164  214 KNGKGNP----PDDRGGKTGPKDQRPKTNPIERRGPERPEAAALPAELTALEAENRAAnpEPATKTIPETTT 281
Phage_fiber_2 pfam03406
Phage tail fibre repeat; This repeat is found in the tail fibres of phage. For example protein ...
 357-392 5.15e-13

Phage tail fibre repeat; This repeat is found in the tail fibres of phage. For example protein K. The repeats are about 40 residues long.


Pssm-ID: 427282 [Multi-domain]  Cd Length: 38  Bit Score: 63.49  E-value: 5.15e-13
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 940372728  357 TTAQKGIVQLSSATDSDDEAKAATPKAVKAAMDVAN 392
Cdd:pfam03406   1 TLTQKGIVQLSSATNSTSETLAATPKAVKTAYDNAN 36
Peptidase_S74 pfam13884
Chaperone of endosialidase; This is the very C-terminal, chaperone, domain of the ...
 600-652 6.41e-11

Chaperone of endosialidase; This is the very C-terminal, chaperone, domain of the bacteriophage protein endosialidase. It releases itself, via the serine-lysine dyad at the N-terminus, from the remainder of the end-tail-spike. Cleavage occurs after the threonine which is the final residue of the End-tail-spike family, pfam12219. The endosialidase protein forms homotrimeric molecules in bacteriophages. The catalytic dyad allows this portion of the molecule to be cleaved from the more N-terminal region such that the latter can fold and bind to polysialic acid in the bacterial outer envelope.


Pssm-ID: 404724  Cd Length: 56  Bit Score: 58.03  E-value: 6.41e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 940372728  600 SDKRNKRNLVKLD-NALDRLEALTGYLYeiQY----SADGWQTSVGLIAQDAQKALPE 652
Cdd:pfam13884   1 SDRRLKTNIKPIDeNALDKIEQLEPVSY--DYkdekGEDGARRHIGVIAQEVEEVFPE 56
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 105-340 1.94e-10

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 64.15  E-value: 1.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 105 ATSRAAEAGQKATDA-TEAATRAVTAAGNAEESSTRAGESEKAAGADAEKARQHAEKARLAQESAGEILKRAEAATVSAE 183
Cdd:PRK12678  53 AAIKEARGGGAAAAAaTPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRE 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 184 EARRMAENARGPRGPQGETGPKGDVGPKGETGPVGPQGPAGPKGERGDVGAQGAVGPAGPRGEKGEQGERGPQGIPGLKG 263
Cdd:PRK12678 133 RGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQG 212

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 940372728 264 DTGERGPKGDQGDmgpkGEKGDPGGPAGPQGPKGERGEAGPQGPMGARGERGETGPRGEpgpagPRGERGETGPQGP 340
Cdd:PRK12678 213 DRREERGRRDGGD----RRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFR-----DRDRRGRRGGDGG 280
COG5301 COG5301
Phage-related tail fiber protein [Mobilome: prophages, transposons];
350-404 2.00e-08

Phage-related tail fiber protein [Mobilome: prophages, transposons];


Pssm-ID: 444101 [Multi-domain]  Cd Length: 254  Bit Score: 55.83  E-value: 2.00e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 940372728 350 AANVADATTAQKGIVQLSSATDSDDEAKAATPKAVKAAMDVANEAKTKAEEAAAG 404
Cdd:COG5301  162 SRNHPDATLTEKGFVQLSSATDSNSETLAATPKAVKTAYDLADTAFVAASGNAAG 216
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 298-350 8.98e-08

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 49.03  E-value: 8.98e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 940372728  298 ERGEAGPQGPMGARGERGETGPRGEPGPAGPRGERGETGPQGPRGEPGPAGSA 350
Cdd:pfam01391   2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 418-474 1.03e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 49.03  E-value: 1.03e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 940372728  418 GPAGPAGPRGVQGPKGDPGPQGPKGDTGAAGAKGEKGATGATGPQGPKGDTGAAGPA 474
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 427-481 1.14e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 48.64  E-value: 1.14e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 940372728  427 GVQGPKGDPGPQGPKGDTGAAGAKGEKGATGATGPQGPKGDTGAAGPAGPQGPKG 481
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 421-476 1.40e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 48.64  E-value: 1.40e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 940372728  421 GPAGPRGVQGPKGDPGPQGPKGDTGAAGAKGEKGATGATGPQGPKGDTGAAGPAGP 476
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 436-491 1.55e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 48.26  E-value: 1.55e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 940372728  436 GPQGPKGDTGAAGAKGEKGATGATGPQGPKGDTGAAGPAGPQGPKGDTGAAGPAGP 491
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 433-489 3.76e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.49  E-value: 3.76e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 940372728  433 GDPGPQGPKGDTGAAGAKGEKGATGATGPQGPKGDTGAAGPAGPQGPKGDTGAAGPA 489
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 197-253 4.06e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 47.10  E-value: 4.06e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 940372728  197 GPQGETGPKGDVGPKGETGPVGPQGPAGPKGERGDVGAQGAVGPAGPRGEKGEQGER 253
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 218-272 8.07e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 46.33  E-value: 8.07e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 940372728  218 GPQGPAGPKGERGDVGAQGAVGPAGPRGEKGEQGERGPQGIPGLKGDTGERGPKG 272
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 298-350 1.05e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.95  E-value: 1.05e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 940372728  298 ERGEAGPQGPMGARGERGETGPRGEPGPAGPRGERGETGPQGPRGEPGPAGSA 350
Cdd:pfam01391   5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 406-458 1.59e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.56  E-value: 1.59e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 940372728  406 GVPGPKGDKGDSGPAGPAGPRGVQGPKGDPGPQGPKGDTGAAGAKGEKGATGA 458
Cdd:pfam01391   4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 409-464 1.64e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.56  E-value: 1.64e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 940372728  409 GPKGDKGDSGPAGPAGPRGVQGPKGDPGPQGPKGDTGAAGAKGEKGATGATGPQGP 464
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 406-461 1.99e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.18  E-value: 1.99e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 940372728  406 GVPGPKGDKGDSGPAGPAGPRGVQGPKGDPGPQGPKGDTGAAGAKGEKGATGATGP 461
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 215-270 2.89e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.79  E-value: 2.89e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 940372728  215 GPVGPQGPAGPKGERGDVGAQGAVGPAGPRGEKGEQGERGPQGIPGLKGDTGERGP 270
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 212-268 3.92e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.41  E-value: 3.92e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 940372728  212 GETGPVGPQGPAGPKGERGDVGAQGAVGPAGPRGEKGEQGERGPQGIPGLKGDTGER 268
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 172-343 6.37e-06

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 49.52  E-value: 6.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 172 LKRAEAATVSAEEARRMAENARGPRGPQGETGPKGDVGPKGETGPVGPQGPAGPKGERGDVGAQGAVGPAGPRGEKGEQG 251
Cdd:PRK12678  55 IKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERG 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 252 ERGPQGIPGLKGDTGERGPKGDQGDMGPKGEKGDPGGPAGPQGPKGERGEAGPQGpMGARGERGETGPRGEPGPAGPRGE 331
Cdd:PRK12678 135 EAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGE-RGRREERGRDGDDRDRRDRREQGD 213

                        170
                 ....*....|..
gi 940372728 332 RGETGPQGPRGE 343
Cdd:PRK12678 214 RREERGRRDGGD 225
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 136-343 7.31e-06

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 49.13  E-value: 7.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 136 SSTRAGESEKAAGADAEKARQHAEKARLAQESAGEILKRAEAATVSAEEARRmaenARGPRGPQGETGPKGDVGPKGETG 215
Cdd:PRK12678  56 KEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPA----ARAAAAAAAEAASAPEAAQARERR 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 216 PVGPQGPAGPKGERGDVGAQGAVGPAGPRGEKGEQGERGPQGIPGLKGDTGERGPKGDQGDmgpkgekgdpggpagpqgp 295
Cdd:PRK12678 132 ERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGR------------------- 192

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 940372728 296 kgeRGEAGPQGPMGARGERGETGPRGEPGPAGPRGERGETGPQGPRGE 343
Cdd:PRK12678 193 ---REERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRRD 237
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 192-560 7.60e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.21  E-value: 7.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 192 ARGPRGPQGeTGPKGDVGPKGETGPVGPQGPAGPKGERGDVGAQGAVGPAGPRGEKGEQG-ERGPQGIPGLKGDTGERGP 270
Cdd:PRK07764 376 ARLERLERR-LGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPApAPAPAPPSPAGNAPAGGAP 454

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 271 KGDQGDMGPKGEKGDPGGPAGPQGPKGERGEAGPQGPMGARGERGETGPRGEPGPAGPR----------GERGE------ 334
Cdd:PRK07764 455 SPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRerwpeilaavPKRSRktwail 534

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 335 ------TGPQGPR---GEPGPA--------GSAANVADATTAQKGIVQLSSATdSDDEAKAATPKAVKAAmdVANEAKTK 397
Cdd:PRK07764 535 lpeatvLGVRGDTlvlGFSTGGlarrfaspGNAEVLVTALAEELGGDWQVEAV-VGPAPGAAGGEGPPAP--ASSGPPEE 611

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 398 AEEAAAGGGVPGPKGDKGDSGPAGPAGPRGVQGPKGDPGPQGPKGDTGAAGAKGEKGATGATGPQGPKGDTGAAGPAGPQ 477
Cdd:PRK07764 612 AARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPA 691

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 478 GPKGDTGAAGPAGPQGPKGDTGAAGPAGAQGPKGDKGDPGVAGPAGPAGAPGPKGDKGDPGVAGPAGPEGPQGPKGDTGA 557
Cdd:PRK07764 692 APAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPA 771


                 ...
gi 940372728 558 PGQ 560
Cdd:PRK07764 772 AAP 774
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 448-496 1.16e-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: 1.16e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 940372728  448 GAKGEKGATGATGPQGPKGDTGAAGPAGPQGPKGDTGAAGPAGPQGPKG 496
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 203-257 1.25e-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: 42.87  E-value: 1.25e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 940372728  203 GPKGDVGPKGETGPVGPQGPAGPKGERGDVGAQGAVGPAGPRGEKGEQGERGPQG 257
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 206-260 1.32e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.87  E-value: 1.32e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 940372728  206 GDVGPKGETGPVGPQGPAGPKGERGDVGAQGAVGPAGPRGEKGEQGERGPQGIPG 260
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 71-276 1.83e-05

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 47.98  E-value: 1.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728  71 RRLNEDTATKNTQATQSKESAAASAKSASDSAKTATSRAAEAGQKATDATEAATRAVTAAGNAEESSTRAGESEKAAGAD 150
Cdd:PRK12678  77 ARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEA 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 151 AEKARQHAEKARLAQESAGEilkraeaatvsaEEARRMAENARGPRGPQGETGPKGDVGPKGETGPVGPQGPAGPKGERG 230
Cdd:PRK12678 157 RADAAERTEEEERDERRRRG------------DREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGG 224

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 940372728 231 DVGAQGAVGPAGPRGEKGEQGERGPQGIPGLKGDTGERGPKGDQGD 276
Cdd:PRK12678 225 DRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDRD 270
PTZ00121 PTZ00121
MAEBL; Provisional
 108-213 1.94e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 1.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728  108 RAAEAGQKATDATEA--ATRAVTAAGNAEESSTRAGESEKA--AGADAEKARQHAEKARLAQESA--GEILKRAEAATVS 181
Cdd:PTZ00121 1432 KADEAKKKAEEAKKAdeAKKKAEEAKKAEEAKKKAEEAKKAdeAKKKAEEAKKADEAKKKAEEAKkkADEAKKAAEAKKK 1511

                          90       100       110
                  ....*....|....*....|....*....|..
gi 940372728  182 AEEARRMAENARGPRGPQGETGPKGDVGPKGE 213
Cdd:PTZ00121 1512 ADEAKKAEEAKKADEAKKAEEAKKADEAKKAE 1543
PTZ00121 PTZ00121
MAEBL; Provisional
 108-193 1.97e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728  108 RAAEAGQKATD---ATEAATRAVTAAGNAEESSTRAGESEKAAGADAEKARQHAEKARLAQESAGEILKRAEAATVSAEE 184
Cdd:PTZ00121 1303 KADEAKKKAEEakkADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA 1382


                  ....*....
gi 940372728  185 ARRMAENAR 193
Cdd:PTZ00121 1383 AKKKAEEKK 1391
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
436-559 2.16e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 47.72  E-value: 2.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 436 GPQGPK--GDTGAAGAKGEKGATGATGPQGPKGDTGAAGPAGPQGPKGDTGAAGPAGPQGPKGDTGAAGPAGAQGPKGDK 513
Cdd:COG5164    2 GLYGPGktGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGT 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 940372728 514 GDPGVAGPAGPAGAPGPKGDKGDPGVAGPAGPEGPQGPKGDTGAPG 559
Cdd:COG5164   82 TPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTT 127
PHA03169 PHA03169
hypothetical protein; Provisional
 111-324 2.61e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 47.27  E-value: 2.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 111 EAGQKATDATEAATRAVTAAGNAEESSTRAGESEKAAGADAEKARQHAEKARLAQESAGEILKRAEAATVSAEEARRMAE 190
Cdd:PHA03169  53 TSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPA 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 191 NARGPRGPQGETGPKGDVGPK--GETGPVGPQGPAGPKGERGDVGAQGAVGPAGPRGEKGEQGERGPQGIPGLKGDTGER 268
Cdd:PHA03169 133 SHSPPPSPPSHPGPHEPAPPEshNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPG 212

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 940372728 269 GPKGDQGDMGPKGEkGDPGGPAGPQGPKGERGEAGPQGPMGARGERGETGPRGEPG 324
Cdd:PHA03169 213 EPQSPTPQQAPSPN-TQQAVEHEDEPTEPEREGPPFPGHRSHSYTVVGWKPSTRPG 267
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 174-391 3.79e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.90  E-value: 3.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 174 RAEAATVSAEEARRMAENARGPRGPQGETGPKGDVGPKGETGPVGPQGPAGPKGERGDVGAQGAVGPAGPRGEKGEQGER 253
Cdd:PRK07764 585 EAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASD 664

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 254 GPQGIPGLKGD---TGERGPKGDQGDMGPKGEKGDPGGPAGPQGPKGERGEAGPQGPMGARGERGETGPRGEPGPAGPRG 330
Cdd:PRK07764 665 GGDGWPAKAGGaapAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPE 744

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 940372728 331 ERGETGPQGPRGEPGPAGSAANVADATTAQKGIVQLSSATDSDDEAKAATPKAVKAAMDVA 391
Cdd:PRK07764 745 PDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAEEVA 805
PTZ00121 PTZ00121
MAEBL; Provisional
 105-193 4.06e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 4.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728  105 ATSRAAEAGQKAtdatEAATRAVTAAGNAEESSTRAGESEKAAGAD--AEKARQHAEKARLAQESA--GEILKRAEAATV 180
Cdd:PTZ00121 1376 AKKKADAAKKKA----EEKKKADEAKKKAEEDKKKADELKKAAAAKkkADEAKKKAEEKKKADEAKkkAEEAKKADEAKK 1451

                          90
                  ....*....|...
gi 940372728  181 SAEEARRmAENAR 193
Cdd:PTZ00121 1452 KAEEAKK-AEEAK 1463
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
322-494 6.67e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 46.38  E-value: 6.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 322 EPGPAGPRGERGETGPQGPRGEPGPAGSAANVADATTAQKgivqlsSATDSDDEAKAATPKAVKAAMDVANEAKTKaeea 401
Cdd:PRK07003 359 EPAVTGGGAPGGGVPARVAGAVPAPGARAAAAVGASAVPA------VTAVTGAAGAALAPKAAAAAAATRAEAPPA---- 428

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 402 aagGGVPGPKGDKGDSGPAGPAG-PRGVQGPKGDPGPQGPKGDTGAAGAKGEKGATGATGPQGPKGDTGAAGPAGPQGPK 480
Cdd:PRK07003 429 ---APAPPATADRGDDAADGDAPvPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPA 505

                        170
                 ....*....|....
gi 940372728 481 GDTGAAGPAGPQGP 494
Cdd:PRK07003 506 AVPDARAPAAASRE 519
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 192-238 8.39e-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: 40.55  E-value: 8.39e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 940372728  192 ARGPRGPQGETGPKGDVGPKGETGPVGPQGPAGPKGERGDVGAQGAV 238
Cdd:pfam01391  11 PPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 233-282 1.22e-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: 40.17  E-value: 1.22e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 940372728  233 GAQGAVGPAGPRGEKGEQGERGPQGIPGLKGDTGERGPKGDQGDMGPKGE 282
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 236-283 1.43e-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: 40.17  E-value: 1.43e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 940372728  236 GAVGPAGPRGEKGEQGERGPQGIPGLKGDTGERGPKGDQGDMGPKGEK 283
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPP 48
PHA03169 PHA03169
hypothetical protein; Provisional
 409-563 1.62e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 44.58  E-value: 1.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 409 GPKGDKGDSGPAGpAGPRGVQGPKGDPGPQGPKGDTGaagakGEKGATGATGPQGPKGDTGAAGPAGPQGP--KGDTGAA 486
Cdd:PHA03169  82 GEKEERGQGGPSG-SGSESVGSPTPSPSGSAEELASG-----LSPENTSGSSPESPASHSPPPSPPSHPGPhePAPPESH 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 487 GPAGPQGPkgDTGAAGPAGAQGPKGDKGDPGVAGPAGPAGAPGPKGDKGDPGVAG-----PAGPEGPQGPKGDTGAPGQG 561
Cdd:PHA03169 156 NPSPNQQP--SSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPdepgePQSPTPQQAPSPNTQQAVEH 233


                 ..
gi 940372728 562 TE 563
Cdd:PHA03169 234 ED 235
PTZ00121 PTZ00121
MAEBL; Provisional
 27-193 2.04e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728   27 EGTESTVTLNMLLRRSLVEVSIPGELLTDF-RQIQNNVADDLANIRRLNEDTATKN---TQATQSKESAAASAKSASDSA 102
Cdd:PTZ00121 1031 ELTEYGNNDDVLKEKDIIDEDIDGNHEGKAeAKAHVGQDEGLKPSYKDFDFDAKEDnraDEATEEAFGKAEEAKKTETGK 1110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728  103 KTATSRAAEAGQKATDAteaatRAVTAAGNAEESStRAGESEKAAGADAEKARQHAEKARLAQES-AGEILKRAEAATvS 181
Cdd:PTZ00121 1111 AEEARKAEEAKKKAEDA-----RKAEEARKAEDAR-KAEEARKAEDAKRVEIARKAEDARKAEEArKAEDAKKAEAAR-K 1183

                         170
                  ....*....|....*..
gi 940372728  182 AEEAR-----RMAENAR 193
Cdd:PTZ00121 1184 AEEVRkaeelRKAEDAR 1200
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 110-334 2.57e-04

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


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 44.60  E-value: 2.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728   110 AEAGQKATDATEAATRAVTAAG-NAEESSTRA---GESEKAAGADAEKARQHAEKARlaQESAGEILKRAEAATVSAEEA 185
Cdd:TIGR00927  636 AEAEHTGERTGEEGERPTEAEGeNGEESGGEAeqeGETETKGENESEGEIPAERKGE--QEGEGEIEAKEADHKGETEAE 713

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728   186 RRMAENARGPRGP----QGETGPKGDVGPKGETGPVGPQGPAGPKGERGDVGAQGAVGPAGPRGEkgEQGERGPQGIPGL 261
Cdd:TIGR00927  714 EVEHEGETEAEGTedegEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDE--DEGEIQAGEDGEM 791

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940372728   262 KGDTGERGPKGDQGDMGPKGEKGDPGGPAGPQGPKGERGEAGPQ---GPMGARGERGETGPRGEPGPAGPRGERGE 334
Cdd:TIGR00927  792 KGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQelnAENQGEAKQDEKGVDGGGGSDGGDSEEEE 867
PTZ00121 PTZ00121
MAEBL; Provisional
 105-193 2.59e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 2.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728  105 ATSRAAEAGQKATD----ATEAATRAVTAAGNAEESSTRAGESEKAAGAD----------AEKARQHAEKARLAQES--- 167
Cdd:PTZ00121 1320 AKKKAEEAKKKADAakkkAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAekkkeeakkkADAAKKKAEEKKKADEAkkk 1399

                          90       100       110
                  ....*....|....*....|....*....|..
gi 940372728  168 ------AGEILKRAEAATVSAEEARRMAENAR 193
Cdd:PTZ00121 1400 aeedkkKADELKKAAAAKKKADEAKKKAEEKK 1431
PHA03169 PHA03169
hypothetical protein; Provisional
 331-493 3.39e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 43.42  E-value: 3.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 331 ERGETGPQGPRGEPGPAGSAANVADATTAQKGivqlssaTDSDDEAKAATPKAVKAAMDVANEAKTKAEEAAAGGGvPGP 410
Cdd:PHA03169  77 EESRHGEKEERGQGGPSGSGSESVGSPTPSPS-------GSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPG-PHE 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 411 KGDKGDSGPAGPAGPRGVQGPKGDPGPQGPKGDTGAAGAKGEKGATGATGPQGPKGDTGAAGPAGPQGPKGDtGAAGPAG 490
Cdd:PHA03169 149 PAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQ-QAPSPNT 227


                 ...
gi 940372728 491 PQG 493
Cdd:PHA03169 228 QQA 230
PTZ00121 PTZ00121
MAEBL; Provisional
 107-193 3.42e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 3.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728  107 SRAAEAGQKATDAteaatRAVTAAGNAEESStRAGESEKAAGA-DAEKARQHAEKARLAQESAGEILKRAEAATvSAEEA 185
Cdd:PTZ00121 1163 ARKAEEARKAEDA-----KKAEAARKAEEVR-KAEELRKAEDArKAEAARKAEEERKAEEARKAEDAKKAEAVK-KAEEA 1235


                  ....*...
gi 940372728  186 RRMAENAR 193
Cdd:PTZ00121 1236 KKDAEEAK 1243
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 300-494 4.40e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 4.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 300 GEAGPQGPMGARGERGETGPRGEPGPAGPRGERGETGPQGPRGEPGPAgsaanVADATTAQKGIVQLSSATDSDDEAKAA 379
Cdd:PRK07764 599 GPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPG-----VAAPEHHPKHVAVPDASDGGDGWPAKA 673

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 380 TPKAVKAAMdvaneaktkaeEAAAGGGVPGPKGD-KGDSGPAGPAGPRGVQGPkgDPGPQGPKGDTGAAGAKGEkGATGA 458
Cdd:PRK07764 674 GGAAPAAPP-----------PAPAPAAPAAPAGAaPAQPAPAPAATPPAGQAD--DPAAQPPQAAQGASAPSPA-ADDPV 739

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 940372728 459 TGPQGPKGDTGAAGPAGPQGPKGDTGAAGPAGPQGP 494
Cdd:PRK07764 740 PLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPP 775
PTZ00121 PTZ00121
MAEBL; Provisional
 105-193 5.79e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 5.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728  105 ATSRAAEAGQKATDATEA--ATRAVTAAGNAEESSTRAGESEKAagadaEKARQHAEKARLAQESAgeilKRAEAATvSA 182
Cdd:PTZ00121 1416 AKKKADEAKKKAEEKKKAdeAKKKAEEAKKADEAKKKAEEAKKA-----EEAKKKAEEAKKADEAK----KKAEEAK-KA 1485

                          90
                  ....*....|.
gi 940372728  183 EEARRMAENAR 193
Cdd:PTZ00121 1486 DEAKKKAEEAK 1496
PTZ00121 PTZ00121
MAEBL; Provisional
 108-190 6.20e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 6.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728  108 RAAEAGQKATDA---TEAATRAVTAAGNAEESSTRAGESEKAAGA--DAEKARQhAEKARLAQEsageiLKRAEAATvSA 182
Cdd:PTZ00121 1464 KKAEEAKKADEAkkkAEEAKKADEAKKKAEEAKKKADEAKKAAEAkkKADEAKK-AEEAKKADE-----AKKAEEAK-KA 1536


                  ....*...
gi 940372728  183 EEARRMAE 190
Cdd:PTZ00121 1537 DEAKKAEE 1544
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 406-447 8.47e-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: 37.86  E-value: 8.47e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 940372728  406 GVPGPKGDKGDSGPAGPAGPRGVQGPKGDPGPQGPKGDTGAA 447
Cdd:pfam01391  16 GPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 304-494 8.49e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 42.75  E-value: 8.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 304 PQGPMGARGERGETGPRGEPGPAGPRGERGETGPQGPRGEPGPAGSAANVADATTAQkgivqlssatdsddeaKAATPKA 383
Cdd:PTZ00449 521 PKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKEHKPSKIPTLSK----------------KPEFPKD 584

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 384 vkaamdvaneaktkaeeaaagggvpgPKGDKGDSGPAGPAGPRGVQGPKGDPGPQGPKgdtGAAGAKGEKGATGATGPQG 463
Cdd:PTZ00449 585 --------------------------PKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPE---LLDIPKSPKRPESPKSPKR 635

                        170       180       190
                 ....*....|....*....|....*....|.
gi 940372728 464 PKGDTGAAGPAGPQGPKGDTGAAGPAGPQGP 494
Cdd:PTZ00449 636 PPPPQRPSSPERPEGPKIIKSPKPPKSPKPP 666
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 294-341 2.27e-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: 2.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 940372728  294 GPKGERGEAGPQGPMGARGERGETGPRGEPGPAGPRGERGETGPQGPR 341
Cdd:pfam01391  10 GPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
105-247 2.51e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 40.99  E-value: 2.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 105 ATSRAAEAGqKATDATEAATRAVTAAGNAEESSTRAGESEKAAGADAekARQHAEKARLAQESAGEILKRA---EAATVS 181
Cdd:PRK07003 375 RVAGAVPAP-GARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAA--TRAEAPPAAPAPPATADRGDDAadgDAPVPA 451

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940372728 182 AEEARRMAENARGPRGPQGETGPKGDVGPKGETGPVGPQGPAGPKGERGDVGAQGAVGPAGPRGEK 247
Cdd:PRK07003 452 KANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAAS 517
PHA03169 PHA03169
hypothetical protein; Provisional
 224-381 2.63e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 40.72  E-value: 2.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 224 GPKGERGDvGAQGAVGPAGPRGEKGEQGERGPQGIPGLKGD-TGERGPKGDQGDMGPKGEkgDPGGPAGPQGPKGERGEA 302
Cdd:PHA03169  82 GEKEERGQ-GGPSGSGSESVGSPTPSPSGSAEELASGLSPEnTSGSSPESPASHSPPPSP--PSHPGPHEPAPPESHNPS 158

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940372728 303 GPQGPMGARGERGETGPRGEPGPAGPRGERGETGPQGPRGEPGPAGSAANVADATTAQKGIVQLSSATDSDDEAKAATP 381
Cdd:PHA03169 159 PNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEP 237
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 118-375 4.46e-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: 40.36  E-value: 4.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728   118 DATEAATRAVTAAGNAEESSTRAGESEKAAGADAEKARQHAEKARlaQESAGEIlkraeaatvsaeEARRMAENArgprg 197
Cdd:TIGR00927  634 DVAEAEHTGERTGEEGERPTEAEGENGEESGGEAEQEGETETKGE--NESEGEI------------PAERKGEQE----- 694

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728   198 PQGETGPKGDvGPKGETGPVGPQGPAGPKGERGDVGAQGAVGPAGPRGEKGEQGERGPQGIPGLKGDTGERGPKGDQGDM 277
Cdd:TIGR00927  695 GEGEIEAKEA-DHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAE 773

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728   278 GPKGEKGDPGGPAGPQGPKGERGEAGPQGPMGARGERGETGPRGEPGP-AGPRGERGETGPQgprgepgpAGSAANVADA 356
Cdd:TIGR00927  774 GKEDEDEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETqADDTEVKDETGEQ--------ELNAENQGEA 845

                          250       260
                   ....*....|....*....|.
gi 940372728   357 TTAQKGI--VQLSSATDSDDE 375
Cdd:TIGR00927  846 KQDEKGVdgGGGSDGGDSEEE 866
PRK13735 PRK13735
conjugal transfer mating pair stabilization protein TraG; Provisional
 109-257 4.62e-03

conjugal transfer mating pair stabilization protein TraG; Provisional


Pssm-ID: 184287 [Multi-domain]  Cd Length: 942  Bit Score: 40.50  E-value: 4.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728 109 AAEAGQKATDATEAATRAVTAAGN--AEESSTRAGESEKAAGADAEKARQhAEKARLAQESAGEILkrAEAATVSAEEAR 186
Cdd:PRK13735 533 AREASNQAESALHGFSSSIASAWNqlSQFGSNRGSSDSVTGGADSTMSAQ-DSMMASRMRSAVESY--AKAHNISNEQAT 609

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 940372728 187 RMAENargpRGPQGETGPKGDVGPKGETGPVgPQGPAGPKGERGDVGAQGAVGPAGPRGEKGEQGERGPQG 257
Cdd:PRK13735 610 QELAS----RSTRGSAGGYGDAHAEWGVGPK-ILGKGGKLGLGVKGGGRAGIDWSDSDGHSASSSSRSSHD 675
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 303-561 7.02e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 39.77  E-value: 7.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728  303 GPQGPMGARGERGETGPRGEPGPAGPRGERGETGPQGPRGEPGPAGSAAN--VADATTAQKGIVQLSSATDSDDEAKAAT 380
Cdd:PHA03307   38 GSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTptWSLSTLAPASPAREGSPTPPGPSSPDPP 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728  381 PKAV-------KAAMDVANEAKTKAEEAAAGGGVPGPKGDKGDSGPAGPAGPRGVQGPKGDPGPQGPKGDTGAAGAKGEK 453
Cdd:PHA03307  118 PPTPppaspppSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPST 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728  454 GATGATGPQGPKGDTGAAGPAGPQGPKGDTGAAG-PAGPQGPKGDTGAAGPAGAQGPKGDKGDPGVAGPAGPAGAPGPKG 532
Cdd:PHA03307  198 PPAAASPRPPRRSSPISASASSPAPAPGRSAADDaGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNG 277

                         250       260
                  ....*....|....*....|....*....
gi 940372728  533 DKGDPGVAGPAGPEGPQGPKGDTGAPGQG 561
Cdd:PHA03307  278 PSSRPGPASSSSSPRERSPSPSPSSPGSG 306
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 469-558 7.55e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.16  E-value: 7.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940372728  469 GAAGPAGPQGPKGDTGAAGPAGPQGPKGDtgaagpagaqgpkgdkgdpgvagpagpagapgpKGDKGDPGVAGPAGPEGP 548
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGP---------------------------------PGEPGPPGPPGPPGPPGP 47

                          90
                  ....*....|
gi 940372728  549 QGPKGDTGAP 558
Cdd:pfam01391  48 PGAPGAPGPP 57
PHA00430 PHA00430
tail fiber protein
 111-173 9.43e-03

tail fiber protein


Pssm-ID: 222790 [Multi-domain]  Cd Length: 568  Bit Score: 39.10  E-value: 9.43e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 940372728 111 EAGQKATDATEAATRAVTAAGNAEESSTRAGESEKAAGADAEKARQHAEKARLAQESAGEILK 173
Cdd:PHA00430 240 TAGDYATKAAASASAAHASEVNAANSATAAATSANRAKQQADRAKTEADKLGNMNGFAGAIEK 302
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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