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Conserved domains on  [gi|15832195|ref|NP_310968|]
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phage tail fiber protein [Escherichia coli O157:H7 str. Sakai]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_M14NE-CP-C_like super family cl21470
Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, ...
 1-141 8.68e-66

Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, regulation, or interaction domain; This domain is found C-terminal to the M14 carboxypeptidase (CP) N/E subfamily containing zinc-binding enzymes that hydrolyze single C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. The N/E subfamily includes enzymatically active members (carboxypeptidase N, E, M, D, and Z), as well as non-active members (carboxypeptidase-like protein 1, -2, aortic CP-like protein, and adipocyte enhancer binding protein-1) which lack the critical active site and substrate-binding residues considered necessary for activity. The active N/E enzymes fulfill a variety of cellular functions, including prohormone processing, regulation of peptide hormone activity, alteration of protein-protein or protein-cell interactions and transcriptional regulation. For M14 CPs, it has been suggested that this domain may assist in folding of the CP domain, regulate enzyme activity, or be involved in interactions with other proteins or with membranes; for carboxypeptidase M, it may interact with the bradykinin 1 receptor at the cell surface. This domain may also be found in other peptidase families.


The actual alignment was detected with superfamily member pfam08400:

Pssm-ID: 473874  Cd Length: 134  Bit Score: 206.74  E-value: 8.68e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195     1 MAVKISGVLKDGTGKPVENCTIQLKARRNSATVVVNTVASENPDEAGRYSMDVEYGQYSVILLVEGFPPSHAGTITVYED 80
Cdd:pfam08400   1 MSVVISGVLKDGTGIPVQNCTIQLKARRTSTTVVVNTVASENPDNAGRYSMDVETGQYGVYLKVDGRPPSHAGDITVYED 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15832195    81 SQPGTLNDFLGAMSEDDVRPEALRRFELMVeeaarhaEEAKKNAGEAETSARNAGISASQA 141
Cdd:pfam08400  81 SKPGTLNDFLIAMTEDDLRPEVLRRFEEMV-------EEVARSASAAAGNARQAAQDAGDA 134
Phage_fiber_C pfam06820
Putative prophage tail fibre C-terminus; This family represents the C-terminus of a prophage ...
 363-426 9.68e-32

Putative prophage tail fibre C-terminus; This family represents the C-terminus of a prophage tail fibre protein found mostly in E. coli. All family members contain a conserved RLGP motif.


:

Pssm-ID: 148432  Cd Length: 64  Bit Score: 115.40  E-value: 9.68e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15832195   363 IRFRLGPASIIETNSNGWFPDTDGALITGLTFLDPKDATQVQGLFRHLQVRFGDGPWQDVKGLD 426
Cdd:pfam06820   1 AQFRLGPADIIESDEHGIFPEQDGALITGLTFLADADKKQIQCFFQHLQILFADGPWEDIGGLD 64
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 250-370 2.23e-28

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: 116.16  E-value: 2.23e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  250 VGPPGPKGEQGPAGPQGPKGDKGERGDTGPVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAA- 328
Cdd:NF038329 125 AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAg 204

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 15832195  329 --GPAGPQGPKGETGAAGPVGATGP-----QGPKGDPGETQIRFRLGPA 370
Cdd:NF038329 205 eqGPAGPAGPDGEAGPAGEDGPAGPagdgqQGPDGDPGPTGEDGPQGPD 253
PRK12678 super family cl36163
transcription termination factor Rho; Provisional
 126-334 2.55e-06

transcription termination factor Rho; Provisional


The actual alignment was detected with superfamily member PRK12678:

Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 49.90  E-value: 2.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  126 EAETSARNAGISASQAEESAANADTSAGDALESARQAAESAAAAKQSEDASSSSASAAAQKASESSQSAAEAELSRKTAE 205
Cdd:PRK12678  53 AAIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRE 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  206 SAAGNAARDATTATEKARESAESAQSAEQSRIAAEEAVNRiptvvgppgpkGEQGPAGPQGPKGDKGERGDTGPVGATGE 285
Cdd:PRK12678 133 RGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDER-----------RRRGDREDRQAEAERGERGRREERGRDGD 201

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 15832195  286 RGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGPAGPQ 334
Cdd:PRK12678 202 DRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDR 250
 
Name Accession Description Interval E-value
phage_tail_N pfam08400
Prophage tail fibre N-terminal; This domain is found at the N-terminus of prophage tail fibre ...
 1-141 8.68e-66

Prophage tail fibre N-terminal; This domain is found at the N-terminus of prophage tail fibre proteins.


Pssm-ID: 285585  Cd Length: 134  Bit Score: 206.74  E-value: 8.68e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195     1 MAVKISGVLKDGTGKPVENCTIQLKARRNSATVVVNTVASENPDEAGRYSMDVEYGQYSVILLVEGFPPSHAGTITVYED 80
Cdd:pfam08400   1 MSVVISGVLKDGTGIPVQNCTIQLKARRTSTTVVVNTVASENPDNAGRYSMDVETGQYGVYLKVDGRPPSHAGDITVYED 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15832195    81 SQPGTLNDFLGAMSEDDVRPEALRRFELMVeeaarhaEEAKKNAGEAETSARNAGISASQA 141
Cdd:pfam08400  81 SKPGTLNDFLIAMTEDDLRPEVLRRFEEMV-------EEVARSASAAAGNARQAAQDAGDA 134
Phage_fiber_C pfam06820
Putative prophage tail fibre C-terminus; This family represents the C-terminus of a prophage ...
 363-426 9.68e-32

Putative prophage tail fibre C-terminus; This family represents the C-terminus of a prophage tail fibre protein found mostly in E. coli. All family members contain a conserved RLGP motif.


Pssm-ID: 148432  Cd Length: 64  Bit Score: 115.40  E-value: 9.68e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15832195   363 IRFRLGPASIIETNSNGWFPDTDGALITGLTFLDPKDATQVQGLFRHLQVRFGDGPWQDVKGLD 426
Cdd:pfam06820   1 AQFRLGPADIIESDEHGIFPEQDGALITGLTFLADADKKQIQCFFQHLQILFADGPWEDIGGLD 64
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 250-370 2.23e-28

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: 116.16  E-value: 2.23e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  250 VGPPGPKGEQGPAGPQGPKGDKGERGDTGPVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAA- 328
Cdd:NF038329 125 AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAg 204

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 15832195  329 --GPAGPQGPKGETGAAGPVGATGP-----QGPKGDPGETQIRFRLGPA 370
Cdd:NF038329 205 eqGPAGPAGPDGEAGPAGEDGPAGPagdgqQGPDGDPGPTGEDGPQGPD 253
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 254-379 1.94e-27

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: 113.46  E-value: 1.94e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  254 GPKGEQGPAGPQGPKGDKGERGDTGPvgaTGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGPAGP 333
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGE---TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 15832195  334 QGPKGETGAAGPVGATGPQGPKGDPGETQIRFRLGPASIIETNSNG 379
Cdd:NF038329 194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDG 239
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 251-386 1.09e-26

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: 111.54  E-value: 1.09e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  251 GPPGPKGEQGPAGPQGPKGDKGERGDTGPVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGP--------QGPK 322
Cdd:NF038329 159 GEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPagpagdgqQGPD 238

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15832195  323 GDTGAAGPAGPQGPKGETGAAGPVGATGPQGPKGDPGETQIRFRLGPASIIETNSNGWFPDTDG 386
Cdd:NF038329 239 GDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG 302
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 251-360 2.19e-19

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: 89.96  E-value: 2.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  251 GPPGPKGEQGPAGPQGPKGDKGERGDTGP--------------VGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNA 316
Cdd:NF038329 192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPagedgpagpagdgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD 271

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 15832195  317 GPQGPKGDTGAAGPAGPQGPKGETGAAGPVGATGPQGPKGDPGE 360
Cdd:NF038329 272 GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGK 315
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 250-359 7.39e-19

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: 88.42  E-value: 7.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  250 VGPPGPKGEQGPAGPQGPKGD--KGERGDTGPVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGP------ 321
Cdd:NF038329 209 AGPAGPDGEAGPAGEDGPAGPagDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPvgpagk 288

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 15832195  322 ---KGDTGAAGPAGPQGPKGETGAAGPVGATGPQGPKGDPG 359
Cdd:NF038329 289 dgqNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 251-354 2.42e-16

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 80.72  E-value: 2.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  251 GPPGPKGEQGPAGPQGPKGDKGERGDTGPVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGP 330
Cdd:NF038329 242 GPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ 321

                         90       100
                 ....*....|....*....|....
gi 15832195  331 AGPQGPKGETGAAGPVGATGPQGP 354
Cdd:NF038329 322 PGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 251-355 7.06e-16

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 79.18  E-value: 7.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  251 GPPGPKGEQGPAGPQGPKGDKGERGDTGPVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGP 330
Cdd:NF038329 239 GDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGK 318

                         90       100
                 ....*....|....*....|....*
gi 15832195  331 AGPQGPKGETGAAGPVGATGPQGPK 355
Cdd:NF038329 319 DGQPGKDGLPGKDGKDGQPGKPAPK 343
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 251-307 6.78e-11

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: 57.50  E-value: 6.78e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15832195   251 GPPGPKGEQGPAGPQGPKGDKGERGDTGPVGATGERGPAGDAGPAGPQGPKGDRGER 307
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
251-356 1.41e-08

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 56.58  E-value: 1.41e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195 251 GPPGPKGEQGPAGPQGPKGDKGERGDTGPVGATGERGPAGDAGPAGP------QGPKGDRGERGETGLTGNAGPQGPKGD 324
Cdd:COG5164  28 KPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPaqnqggTTPAQNQGGTRPAGNTGGTTPAGDGGA 107

                        90       100       110
                ....*....|....*....|....*....|....
gi 15832195 325 TGAAGPAGPQGPKGETGAAGPV--GATGPQGPKG 356
Cdd:COG5164 108 TGPPDDGGATGPPDDGGSTTPPsgGSTTPPGDGG 141
PHA03169 PHA03169
hypothetical protein; Provisional
 192-361 2.40e-06

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 49.58  E-value: 2.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  192 QSAAEAELSRKTAESAAGNAARDATTATEKARESAESAQSAEQ--SRIAAEEAVNRIPTVVGPPGPKGEQGPAGPQGPKG 269
Cdd:PHA03169  57 QVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGSESvgSPTPSPSGSAEELASGLSPENTSGSSPESPASHSP 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  270 DKGERGDTGPvgatGERGPAGDAGPAGPQGPKGDRGERGETgltgnaGPQGPKGDTGAAGPAGPQGPKGETGAAGPVGAT 349
Cdd:PHA03169 137 PPSPPSHPGP----HEPAPPESHNPSPNQQPSSFLQPSHED------SPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQS 206

                        170
                 ....*....|..
gi 15832195  350 GPQGPKGDPGET 361
Cdd:PHA03169 207 PPDEPGEPQSPT 218
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 126-334 2.55e-06

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 49.90  E-value: 2.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  126 EAETSARNAGISASQAEESAANADTSAGDALESARQAAESAAAAKQSEDASSSSASAAAQKASESSQSAAEAELSRKTAE 205
Cdd:PRK12678  53 AAIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRE 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  206 SAAGNAARDATTATEKARESAESAQSAEQSRIAAEEAVNRiptvvgppgpkGEQGPAGPQGPKGDKGERGDTGPVGATGE 285
Cdd:PRK12678 133 RGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDER-----------RRRGDREDRQAEAERGERGRREERGRDGD 201

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 15832195  286 RGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGPAGPQ 334
Cdd:PRK12678 202 DRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDR 250
 
Name Accession Description Interval E-value
phage_tail_N pfam08400
Prophage tail fibre N-terminal; This domain is found at the N-terminus of prophage tail fibre ...
 1-141 8.68e-66

Prophage tail fibre N-terminal; This domain is found at the N-terminus of prophage tail fibre proteins.


Pssm-ID: 285585  Cd Length: 134  Bit Score: 206.74  E-value: 8.68e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195     1 MAVKISGVLKDGTGKPVENCTIQLKARRNSATVVVNTVASENPDEAGRYSMDVEYGQYSVILLVEGFPPSHAGTITVYED 80
Cdd:pfam08400   1 MSVVISGVLKDGTGIPVQNCTIQLKARRTSTTVVVNTVASENPDNAGRYSMDVETGQYGVYLKVDGRPPSHAGDITVYED 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15832195    81 SQPGTLNDFLGAMSEDDVRPEALRRFELMVeeaarhaEEAKKNAGEAETSARNAGISASQA 141
Cdd:pfam08400  81 SKPGTLNDFLIAMTEDDLRPEVLRRFEEMV-------EEVARSASAAAGNARQAAQDAGDA 134
Phage_fiber_C pfam06820
Putative prophage tail fibre C-terminus; This family represents the C-terminus of a prophage ...
 363-426 9.68e-32

Putative prophage tail fibre C-terminus; This family represents the C-terminus of a prophage tail fibre protein found mostly in E. coli. All family members contain a conserved RLGP motif.


Pssm-ID: 148432  Cd Length: 64  Bit Score: 115.40  E-value: 9.68e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15832195   363 IRFRLGPASIIETNSNGWFPDTDGALITGLTFLDPKDATQVQGLFRHLQVRFGDGPWQDVKGLD 426
Cdd:pfam06820   1 AQFRLGPADIIESDEHGIFPEQDGALITGLTFLADADKKQIQCFFQHLQILFADGPWEDIGGLD 64
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 250-370 2.23e-28

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: 116.16  E-value: 2.23e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  250 VGPPGPKGEQGPAGPQGPKGDKGERGDTGPVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAA- 328
Cdd:NF038329 125 AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAg 204

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 15832195  329 --GPAGPQGPKGETGAAGPVGATGP-----QGPKGDPGETQIRFRLGPA 370
Cdd:NF038329 205 eqGPAGPAGPDGEAGPAGEDGPAGPagdgqQGPDGDPGPTGEDGPQGPD 253
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 254-379 1.94e-27

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: 113.46  E-value: 1.94e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  254 GPKGEQGPAGPQGPKGDKGERGDTGPvgaTGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGPAGP 333
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGE---TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP 193

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 15832195  334 QGPKGETGAAGPVGATGPQGPKGDPGETQIRFRLGPASIIETNSNG 379
Cdd:NF038329 194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDG 239
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 251-386 1.09e-26

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: 111.54  E-value: 1.09e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  251 GPPGPKGEQGPAGPQGPKGDKGERGDTGPVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGP--------QGPK 322
Cdd:NF038329 159 GEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPagpagdgqQGPD 238

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15832195  323 GDTGAAGPAGPQGPKGETGAAGPVGATGPQGPKGDPGETQIRFRLGPASIIETNSNGWFPDTDG 386
Cdd:NF038329 239 GDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG 302
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 251-360 2.19e-19

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: 89.96  E-value: 2.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  251 GPPGPKGEQGPAGPQGPKGDKGERGDTGP--------------VGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNA 316
Cdd:NF038329 192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPagedgpagpagdgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD 271

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 15832195  317 GPQGPKGDTGAAGPAGPQGPKGETGAAGPVGATGPQGPKGDPGE 360
Cdd:NF038329 272 GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGK 315
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 250-359 7.39e-19

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: 88.42  E-value: 7.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  250 VGPPGPKGEQGPAGPQGPKGD--KGERGDTGPVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGP------ 321
Cdd:NF038329 209 AGPAGPDGEAGPAGEDGPAGPagDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPvgpagk 288

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 15832195  322 ---KGDTGAAGPAGPQGPKGETGAAGPVGATGPQGPKGDPG 359
Cdd:NF038329 289 dgqNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 251-354 2.42e-16

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 80.72  E-value: 2.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  251 GPPGPKGEQGPAGPQGPKGDKGERGDTGPVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGP 330
Cdd:NF038329 242 GPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ 321

                         90       100
                 ....*....|....*....|....
gi 15832195  331 AGPQGPKGETGAAGPVGATGPQGP 354
Cdd:NF038329 322 PGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 251-355 7.06e-16

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 79.18  E-value: 7.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  251 GPPGPKGEQGPAGPQGPKGDKGERGDTGPVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGP 330
Cdd:NF038329 239 GDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGK 318

                         90       100
                 ....*....|....*....|....*
gi 15832195  331 AGPQGPKGETGAAGPVGATGPQGPK 355
Cdd:NF038329 319 DGQPGKDGLPGKDGKDGQPGKPAPK 343
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 251-307 6.78e-11

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: 57.50  E-value: 6.78e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15832195   251 GPPGPKGEQGPAGPQGPKGDKGERGDTGPVGATGERGPAGDAGPAGPQGPKGDRGER 307
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 290-346 8.25e-11

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: 57.12  E-value: 8.25e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15832195   290 GDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGPAGPQGPKGETGAAGPV 346
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 278-333 1.31e-09

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: 53.65  E-value: 1.31e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15832195   278 GPVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGPAGP 333
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 305-360 2.44e-09

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: 52.88  E-value: 2.44e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15832195   305 GERGETGLTGNAGPQGPKGDTGAAGPAGPQGPKGETGAAGPVGATGPQGPKGDPGE 360
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 257-311 3.90e-09

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: 52.50  E-value: 3.90e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15832195   257 GEQGPAGPQGPKGDKGERGDTGPVGATGERGPAGDAGPAGPQGPKGDRGERGETG 311
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
251-356 1.41e-08

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 56.58  E-value: 1.41e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195 251 GPPGPKGEQGPAGPQGPKGDKGERGDTGPVGATGERGPAGDAGPAGP------QGPKGDRGERGETGLTGNAGPQGPKGD 324
Cdd:COG5164  28 KPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPaqnqggTTPAQNQGGTRPAGNTGGTTPAGDGGA 107

                        90       100       110
                ....*....|....*....|....*....|....
gi 15832195 325 TGAAGPAGPQGPKGETGAAGPV--GATGPQGPKG 356
Cdd:COG5164 108 TGPPDDGGATGPPDDGGSTTPPsgGSTTPPGDGG 141
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
251-379 2.18e-08

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 56.19  E-value: 2.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195 251 GPPGPkGEQGPAGPQGPKGDKGERGDTGPVGATGERGPAGDAG---PAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGA 327
Cdd:COG5164   2 GLYGP-GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGgtrPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGG 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15832195 328 AGPAGPQG---PKGETGAAGPVGATGPQGPKGDPGETQIRFRLGPASIIETNSNG 379
Cdd:COG5164  81 TTPAQNQGgtrPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTT 135
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
251-359 2.99e-07

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 52.72  E-value: 2.99e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195 251 GPPGPKGEQGPAGPQGPKGDKGERGDTGPVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKG--DTGAA 328
Cdd:COG5164  55 TPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTppSGGST 134

                        90       100       110
                ....*....|....*....|....*....|..
gi 15832195 329 GPAGPQGPK-GETGAAGPVGATGPQGPKGDPG 359
Cdd:COG5164 135 TPPGDGGSTpPGPGSTGPGGSTTPPGDGGSTT 166
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 314-361 1.10e-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: 1.10e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 15832195   314 GNAGPQGPKGDTGAAGPAGPQGPKGETGAAGPVGATGPQGPKGDPGET 361
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPP 48
PHA03169 PHA03169
hypothetical protein; Provisional
 192-361 2.40e-06

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 49.58  E-value: 2.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  192 QSAAEAELSRKTAESAAGNAARDATTATEKARESAESAQSAEQ--SRIAAEEAVNRIPTVVGPPGPKGEQGPAGPQGPKG 269
Cdd:PHA03169  57 QVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGSESvgSPTPSPSGSAEELASGLSPENTSGSSPESPASHSP 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  270 DKGERGDTGPvgatGERGPAGDAGPAGPQGPKGDRGERGETgltgnaGPQGPKGDTGAAGPAGPQGPKGETGAAGPVGAT 349
Cdd:PHA03169 137 PPSPPSHPGP----HEPAPPESHNPSPNQQPSSFLQPSHED------SPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQS 206

                        170
                 ....*....|..
gi 15832195  350 GPQGPKGDPGET 361
Cdd:PHA03169 207 PPDEPGEPQSPT 218
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 126-334 2.55e-06

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 49.90  E-value: 2.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  126 EAETSARNAGISASQAEESAANADTSAGDALESARQAAESAAAAKQSEDASSSSASAAAQKASESSQSAAEAELSRKTAE 205
Cdd:PRK12678  53 AAIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRE 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  206 SAAGNAARDATTATEKARESAESAQSAEQSRIAAEEAVNRiptvvgppgpkGEQGPAGPQGPKGDKGERGDTGPVGATGE 285
Cdd:PRK12678 133 RGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDER-----------RRRGDREDRQAEAERGERGRREERGRDGD 201

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 15832195  286 RGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGPAGPQ 334
Cdd:PRK12678 202 DRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDR 250
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 201-360 5.53e-06

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 48.75  E-value: 5.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  201 RKTAESAAGNAARDATTATEKARESAESAQSAEQSRIAAEEAVNRIPTVVGPPGPKGEQGPAGPQGPKGDKGERGDTGpv 280
Cdd:PRK12678  47 RKGELIAAIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEA-- 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  281 GATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGPAGPQGPKGETGAAGPVGATGPQGPKGDPGE 360
Cdd:PRK12678 125 AQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRD 204
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 202-337 1.70e-05

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 47.38  E-value: 1.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  202 KTAESAAGNAARDATTATE-KARESAESAQSAEQSRIAAEEAVNRIPTVVG-PPGPKGEQGPAGPQGPKGDKGERGDTGP 279
Cdd:PTZ00449 527 KEGEEGEHEDSKESDEPKEgGKPGETKEGEVGKKPGPAKEHKPSKIPTLSKkPEFPKDPKHPKDPEEPKKPKRPRSAQRP 606

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15832195  280 VGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGPAGPQGPK 337
Cdd:PTZ00449 607 TRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPSSPERPEGPKIIKSPKPPKSPK 664
CarboxypepD_reg pfam13620
Carboxypeptidase regulatory-like domain;
5-87 5.30e-05

Carboxypeptidase regulatory-like domain;


Pssm-ID: 433354 [Multi-domain]  Cd Length: 81  Bit Score: 41.50  E-value: 5.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195     5 ISGVLKDGTGKPVENCTIQLKARRNSATVVVNTvasenpDEAGRYSM-DVEYGQYSVILLVEGFPPSHAGTITVyEDSQP 83
Cdd:pfam13620   2 ISGTVTDPSGAPVPGATVTVTNTDTGTVRTTTT------DADGRYRFpGLPPGTYTVTVSAPGFKTATRTGVTV-TAGQT 74


                  ....
gi 15832195    84 GTLN 87
Cdd:pfam13620  75 TTLD 78
PHA03169 PHA03169
hypothetical protein; Provisional
 122-345 1.73e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 43.81  E-value: 1.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  122 KNAGEAETSARNAGISASQAEESAANADTSAGDALESARQAAESAAAAKQSEDASSSSASAAAQKASESSQSAAEAELSR 201
Cdd:PHA03169  24 KRHGGTREQAGRRRGTAARAAKPAPPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGSP 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  202 KTAESAAGNAARDATTATEKARESAESAQSAEQsriAAEEAVNRIPtvvGPPGPKGEQGPAGPQGPKGDKGERGDTGPVG 281
Cdd:PHA03169 104 TPSPSGSAEELASGLSPENTSGSSPESPASHSP---PPSPPSHPGP---HEPAPPESHNPSPNQQPSSFLQPSHEDSPEE 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15832195  282 ATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDtGAAGPAGPQGPKGETGAAGP 345
Cdd:PHA03169 178 PEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQ-QAPSPNTQQAVEHEDEPTEP 240
PHA03247 PHA03247
large tegument protein UL36; Provisional
 194-354 2.43e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 2.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195   194 AAEAELSRKTAESAAGNAARDATTATEKARESAESAQSAEQSRIAAEEAVNRIPTVVGPPGPKGEQGPAGPQGPKGDKGE 273
Cdd:PHA03247 2643 PPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLP 2722

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195   274 RGdtgpVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGPAGPQGPKGETGAAGPVGATGPQG 353
Cdd:PHA03247 2723 PG----PAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESL 2798


                  .
gi 15832195   354 P 354
Cdd:PHA03247 2799 P 2799
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 216-355 3.31e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 43.14  E-value: 3.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  216 TTATEKARESAESAQSAEQSRIAAEeavNRIPTVVGPPGPKGEQGPAG-------PQGPKGDKGERGDTGPVGATGERGP 288
Cdd:PTZ00449 527 KEGEEGEHEDSKESDEPKEGGKPGE---TKEGEVGKKPGPAKEHKPSKiptlskkPEFPKDPKHPKDPEEPKKPKRPRSA 603

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15832195  289 AGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGPAGPQGPKGETGAAGPVGATGPQGPK 355
Cdd:PTZ00449 604 QRPTRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPSSPERPEGPKIIKSPKPPKSPKPPFDPK 670
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 215-362 6.10e-04

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 40.41  E-value: 6.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195   215 ATTATEKARESAESAQSAEQSRIAAEEAVNRIPTVVGPPGPkgEQGPAGPQGPKGDKGErgdtGPVGATGERGPAGDAGP 294
Cdd:pfam15240   9 ALLALSSAQSSSEDVSQEDSPSLISEEEGQSQQGGQGPQGP--PPGGFPPQPPASDDPP----GPPPPGGPQQPPPQGGK 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15832195   295 AGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGPAGPQGPKGETGAAGPVGATGPQGPKGDPGETQ 362
Cdd:pfam15240  83 QKPQGPPPQGGPRPPPGKPQGPPPQGGNQQQGPPPPGKPQGPPPQGGGPPPQGGNQQGPPPPPPGNPQ 150
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 251-353 6.72e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 6.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  251 GPPGPKGEQGPAGPQGPKGDKGERGDTGPVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGP 330
Cdd:PRK07764 599 GPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAP 678

                         90       100
                 ....*....|....*....|...
gi 15832195  331 AGPQGPKGETGAAGPVGATGPQG 353
Cdd:PRK07764 679 AAPPPAPAPAAPAAPAGAAPAQP 701
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 235-362 8.85e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 8.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  235 SRIAAEEAVNRIPTVVGPPG----PKGEQGPAGPQGPKGDKGERGDTGPVGATGERGPAGDAGPAGPQGPKGDRGERGET 310
Cdd:PRK07764 591 APGAAGGEGPPAPASSGPPEeaarPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWP 670

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15832195  311 GLTGNAGPQGPKGDTGAAGPAGPQGPKGETGAAGPVGATGPQGPKGDPGETQ 362
Cdd:PRK07764 671 AKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPP 722
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 247-286 2.09e-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: 36.32  E-value: 2.09e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 15832195   247 PTVVGPPGPKGEQGPAGPQGPKGDKGERGDTGPVGATGER 286
Cdd:pfam01391  18 PGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 194-359 2.10e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.54  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195   194 AAEAELSRKTAESAAGNAARDATTATEKARESAESAQSAEQSRIAAEEAVNRIPTVVGPPGPKGEQGPAGPQGPKGDkge 273
Cdd:PHA03307  768 LAEALALLEPAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAADAASRTASKRKSRSHTPDGGSESSGPARPPGAAAR--- 844

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195   274 rgdTGPVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTgAAGPAGPQGPKGETGAAGPVGATGPQG 353
Cdd:PHA03307  845 ---PPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRARPGAAAPPKAAA-AAPPAGAPAPRPRPAPRVKLGPMPPGG 920


                  ....*.
gi 15832195   354 PKGDPG 359
Cdd:PHA03307  921 PDPRGG 926
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 203-362 2.86e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.97  E-value: 2.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  203 TAESAAGNAARDATTATEKARESAESAQSAEQsriaaeeavnriptvVGPPGPKGEQGPAGPQGPKgdkgerGDTGPVGA 282
Cdd:PRK07764 590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAP---------------AAPAAPAPAGAAAAPAEAS------AAPAPGVA 648

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832195  283 TGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGPAGPQGPKGETGAAGPVGATGPQGPKGDPGETQ 362
Cdd:PRK07764 649 APEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGA 728
 
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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