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Conserved domains on  [gi|1744921521|dbj|BBK57462|]
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phage tail fiber protein [Escherichia coli O145:H28]

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, ...
 1-134 4.05e-69

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: 215.60  E-value: 4.05e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521   1 MAVKISGVLKDGTGKPIQNCTIQLKARRNSTTVVVNTVASENPDEAGRYSTDVEYGQYSVILLVEGFPPSHAGTITVYED 80
Cdd:pfam08400   1 MSVVISGVLKDGTGIPVQNCTIQLKARRTSTTVVVNTVASENPDNAGRYSMDVETGQYGVYLKVDGRPPSHAGDITVYED 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1744921521  81 SQPGTLNDFLGAMSEDDVRPEALRRFELMVEEVARHAEEAKKNAGEAETSARNA 134
Cdd:pfam08400  81 SKPGTLNDFLIAMTEDDLRPEVLRRFEEMVEEVARSASAAAGNARQAAQDAGDA 134
Phage_fiber_C pfam06820
Putative prophage tail fibre C-terminus; This family represents the C-terminus of a prophage ...
 363-426 3.19e-33

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: 119.26  E-value: 3.19e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1744921521 363 IRFRLGPASIIETNSHGWFPDTDGALITGLTFLDPKDATRVQGFFQHLQVRFGDGPWQDVKGLD 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 ...
 265-379 1.44e-24

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: 105.37  E-value: 1.44e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 265 QGPKGDKGERGDTGPVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGPAGPQGPKGETGAAG 344
Cdd:NF038329  125 AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAG 204

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1744921521 345 PVGATGPQGPKGDPGETQIRFRLGPASIIETNSHG 379
Cdd:NF038329  205 EQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDG 239
tolA super family cl35847
cell envelope integrity inner membrane protein TolA; Provisional
 111-242 1.22e-07

cell envelope integrity inner membrane protein TolA; Provisional


The actual alignment was detected with superfamily member PRK09510:

Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 53.66  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 111 EEVARHAEEAKKNAGEAetSARNAGISASQAEESAANADTSAGEASESARQAAESAASAKQSEDASSSSASAAAQKASES 190
Cdd:PRK09510  121 EEAAKQAALKQKQAEEA--AAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAE 198

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1744921521 191 SQSAAEAELSRKTAESAAGNAARDATTATEKARESAESAQSAEQSRIAAEEA 242
Cdd:PRK09510  199 AKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKA 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 ...
 1-134 4.05e-69

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: 215.60  E-value: 4.05e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521   1 MAVKISGVLKDGTGKPIQNCTIQLKARRNSTTVVVNTVASENPDEAGRYSTDVEYGQYSVILLVEGFPPSHAGTITVYED 80
Cdd:pfam08400   1 MSVVISGVLKDGTGIPVQNCTIQLKARRTSTTVVVNTVASENPDNAGRYSMDVETGQYGVYLKVDGRPPSHAGDITVYED 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1744921521  81 SQPGTLNDFLGAMSEDDVRPEALRRFELMVEEVARHAEEAKKNAGEAETSARNA 134
Cdd:pfam08400  81 SKPGTLNDFLIAMTEDDLRPEVLRRFEEMVEEVARSASAAAGNARQAAQDAGDA 134
Phage_fiber_C pfam06820
Putative prophage tail fibre C-terminus; This family represents the C-terminus of a prophage ...
 363-426 3.19e-33

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: 119.26  E-value: 3.19e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1744921521 363 IRFRLGPASIIETNSHGWFPDTDGALITGLTFLDPKDATRVQGFFQHLQVRFGDGPWQDVKGLD 426
Cdd:pfam06820   1 AQFRLGPADIIESDEHGIFPEQDGALITGLTFLADADKKQIQCFFQHLQILFADGPWEDIGGLD 64
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 265-379 1.44e-24

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: 105.37  E-value: 1.44e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 265 QGPKGDKGERGDTGPVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGPAGPQGPKGETGAAG 344
Cdd:NF038329  125 AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAG 204

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1744921521 345 PVGATGPQGPKGDPGETQIRFRLGPASIIETNSHG 379
Cdd:NF038329  205 EQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDG 239
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 257-370 1.12e-21

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: 96.90  E-value: 1.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 257 GEPGPAGPQGPKGDKGERGDTGPVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAA---GPAGP 333
Cdd:NF038329  132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAgeqGPAGP 211

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1744921521 334 QGPKGETGAAGPVGATGP-----QGPKGDPGETQIRFRLGPA 370
Cdd:NF038329  212 AGPDGEAGPAGEDGPAGPagdgqQGPDGDPGPTGEDGPQGPD 253
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 265-386 5.37e-21

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: 94.59  E-value: 5.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 265 QGPKGDKGERGDTGPVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGP--------QGPKGDTGAAGPAGPQGP 336
Cdd:NF038329  173 QGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPagpagdgqQGPDGDPGPTGEDGPQGP 252

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1744921521 337 KGETGAAGPVGATGPQGPKGDPGETQIRFRLGPASIIETNSHGWFPDTDG 386
Cdd:NF038329  253 DGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG 302
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 265-360 9.51e-15

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: 75.71  E-value: 9.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 265 QGPKGDKGERGDtGPVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGPAGPQGPKGETGAAG 344
Cdd:NF038329  221 AGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPG 299

                          90
                  ....*....|....*.
gi 1744921521 345 PVGATGPQGPKGDPGE 360
Cdd:NF038329  300 KDGKDGQNGKDGLPGK 315
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 265-359 1.12e-14

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: 75.71  E-value: 1.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 265 QGPKGDkGERGDTGPVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGP---------KGDTGAAGPAGPQG 335
Cdd:NF038329  227 AGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPvgpagkdgqNGKDGLPGKDGKDG 305

                          90       100
                  ....*....|....*....|....
gi 1744921521 336 PKGETGAAGPVGATGPQGPKGDPG 359
Cdd:NF038329  306 QNGKDGLPGKDGKDGQPGKDGLPG 329
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 269-359 4.61e-13

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: 70.70  E-value: 4.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 269 GDKGERGDTGPVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGPAGPQGPKGETGAAGPVGA 348
Cdd:NF038329  248 GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327

                          90
                  ....*....|.
gi 1744921521 349 TGPQGPKGDPG 359
Cdd:NF038329  328 PGKDGKDGQPG 338
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 290-346 1.70e-12

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: 61.74  E-value: 1.70e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1744921521 290 GDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGPAGPQGPKGETGAAGPV 346
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 265-354 4.68e-11

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: 64.16  E-value: 4.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 265 QGPKGDKGERGDTGPVGATGERGPagdAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGPAGPQGPKGETGAAG 344
Cdd:NF038329  259 DGPRGDRGEAGPDGPDGKDGERGP---VGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335

                          90
                  ....*....|
gi 1744921521 345 PVGATGPQGP 354
Cdd:NF038329  336 QPGKPAPKTP 345
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 111-242 1.22e-07

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 53.66  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 111 EEVARHAEEAKKNAGEAetSARNAGISASQAEESAANADTSAGEASESARQAAESAASAKQSEDASSSSASAAAQKASES 190
Cdd:PRK09510  121 EEAAKQAALKQKQAEEA--AAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAE 198

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1744921521 191 SQSAAEAELSRKTAESAAGNAARDATTATEKARESAESAQSAEQSRIAAEEA 242
Cdd:PRK09510  199 AKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKA 250
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
266-379 4.43e-07

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 51.95  E-value: 4.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 266 GPKGDKGERGDTGPVGATGERGPAGDAG---PAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGPAGPQG---PKGE 339
Cdd:COG5164    16 GVTTPAGSQGSTKPAQNQGSTRPAGNTGgtrPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGgtrPAGN 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1744921521 340 TGAAGPVGATGPQGPKGDPGETQIRFRLGPASIIETNSHG 379
Cdd:COG5164    96 TGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTT 135
PHA03169 PHA03169
hypothetical protein; Provisional
 193-361 1.53e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 43.81  E-value: 1.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 193 SAAEAELSRKTAESAAGNAARDATTATEKARESAESAQSAEQSRIAAEEAVNRIPTVVGPPGPKGEPGPAGPQGPKGDKG 272
Cdd:PHA03169   51 PTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPES 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 273 ERGDTGPVGATGERGPAGDA-----GPAGPQGPKGDRGERGETgltgnaGPQGPKGDTGAAGPAGPQGPKGETGAAGPVG 347
Cdd:PHA03169  131 PASHSPPPSPPSHPGPHEPAppeshNPSPNQQPSSFLQPSHED------SPEEPEPPTSEPEPDSPGPPQSETPTSSPPP 204

                         170
                  ....*....|....
gi 1744921521 348 ATGPQGPKGDPGET 361
Cdd:PHA03169  205 QSPPDEPGEPQSPT 218
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 101-242 5.06e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 5.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 101 EALRRFELMVEEVARHAEEAKKNAGEAETSARNAGISASQAEESAANADTSAGEAsESARQAAESAASAKQSEDASSSSA 180
Cdd:COG1196   316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA-EAELAEAEEELEELAEELLEALRA 394

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1744921521 181 SAAAQKASESSQSAAEAELSRKTAESAAGNAARDATTATEKARESAESAQSAEQSRIAAEEA 242
Cdd:COG1196   395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 99-242 1.14e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 40.98  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521  99 RPEALRRFELMVEEVARHAEEAKKNAGEAETSARNAGISAsQAEESAANADTSAGEASESARQAAESAASAKqsedasss 178
Cdd:TIGR02794  59 KKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRA-AAEKAAKQAEQAAKQAEEKQKQAEEAKAKQA-------- 129

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1744921521 179 sasaaaqkasESSQSAAEAELSRKTAESAAGNAARDATT--ATEKARESAESAQSAEQSRIAAEEA 242
Cdd:TIGR02794 130 ----------AEAKAKAEAEAERKAKEEAAKQAEEEAKAkaAAEAKKKAEEAKKKAEAEAKAKAEA 185
Peptidase_M14NE-CP-C_like cd11308
Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, ...
 5-87 2.07e-03

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.


Pssm-ID: 200604 [Multi-domain]  Cd Length: 76  Bit Score: 36.73  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521   5 ISGVLKDGTGKPIQNCTIQLKARRNSTTvvvntvasenpdeagrYSTDVEY------GQYSVILLVEGFPPSHAgTITVY 78
Cdd:cd11308     2 IKGFVTDATGNPIANATISVEGINHDVT----------------TAKDGDYwrlllpGTYNVTASAPGYQPVTK-TVTVP 64


                  ....*....
gi 1744921521  79 EDSQPGTLN 87
Cdd:cd11308    65 NNFSATVVN 73
 
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 ...
 1-134 4.05e-69

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: 215.60  E-value: 4.05e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521   1 MAVKISGVLKDGTGKPIQNCTIQLKARRNSTTVVVNTVASENPDEAGRYSTDVEYGQYSVILLVEGFPPSHAGTITVYED 80
Cdd:pfam08400   1 MSVVISGVLKDGTGIPVQNCTIQLKARRTSTTVVVNTVASENPDNAGRYSMDVETGQYGVYLKVDGRPPSHAGDITVYED 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1744921521  81 SQPGTLNDFLGAMSEDDVRPEALRRFELMVEEVARHAEEAKKNAGEAETSARNA 134
Cdd:pfam08400  81 SKPGTLNDFLIAMTEDDLRPEVLRRFEEMVEEVARSASAAAGNARQAAQDAGDA 134
Phage_fiber_C pfam06820
Putative prophage tail fibre C-terminus; This family represents the C-terminus of a prophage ...
 363-426 3.19e-33

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: 119.26  E-value: 3.19e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1744921521 363 IRFRLGPASIIETNSHGWFPDTDGALITGLTFLDPKDATRVQGFFQHLQVRFGDGPWQDVKGLD 426
Cdd:pfam06820   1 AQFRLGPADIIESDEHGIFPEQDGALITGLTFLADADKKQIQCFFQHLQILFADGPWEDIGGLD 64
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 265-379 1.44e-24

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: 105.37  E-value: 1.44e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 265 QGPKGDKGERGDTGPVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGPAGPQGPKGETGAAG 344
Cdd:NF038329  125 AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAG 204

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1744921521 345 PVGATGPQGPKGDPGETQIRFRLGPASIIETNSHG 379
Cdd:NF038329  205 EQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDG 239
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 257-370 1.12e-21

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: 96.90  E-value: 1.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 257 GEPGPAGPQGPKGDKGERGDTGPVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAA---GPAGP 333
Cdd:NF038329  132 GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAgeqGPAGP 211

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1744921521 334 QGPKGETGAAGPVGATGP-----QGPKGDPGETQIRFRLGPA 370
Cdd:NF038329  212 AGPDGEAGPAGEDGPAGPagdgqQGPDGDPGPTGEDGPQGPD 253
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 265-386 5.37e-21

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: 94.59  E-value: 5.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 265 QGPKGDKGERGDTGPVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGP--------QGPKGDTGAAGPAGPQGP 336
Cdd:NF038329  173 QGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPagpagdgqQGPDGDPGPTGEDGPQGP 252

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1744921521 337 KGETGAAGPVGATGPQGPKGDPGETQIRFRLGPASIIETNSHGWFPDTDG 386
Cdd:NF038329  253 DGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG 302
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 265-360 9.51e-15

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: 75.71  E-value: 9.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 265 QGPKGDKGERGDtGPVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGPAGPQGPKGETGAAG 344
Cdd:NF038329  221 AGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPG 299

                          90
                  ....*....|....*.
gi 1744921521 345 PVGATGPQGPKGDPGE 360
Cdd:NF038329  300 KDGKDGQNGKDGLPGK 315
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 265-359 1.12e-14

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: 75.71  E-value: 1.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 265 QGPKGDkGERGDTGPVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGP---------KGDTGAAGPAGPQG 335
Cdd:NF038329  227 AGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPvgpagkdgqNGKDGLPGKDGKDG 305

                          90       100
                  ....*....|....*....|....
gi 1744921521 336 PKGETGAAGPVGATGPQGPKGDPG 359
Cdd:NF038329  306 QNGKDGLPGKDGKDGQPGKDGLPG 329
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 269-359 4.61e-13

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: 70.70  E-value: 4.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 269 GDKGERGDTGPVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGPAGPQGPKGETGAAGPVGA 348
Cdd:NF038329  248 GPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327

                          90
                  ....*....|.
gi 1744921521 349 TGPQGPKGDPG 359
Cdd:NF038329  328 PGKDGKDGQPG 338
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 290-346 1.70e-12

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: 61.74  E-value: 1.70e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1744921521 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 3.56e-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: 58.27  E-value: 3.56e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1744921521 278 GPVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGPAGP 333
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 265-354 4.68e-11

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: 64.16  E-value: 4.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 265 QGPKGDKGERGDTGPVGATGERGPagdAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGPAGPQGPKGETGAAG 344
Cdd:NF038329  259 DGPRGDRGEAGPDGPDGKDGERGP---VGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335

                          90
                  ....*....|
gi 1744921521 345 PVGATGPQGP 354
Cdd:NF038329  336 QPGKPAPKTP 345
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 305-360 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 1744921521 305 GERGETGLTGNAGPQGPKGDTGAAGPAGPQGPKGETGAAGPVGATGPQGPKGDPGE 360
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 266-316 2.73e-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: 49.80  E-value: 2.73e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1744921521 266 GPKGDKGERGDTGPVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNA 316
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 314-361 5.22e-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: 5.22e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1744921521 314 GNAGPQGPKGDTGAAGPAGPQGPKGETGAAGPVGATGPQGPKGDPGET 361
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPP 48
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 111-242 1.22e-07

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 53.66  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 111 EEVARHAEEAKKNAGEAetSARNAGISASQAEESAANADTSAGEASESARQAAESAASAKQSEDASSSSASAAAQKASES 190
Cdd:PRK09510  121 EEAAKQAALKQKQAEEA--AAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAE 198

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1744921521 191 SQSAAEAELSRKTAESAAGNAARDATTATEKARESAESAQSAEQSRIAAEEA 242
Cdd:PRK09510  199 AKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKA 250
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 126-334 2.21e-07

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 52.98  E-value: 2.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 126 EAETSARNAGISASQAEESAANADTSAGEASESARQAAESAASAKQSEDASSSSASAAAQKASESSQSAAEAELSRKTAE 205
Cdd:PRK12678   53 AAIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRE 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 206 SAAGNAARDATTATEKARESAESAQSAEQSRIAAEEAVNRiptvvgppgpkGEPGPAGPQGPKGDKGERGDTGPVGATGE 285
Cdd:PRK12678  133 RGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDER-----------RRRGDREDRQAEAERGERGRREERGRDGD 201

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1744921521 286 RGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGPAGPQ 334
Cdd:PRK12678  202 DRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDR 250
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
266-379 4.43e-07

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 51.95  E-value: 4.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 266 GPKGDKGERGDTGPVGATGERGPAGDAG---PAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGPAGPQG---PKGE 339
Cdd:COG5164    16 GVTTPAGSQGSTKPAQNQGSTRPAGNTGgtrPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGgtrPAGN 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1744921521 340 TGAAGPVGATGPQGPKGDPGETQIRFRLGPASIIETNSHG 379
Cdd:COG5164    96 TGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTT 135
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
264-354 6.52e-07

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 51.57  E-value: 6.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 264 PQGPKGDKGERGDTGPVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGPAGPQG---PKGET 340
Cdd:COG5164    35 STRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGatgPPDDG 114

                          90
                  ....*....|....
gi 1744921521 341 GAAGPVGATGPQGP 354
Cdd:COG5164   115 GATGPPDDGGSTTP 128
PTZ00121 PTZ00121
MAEBL; Provisional
 111-242 1.48e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 1.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521  111 EEVARHAEEAKKNAGEAETSARnagiSASQAEESAANADTSAGEASESARQAAESAASAKQSEDASSSSASAAAQKASES 190
Cdd:PTZ00121  1318 DEAKKKAEEAKKKADAAKKKAE----EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA 1393

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1744921521  191 SQSAAEAELSRKTAESAAGNAArdATTATEKARESAESAQSAEQSRIAAEEA 242
Cdd:PTZ00121  1394 DEAKKKAEEDKKKADELKKAAA--AKKKADEAKKKAEEKKKADEAKKKAEEA 1443
PTZ00121 PTZ00121
MAEBL; Provisional
 95-242 6.93e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 6.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521   95 EDDVRPEALRRFE--LMVEEVaRHAEEAKKNAGE---AETSARNAGISASQAEESAANADTSAGEASESARQAAE--SAA 167
Cdd:PTZ00121  1209 EEERKAEEARKAEdaKKAEAV-KKAEEAKKDAEEakkAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADElkKAE 1287

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1744921521  168 SAKQSEDASSSSASAAAQKASESSQSAAEAELSRKTAESAAGNAardattatEKARESAESAQSAEQSRIAAEEA 242
Cdd:PTZ00121  1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKA--------DAAKKKAEEAKKAAEAAKAEAEA 1354
PTZ00121 PTZ00121
MAEBL; Provisional
 107-242 1.30e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 1.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521  107 ELMVEEVARHAEEAKKNAGEAetsaRNAGISASQAEESAANAD--TSAGEASESARQAAESAASA-KQSEDASSSSASAA 183
Cdd:PTZ00121  1370 EKKKEEAKKKADAAKKKAEEK----KKADEAKKKAEEDKKKADelKKAAAAKKKADEAKKKAEEKkKADEAKKKAEEAKK 1445

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1744921521  184 AQKASESSQSAAEAELSRKTAESAagNAARDATTATEKARESAESAQSAEQSRIAAEEA 242
Cdd:PTZ00121  1446 ADEAKKKAEEAKKAEEAKKKAEEA--KKADEAKKKAEEAKKADEAKKKAEEAKKKADEA 1502
PHA00430 PHA00430
tail fiber protein
 112-231 1.37e-05

tail fiber protein


Pssm-ID: 222790 [Multi-domain]  Cd Length: 568  Bit Score: 47.19  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 112 EVARHAEEAKKNAGEAETSARNAGISASQAEESAANADTSAGEASESARQAAESAASAKQSEDASSSSASAAAQKASESS 191
Cdd:PHA00430  167 EANRSRNEADRARNQAERFNNESGASATNTKQWRSEADGSNSEANRFKGYADSMTSSVEAAKGQAESSSKEANTAGDYAT 246

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1744921521 192 QSAAEAELSRKTAESAAGNAARDATTATeKARESAESAQS 231
Cdd:PHA00430  247 KAAASASAAHASEVNAANSATAAATSAN-RAKQQADRAKT 285
PTZ00121 PTZ00121
MAEBL; Provisional
 94-240 1.47e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 1.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521   94 SEDDVRPEALRRFELMVE-EVARHAEEAKKnageAEtSARNAgISASQAEESAANADTSAGEAS---ESARQAAEsaasA 169
Cdd:PTZ00121  1148 AEDAKRVEIARKAEDARKaEEARKAEDAKK----AE-AARKA-EEVRKAEELRKAEDARKAEAArkaEEERKAEE----A 1217

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1744921521  170 KQSEDASSSSASAAAQKASESSQSAAEAELSRKTAESAAGNAARDATTATEKARESAESAQSAEQSRIAAE 240
Cdd:PTZ00121  1218 RKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE 1288
PTZ00121 PTZ00121
MAEBL; Provisional
 111-242 2.03e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 2.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521  111 EEVARHAEEAKKNAGEAETSARNAGISASQAEESAANADTSAGEASESArQAAESAASAKQSEDASSSSASAAAQKASES 190
Cdd:PTZ00121  1332 DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA-DAAKKKAEEKKKADEAKKKAEEDKKKADEL 1410

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1744921521  191 SQSAAE---AELSRKTAESA--AGNAARDATTA--TEKARESAESAQSAEQSRIAAEEA 242
Cdd:PTZ00121  1411 KKAAAAkkkADEAKKKAEEKkkADEAKKKAEEAkkADEAKKKAEEAKKAEEAKKKAEEA 1469
CarboxypepD_reg pfam13620
Carboxypeptidase regulatory-like domain;
5-87 2.37e-05

Carboxypeptidase regulatory-like domain;


Pssm-ID: 433354 [Multi-domain]  Cd Length: 81  Bit Score: 42.27  E-value: 2.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521   5 ISGVLKDGTGKPIQNCTIQLKARRNSTTVVVNTvasenpDEAGRYS-TDVEYGQYSVILLVEGFPPSHAGTITVyEDSQP 83
Cdd:pfam13620   2 ISGTVTDPSGAPVPGATVTVTNTDTGTVRTTTT------DADGRYRfPGLPPGTYTVTVSAPGFKTATRTGVTV-TAGQT 74


                  ....
gi 1744921521  84 GTLN 87
Cdd:pfam13620  75 TTLD 78
PTZ00121 PTZ00121
MAEBL; Provisional
 107-242 3.41e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 3.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521  107 ELMVEEVARHAEEAKKNAGEAetsaRNAGISASQAEESAANADtsagEASESARQAAESAASAKQSEDASSSSASAAAQK 186
Cdd:PTZ00121  1294 EAKKAEEKKKADEAKKKAEEA----KKADEAKKKAEEAKKKAD----AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK 1365

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1744921521  187 ASESSQSAAEAelsRKTAESAAGNA--ARDATTATEKARES---AESAQSAEQSRIAAEEA 242
Cdd:PTZ00121  1366 AEAAEKKKEEA---KKKADAAKKKAeeKKKADEAKKKAEEDkkkADELKKAAAAKKKADEA 1423
PHA00430 PHA00430
tail fiber protein
 92-233 8.54e-05

tail fiber protein


Pssm-ID: 222790 [Multi-domain]  Cd Length: 568  Bit Score: 44.88  E-value: 8.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521  92 AMSEDDVRPEALRRFELMVEEVARHAEEAKKNAGEAETSARNAGISASQAEESAANA----DTSAGEASEsARQAAESAA 167
Cdd:PHA00430  140 ADAVDDGDAVPLGQIKTWNQSAWNARNEANRSRNEADRARNQAERFNNESGASATNTkqwrSEADGSNSE-ANRFKGYAD 218

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1744921521 168 SAKQSEDASSSSASAAAQKASESSQSAAEAELSRKTAESAAGNAARDATTATEKARESAESAQSAE 233
Cdd:PHA00430  219 SMTSSVEAAKGQAESSSKEANTAGDYATKAAASASAAHASEVNAANSATAAATSANRAKQQADRAK 284
PTZ00121 PTZ00121
MAEBL; Provisional
 101-242 1.02e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521  101 EALRRFELMVEEVARHAEEAKKNAGEAETSARNAGISASQAEESAANADTSAGEASESARQAAE----SAASAKQSEDAS 176
Cdd:PTZ00121  1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADElkkaAAAKKKADEAKK 1425

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521  177 SSSASAAAQKASESSQSAAEAELSRKTAESA--AGNAARDATTA--TEKARESAESAQSAEQSRIAAEEA 242
Cdd:PTZ00121  1426 KAEEKKKADEAKKKAEEAKKADEAKKKAEEAkkAEEAKKKAEEAkkADEAKKKAEEAKKADEAKKKAEEA 1495
PTZ00121 PTZ00121
MAEBL; Provisional
 92-241 1.38e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 1.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521   92 AMSEDDVRPEALRRFELM-------VEEVARHAEEAKKNAGEAETSARNAGISASQ---AEESAANADTSAGEASESARQ 161
Cdd:PTZ00121  1569 AKKAEEDKNMALRKAEEAkkaeearIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkkAEEEKKKVEQLKKKEAEEKKK 1648

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521  162 AAESAASAKQSEDASSSSASAAAQKASESSQSAAEAELSRKTAEsAAGNAARDATTATEKARESAESAQSAEQSRIAAEE 241
Cdd:PTZ00121  1649 AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE-ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE 1727
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 114-309 1.51e-04

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 44.12  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 114 ARHAEEAKKNAGEAETSARNAGISASQAEESAANADTSAGEASESARQAAESAASAKQSEDASSSSASAAAQKASESSQS 193
Cdd:PRK12678   66 AAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKA 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 194 AAEAELSRKTAESAAGNAARDATTATEKAR----ESAESAQSAEQSRI--AAEEAVNRIPTVVGPPGPKGEPGPAGPQGP 267
Cdd:PRK12678  146 GEGGEQPATEARADAAERTEEEERDERRRRgdreDRQAEAERGERGRReeRGRDGDDRDRRDRREQGDRREERGRRDGGD 225

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1744921521 268 KGDKGERGDTGPVGATGERGPAGDAGPAGPQGPKGDRGERGE 309
Cdd:PRK12678  226 RRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFR 267
PHA03169 PHA03169
hypothetical protein; Provisional
 193-361 1.53e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 43.81  E-value: 1.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 193 SAAEAELSRKTAESAAGNAARDATTATEKARESAESAQSAEQSRIAAEEAVNRIPTVVGPPGPKGEPGPAGPQGPKGDKG 272
Cdd:PHA03169   51 PTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPES 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 273 ERGDTGPVGATGERGPAGDA-----GPAGPQGPKGDRGERGETgltgnaGPQGPKGDTGAAGPAGPQGPKGETGAAGPVG 347
Cdd:PHA03169  131 PASHSPPPSPPSHPGPHEPAppeshNPSPNQQPSSFLQPSHED------SPEEPEPPTSEPEPDSPGPPQSETPTSSPPP 204

                         170
                  ....*....|....
gi 1744921521 348 ATGPQGPKGDPGET 361
Cdd:PHA03169  205 QSPPDEPGEPQSPT 218
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
258-361 1.79e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 43.87  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 258 EPGPAGPQGPKGDKGERGDTGPVGATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKG--DTGAAGPAGP-- 333
Cdd:COG5164    62 GTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTppSGGSTTPPGDgg 141

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1744921521 334 -----QGPKGETGAAGPVGATGPQGPKGDPGET 361
Cdd:COG5164   142 stppgPGSTGPGGSTTPPGDGGSTTPPGPGGST 174
PTZ00121 PTZ00121
MAEBL; Provisional
 94-240 1.82e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 1.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521   94 SEDDVRPEALRRfelMVEEVaRHAEEAKKNAGEAETSA---RNAGISASQAEESAANADT--SAGEA---SESARQAAES 165
Cdd:PTZ00121  1374 EEAKKKADAAKK---KAEEK-KKADEAKKKAEEDKKKAdelKKAAAAKKKADEAKKKAEEkkKADEAkkkAEEAKKADEA 1449

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521  166 AASAKQSEDASSSSASAAAQKASESSQSAAE----AELSRKTAESAAGNA--ARDATTATEKARES-------------- 225
Cdd:PTZ00121  1450 KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEeakkADEAKKKAEEAKKKAdeAKKAAEAKKKADEAkkaeeakkadeakk 1529

                          170
                   ....*....|....*
gi 1744921521  226 AESAQSAEQSRIAAE 240
Cdd:PTZ00121  1530 AEEAKKADEAKKAEE 1544
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 201-360 2.43e-04

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 43.35  E-value: 2.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 201 RKTAESAAGNAARDATTATEKARESAESAQSAEQSRIAAEEAVNRIPTVVGPPGPKGEPGPAGPQGPKGDKGERGDTGpv 280
Cdd:PRK12678   47 RKGELIAAIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEA-- 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 281 GATGERGPAGDAGPAGPQGPKGDRGERGETGLTGNAGPQGPKGDTGAAGPAGPQGPKGETGAAGPVGATGPQGPKGDPGE 360
Cdd:PRK12678  125 AQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRD 204
PTZ00121 PTZ00121
MAEBL; Provisional
 111-240 2.53e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 2.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521  111 EEVaRHAEEAKKNAGEAetsaRNAGISASQAEES--AANADTSAGEA--SESARQAAESAASA-----KQSEDASSSSAS 181
Cdd:PTZ00121  1428 EEK-KKADEAKKKAEEA----KKADEAKKKAEEAkkAEEAKKKAEEAkkADEAKKKAEEAKKAdeakkKAEEAKKKADEA 1502

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1744921521  182 AAAQKASESSQSAAEAELSRKTAESAAGNAARDAttatEKAREsAESAQSAEQSRIAAE 240
Cdd:PTZ00121  1503 KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA----DEAKK-AEEKKKADELKKAEE 1556
PTZ00121 PTZ00121
MAEBL; Provisional
 112-237 3.72e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 3.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521  112 EVARHAEEAKKNAGEAetsaRNAGISASQAEESAANADTS--AGEASESARQAAESAASAKQSEDASSSSASAAAQKASE 189
Cdd:PTZ00121  1467 EEAKKADEAKKKAEEA----KKADEAKKKAEEAKKKADEAkkAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKA 1542

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1744921521  190 SSQSAAE----AELSRKTAESAAGNAARDATTATEKARESAESAQSAEQSRI 237
Cdd:PTZ00121  1543 EEKKKADelkkAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 101-242 5.06e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 5.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 101 EALRRFELMVEEVARHAEEAKKNAGEAETSARNAGISASQAEESAANADTSAGEAsESARQAAESAASAKQSEDASSSSA 180
Cdd:COG1196   316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA-EAELAEAEEELEELAEELLEALRA 394

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1744921521 181 SAAAQKASESSQSAAEAELSRKTAESAAGNAARDATTATEKARESAESAQSAEQSRIAAEEA 242
Cdd:COG1196   395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
PTZ00121 PTZ00121
MAEBL; Provisional
 92-242 9.48e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 9.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521   92 AMSEDDVRPEALRRFELMVEEVARHAEEAKKNAGEAETS--ARNAGiSASQAEESAANADTSAGEAS---ESARQAAES- 165
Cdd:PTZ00121  1092 ATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAeeARKAE-DARKAEEARKAEDAKRVEIArkaEDARKAEEAr 1170

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1744921521  166 -AASAKQSEDASSSSASAAAQKASESsQSAAEAELSRKTAESAAGNAARDAttatEKAREsAESAQSAEQSRIAAEEA 242
Cdd:PTZ00121  1171 kAEDAKKAEAARKAEEVRKAEELRKA-EDARKAEAARKAEEERKAEEARKA----EDAKK-AEAVKKAEEAKKDAEEA 1242
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 99-242 1.14e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 40.98  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521  99 RPEALRRFELMVEEVARHAEEAKKNAGEAETSARNAGISAsQAEESAANADTSAGEASESARQAAESAASAKqsedasss 178
Cdd:TIGR02794  59 KKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRA-AAEKAAKQAEQAAKQAEEKQKQAEEAKAKQA-------- 129

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1744921521 179 sasaaaqkasESSQSAAEAELSRKTAESAAGNAARDATT--ATEKARESAESAQSAEQSRIAAEEA 242
Cdd:TIGR02794 130 ----------AEAKAKAEAEAERKAKEEAAKQAEEEAKAkaAAEAKKKAEEAKKKAEAEAKAKAEA 185
PHA00430 PHA00430
tail fiber protein
 123-245 1.15e-03

tail fiber protein


Pssm-ID: 222790 [Multi-domain]  Cd Length: 568  Bit Score: 41.42  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 123 NAGEAETSARNAGISASQAEESAANADTSAGEASESARQAAESAASAKQSEDASSSSASAAAQKASESSQSAAEAELSRK 202
Cdd:PHA00430  150 PLGQIKTWNQSAWNARNEANRSRNEADRARNQAERFNNESGASATNTKQWRSEADGSNSEANRFKGYADSMTSSVEAAKG 229

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1744921521 203 TAESAAGNAARDATTATEKARESAESAQS---AEQSRIAAEEAVNR 245
Cdd:PHA00430  230 QAESSSKEANTAGDYATKAAASASAAHASevnAANSATAAATSANR 275
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 101-243 1.35e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 101 EALRRFELMVEEVARHAEEAKKNAGEAETSARNAGISASQAEESAANADTSAGEASESARQAAESAASAKQSEDASSSSA 180
Cdd:COG1196   323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1744921521 181 SAAAQKASESSQSAAEAELSRKTAESAAGNAARDATTATEKARESAESAQSAEQSRIAAEEAV 243
Cdd:COG1196   403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
PHA00430 PHA00430
tail fiber protein
 123-242 1.36e-03

tail fiber protein


Pssm-ID: 222790 [Multi-domain]  Cd Length: 568  Bit Score: 41.03  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 123 NAGEAETSARNAGISA-SQAEESAANADTSAGEASESARQAAESAASAKQSEDASSSSASAAAQKASESSQSAAEAELSR 201
Cdd:PHA00430  163 NARNEANRSRNEADRArNQAERFNNESGASATNTKQWRSEADGSNSEANRFKGYADSMTSSVEAAKGQAESSSKEANTAG 242

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1744921521 202 KTAESAAGNAARDATTATEKARESAESAQSAEQSRIAAEEA 242
Cdd:PHA00430  243 DYATKAAASASAAHASEVNAANSATAAATSANRAKQQADRA 283
PTZ00121 PTZ00121
MAEBL; Provisional
 106-241 2.03e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 2.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521  106 FELMVEEVARHA-EEAKKNAGEAETSARNAGISASQAEESAANADTSagEASESARQA-----AESAASAKqsedassss 179
Cdd:PTZ00121  1081 FDAKEDNRADEAtEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDA--RKAEEARKAedarkAEEARKAE--------- 1149

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1744921521  180 aSAAAQKASESSQSAAEAELSRKTAESAAGNAARDAtTATEKARE--SAESAQSAEQSRIAAEE 241
Cdd:PTZ00121  1150 -DAKRVEIARKAEDARKAEEARKAEDAKKAEAARKA-EEVRKAEElrKAEDARKAEAARKAEEE 1211
Peptidase_M14NE-CP-C_like cd11308
Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, ...
 5-87 2.07e-03

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.


Pssm-ID: 200604 [Multi-domain]  Cd Length: 76  Bit Score: 36.73  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521   5 ISGVLKDGTGKPIQNCTIQLKARRNSTTvvvntvasenpdeagrYSTDVEY------GQYSVILLVEGFPPSHAgTITVY 78
Cdd:cd11308     2 IKGFVTDATGNPIANATISVEGINHDVT----------------TAKDGDYwrlllpGTYNVTASAPGYQPVTK-TVTVP 64


                  ....*....
gi 1744921521  79 EDSQPGTLN 87
Cdd:cd11308    65 NNFSATVVN 73
PTZ00121 PTZ00121
MAEBL; Provisional
 94-242 2.20e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 2.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521   94 SEDDVRPEALRRFE-LMVEEVARHAEEAKKNAGEAETSARNAGIsASQAEESAANADTSAGEA-----------SESARQ 161
Cdd:PTZ00121  1542 AEEKKKADELKKAEeLKKAEEKKKAEEAKKAEEDKNMALRKAEE-AKKAEEARIEEVMKLYEEekkmkaeeakkAEEAKI 1620

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521  162 AAESAASAKQSEDASSSSASAAAQKASESSQSAAEAELSRKTAESAAGNAARDATTATEKARESAESAQSAEQSRIAAEE 241
Cdd:PTZ00121  1621 KAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE 1700


                   .
gi 1744921521  242 A 242
Cdd:PTZ00121  1701 A 1701
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 117-239 4.88e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 39.06  E-value: 4.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 117 AEEAKKNAgEAETSARNAGISASQAEESAANADTSAGEASESARQAAESAASAKqSEDASSSSASAAAQKASESSQSAAE 196
Cdd:TIGR02794 145 KEEAAKQA-EEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAK-AEAAKAKAAAEAAAKAEAEAAAAAA 222

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1744921521 197 AELSRKTAESAAGNAARDA-TTATEKARESAESAQSAEQSRIAA 239
Cdd:TIGR02794 223 AEAERKADEAELGDIFGLAsGSNAEKQGGARGAAAGSEVDKYAA 266
PRK12472 PRK12472
hypothetical protein; Provisional
 111-240 6.30e-03

hypothetical protein; Provisional


Pssm-ID: 237110 [Multi-domain]  Cd Length: 508  Bit Score: 38.70  E-value: 6.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 111 EEVARHAEEAKKNAGEAETSARNAGISASQAEESAANADTSAGEASESARQAAESAASAKQSEDASSSSASAaaqkases 190
Cdd:PRK12472  200 EDAARAADEAKTAAAAAAREAAPLKASLRKLERAKARADAELKRADKALAAAKTDEAKARAEERQQKAAQQA-------- 271

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1744921521 191 sqSAAEAELSRKTAESAAGNAARDATTATEKARES--AESAQSAEQSRIAAE 240
Cdd:PRK12472  272 --AEAATQLDTAKADAEAKRAAAAATKEAAKAAAAkkAETAKAATDAKLALE 321
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 107-242 7.90e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 7.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921521 107 ELMVEEVARHAEEAKKNAGEAETSARNAGISASQAEESAANADTSAGEASESARQAAESAASAKQSEDASSSSASAAAQK 186
Cdd:COG1196   254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1744921521 187 ASESSQSAAEAELSRKTAESAAGNAARDATTATEKARESAESAQSAEQSRIAAEEA 242
Cdd:COG1196   334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
 
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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