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Conserved domains on  [gi|1822848556|ref|WP_166021492|]
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C40 family peptidase [Streptomyces chilikensis]

Protein Classification

C40 family peptidase( domain architecture ID 13411673)

C40 family peptidase is a cell-wall hydrolase that cleaves peptide cross-bridges between glycan chains and is essential for bacterial growth and viability; typically cleaves the linkage between D-Glu and diaminopimelic acid (or Lys) within peptidoglycan stem peptides

EC:  3.4.-.-
Gene Ontology:  GO:0008233|GO:0016787|GO:0006508
MEROPS:  C40
PubMed:  18715016|12620121|11517925

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NlpC COG0791
Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];
174-387 6.38e-51

Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440554 [Multi-domain]  Cd Length: 218  Bit Score: 169.88  E-value: 6.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556 174 SSSEEDLRTSKATVQEKLTDARKLLAELTAEEKARLAEIERRKEEEARRKAEELARQETAEEKARQEALAEQEAGEATGG 253
Cdd:COG0791     1 ASVASALAAALAAAAAALAAVAAAGALAAADAAVAAALVAAAAAVLAAAALLAGPAAAVAGAAAPAVGSAGAAAAAAAAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556 254 SDAGTGSGAGGTTDASAAQGQKAVAFAEAQIGRPYVWGATGPDSYDCSGLTQAAWKAAGVDLPRTTYDQVNAGTTVPVSE 333
Cdd:COG0791    81 AGSSAAKSAAGASAPPSSTAEAIVAAALSYLGTPYVWGGTSPSGFDCSGLVQYVYRQAGISLPRTSADQAAAGTPVSRSE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1822848556 334 AEPGDLVFFYDD---VTHVGVYAGGGMMIHAPKPGTYVREESIYYDGEGS-IHSIVRP 387
Cdd:COG0791   161 LQPGDLVFFRTGgggISHVGIYLGNGKFIHASSSGKGVRISSLDSPYWKSrYVGARRV 218
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 47-243 8.87e-12

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 65.94  E-value: 8.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556  47 EEVQKKVDDLYREAEAATEKYNSAKEKSEQQREELDELLDEVAERTEELNEARERLGSYAAAQYRSGTAlPDTATFLLAD 126
Cdd:COG4942    51 KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQ-PPLALLLSPE 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556 127 APQDYFDQAQLMDRLTGRQKEAVDEFVERQAATTEKRREATESLETLSSSEEDLRTSKATVQEKLTDARKLLAELTAEEK 206
Cdd:COG4942   130 DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA 209

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1822848556 207 ArLAEIERRKEEEARRKAEELARQETAEEKARQEALA 243
Cdd:COG4942   210 E-LAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
 
Name Accession Description Interval E-value
NlpC COG0791
Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];
174-387 6.38e-51

Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440554 [Multi-domain]  Cd Length: 218  Bit Score: 169.88  E-value: 6.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556 174 SSSEEDLRTSKATVQEKLTDARKLLAELTAEEKARLAEIERRKEEEARRKAEELARQETAEEKARQEALAEQEAGEATGG 253
Cdd:COG0791     1 ASVASALAAALAAAAAALAAVAAAGALAAADAAVAAALVAAAAAVLAAAALLAGPAAAVAGAAAPAVGSAGAAAAAAAAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556 254 SDAGTGSGAGGTTDASAAQGQKAVAFAEAQIGRPYVWGATGPDSYDCSGLTQAAWKAAGVDLPRTTYDQVNAGTTVPVSE 333
Cdd:COG0791    81 AGSSAAKSAAGASAPPSSTAEAIVAAALSYLGTPYVWGGTSPSGFDCSGLVQYVYRQAGISLPRTSADQAAAGTPVSRSE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1822848556 334 AEPGDLVFFYDD---VTHVGVYAGGGMMIHAPKPGTYVREESIYYDGEGS-IHSIVRP 387
Cdd:COG0791   161 LQPGDLVFFRTGgggISHVGIYLGNGKFIHASSSGKGVRISSLDSPYWKSrYVGARRV 218
NLPC_P60 pfam00877
NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.
 285-374 7.18e-32

NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.


Pssm-ID: 395705 [Multi-domain]  Cd Length: 105  Bit Score: 116.23  E-value: 7.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556 285 GRPYVWGATGPDSYDCSGLTQAAWKAAGVDLPRTTYDQVNAGT-TVPVSEAEPGDLVFF--YDDVTHVGVYAGGGMMIHA 361
Cdd:pfam00877   1 GVPYRWGGGSPSGFDCSGLVRYAFAKVGIELPRSSGQQYNAGKkTIPKSEPQRGDLVFFgtGKGISHVGIYLGNGQMLHA 80

                          90
                  ....*....|...
gi 1822848556 362 PKPGTyVREESIY 374
Cdd:pfam00877  81 STGGG-VSISSLN 92
PRK13914 PRK13914
invasion associated endopeptidase;
145-379 1.94e-21

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 95.64  E-value: 1.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556 145 QKEAVDEFVERQAATTEKRREATES-LETLSSSEEDLRTSKATVQEKLTDARKLLAELTAEEKARLAEIERRKEEEARRK 223
Cdd:PRK13914  239 QKLAIKQTANTATPKAEVKTEAPAAeKQAAPVVKENTNTNTATTEKKETTTQQQTAPKAPTEAAKPAPAPSTNTNANKTN 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556 224 AEELARQETAEEKARQEALAEQEAGEATGGSDAGTGSGAGGTTDASAAQGqkAVAFAEAQIGRPYVWGATGPDSYDCSGL 303
Cdd:PRK13914  319 TNTNTNTNNTNTSTPSKNTNTNTNSNTNTNSNTNANQGSSNNNSNSSASA--IIAEAQKHLGKAYSWGGNGPTTFDCSGY 396

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822848556 304 TQAAWKAAGVDLPRTTYDQVNAGTTVPVSEAEPGDLVFF-Y-DDVTHVGVYAGGGMMIHAPKPGtyVREESIYYDGEG 379
Cdd:PRK13914  397 TKYVFAKAGISLPRTSGAQYASTTRISESQAKPGDLVFFdYgSGISHVGIYVGNGQMINAQDNG--VKYDNIHGSGWG 472
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 47-243 8.87e-12

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 65.94  E-value: 8.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556  47 EEVQKKVDDLYREAEAATEKYNSAKEKSEQQREELDELLDEVAERTEELNEARERLGSYAAAQYRSGTAlPDTATFLLAD 126
Cdd:COG4942    51 KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQ-PPLALLLSPE 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556 127 APQDYFDQAQLMDRLTGRQKEAVDEFVERQAATTEKRREATESLETLSSSEEDLRTSKATVQEKLTDARKLLAELTAEEK 206
Cdd:COG4942   130 DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA 209

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1822848556 207 ArLAEIERRKEEEARRKAEELARQETAEEKARQEALA 243
Cdd:COG4942   210 E-LAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 46-286 2.25e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 2.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556   46 LEEVQKKVDDLYREAEAATEKYNSAKEKSEQQREELDELLDEVAERTEELNEARERLGSYAAAQYRsgtaLPDTATFLLA 125
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR----LEQQKQILRE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556  126 DAPQDYFDQAQLMDRLT------GRQKEAVDEFVERQAATTEKRREATESLETLSSSEEDLRTSKATVQEKLTDARKLLA 199
Cdd:TIGR02168  310 RLANLERQLEELEAQLEelesklDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556  200 ELTAEE----------KARLAEIERRKEEEARRKAEELARQETAEEKARQEALAEQEAGEATGGSDAGTGSGAGGTTDAS 269
Cdd:TIGR02168  390 QLELQIaslnneierlEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469

                          250
                   ....*....|....*..
gi 1822848556  270 AAQGQKAVAFAEAQIGR 286
Cdd:TIGR02168  470 LEEAEQALDAAERELAQ 486
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
59-200 3.08e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.19  E-value: 3.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556  59 EAEAATEKYNSAKEKSEQQREELDELLDEVAERTEELNE-----------------ARERLGSYAAAQYRSGTALPDTAT 121
Cdd:PRK02224  217 ELDEEIERYEEQREQARETRDEADEVLEEHEERREELETleaeiedlretiaeterEREELAEEVRDLRERLEELEEERD 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556 122 FLLADAPQDYFDQAQLMDR---LTGRQKEAVDEFVERQAATTEKRREA---TESLETLSSSEEDLRTSKATVQEKLTDAR 195
Cdd:PRK02224  297 DLLAEAGLDDADAEAVEARreeLEDRDEELRDRLEECRVAAQAHNEEAeslREDADDLEERAEELREEAAELESELEEAR 376


                  ....*
gi 1822848556 196 KLLAE 200
Cdd:PRK02224  377 EAVED 381
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
 81-316 1.68e-03

MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.


Pssm-ID: 467957 [Multi-domain]  Cd Length: 1848  Bit Score: 40.59  E-value: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556   81 LDELLDEV---AERTEELNEARERLGSYAAAQyrsgTALPDTATfllADAPQDYFDQ--AQLMDRLTGRQK--EAVDEFV 153
Cdd:NF012221  1527 LGYILDNVvatSESSQQADAVSKHAKQDDAAQ----NALADKER---AEADRQRLEQekQQQLAAISGSQSqlESTDQNA 1599

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556  154 -------ERQAATTEKR------REATESLETLSS-------SEEDLRTSKA-----TVQEKLTDARKLLAELTAEEKAR 208
Cdd:NF012221  1600 letngqaQRDAILEESRavtkelTTLAQGLDALDSqatyageSGDQWRNPFAgglldRVQEQLDDAKKISGKQLADAKQR 1679

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556  209 LAEIERRKEEEARRKAEELARQE--------------TAEEKARQEALA-EQEAGEA-TGGSDAGTGSGAGGTTDASAAQ 272
Cdd:NF012221  1680 HVDNQQKVKDAVAKSEAGVAQGEqnqanaeqdiddakADAEKRKDDALAkQNEAQQAeSDANAAANDAQSRGEQDASAAE 1759

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1822848556  273 GQKAVAFAEAQIG------RPYVWGATGpdsydcSGLTQAAWKAAGVDLP 316
Cdd:NF012221  1760 NKANQAQADAKGAkqdesdKPNRQGAAG------SGLSGKAYSVEGVAEP 1803
 
Name Accession Description Interval E-value
NlpC COG0791
Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];
174-387 6.38e-51

Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440554 [Multi-domain]  Cd Length: 218  Bit Score: 169.88  E-value: 6.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556 174 SSSEEDLRTSKATVQEKLTDARKLLAELTAEEKARLAEIERRKEEEARRKAEELARQETAEEKARQEALAEQEAGEATGG 253
Cdd:COG0791     1 ASVASALAAALAAAAAALAAVAAAGALAAADAAVAAALVAAAAAVLAAAALLAGPAAAVAGAAAPAVGSAGAAAAAAAAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556 254 SDAGTGSGAGGTTDASAAQGQKAVAFAEAQIGRPYVWGATGPDSYDCSGLTQAAWKAAGVDLPRTTYDQVNAGTTVPVSE 333
Cdd:COG0791    81 AGSSAAKSAAGASAPPSSTAEAIVAAALSYLGTPYVWGGTSPSGFDCSGLVQYVYRQAGISLPRTSADQAAAGTPVSRSE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1822848556 334 AEPGDLVFFYDD---VTHVGVYAGGGMMIHAPKPGTYVREESIYYDGEGS-IHSIVRP 387
Cdd:COG0791   161 LQPGDLVFFRTGgggISHVGIYLGNGKFIHASSSGKGVRISSLDSPYWKSrYVGARRV 218
NLPC_P60 pfam00877
NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.
 285-374 7.18e-32

NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.


Pssm-ID: 395705 [Multi-domain]  Cd Length: 105  Bit Score: 116.23  E-value: 7.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556 285 GRPYVWGATGPDSYDCSGLTQAAWKAAGVDLPRTTYDQVNAGT-TVPVSEAEPGDLVFF--YDDVTHVGVYAGGGMMIHA 361
Cdd:pfam00877   1 GVPYRWGGGSPSGFDCSGLVRYAFAKVGIELPRSSGQQYNAGKkTIPKSEPQRGDLVFFgtGKGISHVGIYLGNGQMLHA 80

                          90
                  ....*....|...
gi 1822848556 362 PKPGTyVREESIY 374
Cdd:pfam00877  81 STGGG-VSISSLN 92
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 46-380 2.58e-27

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 111.46  E-value: 2.58e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556  46 LEEVQKKVDDLYREAEAATEKYNSAKEKSEQQREELDELLDEVAERTEELNEARERLGSYAAAQYRSGTALPDTATFLLA 125
Cdd:COG3883    32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVLLGS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556 126 DAPQDYFDQAQLMDRLTGRQKEAVDEFVERQAATTEKRREATESLETLSSSEEDLRTSKATVQEKLTDARKLLAELTAEE 205
Cdd:COG3883   112 ESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEE 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556 206 KARLAEIERRKEEEARRKAEELARQETAEEKARQEALAEQEAGEAT-------------GGSDAGTGSGAGGTTDASAAQ 272
Cdd:COG3883   192 AAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAaaaaaaasaagagAAGAAGAAAGSAGAAGAAAGA 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556 273 GQKAVAFAEAQIGRPYVWGATGPDSYDCSGLTQAAWKAAGVDLPRTTYDQVNAGTTVPVSEAEPGDLVFFYDDVTHVGVY 352
Cdd:COG3883   272 AGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGG 351

                         330       340
                  ....*....|....*....|....*...
gi 1822848556 353 AGGGMMIHAPKPGTYVREESIYYDGEGS 380
Cdd:COG3883   352 GGGGGGSSSGGGGGGVGLSVGGGYVGGA 379
PRK13914 PRK13914
invasion associated endopeptidase;
145-379 1.94e-21

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 95.64  E-value: 1.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556 145 QKEAVDEFVERQAATTEKRREATES-LETLSSSEEDLRTSKATVQEKLTDARKLLAELTAEEKARLAEIERRKEEEARRK 223
Cdd:PRK13914  239 QKLAIKQTANTATPKAEVKTEAPAAeKQAAPVVKENTNTNTATTEKKETTTQQQTAPKAPTEAAKPAPAPSTNTNANKTN 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556 224 AEELARQETAEEKARQEALAEQEAGEATGGSDAGTGSGAGGTTDASAAQGqkAVAFAEAQIGRPYVWGATGPDSYDCSGL 303
Cdd:PRK13914  319 TNTNTNTNNTNTSTPSKNTNTNTNSNTNTNSNTNANQGSSNNNSNSSASA--IIAEAQKHLGKAYSWGGNGPTTFDCSGY 396

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822848556 304 TQAAWKAAGVDLPRTTYDQVNAGTTVPVSEAEPGDLVFF-Y-DDVTHVGVYAGGGMMIHAPKPGtyVREESIYYDGEG 379
Cdd:PRK13914  397 TKYVFAKAGISLPRTSGAQYASTTRISESQAKPGDLVFFdYgSGISHVGIYVGNGQMINAQDNG--VKYDNIHGSGWG 472
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 47-243 8.87e-12

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 65.94  E-value: 8.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556  47 EEVQKKVDDLYREAEAATEKYNSAKEKSEQQREELDELLDEVAERTEELNEARERLGSYAAAQYRSGTAlPDTATFLLAD 126
Cdd:COG4942    51 KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQ-PPLALLLSPE 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556 127 APQDYFDQAQLMDRLTGRQKEAVDEFVERQAATTEKRREATESLETLSSSEEDLRTSKATVQEKLTDARKLLAELTAEEK 206
Cdd:COG4942   130 DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA 209

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1822848556 207 ArLAEIERRKEEEARRKAEELARQETAEEKARQEALA 243
Cdd:COG4942   210 E-LAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
spr PRK10838
bifunctional murein DD-endopeptidase/murein LD-carboxypeptidase;
285-361 5.69e-11

bifunctional murein DD-endopeptidase/murein LD-carboxypeptidase;


Pssm-ID: 236773 [Multi-domain]  Cd Length: 190  Bit Score: 61.32  E-value: 5.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556 285 GRPYVWGATGPDSYDCSGLTQAAWKAA-GVDLPRTTYDQVNAGTTVPVSEAEPGDLVFFYDDVT--HVGVYAGGGMMIHA 361
Cdd:PRK10838   79 GVRYRLGGSTKKGIDCSAFVQRTFREQfGLELPRSTYEQQEMGKSVSRSKLRTGDLVLFRAGSTgrHVGIYIGNNQFVHA 158
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 45-255 1.17e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556  45 GLEEVQKKVDDLYREAEAATEKYNSAKEKSEQQREELDELLDEVAERTEELNEARERLGSYAAAQYRSGTALPDtatfLL 124
Cdd:COG1196   303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE----AE 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556 125 ADAPQDYFDQAQLMDRLTGRQKEAvdEFVERQAATTEKRREATES-LETLSSSEEDLRTSKATVQEKLTDARKLLAELTA 203
Cdd:COG1196   379 EELEELAEELLEALRAAAELAAQL--EELEEAEEALLERLERLEEeLEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1822848556 204 EEKARLAEIERRKEEEARRKAEELARQETAEEKARQEALAEQEAGEATGGSD 255
Cdd:COG1196   457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
46-209 4.55e-07

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.84  E-value: 4.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556   46 LEEVQKKVDDLYREAEAATEKYNSAKEKSEQQREELDELLD---------------EVAERTEELNEARERLGSYAAAQY 110
Cdd:COG4913    290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAqirgnggdrleqlerEIERLERELEERERRRARLEALLA 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556  111 RSGTALPDTATFLLADapqdyfdQAQLMDRLTGRqKEAVDEFVERQAATTEKRREATESLETLSSSEEDLRTSKATVQEK 190
Cdd:COG4913    370 ALGLPLPASAEEFAAL-------RAEAAALLEAL-EEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR 441

                          170
                   ....*....|....*....
gi 1822848556  191 LTDARKLLAELTAEEKARL 209
Cdd:COG4913    442 LLALRDALAEALGLDEAEL 460
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 46-286 2.25e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 2.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556   46 LEEVQKKVDDLYREAEAATEKYNSAKEKSEQQREELDELLDEVAERTEELNEARERLGSYAAAQYRsgtaLPDTATFLLA 125
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR----LEQQKQILRE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556  126 DAPQDYFDQAQLMDRLT------GRQKEAVDEFVERQAATTEKRREATESLETLSSSEEDLRTSKATVQEKLTDARKLLA 199
Cdd:TIGR02168  310 RLANLERQLEELEAQLEelesklDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556  200 ELTAEE----------KARLAEIERRKEEEARRKAEELARQETAEEKARQEALAEQEAGEATGGSDAGTGSGAGGTTDAS 269
Cdd:TIGR02168  390 QLELQIaslnneierlEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469

                          250
                   ....*....|....*..
gi 1822848556  270 AAQGQKAVAFAEAQIGR 286
Cdd:TIGR02168  470 LEEAEQALDAAERELAQ 486
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 46-283 8.65e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 8.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556  46 LEEVQKKVDDLYREAEAAtEKYNSAKEKSEQ--------QREELDELLDEVAERTEELNEARERLgsyaAAQYRSGTALP 117
Cdd:COG1196   195 LGELERQLEPLERQAEKA-ERYRELKEELKEleaellllKLRELEAELEELEAELEELEAELEEL----EAELAELEAEL 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556 118 DTATFLLADApQDYFDQAQLMDRLTGRQKEavdEFVERQAATTEKRREATESLETLSSSEEDLRTSKATVQEKLTDARKL 197
Cdd:COG1196   270 EELRLELEEL-ELELEEAQAEEYELLAELA---RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556 198 LAELTAE----EKARLAEIERRKEEearrKAEELARQETAEEKARQEALAEQEAGEATGGSDAGTGSGAGGTTDASAAQG 273
Cdd:COG1196   346 LEEAEEEleeaEAELAEAEEALLEA----EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421

                         250
                  ....*....|
gi 1822848556 274 QKAVAFAEAQ 283
Cdd:COG1196   422 ELEELEEALA 431
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 46-207 2.88e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 2.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556   46 LEEVQKKVDDLYREAEAATEKYNSAKEKSEQQREELDELLDEVAERTEELNEARERLGSYAAAQYRSGTALPDTatflla 125
Cdd:TIGR02168  346 LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL------ 419

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556  126 dapqdyfdQAQLMDRLTGRQKEAVDEFVERQAATTEKRREATESLETLSSSEEDLRTSKATVQEKLTDARKLLAELTAEE 205
Cdd:TIGR02168  420 --------QQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491


                   ..
gi 1822848556  206 KA 207
Cdd:TIGR02168  492 DS 493
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
59-200 3.08e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.19  E-value: 3.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556  59 EAEAATEKYNSAKEKSEQQREELDELLDEVAERTEELNE-----------------ARERLGSYAAAQYRSGTALPDTAT 121
Cdd:PRK02224  217 ELDEEIERYEEQREQARETRDEADEVLEEHEERREELETleaeiedlretiaeterEREELAEEVRDLRERLEELEEERD 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556 122 FLLADAPQDYFDQAQLMDR---LTGRQKEAVDEFVERQAATTEKRREA---TESLETLSSSEEDLRTSKATVQEKLTDAR 195
Cdd:PRK02224  297 DLLAEAGLDDADAEAVEARreeLEDRDEELRDRLEECRVAAQAHNEEAeslREDADDLEERAEELREEAAELESELEEAR 376


                  ....*
gi 1822848556 196 KLLAE 200
Cdd:PRK02224  377 EAVED 381
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
51-102 2.92e-04

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.21  E-value: 2.92e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1822848556  51 KKVDDLYREAEAATEKYNSAKEKSEQQREELDELLDEVAERTEELNEARERL 102
Cdd:COG1340   202 KEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQ 253
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 46-250 1.44e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556   46 LEEVQKKVDDLYREAEAATEKYNSAKEKSEQQREELDELLDEVAERTEELNEARERLGSyaaaqyrsgtalpdtATFLLA 125
Cdd:TIGR02168  714 LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE---------------AEEELA 778

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556  126 DAPQDYFDQAQLMDRLTGR---QKEAVDEFVERQAATTEKRREATESLETLSSSEEDLRTSKATVQEKLTDARKLLAELT 202
Cdd:TIGR02168  779 EAEAEIEELEAQIEQLKEElkaLREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1822848556  203 AE------EKARLAEIERRKEEEARRKAEELARQETAEEKARQEAL-AEQEAGEA 250
Cdd:TIGR02168  859 AEieeleeLIEELESELEALLNERASLEEALALLRSELEELSEELReLESKRSEL 913
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
46-252 1.56e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556  46 LEEVQKKVDDLYREAEAATEKYNSAKEKSEQQREELDELLDEVAERTEELNEARERLGSyaAAQYRSGTALPdTATFLLA 125
Cdd:PRK02224  386 IEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEE--AEALLEAGKCP-ECGQPVE 462

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556 126 DAPQdyfdqaqlMDRLTGR--QKEAVDEFVERQAATTEKRREATESLETLSSSEEDLrtskatvqEKLTDARKLLAELTA 203
Cdd:PRK02224  463 GSPH--------VETIEEDreRVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRI--------ERLEERREDLEELIA 526

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1822848556 204 EEKARLAEIERRKEEEARRKAEELARQETAEEKARQEALAEQEAGEATG 252
Cdd:PRK02224  527 ERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVA 575
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
 81-316 1.68e-03

MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.


Pssm-ID: 467957 [Multi-domain]  Cd Length: 1848  Bit Score: 40.59  E-value: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556   81 LDELLDEV---AERTEELNEARERLGSYAAAQyrsgTALPDTATfllADAPQDYFDQ--AQLMDRLTGRQK--EAVDEFV 153
Cdd:NF012221  1527 LGYILDNVvatSESSQQADAVSKHAKQDDAAQ----NALADKER---AEADRQRLEQekQQQLAAISGSQSqlESTDQNA 1599

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556  154 -------ERQAATTEKR------REATESLETLSS-------SEEDLRTSKA-----TVQEKLTDARKLLAELTAEEKAR 208
Cdd:NF012221  1600 letngqaQRDAILEESRavtkelTTLAQGLDALDSqatyageSGDQWRNPFAgglldRVQEQLDDAKKISGKQLADAKQR 1679

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556  209 LAEIERRKEEEARRKAEELARQE--------------TAEEKARQEALA-EQEAGEA-TGGSDAGTGSGAGGTTDASAAQ 272
Cdd:NF012221  1680 HVDNQQKVKDAVAKSEAGVAQGEqnqanaeqdiddakADAEKRKDDALAkQNEAQQAeSDANAAANDAQSRGEQDASAAE 1759

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1822848556  273 GQKAVAFAEAQIG------RPYVWGATGpdsydcSGLTQAAWKAAGVDLP 316
Cdd:NF012221  1760 NKANQAQADAKGAkqdesdKPNRQGAAG------SGLSGKAYSVEGVAEP 1803
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
72-246 2.20e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556  72 EKSEQQREELDELLDEVAERTEELNEARERLGSYAAAQYRSGTALP--DTATFLLADAPQDYFDQAQLMDRLTGRQKEAV 149
Cdd:PRK02224  471 EEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIEEKRERAEELRERAAELE 550

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556 150 DEFVERQAATTEKRREATESLETLSSSEEDLRTSKATVqEKLTDARKLLAELTAeekarlaeierrkeeearrkaeelAR 229
Cdd:PRK02224  551 AEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERI-ESLERIRTLLAAIAD------------------------AE 605

                         170
                  ....*....|....*..
gi 1822848556 230 QETAEEKARQEALAEQE 246
Cdd:PRK02224  606 DEIERLREKREALAELN 622
PTZ00121 PTZ00121
MAEBL; Provisional
 47-250 2.26e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 2.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556   47 EEVQKKVDDLYREAEAATEKYNSAKEKSEQQREELDELLDEvAERTEELNEARERLGSYAAAQyrsgtalpdtatfllAD 126
Cdd:PTZ00121  1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADE-AEAAEEKAEAAEKKKEEAKKK---------------AD 1381

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556  127 APQDYFDQAQLMDRLTGR---QKEAVDEfVERQAATTEKRREATESLETLSSSEEdlRTSKATVQEKLTDARKLLAELTA 203
Cdd:PTZ00121  1382 AAKKKAEEKKKADEAKKKaeeDKKKADE-LKKAAAAKKKADEAKKKAEEKKKADE--AKKKAEEAKKADEAKKKAEEAKK 1458

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1822848556  204 EEKARLAEIERRKEEEARRKAEELARQETAEEKARQEALAEQEAGEA 250
Cdd:PTZ00121  1459 AEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA 1505
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 43-189 2.42e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 2.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556   43 RPGLEEVQKKVDDLYREAEAATEKYNSAKEKSEQQREELDELLDEVAERTEELNEARERLGSYAAAQYRsgtalpDTATF 122
Cdd:TIGR02168  882 RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYS------LTLEE 955

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822848556  123 LLADAPQDYFDQAQLMDRLTgRQKEAVDEFVERQAATTEKRREATESLETLSSSEEDLRTSKATVQE 189
Cdd:TIGR02168  956 AEALENKIEDDEEEARRRLK-RLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 46-286 2.70e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556  46 LEEVQKKVDDLYREAEAATEKYNSAKEKSEQQREELDELLDEVAERTEELNEARERLGSYAAAQYRSgtalpdtatflla 125
Cdd:COG1196   342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA------------- 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556 126 dapqdyfdQAQLMDRLTgRQKEAVDEFVERQAATTEKRREATESLETLSSSEEDLRTSKATVQEKLTDARKLLAELTAEE 205
Cdd:COG1196   409 --------EEALLERLE-RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556 206 KARLAEIERRKEEEARRKAEELARQETAEEKARQEALAEQEAGEATGGSDAGTGSGAGGTTDASAAQGQKAVAFAEAQIG 285
Cdd:COG1196   480 AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVA 559


                  .
gi 1822848556 286 R 286
Cdd:COG1196   560 A 560
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 46-207 3.39e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.75  E-value: 3.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556  46 LEEVQKKVDDLYREAEAATEKYNSAKEKSEQQREELDELLDEVAERTEELNEARERLGSYAAAQYRSGTalpdtatflla 125
Cdd:COG1579    19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN----------- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556 126 daPQDYFDQAQLMDRLTGRQKEAVDEFVERQAATTEKRREATESLETLSSSEEDLRTSKATVQEKLTDARKLLAELTAEE 205
Cdd:COG1579    88 --NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165


                  ..
gi 1822848556 206 KA 207
Cdd:COG1579   166 EE 167
PTZ00121 PTZ00121
MAEBL; Provisional
 48-246 3.69e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 3.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556   48 EVQKKVDDLYREAEAAtEKYNSAKEKSEQQR--EELDELLDEvAERTEELNEARERLGSYAAAQYRSGTALPDTATFLLA 125
Cdd:PTZ00121  1428 EEKKKADEAKKKAEEA-KKADEAKKKAEEAKkaEEAKKKAEE-AKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA 1505

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556  126 DAPQDYFDQAQLMDRltGRQKEAVDEFVERQAATTEKRREATESLETLSSSEEdLRTS---KATVQEKLTDARKLLAELT 202
Cdd:PTZ00121  1506 AEAKKKADEAKKAEE--AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE-LKKAeekKKAEEAKKAEEDKNMALRK 1582

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1822848556  203 AE-----EKARLAEIERRKEEEARRKAEELARQETAEEKARQEALAEQE 246
Cdd:PTZ00121  1583 AEeakkaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE 1631
PTZ00121 PTZ00121
MAEBL; Provisional
 47-250 5.08e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 5.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556   47 EEVQKKVDDLyREAEAATEKYNSAKEKSEQQREEldellDEVAERTEELNEARErLGSYAAAQYRSGTALPDTATFLLAD 126
Cdd:PTZ00121  1401 EEDKKKADEL-KKAAAAKKKADEAKKKAEEKKKA-----DEAKKKAEEAKKADE-AKKKAEEAKKAEEAKKKAEEAKKAD 1473

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556  127 APQDYFDQAQLMDRLTGRQKEAvdefvERQAATTEKRREATESLETLSSSEEdlrTSKATVQEKLTDARKLLAELTAEEK 206
Cdd:PTZ00121  1474 EAKKKAEEAKKADEAKKKAEEA-----KKKADEAKKAAEAKKKADEAKKAEE---AKKADEAKKAEEAKKADEAKKAEEK 1545

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1822848556  207 AR---LAEIERRKEEEARRKAEELARQETAEEKARQEALAEQEAGEA 250
Cdd:PTZ00121  1546 KKadeLKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEA 1592
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
46-204 5.86e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 5.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556  46 LEEVQKKVDDLYREAEAATEKYNSAKEKSEQQREELDELLDE----------VAERTEELNEARERLGSYAAAQYRSGTA 115
Cdd:PRK02224  260 IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQA 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556 116 LPDTATFLLADA------PQDYFDQAQLMDRLTGRQKEAVDEFVERQAATTEKRREATESLETLSSSEEDLRTSKATVQE 189
Cdd:PRK02224  340 HNEEAESLREDAddleerAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE 419

                         170
                  ....*....|....*
gi 1822848556 190 KLTDARKLLAELTAE 204
Cdd:PRK02224  420 ERDELREREAELEAT 434
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
75-251 7.27e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 7.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556   75 EQQREELDELLDEVAERTEELNEARERLGSYAAAQYRsgtalpdtatflLADAPQDYFDQAQLMDRLT--GRQKEAVDEF 152
Cdd:COG4913    616 EAELAELEEELAEAEERLEALEAELDALQERREALQR------------LAEYSWDEIDVASAEREIAelEAELERLDAS 683

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556  153 VERQAATTEKRREATESLETLSSSEEDLRTSKATVQEKLTDARKLLAELtaeeKARLAEIERRKEEEARRKAEELARQET 232
Cdd:COG4913    684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL----QDRLEAAEDLARLELRALLEERFAAAL 759

                          170       180
                   ....*....|....*....|.
gi 1822848556  233 AEEKARQ--EALAEQEAGEAT 251
Cdd:COG4913    760 GDAVERElrENLEERIDALRA 780
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
41-205 8.88e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.10  E-value: 8.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556  41 SDRPGLEEVQKKVDDLYREAEAATEKYNSAKEKSEQQREELDELldevAERTEELNEARERLGSYAAaqyrsgtalpdta 120
Cdd:PRK02224  534 EKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAEL----NSKLAELKERIESLERIRT------------- 596

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822848556 121 tflLADAPQDYFDQAQ-LMDRLTGRQkEAVDEFVERQAATTEKRREATESLEtlSSSEEDLRTSKATVQEKLTDARKLLA 199
Cdd:PRK02224  597 ---LLAAIADAEDEIErLREKREALA-ELNDERRERLAEKRERKRELEAEFD--EARIEEAREDKERAEEYLEQVEEKLD 670


                  ....*.
gi 1822848556 200 ELTAEE 205
Cdd:PRK02224  671 ELREER 676
 
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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