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Conserved domains on  [gi|959049293|ref|XP_014727319|]
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PREDICTED: coiled-coil domain-containing protein 93 [Sturnus vulgaris]

Protein Classification

KOG2701 domain-containing protein( domain architecture ID 13763695)

KOG2701 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CCDC93_CC pfam09762
CCDC93, coiled-coil domain; This is a coiled-coil domain found in CCDC93. Human CCDC93 is part ...
 31-206 6.31e-97

CCDC93, coiled-coil domain; This is a coiled-coil domain found in CCDC93. Human CCDC93 is part of the COMMD/CCDC22/CCDC93 (CCC) complex that interacts with the multisubunit WASH complex, which is required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. The CCC complex controls Notch activation by modulating its intracellular trafficking.


:

Pssm-ID: 462886  Cd Length: 173  Bit Score: 293.81  E-value: 6.31e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293   31 LELLVAAGYFRARIKGLSPFDKVVGGMTWCITTCSFDIDVDLLFQENSTIGQKIALTEKIVSVLPKMKCPHRLEPHQIQG 110
Cdd:pfam09762   1 LDLLVAAGYFRARIKSLSPFDKIVGGMTWCIDASNPDVDVDLLFQENSTIGEKIALTEKIVRALPKMKCPYALEPHQIQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293  111 LDFIHIFPVVQWLVKRAIETREEMGDYVRSYSISQFQKTHRLPEDEEFmQRKEKALKTVTDIFEVYKPQRKYKRQtgAEE 190
Cdd:pfam09762  81 LDFIVIFPVVQWLVKRVIETREERGDFLRRFAANQFSKAYQLPEDQAE-RKKERAADTVRRLRDVYAPKRRFKRV--AGI 157

                         170
                  ....*....|....*.
gi 959049293  191 LLDEESKVHATLLEYG 206
Cdd:pfam09762 158 IRDEEARVRSTLLEYG 173
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 281-555 3.41e-08

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.99  E-value: 3.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293   281 GLQSDEIKQIVSEYAEKQSELSAEERPERlgaaqQHRRKVASLNKQILQKNKLLEELQAKCADLQAKCTEAKKTLTEVKS 360
Cdd:TIGR02168  228 ALLVLRLEELREELEELQEELKEAEEELE-----ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ 302

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293   361 YSEKLDKELAALETIESQADSSILQSLRALVAMNENLKSQEQEF------KAHCREEMERLQQNIESLK--AEALENGEE 432
Cdd:TIGR02168  303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLeelkeeLESLEAELEELEAELEELEsrLEELEEQLE 382

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293   433 QEPNKI--IEQQYKAEKEKLQKIRLLLARRNREIAILQRKIDEVPSRAELTQYQkrfiELYSQVSATHKETKQFFTLYNT 510
Cdd:TIGR02168  383 TLRSKVaqLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK----ELQAELEELEEELEELQEELER 458

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 959049293   511 LDDKKVYLEKEVNLLNSIYDNFHQAMASSGSREQFLRQMEQIVEG 555
Cdd:TIGR02168  459 LEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
 
Name Accession Description Interval E-value
CCDC93_CC pfam09762
CCDC93, coiled-coil domain; This is a coiled-coil domain found in CCDC93. Human CCDC93 is part ...
 31-206 6.31e-97

CCDC93, coiled-coil domain; This is a coiled-coil domain found in CCDC93. Human CCDC93 is part of the COMMD/CCDC22/CCDC93 (CCC) complex that interacts with the multisubunit WASH complex, which is required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. The CCC complex controls Notch activation by modulating its intracellular trafficking.


Pssm-ID: 462886  Cd Length: 173  Bit Score: 293.81  E-value: 6.31e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293   31 LELLVAAGYFRARIKGLSPFDKVVGGMTWCITTCSFDIDVDLLFQENSTIGQKIALTEKIVSVLPKMKCPHRLEPHQIQG 110
Cdd:pfam09762   1 LDLLVAAGYFRARIKSLSPFDKIVGGMTWCIDASNPDVDVDLLFQENSTIGEKIALTEKIVRALPKMKCPYALEPHQIQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293  111 LDFIHIFPVVQWLVKRAIETREEMGDYVRSYSISQFQKTHRLPEDEEFmQRKEKALKTVTDIFEVYKPQRKYKRQtgAEE 190
Cdd:pfam09762  81 LDFIVIFPVVQWLVKRVIETREERGDFLRRFAANQFSKAYQLPEDQAE-RKKERAADTVRRLRDVYAPKRRFKRV--AGI 157

                         170
                  ....*....|....*.
gi 959049293  191 LLDEESKVHATLLEYG 206
Cdd:pfam09762 158 IRDEEARVRSTLLEYG 173
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 281-555 3.41e-08

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: 56.99  E-value: 3.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293   281 GLQSDEIKQIVSEYAEKQSELSAEERPERlgaaqQHRRKVASLNKQILQKNKLLEELQAKCADLQAKCTEAKKTLTEVKS 360
Cdd:TIGR02168  228 ALLVLRLEELREELEELQEELKEAEEELE-----ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ 302

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293   361 YSEKLDKELAALETIESQADSSILQSLRALVAMNENLKSQEQEF------KAHCREEMERLQQNIESLK--AEALENGEE 432
Cdd:TIGR02168  303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLeelkeeLESLEAELEELEAELEELEsrLEELEEQLE 382

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293   433 QEPNKI--IEQQYKAEKEKLQKIRLLLARRNREIAILQRKIDEVPSRAELTQYQkrfiELYSQVSATHKETKQFFTLYNT 510
Cdd:TIGR02168  383 TLRSKVaqLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK----ELQAELEELEEELEELQEELER 458

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 959049293   511 LDDKKVYLEKEVNLLNSIYDNFHQAMASSGSREQFLRQMEQIVEG 555
Cdd:TIGR02168  459 LEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 295-473 1.28e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293 295 AEKQSELSAEERPERLGAAQQHRRKVASLNKQILQKNKLLEELQAKCADLQAKCTEAKKTLTEVKSYSEKLDKELAALET 374
Cdd:COG1196  300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293 375 IESQADSSILQSLRALVAMNENLKSQEQEFKAHcREEMERLQQNIESLKAEALENGEEQEPNKIIEQQYKAEKEKLQ--- 451
Cdd:COG1196  380 ELEELAEELLEALRAAAELAAQLEELEEAEEAL-LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEeee 458

                        170       180
                 ....*....|....*....|...
gi 959049293 452 -KIRLLLARRNREIAILQRKIDE 473
Cdd:COG1196  459 eALLELLAELLEEAALLEAALAE 481
PTZ00121 PTZ00121
MAEBL; Provisional
 180-479 6.20e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 6.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293  180 RKYKRQTGAEELLDEESkvhATLLEYGRRYGFSRQAGKTEQAEDKKAALPPGLAAAGKAepcDEVDLQAAEELRIKTLMT 259
Cdd:PTZ00121 1182 RKAEEVRKAEELRKAED---ARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKK---DAEEAKKAEEERNNEEIR 1255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293  260 GMAAMATEEGKLTASTVGQIVGLQSDEIKQivSEYAEKQSELSAEERperlgaaqqhRRKVASLNKQILQKNKLlEELQA 339
Cdd:PTZ00121 1256 KFEEARMAHFARRQAAIKAEEARKADELKK--AEEKKKADEAKKAEE----------KKKADEAKKKAEEAKKA-DEAKK 1322

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293  340 KCADLQAKCTEAKKTLTEVKSYSEKLDKELAA----LETIESQADSSILQSLRALVAMNENLKSQEQEFKA-HCREEMER 414
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAaadeAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAdEAKKKAEE 1402

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 959049293  415 LQQNIESLKAEALENGEEQEPNKIIEQQYKAEKEKLQKIRLLLARRNREIAILQRKIDEVPSRAE 479
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE 1467
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 331-473 3.96e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 39.66  E-value: 3.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293 331 NKLLEELQAKCADLQAKCTEAKKTLTEvksYSEKLDKELAALETIESqadssilqslralvAMNENLKSQEQefkAHCRE 410
Cdd:cd22656  120 KALLDDLLKEAKKYQDKAAKVVDKLTD---FENQTEKDQTALETLEK--------------ALKDLLTDEGG---AIARK 179

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 959049293 411 EMERLQQNIESLKAEALENGEE--QEPNKIIeQQYKAEKEKLQKIRLLLARRNREIAILQRKIDE 473
Cdd:cd22656  180 EIKDLQKELEKLNEEYAAKLKAkiDELKALI-ADDEAKLAAALRLIADLTAADTDLDNLLALIGP 243
 
Name Accession Description Interval E-value
CCDC93_CC pfam09762
CCDC93, coiled-coil domain; This is a coiled-coil domain found in CCDC93. Human CCDC93 is part ...
 31-206 6.31e-97

CCDC93, coiled-coil domain; This is a coiled-coil domain found in CCDC93. Human CCDC93 is part of the COMMD/CCDC22/CCDC93 (CCC) complex that interacts with the multisubunit WASH complex, which is required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. The CCC complex controls Notch activation by modulating its intracellular trafficking.


Pssm-ID: 462886  Cd Length: 173  Bit Score: 293.81  E-value: 6.31e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293   31 LELLVAAGYFRARIKGLSPFDKVVGGMTWCITTCSFDIDVDLLFQENSTIGQKIALTEKIVSVLPKMKCPHRLEPHQIQG 110
Cdd:pfam09762   1 LDLLVAAGYFRARIKSLSPFDKIVGGMTWCIDASNPDVDVDLLFQENSTIGEKIALTEKIVRALPKMKCPYALEPHQIQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293  111 LDFIHIFPVVQWLVKRAIETREEMGDYVRSYSISQFQKTHRLPEDEEFmQRKEKALKTVTDIFEVYKPQRKYKRQtgAEE 190
Cdd:pfam09762  81 LDFIVIFPVVQWLVKRVIETREERGDFLRRFAANQFSKAYQLPEDQAE-RKKERAADTVRRLRDVYAPKRRFKRV--AGI 157

                         170
                  ....*....|....*.
gi 959049293  191 LLDEESKVHATLLEYG 206
Cdd:pfam09762 158 IRDEEARVRSTLLEYG 173
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 281-555 3.41e-08

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: 56.99  E-value: 3.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293   281 GLQSDEIKQIVSEYAEKQSELSAEERPERlgaaqQHRRKVASLNKQILQKNKLLEELQAKCADLQAKCTEAKKTLTEVKS 360
Cdd:TIGR02168  228 ALLVLRLEELREELEELQEELKEAEEELE-----ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ 302

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293   361 YSEKLDKELAALETIESQADSSILQSLRALVAMNENLKSQEQEF------KAHCREEMERLQQNIESLK--AEALENGEE 432
Cdd:TIGR02168  303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLeelkeeLESLEAELEELEAELEELEsrLEELEEQLE 382

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293   433 QEPNKI--IEQQYKAEKEKLQKIRLLLARRNREIAILQRKIDEVPSRAELTQYQkrfiELYSQVSATHKETKQFFTLYNT 510
Cdd:TIGR02168  383 TLRSKVaqLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK----ELQAELEELEEELEELQEELER 458

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 959049293   511 LDDKKVYLEKEVNLLNSIYDNFHQAMASSGSREQFLRQMEQIVEG 555
Cdd:TIGR02168  459 LEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 295-473 1.28e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293 295 AEKQSELSAEERPERLGAAQQHRRKVASLNKQILQKNKLLEELQAKCADLQAKCTEAKKTLTEVKSYSEKLDKELAALET 374
Cdd:COG1196  300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293 375 IESQADSSILQSLRALVAMNENLKSQEQEFKAHcREEMERLQQNIESLKAEALENGEEQEPNKIIEQQYKAEKEKLQ--- 451
Cdd:COG1196  380 ELEELAEELLEALRAAAELAAQLEELEEAEEAL-LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEeee 458

                        170       180
                 ....*....|....*....|...
gi 959049293 452 -KIRLLLARRNREIAILQRKIDE 473
Cdd:COG1196  459 eALLELLAELLEEAALLEAALAE 481
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 282-555 1.86e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 1.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293 282 LQSDEIKQIVSEYAEKQSELSAEErperlGAAQQHRRKVASLNKQILQKNKLLEELQAKCADLQAKCTEAKKTLTEVKSY 361
Cdd:COG1196  243 ELEAELEELEAELEELEAELAELE-----AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293 362 SEKLDKELAALETIESQADSSILQSLRALVAMNENLKSQEQEFKAHCREEMERLQQNIESLKAEALENGEEQEpnkIIEQ 441
Cdd:COG1196  318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE---ALRA 394

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293 442 QYKAEKEKLQKIRLLLARRNREIAILQRKIDEvpsRAELTQYQKRFIELYSQVSATHKETKQFFTLYNTLDDKKVYLEKE 521
Cdd:COG1196  395 AAELAAQLEELEEAEEALLERLERLEEELEEL---EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471

                        250       260       270
                 ....*....|....*....|....*....|....
gi 959049293 522 VNLLNSIYDNFHQAMASSGSREQFLRQMEQIVEG 555
Cdd:COG1196  472 AALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 317-614 2.91e-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: 50.44  E-value: 2.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293   317 RRKVASLNKQIlqknkllEELQAKCADLQAKCTEAKKTLTEVKSYSEKLDKELAALEtiesqadssilqslRALVAMNEN 396
Cdd:TIGR02168  676 RREIEELEEKI-------EELEEKIAELEKALAELRKELEELEEELEQLRKELEELS--------------RQISALRKD 734

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293   397 LKSQEQefkahcreEMERLQQNIESLKAEALEngeeqepnkiIEQQYKAEKEKLQKIRLLLARRNREIAILQRKIDEVps 476
Cdd:TIGR02168  735 LARLEA--------EVEQLEERIAQLSKELTE----------LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL-- 794

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293   477 RAELTQYQKRFIELYSQVSATHKETKQFFTLYNTLDDKKVYLEKE-VNLLNSIYDNFHQAMASSGSREQFLRQMEQIVEG 555
Cdd:TIGR02168  795 KEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRlEDLEEQIEELSEDIESLAAEIEELEELIEELESE 874

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 959049293   556 IKQNrmkmEKKKQENKMRRDQLNDEYLELLEKQRLYFKTVKEFKEECRKNEMLLSKLKA 614
Cdd:TIGR02168  875 LEAL----LNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 200-493 8.39e-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: 48.90  E-value: 8.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293   200 ATLLEYGRRYGFSRQAGKTEQAEDKKAALPPGLAAAGKAEPCDEVDLQAAEELRIKTLMTGMAAMATEEGKLTASTVGQI 279
Cdd:TIGR02168  711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293   280 VGLQSDEIKQIVSEYAEKQSELSA--EERPERLGAAQQHRRKVAS-------LNKQILQKNKLLEELQAKCADLQAKCTE 350
Cdd:TIGR02168  791 IEQLKEELKALREALDELRAELTLlnEEAANLRERLESLERRIAAterrledLEEQIEELSEDIESLAAEIEELEELIEE 870

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293   351 AKKTLTEVKSYSEKLDKELAALETIESQADSSILQSLRALVAMNENLKSQEQEFKAHcREEMERLQQNIESLKAEALENG 430
Cdd:TIGR02168  871 LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL-ELRLEGLEVRIDNLQERLSEEY 949

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 959049293   431 EEQEPNkiIEQQYKAEKEKLQKIRlllarrnREIAILQRKIDEV-----PSRAELTQYQKRFIELYSQ 493
Cdd:TIGR02168  950 SLTLEE--AEALENKIEDDEEEAR-------RRLKRLENKIKELgpvnlAAIEEYEELKERYDFLTAQ 1008
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
283-497 1.84e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.70  E-value: 1.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293 283 QSDEIKQIVSEYAEKQSELSAEERperlgaAQQHRRKVASLNKQILQKNKLLEELQAKCADLQAKCTEAKKTLTEVKSYS 362
Cdd:COG3206  190 ELEEAEAALEEFRQKNGLVDLSEE------AKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSP 263

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293 363 E--KLDKELAALETIESQADSSILQSLRALVAMNENLKSQEQEFKAHCREEMERLQQNIESLKAEalengeeqepnkiiE 440
Cdd:COG3206  264 ViqQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAR--------------E 329

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 959049293 441 QQYKAEKEKLQKIRLLLARRNREIAILQRKIDEvpSRAELTQYQKRFIELYSQVSAT 497
Cdd:COG3206  330 ASLQAQLAQLEARLAELPELEAELRRLEREVEV--ARELYESLLQRLEEARLAEALT 384
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
286-479 5.76e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 5.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293  286 EIKQIVSEYAEKQSELSAEERPERLGAAQQHRRKVASLNKQILQKNKLLEELQAKCADLQAKCTEAKKTLTEVK-SYSEK 364
Cdd:COG4913   256 PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEaQIRGN 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293  365 LDKELAALETIESQADSSILQSLRALVAMNENLKSQEQEFKAHcREEMERLQQNIESLKAEAlengeEQEPNKIIEQQYK 444
Cdd:COG4913   336 GGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS-AEEFAALRAEAAALLEAL-----EEELEALEEALAE 409

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 959049293  445 AEKEkLQKIRLLLARRNREIAILQRKIDEVPSRAE 479
Cdd:COG4913   410 AEAA-LRDLRRELRELEAEIASLERRKSNIPARLL 443
PTZ00121 PTZ00121
MAEBL; Provisional
 180-479 6.20e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 6.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293  180 RKYKRQTGAEELLDEESkvhATLLEYGRRYGFSRQAGKTEQAEDKKAALPPGLAAAGKAepcDEVDLQAAEELRIKTLMT 259
Cdd:PTZ00121 1182 RKAEEVRKAEELRKAED---ARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKK---DAEEAKKAEEERNNEEIR 1255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293  260 GMAAMATEEGKLTASTVGQIVGLQSDEIKQivSEYAEKQSELSAEERperlgaaqqhRRKVASLNKQILQKNKLlEELQA 339
Cdd:PTZ00121 1256 KFEEARMAHFARRQAAIKAEEARKADELKK--AEEKKKADEAKKAEE----------KKKADEAKKKAEEAKKA-DEAKK 1322

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293  340 KCADLQAKCTEAKKTLTEVKSYSEKLDKELAA----LETIESQADSSILQSLRALVAMNENLKSQEQEFKA-HCREEMER 414
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAaadeAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAdEAKKKAEE 1402

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 959049293  415 LQQNIESLKAEALENGEEQEPNKIIEQQYKAEKEKLQKIRLLLARRNREIAILQRKIDEVPSRAE 479
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE 1467
COG5022 COG5022
Myosin heavy chain [General function prediction only];
252-550 1.57e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 45.07  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293  252 LRIKTLMTgmaamATEEGKLTASTVGQIVGLQ-SDEIKQIVSEYAEKQSELSAEERPERLGAAQQHRRKVASLNKQ--IL 328
Cdd:COG5022   797 IKLQPLLS-----LLGSRKEYRSYLACIIKLQkTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKEtiYL 871

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293  329 QKNKLLEELQAKCADLQakctEAKKTLTEVKSYSEKLDKELAALETIESQADSSILQSLRALVAMNENLK-----SQEQE 403
Cdd:COG5022   872 QSAQRVELAERQLQELK----IDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLnnidlEEGPS 947

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293  404 FKAHCREEMERLQQNIESLKAEALENGEEQEPNKIIEQQYKAEKEKLQKIRLLLARRNREIAILQRKIDEVPSR-AELTQ 482
Cdd:COG5022   948 IEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELpVEVAE 1027

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 959049293  483 YQKrfieLYSQVSATHKETKQFftlyNTLDDKKVYLEKEVNLLNSIYDNFHQAMASSGSREQFLRQME 550
Cdd:COG5022  1028 LQS----ASKIISSESTELSIL----KPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLE 1087
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
287-441 1.58e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.85  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293 287 IKQIVSEYAEKqseLSAEERPERLGAAQQHRRKVASLNKQILQKNKLLEELQAKCADLQAKCTEAKKTLtevksysEKLD 366
Cdd:COG2433  378 IEEALEELIEK---ELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERI-------ERLE 447

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 959049293 367 KElaaLETIESQADSSILQS--LRALVAMNENLKSQ-EQEfkahcREEMERLQQNIESLK-AEALENGEEQEPNKIIEQ 441
Cdd:COG2433  448 RE---LSEARSEERREIRKDreISRLDREIERLERElEEE-----RERIEELKRKLERLKeLWKLEHSGELVPVKVVEK 518
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 312-496 3.62e-04

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: 43.21  E-value: 3.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293 312 AAQQHRRKVASLNKQILQKNKLLEELQAK-------CADLQAKCTEAKKTLTEVKSYSEKLDKELAALETIESQADSSIL 384
Cdd:COG4942   21 AAAEAEAELEQLQQEIAELEKELAALKKEekallkqLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293 385 -------QSLRALVAMNEN-----LKSQE------------QEFKAHCREEMERLQQNIESLKAEALENGEEQEPNKIIE 440
Cdd:COG4942  101 aqkeelaELLRALYRLGRQpplalLLSPEdfldavrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 959049293 441 QQYKAEKEKLQKirlLLARRNREIAILQRKIDEVPSR-AELTQYQKRFIELYSQVSA 496
Cdd:COG4942  181 AELEEERAALEA---LKAERQKLLARLEKELAELAAElAELQQEAEELEALIARLEA 234
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
283-458 7.80e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 7.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293 283 QSDEIKQIVSEYAEKQSEL-SAEERPERLGAAQQHRRKVASLNKQILQKNKLLEELQAKCADLQAKCTEAKKTLTEVKSY 361
Cdd:COG4717   79 ELKEAEEKEEEYAELQEELeELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEEL 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293 362 SEKLDKELAALETIESQADSSILQSLRALVAMNENLKSQEQEFKAHcREEMERLQQNIESLKAEaLENGEEQEPNKIIEQ 441
Cdd:COG4717  159 RELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEEL-QQRLAELEEELEEAQEE-LEELEEELEQLENEL 236

                        170
                 ....*....|....*..
gi 959049293 442 QYKAEKEKLQKIRLLLA 458
Cdd:COG4717  237 EAAALEERLKEARLLLL 253
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
163-579 1.38e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293 163 EKALKTVTDIFEVYKPQRKYKRQT--GAEELLDEeskvhatlleygrrYGFSRQAGKTEQAEDKKAALPPGLAAAGKAEP 240
Cdd:PRK02224 212 ESELAELDEEIERYEEQREQARETrdEADEVLEE--------------HEERREELETLEAEIEDLRETIAETEREREEL 277

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293 241 CDEVDLQAAEELRIKTLMTGMAAMATEEGkltastvgqivgLQSDEIKQIVSEYAEKQSELSAEERPERLgAAQQHRRKV 320
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGLDD------------ADAEAVEARREELEDRDEELRDRLEECRV-AAQAHNEEA 344

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293 321 ASLNKQILQKNKLLEELQAKCADLQAKCTEAKKTLTEVKSYSEKLDKELAALEtiESQADSSI----LQSLRALVAMN-E 395
Cdd:PRK02224 345 ESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELR--ERFGDAPVdlgnAEDFLEELREErD 422

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293 396 NLKSQEQEFKAHCREEMERLQQNIESLKA-EALENGEEQEPNKIIEQQYKAEkEKLQKIRLLLARRNREIAILQRKIDEV 474
Cdd:PRK02224 423 ELREREAELEATLRTARERVEEAEALLEAgKCPECGQPVEGSPHVETIEEDR-ERVEELEAELEDLEEEVEEVEERLERA 501

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293 475 PSRAELtqyQKRFIELYSQVSathketkqffTLYNTLDDKKVYLEKEVNLLNSIYDNFHQAMASSGSREQFLRQMEQIVE 554
Cdd:PRK02224 502 EDLVEA---EDRIERLEERRE----------DLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAE 568

                        410       420
                 ....*....|....*....|....*
gi 959049293 555 GIKQNRMKMEKKKQENKMRRDQLND 579
Cdd:PRK02224 569 EAREEVAELNSKLAELKERIESLER 593
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 280-617 1.53e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.59  E-value: 1.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293   280 VGLQSDEIKQIVSEYAEKQSELSAE-ERPERLGAAQQHRRKVAsLNKQILQKNKLLEELQAKCADLQakctEAKKTLTEV 358
Cdd:TIGR02169  182 VEENIERLDLIIDEKRQQLERLRRErEKAERYQALLKEKREYE-GYELLKEKEALERQKEAIERQLA----SLEEELEKL 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293   359 KSYSEKLDKELAALEtiesqadssilqslRALVAMNENLKSQEQEFKAHCREEMERLQQNIESLKAEALENGEEQEPNKI 438
Cdd:TIGR02169  257 TEEISELEKRLEEIE--------------QLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEE 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293   439 IEQQYKAEKEKLQKIRLLLARRNREIAILQRKI-DEVPSRAEltQYQKRFIELySQVSATHKETKQfftlynTLDDKKVY 517
Cdd:TIGR02169  323 RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLtEEYAELKE--ELEDLRAEL-EEVDKEFAETRD------ELKDYREK 393

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293   518 LEKEVNLLNSIYDNFHQAMASSGSREQFLRQMEQIVEGIKQN-----------RMKMEKKKQENKMRRDQLNDEYLELLE 586
Cdd:TIGR02169  394 LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKineleeekedkALEIKKQEWKLEQLAADLSKYEQELYD 473

                          330       340       350
                   ....*....|....*....|....*....|.
gi 959049293   587 KQRLYFKTVKEFKEECRKNEMLLSKLKASSS 617
Cdd:TIGR02169  474 LKEEYDRVEKELSKLQRELAEAEAQARASEE 504
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 409-600 1.58e-03

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: 41.29  E-value: 1.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293 409 REEMERLQQNIESLKAEALENGEEQepnKIIEQQYKAEKEKLQKIRLLLARRNREIAILQRKIDEVpsRAELTQYQKRFI 488
Cdd:COG4942   26 EAELEQLQQEIAELEKELAALKKEE---KALLKQLAALERRIAALARRIRALEQELAALEAELAEL--EKEIAELRAELE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293 489 ELYSQVSathketKQFFTLYNTLDDKKVYLekevnLLNSiyDNFHQAMASSGSREQFLRQMEQIVEGIKQNRMKMEKKKQ 568
Cdd:COG4942  101 AQKEELA------ELLRALYRLGRQPPLAL-----LLSP--EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167

                        170       180       190
                 ....*....|....*....|....*....|..
gi 959049293 569 ENKMRRDQLNDEYLELLEKQRLYFKTVKEFKE 600
Cdd:COG4942  168 ELEAERAELEALLAELEEERAALEALKAERQK 199
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 319-615 1.68e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.54  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293  319 KVASLNKQILQKNKLLEELQAKCAD---LQAKCTEAKKTLTEVKSYSEKLDKELAALETIESQADSSILQSLRALVAMNE 395
Cdd:TIGR04523 188 NIDKIKNKLLKLELLLSNLKKKIQKnksLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKK 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293  396 NLKSQEQEFKAHCR--EEMERLQQNIESlKAEALENGEEQEPNKIIEQQYKAEKEKLQKIRLLLARRNREIAILQRKIDE 473
Cdd:TIGR04523 268 QLSEKQKELEQNNKkiKELEKQLNQLKS-EISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293  474 VpsRAELTQYQKRFIELYSQVSATHKETKQFFTLYNTLDDKKVYLEKEVNLLNSIYDNfhqamassgsREQFLRQMEQIV 553
Cdd:TIGR04523 347 L--KKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQN----------QEKLNQQKDEQI 414

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 959049293  554 EGIKQNRMKMEKKKQENKMRRDQLNDEYLELLEKQRLYFKTVKEFKEECRKNEMLLSKLKAS 615
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRS 476
PTZ00121 PTZ00121
MAEBL; Provisional
 180-448 2.34e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293  180 RKYKRQTGAEEL--LDEESKVHATLLEYGRRYGFSRQAGKTEQAEDKKAALPPGLAAAGKAEPCDEvdLQAAEELRIKTL 257
Cdd:PTZ00121 1546 KKADELKKAEELkkAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEE--AKKAEEAKIKAE 1623

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293  258 MTGMA----AMATEEGKLTASTVGQIVGLQSDEIKQIVSEYAEKQSELSAEERPERLGAAQQHRRKVASLNKQILQKNKL 333
Cdd:PTZ00121 1624 ELKKAeeekKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK 1703

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293  334 LEELQAKCADLQAKCTEAKKTLTEVKSYSEKLDKElaaLETIESQAdssilqslralvamnENLKSQEQEFK--AHCREE 411
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE---AEEDKKKA---------------EEAKKDEEEKKkiAHLKKE 1765

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 959049293  412 MERLQQNIESLKAEALENGEEQEPNKIIEQQYKAEKE 448
Cdd:PTZ00121 1766 EEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKD 1802
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 294-497 2.70e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 2.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293 294 YAEKQSELSAEERPERLGAAQQHRRKVASLNKQILQKNKLLEELQAKCADLQAKCTEAKKTLTEVKSYSEKLDKELAA-- 371
Cdd:COG3883   13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEra 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293 372 ------------LETI-ESQADSSILQSLRALVAMNENLKSQEQEFKAHcREEMERLQQNIESLKAEALENGEEQEPNKI 438
Cdd:COG3883   93 ralyrsggsvsyLDVLlGSESFSDFLDRLSALSKIADADADLLEELKAD-KAELEAKKAELEAKLAELEALKAELEAAKA 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 959049293 439 IEQQYKAEKEKL-----QKIRLLLARRNREIAILQRKIDEVPSRAELTQYQKRFIELYSQVSAT 497
Cdd:COG3883  172 ELEAQQAEQEALlaqlsAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 331-473 3.96e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 39.66  E-value: 3.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293 331 NKLLEELQAKCADLQAKCTEAKKTLTEvksYSEKLDKELAALETIESqadssilqslralvAMNENLKSQEQefkAHCRE 410
Cdd:cd22656  120 KALLDDLLKEAKKYQDKAAKVVDKLTD---FENQTEKDQTALETLEK--------------ALKDLLTDEGG---AIARK 179

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 959049293 411 EMERLQQNIESLKAEALENGEE--QEPNKIIeQQYKAEKEKLQKIRLLLARRNREIAILQRKIDE 473
Cdd:cd22656  180 EIKDLQKELEKLNEEYAAKLKAkiDELKALI-ADDEAKLAAALRLIADLTAADTDLDNLLALIGP 243
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 286-478 4.02e-03

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: 39.75  E-value: 4.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293 286 EIKQIVSEYAEKQSELSAEERPER--LGAAQQHRRKVASLNKQILQKNKLLEELQAKCADLQAKCTEAKKTLTEVKsysE 363
Cdd:COG4942   28 ELEQLQQEIAELEKELAALKKEEKalLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK---E 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293 364 KLDKELAALETIESQAD-------SSILQSLRALVAM---NENLKSQEQEFKAHcREEMERLQQNIESLKAE--ALENGE 431
Cdd:COG4942  105 ELAELLRALYRLGRQPPlalllspEDFLDAVRRLQYLkylAPARREQAEELRAD-LAELAALRAELEAERAEleALLAEL 183

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 959049293 432 EQEPNKIIEQQ----------------YKAEKEKLQKIRlllARRNREIAILQRKIDEVPSRA 478
Cdd:COG4942  184 EEERAALEALKaerqkllarlekelaeLAAELAELQQEA---EELEALIARLEAEAAAAAERT 243
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 286-503 4.99e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 39.94  E-value: 4.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293  286 EIKQIVSEYAEKQSELSAEErperlGAAQQHRRKVASLNKQILQKNKLL--------EELQAKCADLQAKCTEAKktltE 357
Cdd:COG3096   837 ELAALRQRRSELERELAQHR-----AQEQQLRQQLDQLKEQLQLLNKLLpqanlladETLADRLEELREELDAAQ----E 907

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293  358 VKSYSEKLDKELAALETiesqadssILQSLRALVAMNENLKSQEQEFKahcrEEMERLQQNIESLkAEALEN----GEEQ 433
Cdd:COG3096   908 AQAFIQQHGKALAQLEP--------LVAVLQSDPEQFEQLQADYLQAK----EQQRRLKQQIFAL-SEVVQRrphfSYED 974

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 959049293  434 EPNKIIEQQykAEKEKLQKiRLLLARRNREIAILQRKidevPSRAELTQYQKRFIELYSQVSA---THKETKQ 503
Cdd:COG3096   975 AVGLLGENS--DLNEKLRA-RLEQAEEARREAREQLR----QAQAQYSQYNQVLASLKSSRDAkqqTLQELEQ 1040
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 331-503 5.59e-03

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: 39.36  E-value: 5.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293 331 NKLLEELQAKCADLQAKCTEAKKTLTEVKSYSEKLDKELAALETIESQADSSILQSLRALVAMNENLKSQEQEfKAHCRE 410
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE-IAELRA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293 411 EMERLQQNIESLKAEALENGEEQEPNKIIEQQYKAEKEK-LQKIRLLLARRNREIAILQRKIDEVPS-RAELTQYQKRFI 488
Cdd:COG4942   98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRrLQYLKYLAPARREQAEELRADLAELAAlRAELEAERAELE 177

                        170
                 ....*....|....*
gi 959049293 489 ELYSQVSATHKETKQ 503
Cdd:COG4942  178 ALLAELEEERAALEA 192
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
330-614 8.69e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 8.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293 330 KNKLLEELQAKCADLQAKCTEAKKTLTEVKSYSEKLDKELAALETiesqadssilqsLRALVAMNENLKSQEQEFKAHCR 409
Cdd:PRK03918 450 RKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESE------------LIKLKELAEQLKELEEKLKKYNL 517

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293 410 EEMERLQQNIESLKAEALENGEEQ-------EPNKIIEQQYKAEKEKLQKIRLLLARRNREIAILQRK-IDEVPSR-AEL 480
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLIKLKGEIkslkkelEKLEELKKKLAELEKKLDELEEELAELLKELEELGFEsVEELEERlKEL 597

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959049293 481 TQYQKRFIELYSQVSATHKETKQFFTLYNTLDDKKVYLEKEVNLLNSIYDNFHQaMASSGSREQFLRQMEQIVEGIKQNR 560
Cdd:PRK03918 598 EPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE-LEKKYSEEEYEELREEYLELSRELA 676

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 959049293 561 MKMEKKKQENKMRrdqlnDEYLELLEKQRLYFKTVKEFKEECRKNEMLLSKLKA 614
Cdd:PRK03918 677 GLRAELEELEKRR-----EEIKKTLEKLKEELEEREKAKKELEKLEKALERVEE 725
 
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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