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Conserved domains on  [gi|1720412933|ref|XP_030110209|]
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transforming acidic coiled-coil-containing protein 3 isoform X3 [Mus musculus]

Protein Classification

transforming acidic coiled-coil-containing protein( domain architecture ID 12059788)

transforming acidic coiled-coil (TACC)-containing protein similar to human TACC1 that is involved in transcription regulation induced by nuclear receptors, including in T3 thyroid hormone and all-trans retinoic acid pathways

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 444-626 2.65e-76

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


:

Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 241.89  E-value: 2.65e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 444 YSQKDLDAVVNVMQQEN-------LELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIaedKIQKVLKER 516
Cdd:pfam05010   1 YSQKDMDAALEKARNEIeekeleiNELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHA---EIQKVLEEK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 517 DQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSK 596
Cdd:pfam05010  78 DQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSK 157

                         170       180       190
                  ....*....|....*....|....*....|
gi 1720412933 597 AQAEVLALQASLRKAQMQNHSLEMTLEQKV 626
Cdd:pfam05010 158 AKAETAALQASLRKEQMKVQSLERQLEQKT 187
rne super family cl35953
ribonuclease E; Reviewed
 160-310 6.31e-04

ribonuclease E; Reviewed


The actual alignment was detected with superfamily member PRK10811:

Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 43.10  E-value: 6.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933  160 VTPPIEPVLEPSHQGLEPVLESELVTPPVEPVLEPSHQE----------LEPVLESELVTPPIEPVLEPSHQGLEPVLDS 229
Cdd:PRK10811   847 VVRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSApvveavaevvEEPVVVAEPQPEEVVVVETTHPEVIAAPVTE 926

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933  230 E--LVTPPIEPVLEPSHQGLEPVLESELVTPPIEPVLEPSHqglEPVLDSELVTPPIEPVLEPSHQglePVLDSELVTPP 307
Cdd:PRK10811   927 QpqVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAE---VVVAEPEVVAQPAAPVVAEVAA---EVETVTAVEPE 1000


                   ...
gi 1720412933  308 IEP 310
Cdd:PRK10811  1001 VAP 1003
PRK10263 super family cl35903
DNA translocase FtsK; Provisional
 23-274 3.16e-03

DNA translocase FtsK; Provisional


The actual alignment was detected with superfamily member PRK10263:

Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.84  E-value: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933   23 PKLCGVAAPICNPSTgkaDWR-IPGAPWPD-CLAELKENVPPQSQAKATNVTFQTPPRDPqtHRILSPNMTNKREAPFGL 100
Cdd:PRK10263   344 PPVASVDVPPAQPTV---AWQpVPGPQTGEpVIAPAPEGYPQQSQYAQPAVQYNEPLQQP--VQPQQPYYAPAAEQPAQQ 418

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933  101 QNDHCVFLQKENQRPLAPVDDAPVVQMAAEILRAEGELQEgiltssslsastslldselvtppiEPVLEPSHQGLEPVLE 180
Cdd:PRK10263   419 PYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAP------------------------QSTYQTEQTYQQPAAQ 474

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933  181 SELVTPPvEPVLEPSHQELEPVLESelvTPPIEPVLEPSHQGLEP-VLDSELVTPPIEPVLEPshqglepVLESELVTPP 259
Cdd:PRK10263   475 EPLYQQP-QPVEQQPVVEPEPVVEE---TKPARPPLYYFEEVEEKrAREREQLAAWYQPIPEP-------VKEPEPIKSS 543

                          250
                   ....*....|....*
gi 1720412933  260 IEPVLEPSHQGLEPV 274
Cdd:PRK10263   544 LKAPSVAAVPPVEAA 558
 
Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 444-626 2.65e-76

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 241.89  E-value: 2.65e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 444 YSQKDLDAVVNVMQQEN-------LELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIaedKIQKVLKER 516
Cdd:pfam05010   1 YSQKDMDAALEKARNEIeekeleiNELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHA---EIQKVLEEK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 517 DQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSK 596
Cdd:pfam05010  78 DQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSK 157

                         170       180       190
                  ....*....|....*....|....*....|
gi 1720412933 597 AQAEVLALQASLRKAQMQNHSLEMTLEQKV 626
Cdd:pfam05010 158 AKAETAALQASLRKEQMKVQSLERQLEQKT 187
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 426-625 4.18e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 52.52  E-value: 4.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 426 VLEPRGLLPAEPIVDVLKYSQKDLDAVVNVMQQENLELKSKYEDLNTKYLEMGKSVDEFEkiayKSLEEAEKQRELKEIA 505
Cdd:COG3883     5 ALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ----AEIDKLQAEIAEAEAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 506 EDKIQKVLKER-----------DQLNADLNSmeKSFSDLFKRF-------EKRKEVIEGYQKNEESLKKYVGEcivkIEK 567
Cdd:COG3883    81 IEERREELGERaralyrsggsvSYLDVLLGS--ESFSDFLDRLsalskiaDADADLLEELKADKAELEAKKAE----LEA 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720412933 568 EGQRYQALKIHAEEKLRLANEEIAQvhskAQAEVLALQASLRKAQMQNHSLEMTLEQK 625
Cdd:COG3883   155 KLAELEALKAELEAAKAELEAQQAE----QEALLAQLSAEEAAAEAQLAELEAELAAA 208
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 445-627 1.37e-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: 48.51  E-value: 1.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933  445 SQKDLDA-VVNVMQQENLELKSKYEDLNtkylemgKSVDEFEKIAYKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADL 523
Cdd:TIGR02168  330 SKLDELAeELAELEEKLEELKEELESLE-------AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933  524 NSMEKSFSDLFKRFEKRKEVIEGYQKN-EESLKKYVGECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQvhskAQAEVL 602
Cdd:TIGR02168  403 ERLEARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE----AEQALD 478

                          170       180
                   ....*....|....*....|....*
gi 1720412933  603 ALQASLRKAQMQNHSLEMTLEQKVG 627
Cdd:TIGR02168  479 AAERELAQLQARLDSLERLQENLEG 503
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
462-612 3.49e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.98  E-value: 3.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 462 ELKSKYEDLN------TKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEiaedKIQKVLKERDQLNADLNSMEKSFSDLFK 535
Cdd:PRK03918  277 ELEEKVKELKelkekaEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN----GIEERIKELEEKEERLEELKKKLKELEK 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 536 RFEKRKEVIEGYQK------NEESLKKYV-GECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSKAQAEVLALQAsL 608
Cdd:PRK03918  353 RLEELEERHELYEEakakkeELERLKKRLtGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE-L 431


                  ....
gi 1720412933 609 RKAQ 612
Cdd:PRK03918  432 KKAK 435
rne PRK10811
ribonuclease E; Reviewed
 160-310 6.31e-04

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 43.10  E-value: 6.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933  160 VTPPIEPVLEPSHQGLEPVLESELVTPPVEPVLEPSHQE----------LEPVLESELVTPPIEPVLEPSHQGLEPVLDS 229
Cdd:PRK10811   847 VVRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSApvveavaevvEEPVVVAEPQPEEVVVVETTHPEVIAAPVTE 926

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933  230 E--LVTPPIEPVLEPSHQGLEPVLESELVTPPIEPVLEPSHqglEPVLDSELVTPPIEPVLEPSHQglePVLDSELVTPP 307
Cdd:PRK10811   927 QpqVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAE---VVVAEPEVVAQPAAPVVAEVAA---EVETVTAVEPE 1000


                   ...
gi 1720412933  308 IEP 310
Cdd:PRK10811  1001 VAP 1003
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 23-274 3.16e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.84  E-value: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933   23 PKLCGVAAPICNPSTgkaDWR-IPGAPWPD-CLAELKENVPPQSQAKATNVTFQTPPRDPqtHRILSPNMTNKREAPFGL 100
Cdd:PRK10263   344 PPVASVDVPPAQPTV---AWQpVPGPQTGEpVIAPAPEGYPQQSQYAQPAVQYNEPLQQP--VQPQQPYYAPAAEQPAQQ 418

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933  101 QNDHCVFLQKENQRPLAPVDDAPVVQMAAEILRAEGELQEgiltssslsastslldselvtppiEPVLEPSHQGLEPVLE 180
Cdd:PRK10263   419 PYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAP------------------------QSTYQTEQTYQQPAAQ 474

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933  181 SELVTPPvEPVLEPSHQELEPVLESelvTPPIEPVLEPSHQGLEP-VLDSELVTPPIEPVLEPshqglepVLESELVTPP 259
Cdd:PRK10263   475 EPLYQQP-QPVEQQPVVEPEPVVEE---TKPARPPLYYFEEVEEKrAREREQLAAWYQPIPEP-------VKEPEPIKSS 543

                          250
                   ....*....|....*
gi 1720412933  260 IEPVLEPSHQGLEPV 274
Cdd:PRK10263   544 LKAPSVAAVPPVEAA 558
 
Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 444-626 2.65e-76

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 241.89  E-value: 2.65e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 444 YSQKDLDAVVNVMQQEN-------LELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIaedKIQKVLKER 516
Cdd:pfam05010   1 YSQKDMDAALEKARNEIeekeleiNELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHA---EIQKVLEEK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 517 DQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSK 596
Cdd:pfam05010  78 DQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSK 157

                         170       180       190
                  ....*....|....*....|....*....|
gi 1720412933 597 AQAEVLALQASLRKAQMQNHSLEMTLEQKV 626
Cdd:pfam05010 158 AKAETAALQASLRKEQMKVQSLERQLEQKT 187
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 426-625 4.18e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 52.52  E-value: 4.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 426 VLEPRGLLPAEPIVDVLKYSQKDLDAVVNVMQQENLELKSKYEDLNTKYLEMGKSVDEFEkiayKSLEEAEKQRELKEIA 505
Cdd:COG3883     5 ALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ----AEIDKLQAEIAEAEAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 506 EDKIQKVLKER-----------DQLNADLNSmeKSFSDLFKRF-------EKRKEVIEGYQKNEESLKKYVGEcivkIEK 567
Cdd:COG3883    81 IEERREELGERaralyrsggsvSYLDVLLGS--ESFSDFLDRLsalskiaDADADLLEELKADKAELEAKKAE----LEA 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720412933 568 EGQRYQALKIHAEEKLRLANEEIAQvhskAQAEVLALQASLRKAQMQNHSLEMTLEQK 625
Cdd:COG3883   155 KLAELEALKAELEAAKAELEAQQAE----QEALLAQLSAEEAAAEAQLAELEAELAAA 208
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 445-627 1.37e-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: 48.51  E-value: 1.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933  445 SQKDLDA-VVNVMQQENLELKSKYEDLNtkylemgKSVDEFEKIAYKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADL 523
Cdd:TIGR02168  330 SKLDELAeELAELEEKLEELKEELESLE-------AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933  524 NSMEKSFSDLFKRFEKRKEVIEGYQKN-EESLKKYVGECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQvhskAQAEVL 602
Cdd:TIGR02168  403 ERLEARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE----AEQALD 478

                          170       180
                   ....*....|....*....|....*
gi 1720412933  603 ALQASLRKAQMQNHSLEMTLEQKVG 627
Cdd:TIGR02168  479 AAERELAQLQARLDSLERLQENLEG 503
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 442-615 3.01e-05

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: 47.37  E-value: 3.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933  442 LKYSQKDLDAVVNVMQQENLELKSKYEDLNTKYLEMG--KSVDEFEKI---------AYKSLEEAEKQREL-KEIAEDKI 509
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipEIQAELSKLeeevsrieaRLREIEQKLNRLTLeKEYLEKEI 835

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933  510 QKVLKERDQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGEcivkIEKEGQRyqalkihAEEKLRLANEE 589
Cdd:TIGR02169  836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD----LKKERDE-------LEAQLRELERK 904

                          170       180
                   ....*....|....*....|....*.
gi 1720412933  590 IAQVhsKAQAEVLALQASLRKAQMQN 615
Cdd:TIGR02169  905 IEEL--EAQIEKKRKRLSELKAKLEA 928
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
462-612 3.49e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.98  E-value: 3.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 462 ELKSKYEDLN------TKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEiaedKIQKVLKERDQLNADLNSMEKSFSDLFK 535
Cdd:PRK03918  277 ELEEKVKELKelkekaEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN----GIEERIKELEEKEERLEELKKKLKELEK 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 536 RFEKRKEVIEGYQK------NEESLKKYV-GECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSKAQAEVLALQAsL 608
Cdd:PRK03918  353 RLEELEERHELYEEakakkeELERLKKRLtGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE-L 431


                  ....
gi 1720412933 609 RKAQ 612
Cdd:PRK03918  432 KKAK 435
PTZ00121 PTZ00121
MAEBL; Provisional
 462-612 3.53e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 3.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933  462 ELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIAEDKiqkvlKERDQLNADlnSMEKSFSDLFKRFEKRK 541
Cdd:PTZ00121  1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK-----AEAAEKKKE--EAKKKADAAKKKAEEKK 1391

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720412933  542 EVIEGYQKNEESLKKyvGECIVKIEKEGQRYQALKIHAEEKlRLANEEIAQVHSKAQAEVLALQA-SLRKAQ 612
Cdd:PTZ00121  1392 KADEAKKKAEEDKKK--ADELKKAAAAKKKADEAKKKAEEK-KKADEAKKKAEEAKKADEAKKKAeEAKKAE 1460
PTZ00121 PTZ00121
MAEBL; Provisional
 462-612 7.22e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 7.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933  462 ELKSKYEDLNtKYLEMGKSVDEFEKIA--YKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSMEKSFSD-LFKRFE 538
Cdd:PTZ00121  1402 EDKKKADELK-KAAAAKKKADEAKKKAeeKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADeAKKKAE 1480

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720412933  539 KRKEVIEGYQKNEESLKKyvGECIVKIEKEGQRYQALKiHAEEKLRLanEEIAQVHSKAQAEVLALQASLRKAQ 612
Cdd:PTZ00121  1481 EAKKADEAKKKAEEAKKK--ADEAKKAAEAKKKADEAK-KAEEAKKA--DEAKKAEEAKKADEAKKAEEKKKAD 1549
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 441-625 8.45e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 8.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 441 VLKY------SQKDLDAVvnvmqQENL--------ELKSKYEDLNT------KYLEMGKSVDEFEKIAY-KSLEEAEKQR 499
Cdd:COG1196   167 ISKYkerkeeAERKLEAT-----EENLerledilgELERQLEPLERqaekaeRYRELKEELKELEAELLlLKLRELEAEL 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 500 ELkeiAEDKIQKVLKERDQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALKiHA 579
Cdd:COG1196   242 EE---LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE-ER 317

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1720412933 580 EEKLRLANEEIAQVHSKAQAEVLALQASLRKAQMQNHSLEMTLEQK 625
Cdd:COG1196   318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 448-624 1.57e-04

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: 45.05  E-value: 1.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933  448 DLDAVVNVMQQENLELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIAED-------KIQKVLKERDQLN 520
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAeltllneEAANLRERLESLE 830

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933  521 ADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLkkyvGECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSKAQA- 599
Cdd:TIGR02168  831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEEL----EELIEELESELEALLNERASLEEALALLRSELEELSEELREl 906

                          170       180
                   ....*....|....*....|....*..
gi 1720412933  600 --EVLALQASLRKAQMQNHSLEMTLEQ 624
Cdd:TIGR02168  907 esKRSELRRELEELREKLAQLELRLEG 933
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 481-625 3.40e-04

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: 43.90  E-value: 3.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933  481 VDEFEKIAYKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSMEKsfsdlFKRFEKRKEVIEGY------QKNEESL 554
Cdd:TIGR02169  165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAER-----YQALLKEKREYEGYellkekEALERQK 239

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720412933  555 KKYVGEcIVKIEKEGQ----RYQALKIHAEEKLRLANEEIAQVHSKAQAEVLALQASLRKAQMQNHSLEMTLEQK 625
Cdd:TIGR02169  240 EAIERQ-LASLEEELEklteEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEK 313
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
468-611 5.57e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 5.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 468 EDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSMEKSFSDL---FKRFEKRKEVI 544
Cdd:COG4717    49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELreeLEKLEKLLQLL 128

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412933 545 EGYQKNEEsLKKYVGECIVKIEKEGQRYQALKiHAEEKLRLANEEIAQVHSKAQAEVLALQASLRKA 611
Cdd:COG4717   129 PLYQELEA-LEAELAELPERLEELEERLEELR-ELEEELEELEAELAELQEELEELLEQLSLATEEE 193
rne PRK10811
ribonuclease E; Reviewed
 160-310 6.31e-04

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 43.10  E-value: 6.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933  160 VTPPIEPVLEPSHQGLEPVLESELVTPPVEPVLEPSHQE----------LEPVLESELVTPPIEPVLEPSHQGLEPVLDS 229
Cdd:PRK10811   847 VVRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSApvveavaevvEEPVVVAEPQPEEVVVVETTHPEVIAAPVTE 926

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933  230 E--LVTPPIEPVLEPSHQGLEPVLESELVTPPIEPVLEPSHqglEPVLDSELVTPPIEPVLEPSHQglePVLDSELVTPP 307
Cdd:PRK10811   927 QpqVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAE---VVVAEPEVVAQPAAPVVAEVAA---EVETVTAVEPE 1000


                   ...
gi 1720412933  308 IEP 310
Cdd:PRK10811  1001 VAP 1003
PRK12704 PRK12704
phosphodiesterase; Provisional
 479-592 1.38e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 479 KSVDEFEKIAYKSLEEAEKqrELKEIAEDKI----QKVLKERDQLNADLNSMEKSFSDLFKR--------------FEKR 540
Cdd:PRK12704   31 AKIKEAEEEAKRILEEAKK--EAEAIKKEALleakEEIHKLRNEFEKELRERRNELQKLEKRllqkeenldrklelLEKR 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720412933 541 KEVIEGYQKNEESLKKYVGECIVKIEkegqryqalKIHAEEKLRLanEEIAQ 592
Cdd:PRK12704  109 EEELEKKEKELEQKQQELEKKEEELE---------ELIEEQLQEL--ERISG 149
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 457-625 1.47e-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: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 457 QQENLELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSMEKSFSDLFKR 536
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 537 FEKRKEVIEG-----YQKNEESLKKYV--GECIVKIEKEGQRYQALKIHAE---EKLRLANEEIAQVHSKAQAEVLALQA 606
Cdd:COG4942    99 LEAQKEELAEllralYRLGRQPPLALLlsPEDFLDAVRRLQYLKYLAPARReqaEELRADLAELAALRAELEAERAELEA 178

                         170
                  ....*....|....*....
gi 1720412933 607 SLRKAQMQNHSLEMTLEQK 625
Cdd:COG4942   179 LLAELEEERAALEALKAER 197
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 486-601 1.74e-03

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 39.82  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 486 KIAYKSLEEAEKQRELKEIAEDKIQKvlkERDQLNADLNSMEKSFSDLFKRFEKRKEVIegyqkNEESLKKYVGEcIVKI 565
Cdd:COG2825    25 KIGVVDVQRILQESPEGKAAQKKLEK---EFKKRQAELQKLEKELQALQEKLQKEAATL-----SEEERQKKERE-LQKK 95

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1720412933 566 EKEGQRYQALkihAEEKLRLA-NEEIAQVHSKAQAEV 601
Cdd:COG2825    96 QQELQRKQQE---AQQDLQKRqQELLQPILEKIQKAI 129
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 438-630 1.79e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 41.48  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 438 IVDVLKYSQKDLDAVVNVM---QQENLELKSKYEDLNTKYLEMGKSVDEFEKIAYKSL-EEAEKQRELKEIAEDKIQKVL 513
Cdd:COG5185   213 GNLGSESTLLEKAKEIINIeeaLKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLgENAESSKRLNENANNLIKQFE 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 514 KERDQL--NADLNSMEKSFSDL---FKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALK-----IHAEEKL 583
Cdd:COG5185   293 NTKEKIaeYTKSIDIKKATESLeeqLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKeeienIVGEVEL 372

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1720412933 584 RLANEEIAQVHSKAQAEVLALQASLRKAQMQNHSLEMTLEQKVGHRD 630
Cdd:COG5185   373 SKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAAD 419
DUF4407 pfam14362
Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins ...
 431-609 2.02e-03

Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins in this family are typically between 366 and 597 amino acids in length. There is a single completely conserved residue R that may be functionally important.


Pssm-ID: 464151 [Multi-domain]  Cd Length: 295  Bit Score: 40.70  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 431 GLLPAEPIVdvLKYSQKDLDAVVNVMQQEnlelkskyedlntkylemgksvdefekiaykslEEAEKQRELKEIAEDKIQ 510
Cdd:pfam14362  92 GVVISEPLE--LKIFEKEIDRELLEIQQE---------------------------------EADAAKAQLAAAYRARLA 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 511 KVLKERDQLNADLNSMEKSFSDLFKrfEKRKEvIEGYQKNEESLKKYVGECIVK---IEKEGQRYQALKIHAEEKLRLAN 587
Cdd:pfam14362 137 ELEAQIAALDAEIDAAEARLDALQA--EARCE-LDGTPGTGTGVPGDGPVAKTKqaqLDAAQAELAALQAQNDARLAALR 213

                         170       180
                  ....*....|....*....|..
gi 1720412933 588 EEIAQVHSKAQAEVLALQASLR 609
Cdd:pfam14362 214 AELARLTAERAAARARSQAAID 235
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 464-592 2.35e-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: 41.16  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 464 KSKYEDLNTKYLEMGKSVDEF-EKIA-------YKSLEEAEKQRELKEiAEDKIQKVLKERDQLNADLNSMEKSFSDLFK 535
Cdd:TIGR04523 320 EKKLEEIQNQISQNNKIISQLnEQISqlkkeltNSESENSEKQRELEE-KQNEIEKLKKENQSYKQEIKNLESQINDLES 398

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412933 536 RFEKRKEVIEGYQKNEESLKKYVGecivKIEKEGQRYQALKIHAEEKLRLANEEIAQ 592
Cdd:TIGR04523 399 KIQNQEKLNQQKDEQIKKLQQEKE----LLEKEIERLKETIIKNNSEIKDLTNQDSV 451
PRK01156 PRK01156
chromosome segregation protein; Provisional
 440-560 2.52e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 41.04  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 440 DVLKYSQKDLDAVVNVMQQENLELKSKYEDLNtkylEMGKSVDEFEKIayKSLEEAEKQRelkeiAEDKIQKVLKERDQL 519
Cdd:PRK01156  169 DKLKDVIDMLRAEISNIDYLEEKLKSSNLELE----NIKKQIADDEKS--HSITLKEIER-----LSIEYNNAMDDYNNL 237

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1720412933 520 NADLNSMeKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGE 560
Cdd:PRK01156  238 KSALNEL-SSLEDMKNRYESEIKTAESDLSMELEKNNYYKE 277
rne PRK10811
ribonuclease E; Reviewed
 115-292 2.88e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 40.79  E-value: 2.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933  115 PLAPVDDAPVV-QMAAEILRAEGELQEgiltssslSASTSLLDSELVTPPIEPVLEPSHqglEPVLESELVTPPVEPVlE 193
Cdd:PRK10811   846 PVVRPQDVQVEeQREAEEVQVQPVVAE--------VPVAAAVEPVVSAPVVEAVAEVVE---EPVVVAEPQPEEVVVV-E 913

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933  194 PSHQEL--EPVLES-ELVTPPIEPVLEPSHQGLEPVLDSELVTPPIEPVLEPSHqglEPVLESELVTPPIEPVLEPSHQG 270
Cdd:PRK10811   914 TTHPEViaAPVTEQpQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAE---VVVAEPEVVAQPAAPVVAEVAAE 990

                          170       180
                   ....*....|....*....|....*
gi 1720412933  271 L--EPVLDSELVTPPI-EPVLEPSH 292
Cdd:PRK10811   991 VetVTAVEPEVAPAQVpEATVEHNH 1015
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 23-274 3.16e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.84  E-value: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933   23 PKLCGVAAPICNPSTgkaDWR-IPGAPWPD-CLAELKENVPPQSQAKATNVTFQTPPRDPqtHRILSPNMTNKREAPFGL 100
Cdd:PRK10263   344 PPVASVDVPPAQPTV---AWQpVPGPQTGEpVIAPAPEGYPQQSQYAQPAVQYNEPLQQP--VQPQQPYYAPAAEQPAQQ 418

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933  101 QNDHCVFLQKENQRPLAPVDDAPVVQMAAEILRAEGELQEgiltssslsastslldselvtppiEPVLEPSHQGLEPVLE 180
Cdd:PRK10263   419 PYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAP------------------------QSTYQTEQTYQQPAAQ 474

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933  181 SELVTPPvEPVLEPSHQELEPVLESelvTPPIEPVLEPSHQGLEP-VLDSELVTPPIEPVLEPshqglepVLESELVTPP 259
Cdd:PRK10263   475 EPLYQQP-QPVEQQPVVEPEPVVEE---TKPARPPLYYFEEVEEKrAREREQLAAWYQPIPEP-------VKEPEPIKSS 543

                          250
                   ....*....|....*
gi 1720412933  260 IEPVLEPSHQGLEPV 274
Cdd:PRK10263   544 LKAPSVAAVPPVEAA 558
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 491-616 4.34e-03

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 38.89  E-value: 4.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 491 SLEEAEK--QRELKEiAEDKIQKVLKERDQLNADLNSMEKSFSDLFKRFEKRKE-VIEGYQKNEESLKKYVGECIVKIEK 567
Cdd:pfam04012  19 KAEDPEKmlEQAIRD-MQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEkAQAALTKGNEELAREALAEKKSLEK 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720412933 568 EGQRYQALKIHAE---EKLRLANEEIAQVHSKAQAEVLALQASLRKAQMQNH 616
Cdd:pfam04012  98 QAEALETQLAQQRsavEQLRKQLAALETKIQQLKAKKNLLKARLKAAKAQEA 149
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 449-603 5.94e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 39.45  E-value: 5.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 449 LDAVVNVMQQEN------LELKSKYEDLNTKYLE----MGKSVDEFEKIayksLEEAEKQR----ELKE----IAEDKIQ 510
Cdd:pfam06160 106 LEELDELLESEEknreevEELKDKYRELRKTLLAnrfsYGPAIDELEKQ----LAEIEEEFsqfeELTEsgdyLEAREVL 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 511 KVLKER-DQLNADLNSMEKSFSDLFKRFEKR-KEVIEGYQKNEEslKKY------VGECIVKIEKEGQRYQA----LKI- 577
Cdd:pfam06160 182 EKLEEEtDALEELMEDIPPLYEELKTELPDQlEELKEGYREMEE--EGYalehlnVDKEIQQLEEQLEENLAllenLELd 259

                         170       180
                  ....*....|....*....|....*.
gi 1720412933 578 HAEEKLRLANEEIAQVHSKAQAEVLA 603
Cdd:pfam06160 260 EAEEALEEIEERIDQLYDLLEKEVDA 285
PTZ00121 PTZ00121
MAEBL; Provisional
 462-628 7.74e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 7.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933  462 ELKSKYEDLNTKYLEMGKSVDEfEKIAYKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSMEKSFSDLFKRFEKRK 541
Cdd:PTZ00121  1596 EVMKLYEEEKKMKAEEAKKAEE-AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933  542 EVIEGYQKNEESLKKyVGECIVKIEKEGQRYQAL-KIHAEEKLRLANEEIAQVHSKAQAEVLALQASLRKAQMQNHSLEM 620
Cdd:PTZ00121  1675 KKAEEAKKAEEDEKK-AAEALKKEAEEAKKAEELkKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE 1753


                   ....*...
gi 1720412933  621 TLEQKVGH 628
Cdd:PTZ00121  1754 EEKKKIAH 1761
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 446-614 9.02e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 9.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 446 QKDLDAVVNVMQQENLELKSKYEDLNTKYLEMGKSVDEFEKiayksleEAEKQRELKEIAEDKIQKVLKERDQLNADLNS 525
Cdd:COG1196   262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ-------DIARLEERRRELEERLEELEEELAELEEELEE 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 526 MEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSKAQAEVLALQ 605
Cdd:COG1196   335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414


                  ....*....
gi 1720412933 606 ASLRKAQMQ 614
Cdd:COG1196   415 RLERLEEEL 423
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 428-596 9.09e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 39.14  E-value: 9.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 428 EPRGLLPAEPIVDVLKYSQKDLDAV---VNVMQQENLELKSKYEDLNTKYLEMGK----SVDEFEKIAYKSLE------E 494
Cdd:PRK05771   74 EEKKKVSVKSLEELIKDVEEELEKIekeIKELEEEISELENEIKELEQEIERLEPwgnfDLDLSLLLGFKYVSvfvgtvP 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 495 AEKQRELKEIAEDKIQKVLKERDQLN----ADLNSMEKSFSDLFKRFEKRK----------EVIEGYQKNEESLKKYVGE 560
Cdd:PRK05771  154 EDKLEELKLESDVENVEYISTDKGYVyvvvVVLKELSDEVEEELKKLGFERleleeegtpsELIREIKEELEEIEKERES 233

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1720412933 561 CIVKIEKEGQRYQALKIHAEEKLrLANEEIAQVHSK 596
Cdd:PRK05771  234 LLEELKELAKKYLEELLALYEYL-EIELERAEALSK 268
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 442-594 9.39e-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: 39.23  E-value: 9.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 442 LKYSQKDLDAVVNVMQQENLELKSKYEDLNTKYLEmgksvdefekiayKSLEEAEKQRELKEIAEDKIQKVL-KERDQLN 520
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE-------------KESKISDLEDELNKDDFELKKENLeKEIDEKN 567

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 521 ADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKI----------EKEGQRYQALKIHAEEKLRLANEEI 590
Cdd:TIGR04523 568 KEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKIsslekelekaKKENEKLSSIIKNIKSKKNKLKQEV 647


                  ....
gi 1720412933 591 AQVH 594
Cdd:TIGR04523 648 KQIK 651
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 490-611 9.66e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 38.63  E-value: 9.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412933 490 KSLEEAEKQRELKE--IAEDKIQKVLKERDQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEK 567
Cdd:PRK09510   72 KSAKRAEEQRKKKEqqQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEA 151

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1720412933 568 EGQRYQALKIHAEEKLRLANEEIAQVHSKAQAEVLALQASLRKA 611
Cdd:PRK09510  152 EAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKA 195
 
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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