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Conserved domains on  [gi|20532344|ref|NP_620703|]
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TNFAIP3-interacting protein 2 [Mus musculus]

Protein Classification

SMC_prok_B and EABR domain-containing protein( domain architecture ID 13530685)

SMC_prok_B and EABR domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EABR pfam12180
TSG101 and ALIX binding domain of CEP55; This domain family is found in eukaryotes, and is ...
 215-248 9.21e-10

TSG101 and ALIX binding domain of CEP55; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. This domain is the active domain of CEP55. CEP55 is a protein involved in cytokinesis, specifically in abscission of the plasma membrane at the midbody. To perform this function, CEP55 complexes with ESCRT-I (by a Proline rich sequence in its TSG101 domain) and ALIX. This is the domain on CEP55 which binds to both TSG101 and ALIX. It also acts as a hinge between the N and C termini. This domain is called EABR.


:

Pssm-ID: 463486 [Multi-domain]  Cd Length: 34  Bit Score: 53.65  E-value: 9.21e-10
                          10        20        30
                  ....*....|....*....|....*....|....
gi 20532344   215 KQKVTHVEDLNAKWQRYDASRDEYVKGLHAQLKR 248
Cdd:pfam12180   1 KQQVADVLELNQQWQVYDQSREEYVRGLLARLKE 34
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 19-335 8.73e-09

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: 57.76  E-value: 8.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344     19 AALCGLYHEAGQQLQRLKDQLAARDALIASLRTRLAALEghTAPSLVDALLDQVERFREQLRRQEEgasetQLRQEVERL 98
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELS--RQISALRKDLARLEAEVEQLEERIA-----QLSKELTEL 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344     99 TERLEEKEREMQQLmSQPQHEQEKEVVLLRRSVAEKEKARAASDVLCRSLADETHQLRRTLAATAHMCQHLAKclderqc 178
Cdd:TIGR02168  760 EAEIEELEERLEEA-EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER------- 831

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    179 aQGDAGEKSPAELEQTSSDASGQ-----SVIKKLQEENRLLKQKVTHVEDLNAKWQRYDASRDEYVKGLHAQLKRrqvpl 253
Cdd:TIGR02168  832 -RIAATERRLEDLEEQIEELSEDieslaAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE----- 905

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    254 epelMKKEISRLNRQLEEKISDCAEANQELTAMRMSRDTALERV----QMLEQQILAYKDDFKserADRERAHSRIQELE 329
Cdd:TIGR02168  906 ----LESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLseeySLTLEEAEALENKIE---DDEEEARRRLKRLE 978


                   ....*.
gi 20532344    330 EKIMSL 335
Cdd:TIGR02168  979 NKIKEL 984
 
Name Accession Description Interval E-value
EABR pfam12180
TSG101 and ALIX binding domain of CEP55; This domain family is found in eukaryotes, and is ...
 215-248 9.21e-10

TSG101 and ALIX binding domain of CEP55; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. This domain is the active domain of CEP55. CEP55 is a protein involved in cytokinesis, specifically in abscission of the plasma membrane at the midbody. To perform this function, CEP55 complexes with ESCRT-I (by a Proline rich sequence in its TSG101 domain) and ALIX. This is the domain on CEP55 which binds to both TSG101 and ALIX. It also acts as a hinge between the N and C termini. This domain is called EABR.


Pssm-ID: 463486 [Multi-domain]  Cd Length: 34  Bit Score: 53.65  E-value: 9.21e-10
                          10        20        30
                  ....*....|....*....|....*....|....
gi 20532344   215 KQKVTHVEDLNAKWQRYDASRDEYVKGLHAQLKR 248
Cdd:pfam12180   1 KQQVADVLELNQQWQVYDQSREEYVRGLLARLKE 34
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 19-335 8.73e-09

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: 57.76  E-value: 8.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344     19 AALCGLYHEAGQQLQRLKDQLAARDALIASLRTRLAALEghTAPSLVDALLDQVERFREQLRRQEEgasetQLRQEVERL 98
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELS--RQISALRKDLARLEAEVEQLEERIA-----QLSKELTEL 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344     99 TERLEEKEREMQQLmSQPQHEQEKEVVLLRRSVAEKEKARAASDVLCRSLADETHQLRRTLAATAHMCQHLAKclderqc 178
Cdd:TIGR02168  760 EAEIEELEERLEEA-EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER------- 831

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    179 aQGDAGEKSPAELEQTSSDASGQ-----SVIKKLQEENRLLKQKVTHVEDLNAKWQRYDASRDEYVKGLHAQLKRrqvpl 253
Cdd:TIGR02168  832 -RIAATERRLEDLEEQIEELSEDieslaAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE----- 905

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    254 epelMKKEISRLNRQLEEKISDCAEANQELTAMRMSRDTALERV----QMLEQQILAYKDDFKserADRERAHSRIQELE 329
Cdd:TIGR02168  906 ----LESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLseeySLTLEEAEALENKIE---DDEEEARRRLKRLE 978


                   ....*.
gi 20532344    330 EKIMSL 335
Cdd:TIGR02168  979 NKIKEL 984
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 25-324 9.26e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 9.26e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344  25 YHEAGQQLQRLKDQLAARDALIASLRTRLAALEGH--TAPSLVDALLDQVERFREQLRrqEEGASETQLRQEVERLTERL 102
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAEleELRLELEELELELEEAQAEEY--ELLAELARLEQDIARLEERR 311

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344 103 EEKEREMQQLMSQpQHEQEKEVVLLRRSVAEKEKARAASDVLCRSLADETHQLRRTLAATAHmcQHLAKCLDERQCAQGD 182
Cdd:COG1196 312 RELEERLEELEEE-LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA--ELAEAEEELEELAEEL 388

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344 183 AGEKSPAELEQTSSDASGQSVIKKLQEENRLLKQKVTHVEDLNAKWQRYDASRDEYVKGLHAQLKRRQvplepelmkkEI 262
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE----------EE 458

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20532344 263 SRLNRQLEEKISDCAEANQELTAMRMSRDTALERVQMLEQQILAYKDDFKSERADRERAHSR 324
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
CC2-LZ pfam16516
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ...
 259-341 5.41e-05

Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a leucine-zipper domain associated with the CC2 coiled-coil region of NF-kappa-B essential modulator, NEMO. It plays a regulatory role, along with the very C-terminal zinc-finger; it contains a ubiquitin-binding domain (UBD) and represents one region that contributes to NEMO oligomerization. NEMO itself is an integral part of the IkappaB kinase complex and serves as a molecular switch via which the NF-kappaB signalling pathway is regulated.


Pssm-ID: 465155 [Multi-domain]  Cd Length: 100  Bit Score: 41.89  E-value: 5.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344   259 KKEISRLNRQL---EEKISDCAEANQELTAMRMSRDTALERVQMLEQQILAYKDDFKSERADRERAHSRIQELEEKIMSL 335
Cdd:pfam16516  13 KDEIDCLQAQLqaaEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYL 92


                  ....*.
gi 20532344   336 MYQVSQ 341
Cdd:pfam16516  93 QRQNQQ 98
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
49-332 6.19e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 6.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344   49 LRTRLAALEG-HTAPSLVDALLDQVERfreqLRRQEEGASETQLRQEVERLTERLEEKEREMQQLMSQpQHEQEKEVVLL 127
Cdd:PRK03918 350 LEKRLEELEErHELYEEAKAKKEELER----LKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITAR-IGELKKEIKEL 424

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344  128 RRSVAEKEKARAASDVlCRSLADETHQLRRTLAATAHMcqhlaKCLDERQCAQGDAGEKSPAELEQTSSDASGQSVIKKL 207
Cdd:PRK03918 425 KKAIEELKKAKGKCPV-CGRELTEEHRKELLEEYTAEL-----KRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL 498

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344  208 QEENRLLKQ-----KVTHVEDLNAKWQRYdasrdEYVKGLHAQLKRRQVPLEPEL-----MKKEISRLNRQLEEKISDCA 277
Cdd:PRK03918 499 KELAEQLKEleeklKKYNLEELEKKAEEY-----EKLKEKLIKLKGEIKSLKKELekleeLKKKLAELEKKLDELEEELA 573

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 20532344  278 EANQELTAMRMSRDTALE-RVQMLEQqilAYKD--DFKSERADRERAHSRIQELEEKI 332
Cdd:PRK03918 574 ELLKELEELGFESVEELEeRLKELEP---FYNEylELKDAEKELEREEKELKKLEEEL 628
 
Name Accession Description Interval E-value
EABR pfam12180
TSG101 and ALIX binding domain of CEP55; This domain family is found in eukaryotes, and is ...
 215-248 9.21e-10

TSG101 and ALIX binding domain of CEP55; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. This domain is the active domain of CEP55. CEP55 is a protein involved in cytokinesis, specifically in abscission of the plasma membrane at the midbody. To perform this function, CEP55 complexes with ESCRT-I (by a Proline rich sequence in its TSG101 domain) and ALIX. This is the domain on CEP55 which binds to both TSG101 and ALIX. It also acts as a hinge between the N and C termini. This domain is called EABR.


Pssm-ID: 463486 [Multi-domain]  Cd Length: 34  Bit Score: 53.65  E-value: 9.21e-10
                          10        20        30
                  ....*....|....*....|....*....|....
gi 20532344   215 KQKVTHVEDLNAKWQRYDASRDEYVKGLHAQLKR 248
Cdd:pfam12180   1 KQQVADVLELNQQWQVYDQSREEYVRGLLARLKE 34
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 19-335 8.73e-09

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: 57.76  E-value: 8.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344     19 AALCGLYHEAGQQLQRLKDQLAARDALIASLRTRLAALEghTAPSLVDALLDQVERFREQLRRQEEgasetQLRQEVERL 98
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELS--RQISALRKDLARLEAEVEQLEERIA-----QLSKELTEL 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344     99 TERLEEKEREMQQLmSQPQHEQEKEVVLLRRSVAEKEKARAASDVLCRSLADETHQLRRTLAATAHMCQHLAKclderqc 178
Cdd:TIGR02168  760 EAEIEELEERLEEA-EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER------- 831

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    179 aQGDAGEKSPAELEQTSSDASGQ-----SVIKKLQEENRLLKQKVTHVEDLNAKWQRYDASRDEYVKGLHAQLKRrqvpl 253
Cdd:TIGR02168  832 -RIAATERRLEDLEEQIEELSEDieslaAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE----- 905

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    254 epelMKKEISRLNRQLEEKISDCAEANQELTAMRMSRDTALERV----QMLEQQILAYKDDFKserADRERAHSRIQELE 329
Cdd:TIGR02168  906 ----LESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLseeySLTLEEAEALENKIE---DDEEEARRRLKRLE 978


                   ....*.
gi 20532344    330 EKIMSL 335
Cdd:TIGR02168  979 NKIKEL 984
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 25-324 9.26e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 9.26e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344  25 YHEAGQQLQRLKDQLAARDALIASLRTRLAALEGH--TAPSLVDALLDQVERFREQLRrqEEGASETQLRQEVERLTERL 102
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAEleELRLELEELELELEEAQAEEY--ELLAELARLEQDIARLEERR 311

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344 103 EEKEREMQQLMSQpQHEQEKEVVLLRRSVAEKEKARAASDVLCRSLADETHQLRRTLAATAHmcQHLAKCLDERQCAQGD 182
Cdd:COG1196 312 RELEERLEELEEE-LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA--ELAEAEEELEELAEEL 388

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344 183 AGEKSPAELEQTSSDASGQSVIKKLQEENRLLKQKVTHVEDLNAKWQRYDASRDEYVKGLHAQLKRRQvplepelmkkEI 262
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE----------EE 458

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20532344 263 SRLNRQLEEKISDCAEANQELTAMRMSRDTALERVQMLEQQILAYKDDFKSERADRERAHSR 324
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 33-331 3.35e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 3.35e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344  33 QRLKDQLAARDALIASLRTRLAALEGHTAPSLVDALLDQVERFREQLRRQEegASETQLRQEVERLTERLEEK-EREMQQ 111
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELE--AELEELRLELEELELELEEAqAEEYEL 293

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344 112 LMSQPQHEQEKEVVLLRRSVAEKEKARAASDVlcRSLADETHQLRRTLAATAHMCQHLAKCLDERQCAQGDAGEKSPAEL 191
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEEL--AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344 192 EQtssdasgqsVIKKLQEENRLLKQKVTHVEDLNAKwqrydASRDEYVKGLHAQLKRRQvplepELMKKEISRLNRQLEE 271
Cdd:COG1196 372 AE---------LAEAEEELEELAEELLEALRAAAEL-----AAQLEELEEAEEALLERL-----ERLEEELEELEEALAE 432

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344 272 KISDCAEANQELTAMRMSRDTALERVQMLEQQILAYKDDFKSERADRERAHSRIQELEEK 331
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 7-336 4.65e-07

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: 52.38  E-value: 4.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344      7 RSGRQDGAPRAAAALCGLYHEAGQQLQRLKDQLAARDALIASLRTRLAALEGHtapslVDALLDQVERFREQLRRQEEGA 86
Cdd:TIGR02169  651 KSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENR-----LDELSQELSDASRKIGEIEKEI 725

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344     87 SetQLRQEVERLTERLEEKEREMQQLmSQPQHEQEKEVVLLRRSVAEKE----KARAASDVLCRSLADE----------- 151
Cdd:TIGR02169  726 E--QLEQEEEKLKERLEELEEDLSSL-EQEIENVKSELKELEARIEELEedlhKLEEALNDLEARLSHSripeiqaelsk 802

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    152 -THQLRRTLAATAHMCQHLAKCLDERQCAqgdagEKSPAELEQTSSDASGQ---------SVIKKLQEENRLLKQKVTHV 221
Cdd:TIGR02169  803 lEEEVSRIEARLREIEQKLNRLTLEKEYL-----EKEIQELQEQRIDLKEQiksiekeieNLNGKKEELEEELEELEAAL 877

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    222 EDLNAKWQRYDASRDEYVKGL-HAQLKRRQVPLEPELMKKEISRLNRQLEEK------ISDCAEANQELTAMRMSRDTAL 294
Cdd:TIGR02169  878 RDLESRLGDLKKERDELEAQLrELERKIEELEAQIEKKRKRLSELKAKLEALeeelseIEDPKGEDEEIPEEELSLEDVQ 957

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 20532344    295 ERVQMLEQQILAYKDDFKSERADRERAHSRIQELEEKIMSLM 336
Cdd:TIGR02169  958 AELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLE 999
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 26-343 1.50e-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: 50.83  E-value: 1.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344     26 HEAGQQLQRLKDQLAARDALIASLRTRLAALEGHTAPSL-------------VDALLDQVERFREQLRRQEEgaSETQLR 92
Cdd:TIGR02168  175 KETERKLERTRENLDRLEDILNELERQLKSLERQAEKAErykelkaelreleLALLVLRLEELREELEELQE--ELKEAE 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344     93 QEVERLTERLEEKEREMQQLMSQpQHEQEKEVVLLRRSVAEKEKARAASDVLCRSLADETHQLRRTLAATAHMCQHLAKC 172
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELRLE-VSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    173 LDErqcaQGDAGEKSPAELEQTSSDASGQSviKKLQEENRLLKQKVTHVEDLNAKWQRYDASRDEyvkglhAQLKRRQVP 252
Cdd:TIGR02168  332 LDE----LAEELAELEEKLEELKEELESLE--AELEELEAELEELESRLEELEEQLETLRSKVAQ------LELQIASLN 399

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    253 LEPELMKKEISRLNRQLEEKISDCAEANQELTAMRMsrDTALERVQMLEQQILAYKDDFKSERADRERAHSRIQELEEKI 332
Cdd:TIGR02168  400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL--KELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477

                          330
                   ....*....|.
gi 20532344    333 MSLMYQVSQRQ 343
Cdd:TIGR02168  478 DAAERELAQLQ 488
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 73-335 2.10e-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: 50.06  E-value: 2.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344     73 ERFREQLRRQEEGASETQ-----LRQEVERLTERLEEKEREMQQlMSQPQHEQEKEVVLLRRSVaekEKARAASDVLCRS 147
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEkalaeLRKELEELEEELEQLRKELEE-LSRQISALRKDLARLEAEV---EQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    148 LADETHQLRRTLAATAHMCQHLAKCLDERQCAQGDAgEKSPAELEQTSSDASGQSviKKLQEENRLLKQKVTHVEDLNAK 227
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI-EQLKEELKALREALDELR--AELTLLNEEAANLRERLESLERR 832

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    228 wQRYDASRDEYVKGLHAQLKRRQVPLEPEL--MKKEISRLNRQLEEKISDCAEANQELTAMRMSRDTALERVQMLEQQIL 305
Cdd:TIGR02168  833 -IAATERRLEDLEEQIEELSEDIESLAAEIeeLEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911

                          250       260       270
                   ....*....|....*....|....*....|
gi 20532344    306 AYKDDFKSERADRERAHSRIQELEEKIMSL 335
Cdd:TIGR02168  912 ELRRELEELREKLAQLELRLEGLEVRIDNL 941
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
28-334 2.20e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.30  E-value: 2.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344   28 AGQQLQRLKDQLAARDALIASLRTRLAALEghtapslvdALLDQVERFREQLRRQEEGASEtqlRQEVERLTERLEEKER 107
Cdd:COG4913  608 NRAKLAALEAELAELEEELAEAEERLEALE---------AELDALQERREALQRLAEYSWD---EIDVASAEREIAELEA 675

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344  108 EMQQLM-SQPQHEQ-EKEVVLLRRSVAEKEKARAASDVLCRSLADETHQLRRTL--------AATAHMCQHLAKCLDERq 177
Cdd:COG4913  676 ELERLDaSSDDLAAlEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELdelqdrleAAEDLARLELRALLEER- 754

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344  178 cAQGDAGEKSPAELEQTSSDASGQSVIKKLQEENRLLKQKVTHVEDLNAKWQRYD---ASRDEYVKgLHAQLKRRQVP-- 252
Cdd:COG4913  755 -FAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDadlESLPEYLA-LLDRLEEDGLPey 832

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344  253 ------LEPELMKKEISRLNRQLEEKISDC----AEANQELTAMRMSRDTALE-RVQMLE-QQILAYKDDFK-------- 312
Cdd:COG4913  833 eerfkeLLNENSIEFVADLLSKLRRAIREIkeriDPLNDSLKRIPFGPGRYLRlEARPRPdPEVREFRQELRavtsgasl 912

                        330       340
                 ....*....|....*....|..
gi 20532344  313 SERADRERAHSRIQELEEKIMS 334
Cdd:COG4913  913 FDEELSEARFAALKRLIERLRS 934
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 86-347 1.30e-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: 47.74  E-value: 1.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344     86 ASETQLRQEVERLTERLEEKEREMQQLMsqpqHEQEKEVVLLRRSVAEKEKARAASDVLCRSLADETHQLRRTLAATAHM 165
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEELEEKI----AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    166 CQHLAKCLDERQCAQGDAGEKSPAELEQ----TSSDASGQSVIKKLQEE-NRLLKQKVTHVEDLNAKWQRYDASRDEYvk 240
Cdd:TIGR02168  742 VEQLEERIAQLSKELTELEAEIEELEERleeaEEELAEAEAEIEELEAQiEQLKEELKALREALDELRAELTLLNEEA-- 819

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    241 gLHAQLKRRQVPLEPELMKKEISRLNRQLEEKISDCAEANQELTAMRMSRDTALERVQMLEQQILAYKDDFKSERADRER 320
Cdd:TIGR02168  820 -ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898

                          250       260
                   ....*....|....*....|....*..
gi 20532344    321 AHSRIQELEEKIMSLMYQVSQRQDSRE 347
Cdd:TIGR02168  899 LSEELRELESKRSELRRELEELREKLA 925
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 89-350 1.61e-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: 1.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344     89 TQLRQEVERLTERLEEKEREMQQLMSQPQH-------------EQEKEVVLLRRSVAEKEKARAASDVLCRSLADETHQL 155
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKRELSSLQSELRRienrldelsqelsDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    156 RRTLAATAHMCQHLAKCLDERQcAQGDAGEKSPAELEQTSSDASGQSVIKKLQEENRLLKQKVTHVEDLNAKWQRYDASR 235
Cdd:TIGR02169  750 EQEIENVKSELKELEARIEELE-EDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    236 dEYVKGLHAQLKRRQVPLEP--ELMKKEISRLNRQLEEKISDCAEANQELTAMRMSRDTALERVQMLEQQILAYKDDFKS 313
Cdd:TIGR02169  829 -EYLEKEIQELQEQRIDLKEqiKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 20532344    314 ERADRERAHSRIQELEEKIMSLMYQVSQ-----RQDSREPGP 350
Cdd:TIGR02169  908 LEAQIEKKRKRLSELKAKLEALEEELSEiedpkGEDEEIPEE 949
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 27-345 4.79e-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: 45.83  E-value: 4.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344     27 EAGQQLQRLKDQlaaRDALIA--SLRTRLAALEGHTAPSLVDALLDQVERFREQLRRQEEgaSETQLRQEVERLTERLEE 104
Cdd:TIGR02169  195 EKRQQLERLRRE---REKAERyqALLKEKREYEGYELLKEKEALERQKEAIERQLASLEE--ELEKLTEEISELEKRLEE 269

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    105 KEREMQQLMSQPQHEQEKEVVLLRRSVAEKEKARAASDVLCRSLADETHQLRRTLAatahmcqhlaKCLDERQCAQGDAG 184
Cdd:TIGR02169  270 IEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA----------KLEAEIDKLLAEIE 339

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    185 EKSPAELEQTSSDASGQSVIKKLQEENRLLKQKVTHVEDLNAKWQRYDASRDEYVKGL---HAQLKRRQVPLEPEL---- 257
Cdd:TIGR02169  340 ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLkreINELKRELDRLQEELqrls 419

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    258 -----MKKEISRLNRQLEEKISDCAEANQELTAMRMSRDTALERVQMLEQQILAykddfksERADRERAHSRIQELEEKI 332
Cdd:TIGR02169  420 eeladLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD-------LKEEYDRVEKELSKLQREL 492

                          330
                   ....*....|...
gi 20532344    333 MSLMYQVSQRQDS 345
Cdd:TIGR02169  493 AEAEAQARASEER 505
CC2-LZ pfam16516
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ...
 259-341 5.41e-05

Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a leucine-zipper domain associated with the CC2 coiled-coil region of NF-kappa-B essential modulator, NEMO. It plays a regulatory role, along with the very C-terminal zinc-finger; it contains a ubiquitin-binding domain (UBD) and represents one region that contributes to NEMO oligomerization. NEMO itself is an integral part of the IkappaB kinase complex and serves as a molecular switch via which the NF-kappaB signalling pathway is regulated.


Pssm-ID: 465155 [Multi-domain]  Cd Length: 100  Bit Score: 41.89  E-value: 5.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344   259 KKEISRLNRQL---EEKISDCAEANQELTAMRMSRDTALERVQMLEQQILAYKDDFKSERADRERAHSRIQELEEKIMSL 335
Cdd:pfam16516  13 KDEIDCLQAQLqaaEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYL 92


                  ....*.
gi 20532344   336 MYQVSQ 341
Cdd:pfam16516  93 QRQNQQ 98
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 27-316 2.47e-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: 43.51  E-value: 2.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344     27 EAGQQLQRLKDQLaaRDALIASLRTRLAALEGHTAPSLVDALLDQVERFREQLRRQEEGASETQLRQEVERLTERLEEKE 106
Cdd:TIGR02168  210 EKAERYKELKAEL--RELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ 287

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    107 REMQQLmSQPQHEQEKEVVLLRRSVAEKEKARAASDVLCRSLADETHQLRRTLAATAHMCQHLAKCLDERQcAQGDAGEK 186
Cdd:TIGR02168  288 KELYAL-ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE-AELEELEA 365

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    187 SPAELEQTSSDASGQS------VIKKLQEENRL---LKQKVTHVEDLNAKWQRYDASRDEYVKGLHAQ----LKRRQVPL 253
Cdd:TIGR02168  366 ELEELESRLEELEEQLetlrskVAQLELQIASLnneIERLEARLERLEDRRERLQQEIEELLKKLEEAelkeLQAELEEL 445

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20532344    254 EPELMK--KEISRLNRQLEEKISDCAEANQELTAMRMSRDTALERVQMLEQQILAYKDDFKSERA 316
Cdd:TIGR02168  446 EEELEElqEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
30-330 4.48e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 4.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344  30 QQLQRLKDQLAARDALIASLRTRLAALEGHTAPSLVDALLDQVERFRE-QLRRQEEGASETQLRQEVERLTERLEEKERE 108
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEElQQRLAELEEELEEAQEELEELEEELEQLENE 235

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344 109 MQQLMSQPQHEQEKEVVLLRRSVAEKEKARAASDVLCRSLAD------------ETHQLRRTLAATAHMCQHLAKCLDER 176
Cdd:COG4717 236 LEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGvlflvlgllallFLLLAREKASLGKEAEELQALPALEE 315

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344 177 QCAQGDAGEKSPAELEQTSSDASGQSVIKKLQEENRLLKQKVTHVEDL---------NAKWQRYDA-SRDEYVKGLHAQL 246
Cdd:COG4717 316 LEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELqleeleqeiAALLAEAGVeDEEELRAALEQAE 395

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344 247 KRRQvplepelMKKEISRLNRQLEEKISDCAEANQELTamrmsRDTALERVQMLEQQILAYKDDFKSERADRERAHSRIQ 326
Cdd:COG4717 396 EYQE-------LKEELEELEEQLEELLGELEELLEALD-----EEELEEELEELEEELEELEEELEELREELAELEAELE 463


                ....
gi 20532344 327 ELEE 330
Cdd:COG4717 464 QLEE 467
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
27-140 1.19e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 1.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344  27 EAGQQLQRLKDQLAARDALIASLRTRLAALEGHTAPSLVDALLDQVERFREQLRRQEEGASETQLRQ--EVERLTERLEE 104
Cdd:COG3206 223 ELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNhpDVIALRAQIAA 302

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 20532344 105 KEREMQQLMSQPQHEQEKEVVLLRRSVAEKEKARAA 140
Cdd:COG3206 303 LRAQLQQEAQRILASLEAELEALQAREASLQAQLAQ 338
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
10-133 1.27e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344   10 RQDGAPRAAAALCGLYHEAGQQLQRLKDQLAARDALIASLRTRLAALEGhTAPSLVDALLDqvERFREQLRRQEEGASET 89
Cdd:COG4913  693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED-LARLELRALLE--ERFAAALGDAVERELRE 769

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 20532344   90 QLRQEVERLTERLEEKEREMQQLMSQPQHEQEKEVVLLRRSVAE 133
Cdd:COG4913  770 NLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLES 813
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
16-162 1.60e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 1.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344  16 RAAAALCGLYHEAGQQLQRLKDQLAARDALIASLRTRLAALEG----HTAPSLVDALLDQVERFREQLRRQEEGASE-TQ 90
Cdd:COG4717  81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllqlLPLYQELEALEAELAELPERLEELEERLEElRE 160

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20532344  91 LRQEVERLTERLEEKEREMQQLMSQPQHEQEKEVVLLRRSVAEKEKARAASDVLCRSLADETHQLRRTLAAT 162
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 72-348 1.67e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 1.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344     72 VERFREqlRRQEegaSETQL---RQEVERLTERLEEKEREMQQLMSQpqheQEKEVVLLRRSVAEKEKARAASDVLCRSL 148
Cdd:TIGR02168  167 ISKYKE--RRKE---TERKLertRENLDRLEDILNELERQLKSLERQ----AEKAERYKELKAELRELELALLVLRLEEL 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    149 ADETHQLRRTLAATAHMCQHLAKCLDERQcAQGDAGEKSPAELEQTSSDASG-----QSVIKKLQEENRLLKQKVTHVED 223
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELE-EKLEELRLEVSELEEEIEELQKelyalANEISRLEQQKQILRERLANLER 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    224 ----LNAKWQRYDASRDEYVKGLHAQLKRRQVplepelMKKEISRLNRQLEEKISDCAEANQELTAMRMSRDTALERVQM 299
Cdd:TIGR02168  317 qleeLEAQLEELESKLDELAEELAELEEKLEE------LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 20532344    300 LEQQIlaykddfKSERADRERAHSRIQELEEKIMSLMYQVSQRQDSREP 348
Cdd:TIGR02168  391 LELQI-------ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 93-331 2.08e-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: 40.71  E-value: 2.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344   93 QEVERLTERLEEKEREMQQLMSQPQHEQEKevvllRRSVAEKEKARAASDVLCRSLADETHQLRRT---------LAATA 163
Cdd:COG3096  836 AELAALRQRRSELERELAQHRAQEQQLRQQ-----LDQLKEQLQLLNKLLPQANLLADETLADRLEelreeldaaQEAQA 910

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344  164 HMCQHLAKCldERQCAQGDAGEKSPAELEQTSSDasgqsvIKKLQEENRLLKQKVTHVEDLNAKW---------QRYDAS 234
Cdd:COG3096  911 FIQQHGKAL--AQLEPLVAVLQSDPEQFEQLQAD------YLQAKEQQRRLKQQIFALSEVVQRRphfsyedavGLLGEN 982

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344  235 RDeyvkgLHAQLKRRQvplepELMKKEISRLNRQLEEKISDCAEANQELTAMRMSRDTALERVQMLEQQILAY--KDDFK 312
Cdd:COG3096  983 SD-----LNEKLRARL-----EQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELgvQADAE 1052

                        250
                 ....*....|....*....
gi 20532344  313 SEradrERAHSRIQELEEK 331
Cdd:COG3096 1053 AE----ERARIRRDELHEE 1067
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 205-347 2.10e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 2.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344 205 KKLQEENRLLKQKVT--HVEDLNAKWQRYDASRDEYVKGL-HAQLKRRQVPLEPELMKKEISRLNRQLEEKISDCAEANQ 281
Cdd:COG1196 216 RELKEELKELEAELLllKLRELEAELEELEAELEELEAELeELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20532344 282 ELTAMRMSRDTALERVQMLEQQILAYKDDFKSERADRERAHSRIQELEEKIMSLMYQVSQRQDSRE 347
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 32-341 2.32e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 40.49  E-value: 2.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344     32 LQRLKDQLaarDALIASLRTRLAAL--EGHTAPSLVDALLDQVERFREQLRRQeegaSETQLRQ--EVERLTERLEEKER 107
Cdd:pfam15921  262 LQQHQDRI---EQLISEHEVEITGLteKASSARSQANSIQSQLEIIQEQARNQ----NSMYMRQlsDLESTVSQLRSELR 334

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    108 EMQQLMSQPQHEQEKEVVLLRRSVAEkekARAASDVLCRSLADETHQLRRTLA------------------------ATA 163
Cdd:pfam15921  335 EAKRMYEDKIEELEKQLVLANSELTE---ARTERDQFSQESGNLDDQLQKLLAdlhkrekelslekeqnkrlwdrdtGNS 411

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    164 HMCQHLAKCLDERQCAQgdagEKSPAELEQTSSDASGQ--SVIKKLQEENRLLKQkvthVEDLNAKWQrydaSRDEYVKG 241
Cdd:pfam15921  412 ITIDHLRRELDDRNMEV----QRLEALLKAMKSECQGQmeRQMAAIQGKNESLEK----VSSLTAQLE----STKEMLRK 479

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    242 LHAQLKRRQVPLEPElmKKEISRLNRQLEEKISDCAEANQELTAMRMSRDTALERVQMLE------QQILAYKDDFKSER 315
Cdd:pfam15921  480 VVEELTAKKMTLESS--ERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKnegdhlRNVQTECEALKLQM 557

                          330       340
                   ....*....|....*....|....*.
gi 20532344    316 ADRERAhsrIQELEEKIMSLMYQVSQ 341
Cdd:pfam15921  558 AEKDKV---IEILRQQIENMTQLVGQ 580
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 31-332 2.95e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 40.10  E-value: 2.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344     31 QLQRLKDQLAA-RDALIASLRTRLAALEG-HTAPSLVDALLDQVERFREQLRRQEEGASETQLRQE-----VERLTERLE 103
Cdd:pfam15921  427 EVQRLEALLKAmKSECQGQMERQMAAIQGkNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLEssertVSDLTASLQ 506

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    104 EKER---------------------EMQQLMSQPQHEQ--EKEVVLLRRSVAEKEKARAASDVLCRSLADETHQLRRTLA 160
Cdd:pfam15921  507 EKERaieatnaeitklrsrvdlklqELQHLKNEGDHLRnvQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAG 586

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    161 ATAHMCQHLAKCLDERQCAQ------GDAGEKSPAELEQTSSDASGQSV------------IKKL-QEENRLLKQKVTHV 221
Cdd:pfam15921  587 AMQVEKAQLEKEINDRRLELqefkilKDKKDAKIRELEARVSDLELEKVklvnagserlraVKDIkQERDQLLNEVKTSR 666

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    222 EDLNAKWQRYdasrdeyvkglhaQLKRRQVPLEPELMKKEISRLNRQLEEKISDCAEANQELTAMRMSRDTALERVQMLE 301
Cdd:pfam15921  667 NELNSLSEDY-------------EVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQ 733

                          330       340       350
                   ....*....|....*....|....*....|.
gi 20532344    302 QQILAykddfksERADRERAHSRIQELEEKI 332
Cdd:pfam15921  734 KQITA-------KRGQIDALQSKIQFLEEAM 757
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 30-237 3.55e-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: 3.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344  30 QQLQRLKDQLAARDALIASLRTRLAALEghtapSLVDALLDQVERFREQLRRQEEGASEtqLRQEVERLTERLEEKEREM 109
Cdd:COG4942  34 QEIAELEKELAALKKEEKALLKQLAALE-----RRIAALARRIRALEQELAALEAELAE--LEKEIAELRAELEAQKEEL 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344 110 QQLM--SQPQHEQEKEVVLLR-RSVAEKEKARAASDVLCRSLADETHQLRRTLAATAHMCQHLAKCLDERQCAQGDAGEK 186
Cdd:COG4942 107 AELLraLYRLGRQPPLALLLSpEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 20532344 187 ----SPAELEQTSSDASGQSVIKKLQEENRLLKQKVTHVEDLNAKWQRYDASRDE 237
Cdd:COG4942 187 raalEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 94-347 4.73e-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: 39.28  E-value: 4.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344     94 EVERLTERLEEKEREMQQLMSQPQHEQEKevvLLRRSVAEKEKARAASDVLCRSLADETHQLRRTLAATAHMCQHLAKCL 173
Cdd:TIGR02169  181 EVEENIERLDLIIDEKRQQLERLRREREK---AERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLT 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    174 DERQcaqgdAGEKSPAELEQTSSDASGQsvIKKLQEENRLLKQKvtHVEDLNAKWQRYDASRDEYVKGLH-AQLKRRQVP 252
Cdd:TIGR02169  258 EEIS-----ELEKRLEEIEQLLEELNKK--IKDLGEEEQLRVKE--KIGELEAEIASLERSIAEKERELEdAEERLAKLE 328

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    253 LEPELMKKEISRLNRQLEEKISDCAEANQELTAMRMSRDTALERVQMLEQQILAYKDDFKSERADRERAHSRIQELEEKI 332
Cdd:TIGR02169  329 AEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL 408

                          250
                   ....*....|....*
gi 20532344    333 MSLMYQVSQRQDSRE 347
Cdd:TIGR02169  409 DRLQEELQRLSEELA 423
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
61-348 5.11e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.23  E-value: 5.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344  61 APSLVDALLDQVERFREQLRRQEEGASETQLRQEVERLTERLEEKEREMQQLMSQpqheqekevvllRRSVAEKEKARAA 140
Cdd:COG3206 150 AAAVANALAEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQK------------NGLVDLSEEAKLL 217

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344 141 SDVLcRSLADETHQLRRTLAATAhmcqhlakclderqcAQGDAGEKSPAELEQTSSDASGQSVIKKLQEENRLLKQKVth 220
Cdd:COG3206 218 LQQL-SELESQLAEARAELAEAE---------------ARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAEL-- 279

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344 221 vedlnakwqrydasrdeyvkglhAQLKRRQVPLEPEL--MKKEISRLNRQLEEkisdcaEANQELTAMRMSRDTALERVQ 298
Cdd:COG3206 280 -----------------------AELSARYTPNHPDViaLRAQIAALRAQLQQ------EAQRILASLEAELEALQAREA 330

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 20532344 299 MLEQQILAYKDDFKS------ERADRERAHSRIQELEEKIMSLMYQVSQRQDSREP 348
Cdd:COG3206 331 SLQAQLAQLEARLAElpeleaELRRLEREVEVARELYESLLQRLEEARLAEALTVG 386
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
49-332 6.19e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 6.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344   49 LRTRLAALEG-HTAPSLVDALLDQVERfreqLRRQEEGASETQLRQEVERLTERLEEKEREMQQLMSQpQHEQEKEVVLL 127
Cdd:PRK03918 350 LEKRLEELEErHELYEEAKAKKEELER----LKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITAR-IGELKKEIKEL 424

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344  128 RRSVAEKEKARAASDVlCRSLADETHQLRRTLAATAHMcqhlaKCLDERQCAQGDAGEKSPAELEQTSSDASGQSVIKKL 207
Cdd:PRK03918 425 KKAIEELKKAKGKCPV-CGRELTEEHRKELLEEYTAEL-----KRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL 498

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344  208 QEENRLLKQ-----KVTHVEDLNAKWQRYdasrdEYVKGLHAQLKRRQVPLEPEL-----MKKEISRLNRQLEEKISDCA 277
Cdd:PRK03918 499 KELAEQLKEleeklKKYNLEELEKKAEEY-----EKLKEKLIKLKGEIKSLKKELekleeLKKKLAELEKKLDELEEELA 573

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 20532344  278 EANQELTAMRMSRDTALE-RVQMLEQqilAYKD--DFKSERADRERAHSRIQELEEKI 332
Cdd:PRK03918 574 ELLKELEELGFESVEELEeRLKELEP---FYNEylELKDAEKELEREEKELKKLEEEL 628
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 71-327 7.30e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 38.93  E-value: 7.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    71 QVERFREQLRRQEEgaSETQLRQEVERLTERLEEKEREMQQLMSQpqheQEKEVVLLRRSVAEKEKARAASDVLCRSLAD 150
Cdd:pfam05483 528 QEERMLKQIENLEE--KEMNLRDELESVREEFIQKGDEVKCKLDK----SEENARSIEYEVLKKEKQMKILENKCNNLKK 601

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344   151 ETHQLRRTLAATAHMCQHLAKcLDERQCAQGDAGE--KSPAELEQTSSDASGQSVIKKLQEEnrlLKQKVTHVEDLNAKW 228
Cdd:pfam05483 602 QIENKNKNIEELHQENKALKK-KGSAENKQLNAYEikVNKLELELASAKQKFEEIIDNYQKE---IEDKKISEEKLLEEV 677

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344   229 QRYDASRDEYVKgLHAQLKRR---QVPLEPELMKKEISRLNRQLEEKISDCA---EANQELTAMRMSRDTALERvqmLEQ 302
Cdd:pfam05483 678 EKAKAIADEAVK-LQKEIDKRcqhKIAEMVALMEKHKHQYDKIIEERDSELGlykNKEQEQSSAKAALEIELSN---IKA 753

                         250       260
                  ....*....|....*....|....*
gi 20532344   303 QILAYKDDFKSERADRERAHSRIQE 327
Cdd:pfam05483 754 ELLSLKKQLEIEKEEKEKLKMEAKE 778
FUSC pfam04632
Fusaric acid resistance protein family; This family includes a conserved region found in two ...
 5-166 7.33e-03

Fusaric acid resistance protein family; This family includes a conserved region found in two proteins associated with fusaric acid resistance, from Burkholderia cepacia and Klebsiella oxytoca. These proteins are likely to be membrane transporter proteins.


Pssm-ID: 428044 [Multi-domain]  Cd Length: 655  Bit Score: 38.80  E-value: 7.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344     5 DPRSGRQDGAPRAA----AALCGLYHEAGQQLQRLKDQLAARDALIASLRTRLAALEGHTAPslvDALLDQVERFREQLR 80
Cdd:pfam04632 210 SPRGRARARALRRLlarmLALLPRLRSLARLLARLRTEGAGTVPELAALLDELAAWEAALAA---EALQAALAALRARLR 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344    81 RQEEGASETQLRQevERLTERLEEKEREMQQLMSqpqheqekEVVLLRRSVAEKEKARAASDVlcrslADETHQLR---R 157
Cdd:pfam04632 287 ALRPALPLDFDTA--AELLARLADLLAELAEALA--------SCRALRHPIAQGARPARLARH-----RDHGAALLnglR 351


                  ....*....
gi 20532344   158 TLAATAHMC 166
Cdd:pfam04632 352 AALAILLAG 360
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 92-347 7.85e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 7.85e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344  92 RQEVERLTERLEEKEREMQQLmsqpqhEQEKEVVLLRRSVAEKEKARaasDVLCRSLADETHQLRRTLAATAhmcQHLAK 171
Cdd:COG1196 185 EENLERLEDILGELERQLEPL------ERQAEKAERYRELKEELKEL---EAELLLLKLRELEAELEELEAE---LEELE 252

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344 172 CLDERQCAQGDAGEKSPAELEQTSSDASGQsvIKKLQEENRLLKQKVTHVEdlnakwqrydaSRDEYVKGLHAQLKRRQV 251
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELE--LEEAQAEEYELLAELARLE-----------QDIARLEERRRELEERLE 319

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344 252 PLEPEL--MKKEISRLNRQLEEKISDCAEANQELTAMRMSRDTALERVQMLEQQILAYKDDFKSERADRERAHSRIQELE 329
Cdd:COG1196 320 ELEEELaeLEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399

                       250
                ....*....|....*...
gi 20532344 330 EKIMSLMYQVSQRQDSRE 347
Cdd:COG1196 400 AQLEELEEAEEALLERLE 417
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 69-124 9.01e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 38.27  E-value: 9.01e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 20532344   69 LDQV-ERFREQLRRQEEGASETQ-LRQEVERLTERLEEKEREMQQLMSQPQHEQEKEV 124
Cdd:PRK00409 518 LNELiASLEELERELEQKAEEAEaLLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEA 575
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 91-332 9.32e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.38  E-value: 9.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344  91 LRQEVERLTERLE---EKEREMQQLMSQpQHEQEKEVVLLRRSVAEKEKARAASDvlcrsLADETHQLRRTLAATAHMCQ 167
Cdd:COG1196 194 ILGELERQLEPLErqaEKAERYRELKEE-LKELEAELLLLKLRELEAELEELEAE-----LEELEAELEELEAELAELEA 267

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344 168 HLAKCLDERQCAQGDAGEKSPAELEQTSSDASGQSVIKKLQEENRLLKQKVTHVEDLNAKWQRYDASRDEYVKGLHAQLK 247
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE 347

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532344 248 RRQVPLEpeLMKKEISRLNRQLEEKISDCAEANQELTAMRMSRDTALERVQMLEQQILAYKDDFKSERADRERAHSRIQE 327
Cdd:COG1196 348 EAEEELE--EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425


                ....*
gi 20532344 328 LEEKI 332
Cdd:COG1196 426 LEEAL 430
 
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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