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Conserved domains on  [gi|1958652023|ref|XP_038955224|]
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microtubule cross-linking factor 3 isoform X3 [Rattus norvegicus]

Protein Classification

AAA family ATPase( domain architecture ID 1003843)

AAA family ATPase containing an AAA (ATPases Associated with various cellular Activities) domain, may function as an ATP-dependent endonuclease or the ATPase component of an ABC-type transporter; similar to Bacillus subtilis protein YhaN

CATH:  3.40.50.300
Gene Ontology:  GO:0005524|GO:0016887
PubMed:  15037234|18208389|16828312|18466635|15037233

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
355-493 4.57e-08

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


The actual alignment was detected with superfamily member COG4717:

Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.93  E-value: 4.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 355 KLREENETLKNEIDELRTEMDEMrdtffeEDACQLQEMRHELERANKNCRILQYRLRKAERKRLRYAQTGEIdgelLRSL 434
Cdd:COG4717    99 ELEEELEELEAELEELREELEKL------EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEE----LEEL 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 435 EQDLKVAKDVSVRLHHELENVEEKR-TTTEDENEKLRQQLIEVEIAKQALQNELEKMKEN 493
Cdd:COG4717   169 EAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
 
Name Accession Description Interval E-value
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
355-493 4.57e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.93  E-value: 4.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 355 KLREENETLKNEIDELRTEMDEMrdtffeEDACQLQEMRHELERANKNCRILQYRLRKAERKRLRYAQTGEIdgelLRSL 434
Cdd:COG4717    99 ELEEELEELEAELEELREELEKL------EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEE----LEEL 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 435 EQDLKVAKDVSVRLHHELENVEEKR-TTTEDENEKLRQQLIEVEIAKQALQNELEKMKEN 493
Cdd:COG4717   169 EAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 356-498 1.78e-06

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 49.76  E-value: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 356 LREENETLKNEIDELRTEMDEMRDTFFEEdacqLQEMRHELERANKNCRILQYRLRKAERKRLRYAQTgeidgelLRSLE 435
Cdd:pfam09787  59 LREEIQKLRGQIQQLRTELQELEAQQQEE----AESSREQLQELEEQLATERSARREAEAELERLQEE-------LRYLE 127

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958652023 436 QDLKVAKDVSVRLHHELENVEEK----------RTTTEDENEKLRQQLIEVEIAKQALQNELEKMKENTLLRI 498
Cdd:pfam09787 128 EELRRSKATLQSRIKDREAEIEKlrnqltsksqSSSSQSELENRLHQLTETLIQKQTMLEALSTEKNSLVLQL 200
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 355-493 4.06e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 4.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023  355 KLREENETLKNEIDELRTEMDEMRDTFfEEDACQLQEMRHELERANKNCRILQYRLRKAERKRLRYAQTGEIDGELLRSL 434
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKEL-EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958652023  435 EQDLKVAKDVSVRLHHELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNELEKMKEN 493
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
357-492 3.07e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 3.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 357 REENETLKNEIDELRTEMDEMRDTFFEEDAcQLQEMRHELERANKNcrilqYRLRKAERKRlryaqtgeidgELLRSLEQ 436
Cdd:PRK03918  611 EKELEREEKELKKLEEELDKAFEELAETEK-RLEELRKELEELEKK-----YSEEEYEELR-----------EEYLELSR 673

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958652023 437 DLKvakdvsvRLHHELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNeLEKMKE 492
Cdd:PRK03918  674 ELA-------GLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK-LEKALE 721
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 356-499 1.43e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 40.77  E-value: 1.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023  356 LREENETLKNEIDELRTEMDEMRDTFfeedacqlQEMRHELERankncrilqyrLRKAERkrlryaQTGEIDGELLRSLE 435
Cdd:smart00787 156 LKEDYKLLMKELELLNSIKPKLRDRK--------DALEEELRQ-----------LKQLED------ELEDCDPTELDRAK 210

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958652023  436 QDLKVAKDVSVRLHHELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNELEKMKENTLLRIS 499
Cdd:smart00787 211 EKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIE 274
 
Name Accession Description Interval E-value
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
355-493 4.57e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.93  E-value: 4.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 355 KLREENETLKNEIDELRTEMDEMrdtffeEDACQLQEMRHELERANKNCRILQYRLRKAERKRLRYAQTGEIdgelLRSL 434
Cdd:COG4717    99 ELEEELEELEAELEELREELEKL------EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEE----LEEL 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 435 EQDLKVAKDVSVRLHHELENVEEKR-TTTEDENEKLRQQLIEVEIAKQALQNELEKMKEN 493
Cdd:COG4717   169 EAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 356-498 1.78e-06

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 49.76  E-value: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 356 LREENETLKNEIDELRTEMDEMRDTFFEEdacqLQEMRHELERANKNCRILQYRLRKAERKRLRYAQTgeidgelLRSLE 435
Cdd:pfam09787  59 LREEIQKLRGQIQQLRTELQELEAQQQEE----AESSREQLQELEEQLATERSARREAEAELERLQEE-------LRYLE 127

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958652023 436 QDLKVAKDVSVRLHHELENVEEK----------RTTTEDENEKLRQQLIEVEIAKQALQNELEKMKENTLLRI 498
Cdd:pfam09787 128 EELRRSKATLQSRIKDREAEIEKlrnqltsksqSSSSQSELENRLHQLTETLIQKQTMLEALSTEKNSLVLQL 200
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
355-493 3.15e-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: 3.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023  355 KLREENETLKNEIDELRTEMDEMRDTFFEEDACQLQEMRHELERANKncrilqyRLRKAERKRLRYAQtgeidgeLLRSL 434
Cdd:COG4913    306 RLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLER-------ELEERERRRARLEA-------LLAAL 371

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958652023  435 E----QDLKVAKDVSVRLHHELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNELEKMKEN 493
Cdd:COG4913    372 GlplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 355-493 4.06e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 4.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023  355 KLREENETLKNEIDELRTEMDEMRDTFfEEDACQLQEMRHELERANKNCRILQYRLRKAERKRLRYAQTGEIDGELLRSL 434
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKEL-EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958652023  435 EQDLKVAKDVSVRLHHELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNELEKMKEN 493
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
355-493 4.32e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.13  E-value: 4.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 355 KLREENETLKNEIDELRTEMDEMRDtffeedacQLQEMRHELERANKncrilqyRLRKAERKrLRYAQtgeidgELLRSL 434
Cdd:COG4372    42 KLQEELEQLREELEQAREELEQLEE--------ELEQARSELEQLEE-------ELEELNEQ-LQAAQ------AELAQA 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958652023 435 EQDLKVAKDVSVRLHHELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNELEKMKEN 493
Cdd:COG4372   100 QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 355-492 4.58e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 4.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 355 KLREENETLKNEIDELRTEMDEMRDTFFEEDAcQLQEMRHELERANKNCRILQYRLRKAERKRLRYAQTGEIDGELLRSL 434
Cdd:COG1196   250 ELEAELEELEAELAELEAELEELRLELEELEL-ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958652023 435 EQDLKVAKDVSVRLHHELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNELEKMKE 492
Cdd:COG1196   329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 355-486 6.43e-06

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: 49.30  E-value: 6.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023  355 KLREENETLKNEIDELRTEMDEMRDTFFEEDAcQLQEMRHELERANKNCRILQYRLRKAERKRLRY--------AQTGEI 426
Cdd:TIGR02169  361 ELKEELEDLRAELEEVDKEFAETRDELKDYRE-KLEKLKREINELKRELDRLQEELQRLSEELADLnaaiagieAKINEL 439

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958652023  427 DGEL------LRSLEQDLKVAKDVSVRLHHELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNE 486
Cdd:TIGR02169  440 EEEKedkaleIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 355-488 1.41e-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: 48.13  E-value: 1.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023  355 KLREENETLKNEIDELRTEMDEMRDTFFEEDAcQLQEMRHELERANKNCRILQYRLRKAERKRLRYaqtgeidGELLRSL 434
Cdd:TIGR02168  257 ELTAELQELEEKLEELRLEVSELEEEIEELQK-ELYALANEISRLEQQKQILRERLANLERQLEEL-------EAQLEEL 328

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958652023  435 EQDLKVAKDVSVRLHHELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNELE 488
Cdd:TIGR02168  329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 355-493 1.79e-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: 1.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023  355 KLREENETLKNEIDELRTEMDEMRDTF------FEEDACQLQEMRHELERANKNCRILQYRLRKAERKRLRYAQTGEIDG 428
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEELEEELeqlrkeLEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958652023  429 ELLRSLEQDLKVAKDVSVRLHHELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNELEKMKEN 493
Cdd:TIGR02168  768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 355-492 3.29e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 45.30  E-value: 3.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 355 KLREENETLKNEIDELRTEMDEMRDTFfEEDACQLQEMRHELERANKNCRILQYRLRKAERK-------RLRYAQTGEID 427
Cdd:COG1579    21 RLEHRLKELPAELAELEDELAALEARL-EAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnKEYEALQKEIE 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958652023 428 gellrSLEQDLKVAKDVSVRLHHELENVEEKRTTTEDENEKLRQQLI----EVEIAKQALQNELEKMKE 492
Cdd:COG1579   100 -----SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEekkaELDEELAELEAELEELEA 163
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 357-471 4.76e-05

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 45.57  E-value: 4.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 357 REENETLKNEIDELRTEMDEMRDtfFEEDACQLQEMrheLERANKNCRILQYRLRkaERKRLRYAQTGEIDG---ELLRS 433
Cdd:pfam15905 218 KSETEKLLEYITELSCVSEQVEK--YKLDIAQLEEL---LKEKNDEIESLKQSLE--EKEQELSKQIKDLNEkckLLESE 290

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958652023 434 LEQDLKVAKDVSVRLHHELENVEEKRTTTEDENEKLRQ 471
Cdd:pfam15905 291 KEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 355-491 6.57e-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: 45.82  E-value: 6.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023  355 KLREENETLKNEIDELRTEMDEMRDTFFE--EDACQLQEMRHELERANKNcriLQYRLRKAERKRLRYAQTGEIDGELLR 432
Cdd:TIGR02168  793 QLKEELKALREALDELRAELTLLNEEAANlrERLESLERRIAATERRLED---LEEQIEELSEDIESLAAEIEELEELIE 869

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958652023  433 SLEQDLKVAKDV-------SVRLHHELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNELEKMK 491
Cdd:TIGR02168  870 ELESELEALLNErasleeaLALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 355-493 2.12e-04

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: 44.24  E-value: 2.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 355 KLREENETLKNEIDELRTEMDEMRDTF-------------FEEDACQLQEMRHELERANKNCRILQYRLR--KAERKRLR 419
Cdd:TIGR04523 222 ELKKQNNQLKDNIEKKQQEINEKTTEIsntqtqlnqlkdeQNKIKKQLSEKQKELEQNNKKIKELEKQLNqlKSEISDLN 301

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 420 YAQTGEIDGEL---LRSLEQDLKVA--------KDVSvRLHHELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNELE 488
Cdd:TIGR04523 302 NQKEQDWNKELkseLKNQEKKLEEIqnqisqnnKIIS-QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQ 380


                  ....*
gi 1958652023 489 KMKEN 493
Cdd:TIGR04523 381 SYKQE 385
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
357-492 3.07e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 3.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 357 REENETLKNEIDELRTEMDEMRDTFFEEDAcQLQEMRHELERANKNcrilqYRLRKAERKRlryaqtgeidgELLRSLEQ 436
Cdd:PRK03918  611 EKELEREEKELKKLEEELDKAFEELAETEK-RLEELRKELEELEKK-----YSEEEYEELR-----------EEYLELSR 673

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958652023 437 DLKvakdvsvRLHHELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNeLEKMKE 492
Cdd:PRK03918  674 ELA-------GLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK-LEKALE 721
CCDC144C pfam14915
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ...
 355-496 4.52e-04

CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.


Pssm-ID: 464371 [Multi-domain]  Cd Length: 304  Bit Score: 42.28  E-value: 4.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 355 KLREENETLKNEIDELRTEM----DEMRDTFFEEDAcQLQ-------EMRHELERANKNCRILQYRLrKAERKRLRYA-- 421
Cdd:pfam14915  28 KYLEDIEILKEKNDDLQKTLklneETLTKTVFQYNG-QLNvlkaentMLNSKLENEKQNKERLETEV-ESYRSRLAAAiq 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 422 -----QTGEIDgellrsLEQDLKVAKDVSVRLHHELeNVEekRTTTEDENEKLRQQLIEVEIAKQALQNELEKMK----E 492
Cdd:pfam14915 106 dheqsQTSKRD------LELAFQRERDEWLRLQDKM-NFD--VSNLRDENEILSQQLSKAESKANSLENELHRTRdalrE 176


                  ....
gi 1958652023 493 NTLL 496
Cdd:pfam14915 177 KTLL 180
EzrA COG4477
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ...
 356-493 5.75e-04

Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443574 [Multi-domain]  Cd Length: 567  Bit Score: 42.52  E-value: 5.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 356 LREENETLKNEIDELRTEMDEMRDT--FFEEDAC--QLQEMRHELERANKNcrILQYRLRKAErKRLRYAQTgEIDgELL 431
Cdd:COG4477   220 LKELQTELPDQLEELKSGYREMKEQgyVLEHLNIekEIEQLEEQLKEALEL--LEELDLDEAE-EELEEIEE-EID-ELY 294

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958652023 432 RSLEQDLKVAKDV---SVRLHHELENVEEKRTTTEDENEKLRQ--QLIEVEIAK-QALQNELEKMKEN 493
Cdd:COG4477   295 DLLEKEVEAKKYVdknQEELEEYLEHLKEQNRELKEEIDRVQQsyRLNENELEKvRNLEKQIEELEKR 362
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 355-493 7.23e-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: 42.35  E-value: 7.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023  355 KLREENETLKNEIDELRTEMDEMRDTFFEED------ACQLQEMRHELERANKNCRILQYRLRKAERKRLRyAQTGEIDG 428
Cdd:TIGR02168  362 ELEAELEELESRLEELEEQLETLRSKVAQLElqiaslNNEIERLEARLERLEDRRERLQQEIEELLKKLEE-AELKELQA 440

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958652023  429 ELLRSLEQDLKvakdvsvrLHHELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNE---LEKMKEN 493
Cdd:TIGR02168  441 ELEELEEELEE--------LQEELERLEEALEELREELEEAEQALDAAERELAQLQARldsLERLQEN 500
Rootletin pfam15035
Ciliary rootlet component, centrosome cohesion;
385-489 7.68e-04

Ciliary rootlet component, centrosome cohesion;


Pssm-ID: 464459 [Multi-domain]  Cd Length: 190  Bit Score: 40.79  E-value: 7.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 385 DACQLQEMRHELERANKNCRILQYRLRKAE-RKRLRYAQTGEIDGELLRSLEQDLKVAKDVSVRLHHELENV-----EEK 458
Cdd:pfam15035   5 QAYQEAQQRQAQLVQKLQAKVLQYKKRCSElEQQLLEKTSELEKTELLLRKLTLEPRLQRLEREHSADLEEAlirleEER 84

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958652023 459 R--TTTEDENEKLRQQLIEVEIAKQALQNELEK 489
Cdd:pfam15035  85 QrsESLSQVNSLLREQLEQASRANEALREDLQK 117
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 355-490 1.01e-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: 41.97  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023  355 KLREENETLKNEIDELRTEMDEMRDTFFEEDAcQLQEMRHELERANKNCRILQYRLRKAERKRLRYAQTgeidgelLRSL 434
Cdd:TIGR02168  772 EAEEELAEAEAEIEELEAQIEQLKEELKALRE-ALDELRAELTLLNEEAANLRERLESLERRIAATERR-------LEDL 843

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958652023  435 EQDLKVAKDVSVRLHHELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNELEKM 490
Cdd:TIGR02168  844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
357-493 1.39e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 357 REENETLKNEIDELRTEMDEMRDTF------FEEDACQLQEMRHELERANKNCRILQYRLRKAeRKRLRYAQtgeidgEL 430
Cdd:PRK02224  376 REAVEDRREEIEELEEEIEELRERFgdapvdLGNAEDFLEELREERDELREREAELEATLRTA-RERVEEAE------AL 448

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958652023 431 LRS-----LEQDLKVAKDVSVrlhheLENVEEKRTTTEDENEKLRQQLIEVEI----AKQA--LQNELEKMKEN 493
Cdd:PRK02224  449 LEAgkcpeCGQPVEGSPHVET-----IEEDRERVEELEAELEDLEEEVEEVEErlerAEDLveAEDRIERLEER 517
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 356-499 1.43e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 40.77  E-value: 1.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023  356 LREENETLKNEIDELRTEMDEMRDTFfeedacqlQEMRHELERankncrilqyrLRKAERkrlryaQTGEIDGELLRSLE 435
Cdd:smart00787 156 LKEDYKLLMKELELLNSIKPKLRDRK--------DALEEELRQ-----------LKQLED------ELEDCDPTELDRAK 210

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958652023  436 QDLKVAKDVSVRLHHELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNELEKMKENTLLRIS 499
Cdd:smart00787 211 EKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIE 274
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
355-492 1.77e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 355 KLREENETLKNEIDELRTEMDEM------------------RDTFFEEDACQLQEMRHELERANKNCRILQYRLRK---- 412
Cdd:PRK03918  409 KITARIGELKKEIKELKKAIEELkkakgkcpvcgrelteehRKELLEEYTAELKRIEKELKEIEEKERKLRKELRElekv 488

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 413 --AERKRLRYAQTGEidgeLLRSLEQDLKVakdvsvrlhHELENVEEKrtttEDENEKLRQQLIEVEIAKQALQNELEKM 490
Cdd:PRK03918  489 lkKESELIKLKELAE----QLKELEEKLKK---------YNLEELEKK----AEEYEKLKEKLIKLKGEIKSLKKELEKL 551


                  ..
gi 1958652023 491 KE 492
Cdd:PRK03918  552 EE 553
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
355-492 2.27e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 2.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 355 KLREENETLKNEIDELRTEMDEMrdtffEEDACQLQEMRHELERANKNCRILQYRLRKAERKRLRYAQTGEIDGELLRSL 434
Cdd:PRK03918  235 ELKEEIEELEKELESLEGSKRKL-----EEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDEL 309

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958652023 435 EqdlKVAKDVSvRLHHELENVEEKRTTTEDENEKLRqqliEVEIAKQALQNELEKMKE 492
Cdd:PRK03918  310 R---EIEKRLS-RLEEEINGIEERIKELEEKEERLE----ELKKKLKELEKRLEELEE 359
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 356-492 2.72e-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: 40.82  E-value: 2.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023  356 LREENETLKNEIDELRTEMDEMRDtffeedacQLQEMRHELERANKNCRILQYRLRKAERKRLRYAQTGEIDGELLRSLE 435
Cdd:TIGR02169  679 LRERLEGLKRELSSLQSELRRIEN--------RLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958652023  436 QDLKVAKDVSVRLHHELENVEEKRTTTEDENEKLRQQLIEVEIakQALQNELEKMKE 492
Cdd:TIGR02169  751 QEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI--PEIQAELSKLEE 805
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 356-497 3.06e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 40.49  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 356 LREENETLKNEIDELRTEMDEMRDtffEEDACQLQEMRH----ELERANKNCRILQ-------YRLRKAERKRLRYAQTG 424
Cdd:pfam17380 344 MERERELERIRQEERKRELERIRQ---EEIAMEISRMRElerlQMERQQKNERVRQeleaarkVKILEEERQRKIQQQKV 420

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958652023 425 E---IDGELLRSLEQDLKVAKDVSVRlhhELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNELEKMKENTLLR 497
Cdd:pfam17380 421 EmeqIRAEQEEARQREVRRLEEERAR---EMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQR 493
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 355-489 3.55e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 40.20  E-value: 3.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 355 KLREENETLKNEIDELR-------TEMDEMRDtfFEEdacQLQEMRHELER-----ANKNCR--ILQYRLRKAErKRLRY 420
Cdd:PRK04778  321 HAKEQNKELKEEIDRVKqsytlneSELESVRQ--LEK---QLESLEKQYDEiteriAEQEIAysELQEELEEIL-KQLEE 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 421 AQTGEID-GELLRSLEQDLKVAKDVSVRLHHELENVE---EKR-------------TTTEDENEKLRQQLIEVEIAKQAL 483
Cdd:PRK04778  395 IEKEQEKlSEMLQGLRKDELEAREKLERYRNKLHEIKrylEKSnlpglpedylemfFEVSDEIEALAEELEEKPINMEAV 474


                  ....*.
gi 1958652023 484 QNELEK 489
Cdd:PRK04778  475 NRLLEE 480
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
388-493 3.61e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 3.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023  388 QLQEMRHELERANKNCRILQYRLRKAERKRLRYAQTGEIDGELLRSLEQDLKVAkdvsvRLHHELENVEEKRTTTEDEN- 466
Cdd:COG4913    611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA-----SAEREIAELEAELERLDASSd 685

                           90       100
                   ....*....|....*....|....*....
gi 1958652023  467 --EKLRQQLIEVEIAKQALQNELEKMKEN 493
Cdd:COG4913    686 dlAALEEQLEELEAELEELEEELDELKGE 714
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
355-489 3.77e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 3.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023  355 KLREENETLKNEIDELRtEMDEMRDTFFEEDACQL-----QEMRHELERANKNCRILQYRLRKAERKRLR-YAQTGEIDG 428
Cdd:COG4913    259 ELAERYAAARERLAELE-YLRAALRLWFAQRRLELleaelEELRAELARLEAELERLEARLDALREELDElEAQIRGNGG 337

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958652023  429 ELLRSLEQDLKVA-------KDVSVRLHHELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNELEK 489
Cdd:COG4913    338 DRLEQLEREIERLereleerERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE 405
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 356-492 6.05e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 39.43  E-value: 6.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 356 LREENETLKNEIDELRTEMDEMRDT--FFEEDAC--QLQEMRHELERANKNcrILQYRLRKAErKRLRYAQTgEIDG--E 429
Cdd:PRK04778  221 LKELQTELPDQLQELKAGYRELVEEgyHLDHLDIekEIQDLKEQIDENLAL--LEELDLDEAE-EKNEEIQE-RIDQlyD 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 430 LLR--------------SLEQDLKVAKDVSVRLHHELENVEEKRTTTEDENEKLRQ------------QLIEVEIAKQA- 482
Cdd:PRK04778  297 ILErevkarkyveknsdTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESELESVRQlekqleslekqyDEITERIAEQEi 376

                         170
                  ....*....|....
gi 1958652023 483 ----LQNELEKMKE 492
Cdd:PRK04778  377 ayseLQEELEEILK 390
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
355-492 6.41e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 38.74  E-value: 6.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 355 KLREENETLKNEIDELRTEMDEMRDTFFEedacqLQEMRHELERANKNCRILQYRLRKAERKRlryaQTGEIDGEL---- 430
Cdd:COG1340    68 ELNEKVKELKEERDELNEKLNELREELDE-----LRKELAELNKAGGSIDKLRKEIERLEWRQ----QTEVLSPEEekel 138

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958652023 431 ---LRSLEQDLKVAKDvSVRLHHELENVEEKRTTTEDENEKLRQQLieVEIAKQAlQNELEKMKE 492
Cdd:COG1340   139 vekIKELEKELEKAKK-ALEKNEKLKELRAELKELRKEAEEIHKKI--KELAEEA-QELHEEMIE 199
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
358-493 6.97e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 6.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 358 EENETLKNEIDELRTEMDEMrdtffEEDACQLQEMRHELERANKNCRILQYRLRKAERK--RLRYAQTGEIDGELlRSLE 435
Cdd:PRK03918  525 EEYEKLKEKLIKLKGEIKSL-----KKELEKLEELKKKLAELEKKLDELEEELAELLKEleELGFESVEELEERL-KELE 598

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958652023 436 Q------DLKVAKdvsvrlhHELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNELEKMKEN 493
Cdd:PRK03918  599 PfyneylELKDAE-------KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK 655
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
355-492 7.59e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 7.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 355 KLREENETLKNEIDELRTEMDEMrdtffEEDACQLQEMRHELERANKNCRILQYRLRKAERKRlryaqtgeidgELLRSL 434
Cdd:PRK03918  311 EIEKRLSRLEEEINGIEERIKEL-----EEKEERLEELKKKLKELEKRLEELEERHELYEEAK-----------AKKEEL 374

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958652023 435 EQDLKVAKDVSV-RLHHELENVEEKRTTTEDENEKLRQQLIEVEIAKQALQNELEKMKE 492
Cdd:PRK03918  375 ERLKKRLTGLTPeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
355-490 9.90e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 9.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958652023 355 KLREENETLKNEIDELRTEMDEMRDTFFEEDACQLQEMRHELERANKNcriLQYRLRKAERKRlryaqtgeidGELLRSL 434
Cdd:PRK03918  630 KAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAG---LRAELEELEKRR----------EEIKKTL 696

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958652023 435 EqDLKVAKDVSVRLHHELENVEEKRTTTEDENEKLRQqlIEVEIAKQALqNELEKM 490
Cdd:PRK03918  697 E-KLKEELEEREKAKKELEKLEKALERVEELREKVKK--YKALLKERAL-SKVGEI 748
 
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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