NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1276346055|ref|NP_001344901|]
View 

trafficking kinesin-binding protein 1 isoform 5 [Mus musculus]

Protein Classification

trafficking kinesin-binding protein( domain architecture ID 12058656)

trafficking kinesin-binding protein such as human trafficking kinesin-binding protein 1 (TRAK1) that is involved in the regulation of endosome-to-lysosome trafficking, including endocytic trafficking of EGF-EGFR complexes and GABA-A receptors

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 1-249 4.36e-139

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


:

Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 403.64  E-value: 4.36e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055   1 MTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEE 80
Cdd:pfam04849  61 MTKTYNDIEAVTRLLEEKERDLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLLQIYSNDAEE 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  81 SEPESVCSTPLKRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVNDCVKELRDANVQIA 160
Cdd:pfam04849 141 SETESSCSTPLRRNESFSSLHGCVQLDALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQLMSDCVEQLSEANQQMA 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 161 SISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQ 240
Cdd:pfam04849 221 ELSEELARKMEENLRQQEEITSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQ 300


                  ....*....
gi 1276346055 241 EELKNLRNK 249
Cdd:pfam04849 301 EELKELRKK 309
Milton pfam12448
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ...
 308-476 5.03e-79

Kinesin associated protein; This domain family is found in eukaryotes, and is typically between 143 and 173 amino acids in length. The family is found in association with pfam04849. This family is a region of the protein milton. Milton recruits the heavy chain of kinesin to mitochondria to allow the motor movement function of kinesin.


:

Pssm-ID: 463588  Cd Length: 171  Bit Score: 244.88  E-value: 5.03e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 308 KQRSLTPSPMNIPGSNQSSAMNSLLSSCVSTPRSSFYGSDVSNVVLDNKTNSILLETEAADLGNEDHNKKPGTPGTPGSH 387
Cdd:pfam12448   1 RQRSLTPSPMNIPGSNQSSSLTSMRSSSSSTPRSSYYGGDGSSISLDNRTNSILSETSSSQDSGYDRPKKPGTPGTPGAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 388 DLETALRRLSLRRENYLSERRFFEEEQERKLRELAE----KGELHSGSLTPTESIMSLGTHSRfSEFTGFSGmsFSSRSY 463
Cdd:pfam12448  81 DLEAALRRLSLRRQNYLSERRFFEEERERKLLALAGtynyDEGEHGGSLTPNDSIMSLGSNHS-GSSSHSSG--FSSRSY 157

                         170
                  ....*....|...
gi 1276346055 464 LPEKLQIVKPLEG 476
Cdd:pfam12448 158 LPEKLQIVKPLEG 170
 
Name Accession Description Interval E-value
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 1-249 4.36e-139

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 403.64  E-value: 4.36e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055   1 MTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEE 80
Cdd:pfam04849  61 MTKTYNDIEAVTRLLEEKERDLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLLQIYSNDAEE 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  81 SEPESVCSTPLKRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVNDCVKELRDANVQIA 160
Cdd:pfam04849 141 SETESSCSTPLRRNESFSSLHGCVQLDALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQLMSDCVEQLSEANQQMA 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 161 SISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQ 240
Cdd:pfam04849 221 ELSEELARKMEENLRQQEEITSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQ 300


                  ....*....
gi 1276346055 241 EELKNLRNK 249
Cdd:pfam04849 301 EELKELRKK 309
Milton pfam12448
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ...
 308-476 5.03e-79

Kinesin associated protein; This domain family is found in eukaryotes, and is typically between 143 and 173 amino acids in length. The family is found in association with pfam04849. This family is a region of the protein milton. Milton recruits the heavy chain of kinesin to mitochondria to allow the motor movement function of kinesin.


Pssm-ID: 463588  Cd Length: 171  Bit Score: 244.88  E-value: 5.03e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 308 KQRSLTPSPMNIPGSNQSSAMNSLLSSCVSTPRSSFYGSDVSNVVLDNKTNSILLETEAADLGNEDHNKKPGTPGTPGSH 387
Cdd:pfam12448   1 RQRSLTPSPMNIPGSNQSSSLTSMRSSSSSTPRSSYYGGDGSSISLDNRTNSILSETSSSQDSGYDRPKKPGTPGTPGAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 388 DLETALRRLSLRRENYLSERRFFEEEQERKLRELAE----KGELHSGSLTPTESIMSLGTHSRfSEFTGFSGmsFSSRSY 463
Cdd:pfam12448  81 DLEAALRRLSLRRQNYLSERRFFEEERERKLLALAGtynyDEGEHGGSLTPNDSIMSLGSNHS-GSSSHSSG--FSSRSY 157

                         170
                  ....*....|...
gi 1276346055 464 LPEKLQIVKPLEG 476
Cdd:pfam12448 158 LPEKLQIVKPLEG 170
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 8-249 1.51e-12

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: 70.47  E-value: 1.51e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055    8 IDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPEsvc 87
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE--- 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055   88 stpLKRNESsssvqnyfHLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQL---VNDCVKELRDANVQIASISE 164
Cdd:TIGR02168  777 ---LAEAEA--------EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLrerLESLERRIAATERRLEDLEE 845

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  165 ELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDK-------YAECMEMLH 237
Cdd:TIGR02168  846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKrselrreLEELREKLA 925

                          250
                   ....*....|..
gi 1276346055  238 EAQEELKNLRNK 249
Cdd:TIGR02168  926 QLELRLEGLEVR 937
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 15-249 4.71e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.26  E-value: 4.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  15 LEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESVCSTPLKRN 94
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  95 ESSSSVQNYFHLDSLQKKLKDLEEEnvvLRSEACQLKTETITYEEKEQQLvNDCVKELRDANVQIASISEELAKKTEDAA 174
Cdd:COG1196   314 LEERLEELEEELAELEEELEELEEE---LEELEEELEEAEEELEEAEAEL-AEAEEALLEAEAELAEAEEELEELAEELL 389

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1276346055 175 RQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNK 249
Cdd:COG1196   390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
3-286 3.68e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.68  E-value: 3.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055   3 KTYNDIDAVTRLLEEKERDLElaarigqSLLKKNKTLTERNELLEEQVEHIREEVSQLRH------ELSMKDE----LLQ 72
Cdd:PRK03918  228 KEVKELEELKEEIEELEKELE-------SLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEeyikLSE 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  73 FYTSAAEESEPESVCSTPLkRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVN------ 146
Cdd:PRK03918  301 FYEEYLDELREIEKRLSRL-EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEElerlkk 379

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 147 --------DCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHlgAAKDAQRQL 218
Cdd:PRK03918  380 rltgltpeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEE--HRKELLEEY 457

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 219 TAELRELEDKYAECMEMLHEAQEELKNLRNKTMPTSRryhslgLFPMDSLAAEIEGTMRK--ELQLEELE 286
Cdd:PRK03918  458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESE------LIKLKELAEQLKELEEKlkKYNLEELE 521
 
Name Accession Description Interval E-value
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 1-249 4.36e-139

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 403.64  E-value: 4.36e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055   1 MTKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEE 80
Cdd:pfam04849  61 MTKTYNDIEAVTRLLEEKERDLELAARIGQSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLLQIYSNDAEE 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  81 SEPESVCSTPLKRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVNDCVKELRDANVQIA 160
Cdd:pfam04849 141 SETESSCSTPLRRNESFSSLHGCVQLDALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQLMSDCVEQLSEANQQMA 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 161 SISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQ 240
Cdd:pfam04849 221 ELSEELARKMEENLRQQEEITSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQ 300


                  ....*....
gi 1276346055 241 EELKNLRNK 249
Cdd:pfam04849 301 EELKELRKK 309
Milton pfam12448
Kinesin associated protein; This domain family is found in eukaryotes, and is typically ...
 308-476 5.03e-79

Kinesin associated protein; This domain family is found in eukaryotes, and is typically between 143 and 173 amino acids in length. The family is found in association with pfam04849. This family is a region of the protein milton. Milton recruits the heavy chain of kinesin to mitochondria to allow the motor movement function of kinesin.


Pssm-ID: 463588  Cd Length: 171  Bit Score: 244.88  E-value: 5.03e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 308 KQRSLTPSPMNIPGSNQSSAMNSLLSSCVSTPRSSFYGSDVSNVVLDNKTNSILLETEAADLGNEDHNKKPGTPGTPGSH 387
Cdd:pfam12448   1 RQRSLTPSPMNIPGSNQSSSLTSMRSSSSSTPRSSYYGGDGSSISLDNRTNSILSETSSSQDSGYDRPKKPGTPGTPGAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 388 DLETALRRLSLRRENYLSERRFFEEEQERKLRELAE----KGELHSGSLTPTESIMSLGTHSRfSEFTGFSGmsFSSRSY 463
Cdd:pfam12448  81 DLEAALRRLSLRRQNYLSERRFFEEERERKLLALAGtynyDEGEHGGSLTPNDSIMSLGSNHS-GSSSHSSG--FSSRSY 157

                         170
                  ....*....|...
gi 1276346055 464 LPEKLQIVKPLEG 476
Cdd:pfam12448 158 LPEKLQIVKPLEG 170
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 8-249 1.51e-12

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: 70.47  E-value: 1.51e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055    8 IDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPEsvc 87
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE--- 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055   88 stpLKRNESsssvqnyfHLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQL---VNDCVKELRDANVQIASISE 164
Cdd:TIGR02168  777 ---LAEAEA--------EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLrerLESLERRIAATERRLEDLEE 845

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  165 ELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDK-------YAECMEMLH 237
Cdd:TIGR02168  846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKrselrreLEELREKLA 925

                          250
                   ....*....|..
gi 1276346055  238 EAQEELKNLRNK 249
Cdd:TIGR02168  926 QLELRLEGLEVR 937
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-247 3.07e-10

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: 63.15  E-value: 3.07e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055    2 TKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEES 81
Cdd:TIGR02168  701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA 780

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055   82 EPESVCSTPLKRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQLKTETityEEKEQQLVnDCVKELRDANVQIAS 161
Cdd:TIGR02168  781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI---AATERRLE-DLEEQIEELSEDIES 856

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  162 ISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQE 241
Cdd:TIGR02168  857 LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV 936


                   ....*.
gi 1276346055  242 ELKNLR 247
Cdd:TIGR02168  937 RIDNLQ 942
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 15-249 4.71e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.26  E-value: 4.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  15 LEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESVCSTPLKRN 94
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  95 ESSSSVQNYFHLDSLQKKLKDLEEEnvvLRSEACQLKTETITYEEKEQQLvNDCVKELRDANVQIASISEELAKKTEDAA 174
Cdd:COG1196   314 LEERLEELEEELAELEEELEELEEE---LEELEEELEEAEEELEEAEAEL-AEAEEALLEAEAELAEAEEELEELAEELL 389

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1276346055 175 RQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNK 249
Cdd:COG1196   390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 105-286 4.75e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.10  E-value: 4.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 105 HLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVndcvKELRDANVQIASISEELAKKTEDAARQQEEITHLL 184
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELR----LELEELELELEEAQAEEYELLAELARLEQDIARLE 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 185 SQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNKTMPTSRRYHSLglfp 264
Cdd:COG1196   309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL---- 384

                         170       180
                  ....*....|....*....|..
gi 1276346055 265 MDSLAAEIEGTMRKELQLEELE 286
Cdd:COG1196   385 AEELLEALRAAAELAAQLEELE 406
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 15-249 1.12e-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: 54.69  E-value: 1.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055   15 LEEKERDLELAARIGQslLKKnktltERNELLEEQvEHIREEVSQLRHELS---------MKD-ELLQFYTSAA----EE 80
Cdd:TIGR02169  670 RSEPAELQRLRERLEG--LKR-----ELSSLQSEL-RRIENRLDELSQELSdasrkigeiEKEiEQLEQEEEKLkerlEE 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055   81 SEPE-SVCSTPLKRNESSssvqnyfhLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKE-QQLVNDCVKELRDANVQ 158
Cdd:TIGR02169  742 LEEDlSSLEQEIENVKSE--------LKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEiQAELSKLEEEVSRIEAR 813

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  159 IASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHE 238
Cdd:TIGR02169  814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893

                          250
                   ....*....|.
gi 1276346055  239 AQEELKNLRNK 249
Cdd:TIGR02169  894 LEAQLRELERK 904
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 16-248 1.70e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  16 EEKERDLELAarigqslLKKNKTLTERNELLEEQVEHIREEVSQLRHELsmkdellqfytsAAEESEpesvcstplkrne 95
Cdd:COG1196   221 ELKELEAELL-------LLKLRELEAELEELEAELEELEAELEELEAEL------------AELEAE------------- 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  96 ssssvqnyfhLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVndcvKELRDANVQIASISEELAKKTEDAAR 175
Cdd:COG1196   269 ----------LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE----ERRRELEERLEELEEELAELEEELEE 334

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1276346055 176 QQEEITHLLSQIVDLQKKAKSCAVENEELVQhlgAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRN 248
Cdd:COG1196   335 LEEELEELEEELEEAEEELEEAEAELAEAEE---ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 106-287 4.78e-07

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: 52.75  E-value: 4.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  106 LDSLQKKLKDLEEENVVLRSEACQLKTEtityEEKEQQLVNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLS 185
Cdd:TIGR02168  693 IAELEKALAELRKELEELEEELEQLRKE----LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  186 QIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNKTMPTSRRyhslglfpM 265
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR--------L 840

                          170       180
                   ....*....|....*....|..
gi 1276346055  266 DSLAAEIEgtmRKELQLEELES 287
Cdd:TIGR02168  841 EDLEEQIE---ELSEDIESLAA 859
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 13-249 6.79e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 6.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  13 RLLEEKERDLELAARIGQsLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPEsvcstplk 92
Cdd:COG1196   282 ELEEAQAEEYELLAELAR-LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE-------- 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  93 rnessssvqnyfhLDSLQKKLKDLEEEnvvlRSEACQLKTETITYEEKEQQLVNDCVKELRDANVQIASISEELAKKTED 172
Cdd:COG1196   353 -------------LEEAEAELAEAEEA----LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1276346055 173 AARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNK 249
Cdd:COG1196   416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 3-249 1.32e-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: 51.21  E-value: 1.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055    3 KTYNDIDAVTRLLEEKERDLELaarigqslLKKNKTLTERNELLEEQVEHIREEVSQLRHElSMKDELLQFYTSAAEESE 82
Cdd:TIGR02168  183 RTRENLDRLEDILNELERQLKS--------LERQAEKAERYKELKAELRELELALLVLRLE-ELREELEELQEELKEAEE 253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055   83 pesvcstplkrnessssvqnyfHLDSLQKKLKDLEEENVVLRSEACQLKTEtityEEKEQQLVNDCVKELRDANVQIASI 162
Cdd:TIGR02168  254 ----------------------ELEELTAELQELEEKLEELRLEVSELEEE----IEELQKELYALANEISRLEQQKQIL 307

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  163 SEELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEE 242
Cdd:TIGR02168  308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387


                   ....*..
gi 1276346055  243 LKNLRNK 249
Cdd:TIGR02168  388 VAQLELQ 394
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
3-286 3.68e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.68  E-value: 3.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055   3 KTYNDIDAVTRLLEEKERDLElaarigqSLLKKNKTLTERNELLEEQVEHIREEVSQLRH------ELSMKDE----LLQ 72
Cdd:PRK03918  228 KEVKELEELKEEIEELEKELE-------SLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEeyikLSE 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  73 FYTSAAEESEPESVCSTPLkRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVN------ 146
Cdd:PRK03918  301 FYEEYLDELREIEKRLSRL-EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEElerlkk 379

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 147 --------DCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHlgAAKDAQRQL 218
Cdd:PRK03918  380 rltgltpeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEE--HRKELLEEY 457

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 219 TAELRELEDKYAECMEMLHEAQEELKNLRNKTMPTSRryhslgLFPMDSLAAEIEGTMRK--ELQLEELE 286
Cdd:PRK03918  458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESE------LIKLKELAEQLKELEEKlkKYNLEELE 521
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 6-231 9.10e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 9.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055   6 NDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEEsepes 85
Cdd:COG1196   302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE----- 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  86 vcstplkrNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEAcQLKTETITYEEKEQQLvndcVKELRDANVQIASISEE 165
Cdd:COG1196   377 --------AEEELEELAEELLEALRAAAELAAQLEELEEAEE-ALLERLERLEEELEEL----EEALAELEEEEEEEEEA 443

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1276346055 166 LAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKdAQRQLTAELRELEDKYAE 231
Cdd:COG1196   444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA-ARLLLLLEAEADYEGFLE 508
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
15-195 9.48e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 9.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  15 LEEKERDLELAarigQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESVCSTPLKRN 94
Cdd:COG4717    73 LKELEEELKEA----EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERL 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  95 EssSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEqqlVNDCVKELRDANVQIASISEELAKKTEDAA 174
Cdd:COG4717   149 E--ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE---LQDLAEELEELQQRLAELEEELEEAQEELE 223

                         170       180
                  ....*....|....*....|.
gi 1276346055 175 RQQEEITHLLSQIVDLQKKAK 195
Cdd:COG4717   224 ELEEELEQLENELEAAALEER 244
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
19-260 1.48e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 1.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055   19 ERDLELAARIgQSLlKKNKTLTE--RNELLEEQ---------VEH------IREEVSQLRHELSMKDELLQFYTSAAEES 81
Cdd:COG4913    191 EKALRLLHKT-QSF-KPIGDLDDfvREYMLEEPdtfeaadalVEHfddlerAHEALEDAREQIELLEPIRELAERYAAAR 268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055   82 EpesvcstplkRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQLKTEtitYEEKEQQLvNDCVKELRDANVQIAS 161
Cdd:COG4913    269 E----------RLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAE---LERLEARL-DALREELDELEAQIRG 334

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  162 IS----EELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEE--------LVQHLGAAKDAQRQLTAELRELEDKY 229
Cdd:COG4913    335 NGgdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEefaalraeAAALLEALEEELEALEEALAEAEAAL 414

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1276346055  230 AECMEMLHEAQEELKNLRNKTMPTSRRYHSL 260
Cdd:COG4913    415 RDLRRELRELEAEIASLERRKSNIPARLLAL 445
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 8-311 1.69e-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: 47.76  E-value: 1.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055    8 IDAVTRLLEEKERDLELAArigqslLKKNKTLTERNELLEEqVEHIREEVSQLRHELSMKDELLQFYTSAAEESEpesvc 87
Cdd:TIGR02169  197 RQQLERLRREREKAERYQA------LLKEKREYEGYELLKE-KEALERQKEAIERQLASLEEELEKLTEEISELE----- 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055   88 stplKRNESSSSVqnyfhLDSLQKKLKDL-EEENVVLRSEACQLKTETI----TYEEKEQQLvNDCVKELRDANVQIASI 162
Cdd:TIGR02169  265 ----KRLEEIEQL-----LEELNKKIKDLgEEEQLRVKEKIGELEAEIAslerSIAEKEREL-EDAEERLAKLEAEIDKL 334

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  163 SEELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELreledkyaecmEMLHEAQEE 242
Cdd:TIGR02169  335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL-----------EKLKREINE 403

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276346055  243 LKNLRNKTMPTSRRYHSLGLFpmdsLAAEIEgtmRKELQLEELESPDITHQKRVFETVRNVNQVVKQRS 311
Cdd:TIGR02169  404 LKRELDRLQEELQRLSEELAD----LNAAIA---GIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
13-287 4.69e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 4.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  13 RLLEEKERdLELAARIGQSLLKKNKTLTErnelLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESvcstPLK 92
Cdd:PRK03918  443 RELTEEHR-KELLEEYTAELKRIEKELKE----IEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEE----KLK 513

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  93 RNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQ---LKTETITYEEKEQQL---VNDCVKELRDANVQIASISEEL 166
Cdd:PRK03918  514 KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKleeLKKKLAELEKKLDELeeeLAELLKELEELGFESVEELEER 593

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 167 AKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAEcmemlheaqEELKNL 246
Cdd:PRK03918  594 LKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE---------EEYEEL 664

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1276346055 247 RNKTMPTSRRYHSL--GLFPMDSLAAEIEGTMRK-ELQLEELES 287
Cdd:PRK03918  665 REEYLELSRELAGLraELEELEKRREEIKKTLEKlKEELEEREK 708
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
28-245 7.21e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 7.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055   28 IGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPEsvcstplkrnESSSSVQNyfHLD 107
Cdd:COG4913    604 LGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDE----------IDVASAER--EIA 671

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  108 SLQKKLKDLEEENVVLRseacQLKTEtityEEKEQQLVNDCVKELRDANVQIASISEELakktEDAARQQEEITHLLSQI 187
Cdd:COG4913    672 ELEAELERLDASSDDLA----ALEEQ----LEELEAELEELEEELDELKGEIGRLEKEL----EQAEEELDELQDRLEAA 739

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1276346055  188 VDLQKKAkscavENEELVQHLGAA------KDAQRQLTAELRELEDKYAECMEMLHEAQEELKN 245
Cdd:COG4913    740 EDLARLE-----LRALLEERFAAAlgdaveRELRENLEERIDALRARLNRAEEELERAMRAFNR 798
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 150-310 1.13e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.37  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 150 KELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKY 229
Cdd:COG4942    27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 230 AECMEML--HEAQEELKNLRNKTMP--TSRRYHSLGLFpMDSLAAEIEGTMRKELQLEELESpDITHQKRVFETVRNVNQ 305
Cdd:COG4942   107 AELLRALyrLGRQPPLALLLSPEDFldAVRRLQYLKYL-APARREQAEELRADLAELAALRA-ELEAERAELEALLAELE 184


                  ....*
gi 1276346055 306 VVKQR 310
Cdd:COG4942   185 EERAA 189
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
3-249 1.27e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055   3 KTYNDIDAVTRLLEEKERdlELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESe 82
Cdd:PRK03918  362 ELYEEAKAKKEELERLKK--RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKC- 438

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  83 peSVCSTPLKRNESSSSVQNY-FHLDSLQKKLKDLEEENVVLRSEACQLktETITYEEKEQQLVNDCVKELRDANVQIAS 161
Cdd:PRK03918  439 --PVCGRELTEEHRKELLEEYtAELKRIEKELKEIEEKERKLRKELREL--EKVLKKESELIKLKELAEQLKELEEKLKK 514

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 162 IS-EELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQ 240
Cdd:PRK03918  515 YNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERL 594


                  ....*....
gi 1276346055 241 EELKNLRNK 249
Cdd:PRK03918  595 KELEPFYNE 603
mukB PRK04863
chromosome partition protein MukB;
37-246 1.27e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 44.95  E-value: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055   37 KTLTERNEL------LEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESV--CSTPLKRNESSSSvqnyfHLDS 108
Cdd:PRK04863   841 QLNRRRVELeraladHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLADRVeeIREQLDEAEEAKR-----FVQQ 915

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  109 LQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLvndcvkelRDANVQIASISEELAKKT----EDAARQQEEITHLL 184
Cdd:PRK04863   916 HGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQ--------RDAKQQAFALTEVVQRRAhfsyEDAAEMLAKNSDLN 987

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1276346055  185 SQivdLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNL 246
Cdd:PRK04863   988 EK---LRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDL 1046
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 105-249 3.84e-04

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: 42.22  E-value: 3.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 105 HLDSLQKKLKDLEEENVVLRSEACQLKTEtitYEEKEQQLvNDCVKELRDANVQIASISEELAKKTE--DAARQQEEITH 182
Cdd:COG1579    18 ELDRLEHRLKELPAELAELEDELAALEAR---LEAAKTEL-EDLEKEIKRLELEIEEVEARIKKYEEqlGNVRNNKEYEA 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1276346055 183 LLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECM----EMLHEAQEELKNLRNK 249
Cdd:COG1579    94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKaeldEELAELEAELEELEAE 164
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
16-238 5.37e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 5.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  16 EEKERDLE-LAARIGQSLLKKNKTLTERNELLEEqVEHIREEVSQLRHELsmkDELLQfyTSAAEESEPESVCStplkrn 94
Cdd:PRK02224  247 EERREELEtLEAEIEDLRETIAETEREREELAEE-VRDLRERLEELEEER---DDLLA--EAGLDDADAEAVEA------ 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  95 essssvqnyfHLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLvNDCVKELRDanvQIASISEELAKKTEDAA 174
Cdd:PRK02224  315 ----------RREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL-EERAEELRE---EAAELESELEEAREAVE 380

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1276346055 175 RQQEEITHLLSQIVDLQKKAKSCAVE-------NEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHE 238
Cdd:PRK02224  381 DRREEIEELEEEIEELRERFGDAPVDlgnaedfLEELREERDELREREAELEATLRTARERVEEAEALLEA 451
PLN02939 PLN02939
transferase, transferring glycosyl groups
 26-239 5.48e-04

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 42.97  E-value: 5.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  26 ARIgQSLLKKNKTLTERnelleeqvEHIREEVSQLRHELSMKDEllQFYTSAAEESEPESVCSTPLK-RNE-SSSSVQNY 103
Cdd:PLN02939  150 ARL-QALEDLEKILTEK--------EALQGKINILEMRLSETDA--RIKLAAQEKIHVEILEEQLEKlRNElLIRGATEG 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 104 FHLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVNdCVKE--LRDANVQiasiseELAKKTEDAarqQEEIt 181
Cdd:PLN02939  219 LCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFK-LEKErsLLDASLR------ELESKFIVA---QEDV- 287

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1276346055 182 hllSQIVDLQKKAKSCAVENEELVqhLGAAKDAQRQLTAEL---RELEDKYAECMEMLHEA 239
Cdd:PLN02939  288 ---SKLSPLQYDCWWEKVENLQDL--LDRATNQVEKAALVLdqnQDLRDKVDKLEASLKEA 343
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 48-246 5.64e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.44  E-value: 5.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  48 EQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPEsvcstpLKRNESSssvqnyfhLDSLQKKLKDLEEENVVLRSEA 127
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ------LAALERR--------IAALARRIRALEQELAALEAEL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 128 CQLKTETITYEEKEQQLVNDCVKELRDANVQ------------------------IASISEELAKKTEDAARQQEEITHL 183
Cdd:COG4942    86 AELEKEIAELRAELEAQKEELAELLRALYRLgrqpplalllspedfldavrrlqyLKYLAPARREQAEELRADLAELAAL 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1276346055 184 LSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNL 246
Cdd:COG4942   166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
106-249 6.50e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 6.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 106 LDSLQKKLKDLEEENVVLRSEACQLktetityeEKEQQLVNDcVKELRDANVQIASISEELakktEDAARQQEEITHLLS 185
Cdd:COG4717    97 LEELEEELEELEAELEELREELEKL--------EKLLQLLPL-YQELEALEAELAELPERL----EELEERLEELRELEE 163

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1276346055 186 QIVDLQKKAKSCAVENEELVQHLGAAKDAQ--------RQLTAELRELEDKYAECMEMLHEAQEELKNLRNK 249
Cdd:COG4717   164 ELEELEAELAELQEELEELLEQLSLATEEElqdlaeelEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 3-196 8.96e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 8.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055   3 KTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSmkdELLQFYTSAAEESE 82
Cdd:COG4942    45 ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA---ELLRALYRLGRQPP 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  83 PESVcstpLKRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVNDCVKELRDANVQIASI 162
Cdd:COG4942   122 LALL----LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAER 197

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1276346055 163 SEELAKKTEDAARQQEEITHLLSQIVDLQKKAKS 196
Cdd:COG4942   198 QKLLARLEKELAELAAELAELQQEAEELEALIAR 231
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 6-196 1.48e-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: 40.90  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055   6 NDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELS--------MKDELLQF---- 73
Cdd:COG4942    34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAelraeleaQKEELAELlral 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  74 YTSAAEESEPESVCSTPLKRNESSSSVQNYF------HLDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQL--- 144
Cdd:COG4942   114 YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLaparreQAEELRADLAELAALRAELEAERAELEALLAELEEERAALeal 193

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1276346055 145 VNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKS 196
Cdd:COG4942   194 KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 106-249 1.65e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 106 LDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVNDCVKELRDANVQIASIS--EEL--AKKTEDAARQQEEIT 181
Cdd:COG3883    46 LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSylDVLlgSESFSDFLDRLSALS 125

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1276346055 182 HLLSQ---IVDLQKKAKscavenEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNK 249
Cdd:COG3883   126 KIADAdadLLEELKADK------AELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
47-287 1.68e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  47 EEQVEHIREEVSQLRHELSMKDELLQFYTSAAE-ESEPESvcstpLKRNESSSSVQNYFHLDSLQKKLKDLEEenvvLRS 125
Cdd:PRK02224  474 RERVEELEAELEDLEEEVEEVEERLERAEDLVEaEDRIER-----LEERREDLEELIAERRETIEEKRERAEE----LRE 544

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 126 EACQLKTETITYEEKEQQL---VNDCVKELRDANVQIASISEELaKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENE 202
Cdd:PRK02224  545 RAAELEAEAEEKREAAAEAeeeAEEAREEVAELNSKLAELKERI-ESLERIRTLLAAIADAEDEIERLREKREALAELND 623

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 203 ELVQHLGAAKDAQRQLTAE-----LRELEDKYAECMEMLHEAQEELKNLRNKTmptsrryhslglfpmDSLAAEIEGTmr 277
Cdd:PRK02224  624 ERRERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREER---------------DDLQAEIGAV-- 686

                         250
                  ....*....|
gi 1276346055 278 kELQLEELES 287
Cdd:PRK02224  687 -ENELEELEE 695
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
10-246 1.77e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  10 AVTRLLEEKERDLE-LAARIGQsllKKNKTLTER-NEL------LEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEES 81
Cdd:PRK02224  177 GVERVLSDQRGSLDqLKAQIEE---KEEKDLHERlNGLeselaeLDEEIERYEEQREQARETRDEADEVLEEHEERREEL 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  82 EP---------ESVCSTPLKRNESSSSVQnyfhldSLQKKLKDLEEENVVLRSEAcqlktetiTYEEKEQQLVNDCVKEL 152
Cdd:PRK02224  254 ETleaeiedlrETIAETEREREELAEEVR------DLRERLEELEEERDDLLAEA--------GLDDADAEAVEARREEL 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 153 RDanvQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAEC 232
Cdd:PRK02224  320 ED---RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEEL 396

                         250
                  ....*....|....
gi 1276346055 233 MEMLHEAQEELKNL 246
Cdd:PRK02224  397 RERFGDAPVDLGNA 410
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 15-295 1.78e-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: 41.25  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  15 LEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDEllqfytsaAEESEPESVCSTPLKRN 94
Cdd:pfam05483 515 LKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLD--------KSEENARSIEYEVLKKE 586

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  95 ESSSSVQNYFH-----LDSLQKKLKDLEEENVVLRSEAC--------------QLKTETITYEEKEQQLVNDCVKELRDA 155
Cdd:pfam05483 587 KQMKILENKCNnlkkqIENKNKNIEELHQENKALKKKGSaenkqlnayeikvnKLELELASAKQKFEEIIDNYQKEIEDK 666

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 156 NVQIASISEELAKK---TEDAARQQEEI----THLLSQIVDLQKKAKSCAVE-NEELVQHLGAAKDAQRQLTAELRELEd 227
Cdd:pfam05483 667 KISEEKLLEEVEKAkaiADEAVKLQKEIdkrcQHKIAEMVALMEKHKHQYDKiIEERDSELGLYKNKEQEQSSAKAALE- 745

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1276346055 228 kyaecmemlheaqEELKNLRNKTMPTSRRYhslglfpmdslaaEIEGTMRKELQLEELESPDITHQKR 295
Cdd:pfam05483 746 -------------IELSNIKAELLSLKKQL-------------EIEKEEKEKLKMEAKENTAILKDKK 787
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
8-243 2.17e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055   8 IDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHEL-SMKDELLQFYTSAAE-----ES 81
Cdd:PRK02224  316 REELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELeEAREAVEDRREEIEEleeeiEE 395

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  82 EPESVCSTPLKRNESSSsvqnyfHLDSLQKKLKDLEEENVVLRSEacqLKTETITYEEKEQ-----------QLVNDC-- 148
Cdd:PRK02224  396 LRERFGDAPVDLGNAED------FLEELREERDELREREAELEAT---LRTARERVEEAEAlleagkcpecgQPVEGSph 466

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 149 VKELRDANVQIASISEELakktEDAARQQEEITHLLSQIVDLqkkakscaVENEELVQHLGAAKDAQRQLTAELRELEDK 228
Cdd:PRK02224  467 VETIEEDRERVEELEAEL----EDLEEEVEEVEERLERAEDL--------VEAEDRIERLEERREDLEELIAERRETIEE 534

                         250
                  ....*....|....*
gi 1276346055 229 YAECMEMLHEAQEEL 243
Cdd:PRK02224  535 KRERAEELRERAAEL 549
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 106-285 2.21e-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: 40.52  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 106 LDSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQL---VNDCVKELRDANVQIASISEELAKKTEDAARQ------ 176
Cdd:COG4942    36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALeqeLAALEAELAELEKEIAELRAELEAQKEELAELlralyr 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 177 ---QEEITHLLSQ--IVDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKYAECMEMLHEAQEELKNL----- 246
Cdd:COG4942   116 lgrQPPLALLLSPedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALealka 195

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1276346055 247 -RNKTMPTSRRyhslglfPMDSLAAEIEGTMRKELQLEEL 285
Cdd:COG4942   196 eRQKLLARLEK-------ELAELAAELAELQQEAEELEAL 228
COG5022 COG5022
Myosin heavy chain [General function prediction only];
13-249 2.64e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 40.83  E-value: 2.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055   13 RLLEEKERDL---ELAARIGQSLLKKNKTLTERNELLEEQ----VEHIREEVSQLRHELSMKDEL-LQFYTSAAEESEpe 84
Cdd:COG5022    833 RETEEVEFSLkaeVLIQKFGRSLKAKKRFSLLKKETIYLQsaqrVELAERQLQELKIDVKSISSLkLVNLELESEIIE-- 910

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055   85 svcstpLKRNESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQL--KTETITYEEKEQQLvNDCVKELRDANVQIASI 162
Cdd:COG5022    911 ------LKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYvkLPELNKLHEVESKL-KETSEEYEDLLKKSTIL 983

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  163 SEELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEElVQHLGAAKDAQRQLTAELR---ELEDKYAECMEMLHEA 239
Cdd:COG5022    984 VREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVE-VAELQSASKIISSESTELSilkPLQKLKGLLLLENNQL 1062

                          250
                   ....*....|
gi 1276346055  240 QEELKNLRNK 249
Cdd:COG5022   1063 QARYKALKLR 1072
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
111-249 2.99e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 111 KKLKDLEEENVVLRSEACQLKTETITYEEKEQQLVN---------------DCVKELRDANVQIASISEELA---KKTED 172
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEEleaeleelreeleklEKLLQLLPLYQELEALEAELAelpERLEE 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1276346055 173 AARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQ-RQLTAELRELEDKYAECMEMLHEAQEELKNLRNK 249
Cdd:COG4717   151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
3-284 3.77e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 3.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055   3 KTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESE 82
Cdd:PRK03918  162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIE 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  83 pesvcstPLKRNESsssvqnyfhldSLQKKLKDLEEENVVLRSEACQLKTETITYEEKEQQLvndcvKELRDANVQIASI 162
Cdd:PRK03918  242 -------ELEKELE-----------SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-----KELKEKAEEYIKL 298

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 163 SEELAKKTEDAARQQEEITHLLSQIVDLQKKAKscavENEELVQHLGAAKDAQRQLTAELRELEdKYAECMEMLHEAQEE 242
Cdd:PRK03918  299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIK----ELEEKEERLEELKKKLKELEKRLEELE-ERHELYEEAKAKKEE 373

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1276346055 243 LKNLRNKtmptsrryhsLGLFPMDSLAAEIEGTMRKELQLEE 284
Cdd:PRK03918  374 LERLKKR----------LTGLTPEKLEKELEELEKAKEEIEE 405
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2-251 3.90e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055   2 TKTYNDIDAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEeQVEHIREEVSQLR-HELSMKDELLQFYTSAAEE 80
Cdd:PRK03918  458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAE-QLKELEEKLKKYNlEELEKKAEEYEKLKEKLIK 536

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  81 SEPE-SVCSTPLKRNESSSSvqnyfHLDSLQKKLKDLEEENVVLRSEACQLKTETIT-YEEKEQQL---------VNDCV 149
Cdd:PRK03918  537 LKGEiKSLKKELEKLEELKK-----KLAELEKKLDELEEELAELLKELEELGFESVEeLEERLKELepfyneyleLKDAE 611

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 150 KELRDANVQIASISEELAKKTEDAARQQEEITHLLSQIVDLQKKAKScaVENEELVQHLGAAKDAQRQLTAELRELEDKY 229
Cdd:PRK03918  612 KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRR 689

                         250       260
                  ....*....|....*....|..
gi 1276346055 230 AECMEMLHEAQEELKNLRNKTM 251
Cdd:PRK03918  690 EEIKKTLEKLKEELEEREKAKK 711
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 12-246 4.36e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 39.95  E-value: 4.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055   12 TRLLEEKERDLELAARIGQsllkknKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESvcsTPL 91
Cdd:TIGR00618  653 LTLTQERVREHALSIRVLP------KELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREF---NEI 723

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055   92 KRNESSSSVQNYFHLDSLQKKLKDLEEEnvvlrsEACQLKTETITYEEKEQQLVndcVKELRDANVQiasiseELAKKTE 171
Cdd:TIGR00618  724 ENASSSLGSDLAAREDALNQSLKELMHQ------ARTVLKARTEAHFNNNEEVT---AALQTGAELS------HLAAEIQ 788

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  172 DAARQQEEITHLLSQI-VDLQKKAKS----CAVENEELVQHLGAAKDAQRQLTA---ELRELEDKYAECMEMLHEAQEEL 243
Cdd:TIGR00618  789 FFNRLREEDTHLLKTLeAEIGQEIPSdediLNLQCETLVQEEEQFLSRLEEKSAtlgEITHQLLKYEECSKQLAQLTQEQ 868


                   ...
gi 1276346055  244 KNL 246
Cdd:TIGR00618  869 AKI 871
PRK12704 PRK12704
phosphodiesterase; Provisional
 103-251 4.37e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 4.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 103 YFHLDSLQKKLKDLEEENVVLRSEAcQLKTETITYE------EKEQQLVNDCVKELRDANVQIASISEELAKKTEDAARQ 176
Cdd:PRK12704   23 FVRKKIAEAKIKEAEEEAKRILEEA-KKEAEAIKKEalleakEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRK 101

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1276346055 177 QEEITHllsqivdlqkkakscavENEELVQHlgaakdaQRQLTAELRELEDKYAECMEMLHEAQEELKNLRNKTM 251
Cdd:PRK12704  102 LELLEK-----------------REEELEKK-------EKELEQKQQELEKKEEELEELIEEQLQELERISGLTA 152
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
150-310 4.88e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 4.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 150 KELRDANVQIasisEELAKKTEDAARQQEEITHLLSQIVDLQKKAKSCAVENEELVQHLGAAKDAQR--QLTAELRELED 227
Cdd:COG4717    71 KELKELEEEL----KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEleALEAELAELPE 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 228 KYAEcmemLHEAQEELKNLRNKtmptsrryhslglfpMDSLAAEIEgTMRKELQlEELESPDITHQKRVFETVRNVNQVV 307
Cdd:COG4717   147 RLEE----LEERLEELRELEEE---------------LEELEAELA-ELQEELE-ELLEQLSLATEEELQDLAEELEELQ 205


                  ...
gi 1276346055 308 KQR 310
Cdd:COG4717   206 QRL 208
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 9-243 6.02e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 39.44  E-value: 6.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055    9 DAVTRLLEEKERDLELAARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEPESVCS 88
Cdd:pfam12128  269 SDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQ 348

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055   89 TPLKRNESSSSVQNyfhLDSLQKKLKDLEEEnvvlrseacqlktetitYEEKEQQLVNDCVKElrdanvqIASISEELAK 168
Cdd:pfam12128  349 LPSWQSELENLEER---LKALTGKHQDVTAK-----------------YNRRRSKIKEQNNRD-------IAGIKDKLAK 401

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  169 KTEDAARQQEEITHLLSQI-----VDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKyAECMEMLHEAQEEL 243
Cdd:pfam12128  402 IREARDRQLAVAEDDLQALeselrEQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQL-ENFDERIERAREEQ 480
ATG17_like pfam04108
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ...
 47-229 8.41e-03

Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.


Pssm-ID: 427715 [Multi-domain]  Cd Length: 360  Bit Score: 38.52  E-value: 8.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  47 EEQVEHIREEVSQLRHEL-----SMKDELLQFYTSAAEesePESVCSTPLKRNESSSSVQNYFH-LDSLQKKLKDLeeen 120
Cdd:pfam04108 111 EDSVEILRDALKELIDELqaaqeSLDSDLKRFDDDLRD---LQKELESLSSPSESISLIPTLLKeLESLEEEMASL---- 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 121 vvLRS-----EACQL--------KTETITYEEKEQQLVNDCVKELRDANVQIASISEELAKKTEDAARQQEEITHLLSQI 187
Cdd:pfam04108 184 --LESltnhyDQCVTavklteggRAEMLEVLENDARELDDVVPELQDRLDEMENNYERLQKLLEQKNSLIDELLSALQLI 261

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1276346055 188 VDLQKKAKSCAVENEELVQHLGAAKDAQRQLTAELRELEDKY 229
Cdd:pfam04108 262 AEIQSRLPEYLAALKEFEERWEEEKETIEDYLSELEDLREFY 303
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 149-249 8.87e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 38.76  E-value: 8.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055 149 VKELRDAN-VQIASISEEL-AKKTEDAARQQEEITHLLSQIVDLQKKAKScaVENEELVQHLGAAKDAQRQLTAELRELE 226
Cdd:PRK05771   22 LEALHELGvVHIEDLKEELsNERLRKLRSLLTKLSEALDKLRSYLPKLNP--LREEKKKVSVKSLEELIKDVEEELEKIE 99

                          90       100
                  ....*....|....*....|...
gi 1276346055 227 DKYAECMEMLHEAQEELKNLRNK 249
Cdd:PRK05771  100 KEIKELEEEISELENEIKELEQE 122
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 13-181 9.11e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 37.98  E-value: 9.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  13 RLLEEKERDLELA--ARIGQSLLKKNKTLTERNELLEEQVEHIREEVSQLRHELSMKDELLQFYTSAAEESEpesvcstp 90
Cdd:COG1579     8 ALLDLQELDSELDrlEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE-------- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276346055  91 lkrnESSSSVQNYFHLDSLQKKLKDLEEENVVLRSEACQLKTEtityEEKEQQLVNDCVKELRDANVQIASISEELAKKT 170
Cdd:COG1579    80 ----EQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMER----IEELEEELAELEAELAELEAELEEKKAELDEEL 151

                         170
                  ....*....|.
gi 1276346055 171 EDAARQQEEIT 181
Cdd:COG1579   152 AELEAELEELE 162
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH