|
Name |
Accession |
Description |
Interval |
E-value |
| Nuf2 |
pfam03800 |
Nuf2 family; Members of this family are components of the mitotic spindle. It has been shown ... |
5-148 |
1.17e-46 |
|
Nuf2 family; Members of this family are components of the mitotic spindle. It has been shown that Nuf2 from yeast is part of a complex called the Ndc80p complex. This complex is thought to bind to the microtubules of the spindle. An arabidopsis protein has been included in this family that has previously not been identified as a member of this family, Swiss:Q9C953. The match is not strong, but in common with other members of this family contains coiled-coil to the C terminus of this region.
Pssm-ID: 461057 Cd Length: 139 Bit Score: 157.71 E-value: 1.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 5 QDVFPILDLQELVICLQSCDFAlATQENISRPTSDYMVTLYKQIIENFMGISVESLLnssnQETGDGHLQEENENIYLDT 84
Cdd:pfam03800 1 KDSFPRLSVDEIVACLRELGIP-VTEEDLKKPTPDFVQKLYERFLELLMGITREDIE----PPQLAAAALLEYPELHEDS 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324503 85 LNVLVLNKICFKFFENIGVQDFNMTDLYKPEAQRTQRLLSAVVNYARFREERMFDCNSFILQME 148
Cdd:pfam03800 76 LPLLNLYRHLKRFLKACGVDDFSLKDLLKPDPKRTRRILSALINFARFREERLELYDELLEESE 139
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
144-414 |
6.29e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 6.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 144 ILQMESLLGQLRS---KFDDYNL--IQQQLKQYEDV-------DGDNIPDEQELQKLEEQNKELEIQLKKLTKIQETLSi 211
Cdd:PRK03918 495 LIKLKELAEQLKEleeKLKKYNLeeLEKKAEEYEKLkekliklKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELA- 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 212 dyNDYKISKQSIFKDLEALSFQIVELESNRDKLIkisntdmeELSEGIKELNDLLIQRKKTLDDLTAQQKNLQDTVTTFE 291
Cdd:PRK03918 574 --ELLKELEELGFESVEELEERLKELEPFYNEYL--------ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 292 TIISELYDVLRIISSEVQEsnrtetelvglkqNLINNKLKLMNVLEtGIMYKLEILQEQLDLQLKNLEKLSQDTKE-ESR 370
Cdd:PRK03918 644 ELRKELEELEKKYSEEEYE-------------ELREEYLELSRELA-GLRAELEELEKRREEIKKTLEKLKEELEErEKA 709
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 6324503 371 LNDTKLMDLQIKYENEIKPKIDKTDIFIQEELISgKINKLNDEI 414
Cdd:PRK03918 710 KKELEKLEKALERVEELREKVKKYKALLKERALS-KVGEIASEI 752
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
107-388 |
8.35e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 8.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 107 NMTDLYKPEAQRTQRLLSAVVNYARFREERMFDCNSFILQMESLLGQLRSKfddynlIQQQLKQYEDVDGDNIPDEQELQ 186
Cdd:TIGR02168 712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE------IEELEERLEEAEEELAEAEAEIE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 187 KLEEQNKELEIQLKKLTKIQETLSIDYNDYKISKQSIFKDLEALSFQIVELESNRDKLIKISntdmEELSEGIKELNDLL 266
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI----EELSEDIESLAAEI 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 267 IQRKKTLDDLTAQQKNLQDTVTTFETIISELYDVLRIISSEVQESNRTETELVGLKQNL--INNKLKL-MNVLETGIMYK 343
Cdd:TIGR02168 862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELreKLAQLELrLEGLEVRIDNL 941
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 6324503 344 LEILQEQLDLQLKNLEKLSQDTKEESRLNDTKLMDLqikyENEIK 388
Cdd:TIGR02168 942 QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRL----ENKIK 982
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
182-310 |
1.03e-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: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 182 EQELQKLEEQNKELEIQLKKLTKIQETLSIDYNDYKISKQSIF--KDLEALSFQIVELESNRDKLIKiSNTDMEELSEGI 259
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWdeIDVASAEREIAELEAELERLDA-SSDDLAALEEQL 694
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 6324503 260 KELNDLLIQRKKTLDDLTAQQKNLQDTVTTFETIISELYDVLRIISSEVQE 310
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Nuf2 |
pfam03800 |
Nuf2 family; Members of this family are components of the mitotic spindle. It has been shown ... |
5-148 |
1.17e-46 |
|
Nuf2 family; Members of this family are components of the mitotic spindle. It has been shown that Nuf2 from yeast is part of a complex called the Ndc80p complex. This complex is thought to bind to the microtubules of the spindle. An arabidopsis protein has been included in this family that has previously not been identified as a member of this family, Swiss:Q9C953. The match is not strong, but in common with other members of this family contains coiled-coil to the C terminus of this region.
Pssm-ID: 461057 Cd Length: 139 Bit Score: 157.71 E-value: 1.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 5 QDVFPILDLQELVICLQSCDFAlATQENISRPTSDYMVTLYKQIIENFMGISVESLLnssnQETGDGHLQEENENIYLDT 84
Cdd:pfam03800 1 KDSFPRLSVDEIVACLRELGIP-VTEEDLKKPTPDFVQKLYERFLELLMGITREDIE----PPQLAAAALLEYPELHEDS 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324503 85 LNVLVLNKICFKFFENIGVQDFNMTDLYKPEAQRTQRLLSAVVNYARFREERMFDCNSFILQME 148
Cdd:pfam03800 76 LPLLNLYRHLKRFLKACGVDDFSLKDLLKPDPKRTRRILSALINFARFREERLELYDELLEESE 139
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
144-414 |
6.29e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 6.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 144 ILQMESLLGQLRS---KFDDYNL--IQQQLKQYEDV-------DGDNIPDEQELQKLEEQNKELEIQLKKLTKIQETLSi 211
Cdd:PRK03918 495 LIKLKELAEQLKEleeKLKKYNLeeLEKKAEEYEKLkekliklKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELA- 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 212 dyNDYKISKQSIFKDLEALSFQIVELESNRDKLIkisntdmeELSEGIKELNDLLIQRKKTLDDLTAQQKNLQDTVTTFE 291
Cdd:PRK03918 574 --ELLKELEELGFESVEELEERLKELEPFYNEYL--------ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 292 TIISELYDVLRIISSEVQEsnrtetelvglkqNLINNKLKLMNVLEtGIMYKLEILQEQLDLQLKNLEKLSQDTKE-ESR 370
Cdd:PRK03918 644 ELRKELEELEKKYSEEEYE-------------ELREEYLELSRELA-GLRAELEELEKRREEIKKTLEKLKEELEErEKA 709
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 6324503 371 LNDTKLMDLQIKYENEIKPKIDKTDIFIQEELISgKINKLNDEI 414
Cdd:PRK03918 710 KKELEKLEKALERVEELREKVKKYKALLKERALS-KVGEIASEI 752
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
107-388 |
8.35e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 8.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 107 NMTDLYKPEAQRTQRLLSAVVNYARFREERMFDCNSFILQMESLLGQLRSKfddynlIQQQLKQYEDVDGDNIPDEQELQ 186
Cdd:TIGR02168 712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE------IEELEERLEEAEEELAEAEAEIE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 187 KLEEQNKELEIQLKKLTKIQETLSIDYNDYKISKQSIFKDLEALSFQIVELESNRDKLIKISntdmEELSEGIKELNDLL 266
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI----EELSEDIESLAAEI 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 267 IQRKKTLDDLTAQQKNLQDTVTTFETIISELYDVLRIISSEVQESNRTETELVGLKQNL--INNKLKL-MNVLETGIMYK 343
Cdd:TIGR02168 862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELreKLAQLELrLEGLEVRIDNL 941
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 6324503 344 LEILQEQLDLQLKNLEKLSQDTKEESRLNDTKLMDLqikyENEIK 388
Cdd:TIGR02168 942 QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRL----ENKIK 982
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
182-310 |
1.03e-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: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 182 EQELQKLEEQNKELEIQLKKLTKIQETLSIDYNDYKISKQSIF--KDLEALSFQIVELESNRDKLIKiSNTDMEELSEGI 259
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWdeIDVASAEREIAELEAELERLDA-SSDDLAALEEQL 694
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 6324503 260 KELNDLLIQRKKTLDDLTAQQKNLQDTVTTFETIISELYDVLRIISSEVQE 310
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
182-380 |
1.32e-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: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 182 EQELQKLEEQNKELEIQLKKLTKIQETLSIDYNDYKISKQSIFKDLEALSFQIVELESNRDKL----------IKISNTD 251
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLeeriaqlskeLTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 252 MEELSEGIKELNDLLIQRKKTLDDLTAQQKNLQDTVTTFETIISELYDVLRIISSEVQ-----------ESNRTETELVG 320
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAnlrerleslerRIAATERRLED 842
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 321 LKQNLINNKLKLMNVleTGIMYKLEILQEQLDLQLKNLEKLSQDTKEESRLNDTKLMDLQ 380
Cdd:TIGR02168 843 LEEQIEELSEDIESL--AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
182-420 |
7.18e-05 |
|
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: 44.75 E-value: 7.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 182 EQELQKLEEQNKELEIQLKKLTKiqetlsidyndykiSKQSIFKDLEALSFQIVELEsnrdKLIKISNTDMEELSEGIKE 261
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKK--------------EEKALLKQLAALERRIAALA----RRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 262 LNDlliQRKKTLDDLTAQQKNLQDTVTTFETIISELYDVLRIISSEVQESNRTETELVGLKQNLINNKLKLMNVLEtgim 341
Cdd:COG4942 88 LEK---EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA---- 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6324503 342 yKLEILQEQLDLQLKNLEKLsQDTKEESRLNDTKLMDLQIKYENEIKPKIDKTDIFIQEelISGKINKLNDEIKQLQKD 420
Cdd:COG4942 161 -ELAALRAELEAERAELEAL-LAELEEERAALEALKAERQKLLARLEKELAELAAELAE--LQQEAEELEALIARLEAE 235
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
144-418 |
1.13e-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: 44.66 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 144 ILQMESLLGQLRSKFDDYNLIQQQLKQYEDvdgdnipdeqELQKLEEQNKELEIQLKKLTKIQETLSIDYNDYKISKQSI 223
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTA----------ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 224 FKDLEALSFQIVELESNRDKLikisNTDMEELSEGIKELNDLLIQRKKTLDDLTAQQKNLQDTVTTFETIISELydVLRI 303
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEEL----EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL--ESRL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 304 ISSEVQ-ESNRTETELVGLKQNLINNKLKLMNVLETGIMYKLEILQEQLDLQLKNLEKLS-QDTKEESRLNDTKLMDLQI 381
Cdd:TIGR02168 375 EELEEQlETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQE 454
|
250 260 270
....*....|....*....|....*....|....*..
gi 6324503 382 KYENEIKPKIDKTDifiQEELISGKINKLNDEIKQLQ 418
Cdd:TIGR02168 455 ELERLEEALEELRE---ELEEAEQALDAAERELAQLQ 488
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
146-380 |
1.24e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 146 QMESLLGQLRSKFDDYNL-IQQQLKQYEDVDGDNIPDEQELQKLEEQNKELEIQLKKLTKIQETLSidyndykiskqsif 224
Cdd:COG1196 264 ELEAELEELRLELEELELeLEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE-------------- 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 225 KDLEALSFQIVELESNRDKLIKISNTDMEELSEGIKELNDLLIQRKKTLDDLTAQQKNLQDTVTTFETIISELYDVLRII 304
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324503 305 SSEVQESNRTETELVGLKQNLINNKLKLMNVLETGImyKLEILQEQLDLQLKNLEKLSQDTKEESRLNDTKLMDLQ 380
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALE--EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
|
| COG5391 |
COG5391 |
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ... |
161-364 |
3.16e-04 |
|
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only];
Pssm-ID: 227680 [Multi-domain] Cd Length: 524 Bit Score: 42.86 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 161 YNLIQQQLKQYEDVDGDNIPD-EQELQKLEEQNKELEIQLKKLtkIQETLSIDYNDYKISKQS--------------IFK 225
Cdd:COG5391 253 STLLSSFIENRKSVPTPLSLDlTSTTQELDMERKELNESTSKA--IHNILSIFSLFEKILIQLeseeesltrlleslNNL 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 226 DLEALSFQIVE---LESNRDKLIKISNTDMEELSEGIKELNDLLIQRKKTLDDLTAQQKNLQDTVTTFETIISELYDVLR 302
Cdd:COG5391 331 LLLVLNFSGVFakrLEQNQNSILNEGVVQAETLRSSLKELLTQLQDEIKSRESLILTDSNLEKLTDQNLEDVEELSRSLR 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6324503 303 IISSevQESNRTETELVGLKQNLINNKLKLMNVlETGIMYKLEILQEQLDLQLKNLEKLSQD 364
Cdd:COG5391 411 KNSS--QRAVVSQQPEGLTSFSKLSYKLRDFVQ-EKSRSKSIESLQQDKEKLEEQLAIAEKD 469
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
164-419 |
2.41e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 164 IQQQLKQYEDVDGDNIPDEQELQKLEEQNKELEIQLKKLTKIQETLSIDYNDY----------KISKQSIFKDLEALSFQ 233
Cdd:PRK03918 181 LEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELeelkeeieelEKELESLEGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 234 IVELESNRDKLIKisntDMEELSEGIKELNDL------LIQRKKTLDDLTAQQKNLQDTVTTFETIISELYDVLRIISSE 307
Cdd:PRK03918 261 IRELEERIEELKK----EIEELEEKVKELKELkekaeeYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 308 VQESNRTETELVGLKQnlinnklklmnvletgimyKLEILQEQLDLQLKNLEKLSQDTKEESRLNDTKLMDLQIKYENEI 387
Cdd:PRK03918 337 EERLEELKKKLKELEK-------------------RLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELE 397
|
250 260 270
....*....|....*....|....*....|..
gi 6324503 388 KpkiDKTDIFIQEELISGKINKLNDEIKQLQK 419
Cdd:PRK03918 398 K---AKEEIEEEISKITARIGELKKEIKELKK 426
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
182-380 |
2.42e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 182 EQELQKLEEQNKELEIQLKKLTkiqetlsidyndykiskqsifKDLEALSFQIVELESNrdklIKISNTDMEELSEGIKE 261
Cdd:COG3883 22 QKELSELQAELEAAQAELDALQ---------------------AELEELNEEYNELQAE----LEALQAEIDKLQAEIAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 262 LNDLLIQRKKTLDD-LTAQQKNLQDTV--------TTFETIISELYDVLRIISS---EVQESNRTETELVGLKQNLINNK 329
Cdd:COG3883 77 AEAEIEERREELGErARALYRSGGSVSyldvllgsESFSDFLDRLSALSKIADAdadLLEELKADKAELEAKKAELEAKL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6324503 330 LKLMNVLEtgimyKLEILQEQLDLQLKNLEKLSQDTKEESRLNDTKLMDLQ 380
Cdd:COG3883 157 AELEALKA-----ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
182-371 |
2.95e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 182 EQELQKLEEQNKELEIQLKKLTKIQETLSIDYNDYKISKQSIFKDLEALSFQIVELESNRDKLIKisntDMEELSEGIKE 261
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ----DIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 262 LNDLLIQRKKTLDDLTAQQKNLQDTVTTFETIISELYDVLRIISSEVQESNRTETELVGLKQNLINNKLKLMNVLetgim 341
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL----- 388
|
170 180 190
....*....|....*....|....*....|
gi 6324503 342 ykLEILQEQLDLQLKNLEKLSQDTKEESRL 371
Cdd:COG1196 389 --LEALRAAAELAAQLEELEEAEEALLERL 416
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
165-449 |
2.97e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 165 QQQLKQYEDVDGDNIPDEQELQKLEEQNKELEIQLKKLTKIQETLSIDYNDYKISKQSIFKDLEALSFQIVELESNRDKL 244
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 245 ikisNTDMEELSEGIKELNDLLIQRKKTLDDLTAQQKNLQDTVTTFETIISELYDVLR--IISSEVQESNRTETELVGLK 322
Cdd:TIGR04523 502 ----NEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKkeNLEKEIDEKNKEIEELKQTQ 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 323 QNLINNKLKLMNVLETGIMYKLEILQEQ--LDLQLKNLEKLSQDTKEESRLNDTKLMDLQIKYEneikpKIDKTDIFIQE 400
Cdd:TIGR04523 578 KSLKKKQEEKQELIDQKEKEKKDLIKEIeeKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKN-----KLKQEVKQIKE 652
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 6324503 401 EL--ISGKINKLNDEIKQLQKDFEVEVKEIEIEYSLLSGHINKYMNEMLEY 449
Cdd:TIGR04523 653 TIkeIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYITRMIRI 703
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
182-419 |
3.25e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.04 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 182 EQELQKLEEQNKELEIQLKKLtKIQETLSIDYNDYKISKQSIFKDLEALSFQivELESNRDKL---IKISNTDMEELSEG 258
Cdd:TIGR02168 185 RENLDRLEDILNELERQLKSL-ERQAEKAERYKELKAELRELELALLVLRLE--ELREELEELqeeLKEAEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 259 IKELNDLLIQRKKTLDDLTAQQKNLQDTVTTFETIISELYDVLRIISSEVQESNRTETELVGLKQNLINNKLKLMNVLET 338
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 339 gIMYKLEILQEQLDLQLKNLEKLSQDTKEESRLNDtklmDLQIKYENEiKPKIDktDIFIQEELISGKINKLNDEIKQLQ 418
Cdd:TIGR02168 342 -LEEKLEELKEELESLEAELEELEAELEELESRLE----ELEEQLETL-RSKVA--QLELQIASLNNEIERLEARLERLE 413
|
.
gi 6324503 419 K 419
Cdd:TIGR02168 414 D 414
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
146-323 |
4.32e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.04 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 146 QMESLLGQLRSKFDDYNLIQQQLKQyedvdgdnipDEQELQKLEEQNKELEIQLKKLtkiQETLSIDYNDYKISKQSIfK 225
Cdd:COG3883 38 ELDALQAELEELNEEYNELQAELEA----------LQAEIDKLQAEIAEAEAEIEER---REELGERARALYRSGGSV-S 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 226 DLEAL----SFQivELESNRDKLIKISNTD---MEELSEGIKELNDLLIQRKKTLDDLTAQQKNLQDTVTTFETIISELY 298
Cdd:COG3883 104 YLDVLlgseSFS--DFLDRLSALSKIADADadlLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQE 181
|
170 180
....*....|....*....|....*
gi 6324503 299 DVLRIISSEVQESNRTETELVGLKQ 323
Cdd:COG3883 182 ALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
146-326 |
8.80e-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: 38.21 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 146 QMESLLGQLRSKFDDYNLIQQQLKQYEDVDGDNIPDEQELQK-LEEQNKELEIQLKKLTKIQETLSIDYndykISKQSIF 224
Cdd:COG4942 56 QLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAeLEAQKEELAELLRALYRLGRQPPLAL----LLSPEDF 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324503 225 KDLEALSFQIVELESNRDKLIKISNTDMEELSEGIKELNDLLIQRKKTLDDLTAQQKNLQDTVTTFETIISELYDVLRII 304
Cdd:COG4942 132 LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL 211
|
170 180
....*....|....*....|..
gi 6324503 305 SSEVQESNRTETELVGLKQNLI 326
Cdd:COG4942 212 AAELAELQQEAEELEALIARLE 233
|
|
| |
