|
Name |
Accession |
Description |
Interval |
E-value |
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
944-1143 |
9.56e-98 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 308.53 E-value: 9.56e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 944 FQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIPGTER-KILSHQTVQQLVLEKEQA 1022
Cdd:pfam05010 1 YSQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKqKELEHAEIQKVLEEKDQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 1023 LADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQ 1102
Cdd:pfam05010 81 LADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 122066312 1103 EQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELI 1143
Cdd:pfam05010 161 ETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
869-1145 |
4.22e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 4.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 869 AEKnppvfAQKLQEELEfaVMRIEALKLARQIALASRSRQDTKREAAhppdvsisktalysrigSTEVEKppgllfqqpd 948
Cdd:COG1196 212 AER-----YRELKEELK--ELEAELLLLKLRELEAELEELEAELEEL-----------------EAELEE---------- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 949 LDSALQVARAEVIAKEREVSEWRDKYEESRREVvemRKIVAEYEKTIAQMIPGTERKILSHQTVQQLVLEKEQALADLNS 1028
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEE---YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 1029 VEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAYQ 1108
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
250 260 270
....*....|....*....|....*....|....*..
gi 122066312 1109 ASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAK 1145
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
942-1137 |
5.35e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 942 LLFQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTiAQMIPGTERKILSHQ----TVQQLVL 1017
Cdd:PRK03918 184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL-KEEIEELEKELESLEgskrKLEEKIR 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 1018 EKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEEKLDRANA------ 1091
Cdd:PRK03918 263 ELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDE-LREIEKRLSRLEEEINGIEERIKELEEkeerle 341
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 122066312 1092 -----------EIAQVRGKAQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELTK 1137
Cdd:PRK03918 342 elkkklkelekRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEK 398
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
948-1145 |
1.07e-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: 53.14 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 948 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQmipGTERKILSHQTVQQLVLEKEQALADLN 1027
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ---LEERIAQLSKELTELEAEIEELEERLE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 1028 SVEKSLADLFRRYEKMKEVLEGFRKNEEVLKkcaqeylSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAY 1107
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEELKALR-------EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
170 180 190
....*....|....*....|....*....|....*...
gi 122066312 1108 QaslRKEQLRVDalertLEQKNKEIEELTKICDELIAK 1145
Cdd:TIGR02168 845 E---QIEELSED-----IESLAAEIEELEELIEELESE 874
|
|
| PRK13335 |
PRK13335 |
superantigen-like protein SSL3; Reviewed; |
297-408 |
2.10e-04 |
|
superantigen-like protein SSL3; Reviewed;
Pssm-ID: 139494 [Multi-domain] Cd Length: 356 Bit Score: 45.12 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 297 EAGTLTTDACGTGSNSASSTLKRTKKTRPPSLKK-------KQATKKPTETPPVKETQQEPGEESPVPSEEHLAPETKTE 369
Cdd:PRK13335 45 KAERLAMINITAGANSATTQAANTRQERTPKLEKapntneeKTSASKIEKISQPKQEEQKSLNISATPAPKQEQSQTTTE 124
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 122066312 370 SATPEGAGCT---LSDDTPLESPAVPTATCPLTLESAEDVSP 408
Cdd:PRK13335 125 STTPKTKVTTppsTNTPQPMQSTKSDTPQSPTIKQAQTDMTP 166
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
105-433 |
3.08e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 41.70 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 105 APEHTASAPSAAGPGVEVTPTGSPQHLAKNEPRSSDSEEAFETPESTTPVKAPPAPPPPPPEVTPEPEVIDPPAPeepgc 184
Cdd:PHA03307 52 AVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASP----- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 185 isePPVVVPDGPRSSESVEGSPFRPSHSSSAVFDEDKPIASSGTYNLdfDSIELVDNFQSLEPCSaDSKGQECKVSTRRK 264
Cdd:PHA03307 127 ---PPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSR--QAALPLSSPEETARAP-SSPPAEPPPSTPPA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 265 STESVPPSKSTLSRslslqasdfDGASCPGSPEAGTLTTDACGTGSNSASSTLKRTKKTRPPSLKKKQATKKPTETPPVK 344
Cdd:PHA03307 201 AASPRPPRRSSPIS---------ASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 345 ETQQEPGEESPVPSEEHLAPETKTESATPEGAGCTLSDDTP---LESPAVPTATCPLTLESAEDVSPLVSGGGRVQNSPP 421
Cdd:PHA03307 272 ASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPrasSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSP 351
|
330
....*....|...
gi 122066312 422 V-GRKSVPLTTAS 433
Cdd:PHA03307 352 SpSRPPPPADPSS 364
|
|
| PRK08691 |
PRK08691 |
DNA polymerase III subunits gamma and tau; Validated |
643-900 |
7.52e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236333 [Multi-domain] Cd Length: 709 Bit Score: 40.46 E-value: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 643 PLSDPPSQDPTPAATPEAPSA-ISTVVHATDEEKLAVTSQKwtCMTVDLDADKQDFPQPsdlsNFVNETKFNSPSEELDY 721
Cdd:PRK08691 435 PWEDAPDEAQTAAGTAQTSAKsIQTASEAETPPENQVSKNK--AADNETDAPLSEVPSE----NPIQATPNDEAVETETF 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 722 rnSYEIEYMEKLGSSLPQDDDTPKKQALYLMFDTPQESPVKSP---------PVRMSDSPTPCSGSSFEDTEalvNAATK 792
Cdd:PRK08691 509 --AHEAPAEPFYGYGFPDNDCPPEDGAEIPPPDWEHAAPADTAgggadeeaeAGGIGGNNTPSAPPPEFSTE---NWAAI 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 793 LQHpVARGLPSSQEPLLQVPEKPSQKELEAMALGTPAEAIEITAPEGAFASADTLLSRLAHPASLcgALGYLEPDLAEKN 872
Cdd:PRK08691 584 VRH-FARKLGAAQMPAQHSAWTEYHPDTGLMVLAMTAEARATADKKRLDKIRDTLAQAYGLQLTL--QTQDWRDEAGRET 660
|
250 260
....*....|....*....|....*....
gi 122066312 873 PPVFAQKLQ-EELEFAVMRIEALKLARQI 900
Cdd:PRK08691 661 PAMQDKRVQaEDRQKAQALLEADPAAQKI 689
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
944-1143 |
9.56e-98 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 308.53 E-value: 9.56e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 944 FQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIPGTER-KILSHQTVQQLVLEKEQA 1022
Cdd:pfam05010 1 YSQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKqKELEHAEIQKVLEEKDQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 1023 LADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQ 1102
Cdd:pfam05010 81 LADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 122066312 1103 EQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELI 1143
Cdd:pfam05010 161 ETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
869-1145 |
4.22e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 4.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 869 AEKnppvfAQKLQEELEfaVMRIEALKLARQIALASRSRQDTKREAAhppdvsisktalysrigSTEVEKppgllfqqpd 948
Cdd:COG1196 212 AER-----YRELKEELK--ELEAELLLLKLRELEAELEELEAELEEL-----------------EAELEE---------- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 949 LDSALQVARAEVIAKEREVSEWRDKYEESRREVvemRKIVAEYEKTIAQMIPGTERKILSHQTVQQLVLEKEQALADLNS 1028
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEE---YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 1029 VEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAYQ 1108
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
250 260 270
....*....|....*....|....*....|....*..
gi 122066312 1109 ASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAK 1145
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
942-1137 |
5.35e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 942 LLFQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTiAQMIPGTERKILSHQ----TVQQLVL 1017
Cdd:PRK03918 184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL-KEEIEELEKELESLEgskrKLEEKIR 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 1018 EKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEEKLDRANA------ 1091
Cdd:PRK03918 263 ELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDE-LREIEKRLSRLEEEINGIEERIKELEEkeerle 341
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 122066312 1092 -----------EIAQVRGKAQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELTK 1137
Cdd:PRK03918 342 elkkklkelekRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEK 398
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
948-1145 |
1.07e-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: 53.14 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 948 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQmipGTERKILSHQTVQQLVLEKEQALADLN 1027
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ---LEERIAQLSKELTELEAEIEELEERLE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 1028 SVEKSLADLFRRYEKMKEVLEGFRKNEEVLKkcaqeylSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAY 1107
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEELKALR-------EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
170 180 190
....*....|....*....|....*....|....*...
gi 122066312 1108 QaslRKEQLRVDalertLEQKNKEIEELTKICDELIAK 1145
Cdd:TIGR02168 845 E---QIEELSED-----IESLAAEIEELEELIEELESE 874
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
972-1146 |
1.55e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 972 DKYEESRREVVEMRKIVAEYEKTIAQmipgterkilshqtvqqlVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFR 1051
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEE------------------LEELEEELEELEAELEELREELEKLEKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 1052 KNEEvLKKCAQEYLSRVKKEEQRYQALKvHAEEKLDRANAEIAQVRGKAQQEQAAYQASLRKE-----------QLRVDA 1120
Cdd:COG4717 133 ELEA-LEAELAELPERLEELEERLEELR-ELEEELEELEAELAELQEELEELLEQLSLATEEElqdlaeeleelQQRLAE 210
|
170 180
....*....|....*....|....*.
gi 122066312 1121 LERTLEQKNKEIEELTKICDELIAKM 1146
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQLENEL 236
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
945-1145 |
3.43e-06 |
|
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: 50.53 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 945 QQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQmipgtERKILSHQTVQQLVLEKEQALA 1024
Cdd:COG4942 49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA-----QKEELAELLRALYRLGRQPPLA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 1025 DLNSVEkSLADLFRRYEKMKEVLEGFRKNEEVLKKcAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEq 1104
Cdd:COG4942 124 LLLSPE-DFLDAVRRLQYLKYLAPARREQAEELRA-DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL- 200
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 122066312 1105 aayqasLRKEQLRVDALERTLEQKNKEIEELTKICDELIAK 1145
Cdd:COG4942 201 ------LARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
938-1137 |
6.98e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 6.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 938 KPPGLLFQQPDLDSALQVARAEV---IAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAqmipgterkilshqtVQQ 1014
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLLQ---------------LLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 1015 LVLEKEQAladlnsvEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIA 1094
Cdd:COG4717 130 LYQELEAL-------EAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 122066312 1095 QVRGKaqqeqaayqasLRKEQLRVDALERTLEQKNKEIEELTK 1137
Cdd:COG4717 203 ELQQR-----------LAELEEELEEAQEELEELEEELEQLEN 234
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
878-1128 |
1.64e-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: 49.28 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 878 QKLQEELEFAVMRIEAL-----KLARQIALASRSRQDTKREAAhppdvsisktALYSRIGSTEVEKPpgllfqqpDLDSA 952
Cdd:TIGR02168 298 SRLEQQKQILRERLANLerqleELEAQLEELESKLDELAEELA----------ELEEKLEELKEELE--------SLEAE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 953 LQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMipgterkilsHQTVQQLVLEKEQALADLNSVEKS 1032
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL----------EARLERLEDRRERLQQEIEELLKK 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 1033 LADLfrryeKMKEVLEGFRKNEEVLKKcAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGkaqqeqaayqaslr 1112
Cdd:TIGR02168 430 LEEA-----ELKELQAELEELEEELEE-LQEELERLEEALEELREELEEAEQALDAAERELAQLQA-------------- 489
|
250
....*....|....*.
gi 122066312 1113 keqlRVDALERTLEQK 1128
Cdd:TIGR02168 490 ----RLDSLERLQENL 501
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
878-1145 |
7.41e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 7.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 878 QKLQEELEFAVMRIEALKLARQIALASRSRQDTKREAAhppdvsisKTALYSRigSTEVEkppgllfqqpDLDSALQVAR 957
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEEL--------RLELEEL--ELELE----------EAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 958 AEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMipgTERKILSHQTVQQLVLEKEQALADLNSVEKSLADLF 1037
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL---EEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 1038 RRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRG--KAQQEQAAYQASLRKEQ 1115
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEleEEEEEEEEALEEAAEEE 451
|
250 260 270
....*....|....*....|....*....|
gi 122066312 1116 LRVDALERTLEQKNKEIEELTKICDELIAK 1145
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
888-1137 |
7.60e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 7.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 888 VMRIEALKLARQIALASRSRQDTKREAAHPPDVSISKTALYSRIgsTEVEKppglLFQQPDLDSALQVARAEviaKEREV 967
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI--EEVMK----LYEEEKKMKAEEAKKAE---EAKIK 1621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 968 SEWRDKYEESRREVVEMRKIVAEYEKTIAQMIPGTER-KILSHQTVQQLVLEKEQA--LADLNSVEKSLADLFRRYEKMK 1044
Cdd:PTZ00121 1622 AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnKIKAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEALKKEAEEA 1701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 1045 EVLEGFRKNEEVLKKCAQEYlsRVKKEEQRYQALKVHAEEKLDRANAEIAQVR-------GKAQQEQAAYQASLRKEQLR 1117
Cdd:PTZ00121 1702 KKAEELKKKEAEEKKKAEEL--KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDeeekkkiAHLKKEEEKKAEEIRKEKEA 1779
|
250 260
....*....|....*....|..
gi 122066312 1118 V--DALERTLEQKNKEIEELTK 1137
Cdd:PTZ00121 1780 VieEELDEEDEKRRMEVDKKIK 1801
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
958-1144 |
8.73e-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: 46.98 E-value: 8.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 958 AEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTiaqmipgtERKILSHQtVQQLVLEKEQALADLNSVEKSLADL- 1036
Cdd:TIGR02169 187 ERLDLIIDEKRQQLERLRREREKAERYQALLKEKREY--------EGYELLKE-KEALERQKEAIERQLASLEEELEKLt 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 1037 FRRYEKMKEVLEGFRKNEEVLKKcaqeyLSRVKKEEQRyqALKvhaeEKLDRANAEIAQVRGKAQQEQAAYQAS---LRK 1113
Cdd:TIGR02169 258 EEISELEKRLEEIEQLLEELNKK-----IKDLGEEEQL--RVK----EKIGELEAEIASLERSIAEKERELEDAeerLAK 326
|
170 180 190
....*....|....*....|....*....|.
gi 122066312 1114 EQLRVDALERTLEQKNKEIEELTKICDELIA 1144
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTE 357
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
963-1145 |
1.80e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 963 KEREVSEWRDKYEESRREVVEMRKivAEYEKTIAQMIPGTErkilshqtvqqlvlEKEQALADLNSVEKSLADLFRRYEK 1042
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKKADEAKK--AAEAKKKADEAKKAE--------------EAKKADEAKKAEEAKKADEAKKAEE 1544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 1043 MKEVLEgFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAYQASLRK-EQLRVDAL 1121
Cdd:PTZ00121 1545 KKKADE-LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKaEEAKIKAE 1623
|
170 180
....*....|....*....|....*
gi 122066312 1122 E-RTLEQKNKEIEELTKICDELIAK 1145
Cdd:PTZ00121 1624 ElKKAEEEKKKVEQLKKKEAEEKKK 1648
|
|
| PRK13335 |
PRK13335 |
superantigen-like protein SSL3; Reviewed; |
297-408 |
2.10e-04 |
|
superantigen-like protein SSL3; Reviewed;
Pssm-ID: 139494 [Multi-domain] Cd Length: 356 Bit Score: 45.12 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 297 EAGTLTTDACGTGSNSASSTLKRTKKTRPPSLKK-------KQATKKPTETPPVKETQQEPGEESPVPSEEHLAPETKTE 369
Cdd:PRK13335 45 KAERLAMINITAGANSATTQAANTRQERTPKLEKapntneeKTSASKIEKISQPKQEEQKSLNISATPAPKQEQSQTTTE 124
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 122066312 370 SATPEGAGCT---LSDDTPLESPAVPTATCPLTLESAEDVSP 408
Cdd:PRK13335 125 STTPKTKVTTppsTNTPQPMQSTKSDTPQSPTIKQAQTDMTP 166
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
953-1135 |
2.54e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 953 LQVARAE-VIAKEREVSEWR-----DKYEESRREVVEMRKIVAEYEKTIAQMIPGTERKILSHQTVQQLVLEKEQALADL 1026
Cdd:TIGR02168 207 RQAEKAErYKELKAELRELElallvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 1027 NSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKaqqeqaa 1106
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE------- 359
|
170 180
....*....|....*....|....*....
gi 122066312 1107 yqasLRKEQLRVDALERTLEQKNKEIEEL 1135
Cdd:TIGR02168 360 ----LEELEAELEELESRLEELEEQLETL 384
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
953-1145 |
3.88e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 953 LQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMipgtERKIlshQTvQQLVLEKEQALadlnsVEKs 1032
Cdd:COG1340 76 LKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERL----EWRQ---QT-EVLSPEEEKEL-----VEK- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 1033 LADLFRRYEKMKEVLEGFRKNEEVLKKcAQEYLSRVKKEEQRYQALKvhaeEKLDRANAEIAQVRGKAQqeqaayqaSLR 1112
Cdd:COG1340 142 IKELEKELEKAKKALEKNEKLKELRAE-LKELRKEAEEIHKKIKELA----EEAQELHEEMIELYKEAD--------ELR 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 122066312 1113 KE-----------QLRVDALERTLEQKNKEIEELTKICDELIAK 1145
Cdd:COG1340 209 KEadelhkeiveaQEKADELHEEIIELQKELRELRKELKKLRKK 252
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
948-1145 |
9.63e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 9.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 948 DLDSALQVARAEVIAKEREV--SEWRDKYEESRREvvEMRKIVAEYEKTIAQMIPGTERKILSHQTVQQLVLEKEQALAD 1025
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEELkkAEEKKKAEEAKKA--EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 1026 lnSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEylsrVKKEEQRYqalKVHAEEKLDRANAEiaqvRGKAQQEQA 1105
Cdd:PTZ00121 1616 --EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE----LKKAEEEN---KIKAAEEAKKAEED----KKKAEEAKK 1682
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 122066312 1106 AYQASLRKEQlrvdALERTLEQKNKeIEELTKICDELIAK 1145
Cdd:PTZ00121 1683 AEEDEKKAAE----ALKKEAEEAKK-AEELKKKEAEEKKK 1717
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
965-1137 |
9.97e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 9.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 965 REVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIPGTERKilshqtvQQLVLEKEQALADLNSVEKSLADL---FRRYE 1041
Cdd:PRK03918 269 EELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDEL-------REIEKRLSRLEEEINGIEERIKELeekEERLE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 1042 KMKEVLEGFRKNEEVLKKCAQEYlSRVKKEEQRYQALKVH-AEEKLDRANAEIAQVRGKAQQEQAAyqasLRKEQLRVDA 1120
Cdd:PRK03918 342 ELKKKLKELEKRLEELEERHELY-EEAKAKKEELERLKKRlTGLTPEKLEKELEELEKAKEEIEEE----ISKITARIGE 416
|
170
....*....|....*..
gi 122066312 1121 LERTLEQKNKEIEELTK 1137
Cdd:PRK03918 417 LKKEIKELKKAIEELKK 433
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
960-1144 |
1.03e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 960 VIAKEREVSEWRDKYE-----ESRREVVEMRKIVA---EYEKTIAQMIpGTERKILS----HQTVQQLVLEKEQALADLN 1027
Cdd:PRK03918 488 VLKKESELIKLKELAEqlkelEEKLKKYNLEELEKkaeEYEKLKEKLI-KLKGEIKSlkkeLEKLEELKKKLAELEKKLD 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 1028 SVEKSLADLFRRYEKmkevlEGFRKNEEV------LKKCAQEYL------SRVKKEEQRYQALK---VHAEEKLDRANAE 1092
Cdd:PRK03918 567 ELEEELAELLKELEE-----LGFESVEELeerlkeLEPFYNEYLelkdaeKELEREEKELKKLEeelDKAFEELAETEKR 641
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 122066312 1093 IAQVRGK----AQQEQAAYQASLRKEQLRvdaLERTLEQKNKEIEELTKICDELIA 1144
Cdd:PRK03918 642 LEELRKEleelEKKYSEEEYEELREEYLE---LSRELAGLRAELEELEKRREEIKK 694
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
995-1136 |
1.21e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.13 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 995 IAQMIPGTERKILSHQT-VQQLVLEKEQALADLNSVEKSLadlfrryEKMKEVLEGFRKNEEVLKK---CAQEYLSRVKK 1070
Cdd:TIGR02169 147 FISMSPVERRKIIDEIAgVAEFDRKKEKALEELEEVEENI-------ERLDLIIDEKRQQLERLRRereKAERYQALLKE 219
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 122066312 1071 EEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELT 1136
Cdd:TIGR02169 220 KREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG 285
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
957-1142 |
1.41e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 957 RAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYE-----KTIAQMIPGTERKILSH------------QTVQQLVLEK 1019
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESeliklKELAEQLKELEEKLKKYnleelekkaeeyEKLKEKLIKL 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 1020 EQALADLNSVEKSLADLFRRYEKMKEVLEGF-RKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEiaqvrg 1098
Cdd:PRK03918 538 KGEIKSLKKELEKLEELKKKLAELEKKLDELeEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAE------ 611
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 122066312 1099 kaqQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDEL 1142
Cdd:PRK03918 612 ---KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL 652
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
949-1142 |
1.96e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 949 LDSALQVARAEViakeREVSEW-RDKYEESRREVVEMRKIVAEYEKTIAQMIPGTERKILShQTVQQLVLEKEQALADLN 1027
Cdd:COG3206 162 LEQNLELRREEA----RKALEFlEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLL-QQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 1028 SVEKSLADLFRRYEKMKEVLEGFRKNEEVlkkcaQEYLSRVKKEEQRYQALKVHAEEK---LDRANAEIAQVRGKAQQEQ 1104
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQSPVI-----QQLRAQLAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQEA 311
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 122066312 1105 AAYQASLRKE----QLRVDALERTLEQKNKEIEELTKICDEL 1142
Cdd:COG3206 312 QRILASLEAElealQAREASLQAQLAQLEARLAELPELEAEL 353
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
878-1143 |
2.07e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.36 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 878 QKLQEELEFAVMRIEALKLARQIALASRSRQDTKREAAhppdvsISKTALYSRIGSTEVEKppgLLFQQPDLDSALQVAR 957
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQLERLRREREKA------ERYQALLKEKREYEGYE---LLKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 958 AEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIPGT----ERKILS-HQTVQQL---VLEKEQALADLnsv 1029
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqlrvKEKIGElEAEIASLersIAEKERELEDA--- 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 1030 EKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEkLDRANAEiaqvrgkaqqeqaayqa 1109
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE-VDKEFAE----------------- 382
|
250 260 270
....*....|....*....|....*....|....
gi 122066312 1110 sLRKEQlrvDALERTLEQKNKEIEELTKICDELI 1143
Cdd:TIGR02169 383 -TRDEL---KDYREKLEKLKREINELKRELDRLQ 412
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1012-1136 |
2.62e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 1012 VQQLVLEKEQALADLNsvekSLADLFRRYEKMKEVLEGFRKNEEVL---KKCAQEYLS-RVKKEEQRYQALKVH---AEE 1084
Cdd:COG4913 213 VREYMLEEPDTFEAAD----ALVEHFDDLERAHEALEDAREQIELLepiRELAERYAAaRERLAELEYLRAALRlwfAQR 288
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 122066312 1085 KLDRANAEIAQVRGKaqqeqaayqasLRKEQLRVDALERTLEQKNKEIEELT 1136
Cdd:COG4913 289 RLELLEAELEELRAE-----------LARLEAELERLEARLDALREELDELE 329
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
105-433 |
3.08e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 41.70 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 105 APEHTASAPSAAGPGVEVTPTGSPQHLAKNEPRSSDSEEAFETPESTTPVKAPPAPPPPPPEVTPEPEVIDPPAPeepgc 184
Cdd:PHA03307 52 AVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASP----- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 185 isePPVVVPDGPRSSESVEGSPFRPSHSSSAVFDEDKPIASSGTYNLdfDSIELVDNFQSLEPCSaDSKGQECKVSTRRK 264
Cdd:PHA03307 127 ---PPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSR--QAALPLSSPEETARAP-SSPPAEPPPSTPPA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 265 STESVPPSKSTLSRslslqasdfDGASCPGSPEAGTLTTDACGTGSNSASSTLKRTKKTRPPSLKKKQATKKPTETPPVK 344
Cdd:PHA03307 201 AASPRPPRRSSPIS---------ASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 345 ETQQEPGEESPVPSEEHLAPETKTESATPEGAGCTLSDDTP---LESPAVPTATCPLTLESAEDVSPLVSGGGRVQNSPP 421
Cdd:PHA03307 272 ASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPrasSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSP 351
|
330
....*....|...
gi 122066312 422 V-GRKSVPLTTAS 433
Cdd:PHA03307 352 SpSRPPPPADPSS 364
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
965-1142 |
3.50e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 965 REVSEWRDKYEESRREVVEMRKivaeyektiaqmipgtERKILSHqtVQQLVLEKEQALADLNSVE--KSLADLFRRYEK 1042
Cdd:COG4913 228 DALVEHFDDLERAHEALEDARE----------------QIELLEP--IRELAERYAAARERLAELEylRAALRLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 1043 MKEVlegfrknEEVLKKCAQEyLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKaqqeqaayqaslRKEQLR--VDA 1120
Cdd:COG4913 290 LELL-------EAELEELRAE-LARLEAELERLEARLDALREELDELEAQIRGNGGD------------RLEQLEreIER 349
|
170 180
....*....|....*....|..
gi 122066312 1121 LERTLEQKNKEIEELTKICDEL 1142
Cdd:COG4913 350 LERELEERERRRARLEALLAAL 371
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
972-1142 |
5.31e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 972 DKYEESRREVVEMRKIVAEYEKTIAQMIPGTERkilshqtVQQLVLEKEQALAdlnsveksladlfrryekmkEVLEGFR 1051
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTEN-------IEELIKEKEKELE--------------------EVLREIN 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 1052 KNEEVLKKCAQEyLSRVKKEEQRYQALKvhaeEKLDRANAEIAQVRGkaqqeqaayqaSLRKEQLRVDALERTLEQKNKE 1131
Cdd:PRK03918 211 EISSELPELREE-LEKLEKEVKELEELK----EEIEELEKELESLEG-----------SKRKLEEKIRELEERIEELKKE 274
|
170
....*....|.
gi 122066312 1132 IEELTKICDEL 1142
Cdd:PRK03918 275 IEELEEKVKEL 285
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1041-1145 |
5.38e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 1041 EKMKEVLEGFRKNEEVLKKcaqEYLSRVKKEEQRyqaLKVHAEEKLDRANAEIAQVRGKAQQEQAA---YQASLRKEQLR 1117
Cdd:PRK12704 38 EEAKRILEEAKKEAEAIKK---EALLEAKEEIHK---LRNEFEKELRERRNELQKLEKRLLQKEENldrKLELLEKREEE 111
|
90 100
....*....|....*....|....*...
gi 122066312 1118 VDALERTLEQKNKEIEELTKICDELIAK 1145
Cdd:PRK12704 112 LEKKEKELEQKQQELEKKEEELEELIEE 139
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
964-1148 |
6.08e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 964 EREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQM------IPGTERKILSHQTVQQLvlekEQALADLNSVEKSLADLF 1037
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKELKKAIEELkkakgkCPVCGRELTEEHRKELL----EEYTAELKRIEKELKEIE 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 1038 RRYEKMKEV---LEGFRKNEEVLKKcAQEYLSRVKKEEQRyqaLKVHAEEKLDRANAEIAQVRGKAQQEQAAYQaSLRKE 1114
Cdd:PRK03918 473 EKERKLRKElreLEKVLKKESELIK-LKELAEQLKELEEK---LKKYNLEELEKKAEEYEKLKEKLIKLKGEIK-SLKKE 547
|
170 180 190
....*....|....*....|....*....|....
gi 122066312 1115 QLRVDALERTLEQKNKEIEELTKICDELIAKMGK 1148
Cdd:PRK03918 548 LEKLEELKKKLAELEKKLDELEEELAELLKELEE 581
|
|
| PRK08691 |
PRK08691 |
DNA polymerase III subunits gamma and tau; Validated |
643-900 |
7.52e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236333 [Multi-domain] Cd Length: 709 Bit Score: 40.46 E-value: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 643 PLSDPPSQDPTPAATPEAPSA-ISTVVHATDEEKLAVTSQKwtCMTVDLDADKQDFPQPsdlsNFVNETKFNSPSEELDY 721
Cdd:PRK08691 435 PWEDAPDEAQTAAGTAQTSAKsIQTASEAETPPENQVSKNK--AADNETDAPLSEVPSE----NPIQATPNDEAVETETF 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 722 rnSYEIEYMEKLGSSLPQDDDTPKKQALYLMFDTPQESPVKSP---------PVRMSDSPTPCSGSSFEDTEalvNAATK 792
Cdd:PRK08691 509 --AHEAPAEPFYGYGFPDNDCPPEDGAEIPPPDWEHAAPADTAgggadeeaeAGGIGGNNTPSAPPPEFSTE---NWAAI 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 793 LQHpVARGLPSSQEPLLQVPEKPSQKELEAMALGTPAEAIEITAPEGAFASADTLLSRLAHPASLcgALGYLEPDLAEKN 872
Cdd:PRK08691 584 VRH-FARKLGAAQMPAQHSAWTEYHPDTGLMVLAMTAEARATADKKRLDKIRDTLAQAYGLQLTL--QTQDWRDEAGRET 660
|
250 260
....*....|....*....|....*....
gi 122066312 873 PPVFAQKLQ-EELEFAVMRIEALKLARQI 900
Cdd:PRK08691 661 PAMQDKRVQaEDRQKAQALLEADPAAQKI 689
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
987-1135 |
8.36e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 38.73 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 987 IVAEYEKTIAQMipgteRKILSHQTVQQLVL------EKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKC 1060
Cdd:pfam13851 2 LMKNHEKAFNEI-----KNYYNDITRNNLELikslkeEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 1061 AQEYL----------SRVKKEEQRYQALKVHAEEKL--------------DRANAEIAQVRGKaqqeqaayqaSLRKEQL 1116
Cdd:pfam13851 77 LENYEkdkqslknlkARLKVLEKELKDLKWEHEVLEqrfekvererdelyDKFEAAIQDVQQK----------TGLKNLL 146
|
170 180
....*....|....*....|..
gi 122066312 1117 ---RVDALERTLEQKNKEIEEL 1135
Cdd:pfam13851 147 lekKLQALGETLEKKEAQLNEV 168
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
943-1134 |
9.05e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 9.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 943 LFQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMipgTERKILSHQTVQQLVLEKEQA 1022
Cdd:COG4372 37 LFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAA---QAELAQAQEELESLQEEAEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 1023 LADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQAL-KVHAEEKLDRANAEIAQV----- 1096
Cdd:COG4372 114 QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALeQELQALSEAEAEQALDELlkean 193
|
170 180 190
....*....|....*....|....*....|....*...
gi 122066312 1097 RGKAQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEE 1134
Cdd:COG4372 194 RNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKL 231
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
952-1099 |
9.34e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 952 ALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQmIPGTERKILSHQtVQQLVLEKEQALADLNSVEK 1031
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG-NGGDRLEQLERE-IERLERELEERERRRARLEA 366
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 122066312 1032 SLADLfrrYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKK-EEQRYQALKVH--AEEKLDRANAEIAQVRGK 1099
Cdd:COG4913 367 LLAAL---GLPLPASAEEFAALRAEAAALLEALEEELEAlEEALAEAEAALrdLRRELRELEAEIASLERR 434
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
975-1137 |
9.37e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 9.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 975 EESRREVVEMRKIVAEYEKTIAQMIPGTERKILSHQTVQQLVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNE 1054
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122066312 1055 EVLkkcaQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQvrgkaqqeqaayqaslRKEQLRvdALERTLEQKNKEIEE 1134
Cdd:COG4372 111 EEL----QEELEELQKERQDLEQQRKQLEAQIAELQSEIAE----------------REEELK--ELEEQLESLQEELAA 168
|
...
gi 122066312 1135 LTK 1137
Cdd:COG4372 169 LEQ 171
|
|
| |
