|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
855-1155 |
5.40e-16 |
|
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: 83.57 E-value: 5.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 855 ILHLRQLLSRGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASsacEKLEKARADLQ--TAYQEFVQKL 932
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS---RQISALRKDLArlEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 933 NQQHQTDRTELENRLKdLYTAECEKLQSiYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEkVELLKKTY---ETS 1009
Cdd:TIGR02168 749 IAQLSKELTELEAEIE-ELEERLEEAEE-ELAEAEAEIEELEAQIEQLKEELKALREALDELRAE-LTLLNEEAanlRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1010 LSEIKKSHEMEKKSLEDL------LNEKQESLEKQINDLKSE--------NDALNERLKSEEQKQLSREKANSKNPQVMY 1075
Cdd:TIGR02168 826 LESLERRIAATERRLEDLeeqieeLSEDIESLAAEIEELEELieeleselEALLNERASLEEALALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1076 LEQELESLKAVLEIKNEKLHQQDMKLMKMEKLVDNNtalvdklkrFQQENEELKARMDKHMAISRQLSTEQAALQESLEK 1155
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLEGLEVRIDNL---------QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
836-1140 |
1.17e-13 |
|
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: 75.86 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 836 ERTLELAQYKTKCESQSGFILHLRQLLSRGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSACEKLE 915
Cdd:TIGR02168 222 LRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 916 KaRADLQTAYQEFVQKLNQQHQTDRTELENRLKDLYTAEceklqsiyiEEAEKYKTQLQEQFDNLNAAHETTKLEIEASH 995
Cdd:TIGR02168 302 Q-QKQILRERLANLERQLEELEAQLEELESKLDELAEEL---------AELEEKLEELKEELESLEAELEELEAELEELE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 996 SeKVELLKKTYETSLSEIkksHEMEKKslEDLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNpQVMY 1075
Cdd:TIGR02168 372 S-RLEELEEQLETLRSKV---AQLELQ--IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA-ELEE 444
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158706129 1076 LEQELESLKAVLEIKNEKLHQQDMKLMKMEKLVDnntALVDKLKRFQQENEELKARMDKHMAISR 1140
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREELEEAEQALD---AAERELAQLQARLDSLERLQENLEGFSE 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
879-1158 |
1.77e-13 |
|
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: 75.48 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 879 LLSEREEALKQHKTLSQELVSLRGELVAASSACEKLEKARADLQTAYQEFVQK---LNQQHQTDRTELENRLKDL--YTA 953
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEisrLEQQKQILRERLANLERQLeeLEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 954 ECEKLQSiYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELlkktyETSLSEIKKSHEmEKKSLEDLLNEKQE 1033
Cdd:TIGR02168 324 QLEELES-KLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL-----ESRLEELEEQLE-TLRSKVAQLELQIA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1034 SLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNpQVMYLEQELESLKAVLEIKNEKLHQQDMKLMKMEKLVDNNTA 1113
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA-ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 158706129 1114 LVDKLKRfqqENEELKARMDKHMAISRQLSTEQAALQESLEKESK 1158
Cdd:TIGR02168 476 ALDAAER---ELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
858-1172 |
6.82e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 6.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 858 LRQLLSRGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSACEKLEKARADLQTAYQEFVQKLNQQhQ 937
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL-E 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 938 TDRTELENRLKDLyTAECEKLQSIYIEEAEKYKTQLQEQfdnlnAAHETTKLEIEASHSEKVELLKKTYETSLSEIKKsh 1017
Cdd:COG1196 323 EELAELEEELEEL-EEELEELEEELEEAEEELEEAEAEL-----AEAEEALLEAEAELAEAEEELEELAEELLEALRA-- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1018 EMEKKSLEDLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKAnsknpqvmylEQELESLKAVLEIKNEKLHQQ 1097
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA----------LEEAAEEEAELEEEEEALLEL 464
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158706129 1098 dmklmkmeklvdnntaLVDKLKRFQQENEELKARMDKHMAISRQLSTEQAALQESLEKESKVNKRLSMENEELLW 1172
Cdd:COG1196 465 ----------------LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
912-1170 |
1.17e-10 |
|
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: 66.24 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 912 EKLEKARADLqtayqEFVQKLNQQHQTDRTELENRLKDLytaECEKlqsiyiEEAEKYKTQLQEqfdnlnaahettKLEI 991
Cdd:TIGR02169 170 RKKEKALEEL-----EEVEENIERLDLIIDEKRQQLERL---RRER------EKAERYQALLKE------------KREY 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 992 EAShsekvELLKKtyetslseiKKSHEMEKKSLEDLLNEKQESLEK---QINDLKSENDALNERLK--SEEQKQLSREKA 1066
Cdd:TIGR02169 224 EGY-----ELLKE---------KEALERQKEAIERQLASLEEELEKlteEISELEKRLEEIEQLLEelNKKIKDLGEEEQ 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1067 NSKNPQVMYLEQELESLKAVLEIKNEKLHQQDMKLMKMEKLVDNNTALVDKLKRFQQE--------NEELKARMDKHMAI 1138
Cdd:TIGR02169 290 LRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEerkrrdklTEEYAELKEELEDL 369
|
250 260 270
....*....|....*....|....*....|..
gi 158706129 1139 SRQLSTEQAALQESLEKESKVNKRLSMENEEL 1170
Cdd:TIGR02169 370 RAELEEVDKEFAETRDELKDYREKLEKLKREI 401
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
879-1170 |
1.79e-10 |
|
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: 65.47 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 879 LLSEREEALKQHKTLSQELVSLRGELvaassacEKLEKARADLQTAYQEFVQKLNQ--------------QHQTDRTELE 944
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEEL-------EKLTEEISELEKRLEEIEQLLEElnkkikdlgeeeqlRVKEKIGELE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 945 NRLKDLYTAECEKLQSIyiEEAEKYKTQLQEQFDNLNAAHETTKLEIE------ASHSEKVELLKKTYETSLSEIKkshE 1018
Cdd:TIGR02169 301 AEIASLERSIAEKEREL--EDAEERLAKLEAEIDKLLAEIEELEREIEeerkrrDKLTEEYAELKEELEDLRAELE---E 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1019 MEKKSLEdlLNEKQESLEKQINDLKSENDAL--NERLKSEEQKQLSREKANSKNpQVMYLEQELESLKAVLEIKNEKLHQ 1096
Cdd:TIGR02169 376 VDKEFAE--TRDELKDYREKLEKLKREINELkrELDRLQEELQRLSEELADLNA-AIAGIEAKINELEEEKEDKALEIKK 452
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158706129 1097 QDMKLMKmeklvdnntaLVDKLKRFQQENEELKarmdkhmaisrqlsteqaalqeslEKESKVNKRLSMENEEL 1170
Cdd:TIGR02169 453 QEWKLEQ----------LAADLSKYEQELYDLK------------------------EEYDRVEKELSKLQREL 492
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
934-1171 |
4.41e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 934 QQHQTDRTELENRLK----DLYTAECEKLQSIyIEEAEKYKTQLQEQFDNLNAAHETTKLEIEAShSEKVELLKKTYETS 1009
Cdd:COG1196 216 RELKEELKELEAELLllklRELEAELEELEAE-LEELEAELEELEAELAELEAELEELRLELEEL-ELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1010 LSEIKkshEMEKKslEDLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKansknpQVMYLEQELESLKAVLEI 1089
Cdd:COG1196 294 LAELA---RLEQD--IARLEERRRELEERLEELEEELAELEEELEELEEELEELEE------ELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1090 KNEKLHQQDMKLMKMEKLVDNNT----ALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAALQESLEKESKVNKRLSM 1165
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAeellEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
....*.
gi 158706129 1166 ENEELL 1171
Cdd:COG1196 443 ALEEAA 448
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
855-1064 |
1.06e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 855 ILHLRQLLSRGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSACEKLEKARADLQTAYQEFVQKLNQ 934
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 935 QHQTDRTELENRLKDLYTAECEKLQSIYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKTYETSLSEIK 1014
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 158706129 1015 KSHEMEKKSLEDLlnEKQESLEKQINDLKSENDALNERLKSEEQKQLSRE 1064
Cdd:COG1196 457 EEEALLELLAELL--EEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
857-1171 |
1.81e-09 |
|
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: 62.39 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 857 HLRQLLSRGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELvaassacEKLEKARADLQTAYQEFVQKLNQQh 936
Cdd:TIGR02169 699 RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL-------SSLEQEIENVKSELKELEARIEEL- 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 937 QTDRTELENRLKDLYTAEC-EKLQSI--YIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKTYETSL--S 1011
Cdd:TIGR02169 771 EEDLHKLEEALNDLEARLShSRIPEIqaELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEqiK 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1012 EIKKSHEMEKKSLEDLLNEKQE------SLEKQINDLKSENDALNERLKSEEQKQlsrEKANSknpQVMYLEQELESLKA 1085
Cdd:TIGR02169 851 SIEKEIENLNGKKEELEEELEEleaalrDLESRLGDLKKERDELEAQLRELERKI---EELEA---QIEKKRKRLSELKA 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1086 VLEIKNEKLHQQDMKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAALQESLEKESKvnkrLSM 1165
Cdd:TIGR02169 925 KLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAK----LEE 1000
|
....*.
gi 158706129 1166 ENEELL 1171
Cdd:TIGR02169 1001 ERKAIL 1006
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
963-1175 |
1.92e-09 |
|
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: 62.29 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 963 IEEAEKYKTQLQEQFDNLNAAHetTKLEIEASHSEKVELLKKTYETSLSEIKKSHEMEKKSLEDLLNEKQESLEKqindL 1042
Cdd:TIGR00618 172 LFPLDQYTQLALMEFAKKKSLH--GKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY----L 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1043 KSENDALNERLKSEEQKQlsrekansknpQVMYLEQELESLKAVLEIKNEKLHQQdmklMKMEKLVDNNTALVDKLKRFQ 1122
Cdd:TIGR00618 246 TQKREAQEEQLKKQQLLK-----------QLRARIEELRAQEAVLEETQERINRA----RKAAPLAAHIKAVTQIEQQAQ 310
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1123 QENEELKARMDKHMAISRQLSTEQAALQESLEKESKVNKRLSME-------NEELLWKLH 1175
Cdd:TIGR00618 311 RIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEihirdahEVATSIREI 370
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
874-1173 |
5.79e-09 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 60.76 E-value: 5.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 874 VVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSACEKLEKARADLQTAYQ----EFVQKLNQ---QHQTDRTELENR 946
Cdd:pfam02463 162 AAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQlkekLELEEEYLlylDYLKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 947 LKDLYTAECEKLQS-IYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKTYET------SLSEIKKSHEM 1019
Cdd:pfam02463 242 LQELLRDEQEEIESsKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKlerrkvDDEEKLKESEK 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1020 EKKSLEDLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQVMYLEQEL-ESLKAVLEIKNEKLHQQD 1098
Cdd:pfam02463 322 EKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLEsERLSSAAKLKEEELELKS 401
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158706129 1099 MKLMKMEKLVDN-NTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAALQESLEKESKvnKRLSMENEELLWK 1173
Cdd:pfam02463 402 EEEKEAQLLLELaRQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK--DELELKKSEDLLK 475
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
825-1162 |
6.80e-09 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 60.37 E-value: 6.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 825 QTQTAPDVLSSERTLELAQYKTKCESQSGFILHLRQLLSRGNTKFEALTVVIQHLLSERE-----EALKQHKTLSQELVS 899
Cdd:pfam02463 662 SEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEElladrVQEAQDKINEELKLL 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 900 LRGELVAASSACEKLEKARADLQTAYQEFVQKLNQQHQTDRTELENRLKDLYTAECEKLQSIY-IEEAEKYKTQLQEQFD 978
Cdd:pfam02463 742 KQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRaLEEELKEEAELLEEEQ 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 979 NLNAAHEttKLEIEASHSEKVELLKKTYETSLSEIKKSHEMEKKSLEDLLNEKQESLEKQINDLKSENDALNERLKSEEQ 1058
Cdd:pfam02463 822 LLIEQEE--KIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEK 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1059 KQLS-REKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQDMKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMA 1137
Cdd:pfam02463 900 KELEeESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMA 979
|
330 340
....*....|....*....|....*
gi 158706129 1138 ISRQLSTEQAALQESLEKESKVNKR 1162
Cdd:pfam02463 980 IEEFEEKEERYNKDELEKERLEEEK 1004
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
855-1170 |
9.11e-09 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 60.19 E-value: 9.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 855 ILHLRQLLSRGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSACEKLEKARADLqtayQEFVQKLnq 934
Cdd:pfam01576 231 IAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDL----GEELEAL-- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 935 qhqtdRTELENRLKDlyTAECEKLQSiyieEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKTYETSlSEIK 1014
Cdd:pfam01576 305 -----KTELEDTLDT--TAAQQELRS----KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQA-KRNK 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1015 KSHEMEKKSLEDLLNEKQESLeKQINDLKSENDalNERLKSEEQKQLSREKANSKNPQVMYLEQELESLKAVLEIKNEKL 1094
Cdd:pfam01576 373 ANLEKAKQALESENAELQAEL-RTLQQAKQDSE--HKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1095 HQQDMKLMKMEKLVDN-NTALVDKLKRFQqenEELKARMDKHMAIsRQLSTEQAALQESLEKESK----VNKRLSMENEE 1169
Cdd:pfam01576 450 NEAEGKNIKLSKDVSSlESQLQDTQELLQ---EETRQKLNLSTRL-RQLEDERNSLQEQLEEEEEakrnVERQLSTLQAQ 525
|
.
gi 158706129 1170 L 1170
Cdd:pfam01576 526 L 526
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
876-1127 |
1.15e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 876 IQHLLSEREEALKQHKTLSQeLVSLRGELvaASSACEKLEKARADLQTAYQEFVqKLNQQHQTDRTELE--NRLKDLYTA 953
Cdd:PRK03918 485 LEKVLKKESELIKLKELAEQ-LKELEEKL--KKYNLEELEKKAEEYEKLKEKLI-KLKGEIKSLKKELEklEELKKKLAE 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 954 ECEKLQSIYIEEAEKYKTQLQEQFDNLNAAHETTKlEIEASHSEKVELL--KKTYETSLSEIKKSHEMEKKSLEDL--LN 1029
Cdd:PRK03918 561 LEKKLDELEEELAELLKELEELGFESVEELEERLK-ELEPFYNEYLELKdaEKELEREEKELKKLEEELDKAFEELaeTE 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1030 EKQESLEKQINDLKSENDALNERLKSEEQKQLSREKAnSKNPQVMYLEQELESLKAVLE-IKNEK--LHQQDMKLMKMEK 1106
Cdd:PRK03918 640 KRLEELRKELEELEKKYSEEEYEELREEYLELSRELA-GLRAELEELEKRREEIKKTLEkLKEELeeREKAKKELEKLEK 718
|
250 260
....*....|....*....|.
gi 158706129 1107 LVDNNTALVDKLKRFQQENEE 1127
Cdd:PRK03918 719 ALERVEELREKVKKYKALLKE 739
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
831-1150 |
1.18e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 59.75 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 831 DVLSSERTlELAQYKTKCESQSGFILHLRQLL-----SRGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELV 905
Cdd:pfam15921 163 DMLEDSNT-QIEQLRKMMLSHEGVLQEIRSILvdfeeASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIF 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 906 AASsacEKLEKARADLQTAyqefVQKLNQQHQTDRTELENRLKDLYTAECEKLQSIYiEEAEKYKTQL---QEQFDNLNA 982
Cdd:pfam15921 242 PVE---DQLEALKSESQNK----IELLLQQHQDRIEQLISEHEVEITGLTEKASSAR-SQANSIQSQLeiiQEQARNQNS 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 983 AHETTKLEIEASHSE-KVEL--LKKTYETSLSEIKKS-----------------HEMEKKSLEDLLN---------EKQE 1033
Cdd:pfam15921 314 MYMRQLSDLESTVSQlRSELreAKRMYEDKIEELEKQlvlanseltearterdqFSQESGNLDDQLQklladlhkrEKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1034 SLEKQ---------------INDLKSEND----------ALNERLKSEEQKQLSREKA-----NSKNPQVMYLEQELESL 1083
Cdd:pfam15921 394 SLEKEqnkrlwdrdtgnsitIDHLRRELDdrnmevqrleALLKAMKSECQGQMERQMAaiqgkNESLEKVSSLTAQLEST 473
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158706129 1084 KAVLEIKNEKLHQQDMKLMKMEKLV-DNNTALVDKLKRFQQENEE---LKARMDKHMAISRQLSTEQAALQ 1150
Cdd:pfam15921 474 KEMLRKVVEELTAKKMTLESSERTVsDLTASLQEKERAIEATNAEitkLRSRVDLKLQELQHLKNEGDHLR 544
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
876-1175 |
1.57e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 876 IQHLLSEREEALKQHKTLSQELVSLRGELVAASSACEKLEKARADLQTAYQEfvqkLNQQHqtdrtelENRLKDLYTAEC 955
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRE----LTEEH-------RKELLEEYTAEL 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 956 EKLQSiYIEEAEKYKTQLQEqfdnlnaahETTKLEIEASHSEKVELLKKTYEtSLSEIKKshEMEKKSLEDL--LNEKQE 1033
Cdd:PRK03918 462 KRIEK-ELKEIEEKERKLRK---------ELRELEKVLKKESELIKLKELAE-QLKELEE--KLKKYNLEELekKAEEYE 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1034 SLEKQINDLKSENDALNERLKSEEQKQLSREKANSKnpqVMYLEQELESLKAVLEIKN-EKLHQQDMKLMKMEKLVDNNT 1112
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKK---LDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYL 605
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158706129 1113 ALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAALQESLEKESKVNKRLSMENEELLWKLH 1175
Cdd:PRK03918 606 ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEY 668
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
859-1171 |
1.99e-08 |
|
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: 58.58 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 859 RQLLSRGNTKFEALTVVIQHLLSEREE--ALKQHKTLS-QELVSLRGELVAASSACEKLEKARADLQTAYQEFVQKLnQQ 935
Cdd:pfam05483 369 QQRLEKNEDQLKIITMELQKKSSELEEmtKFKNNKEVElEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLL-QA 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 936 HQTDRTELENRLKDLYTAEceklqSIYIEEAEKYKTQLQEQ---------------FDNLNAAHETTKLEIE-ASHSEKV 999
Cdd:pfam05483 448 REKEIHDLEIQLTAIKTSE-----EHYLKEVEDLKTELEKEklknieltahcdkllLENKELTQEASDMTLElKKHQEDI 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1000 ELLKKTYETSLSEIKKSHEMEKKsLEDLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKA------------- 1066
Cdd:pfam05483 523 INCKKQEERMLKQIENLEEKEMN-LRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQmkilenkcnnlkk 601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1067 --NSKNPQVMYLEQELESLKAVLEIKNEKLHQQDMKLMKME-KLVDNNTALVDKLKRFQQENEELKARMDKHMAisrQLS 1143
Cdd:pfam05483 602 qiENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLElELASAKQKFEEIIDNYQKEIEDKKISEEKLLE---EVE 678
|
330 340
....*....|....*....|....*...
gi 158706129 1144 TEQAALQESLEKESKVNKRLSMENEELL 1171
Cdd:pfam05483 679 KAKAIADEAVKLQKEIDKRCQHKIAEMV 706
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
877-1154 |
3.14e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 58.26 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 877 QHLLSEREEALKQHKTLSQELVSLRGELVAASSACEKLEKARADLQTAYQEFVQKLnqqhqtdrTELENRLKDlytaECE 956
Cdd:pfam01576 22 QKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEIL--------HELESRLEE----EEE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 957 KLQSIYIEeaekyKTQLQEQFDNLNAahettKLEIEASHSEKVELLKKTYEtslSEIKKSHE-------------MEKKS 1023
Cdd:pfam01576 90 RSQQLQNE-----KKKMQQHIQDLEE-----QLDEEEAARQKLQLEKVTTE---AKIKKLEEdillledqnsklsKERKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1024 LEDLLNE------KQESLEKQINDLKSENDA----LNERLKSEEQKQLSREKANSK--------NPQVMYLEQELESLKA 1085
Cdd:pfam01576 157 LEERISEftsnlaEEEEKAKSLSKLKNKHEAmisdLEERLKKEEKGRQELEKAKRKlegestdlQEQIAELQAQIAELRA 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158706129 1086 VLEIKNEKLHQqdmKLMKMEKLVDNNTALVDKLKRFQQENEELKARMD-------KHMAISRQLSTEQAALQESLE 1154
Cdd:pfam01576 237 QLAKKEEELQA---ALARLEEETAQKNNALKKIRELEAQISELQEDLEseraarnKAEKQRRDLGEELEALKTELE 309
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
876-1128 |
5.84e-08 |
|
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: 57.34 E-value: 5.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 876 IQHLLSEREEALKQHKTLSQELVSLRGELVAASSACEKLEKARADLQTAYQefvqKLNQQHQ---TDRTELENRLKDLYT 952
Cdd:TIGR04523 372 IEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE----LLEKEIErlkETIIKNNSEIKDLTN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 953 AECEKlqSIYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEAShseKVELLKKTYE-TSLSEIKKSHEMEKKSLED---LL 1028
Cdd:TIGR04523 448 QDSVK--ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK---QKELKSKEKElKKLNEEKKELEEKVKDLTKkisSL 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1029 NEKQESLEKQINDLKSENDALNERLKSEEQ---KQLSREKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQDMKLMKME 1105
Cdd:TIGR04523 523 KEKIEKLESEKKEKESKISDLEDELNKDDFelkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLI 602
|
250 260
....*....|....*....|....*..
gi 158706129 1106 KLVDNNTALVDKLKR----FQQENEEL 1128
Cdd:TIGR04523 603 KEIEEKEKKISSLEKelekAKKENEKL 629
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
959-1163 |
8.39e-08 |
|
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: 55.93 E-value: 8.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 959 QSIYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELlkktyETSLSEIKKshemekksLEDLLNEKQESLEKQ 1038
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL-----ERRIAALAR--------RIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1039 INDLKSENDALNERLKsEEQKQLSREKAnsknpqVMYLEQELESLKAVLeiKNEKLHQQDMKLMKMEKLVDNNTALVDKL 1118
Cdd:COG4942 85 LAELEKEIAELRAELE-AQKEELAELLR------ALYRLGRQPPLALLL--SPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 158706129 1119 KRFQQENEELKARMDKHMAISRQLSTEQAALQESLEKESKVNKRL 1163
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
940-1171 |
9.72e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 9.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 940 RTELENRLKDLytaeceKLQSiyiEEAEKYKtQLQEQFDNLnaahettKLEIEASHSEKVELLKKTYETSLSEIKKSHEM 1019
Cdd:COG1196 195 LGELERQLEPL------ERQA---EKAERYR-ELKEELKEL-------EAELLLLKLRELEAELEELEAELEELEAELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1020 EKKSLEDL------LNEKQESLEKQINDLKSENDALNERLkSEEQKQLSREKANSKNpqvmyLEQELESLKAVLEIKNEK 1093
Cdd:COG1196 258 LEAELAELeaeleeLRLELEELELELEEAQAEEYELLAEL-ARLEQDIARLEERRRE-----LEERLEELEEELAELEEE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1094 LHQQDMKL---------------MKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAALQESLEKESK 1158
Cdd:COG1196 332 LEELEEELeeleeeleeaeeeleEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
250
....*....|...
gi 158706129 1159 VNKRLSMENEELL 1171
Cdd:COG1196 412 LLERLERLEEELE 424
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
915-1123 |
1.12e-07 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 55.07 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 915 EKARADLQTAYQEFVQKLNQQHQTDRTELENRLKDLYTAECEKLqsiyIEEAEKYKTQLQEQFDNLNAAHETTKleieaS 994
Cdd:cd22656 83 QNAGGTIDSYYAEILELIDDLADATDDEELEEAKKTIKALLDDL----LKEAKKYQDKAAKVVDKLTDFENQTE-----K 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 995 HSEKVELLKKTYETSLSeiKKSHEMEKKSLEDLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKA-------- 1066
Cdd:cd22656 154 DQTALETLEKALKDLLT--DEGGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLiadltaad 231
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158706129 1067 -------NSKNPQVMYLEQ----------ELESLKAVLEIKNEKLHQQDMKLMKMEKLVDNNTALVDKLKRFQQ 1123
Cdd:cd22656 232 tdldnllALIGPAIPALEKlqgawqaiatDLDSLKDLLEDDISKIPAAILAKLELEKAIEKWNELAEKADKFRQ 305
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
881-1170 |
1.15e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 56.29 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 881 SEREEALKQHKTLSQELVSLRGELVAASSACEKLEKARADLQTAYQEFVQKLNQQHQTDRTELEN-RLKDLYTAECEKLQ 959
Cdd:pfam05557 27 RARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKlNEKESQLADAREVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 960 SIYIEEAEKYKTQLQEQfdnlNAAHETTKLEIEASHsEKVELLKKTYeTSLSEIKKSHEMEKKSLEDLlNEKQESLEKQI 1039
Cdd:pfam05557 107 SCLKNELSELRRQIQRA----ELELQSTNSELEELQ-ERLDLLKAKA-SEAEQLRQNLEKQQSSLAEA-EQRIKELEFEI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1040 ---NDLKSENDALNERLKS--EEQKQLSR-----EKANSKNPQVMYLEQELESLK-------------AVLEIKNEKLHQ 1096
Cdd:pfam05557 180 qsqEQDSEIVKNSKSELARipELEKELERlrehnKHLNENIENKLLLKEEVEDLKrklereekyreeaATLELEKEKLEQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1097 qdmKLMKMEKLVDNNT-------ALVDKLKRFQQENEELKARMD------KHMAISR-QLSTEQAALQESLEKESKVNKR 1162
Cdd:pfam05557 260 ---ELQSWVKLAQDTGlnlrspeDLSRRIEQLQQREIVLKEENSsltssaRQLEKARrELEQELAQYLKKIEDLNKKLKR 336
|
....*...
gi 158706129 1163 LSMENEEL 1170
Cdd:pfam05557 337 HKALVRRL 344
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
840-1135 |
1.16e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 56.00 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 840 ELAQYKTKCESQSGFILHLRQL-------LSRGNTKFEALTVVIQHLLSEREEALKQHKTLSQE---------LVSLRGE 903
Cdd:PRK04778 127 ELQELLESEEKNREEVEQLKDLyrelrksLLANRFSFGPALDELEKQLENLEEEFSQFVELTESgdyveareiLDQLEEE 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 904 LVAASSACEKLEKARADLQTAYQEFVQKLNQQHQT--------DRTELENRLKDLYTA--ECEK-LQSIYIEEAEKYKTQ 972
Cdd:PRK04778 207 LAALEQIMEEIPELLKELQTELPDQLQELKAGYRElveegyhlDHLDIEKEIQDLKEQidENLAlLEELDLDEAEEKNEE 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 973 LQEQFDNLNAAHETtklEIEASHseKVELLKKTYETSLSEIKKSHEMEKKSLEDL-----LN----EKQESLEKQINDLK 1043
Cdd:PRK04778 287 IQERIDQLYDILER---EVKARK--YVEKNSDTLPDFLEHAKEQNKELKEEIDRVkqsytLNeselESVRQLEKQLESLE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1044 SENDALNERLksEEQKQLSREkansknpqvmyLEQELESLKAVL-EIKNEKLHQQDMkLMKMEKlvDNNTALvDKLKRFQ 1122
Cdd:PRK04778 362 KQYDEITERI--AEQEIAYSE-----------LQEELEEILKQLeEIEKEQEKLSEM-LQGLRK--DELEAR-EKLERYR 424
|
330
....*....|...
gi 158706129 1123 QENEELKARMDKH 1135
Cdd:PRK04778 425 NKLHEIKRYLEKS 437
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
913-1170 |
1.22e-07 |
|
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: 56.27 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 913 KLEKARADLQTAYQEFVQKLNQQHQT------DRTELENRLKDL-YTAECEKLQSIYIEEAEKYKT----QLQEQFDNLN 981
Cdd:pfam05483 216 KLKEDHEKIQHLEEEYKKEINDKEKQvsllliQITEKENKMKDLtFLLEESRDKANQLEEKTKLQDenlkELIEKKDHLT 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 982 AAHETTKLEIEASHS------EKVELLKKTY-------ETSLSEIKKSH--------EMEKK--SLEDLLNEKQESLEKQ 1038
Cdd:pfam05483 296 KELEDIKMSLQRSMStqkaleEDLQIATKTIcqlteekEAQMEELNKAKaahsfvvtEFEATtcSLEELLRTEQQRLEKN 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1039 INDLKSENDALNErlKSEEQKQLSREKANSknpqvmylEQELESLKAVLEiKNEKLHQQDMKLMKM-EKLVDNNTALVDK 1117
Cdd:pfam05483 376 EDQLKIITMELQK--KSSELEEMTKFKNNK--------EVELEELKKILA-EDEKLLDEKKQFEKIaEELKGKEQELIFL 444
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1118 LKRFQQENEELKARMDKHMAISRQLSTEQAALQESLEKESKVN-------KRLSMENEEL 1170
Cdd:pfam05483 445 LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNieltahcDKLLLENKEL 504
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
934-1085 |
2.48e-07 |
|
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: 53.00 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 934 QQHQTDRTELENRLKDLyTAEceklqsiyIEEAEKYKTQLQEQFDNLNAAHETTKLEIEA--SHSEKVELLKKTYETSLS 1011
Cdd:COG1579 13 QELDSELDRLEHRLKEL-PAE--------LAELEDELAALEARLEAAKTELEDLEKEIKRleLEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1012 EIKK-------SHEME-----KKSLEDL---LNEKQESLEKQINDLKSENDALNERLKsEEQKQLSREKANsknpqvmyL 1076
Cdd:COG1579 84 NVRNnkeyealQKEIEslkrrISDLEDEileLMERIEELEEELAELEAELAELEAELE-EKKAELDEELAE--------L 154
|
....*....
gi 158706129 1077 EQELESLKA 1085
Cdd:COG1579 155 EAELEELEA 163
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
868-1093 |
2.89e-07 |
|
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: 54.38 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 868 KFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSACEKLEKARADLQTAyqefVQKLNQQHQTDRTELENRL 947
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE----LAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 948 KDLYtaecEKLQSIYIEEAEKYKTQLQEQFDNLNAAHETTKLE-IEASHSEKVELLKKTYETsLSEIKKSHEMEKKSLED 1026
Cdd:COG4942 104 EELA----ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKyLAPARREQAEELRADLAE-LAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158706129 1027 LLNEKQESLeKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQvmYLEQELESLKAVLEIKNEK 1093
Cdd:COG4942 179 LLAELEEER-AALEALKAERQKLLARLEKELAELAAELAELQQEAE--ELEALIARLEAEAAAAAER 242
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
898-1174 |
3.01e-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: 55.07 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 898 VSLRGELVAASSACEKLEKARADLQTayqefVQKLNQQHQTDRTELENRLKDLytaeceklqSIYIEEAEKYKTQLQEQF 977
Cdd:TIGR02169 660 RAPRGGILFSRSEPAELQRLRERLEG-----LKRELSSLQSELRRIENRLDEL---------SQELSDASRKIGEIEKEI 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 978 DNLNAAHETTKLEIEAShsekvellkktyETSLSEIKKSHEMEKKSLEDLLNEKQEsLEKQINDLKSENDALNERLkSEE 1057
Cdd:TIGR02169 726 EQLEQEEEKLKERLEEL------------EEDLSSLEQEIENVKSELKELEARIEE-LEEDLHKLEEALNDLEARL-SHS 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1058 QKQLSREKANSKNPQVMYLEQELESLKAVLEikneKLHQQDMKLMK-MEKLVDNNTALVDKLKRFQQENEELKAR----- 1131
Cdd:TIGR02169 792 RIPEIQAELSKLEEEVSRIEARLREIEQKLN----RLTLEKEYLEKeIQELQEQRIDLKEQIKSIEKEIENLNGKkeele 867
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 158706129 1132 --MDKHMAISRQLSTEQAALQESLEKESKVNKRLSMENEELLWKL 1174
Cdd:TIGR02169 868 eeLEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQI 912
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
972-1155 |
3.21e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 972 QLQEQFDNLNAAH---ETTKLEIEA-----SHSEKVELLKKTYETsLSEIKKSHEMEKKSLE-DLLNEKQESLEKQINDL 1042
Cdd:COG4913 229 ALVEHFDDLERAHealEDAREQIELlepirELAERYAAARERLAE-LEYLRAALRLWFAQRRlELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1043 KSENDALNERLKSEEQK--QLSREKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQDmKLMKM---------EKLVDNN 1111
Cdd:COG4913 308 EAELERLEARLDALREEldELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLE-ALLAAlglplpasaEEFAALR 386
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 158706129 1112 TALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAALQ---ESLEK 1155
Cdd:COG4913 387 AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEaeiASLER 433
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
876-1052 |
3.30e-07 |
|
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: 52.62 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 876 IQHLLSEREEALKQHKTLSQELVSLRGELVAASSACEKLEKARADLqtayqefvqklnqqhQTDRTELENRLKDLYtaec 955
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDL---------------EKEIKRLELEIEEVE---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 956 eklqsiyiEEAEKYKTQL-----QEQFDNLNAAHETTKLEIEASHSEKVELLKK--TYETSLSEIKKshemEKKSLEDLL 1028
Cdd:COG1579 73 --------ARIKKYEEQLgnvrnNKEYEALQKEIESLKRRISDLEDEILELMERieELEEELAELEA----ELAELEAEL 140
|
170 180
....*....|....*....|....
gi 158706129 1029 NEKQESLEKQINDLKSENDALNER 1052
Cdd:COG1579 141 EEKKAELDEELAELEAELEELEAE 164
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
855-1177 |
3.70e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 54.80 E-value: 3.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 855 ILHLRQLLSRGNTKFEALTVVIQHLlserEEALKQhktLSQELVSLRGELVAASSACEKLEKARADLQTAYQEFVQKLNQ 934
Cdd:pfam01576 519 LSTLQAQLSDMKKKLEEDAGTLEAL----EEGKKR---LQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDH 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 935 QHQT-----------------------------DRTELENRLKDL----YTAECEKLQSIyIEEAEKYKTQLQEQFDNL- 980
Cdd:pfam01576 592 QRQLvsnlekkqkkfdqmlaeekaisaryaeerDRAEAEAREKETralsLARALEEALEA-KEELERTNKQLRAEMEDLv 670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 981 -------NAAHE------------------TTKLEIEASHSEKVELlkkTYETSLSEIKKSHEMEKKSLEDLLNEKQESL 1035
Cdd:pfam01576 671 sskddvgKNVHElerskraleqqveemktqLEELEDELQATEDAKL---RLEVNMQALKAQFERDLQARDEQGEEKRRQL 747
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1036 EKQINDLKSENDalnerlksEEQKQLSREKANSKNpqvmyLEQELESLKAVLEIKNEKLHQQDMKLMKMEKlvdnntalv 1115
Cdd:pfam01576 748 VKQVRELEAELE--------DERKQRAQAVAAKKK-----LELDLKELEAQIDAANKGREEAVKQLKKLQA--------- 805
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158706129 1116 dKLKRFQQENEELKARMDKHMAISRQ-------LSTEQAALQESLEKESKVNKRLSMENEELLWKLHNG 1177
Cdd:pfam01576 806 -QMKDLQRELEEARASRDEILAQSKEsekklknLEAELLQLQEDLAASERARRQAQQERDELADEIASG 873
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
884-1101 |
3.78e-07 |
|
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: 54.84 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 884 EEALKQHKTLSQELVSLRGELVAASSACEKLEKARADLQTAYQEFVQKLNQQHQTDRTELENRLKDLYTA------ECEK 957
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAvakdrsELEA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 958 LQS---IYIEE-AEKYKT------QLQEQFDNLNAAH--------------ETTKLEIEASHSEKVELLKKTYETSLSEI 1013
Cdd:pfam12128 327 LEDqhgAFLDAdIETAAAdqeqlpSWQSELENLEERLkaltgkhqdvtakyNRRRSKIKEQNNRDIAGIKDKLAKIREAR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1014 KKSHEMEKKSLEDLLNEKQESLEKQINDLKSENDALNERL------------KSEEQKQL---------SREKANSKNPQ 1072
Cdd:pfam12128 407 DRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLgelklrlnqataTPELLLQLenfderierAREEQEAANAE 486
|
250 260
....*....|....*....|....*....
gi 158706129 1073 VMYLEQELESLKAVLEIKNEKLHQQDMKL 1101
Cdd:pfam12128 487 VERLQSELRQARKRRDQASEALRQASRRL 515
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
836-1176 |
3.86e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 836 ERTLELAQYKTKCESQSGFILHLRQLLSRGN---TKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELvaassacE 912
Cdd:PRK03918 283 KELKELKEKAEEYIKLSEFYEEYLDELREIEkrlSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL-------E 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 913 KLEKAradlQTAYQEFVQKLNQQHQtdrteLENRLKDLYTAECEKLqsiyIEEAEKYKTQLQEQFDNLNAahettklEIE 992
Cdd:PRK03918 356 ELEER----HELYEEAKAKKEELER-----LKKRLTGLTPEKLEKE----LEELEKAKEEIEEEISKITA-------RIG 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 993 ASHSEKVELlkktyETSLSEIKKS--------HEMEKKSLEDLLNEKQESLEKQINDLKsENDALNERLKSEEQKQlsrE 1064
Cdd:PRK03918 416 ELKKEIKEL-----KKAIEELKKAkgkcpvcgRELTEEHRKELLEEYTAELKRIEKELK-EIEEKERKLRKELREL---E 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1065 KANSKNPQVMYLEQELESLKAVleikNEKLHQQDmklmkmeklvdnntalVDKLKRFQQENEELKARMDKhmaisrqLST 1144
Cdd:PRK03918 487 KVLKKESELIKLKELAEQLKEL----EEKLKKYN----------------LEELEKKAEEYEKLKEKLIK-------LKG 539
|
330 340 350
....*....|....*....|....*....|..
gi 158706129 1145 EQAALQESLEKESKVNKRLsmenEELLWKLHN 1176
Cdd:PRK03918 540 EIKSLKKELEKLEELKKKL----AELEKKLDE 567
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1007-1156 |
5.81e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 5.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1007 ETSLSEIKKSHEMEKKSLEDL------LNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQVMYLEQEL 1080
Cdd:COG3883 22 QKELSELQAELEAAQAELDALqaeleeLNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGS 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158706129 1081 ES-LKAVLEIKN--EKLHQQDMklmkMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAALQESLEKE 1156
Cdd:COG3883 102 VSyLDVLLGSESfsDFLDRLSA----LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
877-1170 |
6.02e-07 |
|
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: 53.87 E-value: 6.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 877 QHLLSEREEALKQHKTLSQELVSLRGELVAASSACEKLEKARADLQTAYQEFVQKLNQ---QHQTDRTELENRLKDLYTA 953
Cdd:TIGR04523 200 ELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQlkdEQNKIKKQLSEKQKELEQN 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 954 EC------EKLQSIY--IEEAEKYKTQ-----LQEQFDNLNAAHETTKLEIEASHS------EKVELLKKTYETSLSE-I 1013
Cdd:TIGR04523 280 NKkikeleKQLNQLKseISDLNNQKEQdwnkeLKSELKNQEKKLEEIQNQISQNNKiisqlnEQISQLKKELTNSESEnS 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1014 KKSHEMEKKS--LEDLLNEKQ------ESLEKQINDLKSE-------NDALNERLKSEEQ--KQLSREKANSKNpQVMYL 1076
Cdd:TIGR04523 360 EKQRELEEKQneIEKLKKENQsykqeiKNLESQINDLESKiqnqeklNQQKDEQIKKLQQekELLEKEIERLKE-TIIKN 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1077 EQELESLK---AVLEIKNEKLH----QQDMKLMKMEKLVDNN-TALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAA 1148
Cdd:TIGR04523 439 NSEIKDLTnqdSVKELIIKNLDntreSLETQLKVLSRSINKIkQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKK 518
|
330 340
....*....|....*....|..
gi 158706129 1149 LQESLEKESKVNKRLSMENEEL 1170
Cdd:TIGR04523 519 ISSLKEKIEKLESEKKEKESKI 540
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
921-1170 |
6.45e-07 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 53.81 E-value: 6.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 921 LQTAYQEFVQKLNQQHQTDRTElENRLKDLYTAECEKLqsiyIEEAEKYKT----QLQEQFDNLNAAHETTKLEIEASH- 995
Cdd:COG5185 222 LEKAKEIINIEEALKGFQDPES-ELEDLAQTSDKLEKL----VEQNTDLRLeklgENAESSKRLNENANNLIKQFENTKe 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 996 --SEKVELLKKTYET-SLSEIKKSHEmEKKSLEDLLNEKQESLEKQINDLKSENDALNERLKS--EEQKQLSREKANSKN 1070
Cdd:COG5185 297 kiAEYTKSIDIKKATeSLEEQLAAAE-AEQELEESKRETETGIQNLTAEIEQGQESLTENLEAikEEIENIVGEVELSKS 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1071 pqvmylEQELESLKAVLEIKNEKLHQQDMKLMKMEKlvDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAALQ 1150
Cdd:COG5185 376 ------SEELDSFKDTIESTKESLDEIPQNQRGYAQ--EILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELI 447
|
250 260
....*....|....*....|....*
gi 158706129 1151 ESLEK-----ESKVNKRLSMENEEL 1170
Cdd:COG5185 448 SELNKvmreaDEESQSRLEEAYDEI 472
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
837-1157 |
6.67e-07 |
|
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: 54.07 E-value: 6.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 837 RTLElAQYKTKCESQSGFILHLRQLLSRGNTKFEALTVVIQHLLSEREEALKQHKtlsQELVSLRGELVAASSACEKLEK 916
Cdd:pfam12128 293 RTLD-DQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQ---EQLPSWQSELENLEERLKALTG 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 917 ARADLQTAYQEFVQKLNQQHQTDRTELENRL------KDLYTAECE----KLQSIYIEEAEKYKTQLQEQFDNLNAAHET 986
Cdd:pfam12128 369 KHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLakireaRDRQLAVAEddlqALESELREQLEAGKLEFNEEEYRLKSRLGE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 987 TKLEIEASHSEKVELLKKtyETSLSEIKKSHEMEKKSledllNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKA 1066
Cdd:pfam12128 449 LKLRLNQATATPELLLQL--ENFDERIERAREEQEAA-----NAEVERLQSELRQARKRRDQASEALRQASRRLEERQSA 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1067 NSKNPQVM---------YLEQEL----ESLKAVleIKNEKLHQQDMKLMKMEKLVDNNTALVD---KLKRFQ-----QEN 1125
Cdd:pfam12128 522 LDELELQLfpqagtllhFLRKEApdweQSIGKV--ISPELLHRTDLDPEVWDGSVGGELNLYGvklDLKRIDvpewaASE 599
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 158706129 1126 EELKARMDK-----------HMAISRQLSTEQAALQESLEKES 1157
Cdd:pfam12128 600 EELRERLDKaeealqsarekQAAAEEQLVQANGELEKASREET 642
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
912-1102 |
6.80e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 6.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 912 EKLEKARADLQTAYQEFVQKLNQQHqtdrtELENRLKDLYTAeceklqsiyIEEAEKYKTQLQEQFDNLNAAHETTKLEI 991
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELE-----ELEEELEELEAE---------LEELREELEKLEKLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 992 E-ASHSEKVELLKKTYET------SLSEIKKSHEMEKKSLEDLLNEKQESLEKQINDLKSENDALNERLKS--EEQKQLS 1062
Cdd:COG4717 140 ElAELPERLEELEERLEElreleeELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEleEELEEAQ 219
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 158706129 1063 REKANsknpqvmyLEQELESLKAVLEI--KNEKLHQQDMKLM 1102
Cdd:COG4717 220 EELEE--------LEEELEQLENELEAaaLEERLKEARLLLL 253
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
912-1158 |
7.26e-07 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 53.19 E-value: 7.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 912 EKLEKARADLQTAYQEFVQKLNQQHQtdrtelenRLKDLYTAECEKL--QSIYIEEAEKYKTQLQEQFDNLNAAHETTKL 989
Cdd:pfam03528 11 AELEKENAEFYRLKQQLEAEFNQKRA--------KFKELYLAKEEDLkrQNAVLQEAQVELDALQNQLALARAEMENIKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 990 EIEASHSEKVEllkktyetSLSEIKKSHEMEKKSLEDLLNEK----------------------QESLEKQINDLKSEND 1047
Cdd:pfam03528 83 VATVSENTKQE--------AIDEVKSQWQEEVASLQAIMKETvreyevqfhrrleqeraqwnqyRESAEREIADLRRRLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1048 ALNERLKSEEQKQLSREKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQDMKLMKmeklvdnntalvdKLKRFQQENEE 1127
Cdd:pfam03528 155 EGQEEENLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKELEASKMK-------------ELNHYLEAEKS 221
|
250 260 270
....*....|....*....|....*....|.
gi 158706129 1128 LKARMDKHMAIsrqLSTEQAALQESLEKESK 1158
Cdd:pfam03528 222 CRTDLEMYVAV---LNTQKSVLQEDAEKLRK 249
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
875-1164 |
7.38e-07 |
|
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: 53.49 E-value: 7.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 875 VIQHLLSEREEALK----QHKTLSQELVSLRGELVAASSaceKLEKARADLQTAYQEFVQKlNQQHQTDRTELENRLKDL 950
Cdd:TIGR04523 58 NLDKNLNKDEEKINnsnnKIKILEQQIKDLNDKLKKNKD---KINKLNSDLSKINSEIKND-KEQKNKLEVELNKLEKQK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 951 ytAECEKLQSIYIEEAEKYKTQLQEqfdnLNAAHETTKLEIEASHSEKVELLKK--TYETSLSEIKKSHEMEKKSLEDL- 1027
Cdd:TIGR04523 134 --KENKKNIDKFLTEIKKKEKELEK----LNNKYNDLKKQKEELENELNLLEKEklNIQKNIDKIKNKLLKLELLLSNLk 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1028 -LNEKQESLEKQINDLKSENDALNERLKsEEQKQLSREKA--NSKNPQVMYLEQELESLKAVLEIKNEKLHQQDMKLMKM 1104
Cdd:TIGR04523 208 kKIQKNKSLESQISELKKQNNQLKDNIE-KKQQEINEKTTeiSNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL 286
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158706129 1105 EKLVDNNTALVDKLKRFQQEN--EELKARMDKhmaISRQLSTEQAALQESLEKESKVNKRLS 1164
Cdd:TIGR04523 287 EKQLNQLKSEISDLNNQKEQDwnKELKSELKN---QEKKLEEIQNQISQNNKIISQLNEQIS 345
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
919-1135 |
8.21e-07 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 53.32 E-value: 8.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 919 ADLQTAYQEFvqkLNQQHQTDRTELENRLKDLYTA--ECEK-LQSIYIEEAEKYKTQLQEQFDNLNAAHETtklEIEASH 995
Cdd:pfam06160 214 EELKEGYREM---EEEGYALEHLNVDKEIQQLEEQleENLAlLENLELDEAEEALEEIEERIDQLYDLLEK---EVDAKK 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 996 seKVELLKKTYETSLSEIKKSHEMEKKSLEDL-----LN----EKQESLEKQINDLKSENDALNERLKSEEQkqlsreka 1066
Cdd:pfam06160 288 --YVEKNLPEIEDYLEHAEEQNKELKEELERVqqsytLNenelERVRGLEKQLEELEKRYDEIVERLEEKEV-------- 357
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158706129 1067 nsknPQVMYLEQELESLKAVLEIKNEklhQQDMK--LMKMEKlvDNNTALvDKLKRFQQENEELKARMDKH 1135
Cdd:pfam06160 358 ----AYSELQEELEEILEQLEEIEEE---QEEFKesLQSLRK--DELEAR-EKLDEFKLELREIKRLVEKS 418
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
868-1155 |
9.41e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 9.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 868 KFEALTVVIQHLLSERE----EALKQHKTLSQELVSLRGELVAASSACEKLEKARADLQTAyqefvqklnqqhqtdRTEL 943
Cdd:PRK03918 183 KFIKRTENIEELIKEKEkeleEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEL---------------EKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 944 ENRLKDLYTAEcEKLQSI--YIEEAEKYKTQLQEQfdnlnaAHETTKLEIEASHSEKVELLKKTYETSLSEIKKshemEK 1021
Cdd:PRK03918 248 ESLEGSKRKLE-EKIRELeeRIEELKKEIEELEEK------VKELKELKEKAEEYIKLSEFYEEYLDELREIEK----RL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1022 KSLEDLLNEkqesLEKQINDLKSENDALNERLKSEEqkqlsrekansknpqvmyleqELESLKAVLEIKNEKLHQQDMKL 1101
Cdd:PRK03918 317 SRLEEEING----IEERIKELEEKEERLEELKKKLK---------------------ELEKRLEELEERHELYEEAKAKK 371
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 158706129 1102 MKMEKLVDNNTA-----LVDKLKRFQQENEELKARMDKHMAISRQLSTEQAALQESLEK 1155
Cdd:PRK03918 372 EELERLKKRLTGltpekLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
880-1068 |
1.05e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 880 LSEREEALKQHKTLSQELVSLRGELVAASSACEKLEKARADLQTAYQEFVQKL-NQQHQTDRTELENRLKDLytaeCEKL 958
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqLLPLYQELEALEAELAEL----PERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 959 QSIYiEEAEKYKtQLQEQFDNLNAAHETTKLEIEashsEKVELLKKTYETSLSEIKKSHEMekksledlLNEKQESLEKQ 1038
Cdd:COG4717 149 EELE-ERLEELR-ELEEELEELEAELAELQEELE----ELLEQLSLATEEELQDLAEELEE--------LQQRLAELEEE 214
|
170 180 190
....*....|....*....|....*....|
gi 158706129 1039 INDLKSENDALNERLKSEEQKQLSREKANS 1068
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
856-1174 |
1.05e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.60 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 856 LHLRQLLSRGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASsacEKLEKARADLQTAYQEfVQKLNQQ 935
Cdd:COG4372 13 LSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLE---EELEQARSELEQLEEE-LEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 936 HQTDRTELENRLKDLYTA--ECEKLQSiYIEEAEKYKTQLQEQFDNLNAAHEttklEIEASHSEKVELLKKtyetslsei 1013
Cdd:COG4372 89 LQAAQAELAQAQEELESLqeEAEELQE-ELEELQKERQDLEQQRKQLEAQIA----ELQSEIAEREEELKE--------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1014 kkshemekksledlLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKnpqvmYLEQELESLKAVLEIKNEK 1093
Cdd:COG4372 155 --------------LEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNA-----EKEEELAEAEKLIESLPRE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1094 LHQQDMKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAALQESLEKESKVNKRLSMENEELLWK 1173
Cdd:COG4372 216 LAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALEL 295
|
.
gi 158706129 1174 L 1174
Cdd:COG4372 296 K 296
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
833-1171 |
1.21e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 52.87 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 833 LSSERTLELAQYKTKCESQS-GFILHLRQLLSRGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSAC 911
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETrSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 912 EKLEKARADLQTAYQEFVQKLNQQHQTdRTELENRLKDLyTAECEKLQSIyIEEAEKYKTQLQEQFDNLNAAHETTKlei 991
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQ-RAELAEKLSKL-QSELESVSSL-LNEAEGKNIKLSKDVSSLESQLQDTQ--- 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 992 eashsekvELLKKtyET----SLSEIKKSHEMEKKSLEDLLNEKQES---LEKQINDL---------KSENDALNERLKS 1055
Cdd:pfam01576 475 --------ELLQE--ETrqklNLSTRLRQLEDERNSLQEQLEEEEEAkrnVERQLSTLqaqlsdmkkKLEEDAGTLEALE 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1056 EEQKQLSREkANSKNPQvmylEQELESLKAVLEIKNEKLHQQ-DMKLMKMEKLVDNNTALVDKLKRFQQENEELKA---- 1130
Cdd:pfam01576 545 EGKKRLQRE-LEALTQQ----LEEKAAAYDKLEKTKNRLQQElDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAisar 619
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 158706129 1131 ---RMDKHMAISRQ-------LSTEQAALQESLEKESKVNKRLSMENEELL 1171
Cdd:pfam01576 620 yaeERDRAEAEAREketralsLARALEEALEAKEELERTNKQLRAEMEDLV 670
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
859-1170 |
1.37e-06 |
|
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: 52.92 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 859 RQLLSRGNTKFEALTVVIqhllSEREEALKQhktLSQELVSLRGELVAASSACEKLEKARADLQTAYQEFVQKLnqqhQT 938
Cdd:pfam12128 707 EQKREARTEKQAYWQVVE----GALDAQLAL---LKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKL----KR 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 939 DRTELENRLKDlytaeCEKLQSiyieEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSE-KVELLKKTYETSLSeiKKSH 1017
Cdd:pfam12128 776 EIRTLERKIER-----IAVRRQ----EVLRYFDWYQETWLQRRPRLATQLSNIERAISElQQQLARLIADTKLR--RAKL 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1018 EMEKKSLEDLLNEKQESLEK-----------------------------QINDLKSENDALNERLKSE------------ 1056
Cdd:pfam12128 845 EMERKASEKQQVRLSENLRGlrcemsklatlkedanseqaqgsigerlaQLEDLKLKRDYLSESVKKYvehfknviadhs 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1057 -----EQKQLSREKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQDMKLMKMEKLVDNN-TALVDKLKRFQQeneelka 1130
Cdd:pfam12128 925 gsglaETWESLREEDHYQNDKGIRLLDYRKLVPYLEQWFDVRVPQSIMVLREQVSILGVDlTEFYDVLADFDR------- 997
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 158706129 1131 RMDkhmAISRQLSTEQAALQEsLEKESKVNKRLSMENEEL 1170
Cdd:pfam12128 998 RIA---SFSRELQREVGEEAF-FEGVSESAVRIRSKVSEL 1033
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
868-1166 |
1.39e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.20 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 868 KFEALTVVIQHLLSEREEALKQHKtlsqELVSLRGELVAASSACEKLEKARADLQTAYQEFVQKLNQQHQTDRTELEnRL 947
Cdd:pfam07888 81 RVAELKEELRQSREKHEELEEKYK----ELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELE-RM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 948 KDlytaeceklqsiyieEAEKYKTQLQEQfdnlNAAHETTKLEIEASHSEKVELLKKtyetsLSEIKKSHEMEKKSLEDL 1027
Cdd:pfam07888 156 KE---------------RAKKAGAQRKEE----EAERKQLQAKLQQTEEELRSLSKE-----FQELRNSLAQRDTQVLQL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1028 LNEKQESLEK--QINDLKSENDALNERLKSeeqkqlSREKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQDMKLMKME 1105
Cdd:pfam07888 212 QDTITTLTQKltTAHRKEAENEALLEELRS------LQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLT 285
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158706129 1106 -KLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAALQESLEKESKVNKRLSME 1166
Cdd:pfam07888 286 lQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVE 347
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
884-1169 |
1.53e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.43 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 884 EEALKQHKTLSQELVSLRGELVAAssacEKLEKARADLQTA-YQEFVQ-KLNQQHQTDRTELENRLKDLYTAECEKLQSI 961
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEA----EKARQAEMDRQAAiYAEQERmAMERERELERIRQEERKRELERIRQEEIAME 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 962 YIEEAEKYKTQLQEQFDN------LNAAHETTKLEIEasHSEKVELLKKTYETSLSEIKKSHEMEKKSLED-----LLNE 1030
Cdd:pfam17380 374 ISRMRELERLQMERQQKNervrqeLEAARKVKILEEE--RQRKIQQQKVEMEQIRAEQEEARQREVRRLEEerareMERV 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1031 KQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQVMYLEQELESLK-AVLEIKNEKlhqqdmKLMKMEkLVD 1109
Cdd:pfam17380 452 RLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKqAMIEEERKR------KLLEKE-MEE 524
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158706129 1110 NNTALVDKLKRFQQENEELKAR-MDKHMAISRQL--STEQAALQESLEKESKVNKRLsMENEE 1169
Cdd:pfam17380 525 RQKAIYEEERRREAEEERRKQQeMEERRRIQEQMrkATEERSRLEAMEREREMMRQI-VESEK 586
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
993-1163 |
1.79e-06 |
|
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: 50.69 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 993 ASHSEKVELLK-KTYETSLSEIK---KSHEMEKKSLEDLLNEKQ----------ESLEKQINDLKSENDALNERLKSEEQ 1058
Cdd:COG1579 1 AMPEDLRALLDlQELDSELDRLEhrlKELPAELAELEDELAALEarleaaktelEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1059 KQlsreKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQDMKLMKMEKLVDnntALVDKLKRFQQENEELKARMDkhmAI 1138
Cdd:COG1579 81 QL----GNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELA---ELEAELAELEAELEEKKAELD---EE 150
|
170 180
....*....|....*....|....*.
gi 158706129 1139 SRQLSTEQAALQESLEK-ESKVNKRL 1163
Cdd:COG1579 151 LAELEAELEELEAEREElAAKIPPEL 176
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
879-1128 |
1.88e-06 |
|
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: 52.28 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 879 LLSEREEALKQHKTLSQElVSLRGELVAASSACEKLEKARADLQTAYQEFVQKLNQQHQTDRTELENRLKDLYTAECEKL 958
Cdd:TIGR00618 612 CEQHALLRKLQPEQDLQD-VRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKE 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 959 QSIYIEEAEKYK-TQLQE----------QFDNLNAAHETTKLEIEASHSEKVELLKKTYETSLSEIKKSHEMEKKSLEDL 1027
Cdd:TIGR00618 691 QLTYWKEMLAQCqTLLRElethieeydrEFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEV 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1028 LNEKQ--ESLEKQINDLKSENDALNER-----LKSEEQKQLSREKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQDMK 1100
Cdd:TIGR00618 771 TAALQtgAELSHLAAEIQFFNRLREEDthllkTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQ 850
|
250 260
....*....|....*....|....*...
gi 158706129 1101 LMKMEKLVDNNTALVDKLKRFQQENEEL 1128
Cdd:TIGR00618 851 LLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
957-1170 |
2.34e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 957 KLQSIYIEEAEKYKTQLQEQFDNL------NAAHETTKLE------IEASHSEKVELLKKTYETSLSEIKKSHEMEKK-- 1022
Cdd:COG4717 2 KIKELEIYGFGKFRDRTIEFSPGLnviygpNEAGKSTLLAfiramlLERLEKEADELFKPQGRKPELNLKELKELEEElk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1023 -------SLEDLLNEKQEsLEKQINDLKSENDALNERLKSEEQKQlsrekansknpQVMYLEQELESLKAVLEIKNEKLH 1095
Cdd:COG4717 82 eaeekeeEYAELQEELEE-LEEELEELEAELEELREELEKLEKLL-----------QLLPLYQELEALEAELAELPERLE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158706129 1096 QQDMKLMKMEklvdnntALVDKLKRFQQENEELKARMDKHMaisRQLSTE-QAALQESLEKESKVNKRLSMENEEL 1170
Cdd:COG4717 150 ELEERLEELR-------ELEEELEELEAELAELQEELEELL---EQLSLAtEEELQDLAEELEELQQRLAELEEEL 215
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
855-1071 |
2.38e-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: 51.30 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 855 ILHLRQLLSRGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSACEKLEKARADLQTAYQEFVQKLNQ 934
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 935 QHQTDRTELENRLKDLYTAEcekLQSIYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKTYE--TSLSE 1012
Cdd:COG4942 116 LGRQPPLALLLSPEDFLDAV---RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEerAALEA 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 158706129 1013 IKKshemEKKSLEDLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNP 1071
Cdd:COG4942 193 LKA----ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
963-1170 |
3.67e-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: 51.60 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 963 IEEA---EKYKTQLQEQFDNLNAAHET-TKLE-IEASHSEKVELLKKTYETSLSEIKKSHEMEKKSLEDLLNEKqESLEK 1037
Cdd:TIGR02168 161 FEEAagiSKYKERRKETERKLERTRENlDRLEdILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRL-EELRE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1038 QINDLKSENDALNERLKS-EEQKQLSREKANSKNPQVMYLEQELESL-KAVLEIKNEklhQQDMKLMKMEkLVDNNTALV 1115
Cdd:TIGR02168 240 ELEELQEELKEAEEELEElTAELQELEEKLEELRLEVSELEEEIEELqKELYALANE---ISRLEQQKQI-LRERLANLE 315
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 158706129 1116 DKLKRFQQENEELKARMDKHMAISRQLSTEQAALQESLEKESKVNKRLSMENEEL 1170
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
963-1171 |
4.61e-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: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 963 IEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKtyetsLSEIKKSHEMEKKSLEDLLNEkQESLEKQINDL 1042
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE-----LEELSRQISALRKDLARLEAE-VEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1043 KSEndalneRLKSEEQKQLSREKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQDMKLMKMEK----LVDNNTALVDKL 1118
Cdd:TIGR02168 753 SKE------LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAeltlLNEEAANLRERL 826
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 158706129 1119 KRFQQENEELKARMDKHMAISRQLSTEQAALQESLEKESKVNKRLSMENEELL 1171
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL 879
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
915-1104 |
6.40e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.60 E-value: 6.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 915 EKARADLQTAYQEF---VQKLNQQhqtdRTELENRLKdlytaECEKLqsiyIEEAEKYKTQLQEQFDNLNAAHETTKLEi 991
Cdd:PRK00409 505 EEAKKLIGEDKEKLnelIASLEEL----ERELEQKAE-----EAEAL----LKEAEKLKEELEEKKEKLQEEEDKLLEE- 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 992 eashsekvelLKKTYETSLSEIKKSHEMEKKSLEDLLNEKQESLEKQinDLKSENDALNERLKSEEQKQLSrEKANSKNP 1071
Cdd:PRK00409 571 ----------AEKEAQQAIKEAKKEADEIIKELRQLQKGGYASVKAH--ELIEARKRLNKANEKKEKKKKK-QKEKQEEL 637
|
170 180 190
....*....|....*....|....*....|....*.
gi 158706129 1072 QV---MYLEQeLESLKAVLEIKNEKLHQQDMKLMKM 1104
Cdd:PRK00409 638 KVgdeVKYLS-LGQKGEVLSIPDDKEAIVQAGIMKM 672
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
876-1125 |
7.55e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 876 IQHLLSEREEALKQHKTLSQELVSLRGELVAASSACEKLEKaRADLQTAYQEFVQKLNQQHQTDRTELENRLkdlytaec 955
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE-ELQLEELEQEIAALLAEAGVEDEEELRAAL-------- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 956 eklqsiyiEEAEKYKtQLQEQFDNLNAahettklEIEASHSEKVELLKKTYETSLSEikkshEMEKksledlLNEKQESL 1035
Cdd:COG4717 392 --------EQAEEYQ-ELKEELEELEE-------QLEELLGELEELLEALDEEELEE-----ELEE------LEEELEEL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1036 EKQINDLKSENDALNERLKS-EEQKQLSRekansknpqvmyLEQELESLKAVLeiknEKLHQQDMKLMKMEKLVDnntal 1114
Cdd:COG4717 445 EEELEELREELAELEAELEQlEEDGELAE------------LLQELEELKAEL----RELAEEWAALKLALELLE----- 503
|
250
....*....|.
gi 158706129 1115 vDKLKRFQQEN 1125
Cdd:COG4717 504 -EAREEYREER 513
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
867-1072 |
8.04e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 8.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 867 TKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSACEKLEKARADLQTAyqefVQKLNQQHQTDRTELENR 946
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE----IAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 947 LKDLYTAeceKLQSIYIE---EAEKYkTQLQEQFDNLNAAHETTKLEIEASHSEKVELlkKTYETSLSEIKKSHEMEKKS 1023
Cdd:COG3883 92 ARALYRS---GGSVSYLDvllGSESF-SDFLDRLSALSKIADADADLLEELKADKAEL--EAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 158706129 1024 LEDL---LNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQ 1072
Cdd:COG3883 166 LEAAkaeLEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
870-1169 |
8.06e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.50 E-value: 8.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 870 EALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSACEKLEKARADLQTAYQEFvqklnQQHQTDRTELENrlkd 949
Cdd:pfam15921 475 EMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQEL-----QHLKNEGDHLRN---- 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 950 lYTAECEKLQsIYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKTYETSLsEIKkshemEKKSLEDLLN 1029
Cdd:pfam15921 546 -VQTECEALK-LQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRL-ELQ-----EFKILKDKKD 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1030 EKQESLEKQINDLKSEN----DALNERLKS-----EEQKQLSREKANSKNpQVMYLEQELESLKAVLEIKNEKLHQQDMK 1100
Cdd:pfam15921 618 AKIRELEARVSDLELEKvklvNAGSERLRAvkdikQERDQLLNEVKTSRN-ELNSLSEDYEVLKRNFRNKSEEMETTTNK 696
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158706129 1101 L-MKMEKLVDNNTALVDKLKRFQQENE---ELKARMDKHMAISR-QLSTEQAALQESLEKESKVNKRLSMENEE 1169
Cdd:pfam15921 697 LkMQLKSAQSELEQTRNTLKSMEGSDGhamKVAMGMQKQITAKRgQIDALQSKIQFLEEAMTNANKEKHFLKEE 770
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
840-1131 |
8.35e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 8.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 840 ELAQYKTKCESQSGFILHLRQLLSRGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSACEKLEKARA 919
Cdd:COG4372 60 ELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 920 DLQTAYQEFVQKLNQQhQTDRTELENRLKDLYtaecEKLQSIYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKV 999
Cdd:COG4372 140 ELQSEIAEREEELKEL-EEQLESLQEELAALE----QELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1000 EllkktyetsLSEIKKSHEMEKKSLEDLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQVMYLEQE 1079
Cdd:COG4372 215 E---------LAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALEL 285
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 158706129 1080 LESLKAVLEIKNEKLHQQDMKLMKMEKLVDNNTALVDKLKRFQQENEELKAR 1131
Cdd:COG4372 286 EALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLA 337
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
882-1171 |
8.49e-06 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 49.68 E-value: 8.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 882 EREEALKQHKTL-SQELVSLRGELVAASSACEKLEKARADLQTAYQEFVQK-----LNQQHQTDRTELENRLKDLYTAEC 955
Cdd:pfam15742 41 GKNLDLKQHNSLlQEENIKIKAELKQAQQKLLDSTKMCSSLTAEWKHCQQKireleLEVLKQAQSIKSQNSLQEKLAQEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 956 EKLQsiyieEAEKYKTQLQEQfdnLNAAHETTKLEIEASHSEKVELLKKTYETSLSEIKkSHEMEKKSLEDLLNEKQESL 1035
Cdd:pfam15742 121 SRVA-----DAEEKILELQQK---LEHAHKVCLTDTCILEKKQLEERIKEASENEAKLK-QQYQEEQQKRKLLDQNVNEL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1036 EKQINDLKsENDALNERLKSEEQ----------KQLSREKANS----KNPQ-----VMYLEQELESLKAVLEI------- 1089
Cdd:pfam15742 192 QQQVRSLQ-DKEAQLEMTNSQQQlriqqqeaqlKQLENEKRKSdehlKSNQelsekLSSLQQEKEALQEELQQvlkqldv 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1090 ----KNEKLHQQDMKLMKMEKlvdnntalvdklkRFQQENEELKARMdkhmaisRQLSTEQAALQESLEKESKVNKRLSM 1165
Cdd:pfam15742 271 hvrkYNEKHHHHKAKLRRAKD-------------RLVHEVEQRDERI-------KQLENEIGILQQQSEKEKAFQKQVTA 330
|
....*.
gi 158706129 1166 ENEELL 1171
Cdd:pfam15742 331 QNEILL 336
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
914-1163 |
8.84e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.12 E-value: 8.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 914 LEKARADLQTAYQEF---------VQKLNQQHQTD-RTELENRLKDLYTAECEKLQSIyieeaEKYKTQLqEQFDNLNAA 983
Cdd:pfam15921 108 LRQSVIDLQTKLQEMqmerdamadIRRRESQSQEDlRNQLQNTVHELEAAKCLKEDML-----EDSNTQI-EQLRKMMLS 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 984 HETTKLEI--------EAS------HSEKVELLKKTYETSLSEIKKSHEME----------------------KKSLEDL 1027
Cdd:pfam15921 182 HEGVLQEIrsilvdfeEASgkkiyeHDSMSTMHFRSLGSAISKILRELDTEisylkgrifpvedqlealksesQNKIELL 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1028 LNEKQESLEKQINDLKSENDALNERLKSEE------QKQLSREKANSKNPQVMYLEQ--ELESLKAVL--EIKNEKLHQQ 1097
Cdd:pfam15921 262 LQQHQDRIEQLISEHEVEITGLTEKASSARsqansiQSQLEIIQEQARNQNSMYMRQlsDLESTVSQLrsELREAKRMYE 341
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1098 DmKLMKMEK-LVDNNTALVD---KLKRFQQENEELKARMDKHMAisrQLSTEQAALqeSLEKESkvNKRL 1163
Cdd:pfam15921 342 D-KIEELEKqLVLANSELTEartERDQFSQESGNLDDQLQKLLA---DLHKREKEL--SLEKEQ--NKRL 403
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
891-1133 |
9.12e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 9.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 891 KTLSQELVSLRGELVAASSACEKLEKARADLQT---AYQE-----FVQKLNQQHQTDRTELENRLKDLyTAECEKLQSIY 962
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQErreALQRlaeysWDEIDVASAEREIAELEAELERL-DASSDDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 963 --IEEAEKYKTQLQEQFDNLNAAHETTKLEIEAsHSEKVELLKKTYETSLSEIKKSH--EMEKK----SLEDLLNEKQES 1034
Cdd:COG4913 692 eqLEELEAELEELEEELDELKGEIGRLEKELEQ-AEEELDELQDRLEAAEDLARLELraLLEERfaaaLGDAVERELREN 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1035 LEKQINDLKSENDALNERLKSEEQKQLSREKANSKN--PQVMYLEQELESLKavlEIKNEKL--HQQDMKLMKMEKLVDN 1110
Cdd:COG4913 771 LEERIDALRARLNRAEEELERAMRAFNREWPAETADldADLESLPEYLALLD---RLEEDGLpeYEERFKELLNENSIEF 847
|
250 260
....*....|....*....|...
gi 158706129 1111 NTALVDKLKRfqqENEELKARMD 1133
Cdd:COG4913 848 VADLLSKLRR---AIREIKERID 867
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
881-1133 |
1.22e-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: 48.99 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 881 SEREEALKQHKTLSQELVSLRGELVAASSACEKLEKARADLQTAYQEfVQKLNQQHQTDRTELENRLKDLyTAECEKLQs 960
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA-LARRIRALEQELAALEAELAEL-EKEIAELR- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 961 iyiEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKK-TYETSLSEikkshemEKKSLEDLLNEKQESLEKQI 1039
Cdd:COG4942 97 ---AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRlQYLKYLAP-------ARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1040 NDLKSENDALnERLKSEEQKQLSRekansknpqvmyLEQELESLKAVLEIKNEKLHQQDMKLMKMEKLVDNNTALVDKLK 1119
Cdd:COG4942 167 AELEAERAEL-EALLAELEEERAA------------LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
250
....*....|....
gi 158706129 1120 RFQQENEELKARMD 1133
Cdd:COG4942 234 AEAAAAAERTPAAG 247
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
882-1125 |
1.34e-05 |
|
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: 49.33 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 882 EREEALKQHKTLSQELVSLRGELvaassaceklEKARADLQTAYQEFVQKLNQQHQTDRTELENRLKD-----LYTAECE 956
Cdd:pfam05483 528 QEERMLKQIENLEEKEMNLRDEL----------ESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKekqmkILENKCN 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 957 KLQSiYIEEAEKYKTQLQEQFDNLN--AAHETTKLEIEASHSEKVEL----LKKTYETSLSEIKKSHEMEKKSLEDLLNE 1030
Cdd:pfam05483 598 NLKK-QIENKNKNIEELHQENKALKkkGSAENKQLNAYEIKVNKLELelasAKQKFEEIIDNYQKEIEDKKISEEKLLEE 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1031 KQES---------LEKQInDLK-----SENDALNERLKSEEQKQLsrEKANSKNPQVMYLEQELESLKAVLEIKNEKLHQ 1096
Cdd:pfam05483 677 VEKAkaiadeavkLQKEI-DKRcqhkiAEMVALMEKHKHQYDKII--EERDSELGLYKNKEQEQSSAKAALEIELSNIKA 753
|
250 260
....*....|....*....|....*....
gi 158706129 1097 QdmkLMKMEKLVDNNTALVDKLKRFQQEN 1125
Cdd:pfam05483 754 E---LLSLKKQLEIEKEEKEKLKMEAKEN 779
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
882-1164 |
1.40e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 882 EREEALKQHKtlsQELVSLRGELVAASSACEKLEKARADLQTAYQEfVQKLNQQHQTdrtelenrLKDLYTAEcEKLQSI 961
Cdd:PRK03918 449 HRKELLEEYT---AELKRIEKELKEIEEKERKLRKELRELEKVLKK-ESELIKLKEL--------AEQLKELE-EKLKKY 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 962 YIEEAEKYKTQ---LQEQFDNLNAAHETTKLEIE---ASHSEKVELLKK--TYETSLSEIKKSHEMEKKSLEDLLNEKQE 1033
Cdd:PRK03918 516 NLEELEKKAEEyekLKEKLIKLKGEIKSLKKELEkleELKKKLAELEKKldELEEELAELLKELEELGFESVEELEERLK 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1034 SLEKQIN------DLKSENDALNERLKSEEQKQLSREKANSKnpqvmyLEQELESLKAVLEIKNEKLHQQDmklmkMEKL 1107
Cdd:PRK03918 596 ELEPFYNeylelkDAEKELEREEKELKKLEEELDKAFEELAE------TEKRLEELRKELEELEKKYSEEE-----YEEL 664
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 158706129 1108 VDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAALQESLEKESKVNKRLS 1164
Cdd:PRK03918 665 REEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE 721
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
921-1167 |
2.39e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 921 LQTAYQEFVQKLNQQHQTDRTE-LENRLKDLYtaecEKLQSIyiEEA-EKYKTQ-----LQEQFDNLNAAHETTKLEIEA 993
Cdd:COG3206 157 LAEAYLEQNLELRREEARKALEfLEEQLPELR----KELEEA--EAAlEEFRQKnglvdLSEEAKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 994 SHSEKVELlkktyETSLSEIKKSHEMEKKSLEDLLNEKQ-ESLEKQINDLKSENDALNERLKSEeqkqlsrekanskNPQ 1072
Cdd:COG3206 231 ARAELAEA-----EARLAALRAQLGSGPDALPELLQSPViQQLRAQLAELEAELAELSARYTPN-------------HPD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1073 VMYLEQELESLKAvlEIKNEKLHQQDMKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAALQES 1152
Cdd:COG3206 293 VIALRAQIAALRA--QLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESL 370
|
250
....*....|....*..
gi 158706129 1153 LEK--ESKVNKRLSMEN 1167
Cdd:COG3206 371 LQRleEARLAEALTVGN 387
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1006-1174 |
2.51e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1006 YETS---LSEIKKSHEMEKKSLEDLL----------NEKQESLE---KQINDLKSENDALNERLK--SEEQKQLS--REK 1065
Cdd:PRK03918 160 YENAyknLGEVIKEIKRRIERLEKFIkrtenieeliKEKEKELEevlREINEISSELPELREELEklEKEVKELEelKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1066 ANSKNPQVMYLEQELESLKAVLEIKNEKLHQQDMKLMKMEKLVDNNTALVDK------LKRFQQENEELKARMDKHMAI- 1138
Cdd:PRK03918 240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKaeeyikLSEFYEEYLDELREIEKRLSRl 319
|
170 180 190
....*....|....*....|....*....|....*.
gi 158706129 1139 SRQLSTEQAALQESLEKESKVNKrLSMENEELLWKL 1174
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEE-LKKKLKELEKRL 354
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
988-1158 |
2.67e-05 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 47.39 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 988 KLEIEASHSEKVELLKKTY-----ETSLSEIKKSHEMEKKSLEDLlNEK--QESLEKQINDLKSENDALNERLKSEEQKQ 1060
Cdd:pfam15294 78 KLQADISELENRELLEQIAefeerEFTSSNKKPNFELNKPKLEPL-NEGggSALLHMEIERLKEENEKLKERLKTLESQA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1061 LSREKANSKnpqvmyLEQELESLKAVL-EIKNEKLHQQDMKlmKMEKLVdnnTALVDKLKRFQQENEELKARMDKHMAIS 1139
Cdd:pfam15294 157 TQALDEKSK------LEKALKDLQKEQgAKKDVKSNLKEIS--DLEEKM---AALKSDLEKTLNASTALQKSLEEDLAST 225
|
170
....*....|....*....
gi 158706129 1140 RQlstEQAALQESLEKESK 1158
Cdd:pfam15294 226 KH---ELLKVQEQLEMAEK 241
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
792-1182 |
3.62e-05 |
|
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: 48.04 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 792 LKTSPKgpSRKSLFTAFNSVEKGRQknprsLCIQTQTAPDVLSSERTLELAQYktkcesqSGFILHLRQLLSRGNTKFEA 871
Cdd:TIGR00618 158 LKAKSK--EKKELLMNLFPLDQYTQ-----LALMEFAKKKSLHGKAELLTLRS-------QLLTLCTPCMPDTYHERKQV 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 872 LTVVIQHLlserEEALKQHKTLSQELVSLRGELVAASSACEKLEKARADLQTAYQEFVQKLNQQHQTDRTelenRLKDLY 951
Cdd:TIGR00618 224 LEKELKHL----REALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRA----RKAAPL 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 952 TAECEKLQSIYiEEAEKYKTQLQEQFDNLNAA-HETTKLEIEASHSEKVELLKKTYETSLSEIKKSHEMEKKSLEDLlnE 1030
Cdd:TIGR00618 296 AAHIKAVTQIE-QQAQRIHTELQSKMRSRAKLlMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREIS--C 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1031 KQESLEKQINDLKSENDALNERLKSEEQK--QLSREKAN------SKNPqvmyLEQELESLKAVLEIKNEKLHQQDMKLM 1102
Cdd:TIGR00618 373 QQHTLTQHIHTLQQQKTTLTQKLQSLCKEldILQREQATidtrtsAFRD----LQGQLAHAKKQQELQQRYAELCAAAIT 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1103 K-MEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAALQESLEKESKVNKRLSMENEELLWKLHNGDLCS 1181
Cdd:TIGR00618 449 CtAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTR 528
|
.
gi 158706129 1182 P 1182
Cdd:TIGR00618 529 R 529
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
985-1170 |
4.31e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.04 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 985 ETTKLEIEASHSE----KVELLKKTYETSLSEIKKSHEM--EKKSLEDLLNEKQESLEKQinDLKSENDALNERLKSEEQ 1058
Cdd:pfam02463 154 RRLEIEEEAAGSRlkrkKKEALKKLIEETENLAELIIDLeeLKLQELKLKEQAKKALEYY--QLKEKLELEEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1059 KQLSREKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQDmKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAI 1138
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVL-KENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKV 310
|
170 180 190
....*....|....*....|....*....|..
gi 158706129 1139 SrqLSTEQAALQESLEKESKVNKRLSMENEEL 1170
Cdd:pfam02463 311 D--DEEKLKESEKEKKKAEKELKKEKEEIEEL 340
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
923-1168 |
4.34e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.12 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 923 TAYQ--EFVQKLNQQHQTDRTELENRLKDLYTAECEKLQSIYIEEA-----EKYKTQ-LQEQFDNLNAAHETTKLEIEAS 994
Cdd:TIGR01612 643 SPYQvpEHLKNKDKIYSTIKSELSKIYEDDIDALYNELSSIVKENAidnteDKAKLDdLKSKIDKEYDKIQNMETATVEL 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 995 HSEKVELLKKTYETSLSEIKKSHEME-----KKSLEDLLNeKQESLEKQINDLKSENDALN------ERLKSEEQKQLSR 1063
Cdd:TIGR01612 723 HLSNIENKKNELLDIIVEIKKHIHGEinkdlNKILEDFKN-KEKELSNKINDYAKEKDELNkykskiSEIKNHYNDQINI 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1064 EKANSKNPQVMYlEQELESLKAVlEIKNEKLHQ--QDMKLMKMEKL--VDNNTALVDKLK-RFQQENEELKARMDKhmaI 1138
Cdd:TIGR01612 802 DNIKDEDAKQNY-DKSKEYIKTI-SIKEDEIFKiiNEMKFMKDDFLnkVDKFINFENNCKeKIDSEHEQFAELTNK---I 876
|
250 260 270
....*....|....*....|....*....|
gi 158706129 1139 SRQLSTEQAALQeslekESKVNKRLSMENE 1168
Cdd:TIGR01612 877 KAEISDDKLNDY-----EKKFNDSKSLINE 901
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
882-1132 |
5.99e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.66 E-value: 5.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 882 EREEALKQHKTLSQELVSLRGELVAASSACEKLEKARADLQTAYQEFVQ----KLNQQHQTDRTELENRLKDLYTAECE- 956
Cdd:pfam02463 251 EEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKsellKLERRKVDDEEKLKESEKEKKKAEKEl 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 957 KLQSIYIEEAEKYKTQLQEQFDNLNAAHETT--KLEIEASHSEKVELLKKTYETSLSEIKKSHEMEkksLEDLLNEKQES 1034
Cdd:pfam02463 331 KKEKEEIEELEKELKELEIKREAEEEEEEELekLQEKLEQLEEELLAKKKLESERLSSAAKLKEEE---LELKSEEEKEA 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1035 -----LEKQINDLKseNDALNERLKSEEQKQLSREKANSKNPQVmylEQELESLKAVLEIKNEKLhQQDMKLMKMEKLVD 1109
Cdd:pfam02463 408 qllleLARQLEDLL--KEEKKEELEILEEEEESIELKQGKLTEE---KEELEKQELKLLKDELEL-KKSEDLLKETQLVK 481
|
250 260
....*....|....*....|...
gi 158706129 1110 NNTALVDKLKRFQQENEELKARM 1132
Cdd:pfam02463 482 LQEQLELLLSRQKLEERSQKESK 504
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
868-1171 |
6.52e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.44 E-value: 6.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 868 KFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVaassacEKLEKARaDLQTAYQEFVQKLnQQHQTDRTELENRL 947
Cdd:COG1340 16 KIEELREEIEELKEKRDELNEELKELAEKRDELNAQVK------ELREEAQ-ELREKRDELNEKV-KELKEERDELNEKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 948 KDLYtAECEKLQSIY--IEEAEKYKTQLQEQFDNLNAAHETTKLEIEAshsEKvELLKK--TYETSLSEIKKSHEmekks 1023
Cdd:COG1340 88 NELR-EELDELRKELaeLNKAGGSIDKLRKEIERLEWRQQTEVLSPEE---EK-ELVEKikELEKELEKAKKALE----- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1024 ledlLNEKQESLEKQINDLKSENDALNERLKSeeqkqlSREKANSKNPQVMYLEQELESLKAvleiKNEKLHQQdmklmk 1103
Cdd:COG1340 158 ----KNEKLKELRAELKELRKEAEEIHKKIKE------LAEEAQELHEEMIELYKEADELRK----EADELHKE------ 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158706129 1104 meklVDNNTALVDKL-KRFQQENEELKARMDKHMAIS-RQLSTEQAALQESLEKESKV-------NKRLSMENEELL 1171
Cdd:COG1340 218 ----IVEAQEKADELhEEIIELQKELRELRKELKKLRkKQRALKREKEKEELEEKAEEifeklkkGEKLTTEELKLL 290
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
963-1096 |
7.23e-05 |
|
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: 45.28 E-value: 7.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 963 IEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKtyetslseiKKSHEMEKKSLEDLlNEKQESLEKQINDL 1042
Cdd:pfam13851 35 IAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQ---------LENYEKDKQSLKNL-KARLKVLEKELKDL 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158706129 1043 KSENDALNERLK--SEEQKQLSR----------EKANSKNpqvMYLEQELESLKAVLEIKNEKLHQ 1096
Cdd:pfam13851 105 KWEHEVLEQRFEkvERERDELYDkfeaaiqdvqQKTGLKN---LLLEKKLQALGETLEKKEAQLNE 167
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1018-1179 |
7.32e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 7.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1018 EMEKKSLEDLLNEKQEsLEKQINDLKSENDALNERLKSeeqkqlSREKANSKNPQVMYLEQELESLKavlEIKNEklhqq 1097
Cdd:COG1340 4 DELSSSLEELEEKIEE-LREEIEELKEKRDELNEELKE------LAEKRDELNAQVKELREEAQELR---EKRDE----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1098 dmklmkmeklvdnntaLVDKLKRFQQENEELKARMDKHMAISRQLSTEQAALQESLEKESKVNKRLsmenEELLWKLHNG 1177
Cdd:COG1340 69 ----------------LNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEI----ERLEWRQQTE 128
|
..
gi 158706129 1178 DL 1179
Cdd:COG1340 129 VL 130
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
883-1158 |
8.04e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 47.05 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 883 REEALKQHKTLSQELVSLRGELVAASSACEKLEKARADLQTAyqEFVQKlnqqhqtdrtelenRLKDLYTAECEKLQSIY 962
Cdd:pfam07111 86 RETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGA--EMVRK--------------NLEEGSQRELEEIQRLH 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 963 ieeaekyktqlQEQFDNLNAAHETTkLEIEASHSEKVELLKKTYETSLS-EIKKSHEMEKKS--LEDLLNEKQESLEKQI 1039
Cdd:pfam07111 150 -----------QEQLSSLTQAHEEA-LSSLTSKAEGLEKSLNSLETKRAgEAKQLAEAQKEAelLRKQLSKTQEELEAQV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1040 NDLKSENDALNERLKSE--------EQKQLS------REKANSKNPQVMYLEQELESLKAVLEIKNEKLHQqdmKLMKME 1105
Cdd:pfam07111 218 TLVESLRKYVGEQVPPEvhsqtwelERQELLdtmqhlQEDRADLQATVELLQVRVQSLTHMLALQEEELTR---KIQPSD 294
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 158706129 1106 KLVDNNTALVDKLKRFQQENE-----ELKARMDKHMAISRQLSTEQAALQESLEKESK 1158
Cdd:pfam07111 295 SLEPEFPKKCRSLLNRWREKVfalmvQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQ 352
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
859-1170 |
1.00e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.87 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 859 RQLLSRGNTKFEALtvVIQHL----LSEREEALKQhktLSQELVSLRGELVAASSACEKLEKARADLQTAYQEFVQKLNQ 934
Cdd:COG3096 808 VQKLQRLHQAFSQF--VGGHLavafAPDPEAELAA---LRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQ 882
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 935 QHQTDRTELENRLKDLyTAECEKLQS--IYIEEAEKYKTQLQEQFDNLN---AAHETTKLEIEASHSEKVELLKKTYetS 1009
Cdd:COG3096 883 ANLLADETLADRLEEL-REELDAAQEaqAFIQQHGKALAQLEPLVAVLQsdpEQFEQLQADYLQAKEQQRRLKQQIF--A 959
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1010 LSE-IKKSHEMEKKSLEDLLNEKQESlekqindlkseNDALNERL-KSEEQKQLSREKANSKNPQVMYLEQELESLKAVL 1087
Cdd:COG3096 960 LSEvVQRRPHFSYEDAVGLLGENSDL-----------NEKLRARLeQAEEARREAREQLRQAQAQYSQYNQVLASLKSSR 1028
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1088 EIKNEKLHQQDMKLMKMEKLVDNNTAlvdklKRFQQENEELKARMDKHMAISRQLSTeQAALQESlEKESkVNKRLSMEN 1167
Cdd:COG3096 1029 DAKQQTLQELEQELEELGVQADAEAE-----ERARIRRDELHEELSQNRSRRSQLEK-QLTRCEA-EMDS-LQKRLRKAE 1100
|
...
gi 158706129 1168 EEL 1170
Cdd:COG3096 1101 RDY 1103
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
953-1148 |
1.20e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 953 AECEKLQSIYIEEAEKyktqlqeqfdnlNAAHETTKLEIEAShsEKVELLKKTYETSLSEIKKshemEKKSLEDLLNEKQ 1032
Cdd:PRK12704 34 KEAEEEAKRILEEAKK------------EAEAIKKEALLEAK--EEIHKLRNEFEKELRERRN----ELQKLEKRLLQKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1033 ESLEKQINDLKSENDALNERLKSEEQKQLSREKansknpqvmyLEQELESLKAVLEIKNEK---LHQQDMKLMKMEKLVD 1109
Cdd:PRK12704 96 ENLDRKLELLEKREEELEKKEKELEQKQQELEK----------KEEELEELIEEQLQELERisgLTAEEAKEILLEKVEE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 158706129 1110 NNTAlvDKLKRFQQENEELKARMDKH------MAISRqLSTEQAA 1148
Cdd:PRK12704 166 EARH--EAAVLIKEIEEEAKEEADKKakeilaQAIQR-CAADHVA 207
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
912-1169 |
1.50e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 45.29 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 912 EKLEKARADLQTAYQEFVQKLNQQHQTDRTELENRLKDLYTAECEKLQSIYIEEAEKY------KTQLQEQFDNLNAAHE 985
Cdd:pfam13868 61 EEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAeeklekQRQLREEIDEFNEEQA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 986 TTK-LEIEAshsEKVELLK-KTYETSLSEIKKSHEMEKKSLE---DLLNEKQESLEKQINDLKSENDALNERLKSEEQKQ 1060
Cdd:pfam13868 141 EWKeLEKEE---EREEDERiLEYLKEKAEREEEREAEREEIEeekEREIARLRAQQEKAQDEKAERDELRAKLYQEEQER 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1061 LSREKAnsknpqvmyLEQELESLKAVLEIKNEKLHQQDMKLMKMEKLVDNNTALVDKLKRFQQENEElKARMDKHMAisR 1140
Cdd:pfam13868 218 KERQKE---------REEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEE-IEQEEAEKR--R 285
|
250 260
....*....|....*....|....*....
gi 158706129 1141 QLSTEQAALQESLEKESKVNKRLSMENEE 1169
Cdd:pfam13868 286 MKRLEHRRELEKQIEEREEQRAAEREEEL 314
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
895-1198 |
2.10e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.84 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 895 QELVSL---RGELVAASSACEKLEKaradlqTAYQEFV--QKLNQQHQTDRTELENRL----KDLYTAECEKLQSIYI-- 963
Cdd:COG5022 800 QPLLSLlgsRKEYRSYLACIIKLQK------TIKREKKlrETEEVEFSLKAEVLIQKFgrslKAKKRFSLLKKETIYLqs 873
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 964 ----EEAEKYKTQLQEQFDNLNAAHETT----------KLEIEASHSEKVEL-------LKKTYETSLSEIKKSHEMEKK 1022
Cdd:COG5022 874 aqrvELAERQLQELKIDVKSISSLKLVNleleseiielKKSLSSDLIENLEFkteliarLKKLLNNIDLEEGPSIEYVKL 953
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1023 SLEDLLNEKQESLEKQINDLKSENDALNErLKSEEQKQLSR-----EKANSKNPQVMYLEQELESLKaVLEIKNEKLHqQ 1097
Cdd:COG5022 954 PELNKLHEVESKLKETSEEYEDLLKKSTI-LVREGNKANSElknfkKELAELSKQYGALQESTKQLK-ELPVEVAELQ-S 1030
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1098 DMKLMKMEKLVDNNTALVDKLKRFQ-QENEELKARMdKHMAISRQLS------TEQAALQESLEKESKVnKRLSMENEEL 1170
Cdd:COG5022 1031 ASKIISSESTELSILKPLQKLKGLLlLENNQLQARY-KALKLRRENSllddkqLYQLESTENLLKTINV-KDLEVTNRNL 1108
|
330 340
....*....|....*....|....*...
gi 158706129 1171 LwklhngdlcspKRSPTSSAIPFQSPRN 1198
Cdd:COG5022 1109 V-----------KPANVLQFIVAQMIKL 1125
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
826-1146 |
2.46e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.20 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 826 TQTAPDVLSSERTLELAQ---YKTKCESQSGFILHLRQLLSRGNTKFEALTVVIQHLLSEREEAlKQH------------ 890
Cdd:pfam10174 259 LKTNGLLHTEDREEEIKQmevYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDC-KQHievlkesltake 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 891 ---KTLSQELVSLRGELVaassaceklEKARadLQTAYQEFVQKLNQQHQTDRTELENrLKDLYTAECEKLQSIYiEEAE 967
Cdd:pfam10174 338 qraAILQTEVDALRLRLE---------EKES--FLNKKTKQLQDLTEEKSTLAGEIRD-LKDMLDVKERKINVLQ-KKIE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 968 KYKTQLQEQFDNLNAAHETTK-LEIEASHSEKVellKKTYETSLSEIKKSHE--MEKKSLED-LLNEKQESLEKQINDLK 1043
Cdd:pfam10174 405 NLQEQLRDKDKQLAGLKERVKsLQTDSSNTDTA---LTTLEEALSEKERIIErlKEQREREDrERLEELESLKKENKDLK 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1044 SENDALNERLKSEEQKQLS-REKANSKNPQVMYLEQELESLKAVLEIKNE---KLHQQDMKLMKMEKLVDNNTALVDKLK 1119
Cdd:pfam10174 482 EKVSALQPELTEKESSLIDlKEHASSLASSGLKKDSKLKSLEIAVEQKKEecsKLENQLKKAHNAEEAVRTNPEINDRIR 561
|
330 340 350
....*....|....*....|....*....|....
gi 158706129 1120 -------RFQQENEELKARMDKHMAISRQLSTEQ 1146
Cdd:pfam10174 562 lleqevaRYKEESGKAQAEVERLLGILREVENEK 595
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1007-1171 |
2.56e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.29 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1007 ETSLSEIK--KSHEMEKKSLEDLLNEKQESLEkQINDLKSENDALNERLKS--EEQKQLSREKANSKNPQVMYLEQELES 1082
Cdd:PRK11281 42 QAQLDALNkqKLLEAEDKLVQQDLEQTLALLD-KIDRQKEETEQLKQQLAQapAKLRQAQAELEALKDDNDEETRETLST 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1083 LK-AVLEIKNEKLHQQDMKLmkMEKLVDNNTALV--------------DKLKRFQQENEELKARMDKHMAISR----QLS 1143
Cdd:PRK11281 121 LSlRQLESRLAQTLDQLQNA--QNDLAEYNSQLVslqtqperaqaalyANSQRLQQIRNLLKGGKVGGKALRPsqrvLLQ 198
|
170 180
....*....|....*....|....*...
gi 158706129 1144 TEQAALQESLEkeskvNKRLSMENEELL 1171
Cdd:PRK11281 199 AEQALLNAQND-----LQRKSLEGNTQL 221
|
|
| PKK |
pfam12474 |
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ... |
1000-1146 |
2.83e-04 |
|
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.
Pssm-ID: 463600 [Multi-domain] Cd Length: 139 Bit Score: 42.16 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1000 ELLKKTYETSLSEIKKSHEMEKKSLEDLLNEKQESLEK-QINDLKsendALNERLKSEEQKQLSREKANSKNpQVMYLEQ 1078
Cdd:pfam12474 6 EQQKDRFEQERQQLKKRYEKELEQLERQQKQQIEKLEQrQTQELR----RLPKRIRAEQKKRLKMFRESLKQ-EKKELKQ 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158706129 1079 ELESLKavleikneKLHQQDMKLMKMEKLvdnntalvdKLKRFQQENEELKARMDKHMAISRQLSTEQ 1146
Cdd:pfam12474 81 EVEKLP--------KFQRKEAKRQRKEEL---------ELEQKHEELEFLQAQSEALERELQQLQNEK 131
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
980-1180 |
3.08e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 980 LNAAHETTKLEieaSHSEKVELLKKTYETSLSEIK--KSHEMEKKSLEDLLNEKQESLEKQINDLKSENDALNERLKsEE 1057
Cdd:TIGR02169 667 LFSRSEPAELQ---RLRERLEGLKRELSSLQSELRriENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE-EL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1058 QKQLSrekansknpqvmYLEQELESLKAVLEIKNEKLHQQDMKLMKMEKLVDNntaLVDKL--KRFQQENEELKARMDKH 1135
Cdd:TIGR02169 743 EEDLS------------SLEQEIENVKSELKELEARIEELEEDLHKLEEALND---LEARLshSRIPEIQAELSKLEEEV 807
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 158706129 1136 MAISRQL-STEQAALQESLEKESKVNKRLSMENEELLWKLHNGDLC 1180
Cdd:TIGR02169 808 SRIEARLrEIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE 853
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
914-1156 |
3.14e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.14 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 914 LEKARAdLQTAYQEFVQKLNQQHQTDRTElENRLKDLYTAECEKLQSiYIEEAEKYKTQLQEQFDNLNAAHET--TKLEI 991
Cdd:pfam00038 17 IDKVRF-LEQQNKLLETKISELRQKKGAE-PSRLYSLYEKEIEDLRR-QLDTLTVERARLQLELDNLRLAAEDfrQKYED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 992 EASHSE-------------------KVEL-------------LKKTYETSLSEIKKSHEMEKKSLE-------DL---LN 1029
Cdd:pfam00038 94 ELNLRTsaendlvglrkdldeatlaRVDLeakieslkeelafLKKNHEEEVRELQAQVSDTQVNVEmdaarklDLtsaLA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1030 EKQESLEKQINDLKSENDAL----NERLKSE-----EQKQLSREKANSKNPQVMYLEQELESL---KAVLEIKNEKLHQQ 1097
Cdd:pfam00038 174 EIRAQYEEIAAKNREEAEEWyqskLEELQQAaarngDALRSAKEEITELRRTIQSLEIELQSLkkqKASLERQLAETEER 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158706129 1098 DMKLMKM--EKLVDNNTALVDKLKRFQQENEELKARMDKHMAisrqLSTEQAALQESLEKE 1156
Cdd:pfam00038 254 YELQLADyqELISELEAELQETRQEMARQLREYQELLNVKLA----LDIEIATYRKLLEGE 310
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
943-1151 |
3.29e-04 |
|
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: 44.25 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 943 LENRLKDLYTA-----ECEKLQSIYIEEAEKYKTQLQEQFDNLN-AAHETTKleieashseKVELLK-KTYETSLSEIKK 1015
Cdd:pfam04849 75 LEEKERDLELAarigqSLLKQNSVLTERNEALEEQLGSAREEILqLRHELSK---------KDDLLQiYSNDAEESETES 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1016 SHEMEKKSLEDLLNEKQ----ESLEKQINDLKSENDALNE---RLKSE-------EQKQLSR--EKANSKNPQVMYLEQE 1079
Cdd:pfam04849 146 SCSTPLRRNESFSSLHGcvqlDALQEKLRGLEEENLKLRSeasHLKTEtdtyeekEQQLMSDcvEQLSEANQQMAELSEE 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158706129 1080 LESlkavleiKNEK-LHQQDMKLMKMEKLVDnntaLVDKLKRFQQENEELKARMDKHMAISRQLSTEQAALQE 1151
Cdd:pfam04849 226 LAR-------KMEEnLRQQEEITSLLAQIVD----LQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQD 287
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
876-1096 |
3.30e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 44.42 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 876 IQHLLSEREEALKQHKTLSQELVSLRGELVAA-------SSACEKLEKARADLQTAYQEFVQKL-----NQQHQTDRTEL 943
Cdd:pfam15905 82 IRALVQERGEQDKRLQALEEELEKVEAKLNAAvrektslSASVASLEKQLLELTRVNELLKAKFsedgtQKKMSSLSMEL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 944 ENRLKDLYTAECE----------KLQSI--YIEEAEKYKTQLQEQFDNLNAAHETTKLEIE---------ASHSEKVELL 1002
Cdd:pfam15905 162 MKLRNKLEAKMKEvmakqegmegKLQVTqkNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEklleyitelSCVSEQVEKY 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1003 KKTYeTSLSEIKKSHEMEKKSLEDLLNEKQESLEKQINDLksenDALNERLKSEEQKQLSREKANSKNpqvmyLEQELES 1082
Cdd:pfam15905 242 KLDI-AQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDL----NEKCKLLESEKEELLREYEEKEQT-----LNAELEE 311
|
250
....*....|....*..
gi 158706129 1083 LKAVLEIK---NEKLHQ 1096
Cdd:pfam15905 312 LKEKLTLEeqeHQKLQQ 328
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
867-1041 |
4.02e-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: 43.37 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 867 TKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELvaassacEKLEKARADLQTAYQEF---VQKLNQQHQTDRT-- 941
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTEL-------EDLEKEIKRLELEIEEVearIKKYEEQLGNVRNnk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 942 ELENRLKDLYTAECEklqsiyIEEAEKYKTQLQEQFDNLNAAHETTKLEIEAsHSEKVELLKKTYETSLSEIKKshEMEK 1021
Cdd:COG1579 90 EYEALQKEIESLKRR------ISDLEDEILELMERIEELEEELAELEAELAE-LEAELEEKKAELDEELAELEA--ELEE 160
|
170 180
....*....|....*....|
gi 158706129 1022 ksledlLNEKQESLEKQIND 1041
Cdd:COG1579 161 ------LEAEREELAAKIPP 174
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
966-1158 |
4.05e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 966 AEKYKTQLQEQFDNLNAAHETTKLEIEASHsEKVELLKKTYETSLSEIKKSHEmEKKSLEDLLNEKQESLEKQindlkse 1045
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQ-AELEELNEEYNELQAELEALQA-EIDKLQAEIAEAEAEIEER------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1046 NDALNERLKSEEQKQLSREK----ANSKNP-----QVMYLEQELES----LKAVLEIKNEKLHQQDMKLMKMEKLVDNNT 1112
Cdd:COG3883 85 REELGERARALYRSGGSVSYldvlLGSESFsdfldRLSALSKIADAdadlLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 158706129 1113 ALVDKLKRFQQENEELKARMDkhmaisrQLSTEQAALQESLEKESK 1158
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLA-------QLSAEEAAAEAQLAELEA 203
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
836-1004 |
4.89e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 836 ERTLELAQYKTKcesqsgfilhLRQLLSRGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSAC--EK 913
Cdd:COG4717 360 EEELQLEELEQE----------IAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeEE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 914 LEKARADLQTAYQEFVQKLNqQHQTDRTELENRLKDLytAECEKLQSIYIEEAEKyKTQLQE---QFDNLNAAHETTKLE 990
Cdd:COG4717 430 LEEELEELEEELEELEEELE-ELREELAELEAELEQL--EEDGELAELLQELEEL-KAELRElaeEWAALKLALELLEEA 505
|
170
....*....|....*
gi 158706129 991 IEASHSEKV-ELLKK 1004
Cdd:COG4717 506 REEYREERLpPVLER 520
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
948-1101 |
4.92e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.85 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 948 KDLYTAECEKLQSIYIEEAEKYKTqLQEQFDNLnaahetTKLEIEAShSEKVELLKKtYETSLSEIKKSHEMEKKSLEDL 1027
Cdd:smart00787 160 YKLLMKELELLNSIKPKLRDRKDA-LEEELRQL------KQLEDELE-DCDPTELDR-AKEKLKKLLQEIMIKVKKLEEL 230
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158706129 1028 LNEKQEsLEKQINDLKSENDALNERLKSEEQKQLSREKANSKnpQVMYLEQELESLKAVLEIKNEKLHQQDMKL 1101
Cdd:smart00787 231 EEELQE-LESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFK--EIEKLKEQLKLLQSLTGWKITKLSGNTLSM 301
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
841-1054 |
5.64e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 841 LAQYKTKCESQSGFILHLRQLLSRGNTKFEALTVVIQHLLS-----EREEA----------LKQHKTLSQELVSLRGELv 905
Cdd:PRK04863 444 LEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKiagevSRSEAwdvarellrrLREQRHLAEQLQQLRMRL- 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 906 aasSACEKLEKARADLQTAYQEFVQKLNQQHQtDRTELENRLKDLyTAECEKLqSIYIEEAEKYKTQLQEQFDNLNAahE 985
Cdd:PRK04863 523 ---SELEQRLRQQQRAERLLAEFCKRLGKNLD-DEDELEQLQEEL-EARLESL-SESVSEARERRMALRQQLEQLQA--R 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 986 TTKLEIEASH----SEKVELLKK----TYETS--LSEIKKSHEMEKKSL---EDLLNEKQESLEKQINDLKSENDALNER 1052
Cdd:PRK04863 595 IQRLAARAPAwlaaQDALARLREqsgeEFEDSqdVTEYMQQLLERERELtveRDELAARKQALDEEIERLSQPGGSEDPR 674
|
..
gi 158706129 1053 LK 1054
Cdd:PRK04863 675 LN 676
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
880-1170 |
6.19e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 6.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 880 LSEREEALKQHKTLSQELVSLRGELVAASSACEK----LEKARADLQTAYqEFVQKLNQQHQTDRTELE--NRLKDLYTA 953
Cdd:PRK04863 357 LEELEERLEEQNEVVEEADEQQEENEARAEAAEEevdeLKSQLADYQQAL-DVQQTRAIQYQQAVQALEraKQLCGLPDL 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 954 ECEKLQSiYIEEaekYKTQLQEQFDNLNAAHetTKLEI-EASHS--EKV-ELLKK-TYETSLSEikkSHEMEKKSLEDLl 1028
Cdd:PRK04863 436 TADNAED-WLEE---FQAKEQEATEELLSLE--QKLSVaQAAHSqfEQAyQLVRKiAGEVSRSE---AWDVARELLRRL- 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1029 nEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQdmklmkMEKLV 1108
Cdd:PRK04863 506 -REQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSES------VSEAR 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1109 DNNTALvdklkrfQQENEELKARMDKHMAISRQLSTEQAAL---------------------QESLEKEskvnKRLSMEN 1167
Cdd:PRK04863 579 ERRMAL-------RQQLEQLQARIQRLAARAPAWLAAQDALarlreqsgeefedsqdvteymQQLLERE----RELTVER 647
|
...
gi 158706129 1168 EEL 1170
Cdd:PRK04863 648 DEL 650
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1027-1170 |
7.08e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1027 LLNEKQES--LEKQINDLKSENDALNERLKSEEQKQLSrekansknpqvmyLEQELESLKAVLEIKNEKLHQQDMKLMKM 1104
Cdd:TIGR02168 672 ILERRREIeeLEEKIEELEEKIAELEKALAELRKELEE-------------LEEELEQLRKELEELSRQISALRKDLARL 738
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158706129 1105 EKLVDNNTALVDKLkrfQQENEELKARMdkhMAISRQLSTEQAALQESLEKESKVNKRLSMENEEL 1170
Cdd:TIGR02168 739 EAEVEQLEERIAQL---SKELTELEAEI---EELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
875-1195 |
7.78e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.88 E-value: 7.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 875 VIQHLLSEREEALKQHKTLSQELVSLRGELVAASSACEKLEKA-RADLQTAYQEFVQKLNQQHQTDRTELENRLKDLYTa 953
Cdd:TIGR00606 793 IMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQhELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKS- 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 954 ecEKLQsiyIEEAEKYKTQLQEQFDNL------------NAAHETTKLE--IEASHSEKVELL------KKTYETSLSEI 1013
Cdd:TIGR00606 872 --EKLQ---IGTNLQRRQQFEEQLVELstevqslireikDAKEQDSPLEtfLEKDQQEKEELIssketsNKKAQDKVNDI 946
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1014 KKSHEMEKKSLEDLLNEKQESLEKQINDLKSENDALNERLKSEEQKQ--------LSREKANSKNPQVMYLEQELESLKA 1085
Cdd:TIGR00606 947 KEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQekinedmrLMRQDIDTQKIQERWLQDNLTLRKR 1026
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1086 VLEIK----NEKLHQQDMKLMKMEKLVDNNTALVDKLKRFQQENEELKARM----DKHMAISRQLSTEQAALQESLEKES 1157
Cdd:TIGR00606 1027 ENELKeveeELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQkgyeKEIKHFKKELREPQFRDAEEKYREM 1106
|
330 340 350
....*....|....*....|....*....|....*...
gi 158706129 1158 KVNKRLSmeneellwKLHNGDLCSPKRSPTSSAIPFQS 1195
Cdd:TIGR00606 1107 MIVMRTT--------ELVNKDLDIYYKTLDQAIMKFHS 1136
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
988-1133 |
8.60e-04 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 40.75 E-value: 8.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 988 KLEIEASHsEKVELLKktyetslsEIKKSHEMEKKSLEDLLNekqeSLEKQINDLKSENDALNERLKseEQKQLSREKAN 1067
Cdd:pfam12718 6 KLEAENAQ-ERAEELE--------EKVKELEQENLEKEQEIK----SLTHKNQQLEEEVEKLEEQLK--EAKEKAEESEK 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158706129 1068 SK------NPQVMYLEQELESLKAVLEIKNEKLHQQDMKLMKMEKlvdnntalvdKLKRFQQENEELKARMD 1133
Cdd:pfam12718 71 LKtnnenlTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLER----------KVQALEQERDEWEKKYE 132
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
884-1170 |
8.64e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 8.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 884 EEALKQHKTLSQELVSLRGELVAASSACEKLEKARADLQTAYQEFVQKLNQQHQTDRT-----ELENRLKDLYTAECEKL 958
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAkkkaeEDKKKADELKKAAAAKK 1418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 959 QSiyiEEAEKYKTQLQEQFDNLNAAHETTK---LEIEASHSEKVELLKKTYEtslsEIKKSHEMEKKSLEdllNEKQESL 1035
Cdd:PTZ00121 1419 KA---DEAKKKAEEKKKADEAKKKAEEAKKadeAKKKAEEAKKAEEAKKKAE----EAKKADEAKKKAEE---AKKADEA 1488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1036 EKQINDLKSENDALneRLKSEEQKQLSREKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQDmKLMKMEKlvdnntalV 1115
Cdd:PTZ00121 1489 KKKAEEAKKKADEA--KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD-ELKKAEE--------L 1557
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 158706129 1116 DKLKRFQQENEELKARMDKHMAISRQLSTEQAALQESLEKESKVNKRLSMENEEL 1170
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA 1612
|
|
| PRK14160 |
PRK14160 |
heat shock protein GrpE; Provisional |
1020-1134 |
9.23e-04 |
|
heat shock protein GrpE; Provisional
Pssm-ID: 237629 [Multi-domain] Cd Length: 211 Bit Score: 42.05 E-value: 9.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1020 EKKSLEDLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQVmyLEQELESLKAVLEIKNEKLHQQdm 1099
Cdd:PRK14160 1 MEKECKDAKHENMEEDCCKENENKEEDKGKEEDLEFEEIEKEEIIEDSEESNEV--KIEELKDENNKLKEENKKLENE-- 76
|
90 100 110
....*....|....*....|....*....|....*
gi 158706129 1100 klmkMEklvdnntALVDKLKRFQQENEELKARMDK 1134
Cdd:PRK14160 77 ----LE-------ALKDRLLRTVAEYDNYRKRTAK 100
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
884-1164 |
9.56e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 9.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 884 EEALKQHK-TLSQELVSLRGEL----VAASSACEKLEKARADLQTAyQEFVQKLNQQHQTDRTELENRLKDLYTAEcEKL 958
Cdd:PRK02224 309 AEAVEARReELEDRDEELRDRLeecrVAAQAHNEEAESLREDADDL-EERAEELREEAAELESELEEAREAVEDRR-EEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 959 QSI--YIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELlkktyETSLSEIKKSHEMEKKSLE----------- 1025
Cdd:PRK02224 387 EELeeEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAEL-----EATLRTARERVEEAEALLEagkcpecgqpv 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1026 ---------DLLNEKQESLEKQINDLKSENDALNERLKSEEQ-----KQLSREKANSKNpqvmyLEQELESLKAVLEIKN 1091
Cdd:PRK02224 462 egsphvetiEEDRERVEELEAELEDLEEEVEEVEERLERAEDlveaeDRIERLEERRED-----LEELIAERRETIEEKR 536
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158706129 1092 EKLhqqdmklmkmEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAALQESLEKESKVNKRLS 1164
Cdd:PRK02224 537 ERA----------EELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLA 599
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
890-1043 |
9.89e-04 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 41.48 E-value: 9.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 890 HKTLSQELVSLRGELVaassacEKLEKARADLQTAYQEFVQKLNQQHQTDRTELE---NRLKDLYTAECEKLQSIYIEEA 966
Cdd:pfam01442 28 VDRLEKETEALRERLQ------KDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEpytEELRKRLNADAEELQEKLAPYG 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158706129 967 EKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKTYETSLSEIkksHEMekksLEDLLNEKQESLEKQINDLK 1043
Cdd:pfam01442 102 EELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEV---QAQ----LSQRLQELREKLEPQAEDLR 171
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
939-1161 |
1.14e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 939 DRTELENRLKDLYT-AECEKLQSIYIEEAEKYKTQLQEQFDNLN---AAHETTKLEIEASHSEKVELLKKTYETSLSEIK 1014
Cdd:PHA02562 151 ARRKLVEDLLDISVlSEMDKLNKDKIRELNQQIQTLDMKIDHIQqqiKTYNKNIEEQRKKNGENIARKQNKYDELVEEAK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1015 kSHEMEKKSLEDLLNEKQESLEKQINDLKSENDALNeRLKSeEQKQLSREkansknpQVMYLE-QELESLKAVLEIKNEk 1093
Cdd:PHA02562 231 -TIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAA-KIKS-KIEQFQKV-------IKMYEKgGVCPTCTQQISEGPD- 299
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158706129 1094 lhqqdmklmKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISR-------QLSTEQAALQESLEKESKVNK 1161
Cdd:PHA02562 300 ---------RITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKkllelknKISTNKQSLITLVDKAKKVKA 365
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
994-1164 |
1.15e-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: 43.09 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 994 SHSEKVELLKKTYETSLSEIKKShEMEKKSLEDLLNEKQE---SLEKQINDLKSENDALNERLKSEEQK--QLSR----- 1063
Cdd:TIGR04523 30 KQDTEEKQLEKKLKTIKNELKNK-EKELKNLDKNLNKDEEkinNSNNKIKILEQQIKDLNDKLKKNKDKinKLNSdlski 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1064 -EKANSKNPQVMYLEQELESLKavlEIKNEKLHQQDMKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKhmaISRQL 1142
Cdd:TIGR04523 109 nSEIKNDKEQKNKLEVELNKLE---KQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNL---LEKEK 182
|
170 180
....*....|....*....|..
gi 158706129 1143 STEQAALQESLEKESKVNKRLS 1164
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLKLELLLS 204
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
973-1170 |
1.18e-03 |
|
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: 41.59 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 973 LQEQFDNLNAAHETTKLEIEASHSEKVELLK--KTYETS----LSEIKKSHEMEKKSLEDLLNEKQESLekqiNDLKSEN 1046
Cdd:pfam05010 13 ARNEIEEKELEINELKAKYEELRRENLEMRKivAEFEKTiaqmIEEKQKQKELEHAEIQKVLEEKDQAL----ADLNSVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1047 DALNERLK-SEEQKQ-LSREKANSknpqvmyleqelESLKAVLE-----IKNEKLHQQDMKLMKMEKLVDNNTALVDKLK 1119
Cdd:pfam05010 89 KSFSDLFKrYEKQKEvISGYKKNE------------ESLKKCAQdylarIKKEEQRYQALKAHAEEKLDQANEEIAQVRS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 158706129 1120 RFQQENEELKArmdkhmaisrQLSTEQ---AALQESLEKESKvnkrlsmENEEL 1170
Cdd:pfam05010 157 KAKAETAALQA----------SLRKEQmkvQSLERQLEQKTK-------ENEEL 193
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
998-1170 |
1.18e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.96 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 998 KVELLKKTYETSLSEIKKSHEMEKKSLEDLLNEKQ------ESLEKQINDLKSENDALNERLKSEEQKQlsrEKANSKNP 1071
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQAQEAANRQREKEKErykrdrEQWERQRRELESRVAELKEELRQSREKH---EELEEKYK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1072 QVMYLEQELESLKAVLeiknekLHQQDMKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAALQE 1151
Cdd:pfam07888 105 ELSASSEELSEEKDAL------LAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQA 178
|
170
....*....|....*....
gi 158706129 1152 SLEKESKVNKRLSMENEEL 1170
Cdd:pfam07888 179 KLQQTEEELRSLSKEFQEL 197
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
868-1043 |
1.18e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 41.66 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 868 KFEALtvviQHLLSEREEALKQHKTLSQELVSLRGELVAA-SSACEKLEKARADLQTAYQEFVQKLNQQH--QTDRTELE 944
Cdd:cd00176 41 KHEAL----EAELAAHEERVEALNELGEQLIEEGHPDAEEiQERLEELNQRWEELRELAEERRQRLEEALdlQQFFRDAD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 945 NRLKDLYTAECEKLQSIYIEEAEKYKTQLQEqfdnlnaaHETTKLEIEAsHSEKVELLKKTYETSLSEIKKSHEMEKKSL 1024
Cdd:cd00176 117 DLEQWLEEKEAALASEDLGKDLESVEELLKK--------HKELEEELEA-HEPRLKSLNELAEELLEEGHPDADEEIEEK 187
|
170
....*....|....*....
gi 158706129 1025 EDLLNEKQESLEKQINDLK 1043
Cdd:cd00176 188 LEELNERWEELLELAEERQ 206
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
875-1153 |
1.23e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 875 VIQHLLSEREEALKQHKTLSQELVSLRGELvaaSSACEKLEKARADLQTAYQEFVQKLNQQHQT-DRTELENRL------ 947
Cdd:PRK11281 60 LVQQDLEQTLALLDKIDRQKEETEQLKQQL---AQAPAKLRQAQAELEALKDDNDEETRETLSTlSLRQLESRLaqtldq 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 948 -----KDLYTAEC---------EKLQSIyIEEAEKYKTQLQEQFDNLNAAHETTkleieaSHSEKVELlkktyETSLSEI 1013
Cdd:PRK11281 137 lqnaqNDLAEYNSqlvslqtqpERAQAA-LYANSQRLQQIRNLLKGGKVGGKAL------RPSQRVLL-----QAEQALL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1014 KKSHEMEKKSLE-------------DLLNEKQESLEKQINDLKsenDALNE-RLK-SEEQ--KQLSREKANS--KNPqvm 1074
Cdd:PRK11281 205 NAQNDLQRKSLEgntqlqdllqkqrDYLTARIQRLEHQLQLLQ---EAINSkRLTlSEKTvqEAQSQDEAARiqANP--- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1075 YLEQELEslkavleiKNEKLHQqdmKLMKMeklVDNNTALVdklkrfqQENEELKARMDkhmaisRQLSTEQA------A 1148
Cdd:PRK11281 279 LVAQELE--------INLQLSQ---RLLKA---TEKLNTLT-------QQNLRVKNWLD------RLTQSERNikeqisV 331
|
....*
gi 158706129 1149 LQESL 1153
Cdd:PRK11281 332 LKGSL 336
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
879-1120 |
1.43e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 879 LLSEREEALKQHKTLSQELVSLRGELVAASSACEKLEKARADLQTAYQEFVQKLNQQhQTDRTELENRLKDLyTAECEKL 958
Cdd:pfam01576 824 ILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL-QDEKRRLEARIAQL-EEELEEE 901
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 959 QSIYIEEAEKYKtQLQEQFDNLNaahetTKLEIEASHSEKVELLKKTYETSLSEIK-KSHEMEK------KSLEDLLNEK 1031
Cdd:pfam01576 902 QSNTELLNDRLR-KSTLQVEQLT-----TELAAERSTSQKSESARQQLERQNKELKaKLQEMEGtvkskfKSSIAALEAK 975
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1032 QESLEKQINDLKSENDALNERLKSEEQK------QLSREKANSKN--PQVMYLEQELESLKAVLEIKNEKLHQQDMKLMK 1103
Cdd:pfam01576 976 IAQLEEQLEQESRERQAANKLVRRTEKKlkevllQVEDERRHADQykDQAEKGNSRMKQLKRQLEEAEEEASRANAARRK 1055
|
250
....*....|....*..
gi 158706129 1104 MEKLVDNNTALVDKLKR 1120
Cdd:pfam01576 1056 LQRELDDATESNESMNR 1072
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1021-1158 |
1.45e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1021 KKSLEDLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKA------NSKNPQVMYLEQELESLKAVLEIKNEKL 1094
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNefekelRERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158706129 1095 HQQDMKLMKMEKLVDNNTALVDKLkrfQQENEELKARMDKHMAISRQLSTEQA--ALQESLEKESK 1158
Cdd:PRK12704 106 EKREEELEKKEKELEQKQQELEKK---EEELEELIEEQLQELERISGLTAEEAkeILLEKVEEEAR 168
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
975-1119 |
1.62e-03 |
|
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.
Pssm-ID: 462875 [Multi-domain] Cd Length: 150 Bit Score: 40.29 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 975 EQFDNLNAAHETTKLEIEAShSEKVELLKKTYETSlSEIKKSHEMEKKSLEDLLNEKQESLEKQINDLKSENdalnerlk 1054
Cdd:pfam09744 36 ELLESLASRNQEHNVELEEL-REDNEQLETQYERE-KALRKRAEEELEEIEDQWEQETKDLLSQVESLEEEN-------- 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158706129 1055 seeqKQLSREKANSknpqvmyleqeLESLKAVLEIKNEKLHQQDMKLMKmeKLVDnntaLVDKLK 1119
Cdd:pfam09744 106 ----RRLEADHVSR-----------LEEKEAELKKEYSKLHERETEVLR--KLKE----VVDRQR 149
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
861-1133 |
1.73e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.64 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 861 LLSRGNTKFEALTVVIQHLlseREEALKQHKTLSQELVSLRGELVAASSACEKLEKARADLQTAYQEFVQKLNQQHQTD- 939
Cdd:COG5185 247 DLAQTSDKLEKLVEQNTDL---RLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEa 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 940 RTELENRLKDLYT------AECEKLQSIYIEEAEKYK------------TQLQEQFDNLNAAHETTKLEIEASHSEKVEL 1001
Cdd:COG5185 324 EQELEESKRETETgiqnltAEIEQGQESLTENLEAIKeeienivgevelSKSSEELDSFKDTIESTKESLDEIPQNQRGY 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1002 LKKTYETsLSEIKKSHEMEKKSLEDLLNEKQESLE---KQINDLKSENDALNERLKSEEQKQLS----------REKANS 1068
Cdd:COG5185 404 AQEILAT-LEDTLKAADRQIEELQRQIEQATSSNEevsKLLNELISELNKVMREADEESQSRLEeaydeinrsvRSKKED 482
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158706129 1069 KNPQVMYLEQELESLKAVLEIKNEKLHQQdmkLMKMEKLVDNNTALVDKLKRFQQENEELKARMD 1133
Cdd:COG5185 483 LNEELTQIESRVSTLKATLEKLRAKLERQ---LEGVRSKLDQVAESLKDFMRARGYAHILALENL 544
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
882-1169 |
1.73e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 882 EREEALKQHKTLSQELVSLRGELVAA-------SSACEKLEKARADLQTAYQEFVQKLN-------QQHQTDRtelenrl 947
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLAAEqyrlvemARELAELNEAESDLEQDYQAASDHLNlvqtalrQQEKIER------- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 948 kdlYTAECEKLqSIYIEEAEKYKTQLQEQFDNLNAAHETTKLEIE------ASHSEKVELLKK---TYETSLSEIKKShe 1018
Cdd:PRK04863 353 ---YQADLEEL-EERLEEQNEVVEEADEQQEENEARAEAAEEEVDelksqlADYQQALDVQQTraiQYQQAVQALERA-- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1019 mekKSLEDLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQVMYL--------------------EQ 1078
Cdd:PRK04863 427 ---KQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLvrkiagevsrseawdvarelLR 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1079 ELESLKAVLeiknEKLHQQDMKLMKMEKLVDNNTALVDKLKRFQQ-------ENEELKarmdkhmaisrQLSTEQAALQE 1151
Cdd:PRK04863 504 RLREQRHLA----EQLQQLRMRLSELEQRLRQQQRAERLLAEFCKrlgknldDEDELE-----------QLQEELEARLE 568
|
330 340
....*....|....*....|
gi 158706129 1152 SL--EKESKVNKRLSMENEE 1169
Cdd:PRK04863 569 SLseSVSEARERRMALRQQL 588
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1002-1143 |
1.87e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.73 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1002 LKKTYETSLSEIKKSHEMEKKSLEDllNEKQESLEKQINDLksendaLNERLKSEEQkqlsrekanskNPQVMYLEQEL- 1080
Cdd:TIGR01612 546 LKESYELAKNWKKLIHEIKKELEEE--NEDSIHLEKEIKDL------FDKYLEIDDE-----------IIYINKLKLELk 606
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158706129 1081 ESLKAVLEiKNEKLHqqdmKLMKMEKLVDNNTALVDKLKRFQ--QENEELKARMDKHMAISRQLS 1143
Cdd:TIGR01612 607 EKIKNISD-KNEYIK----KAIDLKKIIENNNAYIDELAKISpyQVPEHLKNKDKIYSTIKSELS 666
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
867-1174 |
1.96e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 867 TKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSACEKLEKARADLQTAYQEFvqklnqqhqtdRTELENR 946
Cdd:pfam01576 636 TRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEM-----------KTQLEEL 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 947 LKDLYTAECEKLQ----------------SIYIEEAEKYKTQLQEQFDNLNAahettKLEIEASHSEKVELLKKTYETSL 1010
Cdd:pfam01576 705 EDELQATEDAKLRlevnmqalkaqferdlQARDEQGEEKRRQLVKQVRELEA-----ELEDERKQRAQAVAAKKKLELDL 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1011 SEIKKSHEMEKKSLEDLLneKQ-ESLEKQINDLKSENDALneRLKSEEQKQLSRE---KANSKNPQVMYLEQELE-SLKA 1085
Cdd:pfam01576 780 KELEAQIDAANKGREEAV--KQlKKLQAQMKDLQRELEEA--RASRDEILAQSKEsekKLKNLEAELLQLQEDLAaSERA 855
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1086 VLEIKNEKLHQQD---MKLMKMEKLVDNNTALVDKLKRFQQENEE-------LKARMDKHMAISRQLSTEQAALQESLEK 1155
Cdd:pfam01576 856 RRQAQQERDELADeiaSGASGKSALQDEKRRLEARIAQLEEELEEeqsntelLNDRLRKSTLQVEQLTTELAAERSTSQK 935
|
330
....*....|....*....
gi 158706129 1156 ESKVNKRLSMENEELLWKL 1174
Cdd:pfam01576 936 SESARQQLERQNKELKAKL 954
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
871-1107 |
2.00e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 41.26 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 871 ALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSACEKLEKARADLQTAYQEfvqkLNQQHQtDRTELENRLKDL 950
Cdd:pfam17078 21 QLTVQSQNLLSKLEIAQQKESKFLENLASLKHENDNLSSMLNRKERRLKDLEDQLSE----LKNSYE-ELTESNKQLKKR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 951 ytaeCEKLQSIYIEEAEKYKtQLQEQFDNLNAAHEttkleieashsekveLLKKTYETSLSEIKKShemekksLEDLLNE 1030
Cdd:pfam17078 96 ----LENSSASETTLEAELE-RLQIQYDALVDSQN---------------EYKDHYQQEINTLQES-------LEDLKLE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1031 KQESLEKQINDLKSENDALNERLKSeeqkqLSREKANSKNPQV---MYLEQELESLKAVLEIKN-EKLHQ--QDMKLMKM 1104
Cdd:pfam17078 149 NEKQLENYQQRISSNDKDIDTKLDS-----YNNKFKNLDNIYVnknNKLLTKLDSLAQLLDLPSwLNLYPesRNKILEYA 223
|
...
gi 158706129 1105 EKL 1107
Cdd:pfam17078 224 EKM 226
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
912-1097 |
2.12e-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: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 912 EKLEKARADLQTAYQEfVQKLNQQH-----QTDRTELENRLKDLYTAeceklqsiyIEEAEKYKTQLQEQFDNLNAAHET 986
Cdd:COG3206 182 EQLPELRKELEEAEAA-LEEFRQKNglvdlSEEAKLLLQQLSELESQ---------LAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 987 TKLEI-EASHSEKVELLKKTY---ETSLSEIKKS----H-EME--KKSLEDLLNEKQESLEKQINDLKSENDALNERLKS 1055
Cdd:COG3206 252 GPDALpELLQSPVIQQLRAQLaelEAELAELSARytpnHpDVIalRAQIAALRAQLQQEAQRILASLEAELEALQAREAS 331
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 158706129 1056 EEQkQLSREKANSKN-PQvmyLEQELESLKAVLEIkNEKLHQQ 1097
Cdd:COG3206 332 LQA-QLAQLEARLAElPE---LEAELRRLEREVEV-ARELYES 369
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
974-1124 |
2.15e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 974 QEQFDNLNA--AHETTKLEIEASHSEKVELLKKTYETSLSeikkSHEMEKKSLEDLLNEkqesLEKQINDLKSENDALNE 1051
Cdd:PRK09039 52 DSALDRLNSqiAELADLLSLERQGNQDLQDSVANLRASLS----AAEAERSRLQALLAE----LAGAGAAAEGRAGELAQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1052 RLksEEQKQLSrEKANSK----NPQVMYLEQELESLKAVLEIKNEKLHQQDMKLMKM-EKLvdnNTALVDK---LKRFQQ 1123
Cdd:PRK09039 124 EL--DSEKQVS-ARALAQvellNQQIAALRRQLAALEAALDASEKRDRESQAKIADLgRRL---NVALAQRvqeLNRYRS 197
|
.
gi 158706129 1124 E 1124
Cdd:PRK09039 198 E 198
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
801-1064 |
2.33e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 801 RKSLFTAFNSVEKGRQ-----KNPRslCIQtqtapDVLSSERTLELAQYKTKCESQSGFILHLRQLLSRGNTKFEALTVV 875
Cdd:PRK02224 432 EATLRTARERVEEAEAlleagKCPE--CGQ-----PVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 876 IQhlLSEREEALKQHKTLSQELVSLRGELVAASS-ACEKLEKARADLQTAYQEFVQKLNQQHQ-------------TDRT 941
Cdd:PRK02224 505 VE--AEDRIERLEERREDLEELIAERRETIEEKReRAEELRERAAELEAEAEEKREAAAEAEEeaeeareevaelnSKLA 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 942 ELENRLKDLytaecEKLQSIY--IEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKTYETSLSEIKKSHEM 1019
Cdd:PRK02224 583 ELKERIESL-----ERIRTLLaaIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKER 657
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 158706129 1020 EKKSLEDL------LNEKQESLEKQINDLKSENDALN---ERLKSEEQKQLSRE 1064
Cdd:PRK02224 658 AEEYLEQVeekldeLREERDDLQAEIGAVENELEELEelrERREALENRVEALE 711
|
|
| Ctf13_LRR_LRR-insertion |
cd19611 |
leucine-rich-repeat (LRR) domain and LRR insertion domain of centromere DNA-binding protein ... |
1009-1096 |
2.52e-03 |
|
leucine-rich-repeat (LRR) domain and LRR insertion domain of centromere DNA-binding protein complex CBF3 subunit C (Ctf13); Ctf13, is an F-box protein of the leucine-rich-repeat superfamily; it is a component of CEN binding factor 3 (CBF3), a complex that recognizes point centromeres found in budding yeast, associating specifically with the third centromere DNA element (CDEIII) DNA. CBF3 is comprised of two homodimers of Cep3 and Ndc10, and a Ctf13-Skp1 heterodimer. The Skp1-Ctf13 heterodimer interacts with Cep3, Ndc10 and CDEIII at a completely conserved G, centrally positioned between the TGC/CCG sites. The eight leucine-rich repeat (LRR) motifs of Ctf13 (LRR 1-8) form a solenoid structure. At the N-terminus of the Ctf13 LRR is an expanded F-box, and at the C-terminal end, an alpha-beta domain formed by insertions within the latter LRRs of Ctf13 (LRR insertion domain). This domain model includes the LLR domain and the LRR insertion domain.
Pssm-ID: 381623 Cd Length: 290 Bit Score: 41.17 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1009 SLSEIKK-SHEMEKKSLEDLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQVMYLEQELESLK--A 1085
Cdd:cd19611 14 NPNMVKKiLKVLEKKELLDLVSEVFFGQDEEESDEEDEDDSSKNDRKKLTDDDVKEKSYKLNDPSIIRIISSLESMKnlR 93
|
90
....*....|.
gi 158706129 1086 VLEIKNEKLHQ 1096
Cdd:cd19611 94 KLSVRGDNLYE 104
|
|
| Snf7 |
pfam03357 |
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ... |
1025-1174 |
2.88e-03 |
|
Snf7; This family of proteins are involved in protein sorting and transport from the endosome to the vacuole/lysosome in eukaryotic cells. Vacuoles/lysosomes play an important role in the degradation of both lipids and cellular proteins. In order to perform this degradative function, vacuoles/lysosomes contain numerous hydrolases which have been transported in the form of inactive precursors via the biosynthetic pathway and are proteolytically activated upon delivery to the vacuole/lysosome. The delivery of transmembrane proteins, such as activated cell surface receptors to the lumen of the vacuole/lysosome, either for degradation/downregulation, or in the case of hydrolases, for proper localization, requires the formation of multivesicular bodies (MVBs). These late endosomal structures are formed by invaginating and budding of the limiting membrane into the lumen of the compartment. During this process, a subset of the endosomal membrane proteins is sorted into the forming vesicles. Mature MVBs fuse with the vacuole/lysosome, thereby releasing cargo containing vesicles into its hydrolytic lumen for degradation. Endosomal proteins that are not sorted into the intralumenal MVB vesicles are either recycled back to the plasma membrane or Golgi complex, or remain in the limiting membrane of the MVB and are thereby transported to the limiting membrane of the vacuole/lysosome as a consequence of fusion. Therefore, the MVB sorting pathway plays a critical role in the decision between recycling and degradation of membrane proteins. A few archaeal sequences are also present within this family.
Pssm-ID: 460896 [Multi-domain] Cd Length: 168 Bit Score: 39.91 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1025 EDLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNpQVMYLEQELESLKAVLE-IKNEKLHQQDMKLMK 1103
Cdd:pfam03357 10 IRKLDKKQESLEKKIEKLELEIKKLAKKGNKDAALLLLKQKKRYEK-QLDQLDGQLSNLEQQRMaIENAKSNQEVLNAMK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1104 --------MEKLVDnntalVDKLKRFQQENEELKARMD-KHMAISRQLSTEQAALQESLEKEskVNKRLSMENEELLWKL 1174
Cdd:pfam03357 89 qgakamkaMNKLMD-----IDKIDKLMDEIEDQMEKADeISEMLSDPLDDADEEDEEELDAE--LDALLDEIGDEESVEL 161
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
913-1162 |
3.47e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 913 KLEKARADLQTAYQEFVQKLNQ----QHQTDRTElENRLKDLYTAECEKLQSIYIEEAEKYKTQLQEQFDNLNAAHETTK 988
Cdd:PTZ00121 1213 KAEEARKAEDAKKAEAVKKAEEakkdAEEAKKAE-EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKK 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 989 LEiEASHSE---KVELLKKTYETS--LSEIKKSHEMEKKSLEDLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSR 1063
Cdd:PTZ00121 1292 AD-EAKKAEekkKADEAKKKAEEAkkADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE 1370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1064 EKANSKNPQVMYLEQELESLKAVLEIKneKLHQQDMKLMKMEKLVDNNTALVDKLKRFQQEN---EELKARM-DKHMAIS 1139
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKADEAK--KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKkkaDEAKKKAeEAKKADE 1448
|
250 260
....*....|....*....|...
gi 158706129 1140 RQLSTEQAALQESLEKESKVNKR 1162
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKK 1471
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
859-1175 |
3.53e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 41.43 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 859 RQLLSRGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAAS----SACEKLEKAR-------ADLQTAYQE 927
Cdd:pfam15964 374 KELASQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVEKVTreknSLVSQLEEAQkqlasqeMDVTKVCGE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 928 FVQKLNQ-QHQTDRTELENR------LKDLYTAEcEKLQSIYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEK-- 998
Cdd:pfam15964 454 MRYQLNQtKMKKDEAEKEHReyrtktGRQLEIKD-QEIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLGESEHql 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 999 --VELLKKTYETSLSEIKKSHEMEKKSLEDLLNEKQESLEKQINDLKSENDALnerlkseeqkqlsrekANSKNPQVMYL 1076
Cdd:pfam15964 533 hlTRLEKESIQQSFSNEAKAQALQAQQREQELTQKMQQMEAQHDKTVNEQYSL----------------LTSQNTFIAKL 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1077 EQELESLKAVLEIKNEKLHQqdmklmKMEKLVDNNTALVDKLKRFQQENEELK------ARMDKHMAIS-RQLSTE-QAA 1148
Cdd:pfam15964 597 KEECCTLAKKLEEITQKSRS------EVEQLSQEKEYLQDRLEKLQKRNEELEeqcvqhGRMHERMKQRlRQLDKHcQAT 670
|
330 340
....*....|....*....|....*..
gi 158706129 1149 LQESLEKESKVNKrLSMENEELLWKLH 1175
Cdd:pfam15964 671 AQQLVQLLSKQNQ-LFKERQNLTEEVQ 696
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1007-1170 |
4.30e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1007 ETSLSEIKKSHEMEKKSLEDLLNEkqesLEKQINDLKSENDALNERLKSE-EQKQLSREKANSKNPQVMYLEQELESLKA 1085
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDE----LNEELKELAEKRDELNAQVKELrEEAQELREKRDELNEKVKELKEERDELNE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1086 VLEIKNEKLHQQDMKLMKMEKL------------------------VDNNTALVDKLKRFQQENEELKARMDKHMAIsRQ 1141
Cdd:COG1340 86 KLNELREELDELRKELAELNKAggsidklrkeierlewrqqtevlsPEEEKELVEKIKELEKELEKAKKALEKNEKL-KE 164
|
170 180
....*....|....*....|....*....
gi 158706129 1142 LSTEQAALQESLEKESKVNKRLSMENEEL 1170
Cdd:COG1340 165 LRAELKELRKEAEEIHKKIKELAEEAQEL 193
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
836-1044 |
4.43e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 836 ERTLELAQYKTKCESQSgfILHLRQLLSRGNTKFEALTVVIQHLLSEREEalkqhktLSQELVSLRGELVAASSACEKLE 915
Cdd:TIGR02168 837 ERRLEDLEEQIEELSED--IESLAAEIEELEELIEELESELEALLNERAS-------LEEALALLRSELEELSEELRELE 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 916 KARADLQTAYQEFVQKLNqQHQTDRTELENRlkdlytaeceklqsiyieeaekyktqLQEQFDNLNAAHETTKLEIEASH 995
Cdd:TIGR02168 908 SKRSELRRELEELREKLA-QLELRLEGLEVR--------------------------IDNLQERLSEEYSLTLEEAEALE 960
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 158706129 996 SEKVELLKKTYEtslsEIkKSHEMEKKSL--------EDL--LNEKQESLEKQINDLKS 1044
Cdd:TIGR02168 961 NKIEDDEEEARR----RL-KRLENKIKELgpvnlaaiEEYeeLKERYDFLTAQKEDLTE 1014
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
801-1070 |
5.02e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.19 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 801 RKSLFTAFNSVEKGRQKNPRSLCIQTQTAPdvlSSERTLELAQYKTK---CESQSGFILHLRQLLSRgNTKFEALTVVIQ 877
Cdd:TIGR01612 1575 KKEKFRIEDDAAKNDKSNKAAIDIQLSLEN---FENKFLKISDIKKKindCLKETESIEKKISSFSI-DSQDTELKENGD 1650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 878 HLLSERE--EALKQHKtlsQELVSLRGELVAASSACEKLEKARADLQTAYQ-EFVQKLNQQHQTDRTELENrLKDLYTAE 954
Cdd:TIGR01612 1651 NLNSLQEflESLKDQK---KNIEDKKKELDELDSEIEKIEIDVDQHKKNYEiGIIEKIKEIAIANKEEIES-IKELIEPT 1726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 955 CEKLQSIYI----------EEAEKYKTQLQEQFDNLNAAHE--TTKLEIEASHSEKVELLKKTYETSLSEIKKSHEMEKK 1022
Cdd:TIGR01612 1727 IENLISSFNtndlegidpnEKLEEYNTEIGDIYEEFIELYNiiAGCLETVSKEPITYDEIKNTRINAQNEFLKIIEIEKK 1806
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 158706129 1023 SLEDLLNEKQESLEKQINDLKSENDALNERLKSEEQK------QLSREKANSKN 1070
Cdd:TIGR01612 1807 SKSYLDDIEAKEFDRIINHFKKKLDHVNDKFTKEYSKinegfdDISKSIENVKN 1860
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
962-1170 |
5.59e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 962 YIEEAEKYKTQLQEQFDNLnaahettkLEIEASHSEKVELLKKTYETSLSEI-KKSH-------EMEKK--SLEDL---- 1027
Cdd:PRK04778 113 LLDLIEEDIEQILEELQEL--------LESEEKNREEVEQLKDLYRELRKSLlANRFsfgpaldELEKQleNLEEEfsqf 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1028 --LNEKQESLE--KQINDLKSENDALNERLksEEQKQLSREKANSknpqvmyLEQELESLKAVL-EIKNEKLHQQDMKLM 1102
Cdd:PRK04778 185 veLTESGDYVEarEILDQLEEELAALEQIM--EEIPELLKELQTE-------LPDQLQELKAGYrELVEEGYHLDHLDIE 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1103 KM-----EKLVDNNTALVD-KLKRFQQENEELKARMDK------HMAISRQ-LSTEQAALQESLEKESKVNKRLSMENEE 1169
Cdd:PRK04778 256 KEiqdlkEQIDENLALLEElDLDEAEEKNEEIQERIDQlydileREVKARKyVEKNSDTLPDFLEHAKEQNKELKEEIDR 335
|
.
gi 158706129 1170 L 1170
Cdd:PRK04778 336 V 336
|
|
| DUF4455 |
pfam14643 |
Domain of unknown function (DUF4455); This domain family is found in bacteria and eukaryotes, ... |
925-1168 |
5.70e-03 |
|
Domain of unknown function (DUF4455); This domain family is found in bacteria and eukaryotes, and is approximately 480 amino acids in length. There are two completely conserved residues (W and P) that may be functionally important.
Pssm-ID: 464231 [Multi-domain] Cd Length: 469 Bit Score: 40.73 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 925 YQEFVQKLNQQHQTDR-TELEN---RLKDLYTAECEKLQSI-YIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKV 999
Cdd:pfam14643 190 FKEFIASEEIQNPPERkKELEEmlkEQKKLQQKRLELLQKIsDLLPPAYSKSKVEEWWASLEALNEQLDQYHDQCMTKLR 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1000 ELLKKTYETSLSEIkkshemekksledllnekqESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQVMYLEQE 1079
Cdd:pfam14643 270 AEYEEVWQECLARV-------------------QKLKQELLDYKVCSEEEAEALVNEEFLPLVGKLQRDAEDELEKLDKF 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1080 LESLKAVLEIKNEKLHQQDMKLMKM-----EKLVDNNTALVDKLK----RFQQENEELKARMDKHMAISRQLSTEQaALQ 1150
Cdd:pfam14643 331 LEELAKQTEAQSEDLFKFFREAAQLwdvhqTELAKQELELEKKLEqcrqKHDQENQAKEAALDKKLDQLRQASTEE-KLK 409
|
250
....*....|....*....
gi 158706129 1151 ESLEkesKVNKRLS-MENE 1168
Cdd:pfam14643 410 ECLD---KALKFLDdIEKE 425
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1000-1171 |
6.17e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.80 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1000 ELLKKTYETSLSEIKkSHEMEKKSLEDLLN------------EKQESLEKQINDLK-SENDALNERLKSEEQKQLSreka 1066
Cdd:TIGR00606 189 ETLRQVRQTQGQKVQ-EHQMELKYLKQYKEkaceirdqitskEAQLESSREIVKSYeNELDPLKNRLKEIEHNLSK---- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1067 nsknpqVMYLEQELESLKavleiKNEKLHQQDMKLM--KMEKLvdnntalvdklkrFQQENEELKARMDKHMAISRQLST 1144
Cdd:TIGR00606 264 ------IMKLDNEIKALK-----SRKKQMEKDNSELelKMEKV-------------FQGTDEQLNDLYHNHQRTVREKER 319
|
170 180
....*....|....*....|....*..
gi 158706129 1145 EQAALQESLEKESKVNKRLSMENEELL 1171
Cdd:TIGR00606 320 ELVDCQRELEKLNKERRLLNQEKTELL 346
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
889-1068 |
6.22e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.09 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 889 QHKTLSQELVSLRGELVAASSACEKLEKARADLQT-AYQEFVQKLNQQhqtdrTELENRLK-DLYTAECEKLQSiyieeA 966
Cdd:COG3096 935 QFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHfSYEDAVGLLGEN-----SDLNEKLRaRLEQAEEARREA-----R 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 967 EKYKtQLQEQFDNLNAAHETTKleieASHSEKVELLKKtYETSLSE--IKKSHEME------KKSLEDLLNE---KQESL 1035
Cdd:COG3096 1005 EQLR-QAQAQYSQYNQVLASLK----SSRDAKQQTLQE-LEQELEElgVQADAEAEerarirRDELHEELSQnrsRRSQL 1078
|
170 180 190
....*....|....*....|....*....|....
gi 158706129 1036 EKQINDLKSENDALNERLKSEEQK-QLSREKANS 1068
Cdd:COG3096 1079 EKQLTRCEAEMDSLQKRLRKAERDyKQEREQVVQ 1112
|
|
| Wtap |
pfam17098 |
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and ... |
1020-1170 |
6.64e-03 |
|
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and pre-mRNA-splicing regulator WTAP from mammals. The former is required for female-specific splicing of Sex-lethal RNA, and the latter is a regulatory subunit of the RNA N6-methyladenosine methyltransferase. The family also includes the yeast Mum2p protein which is part of the Mis complex.
Pssm-ID: 465345 [Multi-domain] Cd Length: 155 Bit Score: 38.43 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1020 EKKSLEDLLNEKQESLEKQINDLKSENDalneRLKSEEQKQLSREKANSKNPQVMYLEQELeslKAVLEIKNEKLHQQDM 1099
Cdd:pfam17098 1 ESKRRENLLLARLAEKEQEIQELKAQLQ----DLKQSLQPPSSQLRSLLLDPAVNLEFLRL---KKELEEKKKKLKEAQL 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158706129 1100 KLMKMEKLVDNNT--ALVDKLKRFQQENEELkarmdkhmaiSRQLSTEQAA-LQESLEKESKVNKRLSMENEEL 1170
Cdd:pfam17098 74 ELAAWKFTPDSTTgkRLMAKCRLLQQENEEL----------GRQLSEGRIAkLEIELALQKKVVEELKKSLEEL 137
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
981-1191 |
6.74e-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: 40.98 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 981 NAAHETTKLEIEASHSEKVEL----LKKTYETSLSEIKKSHEMEKKSLEDlLNEKQESLEKQINDLKsenDALNERLKSE 1056
Cdd:pfam12128 238 KIRPEFTKLQQEFNTLESAELrlshLHFGYKSDETLIASRQEERQETSAE-LNQLLRTLDDQWKEKR---DELNGELSAA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1057 E----QKQLSREKANSKNPQvmYLEQELESLKAVLEikNEKLHQQDMKLmkMEKLVDnntALVDKLKRFQQENEELKArm 1132
Cdd:pfam12128 314 DaavaKDRSELEALEDQHGA--FLDADIETAAADQE--QLPSWQSELEN--LEERLK---ALTGKHQDVTAKYNRRRS-- 382
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 158706129 1133 dkhmAISRQLSTEQAALQESLEKESKVNKRLSMENEELLWKlhngdLCSPKRSPTSSAI 1191
Cdd:pfam12128 383 ----KIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQA-----LESELREQLEAGK 432
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
940-1051 |
7.32e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 38.00 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 940 RTELENRLKDLytaecEKLQSIYIEEAEKYKTQLQEQFDNLNAAHEttKLEIE-ASHSEKVELLKKTYETSLSEIKKSHE 1018
Cdd:pfam07926 3 LSSLQSEIKRL-----KEEAADAEAQLQKLQEDLEKQAEIAREAQQ--NYERElVLHAEDIKALQALREELNELKAEIAE 75
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 158706129 1019 MEKK---------SLEDLLNEKQESLEKQINDLKSENDALNE 1051
Cdd:pfam07926 76 LKAEaesakaeleESEESWEEQKKELEKELSELEKRIEDLNE 117
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
884-1073 |
7.56e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 39.59 E-value: 7.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 884 EEALKQHKTLSQELVSLRGELVAASSA------CEKLEKARADLQTAYQEfVQKLNQQHQTDRTELENRLkdlytaecEK 957
Cdd:pfam12795 47 DDAPAELRELRQELAALQAKAEAAPKEilaslsLEELEQRLLQTSAQLQE-LQNQLAQLNSQLIELQTRP--------ER 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 958 LQSIyIEEAEKYKTQLQEQFDNLNAAHET------TKLEIE-ASHSEKVELLKK-----TYETSLSEIKKshemekksle 1025
Cdd:pfam12795 118 AQQQ-LSEARQRLQQIRNRLNGPAPPGEPlseaqrWALQAElAALKAQIDMLEQellsnNNRQDLLKARR---------- 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 158706129 1026 DLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANS--KNPQV 1073
Cdd:pfam12795 187 DLLTLRIQRLEQQLQALQELLNEKRLQEAEQAVAQTEQLAEEAagDHPLV 236
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
933-1172 |
7.77e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 40.81 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 933 NQQHQTDRTEL---ENRLKDLYTAECEKLQSIYIEEAEK---------YKTQLQEQ-------FDNLNAA-------HET 986
Cdd:TIGR01612 1857 NVKNSTDENLLfdiLNKTKDAYAGIIGKKYYSYKDEAEKifinisklaNSINIQIQnnsgidlFDNINIAilssldsEKE 1936
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 987 TKLEIEASHSEKVELLKK---TYETSLSEIKKSHEMEKKSLE--DLLNEKQESLEK--QINDLK--------SENDALNE 1051
Cdd:TIGR01612 1937 DTLKFIPSPEKEPEIYTKirdSYDTLLDIFKKSQDLHKKEQDtlNIIFENQQLYEKiqASNELKdtlsdlkyKKEKILND 2016
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1052 -RL---KSEEQKQLSREKAN-------SKNPQVMY----LEQELESLKAVLEIKNEKlHQQDMKLMKMEKLVDNNTALVD 1116
Cdd:TIGR01612 2017 vKLllhKFDELNKLSCDSQNydtilelSKQDKIKEkidnYEKEKEKFGIDFDVKAME-EKFDNDIKDIEKFENNYKHSEK 2095
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 158706129 1117 KLKRFQQENEELKARMDKHMAISRQLSTEQAALQES-LEKESKVNKRLSMENEELLW 1172
Cdd:TIGR01612 2096 DNHDFSEEKDNIIQSKKKLKELTEAFNTEIKIIEDKiIEKNDLIDKLIEMRKECLLF 2152
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
988-1097 |
8.16e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.45 E-value: 8.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 988 KLEIEASHSEKVELLKKtyetsLSEIKKSHEMEKKSLEDLLNEKQESLEKQINDLKSENDALNERLKSE----EQKQLSR 1063
Cdd:COG0542 403 RMEIDSKPEELDELERR-----LEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEkeliEEIQELK 477
|
90 100 110
....*....|....*....|....*....|....
gi 158706129 1064 EKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQ 1097
Cdd:COG0542 478 EELEQRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
891-986 |
8.20e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 40.10 E-value: 8.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 891 KTLSQELVSLRGELVAASSACEKLEKARADLQTAYQEFVQKLNqQHQTDRTELENRLKDLYTAECEKLQSIYiEEAEKYK 970
Cdd:TIGR04320 257 AALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALA-TAQKELANAQAQALQTAQNNLATAQAAL-ANAEARL 334
|
90
....*....|....*.
gi 158706129 971 TQLQEQFDNLNAAHET 986
Cdd:TIGR04320 335 AKAKEALANLNADLAK 350
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
887-1112 |
8.31e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 39.70 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 887 LKQHKTLSQELVSLRGELVAASSACEKLEKARADLQTAYQEFVQKLNQ---QHQTDRTELE---NRLKDLYTAeceklqs 960
Cdd:pfam06008 18 NYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQtlaKAQQVNAESErtlGHAKELAEA------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 961 iyIEEAEKYKTQLQEQFDNLNA-AHETTKLEIEASHSEKVELLKKTYETSLSEIKKSHEMEKKSLEDLLNEKQESLEKQI 1039
Cdd:pfam06008 91 --IKNLIDNIKEINEKVATLGEnDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQ 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158706129 1040 NDLKSENDALNERLKSEEQK-----QLSREkANSKNPQVMYLEQELEslkavleiKNEKLHQQDMKLMKMEKLVDNNT 1112
Cdd:pfam06008 169 EENKALANALRDSLAEYEAKlsdlrELLRE-AAAKTRDANRLNLANQ--------ANLREFQRKKEEVSEQKNQLEET 237
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
971-1059 |
9.61e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.30 E-value: 9.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 971 TQLQE----QFDNLNAAHETTKLEIEASH----SEKVELLKKTYETSLSEIKKSHEMEKKSLEDLLNEKQESL---EKQI 1039
Cdd:PRK05771 23 EALHElgvvHIEDLKEELSNERLRKLRSLltklSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELekiEKEI 102
|
90 100
....*....|....*....|
gi 158706129 1040 NDLKSENDALNERLKSEEQK 1059
Cdd:PRK05771 103 KELEEEISELENEIKELEQE 122
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
930-1170 |
9.73e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.42 E-value: 9.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 930 QKLNQQHQTDRTELENRLKDLYTAECEKLQSIY------IEEAEKYKTQLQEQFDNLNAahettklEIEASHSEKVELLK 1003
Cdd:TIGR00606 275 KSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYhnhqrtVREKERELVDCQRELEKLNK-------ERRLLNQEKTELLV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1004 KTYETSLSEIKKSHEMEKKSLEDLLNEKQESLEKQINDLKSENDALN-ERLKSEEQKQLSR----------EKANSKNPQ 1072
Cdd:TIGR00606 348 EQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNfHTLVIERQEDEAKtaaqlcadlqSKERLKQEQ 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158706129 1073 VMYLEQELESLKAVLEIKNEKLHQQDMKLMKMEKLVDNNTALVDKLKRFQQE---NEELKARMDKHMAIS------RQLS 1143
Cdd:TIGR00606 428 ADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQElrkAERELSKAEKNSLTEtlkkevKSLQ 507
|
250 260
....*....|....*....|....*..
gi 158706129 1144 TEQAALQESLEKESKVNKRLSMENEEL 1170
Cdd:TIGR00606 508 NEKADLDRKLRKLDQEMEQLNHHTTTR 534
|
|
| |
