|
Name |
Accession |
Description |
Interval |
E-value |
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
86-260 |
2.49e-47 |
|
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: 159.74 E-value: 2.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 86 LFQDKLGEVSTYTDDLQKKLVPFATELHERLTKDSEKLKEEIRKELEDLRARLLPHATEVSQKIGDNVRELQQRLGPYAE 165
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 166 ELRTQVDTQAQQLRRQLTPYAERMEKVMRQNLDQLQASLAPYAEELQATVNQRVEELKGRLTPYADQLQTKIEENVEELR 245
Cdd:pfam01442 81 ELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQELR 160
|
170
....*....|....*
gi 528976936 246 RSLAPYAQDVQGKLN 260
Cdd:pfam01442 161 EKLEPQAEDLREKLD 175
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
235-390 |
3.63e-11 |
|
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: 61.51 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 235 TKIEENVEELRRSLAPYAQDVQGKLNHQLEGLAFQMKKHAEELKAKISAKAEELRQGLVplvnsvhgsqlGNAEDLQKSL 314
Cdd:pfam01442 7 DELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLG-----------QNVEELRQRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 315 A----ELSSRLDQQVEDFRRTVGPYGETFNKAMVQQLDTLRQKLGPLAGDVEDHLSFLEKDLRDKVSSFFNTLKEKESQA 390
Cdd:pfam01442 76 EpyteELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQR 155
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
67-382 |
1.28e-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: 53.92 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 67 AKKAVEHIQK--SELTQQLNTlFQDKLGEVSTYTDDLQKKLVPFATELhERLTKDSEKLKEEI---RKELEDLRARLLPH 141
Cdd:TIGR02169 714 ASRKIGEIEKeiEQLEQEEEK-LKERLEELEEDLSSLEQEIENVKSEL-KELEARIEELEEDLhklEEALNDLEARLSHS 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 142 ATEVSQKIGDNVRELQQRLGPYAEELrtQVDTQAQQLRRQLTPyAERMEKVMRQNLDQLQ-ASLAPYAEELQATV---NQ 217
Cdd:TIGR02169 792 RIPEIQAELSKLEEEVSRIEARLREI--EQKLNRLTLEKEYLE-KEIQELQEQRIDLKEQiKSIEKEIENLNGKKeelEE 868
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 218 RVEELKGRLTPYADQLQtKIEENVEELRRSLAPyAQDVQGKLNHQLEglafQMKKHAEELKAKISAKAEELRQGLVPLVN 297
Cdd:TIGR02169 869 ELEELEAALRDLESRLG-DLKKERDELEAQLRE-LERKIEELEAQIE----KKRKRLSELKAKLEALEEELSEIEDPKGE 942
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 298 SVH-GSQLGNAEDLQKSLAELSSRLDQQVEDFRRTVGPYGETfnkamVQQLDTLRQKLGPLAGDVEDHLSFLEKDLRDKV 376
Cdd:TIGR02169 943 DEEiPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEV-----LKRLDELKEKRAKLEEERKAILERIEEYEKKKR 1017
|
....*.
gi 528976936 377 SSFFNT 382
Cdd:TIGR02169 1018 EVFMEA 1023
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
111-248 |
8.26e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 8.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 111 ELHERLTKDSEKLKEEIRK------ELEDLRARLLPHATEVSQKIG----DNVRELQQRLgPYAEELRTQVDTQAQQLRR 180
Cdd:PRK04863 935 EQFEQLKQDYQQAQQTQRDakqqafALTEVVQRRAHFSYEDAAEMLaknsDLNEKLRQRL-EQAEQERTRAREQLRQAQA 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 181 QLTPYAERMEK------VMRQNLDQLQASLA----PYAEELQATVNQRVEELKGRL------TPYADQLQTKIEENVEEL 244
Cdd:PRK04863 1014 QLAQYNQVLASlkssydAKRQMLQELKQELQdlgvPADSGAEERARARRDELHARLsanrsrRNQLEKQLTFCEAEMDNL 1093
|
....
gi 528976936 245 RRSL 248
Cdd:PRK04863 1094 TKKL 1097
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
105-323 |
8.99e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 8.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 105 LVPFATELHERLTKDSEKLKEEIRKELEDLRARLLPHATEVsQKIGDNVRELQQRLGPYAEELRtQVDTQAQQLRRQLTP 184
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEE-KALLKQLAALERRIAALARRIR-ALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 185 yAERMEKVMRQNLDQLQASLAPYAEELQAtvNQRVEELKGRLTP-----------YADQLQTKIEENVEELRRSLApYAQ 253
Cdd:COG4942 88 -LEKEIAELRAELEAQKEELAELLRALYR--LGRQPPLALLLSPedfldavrrlqYLKYLAPARREQAEELRADLA-ELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 254 DVQGKLNHQLEGLAFQMKKHAEELKAKISAKAEelRQGLVPLVNSVHGSQLGNAEDLQKSLAELSSRLDQ 323
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAE--RQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
117-291 |
1.56e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 40.96 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 117 TKDSEKLKEEIRKELEDLRA---RLLPHATEVSQKIG--DNVRELQqRLGPYAEELRTQVDTQAQQLRRQLTPYAERMEK 191
Cdd:NF041483 322 TKEAEALKAEAEQALADARAeaeKLVAEAAEKARTVAaeDTAAQLA-KAARTAEEVLTKASEDAKATTRAAAEEAERIRR 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 192 VMRQNLDQLQASLAPYAEELQATVNQRVEELKG----------RLTPYADQLQTKIEENVEELRRSLAPYAqdVQgklnh 261
Cdd:NF041483 401 EAEAEADRLRGEAADQAEQLKGAAKDDTKEYRAktvelqeearRLRGEAEQLRAEAVAEGERIRGEARREA--VQ----- 473
|
170 180 190
....*....|....*....|....*....|
gi 528976936 262 QLEGLAfqmkKHAEELKAKISAKAEELRQG 291
Cdd:NF041483 474 QIEEAA----RTAEELLTKAKADADELRST 499
|
|
| antiphage_ZorA_2 |
NF033915 |
anti-phage ZorAB system protein ZorA; Proteins of this subfamily are putative H+ channel ... |
111-257 |
3.00e-03 |
|
anti-phage ZorAB system protein ZorA; Proteins of this subfamily are putative H+ channel proteins, but it has been reported that they are also involved in anti-phage defense.
Pssm-ID: 411476 [Multi-domain] Cd Length: 383 Bit Score: 39.36 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 111 ELHER--------LTKDSEKLKEEIRKELEDLRA----RLLPHATEVSQKIGDN-VRELQQRLGPYAEELRTQVDTQAQQ 177
Cdd:NF033915 224 ELHERigdrlqesLNGMSEAMQTALTDALNNIMApaiqTLVSTTSQQSTQVLESlVGNFMDGMTSAGREQGLQMQQAAAD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 178 LRRQLTPYAERMEKVMRQnLDQLQASLAPYAEELQATVNQRVEELKGRltpyADQLQTKIEENVEELRRSLAPYAQDVQG 257
Cdd:NF033915 304 VNAAVSGMSERLNQLFNS-LSEQQGRQMERAQQQSSTFETQLQRLSGS----ANERQAQLEQRFEELMSGLTEQLQTQLG 378
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
164-386 |
6.24e-03 |
|
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: 38.12 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 164 AEELRTQVDTQAQQLRRQLTPYAERMEKVmRQNLDQLQASLAPYAEELQaTVNQRVEELkgrltpYADQLQTKIEENVEE 243
Cdd:cd22656 112 LEEAKKTIKALLDDLLKEAKKYQDKAAKV-VDKLTDFENQTEKDQTALE-TLEKALKDL------LTDEGGAIARKEIKD 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 244 LRRslapyaqdvqgKLNHQLEGLAFQMKKHAEELKAKISAKAEELRQGlvplvnsvhgsqlgnaedlqKSLAELSSRLDQ 323
Cdd:cd22656 184 LQK-----------ELEKLNEEYAAKLKAKIDELKALIADDEAKLAAA--------------------LRLIADLTAADT 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528976936 324 QVEDFRRTVGPYGETFNK------AMVQQLDTLRQKLGPLAGDVEDhlSFLEKDLRDKVSSFFNTLKEK 386
Cdd:cd22656 233 DLDNLLALIGPAIPALEKlqgawqAIATDLDSLKDLLEDDISKIPA--AILAKLELEKAIEKWNELAEK 299
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
86-260 |
2.49e-47 |
|
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: 159.74 E-value: 2.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 86 LFQDKLGEVSTYTDDLQKKLVPFATELHERLTKDSEKLKEEIRKELEDLRARLLPHATEVSQKIGDNVRELQQRLGPYAE 165
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 166 ELRTQVDTQAQQLRRQLTPYAERMEKVMRQNLDQLQASLAPYAEELQATVNQRVEELKGRLTPYADQLQTKIEENVEELR 245
Cdd:pfam01442 81 ELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQELR 160
|
170
....*....|....*
gi 528976936 246 RSLAPYAQDVQGKLN 260
Cdd:pfam01442 161 EKLEPQAEDLREKLD 175
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
171-337 |
1.02e-20 |
|
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: 88.47 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 171 VDTQAQQLRRQLTPYAermekvmrqnlDQLQASLAPYAEELQATVNQRVEELKGRLTPYADQLQTKIEENVEELRRSLAP 250
Cdd:pfam01442 9 LSTYAEELQEQLGPVA-----------QELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 251 YAQDVQGKLNHQLEGLAFQMKKHAEELKAKISAKAEELRQGLVPLVNSVHGSQLGNAEDLQKSLA----ELSSRLDQQVE 326
Cdd:pfam01442 78 YTEELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLApyaeEVQAQLSQRLQ 157
|
170
....*....|.
gi 528976936 327 DFRRTVGPYGE 337
Cdd:pfam01442 158 ELREKLEPQAE 168
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
78-190 |
4.14e-12 |
|
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: 64.21 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 78 ELTQQLNTLFQDKLGEVSTYTDDLQKKLVPFATELHERLtkdseklkeeiRKELEDLRARLLPHATEVSQKIGDNVRELQ 157
Cdd:pfam01442 70 ELRQRLEPYTEELRKRLNADAEELQEKLAPYGEELRERL-----------EQNVDALRARLAPYAEELRQKLAERLEELK 138
|
90 100 110
....*....|....*....|....*....|...
gi 528976936 158 QRLGPYAEELRTQVDTQAQQLRRQLTPYAERME 190
Cdd:pfam01442 139 ESLAPYAEEVQAQLSQRLQELREKLEPQAEDLR 171
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
235-390 |
3.63e-11 |
|
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: 61.51 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 235 TKIEENVEELRRSLAPYAQDVQGKLNHQLEGLAFQMKKHAEELKAKISAKAEELRQGLVplvnsvhgsqlGNAEDLQKSL 314
Cdd:pfam01442 7 DELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLG-----------QNVEELRQRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 315 A----ELSSRLDQQVEDFRRTVGPYGETFNKAMVQQLDTLRQKLGPLAGDVEDHLSFLEKDLRDKVSSFFNTLKEKESQA 390
Cdd:pfam01442 76 EpyteELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQR 155
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
67-382 |
1.28e-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: 53.92 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 67 AKKAVEHIQK--SELTQQLNTlFQDKLGEVSTYTDDLQKKLVPFATELhERLTKDSEKLKEEI---RKELEDLRARLLPH 141
Cdd:TIGR02169 714 ASRKIGEIEKeiEQLEQEEEK-LKERLEELEEDLSSLEQEIENVKSEL-KELEARIEELEEDLhklEEALNDLEARLSHS 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 142 ATEVSQKIGDNVRELQQRLGPYAEELrtQVDTQAQQLRRQLTPyAERMEKVMRQNLDQLQ-ASLAPYAEELQATV---NQ 217
Cdd:TIGR02169 792 RIPEIQAELSKLEEEVSRIEARLREI--EQKLNRLTLEKEYLE-KEIQELQEQRIDLKEQiKSIEKEIENLNGKKeelEE 868
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 218 RVEELKGRLTPYADQLQtKIEENVEELRRSLAPyAQDVQGKLNHQLEglafQMKKHAEELKAKISAKAEELRQGLVPLVN 297
Cdd:TIGR02169 869 ELEELEAALRDLESRLG-DLKKERDELEAQLRE-LERKIEELEAQIE----KKRKRLSELKAKLEALEEELSEIEDPKGE 942
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 298 SVH-GSQLGNAEDLQKSLAELSSRLDQQVEDFRRTVGPYGETfnkamVQQLDTLRQKLGPLAGDVEDHLSFLEKDLRDKV 376
Cdd:TIGR02169 943 DEEiPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEV-----LKRLDELKEKRAKLEEERKAILERIEEYEKKKR 1017
|
....*.
gi 528976936 377 SSFFNT 382
Cdd:TIGR02169 1018 EVFMEA 1023
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
87-375 |
9.26e-05 |
|
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: 44.72 E-value: 9.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 87 FQDKLGEVSTYTDDLQKKLVPfATELHER-----------LTKDSEKLKEEiRKELEDLRARLLPHATEVSQKIGDNVRE 155
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNE-SNELHEKqkfylrqsvidLQTKLQEMQME-RDAMADIRRRESQSQEDLRNQLQNTVHE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 156 LQQRlGPYAEELRTQVDTQAQQLRRQLTPYAERMEKVMRQNLDQLQAS-----------------LAPYAEELQATVNQR 218
Cdd:pfam15921 154 LEAA-KCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASgkkiyehdsmstmhfrsLGSAISKILRELDTE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 219 VEELKGRLTPYADQLQTKIEENVEELRRSLAPYAQDVQGKLN-HQLE--GL---AFQMKKHAEELKAKISAKAEELRQGl 292
Cdd:pfam15921 233 ISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISeHEVEitGLtekASSARSQANSIQSQLEIIQEQARNQ- 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 293 vplvNSVHGSQLgnaEDLQKSLAELSSRLDQQvedfRRTVGPYGETFNKAMV------QQLDTLRQKLGPLAGDVEDHLS 366
Cdd:pfam15921 312 ----NSMYMRQL---SDLESTVSQLRSELREA----KRMYEDKIEELEKQLVlanselTEARTERDQFSQESGNLDDQLQ 380
|
....*....
gi 528976936 367 FLEKDLRDK 375
Cdd:pfam15921 381 KLLADLHKR 389
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
78-354 |
6.99e-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: 41.97 E-value: 6.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 78 ELTQQLNTLfQDKLGEVSTYTDDLQKKLVPFATELHE------RLTKDSEKLKEEIRkELEDLRARLLPHATEVSQKIGD 151
Cdd:TIGR02168 695 ELEKALAEL-RKELEELEEELEQLRKELEELSRQISAlrkdlaRLEAEVEQLEERIA-QLSKELTELEAEIEELEERLEE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 152 NVRELQQrlgpyAEELRTQVDTQAQQLRRQLtpyaermeKVMRQNLDQLQASLAPYAEELQaTVNQRVEELKGRltpyAD 231
Cdd:TIGR02168 773 AEEELAE-----AEAEIEELEAQIEQLKEEL--------KALREALDELRAELTLLNEEAA-NLRERLESLERR----IA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 232 QLQTKIEENVEELRRslapyAQDVQGKLNHQLEGLAFQMKKHAEELKA--KISAKAEELRQGLVPLVNSVhGSQLGNAED 309
Cdd:TIGR02168 835 ATERRLEDLEEQIEE-----LSEDIESLAAEIEELEELIEELESELEAllNERASLEEALALLRSELEEL-SEELRELES 908
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 528976936 310 LQKSLAELSSRLDQQVEDFRRTVGpygetfnkAMVQQLDTLRQKL 354
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLE--------GLEVRIDNLQERL 945
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
111-248 |
8.26e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 8.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 111 ELHERLTKDSEKLKEEIRK------ELEDLRARLLPHATEVSQKIG----DNVRELQQRLgPYAEELRTQVDTQAQQLRR 180
Cdd:PRK04863 935 EQFEQLKQDYQQAQQTQRDakqqafALTEVVQRRAHFSYEDAAEMLaknsDLNEKLRQRL-EQAEQERTRAREQLRQAQA 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 181 QLTPYAERMEK------VMRQNLDQLQASLA----PYAEELQATVNQRVEELKGRL------TPYADQLQTKIEENVEEL 244
Cdd:PRK04863 1014 QLAQYNQVLASlkssydAKRQMLQELKQELQdlgvPADSGAEERARARRDELHARLsanrsrRNQLEKQLTFCEAEMDNL 1093
|
....
gi 528976936 245 RRSL 248
Cdd:PRK04863 1094 TKKL 1097
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
105-323 |
8.99e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 8.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 105 LVPFATELHERLTKDSEKLKEEIRKELEDLRARLLPHATEVsQKIGDNVRELQQRLGPYAEELRtQVDTQAQQLRRQLTP 184
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEE-KALLKQLAALERRIAALARRIR-ALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 185 yAERMEKVMRQNLDQLQASLAPYAEELQAtvNQRVEELKGRLTP-----------YADQLQTKIEENVEELRRSLApYAQ 253
Cdd:COG4942 88 -LEKEIAELRAELEAQKEELAELLRALYR--LGRQPPLALLLSPedfldavrrlqYLKYLAPARREQAEELRADLA-ELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 254 DVQGKLNHQLEGLAFQMKKHAEELKAKISAKAEelRQGLVPLVNSVHGSQLGNAEDLQKSLAELSSRLDQ 323
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAE--RQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
117-291 |
1.56e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 40.96 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 117 TKDSEKLKEEIRKELEDLRA---RLLPHATEVSQKIG--DNVRELQqRLGPYAEELRTQVDTQAQQLRRQLTPYAERMEK 191
Cdd:NF041483 322 TKEAEALKAEAEQALADARAeaeKLVAEAAEKARTVAaeDTAAQLA-KAARTAEEVLTKASEDAKATTRAAAEEAERIRR 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 192 VMRQNLDQLQASLAPYAEELQATVNQRVEELKG----------RLTPYADQLQTKIEENVEELRRSLAPYAqdVQgklnh 261
Cdd:NF041483 401 EAEAEADRLRGEAADQAEQLKGAAKDDTKEYRAktvelqeearRLRGEAEQLRAEAVAEGERIRGEARREA--VQ----- 473
|
170 180 190
....*....|....*....|....*....|
gi 528976936 262 QLEGLAfqmkKHAEELKAKISAKAEELRQG 291
Cdd:NF041483 474 QIEEAA----RTAEELLTKAKADADELRST 499
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
121-386 |
1.71e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 40.61 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 121 EKLKEEIRKELedlrarllphaTEVSQKIGdnvreLQQRLGPYAEELrTQVDTQAQQLRRQLtpyAERMEKVM------- 193
Cdd:PLN03229 465 EKLKKEIDLEY-----------TEAVIAMG-----LQERLENLREEF-SKANSQDQLMHPVL---MEKIEKLKdefnkrl 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 194 ---------RQNLDQLQA--------SLAPYAEELQATVNQRVEELKGRltpyadqlqTKIEENVEELRRSLAPYAQDVQ 256
Cdd:PLN03229 525 srapnylslKYKLDMLNEfsrakalsEKKSKAEKLKAEINKKFKEVMDR---------PEIKEKMEALKAEVASSGASSG 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 257 GKLNHQLEGLAFQMKKHAEELKAKIsAKAEELRQGLVPlVNSVHGSQLGNAEDLQKSLAELSSRLDQQVEDFRRTVGPyg 336
Cdd:PLN03229 596 DELDDDLKEKVEKMKKEIELELAGV-LKSMGLEVIGVT-KKNKDTAEQTPPPNLQEKIESLNEEINKKIERVIRSSDL-- 671
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 528976936 337 etfnKAMVQQLDTLRQKLGPLAGDVE-DHLSFLEKDLRDKVSSFFNT--LKEK 386
Cdd:PLN03229 672 ----KSKIELLKLEVAKASKTPDVTEkEKIEALEQQIKQKIAEALNSseLKEK 720
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
76-346 |
2.31e-03 |
|
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: 40.49 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 76 KSELtQQLNTLFQDKLGEvstytddLQKKLVPFATELHE------RLTKDSEKLKEEIRKELEDLRARllphATEVSQKI 149
Cdd:pfam15921 330 RSEL-REAKRMYEDKIEE-------LEKQLVLANSELTEarterdQFSQESGNLDDQLQKLLADLHKR----EKELSLEK 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 150 GDNVRELQQRLGP--YAEELRTQVDTQAQQLRRqLTPYAERMEKVMRQNLDQLQASLAPYAEELQ--ATVNQRVEELKGR 225
Cdd:pfam15921 398 EQNKRLWDRDTGNsiTIDHLRRELDDRNMEVQR-LEALLKAMKSECQGQMERQMAAIQGKNESLEkvSSLTAQLESTKEM 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 226 LTPYADQLQTKiEENVEELRRSLAPYAQDVQGKlNHQLEGLAFQMKKhaeeLKAKISAKAEELRQglvpLVNsvHGSQLG 305
Cdd:pfam15921 477 LRKVVEELTAK-KMTLESSERTVSDLTASLQEK-ERAIEATNAEITK----LRSRVDLKLQELQH----LKN--EGDHLR 544
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 528976936 306 NA----EDLQKSLAE---LSSRLDQQVEDFRRTVGPYGETFNKAMVQQ 346
Cdd:pfam15921 545 NVqtecEALKLQMAEkdkVIEILRQQIENMTQLVGQHGRTAGAMQVEK 592
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
90-397 |
2.75e-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: 40.21 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 90 KLGEVSTYTDDLQKKLVPFATELHERLTKDSEKLKEEIRKELED---LRARLLPHATEVSQKIGDNV------------- 153
Cdd:pfam12128 514 RLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGKVISPellHRTDLDPEVWDGSVGGELNLygvkldlkridvp 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 154 -----------------------RELQQRLGPYAEELRTQVDTQAQQLRRQLTPYAE------RMEKVMRQNLDQLQASL 204
Cdd:pfam12128 594 ewaaseeelrerldkaeealqsaREKQAAAEEQLVQANGELEKASREETFARTALKNarldlrRLFDEKQSEKDKKNKAL 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 205 apyaEELQATVNQRVEELKGRLTPYADQLQTKIEENVE---ELRRSLAPYAQDVQGKLNHQLEGLAFQMKKHAEELKAKI 281
Cdd:pfam12128 674 ----AERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEqkrEARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAEL 749
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 282 SAKAEELRQGLVPLvnsvhGSQLGNAEDLQKSLAELSSRLdQQVEDFRRTVGPYGETFNKAMVQQldtlRQKLGPLAGDV 361
Cdd:pfam12128 750 KALETWYKRDLASL-----GVDPDVIAKLKREIRTLERKI-ERIAVRRQEVLRYFDWYQETWLQR----RPRLATQLSNI 819
|
330 340 350
....*....|....*....|....*....|....*.
gi 528976936 362 EDHLSFLEKDLRDKVSSFFNTLKEKESQAPALPAQE 397
Cdd:pfam12128 820 ERAISELQQQLARLIADTKLRRAKLEMERKASEKQQ 855
|
|
| antiphage_ZorA_2 |
NF033915 |
anti-phage ZorAB system protein ZorA; Proteins of this subfamily are putative H+ channel ... |
111-257 |
3.00e-03 |
|
anti-phage ZorAB system protein ZorA; Proteins of this subfamily are putative H+ channel proteins, but it has been reported that they are also involved in anti-phage defense.
Pssm-ID: 411476 [Multi-domain] Cd Length: 383 Bit Score: 39.36 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 111 ELHER--------LTKDSEKLKEEIRKELEDLRA----RLLPHATEVSQKIGDN-VRELQQRLGPYAEELRTQVDTQAQQ 177
Cdd:NF033915 224 ELHERigdrlqesLNGMSEAMQTALTDALNNIMApaiqTLVSTTSQQSTQVLESlVGNFMDGMTSAGREQGLQMQQAAAD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 178 LRRQLTPYAERMEKVMRQnLDQLQASLAPYAEELQATVNQRVEELKGRltpyADQLQTKIEENVEELRRSLAPYAQDVQG 257
Cdd:NF033915 304 VNAAVSGMSERLNQLFNS-LSEQQGRQMERAQQQSSTFETQLQRLSGS----ANERQAQLEQRFEELMSGLTEQLQTQLG 378
|
|
| FldA |
COG0716 |
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ... |
59-167 |
3.16e-03 |
|
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440480 [Multi-domain] Cd Length: 135 Bit Score: 37.58 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 59 YFSQLGNnAKKAVEHIQKsELTQQLNTLFQDKLGEV-------------STYTDDLQKKLVPFATELHERL--------- 116
Cdd:COG0716 5 YGSTTGN-TEKVAEAIAE-ALGAAGVDLFEIEDADLddledydllilgtPTWAGELPDDWEDFLEELKEDLsgkkvalfg 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 528976936 117 TKDSEKLKE---EIRKELEDLRARLLpHATEVSQKIGDNVRELQQRLGPYAEEL 167
Cdd:COG0716 83 TGDSSGYGDalgELKELLEEKGAKVV-GGYDFEGSKAPDAEDTEERAEEWLKQL 135
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
68-324 |
3.27e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 68 KKAVEHIQKSELTQQLNTLfqDKLGEVSTYTDDLQKKlvpfATELH--ERLTKDSEKLK--EEIRKELEDLR-ARLLPHA 142
Cdd:PTZ00121 1418 KKADEAKKKAEEKKKADEA--KKKAEEAKKADEAKKK----AEEAKkaEEAKKKAEEAKkaDEAKKKAEEAKkADEAKKK 1491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 143 TEVSQKIGDNVRELQQRLGPYAEELRTQVDTQAQQLRRqltpyAERMEKV--MRQNLDQLQASLAPYAEELQATVNQRVE 220
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK-----AEEAKKAdeAKKAEEKKKADELKKAEELKKAEEKKKA 1566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 221 ELKGRltpyADQLQTKIEENVEELRRSLAPYAQDVQGKLNHQLEGLAFQMKKHAEE-LKAKISAKAEELRQGlVPLVNSV 299
Cdd:PTZ00121 1567 EEAKK----AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkIKAEELKKAEEEKKK-VEQLKKK 1641
|
250 260
....*....|....*....|....*
gi 528976936 300 HGSQLGNAEDLQKSLAELSSRLDQQ 324
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAAEE 1666
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
65-296 |
3.28e-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: 39.65 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 65 NNAKKAVEHiQKSELTQQLNTLfQDKLGEVSTYTDDLQKKLVPFATELHErltkdSEKLKEEIRKELEDLRARLlPHATE 144
Cdd:TIGR02168 294 ANEISRLEQ-QKQILRERLANL-ERQLEELEAQLEELESKLDELAEELAE-----LEEKLEELKEELESLEAEL-EELEA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 145 VSQKIGDNVRELQQRLGPYAEELR------TQVDTQAQQLRRQLTPYAERMEKVMRQNLDQLQASLAPYAEELQATVNQR 218
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAqlelqiASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 219 VEELKGRLTPYADQLQT--KIEENVEELRRSLAPYAQDVQgKLNHQLEGLAFQMKKHAEELKA-KISAKAEELRQGLVPL 295
Cdd:TIGR02168 446 EEELEELQEELERLEEAleELREELEEAEQALDAAERELA-QLQARLDSLERLQENLEGFSEGvKALLKNQSGLSGILGV 524
|
.
gi 528976936 296 V 296
Cdd:TIGR02168 525 L 525
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
74-405 |
3.45e-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: 39.56 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 74 IQKSELTQQLNTLFQDKLGEVSTYTDDLqKKLVPFATELheRLTKDSEKlkEEIRKELEDLRARLLPHATEVSQKIGDNV 153
Cdd:COG5185 228 IINIEEALKGFQDPESELEDLAQTSDKL-EKLVEQNTDL--RLEKLGEN--AESSKRLNENANNLIKQFENTKEKIAEYT 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 154 RELQQRLGPYAEELRTQVDTQAQQLRRQLtPYAERMEKVMRQNLDQLQASLAPYAEELQATVNQRVEELKGRLTPyaDQL 233
Cdd:COG5185 303 KSIDIKKATESLEEQLAAAEAEQELEESK-RETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSS--EEL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 234 QtKIEENVEELRRSLAPYAQDVQGKLNHQLEGLAFQMKKHAEELK------AKISAKAEELRQGLVPLVNS----VHGSQ 303
Cdd:COG5185 380 D-SFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEelqrqiEQATSSNEEVSKLLNELISElnkvMREAD 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 304 LGNAEDLQKSLAELSSRLDQQVEDFRRTVgpygetfnKAMVQQLDTLRQKLGPLAGDVEDHLSFLEKDLRDKVSSFFNTL 383
Cdd:COG5185 459 EESQSRLEEAYDEINRSVRSKKEDLNEEL--------TQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFM 530
|
330 340
....*....|....*....|..
gi 528976936 384 KEKEsqaPALPAQEEMPVPLGG 405
Cdd:COG5185 531 RARG---YAHILALENLIPASE 549
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
164-386 |
6.24e-03 |
|
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: 38.12 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 164 AEELRTQVDTQAQQLRRQLTPYAERMEKVmRQNLDQLQASLAPYAEELQaTVNQRVEELkgrltpYADQLQTKIEENVEE 243
Cdd:cd22656 112 LEEAKKTIKALLDDLLKEAKKYQDKAAKV-VDKLTDFENQTEKDQTALE-TLEKALKDL------LTDEGGAIARKEIKD 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 244 LRRslapyaqdvqgKLNHQLEGLAFQMKKHAEELKAKISAKAEELRQGlvplvnsvhgsqlgnaedlqKSLAELSSRLDQ 323
Cdd:cd22656 184 LQK-----------ELEKLNEEYAAKLKAKIDELKALIADDEAKLAAA--------------------LRLIADLTAADT 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528976936 324 QVEDFRRTVGPYGETFNK------AMVQQLDTLRQKLGPLAGDVEDhlSFLEKDLRDKVSSFFNTLKEK 386
Cdd:cd22656 233 DLDNLLALIGPAIPALEKlqgawqAIATDLDSLKDLLEDDISKIPA--AILAKLELEKAIEKWNELAEK 299
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
109-269 |
7.58e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.74 E-value: 7.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 109 ATELHERLTKDSEKLKEEIrKELEDLRARLLPHATEVSQKIGDNVRE-LQQRLG-----PYAEELRTQVDTQAQQLRRQL 182
Cdd:COG4913 704 LEEELDELKGEIGRLEKEL-EQAEEELDELQDRLEAAEDLARLELRAlLEERFAaalgdAVERELRENLEERIDALRARL 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528976936 183 TPYAERMEKVMRQ----------NLDQLQASLAPYAEELQATVNQRVEELKGRLTPYAD--------QLQTKIEENVEEL 244
Cdd:COG4913 783 NRAEEELERAMRAfnrewpaetaDLDADLESLPEYLALLDRLEEDGLPEYEERFKELLNensiefvaDLLSKLRRAIREI 862
|
170 180
....*....|....*....|....*
gi 528976936 245 RRSLAPyaqdvqgkLNHQLEGLAFQ 269
Cdd:COG4913 863 KERIDP--------LNDSLKRIPFG 879
|
|
| |
