|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
55-366 |
1.95e-137 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 395.06 E-value: 1.95e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 55 NEKETMQFLNDRLASYMEKVRQLERENAELECRIQERNQQQDPLVCPAYQAYFRTIEELQQKILCGKSENARLVVQIDNA 134
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 135 KLASDDFRTKYETELSLRQLVEADINSLRRILDELTLCKSDLEAQVESLKEELLCLKQNHEQEVNTLRCQLGD-RLNVEV 213
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDtQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 214 DAAPTVDLNRVLNETRCQYEALVETNRREVEEWYTTQTEELNKQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHELR 293
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160333504 294 NSLENTLTESEARYSSQLSQVQCLITNVESQLGEIRADLERQNQEYQVLLDIRSRLECEINTYRGLLESEDCK 366
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
72-362 |
7.14e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 7.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 72 EKVRQLERENAELEcRIQ----ERNQQQDPLVCPAYQA-----------------YFRTIEELQQKILCGKSENARLVVQ 130
Cdd:TIGR02168 176 ETERKLERTRENLD-RLEdilnELERQLKSLERQAEKAerykelkaelrelelalLVLRLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 131 IDNAKLASDDFRTKYETELSLRQLVEADINSLRRILDELTLCKSDLEAQVESLKEELLCLKQNHEqEVNTLRCQLGDRLn 210
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE-ELEAQLEELESKL- 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 211 vEVDAAPTVDLNRVLNETRCQYEALVETNRREVEEW---------YTTQTEELNKQVVSSSEQLQSCQAEIIELRRTVNA 281
Cdd:TIGR02168 333 -DELAEELAELEEKLEELKEELESLEAELEELEAELeelesrleeLEEQLETLRSKVAQLELQIASLNNEIERLEARLER 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 282 LEIELQAQHELRNSLENTLTESE-ARYSSQLSQVQCLITNVESQLGEIRADLERQNQEYQVLLDIRSRLECEINTYRGLL 360
Cdd:TIGR02168 412 LEDRRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
|
..
gi 160333504 361 ES 362
Cdd:TIGR02168 492 DS 493
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
72-350 |
1.07e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.54 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 72 EKVRQLERENAELECRIQERNQQQDPLVcpayqayfRTIEELQQKILCGKSENARLVVQIDNAKLASDDfrtkyetELSL 151
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQLR--------KELEELSRQISALRKDLARLEAEVEQLEERIAQ-------LSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 152 RQLVEADINSLRRILDELTLCKSDLEAQVESLKEELlclkQNHEQEVNTLRCQLgDRLNVEVDAaptvdlnrvLNETRCQ 231
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI----EQLKEELKALREAL-DELRAELTL---------LNEEAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 232 YEALVETNRREVEEWyTTQTEELNKQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHELRNSLENTLTESEARYSSQL 311
Cdd:TIGR02168 822 LRERLESLERRIAAT-ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
250 260 270
....*....|....*....|....*....|....*....
gi 160333504 312 SQVQclitNVESQLGEIRADLERQNQEyqvLLDIRSRLE 350
Cdd:TIGR02168 901 EELR----ELESKRSELRRELEELREK---LAQLELRLE 932
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
77-353 |
6.20e-08 |
|
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: 6.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 77 LERENAELECRIQERNQQqdplvcpaYQAYFRTIEELQQKILcGKSENARLVVQidnAKLASddfrtkyetelslrqlVE 156
Cdd:TIGR02169 249 LEEELEKLTEEISELEKR--------LEEIEQLLEELNKKIK-DLGEEEQLRVK---EKIGE----------------LE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 157 ADINSLRRILDELTLCKSDLEAQVESLKEELLCLKQNHE------QEVNTLRCQLGDRLNvevdaaptvDLNRVLNETRC 230
Cdd:TIGR02169 301 AEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEelereiEEERKRRDKLTEEYA---------ELKEELEDLRA 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 231 QYEALVETNRREVEEwyttqteelnkqVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHELRNSLENTLTESEAR---Y 307
Cdd:TIGR02169 372 ELEEVDKEFAETRDE------------LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKineL 439
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 160333504 308 SSQLSQVQCLITNVESQLGEIRADLERQNQEYQVLLDIRSRLECEI 353
Cdd:TIGR02169 440 EEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL 485
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
108-367 |
6.78e-08 |
|
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: 54.68 E-value: 6.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 108 RTIEELQQKIlcgksenARLVVQIDNAKLAsddfRTKYETELslrQLVEADINSLRRILDELTLCKSDLEAQVESLKEEL 187
Cdd:TIGR02168 677 REIEELEEKI-------EELEEKIAELEKA----LAELRKEL---EELEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 188 lclkQNHEQEVNTLRCQLGDrlnvevdaaptvdlnrvLNETRCQYEALVETNRREVEEwYTTQTEELNKQVVSSSEQLQS 267
Cdd:TIGR02168 743 ----EQLEERIAQLSKELTE-----------------LEAEIEELEERLEEAEEELAE-AEAEIEELEAQIEQLKEELKA 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 268 CQAEIIELRRTVNALEIELQAQHELRNSLENTLTESEARY---SSQLSQVQCLITNVESQLGEIRADLERQNQEYQVLLD 344
Cdd:TIGR02168 801 LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLedlEEQIEELSEDIESLAAEIEELEELIEELESELEALLN 880
|
250 260
....*....|....*....|...
gi 160333504 345 IRSRLECEINTYRGLLESEDCKL 367
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEEL 903
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
98-335 |
6.89e-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: 54.00 E-value: 6.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 98 LVCPAYQAYFRTIEELQQKIlcgksenARLVVQIDNAKLASDDFRTKYETELSLRQLVEADINSLRRILDELTLCKSDLE 177
Cdd:COG4942 10 LLALAAAAQADAAAEAEAEL-------EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 178 AQVESLKEELLCLKQNHEQEVNTLRCQLG--------DRLNVEVDAAPTVDLNRVLNetrcQYEALVETNRREVEEwYTT 249
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEELAELLRalyrlgrqPPLALLLSPEDFLDAVRRLQ----YLKYLAPARREQAEE-LRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 250 QTEELNKQvvssSEQLQSCQAEIIELRRTVNALEIELQAQHELRNSLENTLTESEARYSSQLSQVQCLITNVESQLGEIR 329
Cdd:COG4942 158 DLAELAAL----RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
....*.
gi 160333504 330 ADLERQ 335
Cdd:COG4942 234 AEAAAA 239
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
57-350 |
1.11e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 57 KETMQFLNDRLASYMEKVRQLEREnaelecriqernqqqdplvcpayqayfrtIEELQQKilcgksenaRLVVQIDNakl 136
Cdd:COG3206 174 RKALEFLEEQLPELRKELEEAEAA-----------------------------LEEFRQK---------NGLVDLSE--- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 137 asddfrtkyETELSLRQLveadinslrrildeltlckSDLEAQVESLKEELlclkqnheQEVNTLRCQLGDRLNVEVDAA 216
Cdd:COG3206 213 ---------EAKLLLQQL-------------------SELESQLAEARAEL--------AEAEARLAALRAQLGSGPDAL 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 217 PTVDLNRVLNETRCQYEALvETNRREVEEWYTtqteELNKQVVSSSEQLQSCQAEI-IELRRTVNALEIELQAQHELRNS 295
Cdd:COG3206 257 PELLQSPVIQQLRAQLAEL-EAELAELSARYT----PNHPDVIALRAQIAALRAQLqQEAQRILASLEAELEALQAREAS 331
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 160333504 296 LENTLTESEARYSSqlsqvqclITNVESQLGEIRADLERQNQEYQVLLdirSRLE 350
Cdd:COG3206 332 LQAQLAQLEARLAE--------LPELEAELRRLEREVEVARELYESLL---QRLE 375
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
65-354 |
2.96e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 65 DRLASYMEKVRQLERENAELECRIQERNQQQDPLV--CPAYQAYFRT------IEELQQKIlcgksenARLVVQIDNAKL 136
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQerREALQRLAEYswdeidVASAEREI-------AELEAELERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 137 ASDDFRTkyetelsLRQLVEAdinsLRRILDELTLCKSDLEAQVESLKEELlclkQNHEQEVNTLRCQLgDRLNVEVDAA 216
Cdd:COG4913 683 SSDDLAA-------LEEQLEE----LEAELEELEEELDELKGEIGRLEKEL----EQAEEELDELQDRL-EAAEDLARLE 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 217 PTVDLnrvlnETRCQyEALVETNRREVEEWYTTQTEELNKQVVSSSEQLQSCQAEIIEL-RRTVNALEIELQAQHE---L 292
Cdd:COG4913 747 LRALL-----EERFA-AALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREwPAETADLDADLESLPEylaL 820
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160333504 293 RNSLENT-LTESEARYSSQLSQvqclitNVESQLGEIRADLERQNQEyqvlldIRSRLEcEIN 354
Cdd:COG4913 821 LDRLEEDgLPEYEERFKELLNE------NSIEFVADLLSKLRRAIRE------IKERID-PLN 870
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
144-361 |
6.24e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 6.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 144 KYETElslRQLVEADINsLRRILDELtlckSDLEAQVESLKEELLC---LKQNHEQEVNTLRCQLGDRLNVEVDAAPTvd 220
Cdd:TIGR02168 174 RKETE---RKLERTREN-LDRLEDIL----NELERQLKSLERQAEKaerYKELKAELRELELALLVLRLEELREELEE-- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 221 LNRVLNETRCQYEALvETNRREVEEwyttQTEELNKQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHELRNSLENTL 300
Cdd:TIGR02168 244 LQEELKEAEEELEEL-TAELQELEE----KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160333504 301 TESEARyssqlsqvqclITNVESQLGEIRADLERQNQEYQVLLDIRSRLECEINTYRGLLE 361
Cdd:TIGR02168 319 EELEAQ-----------LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
63-304 |
7.17e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 7.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 63 LNDRLASYMEKVRQLERENAELECRIQERNQqqdplvcpAYQAYFRTIEELQQKILCGKSENARLVVQIDNAKLASDDF- 141
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEVSELEEEIEELQK--------ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELe 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 142 --RTKYETELSLRQ----LVEADINSLRRILDELTLCKSDLEAQVESLKEELLCLKQN---HEQEVNTLRCQLGdRLNVE 212
Cdd:TIGR02168 330 skLDELAEELAELEekleELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKvaqLELQIASLNNEIE-RLEAR 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 213 VDAApTVDLNRVLNETRCQYEALVETNRREVEEWYTTQTEELNK---QVVSSSEQLQSCQAEIIELRRTVNALEIELQAQ 289
Cdd:TIGR02168 409 LERL-EDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEElqeELERLEEALEELREELEEAEQALDAAERELAQL 487
|
250
....*....|....*
gi 160333504 290 HELRNSLENTLTESE 304
Cdd:TIGR02168 488 QARLDSLERLQENLE 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
56-350 |
8.62e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 8.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 56 EKETMQFLNDRLASYMEKVRQLERENAELECRIQERNQQqdplvcpayqayfrtIEELQQKILCGKSENARLVVQIDNAK 135
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELE---------------LEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 136 LASDDFRTKYETELSLRQLVEADINSLRRILDELTLCKSDLEAQVESLKEELlclkQNHEQEVNTLRCQLGDRLNVEVDA 215
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL----AEAEEALLEAEAELAEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 216 AptvdlnrvlnetrcqyEALVETNRREVEEwyTTQTEELNKQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHELRNS 295
Cdd:COG1196 385 A----------------EELLEALRAAAEL--AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 160333504 296 LENTLTESEARYSSQLSQVQCLIT---NVESQLGEIRADLERQNQEYQVLLDIRSRLE 350
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEeaaLLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
155-340 |
9.87e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 9.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 155 VEADINSLRRILDELTLCKSDLEAQVESLKEELLCLKQN---HEQEVNTLRCQLGDRLNVE-VDAAPTVDLNRVLNET-- 228
Cdd:COG3883 35 AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeAEAEIEERREELGERARALyRSGGSVSYLDVLLGSEsf 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 229 -----RCQY-EALVETNRREVEEwYTTQTEELNKQvvssSEQLQSCQAEIIELRRTVNALEIELQAQHELRNSLENTLTE 302
Cdd:COG3883 115 sdfldRLSAlSKIADADADLLEE-LKADKAELEAK----KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSA 189
|
170 180 190
....*....|....*....|....*....|....*...
gi 160333504 303 SEARYSSQLSQVQCLITNVESQLGEIRADLERQNQEYQ 340
Cdd:COG3883 190 EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
144-350 |
4.78e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 144 KYETELSLRQLVEA--DINSLRRILDELTLCKSDLEAQVESLKEELlclkQNHEQEVNTLRCQLgDRLNVEVDAApTVDL 221
Cdd:COG1196 217 ELKEELKELEAELLllKLRELEAELEELEAELEELEAELEELEAEL----AELEAELEELRLEL-EELELELEEA-QAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 222 NRVLNE-TRCQYEALVETNRREVEEwytTQTEELNKQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHELRNSLENTL 300
Cdd:COG1196 291 YELLAElARLEQDIARLEERRRELE---ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 160333504 301 TESEARYSSQLSQVQcliTNVESQLGEIRADLERQNQEYQVLLDIRSRLE 350
Cdd:COG1196 368 LEAEAELAEAEEELE---ELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
63-357 |
5.62e-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: 48.58 E-value: 5.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 63 LNDRLASYMEKVRQLERENAEL-------ECRIQE-----------RNQQQDplvCPAYQAYF----RTIEELQQKIlcg 120
Cdd:pfam15921 498 VSDLTASLQEKERAIEATNAEItklrsrvDLKLQElqhlknegdhlRNVQTE---CEALKLQMaekdKVIEILRQQI--- 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 121 ksENArlvvqidnAKLASDDFRTKYETELSLRQLvEADINSLRRILDELTLCKS-------DLEAQVESLKEELLCLKQN 193
Cdd:pfam15921 572 --ENM--------TQLVGQHGRTAGAMQVEKAQL-EKEINDRRLELQEFKILKDkkdakirELEARVSDLELEKVKLVNA 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 194 HEQEVNTLR--CQLGDRLNVEVDAAPTvDLNRVLNEtrcqYEALVETNRREVEEWYTTqTEELNKQvvssseqLQSCQAE 271
Cdd:pfam15921 641 GSERLRAVKdiKQERDQLLNEVKTSRN-ELNSLSED----YEVLKRNFRNKSEEMETT-TNKLKMQ-------LKSAQSE 707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 272 IIELRRTVNALEIELQAQHELRNSLENTLTESEARYSSQLSQVQCL---ITNVESQLGEIRADLERQNQEYQVLLDIRSR 348
Cdd:pfam15921 708 LEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLeeaMTNANKEKHFLKEEKNKLSQELSTVATEKNK 787
|
....*....
gi 160333504 349 LECEINTYR 357
Cdd:pfam15921 788 MAGELEVLR 796
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
66-350 |
3.81e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 66 RLASYMEKVRQLERENAELECRIQERNQQQDPLVCPAYQAYfRTIEELQQKILCGKSENARLvvqidnaklasddfrtky 145
Cdd:TIGR02169 703 RLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELE-EDLSSLEQEIENVKSELKEL------------------ 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 146 etelslrqlvEADINSLRRILDELTLCKSDLEAqveSLKEELLCLKQNHEQEVNTLRCQLGDRLNvEVDAaptvDLNRVL 225
Cdd:TIGR02169 764 ----------EARIEELEEDLHKLEEALNDLEA---RLSHSRIPEIQAELSKLEEEVSRIEARLR-EIEQ----KLNRLT 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 226 NEtRCQYEALVETNRREVEEWyTTQTEELNKQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHELRNSLENTLTESEA 305
Cdd:TIGR02169 826 LE-KEYLEKEIQELQEQRIDL-KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELER 903
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 160333504 306 RYSSQLSQVQCLitnvESQLGEIRADLERQNQEYQVLLDIRSRLE 350
Cdd:TIGR02169 904 KIEELEAQIEKK----RKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
59-372 |
4.76e-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: 45.48 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 59 TMQFLNDRLASYMEKVRQLERENaelECRIQERNQQQ--DPLVCPAYQAYFRTIEELQqkilcgKSENARLVVQIDNAKL 136
Cdd:pfam05483 311 TQKALEEDLQIATKTICQLTEEK---EAQMEELNKAKaaHSFVVTEFEATTCSLEELL------RTEQQRLEKNEDQLKI 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 137 ASDDFRTK---YETELSLRQLVEADINSLRRILDE---LTLCKSDLEAQVESLK---EELLCLKQNHEQEVNTLRCQLgd 207
Cdd:pfam05483 382 ITMELQKKsseLEEMTKFKNNKEVELEELKKILAEdekLLDEKKQFEKIAEELKgkeQELIFLLQAREKEIHDLEIQL-- 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 208 rlnvevdaaptvdlnrvlnetrcqyealveTNRREVEEWYTTQTE----ELNKQVVSSSEQLQSCQAEIIE---LRRTVN 280
Cdd:pfam05483 460 ------------------------------TAIKTSEEHYLKEVEdlktELEKEKLKNIELTAHCDKLLLEnkeLTQEAS 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 281 ALEIELQAQHELRNSLEntltESEARYSSQLSQVQCLITNVESQLGEIRADLERQNQEYQVLLDiRSRLECEINTYRGLL 360
Cdd:pfam05483 510 DMTLELKKHQEDIINCK----KQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLD-KSEENARSIEYEVLK 584
|
330
....*....|..
gi 160333504 361 ESEDCKLPCNPC 372
Cdd:pfam05483 585 KEKQMKILENKC 596
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
67-367 |
7.22e-05 |
|
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: 45.01 E-value: 7.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 67 LASYMEKVRQLERENAELEcriQERNQQQDplvcpayqayfrTIEELQQKILCGKSENARLVVQIDNAKlasdDFRTKYE 146
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELK---KQNNQLKD------------NIEKKQQEINEKTTEISNTQTQLNQLK----DEQNKIK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 147 TELSLRQLveaDINSLRRILDELtlcksdlEAQVESLKEELLCLKQNHEQEVN-TLRCQLGDRLNVEVDAAPTVDLNRV- 224
Cdd:TIGR04523 267 KQLSEKQK---ELEQNNKKIKEL-------EKQLNQLKSEISDLNNQKEQDWNkELKSELKNQEKKLEEIQNQISQNNKi 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 225 ---LNETRCQYEALVETNRREVEEwYTTQTEELNKQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHELRNSLENTLT 301
Cdd:TIGR04523 337 isqLNEQISQLKKELTNSESENSE-KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIK 415
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 302 ESEARYSSQLSQVQCLITNVESQLGEIRaDLERQNQE----YQVLLDIRSRLECEINTYRGLLESEDCKL 367
Cdd:TIGR04523 416 KLQQEKELLEKEIERLKETIIKNNSEIK-DLTNQDSVkeliIKNLDNTRESLETQLKVLSRSINKIKQNL 484
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
56-337 |
7.94e-05 |
|
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: 45.17 E-value: 7.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 56 EKETMQFLNDRLASYMEKVRQLERENAELECRIQ----ERNQQQDPLvcPAYQAYFRTIEELQQKILCGKSEnARLVVQI 131
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQqlceEKNALQEQL--QAETELCAEAEEMRARLAARKQE-LEEILHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 132 DNAKLASDDFRTKYETelSLRQLVEADINSLRRILDE-------LTLCKSDLEAQVESLKEELLCLkQNHEQEVNTLRCQ 204
Cdd:pfam01576 80 LESRLEEEEERSQQLQ--NEKKKMQQHIQDLEEQLDEeeaarqkLQLEKVTTEAKIKKLEEDILLL-EDQNSKLSKERKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 205 LGDRLN-VEVDAAPTVDLNRVLNETRCQYEALV----------ETNRREVEEWyttqTEELNKQVVSSSEQLQSCQAEII 273
Cdd:pfam01576 157 LEERISeFTSNLAEEEEKAKSLSKLKNKHEAMIsdleerlkkeEKGRQELEKA----KRKLEGESTDLQEQIAELQAQIA 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160333504 274 ELRRTVNALEIELQAqhelrnslenTLTESEARySSQLSQVQCLITNVESQLGEIRADLERQNQ 337
Cdd:pfam01576 233 ELRAQLAKKEEELQA----------ALARLEEE-TAQKNNALKKIRELEAQISELQEDLESERA 285
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
53-333 |
8.37e-05 |
|
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: 44.63 E-value: 8.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 53 NGNEKETMQFLNDRLASYMEKVRQLERENAELECRIQERNQQqdplvcpaYQAYFRTIEELQQKILCGKSENARLVVQID 132
Cdd:TIGR04523 379 NQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQE--------KELLEKEIERLKETIIKNNSEIKDLTNQDS 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 133 NAKLA---SDDFRTKYETELSLrqlVEADINSLRRILD--------------ELTLCKSDLEAQVESLKEELLCLKQNhE 195
Cdd:TIGR04523 451 VKELIiknLDNTRESLETQLKV---LSRSINKIKQNLEqkqkelkskekelkKLNEEKKELEEKVKDLTKKISSLKEK-I 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 196 QEVNTLRCQLGDRLnvevdaaptVDLNRVLNE-----TRCQYEALVETNRREVEEWYTTQTEELNKQvVSSSEQLQSCQA 270
Cdd:TIGR04523 527 EKLESEKKEKESKI---------SDLEDELNKddfelKKENLEKEIDEKNKEIEELKQTQKSLKKKQ-EEKQELIDQKEK 596
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160333504 271 EIIELRRtvnaleiELQAQHELRNSLENTLTESEARYsSQLSQvqcLITNVESQLGEIRADLE 333
Cdd:TIGR04523 597 EKKDLIK-------EIEEKEKKISSLEKELEKAKKEN-EKLSS---IIKNIKSKKNKLKQEVK 648
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
56-342 |
8.68e-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: 8.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 56 EKETMQFLNDRLASYMEKVRQLEREnaelecrIQERNQQQDPLvcpayQAYFRTIEELQQkilcGKSENARLVVQIDNAK 135
Cdd:pfam15921 396 EKEQNKRLWDRDTGNSITIDHLRRE-------LDDRNMEVQRL-----EALLKAMKSECQ----GQMERQMAAIQGKNES 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 136 LasddfrtkyETELSLRQLVEADINSLRRILDELTLCKSDLEAQVESLKEELLCLKQNHE--QEVNTLRCQLGDRLNVEV 213
Cdd:pfam15921 460 L---------EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERaiEATNAEITKLRSRVDLKL 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 214 DaaptvDLNRVLNE--------TRCQYEALVETNRREVEEWYTTQTEELNKQVVSSSEQLQSCQAEIIELRRTVNALEIE 285
Cdd:pfam15921 531 Q-----ELQHLKNEgdhlrnvqTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLE 605
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160333504 286 LQAQHELRNSLENTLTESEARYSS-QLSQVQclITNVESQ---------------LGEI---RADLERQNQEYQVL 342
Cdd:pfam15921 606 LQEFKILKDKKDAKIRELEARVSDlELEKVK--LVNAGSErlravkdikqerdqlLNEVktsRNELNSLSEDYEVL 679
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
153-338 |
1.13e-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: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 153 QLVEADINSLRRILDELTLCKSDLEAQVESLKEELlclkQNHEQEVNTLRCQLgDRLNVEVDAAptvdlnrvlnetrcqy 232
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARL----EAAKTELEDLEKEI-KRLELEIEEV---------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 233 EALVETNRREVEEwyttqteelnkqvVSSSEQLQSCQAEIIELRRTVNALEIELQAQHELRNSLENTLTESEARYSSQLS 312
Cdd:COG1579 72 EARIKKYEEQLGN-------------VRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA 138
|
170 180
....*....|....*....|....*.
gi 160333504 313 QVQCLITNVESQLGEIRADLERQNQE 338
Cdd:COG1579 139 ELEEKKAELDEELAELEAELEELEAE 164
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
252-364 |
1.24e-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: 43.98 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 252 EELNKQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHELRNSLENTLTESEARyssqlsqvqclITNVESQLGEIRAD 331
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE-----------LAELEKEIAELRAE 98
|
90 100 110
....*....|....*....|....*....|...
gi 160333504 332 LERQNQEYQVLLDIRSRLEcEINTYRGLLESED 364
Cdd:COG4942 99 LEAQKEELAELLRALYRLG-RQPPLALLLSPED 130
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
221-332 |
1.27e-04 |
|
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: 44.34 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 221 LNRVLNETRCQYEALvETNRREVEEWYTTQTEELNKQVVSSSEQLQSCQAE---IIELRRTvnaleiELQAQHELRNSLE 297
Cdd:pfam15921 76 IERVLEEYSHQVKDL-QRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMErdaMADIRRR------ESQSQEDLRNQLQ 148
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 160333504 298 NTLTESEA----------RYSSQLSQVQCLITNVESQLGEIRADL 332
Cdd:pfam15921 149 NTVHELEAakclkedmleDSNTQIEQLRKMMLSHEGVLQEIRSIL 193
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
108-344 |
1.49e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.12 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 108 RTIEELQQKILCGKSENARLVVQIDNAKLASDDFR-TKYETE-----LSLRQLVEADINSLRRIldeLTLCKSDLEAqVE 181
Cdd:PLN02939 81 RTVMELPQKSTSSDDDHNRASMQRDEAIAAIDNEQqTNSKDGeqlsdFQLEDLVGMIQNAEKNI---LLLNQARLQA-LE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 182 SLkEELLCLKQNHEQEVNTLRCQL---GDRLNVEVDAAPTVDLNRVLNETRCQYEALVETNRREVEEWYTTQTEELNKQV 258
Cdd:PLN02939 157 DL-EKILTEKEALQGKINILEMRLsetDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEEN 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 259 VSSSEQLQSCQAEIIELRRTVNALeIELQAQHELrnsLENTLTESEARYS------SQLS--QVQCLITNVESqLGEIRA 330
Cdd:PLN02939 236 MLLKDDIQFLKAELIEVAETEERV-FKLEKERSL---LDASLRELESKFIvaqedvSKLSplQYDCWWEKVEN-LQDLLD 310
|
250
....*....|....
gi 160333504 331 DLERQNQEYQVLLD 344
Cdd:PLN02939 311 RATNQVEKAALVLD 324
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
65-338 |
1.71e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 65 DRLASYMEKVRQLERENAELECRIQERNQQQDPLVCPAYQAyfRTIEELQQK--ILCGKSENARLVVQIDNAKLAS---- 138
Cdd:PRK02224 468 ETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAE--DRIERLEERreDLEELIAERRETIEEKRERAEElrer 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 139 -DDFRTKYETELSLRQLVEADINSLRRILDELTLCKSDLEAQVESLK--EELLCLKQNHEQEVNTLRCQLGDRLNVEVDA 215
Cdd:PRK02224 546 aAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLEriRTLLAAIADAEDEIERLREKREALAELNDER 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 216 APTVDLNRvlnETRCQYEALVETNRREVEEWYTTQTEELNKQVvssSEQLQSCQAEIIELRRTVNALEIELQAQHELRN- 294
Cdd:PRK02224 626 RERLAEKR---ERKRELEAEFDEARIEEAREDKERAEEYLEQV---EEKLDELREERDDLQAEIGAVENELEELEELREr 699
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 160333504 295 --SLENTLTESEARYSSqlsqvqclITNVESQLGEIRADLERQNQE 338
Cdd:PRK02224 700 reALENRVEALEALYDE--------AEELESMYGDLRAELRQRNVE 737
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
166-333 |
2.05e-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: 41.87 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 166 LDELTLCKSDLEAQVESLKEELlclKQNHEQEVNTLRCQLGDRLN-VEVDAAPTVD-LNRVLNETRCQYEALVETNRREV 243
Cdd:pfam01442 6 LDELSTYAEELQEQLGPVAQEL---VDRLEKETEALRERLQKDLEeVRAKLEPYLEeLQAKLGQNVEELRQRLEPYTEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 244 EEWYTTQTEELNKQVVSSSEQLQS-CQAEIIELRRTVNALEIELQA---QH--ELRNSLENTLTESEARYSSQLSQVQcl 317
Cdd:pfam01442 83 RKRLNADAEELQEKLAPYGEELRErLEQNVDALRARLAPYAEELRQklaERleELKESLAPYAEEVQAQLSQRLQELR-- 160
|
170
....*....|....*.
gi 160333504 318 iTNVESQLGEIRADLE 333
Cdd:pfam01442 161 -EKLEPQAEDLREKLD 175
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
56-364 |
5.08e-04 |
|
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: 42.25 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 56 EKETMQFLNDRLASYMEKVRQLE----RENAELECRIQERNQQQDPLVcpayqayFRTIEELQQKIlcgKSENARLVVQI 131
Cdd:COG5185 244 ELEDLAQTSDKLEKLVEQNTDLRleklGENAESSKRLNENANNLIKQF-------ENTKEKIAEYT---KSIDIKKATES 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 132 DNAKLASDDFRTKYEtelslrQLVEADINSLRRILDELTLCKSDLEAQVESLKEELLCLKQnhEQEVNTLRCQLGDrLNV 211
Cdd:COG5185 314 LEEQLAAAEAEQELE------ESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVG--EVELSKSSEELDS-FKD 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 212 EVDAAPTVDLNRVLNETRCQYEAL--VETNRREVEEwyttQTEELNKQVVSSSEQLQSCQAEIIEL-----RRTVNALEI 284
Cdd:COG5185 385 TIESTKESLDEIPQNQRGYAQEILatLEDTLKAADR----QIEELQRQIEQATSSNEEVSKLLNELiselnKVMREADEE 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 285 ELQAQHELRNSLENTLTESEARYSSQLSQVQCLITNVESQLGEIRADLERQNQEYQVLLDIRSRLECEINTYRGLLESED 364
Cdd:COG5185 461 SQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILA 540
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
132-350 |
6.12e-04 |
|
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: 42.08 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 132 DNAKLASDDFRTKYETELSLRQLvEADINSLRRILDELTLCKSDLEAQVESLKEELLCLKQNHEQEVNTLRCQLGDRLNV 211
Cdd:pfam01576 472 DTQELLQEETRQKLNLSTRLRQL-EDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRL 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 212 EVDAAptvDLNRVLNETRCQYEALVETNRREVEEWY-TTQTEELNKQVVSSSEQLQ-------------SCQ-------- 269
Cdd:pfam01576 551 QRELE---ALTQQLEEKAAAYDKLEKTKNRLQQELDdLLVDLDHQRQLVSNLEKKQkkfdqmlaeekaiSARyaeerdra 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 270 -AEIIELRRTVNALEIELQAQHELRNSLENTLTESEARYSSQLSQVQCLITNV----------ESQLGEIRADLERQNQE 338
Cdd:pfam01576 628 eAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVhelerskralEQQVEEMKTQLEELEDE 707
|
250
....*....|..
gi 160333504 339 YQVLLDIRSRLE 350
Cdd:pfam01576 708 LQATEDAKLRLE 719
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
156-362 |
6.75e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 156 EADINSLRRILDELTLCKSDLEAQVESLKEELlclkQNHEQEVNTLRCQLgDRLNVEVDAAptvdlnrvlnetrcqyEAL 235
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAEL----EELNEEYNELQAEL-EALQAEIDKL----------------QAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 236 VETNRREVEEwyttQTEELNKQVVSSseQLQSCQAEIIE-----------LRRtVNALEIELQAQHELRNSLENTLTESE 304
Cdd:COG3883 74 IAEAEAEIEE----RREELGERARAL--YRSGGSVSYLDvllgsesfsdfLDR-LSALSKIADADADLLEELKADKAELE 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 160333504 305 ArYSSQLSQVQCLITNVESQLGEIRADLERQNQEYQVLLDirsRLECEINTYRGLLES 362
Cdd:COG3883 147 A-KKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLA---QLSAEEAAAEAQLAE 200
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
101-298 |
9.43e-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: 40.77 E-value: 9.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 101 PAYQAYFRTIEELQQKILCGKSENARLVVQI--DNAKL------ASDDFRTKYETELSL-----RQLVEAD--------I 159
Cdd:smart00787 63 PLLELYQFSCKELKKYISEGRDLFKEIEEETliNNPPLfkeyfsASPDVKLLMDKQFQLvktfaRLEAKKMwyewrmklL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 160 NSLRRILDE-LTLCKSDLE------AQVESLKEELLCLKQNHEQEVNTLRcqlgdRLNVEVDAAPTVDLNRVLNETRCQY 232
Cdd:smart00787 143 EGLKEGLDEnLEGLKEDYKllmkelELLNSIKPKLRDRKDALEEELRQLK-----QLEDELEDCDPTELDRAKEKLKKLL 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160333504 233 EALVEtNRREVEEwYTTQTEELNKQVVSSSEQLQSCQAEIIELRRTVN------ALEIE-LQAQHELRNSLEN 298
Cdd:smart00787 218 QEIMI-KVKKLEE-LEEELQELESKIEDLTNKKSELNTEIAEAEKKLEqcrgftFKEIEkLKEQLKLLQSLTG 288
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
81-262 |
1.12e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.51 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 81 NAELECRIQERNQQQDPLvcpayQAYFRTIEELQQKILcgkSENARLVVQIDNAKLASDDFRTKYETELSLRQLVEADIN 160
Cdd:pfam09787 46 TLELEELRQERDLLREEI-----QKLRGQIQQLRTELQ---ELEAQQQEEAESSREQLQELEEQLATERSARREAEAELE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 161 SL----RRILDELTLCKS-------DLEAQVESLKEELLCLKQNheqevNTLRCQLGDRLnvevdaaptvdlnRVLNETR 229
Cdd:pfam09787 118 RLqeelRYLEEELRRSKAtlqsrikDREAEIEKLRNQLTSKSQS-----SSSQSELENRL-------------HQLTETL 179
|
170 180 190
....*....|....*....|....*....|...
gi 160333504 230 CQYEALVETNRREVEEwYTTQTEELNKQVVSSS 262
Cdd:pfam09787 180 IQKQTMLEALSTEKNS-LVLQLERMEQQIKELQ 211
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
121-356 |
1.65e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 121 KSENARLVVQIDNAKlasDDFRTKYETELSLRQLVEADINSLRRILDELTLCKSDLEAQVESLKEELlclkqnheqevnt 200
Cdd:PHA02562 180 NQQIQTLDMKIDHIQ---QQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDEL------------- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 201 lrcqlgdrLNVEVDAA-PTVDLNRvLNETRCQYEALVETNRREvEEWY---------TTQTEELNKQVVSSSEQLQSCQA 270
Cdd:PHA02562 244 --------LNLVMDIEdPSAALNK-LNTAAAKIKSKIEQFQKV-IKMYekggvcptcTQQISEGPDRITKIKDKLKELQH 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 271 EIIEL---RRTVNALEIELQAQ----HELRNSLEnTLTESEARYSSQLSQVQCLITNVESQLGEIRADLERQNQEYQVLL 343
Cdd:PHA02562 314 SLEKLdtaIDELEEIMDEFNEQskklLELKNKIS-TNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIV 392
|
250
....*....|...
gi 160333504 344 DIRSRLECEINTY 356
Cdd:PHA02562 393 KTKSELVKEKYHR 405
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
159-357 |
2.14e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 159 INSLRRILDELTLCKSDLEAQVESLKEELlclkQNHEQEVNTLRcQLGDRLNVEVDAAPTVdlnRVLNETRCQYEALVET 238
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAEL----DALQERREALQ-RLAEYSWDEIDVASAE---REIAELEAELERLDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 239 NrreveewytTQTEELNKQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHELRNSLENTLTESEARYSSQLSQV---Q 315
Cdd:COG4913 684 S---------DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALleeR 754
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 160333504 316 CLITNVESQLGEIRADLERQNQEYQVLLD-IRSRLECEINTYR 357
Cdd:COG4913 755 FAAALGDAVERELRENLEERIDALRARLNrAEEELERAMRAFN 797
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
63-281 |
2.27e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 63 LNDRLASYMEKVRQLERENAELECRIQERNQQqdplvcpayqayfrtIEELQQKILCGKSENARLVV------QIDNAK- 135
Cdd:COG4942 60 LERRIAALARRIRALEQELAALEAELAELEKE---------------IAELRAELEAQKEELAELLRalyrlgRQPPLAl 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 136 -LASDDFRTKYETELSLRQLVEAD---INSLRRILDELTlcksDLEAQVESLKEELLCLKQNHEQEVNTLRCQLGDRlnv 211
Cdd:COG4942 125 lLSPEDFLDAVRRLQYLKYLAPARreqAEELRADLAELA----ALRAELEAERAELEALLAELEEERAALEALKAER--- 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 212 evdaaptvdlnrvlnetrcqyEALVETNRREVEEwYTTQTEELNKQVVSSSEQLQSCQAEIIELRRTVNA 281
Cdd:COG4942 198 ---------------------QKLLARLEKELAE-LAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
176-362 |
2.47e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 176 LEAQVESLKEELlclkQNHEQEVNTLRCQ-----LGDRLNVEVDAapTVDLNRVLNETRCQYEALvETNRREVEEWYTTQ 250
Cdd:COG3206 180 LEEQLPELRKEL----EEAEAALEEFRQKnglvdLSEEAKLLLQQ--LSELESQLAEARAELAEA-EARLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 251 TEELNKqvVSSSEQLQSCQAEIIELRRTVNALEIELQAQH----ELRNSLENTLTESEARYSSQLSQVQCLITNVESQLg 326
Cdd:COG3206 253 PDALPE--LLQSPVIQQLRAQLAELEAELAELSARYTPNHpdviALRAQIAALRAQLQQEAQRILASLEAELEALQARE- 329
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 160333504 327 eirADLERQ----NQEYQVLLDIR---SRLECEINTYRGLLES 362
Cdd:COG3206 330 ---ASLQAQlaqlEARLAELPELEaelRRLEREVEVARELYES 369
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
56-363 |
2.57e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 56 EKETMQFLNDRLASYMEKVRQLERENAELECRIQERNQQQDPLVcpayqayfRTIEELQQKI-----LCGKSENARLVVq 130
Cdd:PRK03918 229 EVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK--------KEIEELEEKVkelkeLKEKAEEYIKLS- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 131 idnaKLASDDFRTKYETELSLRQLvEADINSLRRILDELTLCKS---DLEAQVESLKEELLCLKQNHE--QEVNTLRCQL 205
Cdd:PRK03918 300 ----EFYEEYLDELREIEKRLSRL-EEEINGIEERIKELEEKEErleELKKKLKELEKRLEELEERHElyEEAKAKKEEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 206 gDRLNVEVDAAPTVDLNRVLNEtrcqyealVETNRREVEEWYTTQTEELN------KQVVSSSEQLQS-------CQAEI 272
Cdd:PRK03918 375 -ERLKKRLTGLTPEKLEKELEE--------LEKAKEEIEEEISKITARIGelkkeiKELKKAIEELKKakgkcpvCGREL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 273 IE---------LRRTVNALEIELQAQHELRNSLENTLTE-----SEARYSSQLSQVQCLITNVESQLGEIRA-DLERQNQ 337
Cdd:PRK03918 446 TEehrkelleeYTAELKRIEKELKEIEEKERKLRKELRElekvlKKESELIKLKELAEQLKELEEKLKKYNLeELEKKAE 525
|
330 340
....*....|....*....|....*.
gi 160333504 338 EYQVLLDIRSRLECEINTYRGLLESE 363
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIKSLKKELEKL 551
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
152-335 |
2.66e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 152 RQLVEADINSLRRILDELTLCKSDLEAQVESLKEELLCLKQNHEQevntlrcQLGDRLNvevdaaptvdlnrvlnetrcQ 231
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG-------NGGDRLE--------------------Q 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 232 YEALVETNRREVEEW------YTTQTEELNKQVVSSSEQLQSCQAeiiELRRTVNALEIELQAQHELRNSLENTLTESEA 305
Cdd:COG4913 343 LEREIERLERELEERerrrarLEALLAALGLPLPASAEEFAALRA---EAAALLEALEEELEALEEALAEAEAALRDLRR 419
|
170 180 190
....*....|....*....|....*....|...
gi 160333504 306 RY---SSQLSQVQCLITNVESQLGEIRADLERQ 335
Cdd:COG4913 420 ELrelEAEIASLERRKSNIPARLLALRDALAEA 452
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
71-366 |
2.87e-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: 40.16 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 71 MEKV-RQLERENAELECRIQERNQQqdplVCPAYQAYFRTIEELQQKILCGKSENARlvvqidnaklasddfrtKYETEL 149
Cdd:pfam01576 206 LEKAkRKLEGESTDLQEQIAELQAQ----IAELRAQLAKKEEELQAALARLEEETAQ-----------------KNNALK 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 150 SLRQLvEADINSLRRILDELTLCKSDLEAQVESLKEELLCLKQNHEQEVNTLRCQLGDRLNVEVDAAptvDLNRVLNETR 229
Cdd:pfam01576 265 KIREL-EAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVT---ELKKALEEET 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 230 CQYEALVETNRREveewYTTQTEELNkqvvsssEQLQSCQAEIIELRRTVNALEIE-LQAQHELRnSLENTLTESEARYS 308
Cdd:pfam01576 341 RSHEAQLQEMRQK----HTQALEELT-------EQLEQAKRNKANLEKAKQALESEnAELQAELR-TLQQAKQDSEHKRK 408
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160333504 309 SQlsqvqclitnvESQLGEIRA---DLERQNQEyqvLLDIRSRLECEINTYRGLLESEDCK 366
Cdd:pfam01576 409 KL-----------EGQLQELQArlsESERQRAE---LAEKLSKLQSELESVSSLLNEAEGK 455
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
143-350 |
3.14e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 143 TKY-----ETELSLRQlVEADINSLRRILDELtlcksdlEAQVESLKEEllclkqnheqevntlrcqlgdrlnVEVdAAP 217
Cdd:COG1196 168 SKYkerkeEAERKLEA-TEENLERLEDILGEL-------ERQLEPLERQ------------------------AEK-AER 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 218 TVDLNRVLNETRCQYEALVETNRREVEEWYTTQTEELNKQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHELRNSLE 297
Cdd:COG1196 215 YRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 160333504 298 NTLTESEARYSSQLSQVQCLITNVESQLGEIRADLERQNQEYQVLLDIRSRLE 350
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE 347
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
223-357 |
3.21e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.61 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 223 RVLNETrcqYEALVETNRREVEEWYTTQTEELNKQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHELR--NSLENTL 300
Cdd:COG3206 152 AVANAL---AEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQqlSELESQL 228
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 160333504 301 TESEAryssQLSQVQCLITNVESQLGEIRADLER--QNQEYQVLLDIRSRLECEINTYR 357
Cdd:COG3206 229 AEARA----ELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELS 283
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
176-339 |
3.30e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 38.97 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 176 LEAQVESLKEELLCLKQNHEQEVNTLRCQLGDRLNvevdaaptvdlnRVLNETRCQYEALVETNRREVEEWYTTqtEELN 255
Cdd:pfam09787 66 LRGQIQQLRTELQELEAQQQEEAESSREQLQELEE------------QLATERSARREAEAELERLQEELRYLE--EELR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 256 KQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHELRNSLEnTLTESearyssqLSQVQCLITNVESQLGEIRADLERQ 335
Cdd:pfam09787 132 RSKATLQSRIKDREAEIEKLRNQLTSKSQSSSSQSELENRLH-QLTET-------LIQKQTMLEALSTEKNSLVLQLERM 203
|
....
gi 160333504 336 NQEY 339
Cdd:pfam09787 204 EQQI 207
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
195-348 |
3.91e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.12 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 195 EQEVNTLRCQLgDRLNVEVDAaptvdLNRVLNETRCQYEALVEtnrrEVEEWyTTQTEELNKQVVSSSEQLQSCQAEIIE 274
Cdd:COG4372 44 QEELEQLREEL-EQAREELEQ-----LEEELEQARSELEQLEE----ELEEL-NEQLQAAQAELAQAQEELESLQEEAEE 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160333504 275 LRRTVNALEIELQAQHELRNSLENTLTESEARYSSQLSQVQclitNVESQLGEIRADLERQNQEYQVLLDIRSR 348
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK----ELEEQLESLQEELAALEQELQALSEAEAE 182
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
239-361 |
4.16e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 239 NRREVEEWY-----TTQTEELNKQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHELRN---------SLENTLTESE 304
Cdd:COG4913 595 RRRIRSRYVlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeidvaSAEREIAELE 674
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 160333504 305 ARYSsQLSQVQCLITNVESQLGEIRADLERQNQEYQVLLDIRSRLECEINTYRGLLE 361
Cdd:COG4913 675 AELE-RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
146-334 |
4.26e-03 |
|
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: 39.07 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 146 ETELSLRQLVEADINSLRRILDELtlcksdlEAQVESLKEELLCLKQN---HEQEVNTLRcQLGDRLNvEVDAAPTVDLN 222
Cdd:pfam06160 280 EKEVDAKKYVEKNLPEIEDYLEHA-------EEQNKELKEELERVQQSytlNENELERVR-GLEKQLE-ELEKRYDEIVE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 223 RVLNETRCqYEALVEtnrrEVEEWYTtQTEELNKQVVSSSEQLQS-------CQAEIIELRRTVNALEIELQAQH--ELR 293
Cdd:pfam06160 351 RLEEKEVA-YSELQE----ELEEILE-QLEEIEEEQEEFKESLQSlrkdeleAREKLDEFKLELREIKRLVEKSNlpGLP 424
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 160333504 294 NSLENTLTESEARYSS---QLSQVQCLITNVESQLGEIRADLER 334
Cdd:pfam06160 425 ESYLDYFFDVSDEIEDladELNEVPLNMDEVNRLLDEAQDDVDT 468
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
163-362 |
4.41e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.28 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 163 RRILDELTLCkSDLEAQVESLKEELLCLKQNHEQ---EVNTLRCQLgDRLNVEVDAAPTVD-LNRVLNETRcQYEALVET 238
Cdd:TIGR02169 156 RKIIDEIAGV-AEFDRKKEKALEELEEVEENIERldlIIDEKRQQL-ERLRREREKAERYQaLLKEKREYE-GYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 239 NRREveewytTQTEELNKQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQhelrNSLENTLTESEARyssqlsQVQCLI 318
Cdd:TIGR02169 233 EALE------RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL----NKKIKDLGEEEQL------RVKEKI 296
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 160333504 319 TNVESQLGEIRADLERQNQEYQVLLDIRSRLECEINTYRGLLES 362
Cdd:TIGR02169 297 GELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE 340
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
54-357 |
4.52e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.50 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 54 GNEKETMQFLNDRLASYMEKVRQLE------RENAELECRIQERNQQQDPLVC--PAYQAYFRTIEELQQKIlcgksENA 125
Cdd:PRK01156 308 ENKKQILSNIDAEINKYHAIIKKLSvlqkdyNDYIKKKSRYDDLNNQILELEGyeMDYNSYLKSIESLKKKI-----EEY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 126 RlvvqIDNAKLASDDFRTKYETELSLRQLVeADINSLRRILDELTLCKSDLEAQVESLKEELLCLKQNHEQEVNTLRC-- 203
Cdd:PRK01156 383 S----KNIERMSAFISEILKIQEIDPDAIK-KELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCpv 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 204 ---QLGDRLNVEVDAAPTVDLNRV---LNETRCQYEALVETNRREVEEWYTTQTEELNKqVVSSSEQLQSCQAEIIELRR 277
Cdd:PRK01156 458 cgtTLGEEKSNHIINHYNEKKSRLeekIREIEIEVKDIDEKIVDLKKRKEYLESEEINK-SINEYNKIESARADLEDIKI 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 278 TVNALEIELQAQHELRNSLENT-LTESEARYSSQL---SQVQCL-ITNVESQLGEIRA---DLERQNQEYQV-LLDIRS- 347
Cdd:PRK01156 537 KINELKDKHDKYEEIKNRYKSLkLEDLDSKRTSWLnalAVISLIdIETNRSRSNEIKKqlnDLESRLQEIEIgFPDDKSy 616
|
330
....*....|....*.
gi 160333504 348 ------RLECEINTYR 357
Cdd:PRK01156 617 idksirEIENEANNLN 632
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
146-306 |
5.11e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 146 ETELSLRQLVEADINSLRRILDELTLCKSDLEAQVESLKEELLCLKQNHE-QEVNTLRCQLGDRLNVEVDAAPTVDLN-R 223
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQlLPLYQELEALEAELAELPERLEELEERlE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 224 VLNETRCQYEAL---VETNRREVEEWYTTQTEELNKQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHELRNSLENTL 300
Cdd:COG4717 157 ELRELEEELEELeaeLAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
....*.
gi 160333504 301 TESEAR 306
Cdd:COG4717 237 EAAALE 242
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
61-360 |
6.27e-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: 38.79 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 61 QFLNDRLASY-MEKVRQLE-RENAELECRIQERNQQQDPLVCPAYQAYFRTIEELQQKILCGKSENARLVVQIdNAKLAS 138
Cdd:COG5185 211 ETGNLGSESTlLEKAKEIInIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNEN-ANNLIK 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 139 DDFRTKYE-TELSLRQLVEADINSLRRILDELTLCKSdLEAQVESLKEELLCLKQNHEQEVNTLRCQLgDRLNVEVDAAP 217
Cdd:COG5185 290 QFENTKEKiAEYTKSIDIKKATESLEEQLAAAEAEQE-LEESKRETETGIQNLTAEIEQGQESLTENL-EAIKEEIENIV 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 218 TVDLNRVLNETRCQYEALVETNRREVEEWYTTQTEELNKQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHELRNSLE 297
Cdd:COG5185 368 GEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELI 447
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160333504 298 NTLTESEARYSSQLSQ-----VQCLITNVESQLGEIRADLERQNQEYQVLLD----IRSRLECEINTYRGLL 360
Cdd:COG5185 448 SELNKVMREADEESQSrleeaYDEINRSVRSKKEDLNEELTQIESRVSTLKAtlekLRAKLERQLEGVRSKL 519
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
65-364 |
7.05e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.60 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 65 DRLASYMEKVRQLERENAELECRIQERNQQQDPLVCPAYQAYFRTIEELQQKILCGKSENARLVVQIDNAKLASDDFRTK 144
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 145 YETELSLRQLVEADI-------------------NSLRRILDELTLC--------------KSDLEAQVESLkEELLCLK 191
Cdd:COG4717 236 LEAAALEERLKEARLllliaaallallglggsllSLILTIAGVLFLVlgllallflllareKASLGKEAEEL-QALPALE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 192 QNHEQEVNTLRCQLGdrLNVEVDAAPTVDLNRVLNETRCQYEALVETNRR-EVEEWYTTQTEELNKQVVSSSEQLQSC-- 268
Cdd:COG4717 315 ELEEEELEELLAALG--LPPDLSPEELLELLDRIEELQELLREAEELEEElQLEELEQEIAALLAEAGVEDEEELRAAle 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 269 -QAEIIELRRTVNALEIELQAQHELRNSLENTLTESEaryssqlsqvqclitnVESQLGEIRADLERQNQEYQVLLDIRS 347
Cdd:COG4717 393 qAEEYQELKEELEELEEQLEELLGELEELLEALDEEE----------------LEEELEELEEELEELEEELEELREELA 456
|
330
....*....|....*..
gi 160333504 348 RLECEINTyrglLESED 364
Cdd:COG4717 457 ELEAELEQ----LEEDG 469
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
126-293 |
7.49e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.60 E-value: 7.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 126 RLVVQIDNAKLASDDFRTKYETELSLRQLV---EADINSLRRILDELTLCKS--DLEAQVESLKEELlclkQNHEQEVNT 200
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELeelEAELEELREELEKLEKLLQllPLYQELEALEAEL----AELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 201 LRCQLGDRLNVEVDAAptvDLNRVLNETRCQYEALVE----TNRREVEEWyTTQTEELNKQVVSSSEQLQSCQAEIIELR 276
Cdd:COG4717 151 LEERLEELRELEEELE---ELEAELAELQEELEELLEqlslATEEELQDL-AEELEELQQRLAELEEELEEAQEELEELE 226
|
170
....*....|....*..
gi 160333504 277 RTVNALEIELQAQHELR 293
Cdd:COG4717 227 EELEQLENELEAAALEE 243
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
146-338 |
7.78e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 38.28 E-value: 7.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 146 ETELSLRQLVEADINSLRRILDELtlcksdlEAQVESLKEELLCLKQNHEqevntlrcqlgdrLNvEVDAAPTVDLNRVL 225
Cdd:PRK04778 299 EREVKARKYVEKNSDTLPDFLEHA-------KEQNKELKEEIDRVKQSYT-------------LN-ESELESVRQLEKQL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 226 NETRCQYEALVEtnrrEVEEW---YTTQTEELNKQVvsssEQLQSCQAEIIELRRTVNALE-IELQAQH---ELRNSLEN 298
Cdd:PRK04778 358 ESLEKQYDEITE----RIAEQeiaYSELQEELEEIL----KQLEEIEKEQEKLSEMLQGLRkDELEAREkleRYRNKLHE 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 160333504 299 TLTESEAR--------YSSQLSQVQCLITNVESQLGEIRADLERQNQE 338
Cdd:PRK04778 430 IKRYLEKSnlpglpedYLEMFFEVSDEIEALAEELEEKPINMEAVNRL 477
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
61-375 |
9.86e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 38.41 E-value: 9.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 61 QFLNDRLASYMEKVRQLERENAELECRIQERNQQQdplvcpayqAYFRTIEELQQKILCGKSENARLVVQIDnaklasdd 140
Cdd:TIGR00618 208 LCTPCMPDTYHERKQVLEKELKHLREALQQTQQSH---------AYLTQKREAQEEQLKKQQLLKQLRARIE-------- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 141 frtKYETELSLRQLVEADINSLRRILDELTLCKS--DLEAQVESLKEELLCLKQNHEQEVNTLRCQLGDRLNVEVDAAPT 218
Cdd:TIGR00618 271 ---ELRAQEAVLEETQERINRARKAAPLAAHIKAvtQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 219 VDLNRVLNETRCQYEalVETNRREVEEWYTTQTEELNK---QVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHELRNS 295
Cdd:TIGR00618 348 QTLHSQEIHIRDAHE--VATSIREISCQQHTLTQHIHTlqqQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333504 296 LENTLTESEA--RYSSQLS-----QVQCLITNvESQLGEIRADLERQNQEYQVLLDIRSRlECEINTYRGLLESEDCKLP 368
Cdd:TIGR00618 426 LAHAKKQQELqqRYAELCAaaitcTAQCEKLE-KIHLQESAQSLKEREQQLQTKEQIHLQ-ETRKKAVVLARLLELQEEP 503
|
....*..
gi 160333504 369 CNPCATT 375
Cdd:TIGR00618 504 CPLCGSC 510
|
|
| |
