|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
92-403 |
8.56e-144 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 413.93 E-value: 8.56e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 92 SEKETMQFLNDRLANYLEKVRQLERENAELESRIQEWYEFQIPYICPDYQSYFKTIEDFQQKILLTKSENARLVLQIDNA 171
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 172 KLAADDFRTKYETELSLRQLVEADINGLRRILDELTLCKADLEAQVESLKEELMCLKKNHEEEVSVLRCQLGD-RLNVEV 250
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDtQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 251 DAAPPVDLNKILEDMRCQYEALVENNRRDVEAWFNTQTEELNQQVVSSSEQLQCCQTEIIELRRTVNALEIELQAQHSMR 330
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4504927 331 NSLESTLAETEARYSSQLAQMQCLISNVEAQLSEIRCDLERQNQEYQVLLDVKARLEGEIATYRHLLEGEDCK 403
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
147-398 |
1.42e-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: 57.37 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 147 IEDFQQKILLTKSENARLVLQIDNAKLAADDFRTKYETELSLRQLVEADINGLRRILDELTLCKADLEAQVESLKEELMC 226
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 227 LKKNhEEEVSVLRCQLGDRLnvEVDAAPPVDLNKILEDMRCQYEALVENNRRDVEAWfntqtEELNQQVVSSSEQLQCCQ 306
Cdd:TIGR02168 314 LERQ-LEELEAQLEELESKL--DELAEELAELEEKLEELKEELESLEAELEELEAEL-----EELESRLEELEEQLETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 307 TEIIELRRTVNALEIELQAQHSMRNSLESTLAETEARYSSQLAQMQclisnvEAQLSEIRCDLERQNQEYQVLLDVKARL 386
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE------EAELKELQAELEELEEELEELQEELERL 459
|
250
....*....|..
gi 4504927 387 EGEIATYRHLLE 398
Cdd:TIGR02168 460 EEALEELREELE 471
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
148-398 |
2.07e-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: 56.99 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 148 EDFQQKILLTKSENARLVLQIDNAKLAADDFRTKYETELSLRQLVEADINGLRRILDELTLCKADLEAQVESLKEELmcl 227
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV--- 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 228 kKNHEEEVsvlrcqlgDRLNVEvdaappvdLNKILEDMRCQYEALVENNRRDVEAwfNTQTEELNQQVVSSSEQLQCCQT 307
Cdd:TIGR02168 743 -EQLEERI--------AQLSKE--------LTELEAEIEELEERLEEAEEELAEA--EAEIEELEAQIEQLKEELKALRE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 308 EIIELRRTVNALEIELQAQHSMRNSLESTLAETEARY---SSQLAQMQCLISNVEAQLSEIRCDLERQNQEYQVLLDVKA 384
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLedlEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA 883
|
250
....*....|....
gi 4504927 385 RLEGEIATYRHLLE 398
Cdd:TIGR02168 884 SLEEALALLRSELE 897
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
91-398 |
7.98e-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: 55.06 E-value: 7.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 91 GSEKETMQFLNDR--LANYLEKVRQLERENAELESRIQEwyefqipyicpdyqsYFKTIEDFQQKILLTKSENARLVLQI 168
Cdd:TIGR02168 664 GSAKTNSSILERRreIEELEEKIEELEEKIAELEKALAE---------------LRKELEELEEELEQLRKELEELSRQI 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 169 DNAKLAADDFRTKYETELSLRQL-------VEADINGLRRILDELTLCKADLEAQVESLKEELmclkKNHEEEVSVLRCQ 241
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQlskelteLEAEIEELEERLEEAEEELAEAEAEIEELEAQI----EQLKEELKALREA 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 242 LgDRLNVEVDaappvDLNKILEDMRCQYEALvENNRRDVEawfnTQTEELNQQVVSSSEQLQCCQTEIIELRRTVNALEI 321
Cdd:TIGR02168 805 L-DELRAELT-----LLNEEAANLRERLESL-ERRIAATE----RRLEDLEEQIEELSEDIESLAAEIEELEELIEELES 873
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4504927 322 ELQAQHSMRNSLESTLAETEARYSSQLAQMQclisNVEAQLSEIRCDLERQNQEyqvLLDVKARLEGEIATYRHLLE 398
Cdd:TIGR02168 874 ELEALLNERASLEEALALLRSELEELSEELR----ELESKRSELRRELEELREK---LAQLELRLEGLEVRIDNLQE 943
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
151-372 |
1.27e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 151 QQKILLTKSENARLVLQIDNAKLAADDFRTKYETELSLRQLVEADINGLRRILDELTLCKADLEAQVESLKEELMCLKKN 230
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 231 HEEEVSVLRCQLG--------DRLNVEVDAAPPVDLNKILEDMRcqyeALVENNRRDVEAwFNTQTEELNQQVVSSSEQl 302
Cdd:COG4942 99 LEAQKEELAELLRalyrlgrqPPLALLLSPEDFLDAVRRLQYLK----YLAPARREQAEE-LRADLAELAALRAELEAE- 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 303 qccQTEIIELRRTVNALEIELQAQHSMRNSLESTLAETEARYSSQLAQMQCLISNVEAQLSEIRCDLERQ 372
Cdd:COG4942 173 ---RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
97-398 |
1.67e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 97 MQFLNDRLANYLEKVRQLERENAELESRIQEwYEFQIPYICPDYQSYFKTIEDFQQKILLTKSENARLVLQIDNAKLAAD 176
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQE-LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 177 DFRTKYETELSLRQLVEADINGLRRILDELTLCKADLEAQVESLKEELmclkknhEEevsvlrcqlgdrlnvevdaappv 256
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL-------EE----------------------- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 257 dLNKILEDMRCQYEALvennrrdveawfNTQTEELNQQVVSSSEQLQCCQTEIIELRRTVNALEIELQAQHSMRNSLEST 336
Cdd:TIGR02168 363 -LEAELEELESRLEEL------------EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 337 LAETEARYSS--------QLAQMQCLISNVEAQLSEIRCDLERQNQEYQVLLDVKARLEGEIATYRHLLE 398
Cdd:TIGR02168 430 LEEAELKELQaeleeleeELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
100-400 |
2.19e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.50 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 100 LNDRLANYLEKVRQLERENAE---LESRIQ-EWYEFQipyicpdyqsYFKTIEDFQQKILlTKSENARLVL--------- 166
Cdd:pfam15921 498 VSDLTASLQEKERAIEATNAEitkLRSRVDlKLQELQ----------HLKNEGDHLRNVQ-TECEALKLQMaekdkviei 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 167 ---QIDN-AKLAADDFRTKYETELSLRQLvEADINGLRRILDELTLCK-------ADLEAQVESLKEELMCLKKNHEEEV 235
Cdd:pfam15921 567 lrqQIENmTQLVGQHGRTAGAMQVEKAQL-EKEINDRRLELQEFKILKdkkdakiRELEARVSDLELEKVKLVNAGSERL 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 236 SVLR--CQLGDRLNVEVDAAPPvDLNKILEDmrcqYEALVENnrrdveawFNTQTEELNQQVVSSSEQLQCCQTEIIELR 313
Cdd:pfam15921 646 RAVKdiKQERDQLLNEVKTSRN-ELNSLSED----YEVLKRN--------FRNKSEEMETTTNKLKMQLKSAQSELEQTR 712
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 314 RTVNALeiELQAQHSMRNSLESTLAETEARysSQLAQMQCLISNVEAQLSEircdlerQNQEYQVLLDVKARLEGE---I 390
Cdd:pfam15921 713 NTLKSM--EGSDGHAMKVAMGMQKQITAKR--GQIDALQSKIQFLEEAMTN-------ANKEKHFLKEEKNKLSQElstV 781
|
330
....*....|
gi 4504927 391 ATYRHLLEGE 400
Cdd:pfam15921 782 ATEKNKMAGE 791
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
196-335 |
7.88e-06 |
|
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: 47.70 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 196 INGLRRILDE-LTLCKADLE------AQVESLKEELMCLKKNHEEEVSVLRcqlgdRLNVEVDAAPPVDLNKILEDMRCQ 268
Cdd:smart00787 142 LEGLKEGLDEnLEGLKEDYKllmkelELLNSIKPKLRDRKDALEEELRQLK-----QLEDELEDCDPTELDRAKEKLKKL 216
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4504927 269 YEALVENNRRDVEawFNTQTEELNQQVVSSSEQLQCCQTEIIELRRTVN------ALEIE-LQAQHsmrNSLES 335
Cdd:smart00787 217 LQEIMIKVKKLEE--LEEELQELESKIEDLTNKKSELNTEIAEAEKKLEqcrgftFKEIEkLKEQL---KLLQS 285
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
105-398 |
1.46e-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: 47.81 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 105 ANYLEKVRQLERENAELESRIQEwyefqipyicpDYQSYFKTIEDFQQKILLTKSENARLVLQIDN------------AK 172
Cdd:pfam15921 313 SMYMRQLSDLESTVSQLRSELRE-----------AKRMYEDKIEELEKQLVLANSELTEARTERDQfsqesgnlddqlQK 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 173 LAADdfRTKYETELSL-----RQLVEAD------INGLRRILDELTLCKADLEAQVESLKEE--------LMCLKKNHE- 232
Cdd:pfam15921 382 LLAD--LHKREKELSLekeqnKRLWDRDtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSEcqgqmerqMAAIQGKNEs 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 233 -EEVSVLRCQLGDRLNVevdaappvdLNKILEDMRCQYEALvENNRRDVeawfntqtEELNQQVVSSSEQLQCCQTEIIE 311
Cdd:pfam15921 460 lEKVSSLTAQLESTKEM---------LRKVVEELTAKKMTL-ESSERTV--------SDLTASLQEKERAIEATNAEITK 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 312 LRRTVNALEIELQAQHSMRNSLESTLAETEArYSSQLAQMQCLISNVEAQLSEIRCDLERQNQEYQVLLDVKARLEGEIA 391
Cdd:pfam15921 522 LRSRVDLKLQELQHLKNEGDHLRNVQTECEA-LKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEIN 600
|
....*..
gi 4504927 392 TYRHLLE 398
Cdd:pfam15921 601 DRRLELQ 607
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
94-387 |
2.10e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 94 KETMQFLNDRLANYLEKVRQLEREnaelesriqewyefqipyicpdyqsyfktIEDFQQKILLTKSENarlvlqidnakl 173
Cdd:COG3206 174 RKALEFLEEQLPELRKELEEAEAA-----------------------------LEEFRQKNGLVDLSE------------ 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 174 aaddfrtkyETELSLRQLVEadingLRRILDELTLCKADLEAQVESLKEelmclkknheeevsvlrcqlgdRLNVEVDAA 253
Cdd:COG3206 213 ---------EAKLLLQQLSE-----LESQLAEARAELAEAEARLAALRA----------------------QLGSGPDAL 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 254 PPVDLNKILEDMRCQYEALvENNRRDVEAWF---NTQTEELNQQVVSSSEQLQccqteiIELRRTVNALEIELQAQHSMR 330
Cdd:COG3206 257 PELLQSPVIQQLRAQLAEL-EAELAELSARYtpnHPDVIALRAQIAALRAQLQ------QEAQRILASLEAELEALQARE 329
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 4504927 331 NSLESTLAETEARYSSqlaqmqclISNVEAQLSEIRCDLERQNQEYQVLLdvkARLE 387
Cdd:COG3206 330 ASLQAQLAQLEARLAE--------LPELEAELRRLEREVEVARELYESLL---QRLE 375
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
103-390 |
4.20e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 103 RLANYLEKVRQLERENAELES--RIQEWYEFQIPYICPDYQSYFKTIEDFQQKILlTKSENARLVLQIDNAKLAADDFRT 180
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASleEELEKLTEEISELEKRLEEIEQLLEELNKKIK-DLGEEEQLRVKEKIGELEAEIASL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 181 KYETELSLRQLVEADinGLRRILDELtlcKADLEAQVESLKEELmclkknheEEVSVLRCQLGDRLNvevdaappvDLNK 260
Cdd:TIGR02169 307 ERSIAEKERELEDAE--ERLAKLEAE---IDKLLAEIEELEREI--------EEERKRRDKLTEEYA---------ELKE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 261 ILEDMRCQYEALVENNRrdveawfntqteELNQQVVSSSEQLQCCQTEIIELRRTVNALEIELQAQHSMRNSLESTLAET 340
Cdd:TIGR02169 365 ELEDLRAELEEVDKEFA------------ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 4504927 341 EAR---YSSQLAQMQCLISNVEAQLSEIRCDLERQNQEYQVLLDVKARLEGEI 390
Cdd:TIGR02169 433 EAKineLEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL 485
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
93-398 |
6.46e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 93 EKETMQFLNDRLANYLEKVRQLERENAELESRIQEWYEfqipyicpdyqsyfkTIEDFQQKILLTKSENARLVLQIDNAK 172
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELEL---------------ELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 173 LAADDFRTKYETELSLRQLVEADINGLRRILDELTLCKADLEAQVESLKEELmclkKNHEEEVSVLRCQLGDRLNVEVDA 252
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL----AEAEEALLEAEAELAEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 253 AppvdlnkiledmrcqyEALVENNRRDVEAwfNTQTEELNQQVVSSSEQLQCCQTEIIELRRTVNALEIELQAQHSMRNS 332
Cdd:COG1196 385 A----------------EELLEALRAAAEL--AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4504927 333 LESTLAETEARYSSQLAQMQCL---ISNVEAQLSEIRCDLERQNQEYQVLLDVKARLEGEIATYRHLLE 398
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELleeAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
213-387 |
1.17e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 44.73 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 213 LEAQVESLKEELMCLKKNHEEEVSVL-RCQLGDRLNVEVDAAPPVDLNKILEDMRCQYEALVENNRRDVE---------A 282
Cdd:pfam05557 7 SKARLSQLQNEKKQMELEHKRARIELeKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAElnrlkkkylE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 283 WFNTQTEELNQQVVSSSEQLQCCQTEIIELRRTVNALEIELQAQHSMRNSLESTLAETEARYS------SQLAQMQCLIS 356
Cdd:pfam05557 87 ALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASeaeqlrQNLEKQQSSLA 166
|
170 180 190
....*....|....*....|....*....|.
gi 4504927 357 NVEAQLSEIRCDLERQNQEYQVLLDVKARLE 387
Cdd:pfam05557 167 EAEQRIKELEFEIQSQEQDSEIVKNSKSELA 197
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
94-375 |
1.23e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 94 KETMQFLNDRLANYLEKVRQLERENAELESRIQEwYEFQIPYICPDYQSYFKTIEDFQQKILLTKSENARLVLQIDNAKL 173
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEE-LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 174 AADDFRTKYETELSLRQLVEADINGLRRILDELTLCKADLEAQVESLKEELMCLKKNHEEEVSvlrcqlgdrlnvevdaa 253
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES----------------- 873
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 254 ppvDLNKILEDMRCQYEALVEnnRRDVEAWFNTQTEELNQQVVSSSEQLQCCQTEIIELRRTVNALEIELQaqhsmrnSL 333
Cdd:TIGR02168 874 ---ELEALLNERASLEEALAL--LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID-------NL 941
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 4504927 334 ESTLAEteaRYSSQLAQMQCLISNVEAQLSEIRCDLERQNQE 375
Cdd:TIGR02168 942 QERLSE---EYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
169-387 |
2.67e-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: 43.63 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 169 DNAKLAADDFRTKYETELSLRQLvEADINGLRRILDELTLCKADLEAQVESLKEELMCLKKNHEEEVSVLRCQLGDRLNV 248
Cdd:pfam01576 472 DTQELLQEETRQKLNLSTRLRQL-EDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRL 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 249 EVDAAppvDLNKILEDMRCQYEALVENNRRDVEAWFNTQTEELNQ-QVVSSSEQLQ------CCQTEIIELRRTVNALEI 321
Cdd:pfam01576 551 QRELE---ALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQrQLVSNLEKKQkkfdqmLAEEKAISARYAEERDRA 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 322 ELQAQH------SMRNSLES---TLAETEARYSSQLAQMQCLIS-------NV----------EAQLSEIRCDLERQNQE 375
Cdd:pfam01576 628 EAEAREketralSLARALEEaleAKEELERTNKQLRAEMEDLVSskddvgkNVhelerskralEQQVEEMKTQLEELEDE 707
|
250
....*....|..
gi 4504927 376 YQVLLDVKARLE 387
Cdd:pfam01576 708 LQATEDAKLRLE 719
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
92-402 |
3.02e-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: 43.41 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 92 SEKETMQFLNDRLANYLEKVRQLE----RENAELESRIQEWYEFQIpyicpdyqsyfKTIEDFQQKIL-LTKSENARLVL 166
Cdd:COG5185 243 SELEDLAQTSDKLEKLVEQNTDLRleklGENAESSKRLNENANNLI-----------KQFENTKEKIAeYTKSIDIKKAT 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 167 QIDNAKLAADDFRTKYEtelslrQLVEADINGLRRILDELTLCKADLEAQVESLKEELMCLKKnhEEEVSVLRCQLGDrL 246
Cdd:COG5185 312 ESLEEQLAAAEAEQELE------ESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVG--EVELSKSSEELDS-F 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 247 NVEVDAAP------PVDLNKILEDMRCQYEALVENNRRDVEAwFNTQTEELNQQVVSSSEQLQCCQTEIIELRRTVNALE 320
Cdd:COG5185 383 KDTIESTKesldeiPQNQRGYAQEILATLEDTLKAADRQIEE-LQRQIEQATSSNEEVSKLLNELISELNKVMREADEES 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 321 IELQAQHSmrNSLESTLAETEARYSSQLAQMQCLISNVEAQLSEIRCDLERQNQEYQVLLDVKARLEGEIATYR---HLL 397
Cdd:COG5185 462 QSRLEEAY--DEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARgyaHIL 539
|
....*
gi 4504927 398 EGEDC 402
Cdd:COG5185 540 ALENL 544
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
181-392 |
9.31e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 9.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 181 KYETELSLRQLVEADINGLRRILDELTLCKADLEAQVESLKEELmclkknHEEEVSVLRCQLGDRLNVEvdaappvDLNK 260
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLEL------EELELELEEAQAEEYELLA-------ELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 261 ILEDMRCQYEALVENNRRDVEAwfNTQTEELNQQVVSSSEQLQCCQTEIIELRRTVNALEIELQAQHSMRNSLESTLAET 340
Cdd:COG1196 300 LEQDIARLEERRRELEERLEEL--EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 4504927 341 EARYSSQLAQmqclISNVEAQLSEIRCDLERQNQEYQVLLDVKARLEGEIAT 392
Cdd:COG1196 378 EEELEELAEE----LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
87-390 |
1.63e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 87 GSFNGSEKETMQfLNDRLANYLEKVRQLERENAELESRIQEWYEF--QIPYICPDYQSYFKTIEdFQQKILltksenarl 164
Cdd:PRK03918 238 EEIEELEKELES-LEGSKRKLEEKIRELEERIEELKKEIEELEEKvkELKELKEKAEEYIKLSE-FYEEYL--------- 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 165 vlqidnaklaaddfRTKYETELSLRQLvEADINGLRRILDELTLCKA---DLEAQVESLKEELMCLKKNHE--EEVSVLR 239
Cdd:PRK03918 307 --------------DELREIEKRLSRL-EEEINGIEERIKELEEKEErleELKKKLKELEKRLEELEERHElyEEAKAKK 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 240 CQLgDRLNVEVDAAPPVDLNKILEdmrcqyeaLVENNRRDVEAWFNTQTEELNQqvvssseqlqcCQTEIIELRRTVNAL 319
Cdd:PRK03918 372 EEL-ERLKKRLTGLTPEKLEKELE--------ELEKAKEEIEEEISKITARIGE-----------LKKEIKELKKAIEEL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 320 E----------IELQAQHSMR---------NSLESTLAETEARYS-------------------SQLAQMQCLISNVEAQ 361
Cdd:PRK03918 432 KkakgkcpvcgRELTEEHRKElleeytaelKRIEKELKEIEEKERklrkelrelekvlkkeselIKLKELAEQLKELEEK 511
|
330 340 350
....*....|....*....|....*....|
gi 4504927 362 LSEIRC-DLERQNQEYQVLLDVKARLEGEI 390
Cdd:PRK03918 512 LKKYNLeELEKKAEEYEKLKEKLIKLKGEI 541
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
181-398 |
1.85e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.81 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 181 KYETElslRQLVEADINgLRRILDELtlckADLEAQVESLKEELMCLKKNHEeevsvLRCQLgDRLNVEVDAAppvdlnk 260
Cdd:TIGR02168 174 RKETE---RKLERTREN-LDRLEDIL----NELERQLKSLERQAEKAERYKE-----LKAEL-RELELALLVL------- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 261 iledmrcQYEALVENNRRdveawFNTQTEELNQQVVSSSEQLQCCQTEIIELRRTVNALEIELQAQHSMRNSLESTLAET 340
Cdd:TIGR02168 233 -------RLEELREELEE-----LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4504927 341 E----------ARYSSQLAQMQCLISNVEAQLSEIRCDLERQNQEYQVLLDVKARLEGEIATYRHLLE 398
Cdd:TIGR02168 301 EqqkqilrerlANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
145-375 |
2.45e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.20 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 145 KTIEDFQQKILLTKSENARLvlQIDNAKLAADDFRTK----Y---ETELSLRQLVEADINGLRRILDELtlckadlEAQV 217
Cdd:PRK04778 256 KEIQDLKEQIDENLALLEEL--DLDEAEEKNEEIQERidqlYdilEREVKARKYVEKNSDTLPDFLEHA-------KEQN 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 218 ESLKEELMCLKKNH---EEEVSVLRcqlgdrlnvevdaappvDLNKILEDMRCQYEALVENnrrdveawFNTQTE---EL 291
Cdd:PRK04778 327 KELKEEIDRVKQSYtlnESELESVR-----------------QLEKQLESLEKQYDEITER--------IAEQEIaysEL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 292 NQQVVSSSEQLQCCQTEIIELRRTVNALE-IELQAQHS---MRNSLESTLAETEAR--------YSSQLAQMQCLISNVE 359
Cdd:PRK04778 382 QEELEEILKQLEEIEKEQEKLSEMLQGLRkDELEAREKlerYRNKLHEIKRYLEKSnlpglpedYLEMFFEVSDEIEALA 461
|
250
....*....|....*.
gi 4504927 360 AQLSEIRCDLERQNQE 375
Cdd:PRK04778 462 EELEEKPINMEAVNRL 477
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
295-391 |
2.62e-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: 40.13 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 295 VVSSSEQLQCCQTEIIELRRTVNALEIELQAQHSMRNSLESTLAETEAryssQLAQMQCLISNVEAQLSEIRCDLERQNQ 374
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER----RIAALARRIRALEQELAALEAELAELEK 90
|
90
....*....|....*..
gi 4504927 375 EYQVLLDVKARLEGEIA 391
Cdd:COG4942 91 EIAELRAELEAQKEELA 107
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
102-375 |
2.84e-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: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 102 DRLANYLEKVRQLERENAELESRIQE---WYEfqipyICPDYQSYFKTIEDF---QQKILLTKSENARLVLQIDNAKLAA 175
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEAleaELD-----ALQERREALQRLAEYswdEIDVASAEREIAELEAELERLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 176 DDFRTkyetelsLRQLVEAdingLRRILDELTLCKADLEAQVESLKEELmclkKNHEEEVSVLRCQLgdrlnVEVDAAPP 255
Cdd:COG4913 685 DDLAA-------LEEQLEE----LEAELEELEEELDELKGEIGRLEKEL----EQAEEELDELQDRL-----EAAEDLAR 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 256 VDLNKILEDMRcqYEALVENNRRDVEAWFNTQTEELNQQVVSSSEQLQCCQTEII--------ELRRTVNALEiELQAqh 327
Cdd:COG4913 745 LELRALLEERF--AAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNrewpaetaDLDADLESLP-EYLA-- 819
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 4504927 328 sMRNSLEST-LAETEARYSSQLAQ-----MQCLISNVEAQLSEIRCDLERQNQE 375
Cdd:COG4913 820 -LLDRLEEDgLPEYEERFKELLNEnsiefVADLLSKLRRAIREIKERIDPLNDS 872
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
218-398 |
3.48e-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: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 218 ESLKEELMCLKKNHEEEVSV---LRCQLGdRLNVEVDAAppvdlNKILEDMRCQYEalveNNRRDVEAWFNTQTEELNQQ 294
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKqaaAEEQLV-QANGELEKA-----SREETFARTALK----NARLDLRRLFDEKQSEKDKK 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 295 VVSSSEQLQCCQTEIIELRRTVNALEIELQA--QHSMRNSLESTLAETEAR------YSSQLAQMQCLI----SNVEAQL 362
Cdd:pfam12128 670 NKALAERKDSANERLNSLEAQLKQLDKKHQAwlEEQKEQKREARTEKQAYWqvvegaLDAQLALLKAAIaarrSGAKAEL 749
|
170 180 190
....*....|....*....|....*....|....*.
gi 4504927 363 SEIRCDLERQNQEYQVLLDVKARLEGEIATYRHLLE 398
Cdd:pfam12128 750 KALETWYKRDLASLGVDPDVIAKLKREIRTLERKIE 785
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
246-366 |
3.80e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 39.45 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 246 LNVEVDAAPPVDLNKILEDMRCQYEALV----ENNRRDveawfntQTEELNQQVVSSSEQLQCCQTEIIELRRTVNAL-- 319
Cdd:COG3524 140 ITLEVRAFDPEDAQAIAEALLAESEELVnqlsERARED-------AVRFAEEEVERAEERLRDAREALLAFRNRNGILdp 212
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 4504927 320 EIELQAQHSMRNSLESTLAETEARY----------SSQLAQMQCLISNVEAQLSEIR 366
Cdd:COG3524 213 EATAEALLQLIATLEGQLAELEAELaalrsylspnSPQVRQLRRRIAALEKQIAAER 269
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
93-390 |
4.01e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 39.62 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 93 EKET-MQFLNDRLANYLEKVRQLERENAELESRIQEW------YEFQIPYICPDYQSYFKTIEDFQQKILLTKSENARLV 165
Cdd:TIGR04523 367 EKQNeIEKLKKENQSYKQEIKNLESQINDLESKIQNQeklnqqKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 166 LQIDNAKLAA---DDFRTKYETELSlrqLVEADINGLRRILDELTLCKADLEAQVESLKEElmclKKNHEEEVSVLRCQL 242
Cdd:TIGR04523 447 NQDSVKELIIknlDNTRESLETQLK---VLSRSINKIKQNLEQKQKELKSKEKELKKLNEE----KKELEEKVKDLTKKI 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 243 gDRLNVEVDaappvDLNK-ILEdmrcqyealVENNRRDVEAWFNTQTEELNQQVVssSEQLQCCQTEIIELRRTVNALEI 321
Cdd:TIGR04523 520 -SSLKEKIE-----KLESeKKE---------KESKISDLEDELNKDDFELKKENL--EKEIDEKNKEIEELKQTQKSLKK 582
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4504927 322 ElQAQhsmrnsLESTLAETEARYS---SQLAQMQCLISNVEAQLSEIRCDLERQNQEYQVLLDVKARLEGEI 390
Cdd:TIGR04523 583 K-QEE------KQELIDQKEKEKKdliKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEV 647
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
292-401 |
4.63e-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: 39.36 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 292 NQQVVSSSEQLQCCQTEIIELRRTVNALEIELQAQHSMRNSLESTLAETEAR---YSSQLAQMQCLISNVEAQLSEIRCD 368
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAE 98
|
90 100 110
....*....|....*....|....*....|...
gi 4504927 369 LERQNQEYQVLLDVKARLeGEIATYRHLLEGED 401
Cdd:COG4942 99 LEAQKEELAELLRALYRL-GRQPPLALLLSPED 130
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
141-372 |
5.50e-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: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 141 QSYFKTIEDFQQKILLTKsENARLVLQIdnaKLAADDFRTKYETELSLRQLVEA-DINGLRRILDELTLCKADLEAQVES 219
Cdd:COG4913 231 VEHFDDLERAHEALEDAR-EQIELLEPI---RELAERYAAARERLAELEYLRAAlRLWFAQRRLELLEAELEELRAELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 220 LKEELMCLK---KNHEEEVSVLRCQL----GDRLNvevdaappvDLNKILEDMRCQYEAlVENNRRDVEAWfntqTEELN 292
Cdd:COG4913 307 LEAELERLEarlDALREELDELEAQIrgngGDRLE---------QLEREIERLERELEE-RERRRARLEAL----LAALG 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 293 QQVVSSSEQLQCCQTEIIELRRTVNALEIELQAQHSMRNSLESTLAETEARYSSQLAQMQCLISNVEAQLSEIRCDLERQ 372
Cdd:COG4913 373 LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
294-409 |
7.46e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 39.01 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 294 QVVSSSEQLQCCQTEIIELRRTVNAL-EIELQ----------AQHSMRNSLESTLAETEARYSSQ---LAQMQCLISNVE 359
Cdd:PRK10246 374 QQTSDREQLRQWQQQLTHAEQKLNALpAITLTltadevaaalAQHAEQRPLRQRLVALHGQIVPQqkrLAQLQVAIQNVT 453
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 4504927 360 AQLSEIRCDLERQNQEY----QVLLDVKA--RLEGEIATyrhlLEGEDCKLPP-QPC 409
Cdd:PRK10246 454 QEQTQRNAALNEMRQRYkektQQLADVKTicEQEARIKD----LEAQRAQLQAgQPC 506
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
285-385 |
8.06e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 38.34 E-value: 8.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504927 285 NTQTEELNQQVVSSSEQLQCCQTEIIELRRTVNALEIELQAQHSMRNSLESTLAETEARYSSQLAQmqclISNVEAQLSE 364
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEE----LKELEEQLES 161
|
90 100
....*....|....*....|.
gi 4504927 365 IRCDLERQNQEYQVLLDVKAR 385
Cdd:COG4372 162 LQEELAALEQELQALSEAEAE 182
|
|
| |
