|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
84-333 |
1.41e-73 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 235.97 E-value: 1.41e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 84 YEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQL--------------EASLAAAKKQLADETLLKVDLENRCQSLTE 149
Cdd:pfam00038 52 YEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFrqkyedelnlrtsaENDLVGLRKDLDEATLARVDLEAKIESLKE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 150 DLEFRKSMYEEEINETRRKH--ETRLVEVDSGRQIEyeykLAQALHEMREQHDAQVRLYKEELEQTYHAKLENARLSSEM 227
Cdd:pfam00038 132 ELAFLKKNHEEEVRELQAQVsdTQVNVEMDAARKLD----LTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAAR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 228 NTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDLLAKEKDNSRRMLTDKEREMAEIRDQMQQQLNDYE 307
Cdd:pfam00038 208 NGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQ 287
|
250 260
....*....|....*....|....*.
gi 2217355802 308 QLLDVKLALDMEISAYRKLLEGEEER 333
Cdd:pfam00038 288 ELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| LTD |
pfam00932 |
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ... |
385-489 |
1.99e-23 |
|
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.
Pssm-ID: 460003 [Multi-domain] Cd Length: 108 Bit Score: 94.80 E-value: 1.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 385 TGNVCIEEIDVDG-----KFIRLKNTSEQDQPMGGWEMIRKIGDTsvsYKYTSRYVLKAGQTVTIWAANAGVTAS----P 455
Cdd:pfam00932 4 TGDVVISEVVYDGsggndEFIELYNTGSKAVDLSGWKLQDASGGT---YTFPNGTTLAPGQTVVVWTGSGTNSATagywG 80
|
90 100 110
....*....|....*....|....*....|....
gi 2217355802 456 PTDLIWKNQNSWgtgedvkVILKNSQGEEVAQRS 489
Cdd:pfam00932 81 PSNAVWNNGGDA-------VALYDANGELVDSVG 107
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
69-334 |
2.08e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 69 KKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLT 148
Cdd:COG1196 222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 149 EDLEFRKsmyEEEINETRRKHETRLVEVDSGRQIEYEYKLAQALHEMREQHDAQVRLYKEELEQTyHAKLENARLSSEMN 228
Cdd:COG1196 302 QDIARLE---ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA-EEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 229 TSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDLLAKEKDNSRRMLTDKEREMAEIRDQMQQQLNDYEQ 308
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250 260
....*....|....*....|....*.
gi 2217355802 309 LLDVKLALDMEISAYRKLLEGEEERL 334
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELL 483
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
80-334 |
1.19e-09 |
|
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: 61.23 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 80 KLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADetllkvdLENRCQSLTE---DLEFRKS 156
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR-------LEAEVEQLEEriaQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 157 MYEEEINETR-RKHETRLVEVDSGRQIEYEYKLAQALHEMREQHDAQVRLYKEELEQTyHAKLENARLSSEMNTSTVNSA 235
Cdd:TIGR02168 758 ELEAEIEELEeRLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL-NEEAANLRERLESLERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 236 REELMESRMRIESLSSQLSNLQKESRACLERIQELEDLLAKEKDNSRRMltdkEREMAEIRDQMQQQLNDYEQLLDVKLA 315
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL----EEALALLRSELEELSEELRELESKRSE 912
|
250
....*....|....*....
gi 2217355802 316 LDMEISAYRKLLEGEEERL 334
Cdd:TIGR02168 913 LRRELEELREKLAQLELRL 931
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
82-336 |
1.75e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 82 REYEAALNSKDAALAtaLGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTEDLefrksmyeEE 161
Cdd:COG1196 216 RELKEELKELEAELL--LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL--------EE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 162 INETRRKHETRLVEVDsgRQIEYEYKLAQALHEMREQHDAQVRLYKEELEQTyHAKLENARLSSEMNTSTVNSAREELME 241
Cdd:COG1196 286 AQAEEYELLAELARLE--QDIARLEERRRELEERLEELEEELAELEEELEEL-EEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 242 SRMRIESLSSQLSNLQKESRACLERIQELEDLLAKEKDNSRRMLTDKEREMAEIRDQMQQQLNDYEQLLDVKLALDMEIS 321
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
250
....*....|....*
gi 2217355802 322 AYRKLLEGEEERLKL 336
Cdd:COG1196 443 ALEEAAEEEAELEEE 457
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
80-309 |
1.98e-09 |
|
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: 60.46 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 80 KLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTEDLEFRKSMYE 159
Cdd:TIGR02168 282 EIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 160 EEiNETRRKHETRLVEVDSGRQiEYEYKLAQALHEMrEQHDAQVRLYKEELEQtyhAKLENARLSSEMNTSTVNSAREEL 239
Cdd:TIGR02168 362 EL-EAELEELESRLEELEEQLE-TLRSKVAQLELQI-ASLNNEIERLEARLER---LEDRRERLQQEIEELLKKLEEAEL 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217355802 240 MESRMRIESLSSQLSNLQKEsracLERIQELEDLLAKEKDNSRRMLTDKEREMAEIR---DQMQQQLNDYEQL 309
Cdd:TIGR02168 436 KELQAELEELEEELEELQEE----LERLEEALEELREELEEAEQALDAAERELAQLQarlDSLERLQENLEGF 504
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
68-333 |
3.15e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 68 AKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSL 147
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 148 TEDLEFRksmyEEEINETRRKHETRLVEVDSGRQIEYEykLAQALHEMREQHDAQVRLYKEELEQTYHAKLENARLSSEm 227
Cdd:COG1196 329 EEELEEL----EEELEELEEELEEAEEELEEAEAELAE--AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 228 ntstVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDLLAKEKDNSRRMLTDKEREMAEIRDQMQQQLNDYE 307
Cdd:COG1196 402 ----LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
250 260
....*....|....*....|....*.
gi 2217355802 308 QLLDVKLALDMEISAYRKLLEGEEER 333
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLEAEADY 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
71-295 |
7.72e-09 |
|
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: 58.53 E-value: 7.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 71 ESDLNGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCqsltED 150
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL----ES 828
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 151 LEFRKSMYEEEINETRRKHETRLVEV-----------DSGRQIEYEYKLAQALHEMREQHDAQVRLYKEELEQTYH---- 215
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIeslaaeieeleELIEELESELEALLNERASLEEALALLRSELEELSEELReles 908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 216 AKLENARLSSEMNTStVNSAREELMESRMRIESLSSQLSNLQKESracLERIQELEDLLAKEKDNSRRMLTDKEREMAEI 295
Cdd:TIGR02168 909 KRSELRRELEELREK-LAQLELRLEGLEVRIDNLQERLSEEYSLT---LEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
105-335 |
1.09e-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: 58.16 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 105 LEGDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTEDLEFR----KSMYEEEINETRRKHETRLVEVDSGR 180
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkiKDLGEEEQLRVKEKIGELEAEIASLE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 181 QIEYEYKL-AQALHEMREQHDAQVRLYKEELEQtYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKE 259
Cdd:TIGR02169 308 RSIAEKEReLEDAEERLAKLEAEIDKLLAEIEE-LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE 386
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217355802 260 SRACLERIQELEDLLAKEKDNSRRMLTDKER---EMAEIRDQMQQQLNDYEQLLDVKLALDMEISAyrklLEGEEERLK 335
Cdd:TIGR02169 387 LKDYREKLEKLKREINELKRELDRLQEELQRlseELADLNAAIAGIEAKINELEEEKEDKALEIKK----QEWKLEQLA 461
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
77-299 |
2.11e-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: 56.31 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 77 AQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTEDLEFRKS 156
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 157 MYEEEINET-RRKHETRLVEVDSGRQIEYEYKLAQALHEMREQHDAQVRLYKEELEQtyhakLENARLSSEMNTSTVNSA 235
Cdd:COG4942 105 ELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-----LAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217355802 236 REELMESRMRIESLSSQLSNLQKESRACLERIQELEDLLAKEKDNSRRMLTDKEREMAEIRDQM 299
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
109-336 |
3.08e-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: 56.60 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 109 LEDLKDQIAQLEASLAAAKKQLADetlLKVDLENR------CQSLTEDLEFRKSMYEEEINETRRKHETRLVEVDS---- 178
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAE---LRKELEELeeeleqLRKELEELSRQISALRKDLARLEAEVEQLEERIAQlske 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 179 -GRQIEYEYKLAQALHEMREQHDAQVRLyKEELEQtyhaKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQ 257
Cdd:TIGR02168 756 lTELEAEIEELEERLEEAEEELAEAEAE-IEELEA----QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 258 KESRACLERIQELEDLLAKEKDNSRRM---LTDKEREMAEIRDQMQQQLNDYEQL-LDVKLALDMEISAYRKLLEGEEER 333
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLaaeIEELEELIEELESELEALLNERASLeEALALLRSELEELSEELRELESKR 910
|
...
gi 2217355802 334 LKL 336
Cdd:TIGR02168 911 SEL 913
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
53-343 |
6.16e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.69 E-value: 6.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 53 SLIRAPPASPGQVSYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLAD 132
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 133 etllkvdLENRCQSLTEDLEFRKSMYEEeinetrrkhetrlvevdsgrqieyeykLAQALHEMREQHDAQVRLYKEELEQ 212
Cdd:COG4942 88 -------LEKEIAELRAELEAQKEELAE---------------------------LLRALYRLGRQPPLALLLSPEDFLD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 213 TYHaklenarlsSEMNTSTVNSAREElmesrmRIESLSSQLSNLQKESRACLERIQELEDLLAKEKDNSRRM---LTDKE 289
Cdd:COG4942 134 AVR---------RLQYLKYLAPARRE------QAEELRADLAELAALRAELEAERAELEALLAELEEERAALealKAERQ 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2217355802 290 REMAEIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLLEGEEERLKLSPSPSSR 343
Cdd:COG4942 199 KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
111-328 |
1.51e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 111 DLKDQIAQLEASLAAAKKQLADETLLKVDLE-NRCQSLTEDLEFRKSMYEEEINETRRKHETRLVEVDSGRQIEYEYK-L 188
Cdd:TIGR02168 217 ELKAELRELELALLVLRLEELREELEELQEElKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAnE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 189 AQALHEMREQHDAQVRLYKEELEQ--TYHAKLENARLSSEMNTSTVNSAREELMEsrmRIESLSSQLSNLQKESRACLER 266
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLEEleAQLEELESKLDELAEELAELEEKLEELKE---ELESLEAELEELEAELEELESR 373
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217355802 267 IQELEDLLakekDNSRRMLTDKEREMAEIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLLE 328
Cdd:TIGR02168 374 LEELEEQL----ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
66-151 |
6.11e-06 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 48.57 E-value: 6.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 66 SYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQL-EASLAAAKKQLADETLLKVDLENRC 144
Cdd:TIGR04320 262 KLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTaQNNLATAQAALANAEARLAKAKEAL 341
|
....*..
gi 2217355802 145 QSLTEDL 151
Cdd:TIGR04320 342 ANLNADL 348
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
109-334 |
1.02e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 109 LEDLKDQIAQLEASLAAAKKQLAdetllkvDLENRCQSLTEdlefrksmyeeeinetRRKHETRLVEVDsgrqiEYEYKL 188
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLE-------ALEAELDALQE----------------RREALQRLAEYS-----WDEIDV 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 189 AQALHEMReqhdaqvrlykeELEQtyhaKLENARLSSemntSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQ 268
Cdd:COG4913 664 ASAEREIA------------ELEA----ELERLDASS----DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELE 723
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217355802 269 ELEDLLAKEKDNSRRMLTDKEREMAEIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLLEGEEERL 334
Cdd:COG4913 724 QAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL 789
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
189-335 |
1.61e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 189 AQALHEMREQHDAQVRLYK----EELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACL 264
Cdd:COG1196 215 YRELKEELKELEAELLLLKlrelEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217355802 265 ERIQELEDLLAKEKDNSRRMLTDKEREMAEIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLLEGEEERLK 335
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
117-329 |
1.98e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.60 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 117 AQLEASLAAAKKQ---LADETLLKVDLENrcqslTEDLEFRKSMYEEEINETRRKhetrlvevdsgrqieyeykLAQALH 193
Cdd:PRK11281 39 ADVQAQLDALNKQkllEAEDKLVQQDLEQ-----TLALLDKIDRQKEETEQLKQQ-------------------LAQAPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 194 EMREQHDAQVRLYK---EELEQTYhAKLENARLSSEMN--TSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQ 268
Cdd:PRK11281 95 KLRQAQAELEALKDdndEETRETL-STLSLRQLESRLAqtLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQ 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217355802 269 ELEDLLAKEKDNSRrmltdkeremaEIRDQMQQQLNDYEQLLDVKLALDmeisayRKLLEG 329
Cdd:PRK11281 174 QIRNLLKGGKVGGK-----------ALRPSQRVLLQAEQALLNAQNDLQ------RKSLEG 217
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
81-273 |
2.11e-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: 47.37 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 81 LREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLAD------ETLLKV-DLENRCQSLTEDLEF 153
Cdd:TIGR02169 814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEleeeleELEAALrDLESRLGDLKKERDE 893
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 154 RKSMYEE------EINETRRKHETRLVEVDSGRQIEyEYKLAQALHEMRE-QHDAQVRLYKEELEQTYHAKLENARLSSE 226
Cdd:TIGR02169 894 LEAQLRElerkieELEAQIEKKRKRLSELKAKLEAL-EEELSEIEDPKGEdEEIPEEELSLEDVQAELQRVEEEIRALEP 972
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2217355802 227 MNtstvNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDL 273
Cdd:TIGR02169 973 VN----MLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
102-332 |
2.16e-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: 47.48 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 102 KKSLEGDLEDLKDQIAQLEASLAAAKKQLA--------------DETL------------------LKVDLENRCQS--- 146
Cdd:pfam01576 210 KRKLEGESTDLQEQIAELQAQIAELRAQLAkkeeelqaalarleEETAqknnalkkireleaqiseLQEDLESERAArnk 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 147 -------LTEDLEFRKSMYEEEINET------RRKHETRLVEVDsgRQIEYEYKLAQA-LHEMREQHDAQVRLYKEELEQ 212
Cdd:pfam01576 290 aekqrrdLGEELEALKTELEDTLDTTaaqqelRSKREQEVTELK--KALEEETRSHEAqLQEMRQKHTQALEELTEQLEQ 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 213 TYHAKL-----------ENARLSSEMntSTVNSAREELMESRMRIEslsSQLSNLQKESRACLERIQELEDLLAK---EK 278
Cdd:pfam01576 368 AKRNKAnlekakqalesENAELQAEL--RTLQQAKQDSEHKRKKLE---GQLQELQARLSESERQRAELAEKLSKlqsEL 442
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217355802 279 DNSRRMLTDKERE---MAEIRDQMQQQLNDYEQLLD----VKL-------ALDMEISAYRKLLEGEEE 332
Cdd:pfam01576 443 ESVSSLLNEAEGKnikLSKDVSSLESQLQDTQELLQeetrQKLnlstrlrQLEDERNSLQEQLEEEEE 510
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
74-305 |
3.40e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 74 LNGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAK-----KQLADETllKVDLENRCQSLT 148
Cdd:PRK02224 400 FGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgQPVEGSP--HVETIEEDRERV 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 149 EDLEFRKSMYEEEINETRRKHETRLVEVDSGRQIEYEYKLAQALHEMREQHDAQVRLYKEELEQTYHAKLEnarLSSEMN 228
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE---LEAEAE 554
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217355802 229 T--STVNSAREELMESRMRIESLSSQLSNLqKESRACLERIQELEDLLAKEKDNSRRmLTDKEREMAEIRDQMQQQLND 305
Cdd:PRK02224 555 EkrEAAAEAEEEAEEAREEVAELNSKLAEL-KERIESLERIRTLLAAIADAEDEIER-LREKREALAELNDERRERLAE 631
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
68-300 |
7.05e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 7.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 68 AKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLAD-ETLLK--------- 137
Cdd:PRK02224 380 EDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEaEALLEagkcpecgq 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 138 -------VDLENRCQSLTEDLEFRKSMYEEEINETRRKHETRLVEVDSGRQIEYEYKLAQALHEMREQHDAQV------- 203
Cdd:PRK02224 460 pvegsphVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIeekrera 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 204 ---RLYKEELE---QTYHAKLENARLSSEMNTSTV---NSAREELMESRMRIESLSSQLSNLQkESRACLERIQELEDLL 274
Cdd:PRK02224 540 eelRERAAELEaeaEEKREAAAEAEEEAEEAREEVaelNSKLAELKERIESLERIRTLLAAIA-DAEDEIERLREKREAL 618
|
250 260
....*....|....*....|....*.
gi 2217355802 275 AKEKDNSRRMLTDKEREMAEIRDQMQ 300
Cdd:PRK02224 619 AELNDERRERLAEKRERKRELEAEFD 644
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
109-336 |
1.47e-04 |
|
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: 44.83 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 109 LEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTEDLEFRKSMYEEEINETRRKHETRLVEVDSgrqieyeyKL 188
Cdd:pfam12128 246 LQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADA--------AV 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 189 AQALHEMrEQHDAQVRLYKEELEQTYHAKLENA-RLSSEMNtsTVNSAREELMESRMRIEslssqlsnlQKESRACLERI 267
Cdd:pfam12128 318 AKDRSEL-EALEDQHGAFLDADIETAAADQEQLpSWQSELE--NLEERLKALTGKHQDVT---------AKYNRRRSKIK 385
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217355802 268 QELEDLLAKEKDNSRRMLTDKEREMAEIRDQMQQQLNDYEQLLDVKLaLDMEISAYRKLLEGEEERLKL 336
Cdd:pfam12128 386 EQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGK-LEFNEEEYRLKSRLGELKLRL 453
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
66-333 |
1.49e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 66 SYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSlegDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQ 145
Cdd:PRK02224 346 SLREDADDLEERAEELREEAAELESELEEAREAVEDRRE---EIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 146 SLTEDL-EFRKSMyeEEINETRRKHETRLVE---VDSGRQIEyEYKLAQALHEMREQHD------AQVRLYKEELEQTYH 215
Cdd:PRK02224 423 ELREREaELEATL--RTARERVEEAEALLEAgkcPECGQPVE-GSPHVETIEEDRERVEeleaelEDLEEEVEEVEERLE 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 216 -----AKLENARLSSEMNTSTVNS----AREELMESRMRIESLSSQLSNLQKESRACLERIQELEDllakEKDNSRRMLT 286
Cdd:PRK02224 500 raedlVEAEDRIERLEERREDLEEliaeRRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEE----EAEEAREEVA 575
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2217355802 287 DKEREMAEIRDQMqQQLNDYEQLLDVKLALDMEISAYRKLLEGEEER 333
Cdd:PRK02224 576 ELNSKLAELKERI-ESLERIRTLLAAIADAEDEIERLREKREALAEL 621
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
64-148 |
1.56e-04 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 43.95 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 64 QVSYAKKESDLNGAQIKLREYEAALNSKDAALATA---LGDKKS-----LEGDLEDLKDQIAQLEASLAAAKKQLADetl 135
Cdd:TIGR04320 267 QADLAAAQTALNTAQAALTSAQTAYAAAQAALATAqkeLANAQAqalqtAQNNLATAQAALANAEARLAKAKEALAN--- 343
|
90
....*....|...
gi 2217355802 136 LKVDLENRCQSLT 148
Cdd:TIGR04320 344 LNADLAKKQAALD 356
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
81-322 |
2.25e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 81 LREYEAALNSKDAALATALgdkKSLEGDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRcQSLTEDLEFRKSMyeE 160
Cdd:TIGR02169 728 LEQEEEKLKERLEELEEDL---SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR-LSHSRIPEIQAEL--S 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 161 EINETRRKHETRLVEVDsgrQIEYEYKLAQALHEMREQHDAQVRLYKEELEQTYHAKLENARLSSEMNTSTVNSAREELM 240
Cdd:TIGR02169 802 KLEEEVSRIEARLREIE---QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 241 ESRMRIESLSSQLSNLQKESRACLERIQELEDLLAKEKDNSRRMLTDKE---REMAEIRDQMQQ------QLNDYEQLLD 311
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEaleEELSEIEDPKGEdeeipeEELSLEDVQA 958
|
250
....*....|.
gi 2217355802 312 VKLALDMEISA 322
Cdd:TIGR02169 959 ELQRVEEEIRA 969
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
180-344 |
2.60e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 180 RQIEYEYKLAQALHEMREQHDAQVRLYKEELEQTYH--AKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQ 257
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLReiNEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 258 KESRACLERIQELEDLLaKEKDNSRRMLTDKEREMAEIRDQMQQQL---NDYEQLLDVKLALDMEISAYRKLLEGEEERL 334
Cdd:PRK03918 252 GSKRKLEEKIRELEERI-EELKKEIEELEEKVKELKELKEKAEEYIklsEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
170
....*....|
gi 2217355802 335 KLSPSPSSRV 344
Cdd:PRK03918 331 KELEEKEERL 340
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
85-321 |
3.24e-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: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 85 EAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADETllkvDLENRCQSLTEDLEFRKSMYEEEINE 164
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAET----ELCAEAEEMRARLAARKQELEEILHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 165 TrrkhETRLVEvdsgrqieyEYKLAQALHEMREQHDAQVRLYKEELEQTyhaklENARLSSEMNTSTVNSAREELMEsrm 244
Cdd:pfam01576 80 L----ESRLEE---------EEERSQQLQNEKKKMQQHIQDLEEQLDEE-----EAARQKLQLEKVTTEAKIKKLEE--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 245 RIESLSSQLSNLQKESRACLERIQELEDLLAKEKDNSR---RMLTDKEREMAEIRDQMQQQLNDYEQLLDVKLALDMEIS 321
Cdd:pfam01576 139 DILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKslsKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGEST 218
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
74-275 |
3.28e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 74 LNGAQIK-LREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADETLLKvdlenrcqsLTEDLE 152
Cdd:COG4717 68 LNLKELKeLEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ---------ELEALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 153 FRKSMYEEEINETRRKHETRLvevdsgRQIEYEYKLAQALHEMREQHDAQVRLYKEELEQTyhakLENARLSSEMNTSTV 232
Cdd:COG4717 139 AELAELPERLEELEERLEELR------ELEEELEELEAELAELQEELEELLEQLSLATEEE----LQDLAEELEELQQRL 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2217355802 233 NSAREELMESRMRIESLSSQLSNLQKESRAC--LERIQELEDLLA 275
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQLENELEAAalEERLKEARLLLL 253
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
104-332 |
3.55e-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: 43.19 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 104 SLEGDLEDLKDQIAQ-----------LEASLAAAKKQLADETLLKVDLENRCQSLTEDLEFRKSMYEEEINETRRKheTR 172
Cdd:pfam05557 6 ESKARLSQLQNEKKQmelehkrarieLEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLK--KK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 173 LVEVDSGRQIEYEYKLAQAlhemreqHDAQVRLYKEELEqtYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQ 252
Cdd:pfam05557 84 YLEALNKKLNEKESQLADA-------REVISCLKNELSE--LRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 253 LSNLQKESRACLE---RIQELEDLLAKEKDNSRRMLTDKER--EMAEIRDQMQQQLNDYEQL---LDVKLALDMEISAYR 324
Cdd:pfam05557 155 RQNLEKQQSSLAEaeqRIKELEFEIQSQEQDSEIVKNSKSElaRIPELEKELERLREHNKHLnenIENKLLLKEEVEDLK 234
|
....*...
gi 2217355802 325 KLLEGEEE 332
Cdd:pfam05557 235 RKLEREEK 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
67-313 |
3.76e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 67 YAKKESDLNgaqiKLREYEAALNSKDAALATALgdkksLEGDLEDLKDQIAQLEASLAAAKKQLADEtllkvdlenrcqs 146
Cdd:COG4913 264 YAAARERLA----ELEYLRAALRLWFAQRRLEL-----LEAELEELRAELARLEAELERLEARLDAL------------- 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 147 ltedlefrksmyEEEINETRRKHETrlvevDSGRQIEyeyKLAQALHEMREQHDAQvrlykEELEQTYHAKLENARLSSE 226
Cdd:COG4913 322 ------------REELDELEAQIRG-----NGGDRLE---QLEREIERLERELEER-----ERRRARLEALLAALGLPLP 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 227 MNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDLLAKEKDNSRRMLTDKEREMAEIRDQMQQQLNDY 306
Cdd:COG4913 377 ASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLD 456
|
250
....*....|....
gi 2217355802 307 EQ-------LLDVK 313
Cdd:COG4913 457 EAelpfvgeLIEVR 470
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
94-282 |
4.13e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 94 ALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADetllkvdLENRCQSLTEDLEFRksmyeeEINETRRKHETRL 173
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE-------LREELEKLEKLLQLL------PLYQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 174 vevdsgrqIEYEYKLAQALHEMREQHDAQVRLY--KEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSS 251
Cdd:COG4717 142 --------AELPERLEELEERLEELRELEEELEelEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEE 213
|
170 180 190
....*....|....*....|....*....|.
gi 2217355802 252 QLSNLQKESRACLERIQELEDLLAKEKDNSR 282
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
68-271 |
5.02e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.13 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 68 AKKESDLNGAQIKLREYEAALNSKDAalatalgDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADetllkvdLENRCQSL 147
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLA-------EIEELEREIEEERKRRDKLTEEYAELKEELED-------LRAELEEV 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 148 TEDLE--FRKSM-YEEEINETRRKHEtrlvevDSGRQIEYEYKLAQALHEMREQHDAQVRLYKEELEQtYHAKLENARLS 224
Cdd:TIGR02169 377 DKEFAetRDELKdYREKLEKLKREIN------ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE-LEEEKEDKALE 449
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2217355802 225 SEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELE 271
Cdd:TIGR02169 450 IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
188-335 |
5.40e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 188 LAQALHEMREQHDAqvrlykEELEQTYHAKLENARLSSEMntstvnsaREELMESRMRIESLSSQLSNLQKESRACLERI 267
Cdd:COG2433 378 IEEALEELIEKELP------EEEPEAEREKEHEERELTEE--------EEEIRRLEEQVERLEAEVEELEAELEEKDERI 443
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217355802 268 QELEDLLAKEKDNSRRmltdKEREMAEIRdqmqqqlndyeqlldvklALDMEISAYRKLLEGEEERLK 335
Cdd:COG2433 444 ERLERELSEARSEERR----EIRKDREIS------------------RLDREIERLERELEEERERIE 489
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
68-335 |
6.24e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 6.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 68 AKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADETLLK--VDLENRCQ 145
Cdd:PRK03918 434 AKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEqlKELEEKLK 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 146 SLT-EDLEFRKSMYEEEINETRR-KHETRLVEVDSGRQIEYEYKLAQALHEMREqhdaqvrlyKEELEQTYHAKLENARL 223
Cdd:PRK03918 514 KYNlEELEKKAEEYEKLKEKLIKlKGEIKSLKKELEKLEELKKKLAELEKKLDE---------LEEELAELLKELEELGF 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 224 SSEmntstvnsarEELMESRMRIESLSSQLSNLqKESRACLERIQELEDLLAKEKDNSRRMLTDKEREMAEIRDQMQQQL 303
Cdd:PRK03918 585 ESV----------EELEERLKELEPFYNEYLEL-KDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELE 653
|
250 260 270
....*....|....*....|....*....|....*..
gi 2217355802 304 -----NDYEQLLDVKLALDMEISAYRKLLEGEEERLK 335
Cdd:PRK03918 654 kkyseEEYEELREEYLELSRELAGLRAELEELEKRRE 690
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
80-310 |
9.06e-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: 42.03 E-value: 9.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 80 KLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENR--CQSLTEDlEFRKSM 157
Cdd:pfam15921 343 KIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRdtGNSITID-HLRREL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 158 YEEEINETRRKHETRLVEVDSGRQIEYEYKLAQALHEMREQHD---AQVRLYKEELEQTYHaKLENARLSSEMNTSTVNS 234
Cdd:pfam15921 422 DDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSsltAQLESTKEMLRKVVE-ELTAKKMTLESSERTVSD 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 235 AREELMESRMRIESLSSQLSNLQkeSRACLeRIQELEDlLAKEKDNSRRMLTDKER---EMAE---IRDQMQQQLNDYEQ 308
Cdd:pfam15921 501 LTASLQEKERAIEATNAEITKLR--SRVDL-KLQELQH-LKNEGDHLRNVQTECEAlklQMAEkdkVIEILRQQIENMTQ 576
|
..
gi 2217355802 309 LL 310
Cdd:pfam15921 577 LV 578
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
101-198 |
9.24e-04 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 41.97 E-value: 9.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 101 DKKSLEGDL-------EDLKDQIAQLEASLAAAKKQLADETLLKVDLEN--RCQSLT-EDLEFRKSMYEEEINETRRKHE 170
Cdd:pfam05911 696 EKENLEVELasctenlESTKSQLQESEQLIAELRSELASLKESNSLAETqlKCMAESyEDLETRLTELEAELNELRQKFE 775
|
90 100
....*....|....*....|....*...
gi 2217355802 171 TRLVEVDSGRQIeYEYKLAqALHEMREQ 198
Cdd:pfam05911 776 ALEVELEEEKNC-HEELEA-KCLELQEQ 801
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
71-232 |
1.05e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 71 ESDLNGAQIKLREYEAALNSKDAALATALGDKKSLEGD--LEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLT 148
Cdd:COG3206 225 ESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALR 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 149 EDLEFRKSMYEEEINETRRKHETRLVEVDSgRQIEYEYKLAQA------LHEMREQHDAQVRLYkeeleQTYHAKLENAR 222
Cdd:COG3206 305 AQLQQEAQRILASLEAELEALQAREASLQA-QLAQLEARLAELpeleaeLRRLEREVEVARELY-----ESLLQRLEEAR 378
|
170
....*....|
gi 2217355802 223 LSSEMNTSTV 232
Cdd:COG3206 379 LAEALTVGNV 388
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
102-332 |
1.44e-03 |
|
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: 41.63 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 102 KKSLEGDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTEDLEfRKSMYEEEINETRRKHETRlVEVDSGRQ 181
Cdd:pfam05483 554 REEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIE-NKNKNIEELHQENKALKKK-GSAENKQL 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 182 IEYEYKLAQALHEMreqhdAQVRLYKEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESR 261
Cdd:pfam05483 632 NAYEIKVNKLELEL-----ASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMV 706
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217355802 262 ACLERIQELEDLLAKEKDNSRRMLTDKEREMAEIRDQMQQQLNDYE-QLLDVKLALDMEISAYRKLLEGEEE 332
Cdd:pfam05483 707 ALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKaELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
109-335 |
1.62e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 109 LEDLKDQIAQLEASLAAAKKQLADetllkvdlenrcqsltedleFRKSMYEEEINETRRKHETRLVEVDSgrqieyeyKL 188
Cdd:COG3206 177 LEFLEEQLPELRKELEEAEAALEE--------------------FRQKNGLVDLSEEAKLLLQQLSELES--------QL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 189 AQALHEMREQhDAQVRLYKEELEQTyhakleNARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQ 268
Cdd:COG3206 229 AEARAELAEA-EARLAALRAQLGSG------PDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIA 301
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217355802 269 ELEDLLAKEK-------DNSRRMLTDKEREMAEIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLLEGEEERLK 335
Cdd:COG3206 302 ALRAQLQQEAqrilaslEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
57-132 |
1.71e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 1.71e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217355802 57 APPASPGQVSYAKKESDLNGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLAD 132
Cdd:COG3883 8 APTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE 83
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
69-327 |
1.79e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 69 KKESDLNGAQIKLREYEA---ALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQ---------LADETLL 136
Cdd:PRK03918 218 ELREELEKLEKEVKELEElkeEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkelkelkeKAEEYIK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 137 KVDLENRCQSLTEDLEFRKSMYEEEINETRRKHETRLVEVDSGRQIEYEYK-LAQALHEMREQHDA--QVRLYKEELEQT 213
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKeLEKRLEELEERHELyeEAKAKKEELERL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 214 YHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQEledllAKEK-DNSRRMLTDKER-- 290
Cdd:PRK03918 378 KKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK-----AKGKcPVCGRELTEEHRke 452
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2217355802 291 -------EMAEIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLL 327
Cdd:PRK03918 453 lleeytaELKRIEKELKEIEEKERKLRKELRELEKVLKKESELI 496
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
77-341 |
1.80e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 77 AQIKLREYEAALNSKDAALATALGDKksleGDLEDLKDQIAQLEASLAAAKKQLAdetllkvDLENRCQSLTEDLefrks 156
Cdd:COG4913 659 DEIDVASAEREIAELEAELERLDASS----DDLAALEEQLEELEAELEELEEELD-------ELKGEIGRLEKEL----- 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 157 myeEEINETRRKHETRLVEVDSGRQIEYEYKLAQALHEmreqhdaqvrLYKEELEQTYHAKLENARlssEMNTSTVNSAR 236
Cdd:COG4913 723 ---EQAEEELDELQDRLEAAEDLARLELRALLEERFAA----------ALGDAVERELRENLEERI---DALRARLNRAE 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 237 EELMESRMR--------IESLSSQLSNLQkESRACLERIQElEDLLAKEKDNSRRMLTDKEREMAEIRDQMQQQLND-YE 307
Cdd:COG4913 787 EELERAMRAfnrewpaeTADLDADLESLP-EYLALLDRLEE-DGLPEYEERFKELLNENSIEFVADLLSKLRRAIREiKE 864
|
250 260 270
....*....|....*....|....*....|....
gi 2217355802 308 QLLDVKLALdmeisayRKLLEGEEERLKLSPSPS 341
Cdd:COG4913 865 RIDPLNDSL-------KRIPFGPGRYLRLEARPR 891
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
69-193 |
1.95e-03 |
|
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: 40.39 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 69 KKESDLNGAQIKLREYEAALNSKDAALATALGDKKSL-EGDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSL 147
Cdd:smart00787 165 KELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCdPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDL 244
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2217355802 148 TEDlefrKSMYEEEINETRRKHET-RLVEVDSGRQIEYEYKLAQALH 193
Cdd:smart00787 245 TNK----KSELNTEIAEAEKKLEQcRGFTFKEIEKLKEQLKLLQSLT 287
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
81-328 |
2.25e-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: 40.93 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 81 LREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEAslAAAKKQLAdetllKVDLENRCQSLTEDLEFRKSMyEE 160
Cdd:pfam01576 77 LHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEA--ARQKLQLE-----KVTTEAKIKKLEEDILLLEDQ-NS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 161 EINETRRKHETRLVEVDSgrQIEYEYKLAQALHEMREQHDA-----QVRLYKEELEQTyhaKLENARLSSEMNTSTvnsA 235
Cdd:pfam01576 149 KLSKERKLLEERISEFTS--NLAEEEEKAKSLSKLKNKHEAmisdlEERLKKEEKGRQ---ELEKAKRKLEGESTD---L 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 236 REELMESRMRIESLSSQLSNLQKESRACLERIQEledlLAKEKDNSRRMLTDKEREMAEIRDQMQQQLNDYEQLLDVKLA 315
Cdd:pfam01576 221 QEQIAELQAQIAELRAQLAKKEEELQAALARLEE----ETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRD 296
|
250
....*....|...
gi 2217355802 316 LDMEISAYRKLLE 328
Cdd:pfam01576 297 LGEELEALKTELE 309
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
69-335 |
3.08e-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: 40.39 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 69 KKESDLNGAQIKLREYEAA-LNSKDAALATalgDKKSLEGDLEDLKDQIAQLEASLAAAKKQL-ADETLLKV-------- 138
Cdd:TIGR04523 137 KKNIDKFLTEIKKKEKELEkLNNKYNDLKK---QKEELENELNLLEKEKLNIQKNIDKIKNKLlKLELLLSNlkkkiqkn 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 139 --------DLENRCQSLTEDLEFRKSMYEEEINETRRKHETRLVEVDSgrQIEYEYKLAQALHEMrEQHDAQVRLYKEEL 210
Cdd:TIGR04523 214 kslesqisELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDE--QNKIKKQLSEKQKEL-EQNNKKIKELEKQL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 211 eQTYHAKLENarLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELE-DLLAKEKDNS--RRMLTD 287
Cdd:TIGR04523 291 -NQLKSEISD--LNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKkELTNSESENSekQRELEE 367
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2217355802 288 KEREMAEIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLLEGEEERLK 335
Cdd:TIGR04523 368 KQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIK 415
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
187-335 |
3.09e-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: 40.43 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 187 KLAQALHEMREQ-HDAQVRLYKEELEQtYHAKLENARLSSEMNTSTVNSAR-------EELMESRMRIESLSSQLSNLQK 258
Cdd:TIGR02168 210 EKAERYKELKAElRELELALLVLRLEE-LREELEELQEELKEAEEELEELTaelqeleEKLEELRLEVSELEEEIEELQK 288
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217355802 259 ESRACLERIQELEDLLaKEKDNSRRMLTDKEREMAEIRDQMQQQLNDYEQLLDvklALDMEISAYRKLLEGEEERLK 335
Cdd:TIGR02168 289 ELYALANEISRLEQQK-QILRERLANLERQLEELEAQLEELESKLDELAEELA---ELEEKLEELKEELESLEAELE 361
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
153-308 |
4.38e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 153 FRKSMYEEEINETRRKHEtRLVEvDSGRQIEYEYKLA-----QALHEMREQHDAQVRLYKEELEQtyhakLENARLSSEM 227
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAK-RILE-EAKKEAEAIKKEAlleakEEIHKLRNEFEKELRERRNELQK-----LEKRLLQKEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 228 N----TSTVNSAREELMESRMRIESLSSQLSNLQKE-SRACLERIQELEDLLAKEKDNSRRMLTDKEREmaEIRDQMQQQ 302
Cdd:PRK12704 97 NldrkLELLEKREEELEKKEKELEQKQQELEKKEEElEELIEEQLQELERISGLTAEEAKEILLEKVEE--EARHEAAVL 174
|
....*.
gi 2217355802 303 LNDYEQ 308
Cdd:PRK12704 175 IKEIEE 180
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
69-334 |
5.57e-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: 39.77 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 69 KKESDLNGAQIKLREYE---AALNSKDAALATAL----GDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLE 141
Cdd:pfam01576 409 KLEGQLQELQARLSESErqrAELAEKLSKLQSELesvsSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLS 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 142 NRCQSLTEDLEFRKSMYEEEInETRRKHETRLVEV-----DSGRQIEYEYKLAQALHEMREQHDAQVRLYKEELEQTYHA 216
Cdd:pfam01576 489 TRLRQLEDERNSLQEQLEEEE-EAKRNVERQLSTLqaqlsDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAA 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 217 --KLENARlssemntstvNSAREELMESRMRIESLSSQLSNLQKESRacleriqELEDLLAKEKDNSRRMLTDKEREMAE 294
Cdd:pfam01576 568 ydKLEKTK----------NRLQQELDDLLVDLDHQRQLVSNLEKKQK-------KFDQMLAEEKAISARYAEERDRAEAE 630
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2217355802 295 IRDQMQQQLNDYEQLLDVKLALDmEISAYRKLLEGEEERL 334
Cdd:pfam01576 631 AREKETRALSLARALEEALEAKE-ELERTNKQLRAEMEDL 669
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
103-305 |
5.85e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 39.72 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 103 KSLEGDLEDLKDQIAQLEASLAAAKKQLADET-LLKVDLENRCQSLTEDLEFRKSMYEEEINETRRKHETrlveVDSGRQ 181
Cdd:pfam15921 227 RELDTEISYLKGRIFPVEDQLEALKSESQNKIeLLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANS----IQSQLE 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 182 IEYEYKLAQALHEMREQHD-----AQVRLYKEELEQTYHAKLEnarlssEMNTSTVnSAREELMESRMRIESLSSQLSNL 256
Cdd:pfam15921 303 IIQEQARNQNSMYMRQLSDlestvSQLRSELREAKRMYEDKIE------ELEKQLV-LANSELTEARTERDQFSQESGNL 375
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2217355802 257 QKESRACLERIQELEDLLAKEKDNSRRmLTDKEREMAEIRDQMQQQLND 305
Cdd:pfam15921 376 DDQLQKLLADLHKREKELSLEKEQNKR-LWDRDTGNSITIDHLRRELDD 423
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
66-132 |
6.31e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 38.94 E-value: 6.31e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217355802 66 SYAKKESDLNGAQIKLR-----EYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLAD 132
Cdd:TIGR04320 236 SYIADGNKFDKTPIPNPpnslaALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELAN 307
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
92-277 |
6.59e-03 |
|
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: 38.37 E-value: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 92 DAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTEDLEfrksmyeeeinetrrKHET 171
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK---------------KYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 172 RLVEVDSGRQIEyeyklaQALHEMREQHDAQVRLYKEELEQtyHAKLENARLSSEMNTSTVNSAREELMEsrmRIESLSS 251
Cdd:COG1579 81 QLGNVRNNKEYE------ALQKEIESLKRRISDLEDEILEL--MERIEELEEELAELEAELAELEAELEE---KKAELDE 149
|
170 180
....*....|....*....|....*.
gi 2217355802 252 QLSNLQKESRACLERIQELEDLLAKE 277
Cdd:COG1579 150 ELAELEAELEELEAEREELAAKIPPE 175
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
64-296 |
6.71e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 39.33 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 64 QVSYAKKESDLNGAQIKLREYEAALNSKDAALatalgdkKSLEGDLEDLKDQIAQL----EASLAAAK--KQLADETLLK 137
Cdd:pfam15921 589 QVEKAQLEKEINDRRLELQEFKILKDKKDAKI-------RELEARVSDLELEKVKLvnagSERLRAVKdiKQERDQLLNE 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 138 V-DLENRCQSLTEDLEFRKSMYE---EEINETRRKHETRL----------------VEVDSGRQIEYEYKLAQALHEMRE 197
Cdd:pfam15921 662 VkTSRNELNSLSEDYEVLKRNFRnksEEMETTTNKLKMQLksaqseleqtrntlksMEGSDGHAMKVAMGMQKQITAKRG 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 198 QHDA---QVRLYKEEL----EQTYHAKLENARLSSEMNT--STVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQ 268
Cdd:pfam15921 742 QIDAlqsKIQFLEEAMtnanKEKHFLKEEKNKLSQELSTvaTEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFA 821
|
250 260
....*....|....*....|....*...
gi 2217355802 269 ELEDLLAKEKDNSRRMLTDKEREMAEIR 296
Cdd:pfam15921 822 ECQDIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
108-331 |
7.81e-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: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 108 DLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTEDLEFRKSMYEEEINETRRKHETRLVEVDSGRQIEYEYK 187
Cdd:COG5185 237 GFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 188 LAQALHEmrEQHDAQVRLYKEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRmRIESLSSQLSNLQKESRACLERI 267
Cdd:COG5185 317 QLAAAEA--EQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEV-ELSKSSEELDSFKDTIESTKESL 393
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217355802 268 QEL-EDLLAKEKDNSR---RMLTDKEREMAEIRDQMQQQLNDYEQLLDVKLALDMEISAYRKLLEGEE 331
Cdd:COG5185 394 DEIpQNQRGYAQEILAtleDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEES 461
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
81-299 |
8.19e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 37.88 E-value: 8.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 81 LREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQlADETLLKVDLEnrcqsltedlefRKSMYEE 160
Cdd:COG1842 32 IRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEK-GREDLAREALE------------RKAELEA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 161 EINETRRKHETRLVEVDsgrqieyeyKLAQALHEMReqhdAQVRLYKEELEqTYHAKLENARLSSEMNTSTVNSAREELM 240
Cdd:COG1842 99 QAEALEAQLAQLEEQVE---------KLKEALRQLE----SKLEELKAKKD-TLKARAKAAKAQEKVNEALSGIDSDDAT 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 241 ESRMRIEslssqlsnlqkesraclERIQELE------DLLAKEKDNSRRML-----TDKEREMAEIRDQM 299
Cdd:COG1842 165 SALERME-----------------EKIEEMEaraeaaAELAAGDSLDDELAeleadSEVEDELAALKAKM 217
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
106-335 |
8.93e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.17 E-value: 8.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 106 EGDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENRCQSLTEDLEFRKSMYEEEINEtrrkhetRLVEVDSgrqieye 185
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLAD-------RVEEIRE------- 901
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 186 yKLAQALHEMR--EQHDAQVrlykEELEQTYhaklenarlssemntSTVNSAREELMESRMRIESLSSQLSNLQKESRAC 263
Cdd:PRK04863 902 -QLDEAEEAKRfvQQHGNAL----AQLEPIV---------------SVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFAL 961
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 264 LERIQ--------ELEDLLAKEKDNS---RRMLTDKEREMAEIRDQM---QQQLNDYEQLLdvkLALDMEISAYRKLLEG 329
Cdd:PRK04863 962 TEVVQrrahfsyeDAAEMLAKNSDLNeklRQRLEQAEQERTRAREQLrqaQAQLAQYNQVL---ASLKSSYDAKRQMLQE 1038
|
....*.
gi 2217355802 330 EEERLK 335
Cdd:PRK04863 1039 LKQELQ 1044
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
71-305 |
8.95e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 38.84 E-value: 8.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 71 ESDLNGAQIKLREYEAALNSKDAALATALGDKK--SLEGDLEDLKDQIAQLEASLAAAKKQLADETLLKVDLENrcqslt 148
Cdd:COG3206 188 RKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQlsELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ------ 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 149 edlefrksmyeeeiNETRRKHETRLVEVDSgrqieyeyKLAQALHEMREQHdAQVRLYKEELEQTyhakleNARLSSEMN 228
Cdd:COG3206 262 --------------SPVIQQLRAQLAELEA--------ELAELSARYTPNH-PDVIALRAQIAAL------RAQLQQEAQ 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217355802 229 tSTVNSAREELMESRMRIESLSSQLSNLQKESRACLERIQELEDlLAKEKDNSRRMLTDKEREMAEIRDQMQQQLND 305
Cdd:COG3206 313 -RILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR-LEREVEVARELYESLLQRLEEARLAEALTVGN 387
|
|
| PilO |
COG3167 |
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures]; |
86-134 |
9.13e-03 |
|
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
Pssm-ID: 442400 [Multi-domain] Cd Length: 202 Bit Score: 37.62 E-value: 9.13e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2217355802 86 AALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADET 134
Cdd:COG3167 49 EELEAEEAQLKQELEKKQAKAANLPALKAQLEELEQQLGELLKQLPSKA 97
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
80-332 |
9.96e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 38.62 E-value: 9.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 80 KLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLAAAKKQLADetllkvdLENRCQSLTEDLEFRKSMYE 159
Cdd:pfam01576 750 QVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK-------LQAQMKDLQRELEEARASRD 822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 160 EEIN---ETRRKHETRLVEV-----------DSGRQIEYEYKLAQ-----------ALHEMREQHDAQVRLYKEELEQ-- 212
Cdd:pfam01576 823 EILAqskESEKKLKNLEAELlqlqedlaaseRARRQAQQERDELAdeiasgasgksALQDEKRRLEARIAQLEEELEEeq 902
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217355802 213 -------------TYHAKLENARLSSEMNTSTVN-SAREEL----MESRMRIESLSSQLSNLQKESRACLE-RIQELEDL 273
Cdd:pfam01576 903 sntellndrlrksTLQVEQLTTELAAERSTSQKSeSARQQLerqnKELKAKLQEMEGTVKSKFKSSIAALEaKIAQLEEQ 982
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217355802 274 L---AKEKDNSRRMLTDKEREMAEIRDQMQQQLNDYEQLLDV--KLALDMEiSAYRKLLEGEEE 332
Cdd:pfam01576 983 LeqeSRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQaeKGNSRMK-QLKRQLEEAEEE 1045
|
|
| |
