|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
96-407 |
4.56e-143 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 411.62 E-value: 4.56e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 96 NEKETMQSLNDRLAGYLEKVRQLEQENASLESRIREWCEQQVPYMCPDYQSYFRTIEELQKKTLCSKAENARLVVEIDNA 175
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 176 KLAADDFRTKYETEVSLRQLVESDINGLRRILDDLTLCKSDLEAQVESLKEELLCLKKNHEEEVNSLRCQLGD-RLNVEV 254
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDtQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 255 DAAPPVDLNRVLEEMRCQYETLVENNRRDAEDWLDTQSEELNQQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHSMR 334
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 94538345 335 DALESTLAETEARYSSQLAQMQCMITNVEAQLAEIRADLERQNQEYQVLLDVRARLECEINTYRGLLESEDSK 407
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
151-403 |
4.90e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.16 E-value: 4.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 151 IEELQKKTLCSKAENARLVVEIDNAKLAADDFRTKYETEVSLRQLVESDINGLRRILDDLTLCKSDLEAQVESLKEELLC 230
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 231 LKKNhEEEVNSLRCQLGDRLnvEVDAAPPVDLNRVLEEMRCQYETLVENNRRDAEDW---------LDTQSEELNQQVVS 301
Cdd:TIGR02168 314 LERQ-LEELEAQLEELESKL--DELAEELAELEEKLEELKEELESLEAELEELEAELeelesrleeLEEQLETLRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 302 SSEQLQSCQAEIIELRRTVNALEIELQAQHSMRDALESTLAETE-ARYSSQLAQMQCMITNVEAQLAEIRADLERQNQEY 380
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
250 260
....*....|....*....|...
gi 94538345 381 QVLLDVRARLECEINTYRGLLES 403
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQARLDS 493
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
158-408 |
7.33e-11 |
|
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: 64.69 E-value: 7.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 158 TLCSKAENARLVVEIDNAKLAADDFRTKYETEVSLRQLVESDINGLRRILDDLtlcksdlEAQVESLKEELlclkKNHEE 237
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL-------SRQISALRKDL----ARLEA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 238 EVNSLRCQLgDRLNVEvdaappvdLNRVLEEMRCQYETLVENNRRDAEdwLDTQSEELNQQVVSSSEQLQSCQAEIIELR 317
Cdd:TIGR02168 741 EVEQLEERI-AQLSKE--------LTELEAEIEELEERLEEAEEELAE--AEAEIEELEAQIEQLKEELKALREALDELR 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 318 RTVNALEIELQAQHSMRDALESTLAETEARY---SSQLAQMQCMITNVEAQLAEIRADLERQNQEYQVLLDVRARLECEI 394
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRLedlEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
250
....*....|....
gi 94538345 395 NTYRGLLESEDSKL 408
Cdd:TIGR02168 890 ALLRSELEELSEEL 903
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
111-408 |
5.95e-10 |
|
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: 61.67 E-value: 5.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 111 YLEKVRQLEQENASLESRIREwceqqvpymcpDYQSYFRTIEELQKKTLCSKAENARLVVEIDN------------AKLA 178
Cdd:pfam15921 315 YMRQLSDLESTVSQLRSELRE-----------AKRMYEDKIEELEKQLVLANSELTEARTERDQfsqesgnlddqlQKLL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 179 ADdfRTKYETEVSL-----RQLVESD------INGLRRILDDLTLCKSDLEAQVESLKEE--------LLCLKKNHE--E 237
Cdd:pfam15921 384 AD--LHKREKELSLekeqnKRLWDRDtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSEcqgqmerqMAAIQGKNEslE 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 238 EVNSLRCQLGDRLNVevdaappvdLNRVLEEMRCQYETLvENNRRDAEDwldtqseeLNQQVVSSSEQLQSCQAEIIELR 317
Cdd:pfam15921 462 KVSSLTAQLESTKEM---------LRKVVEELTAKKMTL-ESSERTVSD--------LTASLQEKERAIEATNAEITKLR 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 318 RTVNALEIELQAQHSMRDALESTLAETEArYSSQLAQMQCMITNVEAQLAEIRADLERQNQEYQVLLDVRARLECEINTY 397
Cdd:pfam15921 524 SRVDLKLQELQHLKNEGDHLRNVQTECEA-LKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDR 602
|
330
....*....|.
gi 94538345 398 RglLESEDSKL 408
Cdd:pfam15921 603 R--LELQEFKI 611
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
161-376 |
1.08e-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: 56.70 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 161 SKAENARLVVEIDNAKLAADDFRTKYETEVSLRQLVESDINGLRRILDDLTLCKSDLEAQVESLKEELLCLKKNHEEEVN 240
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 241 SLRCQLG--------DRLNVEVDAAPPVDLNRVLEEMRcqyeTLVENNRRDAEDwLDTQSEELNQQVvsssEQLQSCQAE 312
Cdd:COG4942 105 ELAELLRalyrlgrqPPLALLLSPEDFLDAVRRLQYLK----YLAPARREQAEE-LRADLAELAALR----AELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 94538345 313 IIELRRTVNALEIELQAQHSMRDALESTLAETEARYSSQLAQMQCMITNVEAQLAEIRADLERQ 376
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
114-391 |
1.61e-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: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 114 KVRQLEQENASLESRIREwCEQQVpymcpdyQSYFRTIEELQKKTLCSKAENARLVVEIDNAKLAADDFRTKYETEVSLR 193
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAE-LEKAL-------AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 194 QLVESD-------INGLRRILDDLTLCKSDLEAQVESLKEELlclkKNHEEEVNSLRCQLgDRLNVEVDAappvdlnrvL 266
Cdd:TIGR02168 750 AQLSKElteleaeIEELEERLEEAEEELAEAEAEIEELEAQI----EQLKEELKALREAL-DELRAELTL---------L 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 267 EEMRCQYETLVENNRRDAEDWlDTQSEELNQQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHSMRDALESTLAETEA 346
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAAT-ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 94538345 347 RYSSQLAQMQcmitNVEAQLAEIRADLERQNQEyqvLLDVRARLE 391
Cdd:TIGR02168 895 ELEELSEELR----ELESKRSELRRELEELREK---LAQLELRLE 932
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
215-391 |
1.71e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.95 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 215 SDLEAQVESLKEELlclkknheEEVNSLRCQLGDRLNVEVDAAPPVDLNRVLEEMRCQYETLvenNRRDAEdwLDTQSEE 294
Cdd:COG3206 222 SELESQLAEARAEL--------AEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAEL---EAELAE--LSARYTP 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 295 LNQQVVSSSEQLQSCQAEI-IELRRTVNALEIELQAQHSMRDALESTLAETEARYSSqlaqmqcmITNVEAQLAEIRADL 373
Cdd:COG3206 289 NHPDVIALRAQIAALRAQLqQEAQRILASLEAELEALQAREASLQAQLAQLEARLAE--------LPELEAELRRLEREV 360
|
170
....*....|....*...
gi 94538345 374 ERQNQEYQVLLdvrARLE 391
Cdd:COG3206 361 EVARELYESLL---QRLE 375
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
150-399 |
1.71e-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: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 150 TIEELqkktLCSKAENARLVVEidnakLAADDFRTKYETEVSLRQLVESDINGLRriLDDLTlckSDLEAQVESLKEELL 229
Cdd:TIGR02168 145 KISEI----IEAKPEERRAIFE-----EAAGISKYKERRKETERKLERTRENLDR--LEDIL---NELERQLKSLERQAE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 230 CLKKNHE--EEVNSLRCQL-GDRLNVEVDAAPPvdLNRVLEEMRCQYETLVENNRRdaedwLDTQSEELNQQVVSSSEQL 306
Cdd:TIGR02168 211 KAERYKElkAELRELELALlVLRLEELREELEE--LQEELKEAEEELEELTAELQE-----LEEKLEELRLEVSELEEEI 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 307 QSCQAEIIELRRTVNALEIELQAQHSMRDALESTLAETEAR----------YSSQLAQMQCMITNVEAQLAEIRADLERQ 376
Cdd:TIGR02168 284 EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQleeleskldeLAEELAELEEKLEELKEELESLEAELEEL 363
|
250 260
....*....|....*....|...
gi 94538345 377 NQEYQVLLDVRARLECEINTYRG 399
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRS 386
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
151-391 |
9.74e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 9.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 151 IEELQKKTLCSKAENARLVVEIDNAKLAADDFRTKYETEVSLRQLVESDINGLRRILDDLTLCKSDLEAQVESLKEELLC 230
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 231 LKKNHEEEVNSLRCQLGDRLNVEVDAAppvDLNRVLEEMRCQYETLVENNRRDAEDWLDTQSEELNQQvvsssEQLQSCQ 310
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELE---EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL-----RAAAELA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 311 AEIIELRRTVNALEIELQAQHSMRDALESTLAETEARYSSQLAQMQCMITNVEAQLAEIRADLERQNQEYQVLLDVRARL 390
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
.
gi 94538345 391 E 391
Cdd:COG1196 480 A 480
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
98-379 |
8.62e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 8.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 98 KETMQSLNDRLAGYLEKVRQLEQENASLESRIREwCEQQVPYMCPDYQSYFRTIEELQKKTLCSKAENARLVVEIDNAKL 177
Cdd:TIGR02168 690 EEKIAELEKALAELRKELEELEEELEQLRKELEE-LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 178 AADDFRTKYETEVSLRQLVESDINGLRRILDDLTLCKSDLEAQVESLKEELLCLK---KNHEEEVNSLRCQLGDRLN-VE 253
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRerlESLERRIAATERRLEDLEEqIE 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 254 VDAAPPVDLNRVLEEMrcqyETLVENNRRDAEDWLDtQSEELNQQVVSSSEQLQSCQAEIIELRRTVNALE---IELQAQ 330
Cdd:TIGR02168 849 ELSEDIESLAAEIEEL----EELIEELESELEALLN-ERASLEEALALLRSELEELSEELRELESKRSELRrelEELREK 923
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 331 HS-----------MRDALESTLAEteaRYSSQLAQMQCMITNVEAQLAEIRADLERQNQE 379
Cdd:TIGR02168 924 LAqlelrleglevRIDNLQERLSE---EYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
192-332 |
1.60e-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: 49.63 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 192 LRQLVESDINGLRRildDLTLCKSDLEaQVESLKEELLCLKKNHEEEVNSLRcqlgdRLNVEVDAAPPVDLNRVLEEMRC 271
Cdd:smart00787 145 LKEGLDENLEGLKE---DYKLLMKELE-LLNSIKPKLRDRKDALEEELRQLK-----QLEDELEDCDPTELDRAKEKLKK 215
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 94538345 272 QYETLVENNRRDAEdwLDTQSEELNQQVVSSSEQLQSCQAEIIELRRTVN------ALEIE-LQAQHS 332
Cdd:smart00787 216 LLQEIMIKVKKLEE--LEEELQELESKIEDLTNKKSELNTEIAEAEKKLEqcrgftFKEIEkLKEQLK 281
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
193-391 |
2.06e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 193 RQLVESDINGLRRILDDLTLCKSDLEAQVESLKEELLCLKKNHEEEVNSLRCQLGDRLNVEVDAappvdlnRVLEEMRcq 272
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI-------ARLEERR-- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 273 yetlvENNRRDAEDwLDTQSEELNQQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHSMRDALESTLAETEARYSSQL 352
Cdd:COG1196 312 -----RELEERLEE-LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
170 180 190
....*....|....*....|....*....|....*....
gi 94538345 353 AQMQcmitNVEAQLAEIRADLERQNQEYQVLLDVRARLE 391
Cdd:COG1196 386 EELL----EALRAAAELAAQLEELEEAEEALLERLERLE 420
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
185-408 |
2.51e-06 |
|
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: 50.07 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 185 KYETEVSLRQLVESDINGLRRILDDLTLCKSDLEAQVESLKEEL----LCLKKNHEEEVNSLRCQLGDrlnVEVDAAPPV 260
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLeelnKKIKDLGEEEQLRVKEKIGE---LEAEIASLE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 261 DLNRV-------LEEMRCQYETLVENNRRDAEDwLDTQSEELNQQVVSSSEQLQSCQAEIIELRRTVNALEIELQA---- 329
Cdd:TIGR02169 308 RSIAEkereledAEERLAKLEAEIDKLLAEIEE-LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAEtrde 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 330 QHSMRDALE-------------STLAETEARYSSQLAQMQCMITNVEAQLA-----------EIRADLERQNQEYQVLLD 385
Cdd:TIGR02169 387 LKDYREKLEklkreinelkrelDRLQEELQRLSEELADLNAAIAGIEAKINeleeekedkalEIKKQEWKLEQLAADLSK 466
|
250 260
....*....|....*....|...
gi 94538345 386 VRARLECEINTYRgLLESEDSKL 408
Cdd:TIGR02169 467 YEQELYDLKEEYD-RVEKELSKL 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-345 |
5.85e-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: 48.90 E-value: 5.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 101 MQSLNDRLAGYLEKVRQLEQENASLESRIREWcEQQVPYMCPDYQSYFRTIEELQKKTLCSKAENARLV-------VEID 173
Cdd:TIGR02168 276 VSELEEEIEELQKELYALANEISRLEQQKQIL-RERLANLERQLEELEAQLEELESKLDELAEELAELEekleelkEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 174 NAKLAADDFRTKYETEVSLRQLVESDINGLRRILDDLTLCKSDLEAQVESLKEELLCLKKNHEEEVNSLRCQLGDRLNVE 253
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 254 VDA--APPVDLNRVLEEMRCQYETLVENNRRdaedwLDTQSEELNQQVVSSSEQLQSCQAEIielrrtvnaleielqaqh 331
Cdd:TIGR02168 435 LKElqAELEELEEELEELQEELERLEEALEE-----LREELEEAEQALDAAERELAQLQARL------------------ 491
|
250
....*....|....
gi 94538345 332 smrDALESTLAETE 345
Cdd:TIGR02168 492 ---DSLERLQENLE 502
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
97-408 |
1.32e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 97 EKETMQSLNDRLAGYLEKVRQLEQENASLESRIREWCEQqvpymcpdyqsyfrtIEELQKKT--LCSKAENARLVVEIDN 174
Cdd:PRK03918 229 EVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEER---------------IEELKKEIeeLEEKVKELKELKEKAE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 175 AKLAADDFRTKY-----ETEVSLRQLvESDINGLRRILDDLTLCKS---DLEAQVESLKEELLCLKKNHE--EEVNSLRC 244
Cdd:PRK03918 294 EYIKLSEFYEEYldelrEIEKRLSRL-EEEINGIEERIKELEEKEErleELKKKLKELEKRLEELEERHElyEEAKAKKE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 245 QLgDRLNVEVDAAPPVDLNRVLEEMRCQYETLVEN----NRRDAEdwLDTQSEELNQQVvsssEQLQS-------CQAEI 313
Cdd:PRK03918 373 EL-ERLKKRLTGLTPEKLEKELEELEKAKEEIEEEiskiTARIGE--LKKEIKELKKAI----EELKKakgkcpvCGREL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 314 IE---------LRRTVNALEIELQAQHSMRDALESTLAETEARYSSQ-----LAQMQCMITNVEAQLAEIRA-DLERQNQ 378
Cdd:PRK03918 446 TEehrkelleeYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKEselikLKELAEQLKELEEKLKKYNLeELEKKAE 525
|
330 340 350
....*....|....*....|....*....|
gi 94538345 379 EYQVLLDVRARLECEINTyrglLESEDSKL 408
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIKS----LKKELEKL 551
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
299-406 |
1.75e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 299 VVSSSEQLQSCQAEIIELRRTVNALEIELQAQHSMRDALESTLAETEAR----------YSSQLAQMQCMITNVEAQLAE 368
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRiaalarriraLEQELAALEAELAELEKEIAE 94
|
90 100 110
....*....|....*....|....*....|....*...
gi 94538345 369 IRADLERQNQEYQVLLDVRARLEcEINTYRGLLESEDS 406
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLG-RQPPLALLLSPEDF 131
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
194-379 |
1.93e-05 |
|
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: 45.69 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 194 QLVESDINGLRRILDDLTLCKSDLEAQVESLKEELlclkKNHEEEVNSLRCQLgDRLNVEVDAAppvdlnrvleemrcqy 273
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARL----EAAKTELEDLEKEI-KRLELEIEEV---------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 274 ETLVENNRrdaedwldtqsEELNQqvVSSSEQLQSCQAEIIELRRTVNALEIELQAQHSMRDALESTLAETEARYSSQLA 353
Cdd:COG1579 72 EARIKKYE-----------EQLGN--VRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA 138
|
170 180
....*....|....*....|....*.
gi 94538345 354 QMQCMITNVEAQLAEIRADLERQNQE 379
Cdd:COG1579 139 ELEEKKAELDEELAELEAELEELEAE 164
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
150-391 |
2.36e-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: 47.09 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 150 TIEELQKKTLCSKAENARLVVEI-DNAKLAADDFRTKYETEVSLRQLvESDINGLRRILDDLTLCKSDLEAQVESLKEEL 228
Cdd:pfam01576 448 LLNEAEGKNIKLSKDVSSLESQLqDTQELLQEETRQKLNLSTRLRQL-EDERNSLQEQLEEEEEAKRNVERQLSTLQAQL 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 229 LCLKKNHEEEVNSLRC--QLGDRLNVEVDAappvdLNRVLEEMRCQYETLVENNRRDAEDWLDTQSEELNQ-QVVSSSEQ 305
Cdd:pfam01576 527 SDMKKKLEEDAGTLEAleEGKKRLQRELEA-----LTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQrQLVSNLEK 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 306 LQ-------------SCQ---------AEIIELRRTVNALEIELQAQHSMRDALESTL----AETEARYSSQ------LA 353
Cdd:pfam01576 602 KQkkfdqmlaeekaiSARyaeerdraeAEAREKETRALSLARALEEALEAKEELERTNkqlrAEMEDLVSSKddvgknVH 681
|
250 260 270
....*....|....*....|....*....|....*...
gi 94538345 354 QMQCMITNVEAQLAEIRADLERQNQEYQVLLDVRARLE 391
Cdd:pfam01576 682 ELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLE 719
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
151-407 |
2.36e-05 |
|
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: 46.97 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 151 IEEL--QKKTLCSKAENA----RLVVEIDNAKLAA-----DDFRTKYETevslrqlVESDINGLRRILDDLTLCKSDLEA 219
Cdd:TIGR02168 195 LNELerQLKSLERQAEKAerykELKAELRELELALlvlrlEELREELEE-------LQEELKEAEEELEELTAELQELEE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 220 QVESLKEELLCLkknhEEEVNSLRCQLGDrLNVEVDaappvDLNRVLEEMRCQYETLVENNRRdaedwLDTQSEELNQQV 299
Cdd:TIGR02168 268 KLEELRLEVSEL----EEEIEELQKELYA-LANEIS-----RLEQQKQILRERLANLERQLEE-----LEAQLEELESKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 300 VSSSEQLQSCQAEIIELRRTVNALEIELQAQHSMRDALESTLAETEA---RYSSQLAQMqcmitnvEAQLAEIRADLERQ 376
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEqleTLRSKVAQL-------ELQIASLNNEIERL 405
|
250 260 270
....*....|....*....|....*....|.
gi 94538345 377 NQEYQVLLDVRARLECEINTYRGLLESEDSK 407
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKLEEAELK 436
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
236-389 |
2.67e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 236 EEEVNSLRCQLgDRLNVEVDAappvdLNRVLEEMRCQYETLvENNRRDAEDWLDTQSEELNQqvvsSSEQLQSCQAEIIE 315
Cdd:COG4372 44 QEELEQLREEL-EQAREELEQ-----LEEELEQARSELEQL-EEELEELNEQLQAAQAELAQ----AQEELESLQEEAEE 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 94538345 316 LRRTVNALEIELQAQHSMRDALESTLAETEARYSSQLAQMQcmitNVEAQLAEIRADLERQNQEYQVLLDVRAR 389
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK----ELEEQLESLQEELAALEQELQALSEAEAE 182
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
191-391 |
2.73e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 191 SLRQLVESDINgLRRiLDDLTlckSDLEAQVESLKEE----LLCLKKNHEEEVNSLRCQLGDRLNVEVDAAppvDLNRVL 266
Cdd:COG1196 177 AERKLEATEEN-LER-LEDIL---GELERQLEPLERQaekaERYRELKEELKELEAELLLLKLRELEAELE---ELEAEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 267 EEMRCQYETLVENNRRdaedwLDTQSEELNQQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHSMRDALESTLAETEA 346
Cdd:COG1196 249 EELEAELEELEAELAE-----LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 94538345 347 RYSSQLAQmqcmITNVEAQLAEIRADLERQNQEYQVLLDVRARLE 391
Cdd:COG1196 324 ELAELEEE----LEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
97-406 |
2.86e-05 |
|
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: 46.49 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 97 EKETMQSLNDRLAGYLEKVRQLEQ----ENASLESRIREWCEQQVPymcpdyqSYFRTIEELQKKTlcsKAENARLVVEI 172
Cdd:COG5185 244 ELEDLAQTSDKLEKLVEQNTDLRLeklgENAESSKRLNENANNLIK-------QFENTKEKIAEYT---KSIDIKKATES 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 173 DNAKLAADDFRTKY-----ETEVSLRQLVESDINGLRRILDDLTLCKSDL-----EAQVESLKEELLCLKKNHEEEVNSL 242
Cdd:COG5185 314 LEEQLAAAEAEQELeeskrETETGIQNLTAEIEQGQESLTENLEAIKEEIenivgEVELSKSSEELDSFKDTIESTKESL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 243 RCQLGDRLNVEVDAAPPVDlnrvleemrcqyETLVENNRRDAEdwLDTQSEELNQQVVSSSEQLQSCQAEIIELRRTVNA 322
Cdd:COG5185 394 DEIPQNQRGYAQEILATLE------------DTLKAADRQIEE--LQRQIEQATSSNEEVSKLLNELISELNKVMREADE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 323 LEIELQAQHSmrDALESTLAETEARYSSQLAQMQCMITNVEAQLAEIRADLERQNQEYQVLLDVRARLECEINTYRGLLE 402
Cdd:COG5185 460 ESQSRLEEAY--DEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAH 537
|
....
gi 94538345 403 SEDS 406
Cdd:COG5185 538 ILAL 541
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
102-396 |
2.93e-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: 46.65 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 102 QSLNDRLAGYLEKVRQLEQENAS---LESRIrEWCEQQVPYMcPDYQSYFRTIEELQKKTLCSKAENARLV----VEIDN 174
Cdd:pfam15921 496 RTVSDLTASLQEKERAIEATNAEitkLRSRV-DLKLQELQHL-KNEGDHLRNVQTECEALKLQMAEKDKVIeilrQQIEN 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 175 -AKLAADDFRTKYETEVSLRQLvESDINGLRRILDDLTLCKS-------DLEAQVESLKEELLCLKKNHEEEVNSLR--C 244
Cdd:pfam15921 574 mTQLVGQHGRTAGAMQVEKAQL-EKEINDRRLELQEFKILKDkkdakirELEARVSDLELEKVKLVNAGSERLRAVKdiK 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 245 QLGDRLNVEVDAAPPvDLNRVLEEmrcqYETLVENNRRDAEDwLDTQSEELNQQvvssseqLQSCQAEIIELRRTVNALe 324
Cdd:pfam15921 653 QERDQLLNEVKTSRN-ELNSLSED----YEVLKRNFRNKSEE-METTTNKLKMQ-------LKSAQSELEQTRNTLKSM- 718
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 94538345 325 iELQAQHSMRDALESTLAETEARysSQLAQMQCMITNVEAQLAEiradlerQNQEYQVLLDVRARLECEINT 396
Cdd:pfam15921 719 -EGSDGHAMKVAMGMQKQITAKR--GQIDALQSKIQFLEEAMTN-------ANKEKHFLKEEKNKLSQELST 780
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
112-347 |
4.24e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 112 LEKVRQLEQENASLESRIREW--CEQQVPYmcpdyqsYF--RTIEELQKKTLCSKAENARLVVEIDNAKLAADDFRTKYE 187
Cdd:COG4913 254 LEPIRELAERYAAARERLAELeyLRAALRL-------WFaqRRLELLEAELEELRAELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 188 tevSLRQLVESdiNGLRRIlddltlckSDLEAQVESLKEELlclkknheEEVNSLRCQLGDRLNVeVDAAPPVDLnRVLE 267
Cdd:COG4913 327 ---ELEAQIRG--NGGDRL--------EQLEREIERLEREL--------EERERRRARLEALLAA-LGLPLPASA-EEFA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 268 EMRCQYETLVENnRRDAEDWLDTQSEELNQQVVSSSEQLQSCQAEIIELRRTVNALEielQAQHSMRDALESTLAETEAR 347
Cdd:COG4913 384 ALRAEAAALLEA-LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIP---ARLLALRDALAEALGLDEAE 459
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
304-408 |
5.75e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 5.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 304 EQLQSCQAEIIELRRTVNALEIELQAQHSMRDALESTLAETE---ARYSSQLAQMQCMITNVEAQLAEIRADLERQNQEY 380
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNeqlQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124
|
90 100
....*....|....*....|....*...
gi 94538345 381 QVLLDVRARLECEINTYRGLLESEDSKL 408
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSEIAEREEEL 152
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
98-395 |
6.47e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 98 KETMQSLNDRLAGYLEKVRQLEQENASLESRIREWCE-QQVPYMCPDYQSYFRTIEELQKktlcskaenarlvvEIDNAK 176
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQERREALQRlAEYSWDEIDVASAEREIAELEA--------------ELERLD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 177 LAADDFRTkyetevsLRQLVEsdinGLRRILDDLTLCKSDLEAQVESLKEELlclkKNHEEEVNSLRCQLgdrlnVEVDA 256
Cdd:COG4913 682 ASSDDLAA-------LEEQLE----ELEAELEELEEELDELKGEIGRLEKEL----EQAEEELDELQDRL-----EAAED 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 257 APPVDLNRVLEEMRcqYETLVENNRRDAEDWLDTQSEELNQQVVSSSEQLQSCQAEII--------ELRRTVNALEiELQ 328
Cdd:COG4913 742 LARLELRALLEERF--AAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNrewpaetaDLDADLESLP-EYL 818
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 94538345 329 AqhsMRDALEST-LAETEARYSSQLAqmQCMITNVEAQLAEIRADLErqnqeyqvllDVRARLEcEIN 395
Cdd:COG4913 819 A---LLDRLEEDgLPEYEERFKELLN--ENSIEFVADLLSKLRRAIR----------EIKERID-PLN 870
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
288-408 |
7.50e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 7.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 288 LDTQSEELNQQVVSSSEQLQSCQAEIIELRRTVNALEIEL----------------QAQHSMRDALESTLAETEARYSSQ 351
Cdd:COG3206 210 LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLgsgpdalpellqspviQQLRAQLAELEAELAELSARYTPN 289
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 94538345 352 LAQMQcmitNVEAQLAEIRADLERQNQEYQVLLDV-RARLECEINTYRGLLESEDSKL 408
Cdd:COG3206 290 HPDVI----ALRAQIAALRAQLQQEAQRILASLEAeLEALQAREASLQAQLAQLEARL 343
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
217-403 |
7.83e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 7.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 217 LEAQVESLKEELlclkKNHEEEVNSLRCQ-----LGDRLNVEVDAAppVDLNRVLEEMRCQYETLvENNRRDAEDWLDTQ 291
Cdd:COG3206 180 LEEQLPELRKEL----EEAEAALEEFRQKnglvdLSEEAKLLLQQL--SELESQLAEARAELAEA-EARLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 292 SEEL-----NQQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHSMRDALESTLAETEARYssqLAQMQCMITNVEAQL 366
Cdd:COG3206 253 PDALpellqSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI---LASLEAELEALQARE 329
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 94538345 367 AEIRADLERQNQEYQVLLDVRA---RLECEINTYRGLLES 403
Cdd:COG3206 330 ASLQAQLAQLEARLAELPELEAelrRLEREVEVARELYES 369
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
96-379 |
1.36e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 96 NEKETMQSLNDRLAGYLEKVRQLEQENASLESRIREWCEQqvpymcpdyqsyfrtIEEL--QKKTLCSKAENARlvVEID 173
Cdd:PRK02224 499 ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRER---------------AEELreRAAELEAEAEEKR--EAAA 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 174 NAKLAADDFRTKYETEVSLRQLVESDINGLRRILDDLTLcKSDLEAQVESLKEellclKKNHEEEVNSLRC-QLGDRLNV 252
Cdd:PRK02224 562 EAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAA-IADAEDEIERLRE-----KREALAELNDERReRLAEKRER 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 253 EVDAAPPVDLNRVlEEMRcqyetlveNNRRDAEDWLDTQSEELNQQvvssseqlqscQAEIIELRRTVNALEIELQAQHS 332
Cdd:PRK02224 636 KRELEAEFDEARI-EEAR--------EDKERAEEYLEQVEEKLDEL-----------REERDDLQAEIGAVENELEELEE 695
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 94538345 333 MRD---ALESTLAETEARYSSqlaqmqcmITNVEAQLAEIRADLERQNQE 379
Cdd:PRK02224 696 LRErreALENRVEALEALYDE--------AEELESMYGDLRAELRQRNVE 737
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
165-408 |
1.42e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 165 NARLVVEIDNAKLAADDF------RTKYETEVslrQLVESDINgLRRILDDLTLCKS------DLEAQVESLKEELlclk 232
Cdd:COG3206 56 SATLLVEPQSSDVLLSGLsslsasDSPLETQI---EILKSRPV-LERVVDKLNLDEDplgeeaSREAAIERLRKNL---- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 233 knheeEVNSLRcqLGDRLNVEVDAAPPVDLNRVLEEMrcqYETLVENNRRDAEDWLDTQSEELNQQVVSSSEQLQSCQAE 312
Cdd:COG3206 128 -----TVEPVK--GSNVIEISYTSPDPELAAAVANAL---AEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 313 IIELRRTVNALEIELQAQHSM---------RDALESTLAETEARYSS---QLAQMQCMITNVEA--QLAEIRADLERQNQ 378
Cdd:COG3206 198 LEEFRQKNGLVDLSEEAKLLLqqlselesqLAEARAELAEAEARLAAlraQLGSGPDALPELLQspVIQQLRAQLAELEA 277
|
250 260 270
....*....|....*....|....*....|....*...
gi 94538345 379 EYQVLL--------DVRArLECEINTYRGLLESEDSKL 408
Cdd:COG3206 278 ELAELSarytpnhpDVIA-LRAQIAALRAQLQQEAQRI 314
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
250-373 |
1.95e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 43.30 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 250 LNVEVDAAPPVDLNRVLEEMRCQYETLVEN-NRRDAEDWLDTQSEELNQqvvsSSEQLQSCQAEIIELRRTVNAL--EIE 326
Cdd:COG3524 140 ITLEVRAFDPEDAQAIAEALLAESEELVNQlSERAREDAVRFAEEEVER----AEERLRDAREALLAFRNRNGILdpEAT 215
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 94538345 327 LQAQHSMRDALESTLAETEARY----------SSQLAQMQCMITNVEAQLAEIRADL 373
Cdd:COG3524 216 AEALLQLIATLEGQLAELEAELaalrsylspnSPQVRQLRRRIAALEKQIAAERARL 272
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
106-406 |
2.60e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 106 DRLAGYLEKVRQLEQENASLESRIREWCEQQVPYMCPDYQSYFRTIEELQKKTLCSKAENARLVVEIDNAKLAADDFRTK 185
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 186 YETEVSLRQLVE-------------------SDINGLRRILDDLTLC--------------KSDLEAQVESLkEELLCLK 232
Cdd:COG4717 236 LEAAALEERLKEarlllliaaallallglggSLLSLILTIAGVLFLVlgllallflllareKASLGKEAEEL-QALPALE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 233 KNHEEEVNSLRCQLGDRLNVEVDAAPpvDLNRVLEEMRCQYETLVE-NNRRDAEDWLDTQSEELNQQVVSSSEQLQSC-- 309
Cdd:COG4717 315 ELEEEELEELLAALGLPPDLSPEELL--ELLDRIEELQELLREAEElEEELQLEELEQEIAALLAEAGVEDEEELRAAle 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 310 -QAEIIELRRTVNALEIELQAQHSMRDALESTLAETEaryssqlaqmqcmitnVEAQLAEIRADLERQNQEYQVLLDVRA 388
Cdd:COG4717 393 qAEEYQELKEELEELEEQLEELLGELEELLEALDEEE----------------LEEELEELEEELEELEEELEELREELA 456
|
330
....*....|....*...
gi 94538345 389 RLECEINTyrglLESEDS 406
Cdd:COG4717 457 ELEAELEQ----LEEDGE 470
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
97-408 |
2.65e-04 |
|
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: 43.56 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 97 EKETMQSLN--------DRLAGYLEKVRQLEQENASLESRIREWCEQQVPYMCPDYQSYFRTIEELQK------------ 156
Cdd:pfam05483 275 EKTKLQDENlkeliekkDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKakaahsfvvtef 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 157 -KTLCS-----KAENARLVVEIDNAKLAADDFRTK---YETEVSLRQLVESDINGLRRIL-DDLTLC--KSDLEAQVESL 224
Cdd:pfam05483 355 eATTCSleellRTEQQRLEKNEDQLKIITMELQKKsseLEEMTKFKNNKEVELEELKKILaEDEKLLdeKKQFEKIAEEL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 225 K---EELLCLKKNHEEEVNSLRCQLGDRLNVEVDAAPPV-DLNRVLEEMRCQYETLVENNrrdaeDWLDTQSEELNQQVV 300
Cdd:pfam05483 435 KgkeQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVeDLKTELEKEKLKNIELTAHC-----DKLLLENKELTQEAS 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 301 SSSEQLQSCQAEIIELR----RTVNALEIELQAQHSMRDALESTLAEtearYSSQLAQMQCMITNVEAQLAEIRADLERQ 376
Cdd:pfam05483 510 DMTLELKKHQEDIINCKkqeeRMLKQIENLEEKEMNLRDELESVREE----FIQKGDEVKCKLDKSEENARSIEYEVLKK 585
|
330 340 350
....*....|....*....|....*....|....*
gi 94538345 377 NQEYQVLLDVRARLECEI---NTYRGLLESEDSKL 408
Cdd:pfam05483 586 EKQMKILENKCNNLKKQIenkNKNIEELHQENKAL 620
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
104-379 |
2.77e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.29 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 104 LNDRLAGYlekvRQLEQENASLEsrirewcEQQVPymcpdyqsyfRTIEELQKKTLCSKAENARLvvEIDNAKLAADDFR 183
Cdd:PRK04778 232 LQELKAGY----RELVEEGYHLD-------HLDIE----------KEIQDLKEQIDENLALLEEL--DLDEAEEKNEEIQ 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 184 TK----Y---ETEVSLRQLVESDInglRRILDDLTlcksDLEAQVESLKEELLCLKKNH---EEEVNSLRcqlgdrlnve 253
Cdd:PRK04778 289 ERidqlYdilEREVKARKYVEKNS---DTLPDFLE----HAKEQNKELKEEIDRVKQSYtlnESELESVR---------- 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 254 vdaappvDLNRVLEEMRCQYETLVENnrrdaedwLDTQSE---ELNQQVVSSSEQLQSCQAEIIELRRTVNALE-IELQA 329
Cdd:PRK04778 352 -------QLEKQLESLEKQYDEITER--------IAEQEIaysELQEELEEILKQLEEIEKEQEKLSEMLQGLRkDELEA 416
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 94538345 330 QHS---MRDALESTLAETEAR--------YSSQLAQMQCMITNVEAQLAEIRADLERQNQE 379
Cdd:PRK04778 417 REKlerYRNKLHEIKRYLEKSnlpglpedYLEMFFEVSDEIEALAEELEEKPINMEAVNRL 477
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
217-376 |
3.02e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 217 LEAQVESLKEELLCLKKNHEE--EVNSLRCQLGDRLNVEVDAAppVDLNRVLEEmrcqyetlvennrrdaedwLDTQSEE 294
Cdd:COG3096 510 LAQRLQQLRAQLAELEQRLRQqqNAERLLEEFCQRIGQQLDAA--EELEELLAE-------------------LEAQLEE 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 295 LNQQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHSMRDALESTLAETEARYSSQLAQMQCMITNVEA---------Q 365
Cdd:COG3096 569 LEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLERereatverdE 648
|
170
....*....|.
gi 94538345 366 LAEIRADLERQ 376
Cdd:COG3096 649 LAARKQALESQ 659
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
200-408 |
3.15e-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: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 200 INGLRRILDDLTLCKSDLEAQVESLKEELlclkKNHEEEVNSLRcQLGDRLNVEVDAAPpvdLNRVLEEMRCQYETLven 279
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAEL----DALQERREALQ-RLAEYSWDEIDVAS---AEREIAELEAELERL--- 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 280 nrRDAEDWLdtqsEELNQQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHSMRDALESTLAETEARYSSQLAQmqcmi 359
Cdd:COG4913 681 --DASSDDL----AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA----- 749
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 94538345 360 tNVEAQLAEIRADlerqnqeyQVLLDVRARLECEINTYRGLLESEDSKL 408
Cdd:COG4913 750 -LLEERFAAALGD--------AVERELRENLEERIDALRARLNRAEEEL 789
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
96-407 |
5.66e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 5.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 96 NEKETMQS-LNDRLAGYlEKVRQ-LEQENASLESRIREWCEQqvpymcpdyqsyfrtIEELQKKTLCSKAENARLVVEID 173
Cdd:pfam01576 183 NKHEAMISdLEERLKKE-EKGRQeLEKAKRKLEGESTDLQEQ---------------IAELQAQIAELRAQLAKKEEELQ 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 174 NAKLAADDFRT-KYETEVSLRQLvESDINGLRRILDDLTLCKSDLEAQveslkeellclKKNHEEEVNSLRCQLGDRLnv 252
Cdd:pfam01576 247 AALARLEEETAqKNNALKKIREL-EAQISELQEDLESERAARNKAEKQ-----------RRDLGEELEALKTELEDTL-- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 253 evdaappvDLNRVLEEMRCQYETLVENNRRDAEDWL---DTQSEEL----NQQVVSSSEQLQSCQAEIIELRRTVNALEI 325
Cdd:pfam01576 313 --------DTTAAQQELRSKREQEVTELKKALEEETrshEAQLQEMrqkhTQALEELTEQLEQAKRNKANLEKAKQALES 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 326 ELQAQHSMRDALESTLAETEARYSSQlaqmqcmitnvEAQLAEIRA---DLERQNQEyqvLLDVRARLECEINTYRGLLE 402
Cdd:pfam01576 385 ENAELQAELRTLQQAKQDSEHKRKKL-----------EGQLQELQArlsESERQRAE---LAEKLSKLQSELESVSSLLN 450
|
....*
gi 94538345 403 SEDSK 407
Cdd:pfam01576 451 EAEGK 455
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
96-370 |
7.62e-04 |
|
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: 41.93 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 96 NEKET-MQSLNDRLAGYLEKVRQLEQENASLESRIREW------CEQQVPYMCPDYQSYFRTIEELQKKTLCSKAENARL 168
Cdd:TIGR04523 366 EEKQNeIEKLKKENQSYKQEIKNLESQINDLESKIQNQeklnqqKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 169 VVEIDNAKLAA---DDFRTKYETEVSlrqLVESDINGLRRILDD--------------LTLCKSDLEAQVESLKEELLCL 231
Cdd:TIGR04523 446 TNQDSVKELIIknlDNTRESLETQLK---VLSRSINKIKQNLEQkqkelkskekelkkLNEEKKELEEKVKDLTKKISSL 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 232 KKNhEEEVNSLRCQLGDRLnvevdaappVDLNRVLEEM-----RCQYETLVENNRRDAEDWLDTQSEELNQQvVSSSEQL 306
Cdd:TIGR04523 523 KEK-IEKLESEKKEKESKI---------SDLEDELNKDdfelkKENLEKEIDEKNKEIEELKQTQKSLKKKQ-EEKQELI 591
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 94538345 307 QSCQAEIIELRrtvNALEIELQAQHSMRDALESTLAETEaRYSSQLAQMQCMITNVEAQLAEIR 370
Cdd:TIGR04523 592 DQKEKEKKDLI---KEIEEKEKKISSLEKELEKAKKENE-KLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
293-408 |
8.65e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 8.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 293 EELNQQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHSM--RDALESTLAETEARYSS------QLAQMQCMITNVEA 364
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYqeLEALEAELAELPERLEEleerleELRELEEELEELEA 170
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 94538345 365 QLAEIRADLERQN--------QEYQVLLDVRARLECEINTYRGLLESEDSKL 408
Cdd:COG4717 171 ELAELQEELEELLeqlslateEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
261-378 |
9.40e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 9.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 261 DLNRV---LEEMRCQYETLvENNRRDAEDWLDTQSE-ELNQQVVS------SSEQLQSCQAEIIELRRTVNALEIELQAQ 330
Cdd:COG4913 236 DLERAheaLEDAREQIELL-EPIRELAERYAAARERlAELEYLRAalrlwfAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 94538345 331 HSMRDALESTLAETEARYSS----QLAQMQCMITNVEAQLAEIRADLERQNQ 378
Cdd:COG4913 315 EARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEA 366
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
217-380 |
1.27e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.51 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 217 LEAQVESLKEELLCLKKNHEEEVNSLRCQLGDRLNvevdaappvdlnRVLEEMRCQYETLVENNRRDAEdwLDTQSEELN 296
Cdd:pfam09787 66 LRGQIQQLRTELQELEAQQQEEAESSREQLQELEE------------QLATERSARREAEAELERLQEE--LRYLEEELR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 297 QQVVSSSEQLQSCQAEIIELRrtvNALEIELQAQHSmRDALESTLAE-TEAryssqLAQMQCMITNVEAQLAEIRADLER 375
Cdd:pfam09787 132 RSKATLQSRIKDREAEIEKLR---NQLTSKSQSSSS-QSELENRLHQlTET-----LIQKQTMLEALSTEKNSLVLQLER 202
|
....*
gi 94538345 376 QNQEY 380
Cdd:pfam09787 203 MEQQI 207
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
187-404 |
1.34e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 187 ETEVSLRQLVES--DINGLRRILDDLtlcksdlEAQVESLKEellcLKKNHEE------EVNSLRcQLGDRLNVEVDAAP 258
Cdd:COG4913 222 DTFEAADALVEHfdDLERAHEALEDA-------REQIELLEP----IRELAERyaaareRLAELE-YLRAALRLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 259 PVDLNRVLEEMRCQYETLVE--NNRRDAEDWLDTQSEELNQQVVSSS-EQLQSCQAEIIELRRTVNALEIELQAQHSMRD 335
Cdd:COG4913 290 LELLEAELEELRAELARLEAelERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLA 369
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 94538345 336 ALESTLAETEARYSSQLAQmqcmitnVEAQLAEIRADLERQNQEYQVLLDVRARLECEINTyrglLESE 404
Cdd:COG4913 370 ALGLPLPASAEEFAALRAE-------AAALLEALEEELEALEEALAEAEAALRDLRRELRE----LEAE 427
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
217-391 |
1.52e-03 |
|
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: 40.88 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 217 LEAQVESLKEELLCLKKNHEEEVNSL-RCQLGDRLNVEVDAAPPVDLNRVLEEMRCQYETLVENNRRDAE---------D 286
Cdd:pfam05557 7 SKARLSQLQNEKKQMELEHKRARIELeKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAElnrlkkkylE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 287 WLDTQSEELNQQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHSMRDALESTLAETEARYS------SQLAQMQCMIT 360
Cdd:pfam05557 87 ALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASeaeqlrQNLEKQQSSLA 166
|
170 180 190
....*....|....*....|....*....|.
gi 94538345 361 NVEAQLAEIRADLERQNQEYQVLLDVRARLE 391
Cdd:pfam05557 167 EAEQRIKELEFEIQSQEQDSEIVKNSKSELA 197
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
179-381 |
1.76e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 179 ADDFRTKYETEVS----LRQLVESDINGLRRILDDLTLCKSDLEAQVESLKEELLCLKKN---HEEEVNSLRCQLGDR-- 249
Cdd:COG3883 14 ADPQIQAKQKELSelqaELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeAEAEIEERREELGERar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 250 -----------LNVEVDAAPPVD-LNRVLeemrcQYETLVENNRRDAEDwLDTQSEELNQQvvssSEQLQSCQAEIIELR 317
Cdd:COG3883 94 alyrsggsvsyLDVLLGSESFSDfLDRLS-----ALSKIADADADLLEE-LKADKAELEAK----KAELEAKLAELEALK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 94538345 318 RTVNALEIELQAQHSMRDALESTLAETEARYSSQLAQMQCMITNVEAQLAEIRADLERQNQEYQ 381
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
298-413 |
2.33e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.55 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 298 QVVSSSEQLQSCQAEIIELRRTVNAL-EIELQ----------AQHSMRDALESTLAETEARYSSQ---LAQMQCMITNVE 363
Cdd:PRK10246 374 QQTSDREQLRQWQQQLTHAEQKLNALpAITLTltadevaaalAQHAEQRPLRQRLVALHGQIVPQqkrLAQLQVAIQNVT 453
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 94538345 364 AQLAEIRADLERQNQEY----QVLLDVRARLECE-----INTYRGLLESEDsklPCNPC 413
Cdd:PRK10246 454 QEQTQRNAALNEMRQRYkektQQLADVKTICEQEarikdLEAQRAQLQAGQ---PCPLC 509
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
97-401 |
4.29e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.53 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 97 EKETMQSLNDRLAGYLEKVRQLEQENASLESRIREWCEQQVpymcpdyqsyfRTIEELQKKtlcsKAENARLVVEIDNAK 176
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE-----------ELEEELAEL----EEELEELEEELEELE 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 177 LAADDFRTKYET-EVSLRQLVESDINGLRRILDDLTLCKSDLEAQVESLKEELlclkkNHEEEVNSLRCQLGDRLNvevd 255
Cdd:COG1196 344 EELEEAEEELEEaEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA-----ELAAQLEELEEAEEALLE---- 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 256 aappvDLNRVLEEmrcqyetlvENNRRDAEDWLDTQSEELNQQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHSMRD 335
Cdd:COG1196 415 -----RLERLEEE---------LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 94538345 336 ALESTLAETEARYSSQLAqmqcMITNVEAQLAEIRADLERQNQ-----EYQVLLDVRARLECEINTYRGLL 401
Cdd:COG1196 481 ELLEELAEAAARLLLLLE----AEADYEGFLEGVKAALLLAGLrglagAVAVLIGVEAAYEAALEAALAAA 547
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
266-391 |
4.67e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 266 LEEMRCQYETLvENNRRDAEDWLDTQS-----EELNQQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHSMRDALEST 340
Cdd:COG4717 104 LEELEAELEEL-REELEKLEKLLQLLPlyqelEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEEL 182
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 94538345 341 LAETEARYSSQLAQMQCMITNVEAQLAEIRADLERQNQEYQVLLDVRARLE 391
Cdd:COG4717 183 LEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
197-394 |
4.77e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.04 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 197 ESDINGLRRILDDLTLCKSDLEAQVESLKEELlclkKNHEEEVNSLRCQLgDRLNVEVDAAPpVDLNRVLEEMRCQYETL 276
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAEL----EELNEEYNELQAEL-EALQAEIDKLQ-AEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 277 VENNRR-----DAEDWLDT--QSEELNQQV--VSSSEQLQSCQAEIIElrrTVNALEIELQAQhsmRDALESTLAETEAr 347
Cdd:COG3883 89 GERARAlyrsgGSVSYLDVllGSESFSDFLdrLSALSKIADADADLLE---ELKADKAELEAK---KAELEAKLAELEA- 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 94538345 348 yssQLAQMQCMITNVEAQLAEIRADLERQNQEYQVLLDVRARLECEI 394
Cdd:COG3883 162 ---LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
141-396 |
4.78e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 39.64 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 141 CPDYQSYFRT-------IEELQKKTLCSKAENARLVVEIDNAKLAADDFRTKYETEVSLRQLVESDI----NGLRRILDD 209
Cdd:TIGR00606 680 CPVCQRVFQTeaelqefISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIpelrNKLQKVNRD 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 210 LTLCKSDLEAQveslkEELLCLKKNHEEEVNSLRCQLG--DRLNVEvdaappvdlnrvLEEMRCQYETLVenNRRDAEDw 287
Cdd:TIGR00606 760 IQRLKNDIEEQ-----ETLLGTIMPEEESAKVCLTDVTimERFQME------------LKDVERKIAQQA--AKLQGSD- 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 288 LDTQSEELNQQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHSMRDALES---TLAETEARYSSQLAQMQCMITNVEA 364
Cdd:TIGR00606 820 LDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeklQIGTNLQRRQQFEEQLVELSTEVQS 899
|
250 260 270
....*....|....*....|....*....|..
gi 94538345 365 QLAEIRADLERQNQEYQVLLDVRARLECEINT 396
Cdd:TIGR00606 900 LIREIKDAKEQDSPLETFLEKDQQEKEELISS 931
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
302-375 |
6.69e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 38.56 E-value: 6.69e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 94538345 302 SSEQLQSCQAEIIELRRTVNALEIELQAQHSMRDALeSTLAETEARYSSQLAQMQCMITNVEAQLAEIRADLER 375
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELDRLQALESEL-AISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLAR 128
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
202-408 |
7.21e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.87 E-value: 7.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 202 GLRRILDDLTLCKSDLEAQVESLKEELLCLKKN-HEEEVNSLRCQLgDRLNVEVDAAPPV--DLNRVL---EEMRCQYET 275
Cdd:PRK02224 177 GVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNgLESELAELDEEI-ERYEEQREQARETrdEADEVLeehEERREELET 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 276 LVENNRRDAEDWLDTQSE--ELNQQVVSSSEQLQSCQAEIIELRRT--VNALEIELQAQHsmRDALESTLAETEARYSSQ 351
Cdd:PRK02224 256 LEAEIEDLRETIAETEREreELAEEVRDLRERLEELEEERDDLLAEagLDDADAEAVEAR--REELEDRDEELRDRLEEC 333
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 94538345 352 LAQMQCMITNVEAqLAEIRADLERQNQEyqvLLDVRARLECEINTYRGLLESEDSKL 408
Cdd:PRK02224 334 RVAAQAHNEEAES-LREDADDLEERAEE---LREEAAELESELEEAREAVEDRREEI 386
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
178-374 |
9.25e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.48 E-value: 9.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 178 AADDFRTKYETEVSLRQLVESDINGLRrilDDLTLCKSDLEA---QVESLKEELLCLkknhEEEVNSLRCQLG-DRLNVE 253
Cdd:PRK02224 238 EADEVLEEHEERREELETLEAEIEDLR---ETIAETEREREElaeEVRDLRERLEEL----EEERDDLLAEAGlDDADAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538345 254 VDAAPPVDLNRVLEEMR----------CQYETLVENNRRDAEDwLDTQSEELNQQ--------------VVSSSEQLQSC 309
Cdd:PRK02224 311 AVEARREELEDRDEELRdrleecrvaaQAHNEEAESLREDADD-LEERAEELREEaaeleseleeareaVEDRREEIEEL 389
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 94538345 310 QAEIIELRRTVNALEIELQAQHSMRDALESTLAETEARyssqLAQMQCMITNVEAQLAEIRADLE 374
Cdd:PRK02224 390 EEEIEELRERFGDAPVDLGNAEDFLEELREERDELRER----EAELEATLRTARERVEEAEALLE 450
|
|
| |
