|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
93-404 |
1.80e-156 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 445.52 E-value: 1.80e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 93 SEKETMQNLNDRLATYLDRVRALEEANADLEVKIREWYKKQGPGPARDYSPYFKTIEDLRNKILAATIDNASIVLQIDNA 172
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 173 RLAADDFRTKYETELNLRMSVEADINGLRRVLDELTLARADLEMQIESLKEELAYLRKNHEEEMNALRGQVG-GDVNVEM 251
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 252 DAAPGVDLSRILNEMRDQYEKMAEKNRKDAEEWFFTKTEELNREVATNTEALQSSRTEITELRRSVQNLEIELQSQLSMK 331
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 154090941 332 ASLENSLAETEARYGAQLAQLQGLISSVEQQLCELRCDMERQNHEYQVLLDVKTRLEQEIATYRRLLEGEDAH 404
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
193-399 |
1.83e-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: 66.62 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 193 VEADINGLRRVLDELTLARADLEMQIESLKEELAYLRKNHEEEMNALRGQVGGDVNVEMDAAPGVDLSRILNEMRDQYEK 272
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 273 MAEKNRKDAEEWFFTKTE------ELNREVATNTEALQSSRTEITELRRSVQNLEIELQSQLSMKASLENSLAETEARYG 346
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEaeaeieELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 154090941 347 ---AQLAQLQGLISSVEQQLCELRCDMERQNHEYQVLLDVKTRLEQEIATYRRLLE 399
Cdd:TIGR02168 842 dleEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
185-406 |
8.99e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 8.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 185 TELNLRMS-VEADINGLRRVLDELTLARADLEMQIESLKEELAYLRKNHE-----------------EEMNALRGQVgGD 246
Cdd:TIGR02168 270 EELRLEVSeLEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEeleaqleeleskldelaEELAELEEKL-EE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 247 VNVEMDAapgvdLSRILNEMRDQYEKMAEKNRKDAEEWfftktEELNREVATNTEALQSSRTEITELRRSVQNLEIELQS 326
Cdd:TIGR02168 349 LKEELES-----LEAELEELEAELEELESRLEELEEQL-----ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 327 QLSMKASLENSLAEtearygAQLAQLQGLISSVEQQLCELRCDMERQNHEYQVLLDVKTRLEQEIATYRRLLEGEDAHLA 406
Cdd:TIGR02168 419 LQQEIEELLKKLEE------AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
98-421 |
4.69e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 4.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 98 MQNLNDRLATYLDRVRALEEANADLEVKIREWYKKqgpgpardyspyfktIEDLRNKILAATidnasivLQIDNARLAAD 177
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAE---------------LEELRLELEELE-------LELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 178 DFRTKYETELNLRMSVEADINGLRRVLDELTLARADLEMQIESLKEELAYLRKNHEEEMNALRgqvggdvnvemdaapgv 257
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE----------------- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 258 DLSRILNEMRDQYEKMAEKNRKDAEEWfftktEELNREVATNTEALQSSRTEITELRRSVQNLEIELQSQLSMKASLENS 337
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEEL-----EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 338 LAETEARYGAQLAQLQGLISSVEQQlcelrcdmERQNHEYQVLLDVKTRLEQEIATYRRLLEGEDAHLATQYSSSLASQP 417
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAEL--------EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
....
gi 154090941 418 SREG 421
Cdd:COG1196 502 DYEG 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
88-393 |
9.12e-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: 9.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 88 ALLGGSEKETMQNLNDR--LATYLDRVRALEEANADLEVKIREWYKKQGPGpARDYSPYFKTIEDLRNKILAATIDNASI 165
Cdd:TIGR02168 660 VITGGSAKTNSSILERRreIEELEEKIEELEEKIAELEKALAELRKELEEL-EEELEQLRKELEELSRQISALRKDLARL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 166 VLQIDNARLAADDFRTKYETELNLRMSVEADINGLRRVLDELTLARADLEMQIESLKEELAYLRKNHEEEMNALRgqvgg 245
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT----- 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 246 dvnvemdaapgvDLSRILNEMRDQYEKMaEKNRKDAEEWFftktEELNREVATNTEALQSSRTEITELRRSVQNLEIELQ 325
Cdd:TIGR02168 814 ------------LLNEEAANLRERLESL-ERRIAATERRL----EDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 154090941 326 SQLSMKASLENSLAETEARYGAQLAQLQglisSVEQQLCELRCDMERQNHEYQVLLDVKTRLEQEIAT 393
Cdd:TIGR02168 877 ALLNERASLEEALALLRSELEELSEELR----ELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
168-396 |
1.54e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 168 QIDNARLAADDFRTKYETELNLRMSVEADINGLRRVLDELTLARADLEMQIESLKEELAYLRKNHEEEMNALRGQVggdv 247
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL---- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 248 nvemdaapgvdlsRILNEMRDQYEKMAEKNRKDAEEWF--FTKTEELNREVATNTEALQSSRTEITELRRSVQNLEIELQ 325
Cdd:COG4942 111 -------------RALYRLGRQPPLALLLSPEDFLDAVrrLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 154090941 326 SQLSMKASLENSLAETEARYGAQLAQLQGLISSVEQQLCELRCDMERqnheyqvLLDVKTRLEQEIATYRR 396
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE-------LEALIARLEAEAAAAAE 241
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
272-415 |
1.14e-05 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 47.15 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 272 KMAEKNRKDAeewfftkTEELNREVATNTEALQSSRTEITELRRSVQNL--EIELQSQLSMKASLENSLAETEARYGA-- 347
Cdd:COG3524 169 QLSERAREDA-------VRFAEEEVERAEERLRDAREALLAFRNRNGILdpEATAEALLQLIATLEGQLAELEAELAAlr 241
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 154090941 348 --------QLAQLQGLISSVEQQLCELRCDMerqnheyqVLLDVKTRLEQEIATYRRLLegEDAHLATQ-YSSSLAS 415
Cdd:COG3524 242 sylspnspQVRQLRRRIAALEKQIAAERARL--------TGASGGDSLASLLAEYERLE--LEREFAEKaYTSALAA 308
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
211-407 |
4.52e-05 |
|
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: 45.89 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 211 RADLEMQIESLKEELAYLRKNHEEEMN-ALRGQVGGDVNVEMDAAPGVDLSRILNEMRDQYEKMAEKNRKDAE------- 282
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIeLEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAElnrlkkk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 283 --EWFFTKTEELNREVATNTEALQSSRTEITELRRSVQNLEIELQSQLSMKASLENSLAETEARYG------AQLAQLQG 354
Cdd:pfam05557 84 ylEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASeaeqlrQNLEKQQS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 154090941 355 LISSVEQQLCELRCDMERQNHEYQVLLDVKTRLEQeIATYRRLLE---GEDAHLAT 407
Cdd:pfam05557 164 SLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELAR-IPELEKELErlrEHNKHLNE 218
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
192-438 |
4.82e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 192 SVEADINGLRRVLDELTLARADLEMQIESLKEElaylRKNHEEEMNALRGQVGgDVNVEMDAapgvdLSRILNEMRDQYE 271
Cdd:TIGR02169 298 ELEAEIASLERSIAEKERELEDAEERLAKLEAE----IDKLLAEIEELEREIE-EERKRRDK-----LTEEYAELKEELE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 272 KMaeknRKDAEEwFFTKTEELNREVATNTEALQSSRTEITELRRSVQNLEIELQSQLSMKASLENSLAETEAR---YGAQ 348
Cdd:TIGR02169 368 DL----RAELEE-VDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKineLEEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 349 LAQLQGLISSVEQQLCELRCDMErqnheyqvllDVKTRLEQEIATYRRlLEGEDAHLATQYSSSLAS-QPSREGMVTSRQ 427
Cdd:TIGR02169 443 KEDKALEIKKQEWKLEQLAADLS----------KYEQELYDLKEEYDR-VEKELSKLQRELAEAEAQaRASEERVRGGRA 511
|
250
....*....|.
gi 154090941 428 VRTIVEEVQDG 438
Cdd:TIGR02169 512 VEEVLKASIQG 522
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
98-366 |
1.13e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 98 MQNLNDRLATYLDRVRALEEANADLEVKIREwYKKQGPGPARDYSPYFKTIEDLRNKILAATIDNASIVLQIDNARLAAD 177
Cdd:TIGR02168 276 VSELEEEIEELQKELYALANEISRLEQQKQI-LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 178 DFRTKYETELNLRMSVEADINGLRRVLDELTLARADLEMQIESLKEELAYLrknhEEEMNALRGQVggdvnvemdaapgv 257
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL----EARLERLEDRR-------------- 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 258 dlSRILNEMRDQYEKMAEKNRKDAEEWFFTKTEELNR---EVATNTEALQSSRTEITELRRSVQNLEIELQSQLSMKASL 334
Cdd:TIGR02168 417 --ERLQQEIEELLKKLEEAELKELQAELEELEEELEElqeELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
250 260 270
....*....|....*....|....*....|....
gi 154090941 335 ENSL--AETEARYGAQLAQLQGLISSVEQQLCEL 366
Cdd:TIGR02168 495 ERLQenLEGFSEGVKALLKNQSGLSGILGVLSEL 528
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
96-390 |
5.00e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.64 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 96 ETMQNLNDRLAT-YLDRVRALEEANADLEVKIREWYKKQGPGPARdyspyfktIEDLRNKILAATidnASIVLQIDNarL 174
Cdd:COG5185 300 EYTKSIDIKKATeSLEEQLAAAEAEQELEESKRETETGIQNLTAE--------IEQGQESLTENL---EAIKEEIEN--I 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 175 AADDFRTKYETELNlrmSVEADINGLRRVLDEltlARADLEMQIESLKEELAYLRKNHEEEMNALRGQVGGDVNvEMDAA 254
Cdd:COG5185 367 VGEVELSKSSEELD---SFKDTIESTKESLDE---IPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATS-SNEEV 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 255 pgvdlSRILNEMRDQYEKMAEKNRKDAEEWFFTKTEELNREVATNTEALQSSRT----EITELRRSVQNLEIELQSQLSM 330
Cdd:COG5185 440 -----SKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTqiesRVSTLKATLEKLRAKLERQLEG 514
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 331 KASLENSLAETEARYGAQLAQLQGLISSVEQQLCELRCDMERQNHEYQVLLDVKTRLEQE 390
Cdd:COG5185 515 VRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELT 574
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
192-363 |
6.58e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 192 SVEADINGLRRVLDELTLARADLEMQIESLKEELAYLRKN---HEEEMNALRGQVGGDVNVE-MDAAPGVDLSRILN--- 264
Cdd:COG3883 34 AAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeAEAEIEERREELGERARALyRSGGSVSYLDVLLGses 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 265 --EMRDQYEKMAEKNRKDAEEwfFTKTEELNREVATNTEALQSSRTEITELRRSVQNLEIELQSQLSMKASLENSLAETE 342
Cdd:COG3883 114 fsDFLDRLSALSKIADADADL--LEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEE 191
|
170 180
....*....|....*....|.
gi 154090941 343 ARYGAQLAQLQGLISSVEQQL 363
Cdd:COG3883 192 AAAEAQLAELEAELAAAEAAA 212
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
197-399 |
7.25e-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: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 197 INGLRRVLDELTLARADLEMQIESLKEELaylRKNHEEEMNALRGQvggdvNVEMDAapgvdlsriLNEMRDQYEKMAEK 276
Cdd:pfam15921 414 IDHLRRELDDRNMEVQRLEALLKAMKSEC---QGQMERQMAAIQGK-----NESLEK---------VSSLTAQLESTKEM 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 277 NRKDAEEWFFTKT--EELNREVATNTEALQ-------SSRTEITELRRSVQNLEIELQSQLSMKASLENSLAETEArYGA 347
Cdd:pfam15921 477 LRKVVEELTAKKMtlESSERTVSDLTASLQekeraieATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEA-LKL 555
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 154090941 348 QLAQLQGLISSVEQQLCELRCDMERQNHEYQVLLDVKTRLEQEIATYRRLLE 399
Cdd:pfam15921 556 QMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQ 607
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
151-366 |
1.06e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 151 LRNKILAATIDNASIVLQIDNARLAADDF---RTKYETELNlrmSVEADINGLRRVLDELTLARADLEMQIESLKEELAY 227
Cdd:TIGR02169 292 VKEKIGELEAEIASLERSIAEKERELEDAeerLAKLEAEID---KLLAEIEELEREIEEERKRRDKLTEEYAELKEELED 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 228 LRKNHEEEMNALRG--QVGGDVNVEMDaapgvDLSRILNEMRDQYEKMAEKNRKDAEEwfftkTEELNREVATNTEALQS 305
Cdd:TIGR02169 369 LRAELEEVDKEFAEtrDELKDYREKLE-----KLKREINELKRELDRLQEELQRLSEE-----LADLNAAIAGIEAKINE 438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 154090941 306 SRTEITELRRSVQNLEIELQSQLSMKASLENSLAETEARYgaqlAQLQGLISSVEQQLCEL 366
Cdd:TIGR02169 439 LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY----DRVEKELSKLQRELAEA 495
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
193-404 |
1.39e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.03 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 193 VEADINGLRRVLDELTLARADLEMQIESLKEELAYLRKNHEEEMNALRGQvggdvnvemdaapgVDLSRILNEMRDQYEK 272
Cdd:pfam07888 57 REKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKEL--------------SASSEELSEEKDALLA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 273 MAEKNRKdaeewfftKTEELNREVATNTEALQSSRTEITELRRSVQNLEIELQSQLSMKASLENSLAETEARYGAQLAQL 352
Cdd:pfam07888 123 QRAAHEA--------RIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 154090941 353 QGLISSVEQQLCELrcdmerqnheyQVLLDVKTRLEQEIAT-YRRLLEGEDAH 404
Cdd:pfam07888 195 QELRNSLAQRDTQV-----------LQLQDTITTLTQKLTTaHRKEAENEALL 236
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
168-389 |
1.51e-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: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 168 QIDNARLAADDFRTKYETelnlrMSVEADINGLRRVLDELTLARADLEMQIESLKEELAYLRKNheeemnalrgqvggdV 247
Cdd:COG3206 190 ELEEAEAALEEFRQKNGL-----VDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQ---------------L 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 248 NVEMDAAPGVDLSRILNEMRDQYEkmaeknrkdaeewfftkteELNREVATNTEALQSSRTEITELRRSVQNLEIELQSQ 327
Cdd:COG3206 250 GSGPDALPELLQSPVIQQLRAQLA-------------------ELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQE 310
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 154090941 328 LS-MKASLEN---SLAETEARYGAQLAQLQGLISS---VEQQLCELRCDMERQNHEYQVLLdvkTRLEQ 389
Cdd:COG3206 311 AQrILASLEAeleALQAREASLQAQLAQLEARLAElpeLEAELRRLEREVEVARELYESLL---QRLEE 376
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
172-436 |
2.99e-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: 40.09 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 172 ARLAADDFRTKYETE------LNLRMSVEADINGLRRVLDELTLARADLEMQIESLKEELAYLRKNHEEEMNALRGQVGG 245
Cdd:pfam05483 165 ARSAEKTKKYEYEREetrqvyMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 246 D-VNVEMDAAPGVDLSRILNEMRDQYEKMAEKNRKDAE--EWFFTKTEELNREVATNTEALQSSRTEITELRRSVQ---- 318
Cdd:pfam05483 245 LlIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDEnlKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQiatk 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 319 -----NLEIELQSQLSMKASLENSLAETEarYGAQLAQLQGLISSVEQ-------QLCELRCDMERQNHEYQVLLDVKTR 386
Cdd:pfam05483 325 ticqlTEEKEAQMEELNKAKAAHSFVVTE--FEATTCSLEELLRTEQQrleknedQLKIITMELQKKSSELEEMTKFKNN 402
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 154090941 387 LEQEIATYRRLLeGEDAHLatqyssslasqpsregMVTSRQVRTIVEEVQ 436
Cdd:pfam05483 403 KEVELEELKKIL-AEDEKL----------------LDEKKQFEKIAEELK 435
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
95-324 |
6.00e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.23 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 95 KETMQNLNDRLATYLDRVRALEEAnadLEvKIREwyKKQGPGPARDYSPYFKTIEDLRNKILAATIDnasivLQIDNARL 174
Cdd:COG3206 174 RKALEFLEEQLPELRKELEEAEAA---LE-EFRQ--KNGLVDLSEEAKLLLQQLSELESQLAEARAE-----LAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 175 AADDFRTKYETELNLRMSVEADINGLRRVLDELTLARADLEM-------QIESLKEELAYLRKNHEEEMNALRGQVggDV 247
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRILASL--EA 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 154090941 248 NVEMDAAPGVDLSRILNEMRDQYEKMAEKNRkdaeewfftKTEELNREVATNTEALQS--SRTEITELRRSVQNLEIEL 324
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELPELEA---------ELRRLEREVEVARELYESllQRLEEARLAEALTVGNVRV 390
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
200-399 |
6.54e-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: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 200 LRRVLDELTLARADLEMQIESLKEELAylrkNHEEEMNALRGQVGGdVNVEMDAApgvDLSRILNEMRDQYEKmAEKNRK 279
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELE----EAEAALEEFRQKNGL-VDLSEEAK---LLLQQLSELESQLAE-ARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 280 DAEEWFFTKTEELNREVATNTEALQSSrtEITELRRSVQNLEIELqsqlsmkaslenslAETEARYGA---QLAQLQGLI 356
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQSP--VIQQLRAQLAELEAEL--------------AELSARYTPnhpDVIALRAQI 300
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 154090941 357 SSVEQQL-CELRCDMERQNHEYQVLLDVKTRLEQEIATYRRLLE 399
Cdd:COG3206 301 AALRAQLqQEAQRILASLEAELEALQAREASLQAQLAQLEARLA 344
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
290-398 |
6.85e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 38.41 E-value: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 290 EELNREVATNTEALQSSRTEITELRRSVQNLEIELQSQLSMKASLENSLAETEarygAQLAQLQGLISSVEQQLCELRCD 369
Cdd:PRK09039 56 DRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELA----GAGAAAEGRAGELAQELDSEKQV 131
|
90 100
....*....|....*....|....*....
gi 154090941 370 MERQNHeyQVLLdvktrLEQEIATYRRLL 398
Cdd:PRK09039 132 SARALA--QVEL-----LNQQIAALRRQL 153
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
197-317 |
6.88e-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: 38.46 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 197 INGLRRVLDE-LTLARADLEM------QIESLKEELAYLRKNHEEEMNALRgqvggDVNVEMDAAPGVDLSRILNEMRDQ 269
Cdd:smart00787 142 LEGLKEGLDEnLEGLKEDYKLlmkeleLLNSIKPKLRDRKDALEEELRQLK-----QLEDELEDCDPTELDRAKEKLKKL 216
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 154090941 270 YEKMAEKNRKDAEewFFTKTEELNREVATNTEALQSSRTEITELRRSV 317
Cdd:smart00787 217 LQEIMIKVKKLEE--LEEELQELESKIEDLTNKKSELNTEIAEAEKKL 262
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
192-378 |
7.59e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.74 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 192 SVEADINGLRRVLDELTLARADLEMQIESLKEELAYLRKNHEEEmNALRGQVGGDVNV---------------EMDAAPG 256
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL-QRLAEYSWDEIDVasaereiaeleaeleRLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 257 VdlsriLNEMRDQYEKmAEKNRKDAEEwfftKTEELNREVATNTEALQSSRTEITELRRSVQNLEIELQSQLSmkASLEN 336
Cdd:COG4913 686 D-----LAALEEQLEE-LEAELEELEE----ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR--ALLEE 753
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 154090941 337 SLAE--TEARYGAQLAQLQGLISSVEQQLCELRCDMERQNHEYQ 378
Cdd:COG4913 754 RFAAalGDAVERELRENLEERIDALRARLNRAEEELERAMRAFN 797
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
147-388 |
8.26e-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: 8.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 147 TIEDLRNKILAATIDNASIVLQI-DNARLAADDFRTKYETELNLRmSVEADINGLRRVLDELTLARADLEMQIESLKEEL 225
Cdd:pfam01576 448 LLNEAEGKNIKLSKDVSSLESQLqDTQELLQEETRQKLNLSTRLR-QLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQL 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 226 AYLRKNHEEEMNALRGQVGGDVNVEMDAApgvDLSRILNEMRDQYEKMAE-KNRKDAEEWFFTKTEELNREVATNTEALQ 304
Cdd:pfam01576 527 SDMKKKLEEDAGTLEALEEGKKRLQRELE---ALTQQLEEKAAAYDKLEKtKNRLQQELDDLLVDLDHQRQLVSNLEKKQ 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090941 305 SSRTEITELRRSVQNLEIELQSQ------------LSMKASLENSLA---ETEARYGAQLAQLQGLISS----------- 358
Cdd:pfam01576 604 KKFDQMLAEEKAISARYAEERDRaeaeareketraLSLARALEEALEakeELERTNKQLRAEMEDLVSSkddvgknvhel 683
|
250 260 270
....*....|....*....|....*....|....*.
gi 154090941 359 ------VEQQLCELRCDMERQNHEYQVLLDVKTRLE 388
Cdd:pfam01576 684 erskraLEQQVEEMKTQLEELEDELQATEDAKLRLE 719
|
|
| |
