|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
301-557 |
7.31e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.93 E-value: 7.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 301 ENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNnQITKTKN 380
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL-SSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 381 KNVEKMRGQMESHLKELERVCDSLTAAERRL--HECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEEncLI 458
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLeaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE--YL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 459 QLKCENLQQKLEQMDAENKELEKKLANqeecLKHSNLKFKEKSAEYTALARQLEAALEEgrqkVAEEIEKMSSRESALQI 538
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIEN----LNGKKEELEEELEELEAALRDLESRLGD----LKKERDELEAQLRELER 903
|
250
....*....|....*....
gi 2067662289 539 KILDLETELRKKNEEQNQL 557
Cdd:TIGR02169 904 KIEELEAQIEKKRKRLSEL 922
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
38-587 |
6.33e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 49.35 E-value: 6.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 38 CLKQDILNEKT----ELEATLKEAELVTHSVELLLPLFKDTIEKINFENANLSALNLK-ISEQKEILIKELDT----FKS 108
Cdd:pfam15921 159 CLKEDMLEDSNtqieQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRsLGSAISKILRELDTeisyLKG 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 109 VKLALEHLLRKrdYKQTGDNLSSMLLENLTDNesentnLKKKVFEKEAHIQELSclfqsEKSLETKIAKWNLQSRMNkne 188
Cdd:pfam15921 239 RIFPVEDQLEA--LKSESQNKIELLLQQHQDR------IEQLISEHEVEITGLT-----EKASSARSQANSIQSQLE--- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 189 aIVMKEASRQKTValkkaskvYKQRLDHFTGAIEKLTSQIRDQ----EAKLSETISASNAWKSHYEKIVIEKTELEVQIE 264
Cdd:pfam15921 303 -IIQEQARNQNSM--------YMRQLSDLESTVSQLRSELREAkrmyEDKIEELEKQLVLANSELTEARTERDQFSQESG 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 265 TMKKQIINLLEDLKKMEdhgknsceeilrKVHSIEYE-NETLNLENTKLKTTLAALKDEvvsvenelselqevekkqktl 343
Cdd:pfam15921 374 NLDDQLQKLLADLHKRE------------KELSLEKEqNKRLWDRDTGNSITIDHLRRE--------------------- 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 344 IEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEK---MRGQMESHLKELERVCDSLTA-------AERRLHE 413
Cdd:pfam15921 421 LDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKvssLTAQLESTKEMLRKVVEELTAkkmtlesSERTVSD 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 414 CQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENCL-IQLKCENLQQKLEQMDAENKELEKKLANQEECLKH 492
Cdd:pfam15921 501 LTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRnVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQ 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 493 SNLKFKEKSAEYTALARQL-EAALEEGRQKVAEEIEKMSSREsaLQIKILDLETELRKKNEEQNQLVCKMNSKAQHQEVC 571
Cdd:pfam15921 581 HGRTAGAMQVEKAQLEKEInDRRLELQEFKILKDKKDAKIRE--LEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQL 658
|
570
....*....|....*.
gi 2067662289 572 LKEVQNSLEKSENQNE 587
Cdd:pfam15921 659 LNEVKTSRNELNSLSE 674
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
381-557 |
7.33e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 7.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 381 KNVEKMRGQMEsHLKELERVCDSLTAAERRLHEC------------QESLQCCKGKCADQEHTIRELQGQVDGNHNLLTK 448
Cdd:COG4913 242 EALEDAREQIE-LLEPIRELAERYAAARERLAELeylraalrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 449 LSLEEENCLIQL------KCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKV 522
Cdd:COG4913 321 LREELDELEAQIrgnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400
|
170 180 190
....*....|....*....|....*....|....*
gi 2067662289 523 AEEIEKMSSRESALQikilDLETELRKKNEEQNQL 557
Cdd:COG4913 401 EALEEALAEAEAALR----DLRRELRELEAEIASL 431
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
12-524 |
4.75e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 12 EELFCHLKTISEKEDLPRCTSE--SHLSCLKQDILNEKTELEATLKEAELVTHSVELLLPLFKDTIEKINFENANLSALN 89
Cdd:PRK03918 200 KELEEVLREINEISSELPELREelEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 90 LKISEQKEILIKELDTFKSVKLALEHLLRKRDYKQTGDNLSSM---LLENLTDNESENTNLKKKVFEKEAHIQELSCLFQ 166
Cdd:PRK03918 280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEingIEERIKELEEKEERLEELKKKLKELEKRLEELEE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 167 SEKSLETKIAKWNLQSRMNKNEAIVMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNA-- 244
Cdd:PRK03918 360 RHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcp 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 245 -----WKSHYEKIVIEKTELEVQ-IETMKKQIINLLEDLKKMEDHGKN---------SCEEILRKVHSIEYENETLNLEN 309
Cdd:PRK03918 440 vcgreLTEEHRKELLEEYTAELKrIEKELKEIEEKERKLRKELRELEKvlkkeseliKLKELAEQLKELEEKLKKYNLEE 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 310 T--------KLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEmyktqvqKLQEaaeiVKSRCENLLHKNNQITKTKNK 381
Cdd:PRK03918 520 LekkaeeyeKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK-------KLDE----LEEELAELLKELEELGFESVE 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 382 NVEKMRGQMESHLKELERVCDS---LTAAERRLHECQESLQCCKGKCADQEHTIRELQGQVDGnhnlLTKLSLEEENCLI 458
Cdd:PRK03918 589 ELEERLKELEPFYNEYLELKDAekeLEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE----LEKKYSEEEYEEL 664
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2067662289 459 QLKCENLQQKLEQMDAENKELEKKLANQEECLK--HSNLKFKEKSAEYTALARQLEAALEEGRQKVAE 524
Cdd:PRK03918 665 REEYLELSRELAGLRAELEELEKRREEIKKTLEklKEELEEREKAKKELEKLEKALERVEELREKVKK 732
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
219-581 |
8.87e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 8.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 219 GAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEDHGKNS------CEEIL 292
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELkkeieeLEEKV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 293 RKVHSIEYENET----------LNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTL----------IEMYKTQVQ 352
Cdd:PRK03918 283 KELKELKEKAEEyiklsefyeeYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELkkklkelekrLEELEERHE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 353 KLQEAAEIvKSRCENLLHK--NNQITKTKNK--NVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQ 428
Cdd:PRK03918 363 LYEEAKAK-KEELERLKKRltGLTPEKLEKEleELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVC 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 429 EHTIRElqgqvDGNHNLLTKLSLEEENclIQLKCENLQQKLEQMDAENKELEKKLANQEECLKhsnlkFKEKSAEYTALA 508
Cdd:PRK03918 442 GRELTE-----EHRKELLEEYTAELKR--IEKELKEIEEKERKLRKELRELEKVLKKESELIK-----LKELAEQLKELE 509
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2067662289 509 RQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKNEEQNQLVcKMNSKAQHQEVCLKEVQNSLEK 581
Cdd:PRK03918 510 EKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLA-ELEKKLDELEEELAELLKELEE 581
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
193-399 |
2.47e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 193 KEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIIN 272
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 273 LLEDLK-------KMEDHGK-------NSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEK 338
Cdd:COG4942 102 QKEELAellralyRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2067662289 339 KQKTLiemyKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELER 399
Cdd:COG4942 182 ELEEE----RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
132-404 |
5.58e-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: 43.12 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 132 MLLENLTDNESENTNLKKKVFEKEAHIQELSCLFQSEKSLETKIAKWNLQSRMNKNEAIVMKEA-------SRQKTVALK 204
Cdd:TIGR02168 702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEleerleeAEEELAEAE 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 205 KASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKME--- 281
Cdd:TIGR02168 782 AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAaei 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 282 DHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIV 361
Cdd:TIGR02168 862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2067662289 362 KSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELERVCDSL 404
Cdd:TIGR02168 942 QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
268-381 |
1.40e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 39.61 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 268 KQIINLLEDLKKMEDHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMY 347
Cdd:pfam11559 34 ARIINVIYELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNE 113
|
90 100 110
....*....|....*....|....*....|....*
gi 2067662289 348 KTQVQKLQEAAEIVKSRCENLLHKNN-QITKTKNK 381
Cdd:pfam11559 114 KEELQRLKNALQQIKTQFAHEVKKRDrEIEKLKER 148
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
301-557 |
7.31e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.93 E-value: 7.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 301 ENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNnQITKTKN 380
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL-SSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 381 KNVEKMRGQMESHLKELERVCDSLTAAERRL--HECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEEncLI 458
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLeaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE--YL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 459 QLKCENLQQKLEQMDAENKELEKKLANqeecLKHSNLKFKEKSAEYTALARQLEAALEEgrqkVAEEIEKMSSRESALQI 538
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIEN----LNGKKEELEEELEELEAALRDLESRLGD----LKKERDELEAQLRELER 903
|
250
....*....|....*....
gi 2067662289 539 KILDLETELRKKNEEQNQL 557
Cdd:TIGR02169 904 KIEELEAQIEKKRKRLSEL 922
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
254-558 |
3.79e-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: 53.52 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 254 IEKTELEVQIETMKKQIINLLEDLKKMEDhgknSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSEL 333
Cdd:TIGR02168 225 LELALLVLRLEELREELEELQEELKEAEE----ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 334 QEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQItktkNKNVEKMRGQMESHLKELERVCDSLTAAERRLHE 413
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL----EEKLEELKEELESLEAELEELEAELEELESRLEE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 414 CQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENcliqLKCENLQQKLEQMDAENKELEKKLANQEECLKHS 493
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER----LQQEIEELLKKLEEAELKELQAELEELEEELEEL 452
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2067662289 494 NLKFKEKSAEYTALARQLEAALEEgRQKVAEEIEKMSSRESALQikilDLETELRKKNEEQNQLV 558
Cdd:TIGR02168 453 QEELERLEEALEELREELEEAEQA-LDAAERELAQLQARLDSLE----RLQENLEGFSEGVKALL 512
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
194-529 |
4.52e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 194 EASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSET-------ISASNAWKSHYEKIVIEKTELEVQIETM 266
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALrkdlarlEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 267 KKQIINLLEDLKKMEDHGKNSCEEIlrkvhsieyenETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEM 346
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQI-----------EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 347 YKTQVQKLQEAAEIVKSRCENLlhknnqitktkNKNVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCA 426
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESL-----------AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 427 DQEHTIRELQGQVDGNHNLLTKLSLEEENclIQLKCENLQQKL---EQMDAEN-KELEKKLANQEECLKHS--------- 493
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEG--LEVRIDNLQERLseeYSLTLEEaEALENKIEDDEEEARRRlkrlenkik 982
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2067662289 494 -----NL----KFKEKSAEYTALARQLEaALEEGRQKVAEEIEKM 529
Cdd:TIGR02168 983 elgpvNLaaieEYEELKERYDFLTAQKE-DLTEAKETLEEAIEEI 1026
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
38-587 |
6.33e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 49.35 E-value: 6.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 38 CLKQDILNEKT----ELEATLKEAELVTHSVELLLPLFKDTIEKINFENANLSALNLK-ISEQKEILIKELDT----FKS 108
Cdd:pfam15921 159 CLKEDMLEDSNtqieQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRsLGSAISKILRELDTeisyLKG 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 109 VKLALEHLLRKrdYKQTGDNLSSMLLENLTDNesentnLKKKVFEKEAHIQELSclfqsEKSLETKIAKWNLQSRMNkne 188
Cdd:pfam15921 239 RIFPVEDQLEA--LKSESQNKIELLLQQHQDR------IEQLISEHEVEITGLT-----EKASSARSQANSIQSQLE--- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 189 aIVMKEASRQKTValkkaskvYKQRLDHFTGAIEKLTSQIRDQ----EAKLSETISASNAWKSHYEKIVIEKTELEVQIE 264
Cdd:pfam15921 303 -IIQEQARNQNSM--------YMRQLSDLESTVSQLRSELREAkrmyEDKIEELEKQLVLANSELTEARTERDQFSQESG 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 265 TMKKQIINLLEDLKKMEdhgknsceeilrKVHSIEYE-NETLNLENTKLKTTLAALKDEvvsvenelselqevekkqktl 343
Cdd:pfam15921 374 NLDDQLQKLLADLHKRE------------KELSLEKEqNKRLWDRDTGNSITIDHLRRE--------------------- 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 344 IEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEK---MRGQMESHLKELERVCDSLTA-------AERRLHE 413
Cdd:pfam15921 421 LDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKvssLTAQLESTKEMLRKVVEELTAkkmtlesSERTVSD 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 414 CQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENCL-IQLKCENLQQKLEQMDAENKELEKKLANQEECLKH 492
Cdd:pfam15921 501 LTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRnVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQ 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 493 SNLKFKEKSAEYTALARQL-EAALEEGRQKVAEEIEKMSSREsaLQIKILDLETELRKKNEEQNQLVCKMNSKAQHQEVC 571
Cdd:pfam15921 581 HGRTAGAMQVEKAQLEKEInDRRLELQEFKILKDKKDAKIRE--LEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQL 658
|
570
....*....|....*.
gi 2067662289 572 LKEVQNSLEKSENQNE 587
Cdd:pfam15921 659 LNEVKTSRNELNSLSE 674
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
381-557 |
7.33e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 7.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 381 KNVEKMRGQMEsHLKELERVCDSLTAAERRLHEC------------QESLQCCKGKCADQEHTIRELQGQVDGNHNLLTK 448
Cdd:COG4913 242 EALEDAREQIE-LLEPIRELAERYAAARERLAELeylraalrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 449 LSLEEENCLIQL------KCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKV 522
Cdd:COG4913 321 LREELDELEAQIrgnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400
|
170 180 190
....*....|....*....|....*....|....*
gi 2067662289 523 AEEIEKMSSRESALQikilDLETELRKKNEEQNQL 557
Cdd:COG4913 401 EALEEALAEAEAALR----DLRRELRELEAEIASL 431
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
202-487 |
4.42e-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: 46.59 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 202 ALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKme 281
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE-- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 282 dhgknsceeilrkvhsIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIV 361
Cdd:TIGR02168 321 ----------------LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 362 KSRCENLLHKNNQITKTknknVEKMRGQMESHLKELERVCDSLTAAERRLHECQesLQCCKGKCADQEHTIRELQGQVDG 441
Cdd:TIGR02168 385 RSKVAQLELQIASLNNE----IERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELER 458
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2067662289 442 NHNLLTKLSLEEEncLIQLKCENLQQKLEQMDAENKELEKKLANQE 487
Cdd:TIGR02168 459 LEEALEELREELE--EAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
12-524 |
4.75e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 12 EELFCHLKTISEKEDLPRCTSE--SHLSCLKQDILNEKTELEATLKEAELVTHSVELLLPLFKDTIEKINFENANLSALN 89
Cdd:PRK03918 200 KELEEVLREINEISSELPELREelEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 90 LKISEQKEILIKELDTFKSVKLALEHLLRKRDYKQTGDNLSSM---LLENLTDNESENTNLKKKVFEKEAHIQELSCLFQ 166
Cdd:PRK03918 280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEingIEERIKELEEKEERLEELKKKLKELEKRLEELEE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 167 SEKSLETKIAKWNLQSRMNKNEAIVMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNA-- 244
Cdd:PRK03918 360 RHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcp 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 245 -----WKSHYEKIVIEKTELEVQ-IETMKKQIINLLEDLKKMEDHGKN---------SCEEILRKVHSIEYENETLNLEN 309
Cdd:PRK03918 440 vcgreLTEEHRKELLEEYTAELKrIEKELKEIEEKERKLRKELRELEKvlkkeseliKLKELAEQLKELEEKLKKYNLEE 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 310 T--------KLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEmyktqvqKLQEaaeiVKSRCENLLHKNNQITKTKNK 381
Cdd:PRK03918 520 LekkaeeyeKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK-------KLDE----LEEELAELLKELEELGFESVE 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 382 NVEKMRGQMESHLKELERVCDS---LTAAERRLHECQESLQCCKGKCADQEHTIRELQGQVDGnhnlLTKLSLEEENCLI 458
Cdd:PRK03918 589 ELEERLKELEPFYNEYLELKDAekeLEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE----LEKKYSEEEYEEL 664
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2067662289 459 QLKCENLQQKLEQMDAENKELEKKLANQEECLK--HSNLKFKEKSAEYTALARQLEAALEEGRQKVAE 524
Cdd:PRK03918 665 REEYLELSRELAGLRAELEELEKRREEIKKTLEklKEELEEREKAKKELEKLEKALERVEELREKVKK 732
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
219-581 |
8.87e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 8.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 219 GAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEDHGKNS------CEEIL 292
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELkkeieeLEEKV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 293 RKVHSIEYENET----------LNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTL----------IEMYKTQVQ 352
Cdd:PRK03918 283 KELKELKEKAEEyiklsefyeeYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELkkklkelekrLEELEERHE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 353 KLQEAAEIvKSRCENLLHK--NNQITKTKNK--NVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQ 428
Cdd:PRK03918 363 LYEEAKAK-KEELERLKKRltGLTPEKLEKEleELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVC 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 429 EHTIRElqgqvDGNHNLLTKLSLEEENclIQLKCENLQQKLEQMDAENKELEKKLANQEECLKhsnlkFKEKSAEYTALA 508
Cdd:PRK03918 442 GRELTE-----EHRKELLEEYTAELKR--IEKELKEIEEKERKLRKELRELEKVLKKESELIK-----LKELAEQLKELE 509
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2067662289 509 RQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKNEEQNQLVcKMNSKAQHQEVCLKEVQNSLEK 581
Cdd:PRK03918 510 EKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLA-ELEKKLDELEEELAELLKELEE 581
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2-585 |
8.87e-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: 45.88 E-value: 8.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 2 EKAVNDGSHSEELFCHLKTISEKEDLPRCTSESHLSCLKQDILNEKTELEATLKEAELVTHSVELLLPLFKDTIEKINFE 81
Cdd:pfam15921 285 EKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 82 NANLSALNLKISEQKEILIKELDTfKSVKLALEHLLRKRdykqtgdnlssmLLENLTDNESENTNLKKKVFEKEAHIQEL 161
Cdd:pfam15921 365 RDQFSQESGNLDDQLQKLLADLHK-REKELSLEKEQNKR------------LWDRDTGNSITIDHLRRELDDRNMEVQRL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 162 SCLFQSEKSLETKIAKWNLQSRMNKNEAIvmkEASRQKTVALKKASKVYKQRLDHFTG---AIEKLTSQIRDQEAKLSE- 237
Cdd:pfam15921 432 EALLKAMKSECQGQMERQMAAIQGKNESL---EKVSSLTAQLESTKEMLRKVVEELTAkkmTLESSERTVSDLTASLQEk 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 238 --TISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLK--KMEDHGKNSCEEILRKvhSIEYENETLNLENTK-- 311
Cdd:pfam15921 509 erAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEalKLQMAEKDKVIEILRQ--QIENMTQLVGQHGRTag 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 312 -LKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQ-EAAEIVKSRCENLlhknnQITKTKNKNVEKMRGQ 389
Cdd:pfam15921 587 aMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElEKVKLVNAGSERL-----RAVKDIKQERDQLLNE 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 390 MESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQehtIRELQGQVDGNHNLLTklSLEEENCLIQLKCENLQQKL 469
Cdd:pfam15921 662 VKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQ---LKSAQSELEQTRNTLK--SMEGSDGHAMKVAMGMQKQI 736
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 470 EQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEgRQKVAEEIEKMSSRESALQIKILDLETELRK 549
Cdd:pfam15921 737 TAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE-KNKMAGELEVLRSQERRLKEKVANMEVALDK 815
|
570 580 590
....*....|....*....|....*....|....*.
gi 2067662289 550 KNEEQNQlvCKMNSKAQHQEVCLKEVQNSLEKSENQ 585
Cdd:pfam15921 816 ASLQFAE--CQDIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
213-519 |
9.11e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 9.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 213 RLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEdhgknscEEIL 292
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE-------QDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 293 RKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKN 372
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 373 NQITKTKNKNVEKmrgqmESHLKELERVCDSLTAAERRLHECQESLQcckgkcADQEHTIRELqgqvdgnhnlltkLSLE 452
Cdd:COG1196 386 EELLEALRAAAEL-----AAQLEELEEAEEALLERLERLEEELEELE------EALAELEEEE-------------EEEE 441
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2067662289 453 EENCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGR 519
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
257-556 |
1.35e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 257 TELEVQIETMKKQiinlledLKKMEDHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEV 336
Cdd:COG1196 196 GELERQLEPLERQ-------AEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 337 EKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKN----------KNVEKMRGQMESHLKELERVCDSLTA 406
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReleerleeleEELAELEEELEELEEELEELEEELEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 407 AERRLHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENCLIQLK-----CENLQQKLEQMDAENKELEK 481
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEeleeaEEALLERLERLEEELEELEE 428
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2067662289 482 KLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKNEEQNQ 556
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
379-552 |
1.58e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.30 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 379 KNKNVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTK---------- 448
Cdd:PRK11637 59 KEKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLLAAqldaafrqge 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 449 -------LSLEEE-------------NCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLkhSNLKFKEKSAEYTALA 508
Cdd:PRK11637 139 htglqliLSGEESqrgerilayfgylNQARQETIAELKQTREELAAQKAELEEKQSQQKTLL--YEQQAQQQKLEQARNE 216
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2067662289 509 RQ-----LEAALEEGRQKVAEeiekMSSRESALQIKILDLETELRKKNE 552
Cdd:PRK11637 217 RKktltgLESSLQKDQQQLSE----LRANESRLRDSIARAEREAKARAE 261
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
197-552 |
1.74e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 197 RQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLED 276
Cdd:PRK02224 362 REEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARER 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 277 LKKME---DHGK-NSCEEILRK---VHSIEYENEtlnlENTKLKTTLAALKDEVVSVE---NELSELQEVEKKQKTLIEM 346
Cdd:PRK02224 442 VEEAEallEAGKcPECGQPVEGsphVETIEEDRE----RVEELEAELEDLEEEVEEVEerlERAEDLVEAEDRIERLEER 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 347 YKTQVQKLQEAAEIVKSRCENLlhknnqitktknknvEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCA 426
Cdd:PRK02224 518 REDLEELIAERRETIEEKRERA---------------EELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLA 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 427 DQEHTIRELQgqvdgnhNLLTKLSLEEEnclIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYta 506
Cdd:PRK02224 583 ELKERIESLE-------RIRTLLAAIAD---AEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEE-- 650
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2067662289 507 lARQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKNE 552
Cdd:PRK02224 651 -AREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE 695
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
193-399 |
2.47e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 193 KEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIIN 272
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 273 LLEDLK-------KMEDHGK-------NSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEK 338
Cdd:COG4942 102 QKEELAellralyRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2067662289 339 KQKTLiemyKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELER 399
Cdd:COG4942 182 ELEEE----RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
389-557 |
5.35e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 389 QMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENC-----LIQLKCE 463
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLeqdiaRLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 464 NLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKVAEEIEKMSSRESALQIKILDL 543
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170
....*....|....
gi 2067662289 544 ETELRKKNEEQNQL 557
Cdd:COG1196 393 RAAAELAAQLEELE 406
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
132-404 |
5.58e-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: 43.12 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 132 MLLENLTDNESENTNLKKKVFEKEAHIQELSCLFQSEKSLETKIAKWNLQSRMNKNEAIVMKEA-------SRQKTVALK 204
Cdd:TIGR02168 702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEleerleeAEEELAEAE 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 205 KASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKME--- 281
Cdd:TIGR02168 782 AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAaei 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 282 DHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIV 361
Cdd:TIGR02168 862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2067662289 362 KSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELERVCDSL 404
Cdd:TIGR02168 942 QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
379-603 |
5.92e-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: 43.12 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 379 KNKNVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQVdgnhnlltkLSLEEENCLI 458
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL---------TELEAEIEEL 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 459 QLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTalarqleaALEEGRQKVAEEIEKMSSRESALQI 538
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT--------LLNEEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2067662289 539 KILDLETELRKKNEEQNQLVCKMNSkaqhQEVCLKEVQNSLEKSENQNESIKNYLQFLKTSYVTM 603
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEIEE----LEELIEELESELEALLNERASLEEALALLRSELEEL 899
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
394-570 |
7.34e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 394 LKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENCLIQLKCENLQQKLEQMD 473
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 474 AENKELEKKLANQEECLKhsnlKFKEKSAEYTALARQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKNEE 553
Cdd:COG4717 153 ERLEELRELEEELEELEA----ELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170
....*....|....*..
gi 2067662289 554 QNQLVCKMNSKAQHQEV 570
Cdd:COG4717 229 LEQLENELEAAALEERL 245
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
258-536 |
7.39e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 7.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 258 ELEVQIETMKKQIINLLEDLKKME---DHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQ 334
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIEnrlDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 335 EVEKKQKTLIEMYKTQVQKLQEAAEIVKSRcenLLHKNNQITKTKNKNVEKMRGQMESHLKELERVCDSLTA----AERR 410
Cdd:TIGR02169 758 SELKELEARIEELEEDLHKLEEALNDLEAR---LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLekeyLEKE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 411 LHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKL-----SLEEENCLIQLKCENLQQKLEQMDAENKELEKKLAN 485
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELeaalrDLESRLGDLKKERDELEAQLRELERKIEELEAQIEK 914
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2067662289 486 QEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQ-----KVAEEIEKMSSRESAL 536
Cdd:TIGR02169 915 KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEelsleDVQAELQRVEEEIRAL 970
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
166-357 |
9.20e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 9.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 166 QSEKSLETKIAKwnLQSRMNKNEAIVMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKL---------S 236
Cdd:COG3206 175 KALEFLEEQLPE--LRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLaalraqlgsG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 237 ETISASNAWKSHYEKIVIEKTELEVQIETMKK-------QIINLLEDLKKMEDHGKnscEEILRKVHSIEYENETLNLEN 309
Cdd:COG3206 253 PDALPELLQSPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQ---QEAQRILASLEAELEALQARE 329
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2067662289 310 TKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEA 357
Cdd:COG3206 330 ASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
188-597 |
1.16e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 188 EAIVMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKiVIEKTELEVQIETMK 267
Cdd:PTZ00121 1326 EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE-KKKADEAKKKAEEDK 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 268 KQIINL--LEDLKKMEDHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTlie 345
Cdd:PTZ00121 1405 KKADELkkAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE--- 1481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 346 myKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKN-KNVEKMRGQMESHLKELERVCDSLTAAERR-----LHECQESLQ 419
Cdd:PTZ00121 1482 --AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEaKKAEEAKKADEAKKAEEAKKADEAKKAEEKkkadeLKKAEELKK 1559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 420 CCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENCLIQLKCENLQQKLEQM-DAENKELEKKLANQEECLKHSNLKFK 498
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAkKAEEAKIKAEELKKAEEEKKKVEQLK 1639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 499 EKSAEYTALARQLEAALEEGRQKVAEEIEKmsSRESALQIKILDLETELRKKNEEQNQLVCKMNSKAQHQEVCLKEVQNS 578
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKK--AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKK 1717
|
410
....*....|....*....
gi 2067662289 579 LEKSENQNESIKNYLQFLK 597
Cdd:PTZ00121 1718 AEELKKAEEENKIKAEEAK 1736
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
268-381 |
1.40e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 39.61 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 268 KQIINLLEDLKKMEDHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMY 347
Cdd:pfam11559 34 ARIINVIYELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNE 113
|
90 100 110
....*....|....*....|....*....|....*
gi 2067662289 348 KTQVQKLQEAAEIVKSRCENLLHKNN-QITKTKNK 381
Cdd:pfam11559 114 KEELQRLKNALQQIKTQFAHEVKKRDrEIEKLKER 148
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
95-368 |
1.45e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 95 QKEILIKELDTFKSVKLALEHLLRKrdykqtGDNLSSMLLENLTDNESENTNLKKKVFEKEAHIQELSCLfQSEKSLETK 174
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEE------LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE-ISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 175 IAKWNLQSRMNKNEAI-VMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIV 253
Cdd:TIGR02168 306 ILRERLANLERQLEELeAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 254 IEKTELEVQIETMKKQIINLLEDLKKMEDHGKNSCEEILrkvhsiEYENETLNLENTKLKTTLAALKDEVVSVENELSEL 333
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE------ELLKKLEEAELKELQAELEELEEELEELQEELERL 459
|
250 260 270
....*....|....*....|....*....|....*
gi 2067662289 334 QEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENL 368
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
334-558 |
1.66e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 41.55 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 334 QEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKEL--ERVCDSLTAAERRL 411
Cdd:pfam05667 243 RKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKLqfTNEAPAATSSPPTK 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 412 HECQESLQcckgkcADQEHTIRELQGQVDGNHNLLTKLSLEEENCliQLKCENLQQKLEQMDAENKELEKKLANQ----- 486
Cdd:pfam05667 323 VETEEELQ------QQREEELEELQEQLEDLESSIQELEKEIKKL--ESSIKQVEEELEELKEQNEELEKQYKVKkktld 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 487 -----EECLKHSNLKFKEKSAEYTALARQLEA----------ALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKN 551
Cdd:pfam05667 395 llpdaEENIAKLQALVDASAQRLVELAGQWEKhrvplieeyrALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKE 474
|
....*..
gi 2067662289 552 EEQNQLV 558
Cdd:pfam05667 475 ELYKQLV 481
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
328-561 |
2.20e-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: 41.21 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 328 NELSELQEVEKKQKTLIEMYKTQVQKLQeaaeivKSRCENLLHKNNQITKTKNKNVEKMRgQMESHLKELERVCDSLTAA 407
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLR------REREKAERYQALLKEKREYEGYELLK-EKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 408 ERRLHECQESLQCCKGKCADQEHTIRELQGQVDgnhnlltKLSlEEENCLIQLKCENLQQKLEQMDAENKELEKKLANQE 487
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIK-------DLG-EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2067662289 488 ECLKHSNLKFKEKSAEYTALARQLEAALEEgRQKVAEEIEKMSSRESALQIKILDLETELRKKNEEQNQLVCKM 561
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKR-RDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
305-594 |
3.91e-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: 40.42 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 305 LNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLlhkNNQITKTKNkNVE 384
Cdd:TIGR00606 693 LQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKV---NRDIQRLKN-DIE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 385 KMRGQMESHLKELERVCDSLTAAERrLHECQESLQcckgkcaDQEHTIRELQGQVDGNHNLLTKLSLEEENcliqlkcEN 464
Cdd:TIGR00606 769 EQETLLGTIMPEEESAKVCLTDVTI-MERFQMELK-------DVERKIAQQAAKLQGSDLDRTVQQVNQEK-------QE 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 465 LQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLE--AALEEGRQKVAEEIEKMSSRESALQIKILD 542
Cdd:TIGR00606 834 KQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQrrQQFEEQLVELSTEVQSLIREIKDAKEQDSP 913
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2067662289 543 LETELRKKNEEQNQLVCKMNSKAQHQEVCLKEVQNSLEKSENQNESIKNYLQ 594
Cdd:TIGR00606 914 LETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQ 965
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
43-368 |
6.08e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.67 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 43 ILNEKTELEATLKEAELVTHSVELLLPLFKDTIEKINFENANLSALNLKISEQKEILIKELDTFKSVKLALEHLLRKrdY 122
Cdd:TIGR02169 700 IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK--L 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 123 KQTGDNLSSMLLENLTDN-ESENTNLKKKVFEKEAHIQELSCLFQSeKSLETKIAKWNLQSRMNKNEAIVMKEASRQKTV 201
Cdd:TIGR02169 778 EEALNDLEARLSHSRIPEiQAELSKLEEEVSRIEARLREIEQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 202 ALKKAskvykqRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKME 281
Cdd:TIGR02169 857 ENLNG------KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE 930
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 282 DHGKnsceEILRKVHSIEYE-NETLNLEntKLKTTLAALKDEVVSVEN-ELSELQEVEKKQKTLIEmYKTQVQKLQEAAE 359
Cdd:TIGR02169 931 EELS----EIEDPKGEDEEIpEEELSLE--DVQAELQRVEEEIRALEPvNMLAIQEYEEVLKRLDE-LKEKRAKLEEERK 1003
|
....*....
gi 2067662289 360 IVKSRCENL 368
Cdd:TIGR02169 1004 AILERIEEY 1012
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
127-587 |
6.27e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 39.82 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 127 DNLSSMLLENLTDNESENTNLKKK---------------VFEKEAHiqELSCLFQSEKSLETKIAKWNLQSRMNKNEaiV 191
Cdd:pfam12128 196 RDVKSMIVAILEDDGVVPPKSRLNrqqvehwirdiqaiaGIMKIRP--EFTKLQQEFNTLESAELRLSHLHFGYKSD--E 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 192 MKEASRQKtvALKKASKVYKQRLDHFTG----AIEKLTSQIRDQEAKLS---ETISASNAWKSHYEKIVIEKTELEV-QI 263
Cdd:pfam12128 272 TLIASRQE--ERQETSAELNQLLRTLDDqwkeKRDELNGELSAADAAVAkdrSELEALEDQHGAFLDADIETAAADQeQL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 264 ETMKKQIINLLEDLKKMEDHGKNSCEEILRKVHSIEYENETlnlENTKLKTTLAALKDEVVSVENELSElqEVEKKQKTL 343
Cdd:pfam12128 350 PSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNR---DIAGIKDKLAKIREARDRQLAVAED--DLQALESEL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 344 IEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKT---------KNKNVEKMRGQMESHLKELERVCDSLTAAERRLHEC 414
Cdd:pfam12128 425 REQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATpelllqlenFDERIERAREEQEAANAEVERLQSELRQARKRRDQA 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 415 QESLQCCKGKCADQEHTIRELQGQVD-GNHNLLTKLSLE---------------------------EENCLIQLKCENLQ 466
Cdd:pfam12128 505 SEALRQASRRLEERQSALDELELQLFpQAGTLLHFLRKEapdweqsigkvispellhrtdldpevwDGSVGGELNLYGVK 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 467 QKLEQMD-----AENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAA-LEEGRQKVA-----EEIEKMSSRESA 535
Cdd:pfam12128 585 LDLKRIDvpewaASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKAsREETFARTAlknarLDLRRLFDEKQS 664
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2067662289 536 LQIKILD-LETELRKKNEEQNQLVCKMNSKAQHQEVCLKEVQNslEKSENQNE 587
Cdd:pfam12128 665 EKDKKNKaLAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKE--QKREARTE 715
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
461-557 |
9.41e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.07 E-value: 9.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662289 461 KCENLQQKLEQMDAENKELEKKLANQEECLKHsnlkfkeksaeytalarqLEAALEEGRQKVAEEIEKmsSRE-SALQIK 539
Cdd:COG2433 414 EIRRLEEQVERLEAEVEELEAELEEKDERIER------------------LERELSEARSEERREIRK--DREiSRLDRE 473
|
90
....*....|....*...
gi 2067662289 540 ILDLETELRKKNEEQNQL 557
Cdd:COG2433 474 IERLERELEEERERIEEL 491
|
|
|