|
Name |
Accession |
Description |
Interval |
E-value |
| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
468-668 |
3.74e-75 |
|
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper region with similarity to the DNA-binding domain of the cAMP-responsive activating-transcription factor 5. There is evidence that Fez1 inhibits cancer cell growth through regulation of mitosis, and that its alterations result in abnormal cell growth. Note that some family members contain more than one copy of this region.
Pssm-ID: 462015 [Multi-domain] Cd Length: 198 Bit Score: 240.28 E-value: 3.74e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 468 TKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAAC- 546
Cdd:pfam06818 1 TKWEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 547 ------------------LKPALTPVDPAEPQdalATCESDEAKMRRQAgvaaaaslvsvdgeaeaggESGTRALRREVG 608
Cdd:pfam06818 81 eaellrekvgkleeevsgLREALSDVSPSGYE---SVYESDEAKEQRQE-------------------EADLGSLRREVE 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 609 RLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQLERRLR 668
Cdd:pfam06818 139 RLRAELREERQRRERQASSFEQERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
349-643 |
5.50e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 5.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 349 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQvLEERQKAWERELAELRQGCSGKLQQVArRAQRAQQGLQLQVLRLQQ 428
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEE-LRLELEELELELEEAQAEEYELLAELA-RLEQDIARLEERRRELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 429 DKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLR 508
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 509 EGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAACLKPAltpvdpaepQDALATCESDEAKMRRQAGVAAAASLVSV 588
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE---------EEEEALEEAAEEEAELEEEEEALLELLAE 467
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1532527591 589 DGEAEAGGESGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVI 643
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
348-623 |
6.94e-10 |
|
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: 62.77 E-value: 6.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 348 SALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQGCSGKLQQVARRAQRAQQGLQLQvlrlq 427
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL-SRQISALRKDLARLEAEVEQLEERIAQLSKEL----- 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 428 qdkKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQL 507
Cdd:TIGR02168 757 ---TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 508 REGRASLREKEEQLLSLRDSFSSKQASLELGEgelpaaclkpaltpVDPAEPQDALAtcESDEAKMRRQAGVAAAASLVS 587
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELE--------------ELIEELESELE--ALLNERASLEEALALLRSELE 897
|
250 260 270
....*....|....*....|....*....|....*.
gi 1532527591 588 VDGEAEAGGESGTRALRREVGRLQAELAAERRARER 623
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEG 933
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
349-582 |
9.45e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 9.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 349 ALIQELEERLWEKEQEVAALRRSLEQSEAAVA------QVLEERQKAWERELAELrqgcSGKLQQVARRAQRAQQGLQLQ 422
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYALANEISrleqqkQILRERLANLERQLEEL----EAQLEELESKLDELAEELAEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 423 VLRLQQDKKQ---LQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSE 499
Cdd:TIGR02168 343 EEKLEELKEElesLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 500 IVGLRS-----QLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAACLKPALTPVDPAEPQDALATCES-DEAKM 573
Cdd:TIGR02168 423 IEELLKkleeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERlQENLE 502
|
....*....
gi 1532527591 574 RRQAGVAAA 582
Cdd:TIGR02168 503 GFSEGVKAL 511
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
349-528 |
7.59e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 7.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 349 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQV----------------------LEERQKAWERELAELRQGcSGKLQ 406
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALqerrealqrlaeyswdeidvasAEREIAELEAELERLDAS-SDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 407 QVARRAQRAqqglqlqvlrlQQDKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEEtkWEVCQKAGEISLLKQQL 486
Cdd:COG4913 689 ALEEQLEEL-----------EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA--AEDLARLELRALLEERF 755
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1532527591 487 KD-SQADVSQKLSEIvgLRSQLREGRASLREKEEQLLSLRDSF 528
Cdd:COG4913 756 AAaLGDAVERELREN--LEERIDALRARLNRAEEELERAMRAF 796
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
372-523 |
1.16e-06 |
|
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: 51.95 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 372 LEQSEAAVAQVLEERQKAWERELAELRQgcsgKLQQVARRAQRAQQGLQLQVLRLqqdkKQLQEEAARLMRQREELEDKV 451
Cdd:pfam05667 315 ATSSPPTKVETEEELQQQREEELEELQE----QLEDLESSIQELEKEIKKLESSI----KQVEEELEELKEQNEELEKQY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 452 AAcqKEQA-DFLPRIEE--------------------TKWEVCQKA--GEISLLKQQLKDSQADVSQKLSEIVGLRSQLR 508
Cdd:pfam05667 387 KV--KKKTlDLLPDAEEniaklqalvdasaqrlvelaGQWEKHRVPliEEYRALKEAKSNKEDESQRKLEEIKELREKIK 464
|
170
....*....|....*...
gi 1532527591 509 EGRASLREKEE---QLLS 523
Cdd:pfam05667 465 EVAEEAKQKEElykQLVA 482
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
351-641 |
2.74e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 351 IQELEERLWEKEQEVAALRRSLEQSEAAvAQVLEERQKAWERELAELRQgcsgKLQQVARRAQRAQQGLQLQVLrlqqDK 430
Cdd:PRK02224 281 VRDLRERLEELEEERDDLLAEAGLDDAD-AEAVEARREELEDRDEELRD----RLEECRVAAQAHNEEAESLRE----DA 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 431 KQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEEtkwevcqkageislLKQQLKDSQA---DVSQKLSEIVGLRSQL 507
Cdd:PRK02224 352 DDLEERAEELREEAAELESELEEAREAVEDRREEIEE--------------LEEEIEELRErfgDAPVDLGNAEDFLEEL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 508 REGRASLREKEEqllSLRDSFSSKQASLELGEGELPAACLKPALTPVDPAEPQDALATCESDEAKMRRQAGvAAAASLVS 587
Cdd:PRK02224 418 REERDELREREA---ELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELE-DLEEEVEE 493
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1532527591 588 VDGEAEAGGESGTRALRREVGRLQAELAAERRARERQGasfAEERRVWLEEKEK 641
Cdd:PRK02224 494 VEERLERAEDLVEAEDRIERLEERREDLEELIAERRET---IEEKRERAEELRE 544
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
350-522 |
2.35e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 350 LIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQkawerELAELRQGCSGKLQQVARRAQRAqqglqlqvLRLQQD 429
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPELREELEKLEKEVK-----ELEELKEEIEELEKELESLEGSK--------RKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 430 KKQLQEEAARLMRQREELEDKVAACQ--KEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQL 507
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340
|
170
....*....|....*
gi 1532527591 508 REgrasLREKEEQLL 522
Cdd:PRK03918 341 EE----LKKKLKELE 351
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
350-491 |
2.21e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.77 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 350 LIQELEERLWEKEQEVAALRRSLEQSEAAVAQvLEERQKAWERELAELRQG---CSGKLQQVARRAQRAQQGLQLQVLRl 426
Cdd:smart00787 145 LKEGLDENLEGLKEDYKLLMKELELLNSIKPK-LRDRKDALEEELRQLKQLedeLEDCDPTELDRAKEKLKKLLQEIMI- 222
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1532527591 427 qqdKKQLQEEaarLMRQREELEDKVAACQKEQADFLPRI--EETKWEVCQK--AGEISLLKQQLKDSQA 491
Cdd:smart00787 223 ---KVKKLEE---LEEELQELESKIEDLTNKKSELNTEIaeAEKKLEQCRGftFKEIEKLKEQLKLLQS 285
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
602-670 |
3.85e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 38.33 E-value: 3.85e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1532527591 602 ALRREVGRLQAELAAERRARERQGASFAEERRVWLEEK--EKVIEYQKQLQLSYVEMYQRNQQLERRLRER 670
Cdd:smart00935 29 KRQAELEKLEKELQKLKEKLQKDAATLSEAAREKKEKElqKKVQEFQRKQQKLQQDLQKRQQEELQKILDK 99
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
468-668 |
3.74e-75 |
|
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper region with similarity to the DNA-binding domain of the cAMP-responsive activating-transcription factor 5. There is evidence that Fez1 inhibits cancer cell growth through regulation of mitosis, and that its alterations result in abnormal cell growth. Note that some family members contain more than one copy of this region.
Pssm-ID: 462015 [Multi-domain] Cd Length: 198 Bit Score: 240.28 E-value: 3.74e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 468 TKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAAC- 546
Cdd:pfam06818 1 TKWEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 547 ------------------LKPALTPVDPAEPQdalATCESDEAKMRRQAgvaaaaslvsvdgeaeaggESGTRALRREVG 608
Cdd:pfam06818 81 eaellrekvgkleeevsgLREALSDVSPSGYE---SVYESDEAKEQRQE-------------------EADLGSLRREVE 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 609 RLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQLERRLR 668
Cdd:pfam06818 139 RLRAELREERQRRERQASSFEQERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
349-643 |
5.50e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 5.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 349 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQvLEERQKAWERELAELRQGCSGKLQQVArRAQRAQQGLQLQVLRLQQ 428
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEE-LRLELEELELELEEAQAEEYELLAELA-RLEQDIARLEERRRELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 429 DKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLR 508
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 509 EGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAACLKPAltpvdpaepQDALATCESDEAKMRRQAGVAAAASLVSV 588
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE---------EEEEALEEAAEEEAELEEEEEALLELLAE 467
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1532527591 589 DGEAEAGGESGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVI 643
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
352-673 |
6.84e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 6.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 352 QELEERLWEKEQEVAALR-RSLEQSEAAVAQVLEERQKAWERELAELRQgCSGKLQQVARRAQRAQQglqlqvlrlqqDK 430
Cdd:COG1196 216 RELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAE-LEAELEELRLELEELEL-----------EL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 431 KQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREG 510
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 511 RASLREKEEQLLSLRDSFSSKQaslelgegelpaaclkpaltpvdpaepqdalatcesdEAKMRRQAGVAAAASLVSVDG 590
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELA-------------------------------------EELLEALRAAAELAAQLEELE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 591 EAEAGGESGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQLERRLRER 670
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
...
gi 1532527591 671 GAA 673
Cdd:COG1196 487 AEA 489
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
351-644 |
3.69e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 351 IQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQGcSGKLQQVARRAQRAQQGLQLQVLRLQQDK 430
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA-EAELAEAEEE-LEELAEELLEALRAAAELAAQLEELEEAE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 431 KQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEEtkwevcqkageislLKQQLKDSQADVSQKLSEIVGLRSQLREG 510
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEE--------------AAEEEAELEEEEEALLELLAELLEEAALL 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 511 RASLREKEEQLLSLRDSFSSKQASLELGEGELPAAclKPALTPVDPAEPQDALATCESDEAKMRRQAGVAAAASLVSVDG 590
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGV--KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVV 553
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1532527591 591 EAEAGGESGTRALRRE------------VGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIE 644
Cdd:COG1196 554 EDDEVAAAAIEYLKAAkagratflpldkIRARAALAAALARGAIGAAVDLVASDLREADARYYVLG 619
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
349-673 |
3.69e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 349 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAWERELAELRQGCSGKLQQVARRAQRAQQGLQLQVLRLQQ 428
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 429 DKKQLQEEAARLMRQREELEDKVAAcQKEQADFLPRI-----EETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGL 503
Cdd:COG1196 487 AEAAARLLLLLEAEADYEGFLEGVK-AALLLAGLRGLagavaVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEY 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 504 RSQLREGRASLREKEeqLLSLRDSFSSKQASLELGEGELPAACLKPALTPVDPAEPQDAL-ATCESDEAKMRRQAGVAAA 582
Cdd:COG1196 566 LKAAKAGRATFLPLD--KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLgRTLVAARLEAALRRAVTLA 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 583 ASLVSVDGEAEAGGESGTRALRREVGRLQAELAAERRARERQGASFAEERRvwLEEKEKVIEYQKQLQLSYVEMYQRNQQ 662
Cdd:COG1196 644 GRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE--LEEALLAEEEEERELAEAEEERLEEEL 721
|
330
....*....|.
gi 1532527591 663 LERRLRERGAA 673
Cdd:COG1196 722 EEEALEEQLEA 732
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
348-623 |
6.94e-10 |
|
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: 62.77 E-value: 6.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 348 SALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQGCSGKLQQVARRAQRAQQGLQLQvlrlq 427
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL-SRQISALRKDLARLEAEVEQLEERIAQLSKEL----- 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 428 qdkKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQL 507
Cdd:TIGR02168 757 ---TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 508 REGRASLREKEEQLLSLRDSFSSKQASLELGEgelpaaclkpaltpVDPAEPQDALAtcESDEAKMRRQAGVAAAASLVS 587
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELE--------------ELIEELESELE--ALLNERASLEEALALLRSELE 897
|
250 260 270
....*....|....*....|....*....|....*.
gi 1532527591 588 VDGEAEAGGESGTRALRREVGRLQAELAAERRARER 623
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEG 933
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
348-616 |
5.24e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.69 E-value: 5.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 348 SALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAWER------ELAELRQGcSGKLQQVARRAQRAQQGLQL 421
Cdd:TIGR02168 725 SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERleeaeeELAEAEAE-IEELEAQIEQLKEELKALRE 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 422 QVLRLQQDKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIV 501
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA 883
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 502 GLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAACLKPALTPVDPAEPQDALATCESDEAKMrrqagvaa 581
Cdd:TIGR02168 884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE-------- 955
|
250 260 270
....*....|....*....|....*....|....*
gi 1532527591 582 aaslvsvDGEAEAGGESGTRALRREVGRLQAELAA 616
Cdd:TIGR02168 956 -------AEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
349-582 |
9.45e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 9.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 349 ALIQELEERLWEKEQEVAALRRSLEQSEAAVA------QVLEERQKAWERELAELrqgcSGKLQQVARRAQRAQQGLQLQ 422
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYALANEISrleqqkQILRERLANLERQLEEL----EAQLEELESKLDELAEELAEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 423 VLRLQQDKKQ---LQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSE 499
Cdd:TIGR02168 343 EEKLEELKEElesLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 500 IVGLRS-----QLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAACLKPALTPVDPAEPQDALATCES-DEAKM 573
Cdd:TIGR02168 423 IEELLKkleeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERlQENLE 502
|
....*....
gi 1532527591 574 RRQAGVAAA 582
Cdd:TIGR02168 503 GFSEGVKAL 511
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
349-673 |
2.35e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.77 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 349 ALIQELEE-RLWEKEQEVAALRRSLEQSEAAVAQvLEERQKAWERELAELRQgcsgklqQVARRAQRaqqglqlqvlrlq 427
Cdd:TIGR02169 215 ALLKEKREyEGYELLKEKEALERQKEAIERQLAS-LEEELEKLTEEISELEK-------RLEEIEQL------------- 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 428 qdkkqLQEEAARLMRQREEledkvaacqkEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQL 507
Cdd:TIGR02169 274 -----LEELNKKIKDLGEE----------EQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEI 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 508 REGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAACLKPALTPVDPAEPQDAL--ATCESDEAKMRRQAGVAAAASL 585
Cdd:TIGR02169 339 EELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLekLKREINELKRELDRLQEELQRL 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 586 VSVDGEAE---AGGESGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQK---QLQLSYVEMYQR 659
Cdd:TIGR02169 419 SEELADLNaaiAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKelsKLQRELAEAEAQ 498
|
330
....*....|....
gi 1532527591 660 NQQLERRLRERGAA 673
Cdd:TIGR02169 499 ARASEERVRGGRAV 512
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
349-528 |
7.59e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 7.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 349 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQV----------------------LEERQKAWERELAELRQGcSGKLQ 406
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALqerrealqrlaeyswdeidvasAEREIAELEAELERLDAS-SDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 407 QVARRAQRAqqglqlqvlrlQQDKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEEtkWEVCQKAGEISLLKQQL 486
Cdd:COG4913 689 ALEEQLEEL-----------EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA--AEDLARLELRALLEERF 755
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1532527591 487 KD-SQADVSQKLSEIvgLRSQLREGRASLREKEEQLLSLRDSF 528
Cdd:COG4913 756 AAaLGDAVERELREN--LEERIDALRARLNRAEEELERAMRAF 796
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
349-485 |
3.87e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 349 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAWERELAELRQgcsgKLQQVARRAQRAQQGLQLQVLRLQQ 428
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLER----ELEERERRRARLEALLAALGLPLPA 377
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1532527591 429 DKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQQ 485
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
372-523 |
1.16e-06 |
|
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: 51.95 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 372 LEQSEAAVAQVLEERQKAWERELAELRQgcsgKLQQVARRAQRAQQGLQLQVLRLqqdkKQLQEEAARLMRQREELEDKV 451
Cdd:pfam05667 315 ATSSPPTKVETEEELQQQREEELEELQE----QLEDLESSIQELEKEIKKLESSI----KQVEEELEELKEQNEELEKQY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 452 AAcqKEQA-DFLPRIEE--------------------TKWEVCQKA--GEISLLKQQLKDSQADVSQKLSEIVGLRSQLR 508
Cdd:pfam05667 387 KV--KKKTlDLLPDAEEniaklqalvdasaqrlvelaGQWEKHRVPliEEYRALKEAKSNKEDESQRKLEEIKELREKIK 464
|
170
....*....|....*...
gi 1532527591 509 EGRASLREKEE---QLLS 523
Cdd:pfam05667 465 EVAEEAKQKEElykQLVA 482
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
351-641 |
2.74e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 351 IQELEERLWEKEQEVAALRRSLEQSEAAvAQVLEERQKAWERELAELRQgcsgKLQQVARRAQRAQQGLQLQVLrlqqDK 430
Cdd:PRK02224 281 VRDLRERLEELEEERDDLLAEAGLDDAD-AEAVEARREELEDRDEELRD----RLEECRVAAQAHNEEAESLRE----DA 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 431 KQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEEtkwevcqkageislLKQQLKDSQA---DVSQKLSEIVGLRSQL 507
Cdd:PRK02224 352 DDLEERAEELREEAAELESELEEAREAVEDRREEIEE--------------LEEEIEELRErfgDAPVDLGNAEDFLEEL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 508 REGRASLREKEEqllSLRDSFSSKQASLELGEGELPAACLKPALTPVDPAEPQDALATCESDEAKMRRQAGvAAAASLVS 587
Cdd:PRK02224 418 REERDELREREA---ELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELE-DLEEEVEE 493
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1532527591 588 VDGEAEAGGESGTRALRREVGRLQAELAAERRARERQGasfAEERRVWLEEKEK 641
Cdd:PRK02224 494 VEERLERAEDLVEAEDRIERLEERREDLEELIAERRET---IEEKRERAEELRE 544
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
351-531 |
3.58e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.77 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 351 IQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQgcsgKLQQVARRAQRaqqglqlqvlrlqqDK 430
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDL-EKEIKRLEL----EIEEVEARIKK--------------YE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 431 KQL-----QEEAARLMRQREELEDKVAACQKEQADFLPRIEEtkwevcqkageislLKQQLKDSQADVSQKLSEIVGLRS 505
Cdd:COG1579 80 EQLgnvrnNKEYEALQKEIESLKRRISDLEDEILELMERIEE--------------LEEELAELEAELAELEAELEEKKA 145
|
170 180
....*....|....*....|....*.
gi 1532527591 506 QLREGRASLREKEEQLLSLRDSFSSK 531
Cdd:COG1579 146 ELDEELAELEAELEELEAEREELAAK 171
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
352-669 |
3.99e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 3.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 352 QELEERLWEKEQEVAALRRSLEQSEAAVAQV--LEERQKAWERELAELRQGCSGKLQQVARRAQRAQQGLQLQVLRLQQD 429
Cdd:COG4717 135 EALEAELAELPERLEELEERLEELRELEEELeeLEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 430 KKQLQEEAARLMRQREELEDKVAACQKEQadflpRIEETKWEVCQKAG--EISLLKQQLKDSQADVSQKLSEIVGL---- 503
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALEE-----RLKEARLLLLIAAAllALLGLGGSLLSLILTIAGVLFLVLGLlall 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 504 ----------------RSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAACLKPALTPVDPAEPQDALATCE 567
Cdd:COG4717 290 flllarekaslgkeaeELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 568 SDEAKMRRQAGVAAAASLVSVDGEAEAGgesgtRALRREVGRLQAELAAERRARERQGASFAEERrvWLEEKEKVIEYQK 647
Cdd:COG4717 370 QEIAALLAEAGVEDEEELRAALEQAEEY-----QELKEELEELEEQLEELLGELEELLEALDEEE--LEEELEELEEELE 442
|
330 340
....*....|....*....|..
gi 1532527591 648 QLQLSYVEMYQRNQQLERRLRE 669
Cdd:COG4717 443 ELEEELEELREELAELEAELEQ 464
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
344-673 |
6.79e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 6.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 344 PPSPSALIQELEERLWE---KEQEVAALRRSLEQSEAAVAQvLEERQKAWERELAELRQGCS-GKLQQVARRAQRAQQGL 419
Cdd:COG4717 66 PELNLKELKELEEELKEaeeKEEEYAELQEELEELEEELEE-LEAELEELREELEKLEKLLQlLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 420 QLQVLRLQQDKKQLQEEAARLMRQREELEDKVAACQKEQADFLP----RIEETKWEVCQKAGEISLLKQQLKDSQADVSQ 495
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLateeELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 496 KLSEIVGLRSQLREGRASLREKEEQ----LLSLRDSFSSKQASLELGEGELPA---------ACLKPALTPVDPAEPQDA 562
Cdd:COG4717 225 LEEELEQLENELEAAALEERLKEARllllIAAALLALLGLGGSLLSLILTIAGvlflvlgllALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 563 LATCESDEAKMRRQAGVAAAASLVSVDGEAEAGGESG-------TRALRREVGRLQAELAAERRARERQ------GASFA 629
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLElldrieeLQELLREAEELEEELQLEELEQEIAallaeaGVEDE 384
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1532527591 630 EERRVWLEEKEKVIEYQKQLQlsyvemyQRNQQLERRLRERGAA 673
Cdd:COG4717 385 EELRAALEQAEEYQELKEELE-------ELEEQLEELLGELEEL 421
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
355-688 |
8.73e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 8.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 355 EERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAWE-------RELAELRQGCSGKLQQVARRAQ---------RAQQG 418
Cdd:PTZ00121 1144 EARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAarkaeevRKAEELRKAEDARKAEAARKAEeerkaeearKAEDA 1223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 419 LQLQVLRLQQDKKQLQEEAARLMRQREELEDKVAAcQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLS 498
Cdd:PTZ00121 1224 KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFE-EARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKK 1302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 499 EIVGLRSQLREGRAS--LREKEEQLLSLRDSfSSKQASLELGEGELPAACLKPALTPVDPAEPQDALATCESDEAKMRRQ 576
Cdd:PTZ00121 1303 KADEAKKKAEEAKKAdeAKKKAEEAKKKADA-AKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD 1381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 577 AGVAAAASLVSVD---GEAEAGGESGTRALRREVGRLQAElAAERRARERQGasfAEERRVWLEEKEKVIEYQKQlqlsy 653
Cdd:PTZ00121 1382 AAKKKAEEKKKADeakKKAEEDKKKADELKKAAAAKKKAD-EAKKKAEEKKK---ADEAKKKAEEAKKADEAKKK----- 1452
|
330 340 350
....*....|....*....|....*....|....*
gi 1532527591 654 VEMYQRNQQLERRLRERGAAGGAStptpQHGEEKK 688
Cdd:PTZ00121 1453 AEEAKKAEEAKKKAEEAKKADEAK----KKAEEAK 1483
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
351-545 |
1.40e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 351 IQELEERLWEKEQEVAALRRSLEQSEAAVAQvLEERQKAWERELAELRQgcsgKLQQVARRAQRAQQGLQLQVLRLQQDK 430
Cdd:COG4942 57 LAALERRIAALARRIRALEQELAALEAELAE-LEKEIAELRAELEAQKE----ELAELLRALYRLGRQPPLALLLSPEDF 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 431 KQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREG 510
Cdd:COG4942 132 LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL 211
|
170 180 190
....*....|....*....|....*....|....*
gi 1532527591 511 RASLREKEEQLLSLRDSFSSKQASLELGEGELPAA 545
Cdd:COG4942 212 AAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
347-667 |
1.99e-05 |
|
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: 47.58 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 347 PSALIqeLEERLWEKEQEVAALrrsLEQSEAAVAQVLEERQK------AWERELAELRQGCsGKLQQVARRAQRAQQGLQ 420
Cdd:pfam07888 27 PRAEL--LQNRLEECLQERAEL---LQAQEAANRQREKEKERykrdreQWERQRRELESRV-AELKEELRQSREKHEELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 421 LQVLRLQQDKKQLQEEAARLMRQRE-------ELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADV 493
Cdd:pfam07888 101 EKYKELSASSEELSEEKDALLAQRAahearirELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 494 SQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQasLELGEGELPAACLKPALTPVDPAepQDALATCESDEAKM 573
Cdd:pfam07888 181 QQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLT--QKLTTAHRKEAENEALLEELRSL--QERLNASERKVEGL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 574 RRQAGVAAA-------------------------ASLVSVDGEAEAGGESGT------------RALRREVGRLQAELAA 616
Cdd:pfam07888 257 GEELSSMAAqrdrtqaelhqarlqaaqltlqladASLALREGRARWAQERETlqqsaeadkdriEKLSAELQRLEERLQE 336
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1532527591 617 ERRARERQGASFAEER---RVWLEEKEKVIEYQK-----------QLQLSYVEMYQRNQQLERRL 667
Cdd:pfam07888 337 ERMEREKLEVELGREKdcnRVQLSESRRELQELKaslrvaqkekeQLQAEKQELLEYIRQLEQRL 401
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
349-524 |
2.08e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 349 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQ---GCSGKLQQVarRAQRAQQGLQLQVLR 425
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRL-ELEIEEVEArikKYEEQLGNV--RNNKEYEALQKEIES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 426 LQQDKKQLQEEAARLMRQREELEDKVAACQKEQADflprieetkwevcqkageislLKQQLKDSQADVSQKLSEIVGLRS 505
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAE---------------------LEAELEEKKAELDEELAELEAELE 159
|
170 180
....*....|....*....|
gi 1532527591 506 QLREGRASLREK-EEQLLSL 524
Cdd:COG1579 160 ELEAEREELAAKiPPELLAL 179
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
351-669 |
2.80e-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: 47.74 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 351 IQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRqgcsGKLQQVARRAQRAQQglqlqvlrlqqDK 430
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL-EEEIEELQ----KELYALANEISRLEQ-----------QK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 431 KQLQEEAARLMRQREELEDkvaacqkEQADFLPRIEETKWEVCQKAGEISLLKQQLkdsqADVSQKLSEivgLRSQLREG 510
Cdd:TIGR02168 305 QILRERLANLERQLEELEA-------QLEELESKLDELAEELAELEEKLEELKEEL----ESLEAELEE---LEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 511 RASLREKEEQLLSLRDSFSSKQASLELGEGELpaaclkpaltpvdpaEPQDALATCESDEAKMRRQAGVAAAASLVSVDG 590
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLELQIASLNNEI---------------ERLEARLERLEDRRERLQQEIEELLKKLEEAEL 435
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1532527591 591 EAEAGGESGTRALRREvgrLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQlSYVEMYQRNQQLERRLRE 669
Cdd:TIGR02168 436 KELQAELEELEEELEE---LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD-SLERLQENLEGFSEGVKA 510
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
339-545 |
5.38e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 5.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 339 FAACSPPSPSALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQgcsgKLQQVARRAQRAQQG 418
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL-ERRIAALAR----RIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 419 LQLQvlrlqqdKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQ----------QLKD 488
Cdd:COG4942 85 LAEL-------EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlaparreqaeELRA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1532527591 489 SQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAA 545
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE 214
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
352-670 |
8.42e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 352 QELEERLWEKEQEVAALRRSLEQSEAA--VAQVLEERQKAWE-RELAELRQGCSGKLQQVARRAQRAQQGLQLQVLRLQQ 428
Cdd:PTZ00121 1473 DEAKKKAEEAKKADEAKKKAEEAKKKAdeAKKAAEAKKKADEaKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 429 DKKQLQ--EEAARLMRQREELEDKVAACQKeqADFLPRIEETKWEvcqkagEISLLKQQLKDSQADVSQKLSEIVGLRSQ 506
Cdd:PTZ00121 1553 KAEELKkaEEKKKAEEAKKAEEDKNMALRK--AEEAKKAEEARIE------EVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 507 LREGRaSLREKEEQLLSLRDSFSSKQASLELGEGELPAACLKPALTPVDPAEPQDALATCESDEAK----MRRQAGVAAA 582
Cdd:PTZ00121 1625 LKKAE-EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKaaeaLKKEAEEAKK 1703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 583 ASLVSVDGEAEAGGESGTRAlRREVGRLQAELAAERRARERQGAsfaEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQ 662
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKK-AEEENKIKAEEAKKEAEEDKKKA---EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779
|
....*....
gi 1532527591 663 -LERRLRER 670
Cdd:PTZ00121 1780 vIEEELDEE 1788
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
429-672 |
8.48e-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: 46.20 E-value: 8.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 429 DKK---QLQEEAARLMRQREELEDKVAACQ--------------KEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQA 491
Cdd:TIGR02168 237 LREeleELQEELKEAEEELEELTAELQELEekleelrlevseleEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 492 DVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAACLKpaltpvdPAEPQDALATCESDEA 571
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR-------LEELEEQLETLRSKVA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 572 KMRRQAGvAAAASLVSVDGEAEAGGESGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQL 651
Cdd:TIGR02168 390 QLELQIA-SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468
|
250 260
....*....|....*....|.
gi 1532527591 652 SYVEMYQRNQQLERRLRERGA 672
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQA 489
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
429-684 |
8.92e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 8.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 429 DKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLR 508
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 509 EGRASLREkeeqllSLRDSFSSKQASLelgegelpaacLKPALTPVDPAEPQDALATCESDEAKMRRQAG--VAAAASLV 586
Cdd:COG4942 101 AQKEELAE------LLRALYRLGRQPP-----------LALLLSPEDFLDAVRRLQYLKYLAPARREQAEelRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 587 SVDGEAEAGGESgTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQlsyvemyQRNQQLERR 666
Cdd:COG4942 164 ALRAELEAERAE-LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE-------ALIARLEAE 235
|
250
....*....|....*...
gi 1532527591 667 LRERGAAGGASTPTPQHG 684
Cdd:COG4942 236 AAAAAERTPAAGFAALKG 253
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
345-676 |
1.64e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 345 PSPSALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQgcsgKLQQVARRAQRAqqglqlqvl 424
Cdd:COG4372 20 PKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQL-EEELEQARS----ELEQLEEELEEL--------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 425 rlqqdKKQLQEEAARLMRQREELEDKvaacQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLR 504
Cdd:COG4372 86 -----NEQLQAAQAELAQAQEELESL----QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 505 SQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAACLKPALTPVDPAEPQDALATCESDEAKMRRQAGVAAAAS 584
Cdd:COG4372 157 EQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 585 LVSVDGEAEAGGESGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEK--EKVIEYQKQLQLSYVEMYQRNQQ 662
Cdd:COG4372 237 ALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAalELKLLALLLNLAALSLIGALEDA 316
|
330
....*....|....
gi 1532527591 663 LERRLRERGAAGGA 676
Cdd:COG4372 317 LLAALLELAKKLEL 330
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
352-669 |
2.03e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 352 QELE-----ERLWEKEQEVAALRRSLEQseaavaqvLEERQKAWERELAELRQgcsgkLQQVARRAQRAQQGLQLQVLRL 426
Cdd:PRK02224 459 QPVEgsphvETIEEDRERVEELEAELED--------LEEEVEEVEERLERAED-----LVEAEDRIERLEERREDLEELI 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 427 QQDKKQLQEE---AARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQQLkDSQADVSQKLSEIVGL 503
Cdd:PRK02224 526 AERRETIEEKrerAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERI-ESLERIRTLLAAIADA 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 504 RSQ---LREGRASLREKEEQllsLRDSFSSKQASLELGEGELPAACLkpaltpvdpaepqdalatcesDEAKMRRQagvA 580
Cdd:PRK02224 605 EDEierLREKREALAELNDE---RRERLAEKRERKRELEAEFDEARI---------------------EEAREDKE---R 657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 581 AAASLVSVDGEAEAGGESGTRaLRREVGRLQAELAAERRARERQGAsfAEERRVWLEEkekVIEYQKQLQLSY----VEM 656
Cdd:PRK02224 658 AEEYLEQVEEKLDELREERDD-LQAEIGAVENELEELEELRERREA--LENRVEALEA---LYDEAEELESMYgdlrAEL 731
|
330
....*....|....
gi 1532527591 657 YQRN-QQLERRLRE 669
Cdd:PRK02224 732 RQRNvETLERMLNE 745
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
350-522 |
2.35e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 350 LIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQkawerELAELRQGCSGKLQQVARRAQRAqqglqlqvLRLQQD 429
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPELREELEKLEKEVK-----ELEELKEEIEELEKELESLEGSK--------RKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 430 KKQLQEEAARLMRQREELEDKVAACQ--KEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQL 507
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340
|
170
....*....|....*
gi 1532527591 508 REgrasLREKEEQLL 522
Cdd:PRK03918 341 EE----LKKKLKELE 351
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
464-673 |
2.72e-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: 44.28 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 464 RIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELP 543
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 544 AACLKPALTPVDPAEPQDALATCESDEAKmrRQAGVAAAASLVSVDGEAEAGGESGTRALRREVGRLQAELAAERRARER 623
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEE--LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1532527591 624 QGASFAEERRVWLEEKEKVIEY--------------QKQLQLSYVEMYQRNQQLERRLRERGAA 673
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLaaeieeleelieelESELEALLNERASLEEALALLRSELEEL 899
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
351-537 |
5.43e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 351 IQELEERLWEKEQEVAALRRSLEQ----SEAAVAQ---VLE---------ERQKAWERELAELRQGCSgkLQQVARRAQ- 413
Cdd:COG3096 439 AEDYLAAFRAKEQQATEEVLELEQklsvADAARRQfekAYElvckiagevERSQAWQTARELLRRYRS--QQALAQRLQq 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 414 -RAQQGLQLQVLRLQQDKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEislLKQQLKDSQAD 492
Cdd:COG3096 517 lRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSE---LRQQLEQLRAR 593
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1532527591 493 VSQ----------------KLSEIVGL----RSQLREGRASLREKEEQLLSLRDSFSSKQASLEL 537
Cdd:COG3096 594 IKElaarapawlaaqdaleRLREQSGEaladSQEVTAAMQQLLEREREATVERDELAARKQALES 658
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
351-679 |
1.80e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.86 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 351 IQELEERLWEKEQEVAALRRSLEQSEAAvAQVLEERQKAWERELAELRQGC------SGKLQQVARRAQRAQQ------- 417
Cdd:COG3096 356 LEELTERLEEQEEVVEEAAEQLAEAEAR-LEAAEEEVDSLKSQLADYQQALdvqqtrAIQYQQAVQALEKARAlcglpdl 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 418 --GLQLQVLRLQQDKKQLQEEAARLMRQREELEDkVAACQKEQADFLprieetkweVCQKAGEISLL------KQQLKD- 488
Cdd:COG3096 435 tpENAEDYLAAFRAKEQQATEEVLELEQKLSVAD-AARRQFEKAYEL---------VCKIAGEVERSqawqtaRELLRRy 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 489 -SQADVSQKLSeivGLRSQLREGRASLREKEEqLLSLRDSFSsKQASLELGEGELPAACLKPALTPVDpaEPQDALATCE 567
Cdd:COG3096 505 rSQQALAQRLQ---QLRAQLAELEQRLRQQQN-AERLLEEFC-QRIGQQLDAAEELEELLAELEAQLE--ELEEQAAEAV 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 568 SDEAKMRRQagvaaaaslvsvdgeaeaggESGTRALRREVGR-----LQAELAAERrARERQGASFAEERRVwLEEKEKV 642
Cdd:COG3096 578 EQRSELRQQ--------------------LEQLRARIKELAArapawLAAQDALER-LREQSGEALADSQEV-TAAMQQL 635
|
330 340 350
....*....|....*....|....*....|....*..
gi 1532527591 643 IEYQKQLQLSYVEMYQRNQQLERRLRERGAAGGASTP 679
Cdd:COG3096 636 LEREREATVERDELAARKQALESQIERLSQPGGAEDP 672
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
362-559 |
1.97e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 362 EQEVAALRRSLEQSEAAV---------------AQVLEERQKAWERELAELRQGCSGKLQQVAR-RAQRAQQGLQLQVLR 425
Cdd:COG3206 181 EEQLPELRKELEEAEAALeefrqknglvdlseeAKLLLQQLSELESQLAEARAELAEAEARLAAlRAQLGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 426 LQQDKKQLQEEAARLMRQREELEDK-------VAACQKEQADFLPRIEETKWEVCQKAG-EISLLKQQ---LKDSQADVS 494
Cdd:COG3206 261 QSPVIQQLRAQLAELEAELAELSARytpnhpdVIALRAQIAALRAQLQQEAQRILASLEaELEALQAReasLQAQLAQLE 340
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1532527591 495 QKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFssKQASLELGEGELPAACLKPALTPVDPAEP 559
Cdd:COG3206 341 ARLAELPELEAELRRLEREVEVARELYESLLQRL--EEARLAEALTVGNVRVIDPAVVPLKPVSP 403
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
352-520 |
2.09e-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: 41.70 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 352 QELEERlweKEQEVAALRRSLE-QSEAAVAQVLEERQK---AWERELAELRQGCSGK--LQQVARRAQRAQQGLQLQVLR 425
Cdd:pfam01576 319 QELRSK---REQEVTELKKALEeETRSHEAQLQEMRQKhtqALEELTEQLEQAKRNKanLEKAKQALESENAELQAELRT 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 426 LQQDKK-----------QLQEEAARLM---RQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQA 491
Cdd:pfam01576 396 LQQAKQdsehkrkklegQLQELQARLSeseRQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQE 475
|
170 180 190
....*....|....*....|....*....|...
gi 1532527591 492 ----DVSQKLSEIVGLRsQLREGRASLREKEEQ 520
Cdd:pfam01576 476 llqeETRQKLNLSTRLR-QLEDERNSLQEQLEE 507
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
350-491 |
2.21e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.77 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 350 LIQELEERLWEKEQEVAALRRSLEQSEAAVAQvLEERQKAWERELAELRQG---CSGKLQQVARRAQRAQQGLQLQVLRl 426
Cdd:smart00787 145 LKEGLDENLEGLKEDYKLLMKELELLNSIKPK-LRDRKDALEEELRQLKQLedeLEDCDPTELDRAKEKLKKLLQEIMI- 222
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1532527591 427 qqdKKQLQEEaarLMRQREELEDKVAACQKEQADFLPRI--EETKWEVCQK--AGEISLLKQQLKDSQA 491
Cdd:smart00787 223 ---KVKKLEE---LEEELQELESKIEDLTNKKSELNTEIaeAEKKLEQCRGftFKEIEKLKEQLKLLQS 285
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
432-670 |
2.57e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 432 QLQEEAARLMRQREELEDKVAACQK-EQADFlpriEETKWEVCQKagEISLLKQQLKDSQADvSQKLSEivgLRSQLREG 510
Cdd:COG4913 628 EAEERLEALEAELDALQERREALQRlAEYSW----DEIDVASAER--EIAELEAELERLDAS-SDDLAA---LEEQLEEL 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 511 RASLREKEEQLLSLRDSFSSKQASLELGEGELPAAclKPALTPVDPAEPQDALATCEsdeaKMRRQAGVAAAASLVSVDG 590
Cdd:COG4913 698 EAELEELEEELDELKGEIGRLEKELEQAEEELDEL--QDRLEAAEDLARLELRALLE----ERFAAALGDAVERELRENL 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 591 EAEaggesgTRALRREVGRLQAELaaeRRARERQGASFAEERRVWLEEKEKVIEYQKQL-QLSYVEMYQRNQQLERRLRE 669
Cdd:COG4913 772 EER------IDALRARLNRAEEEL---ERAMRAFNREWPAETADLDADLESLPEYLALLdRLEEDGLPEYEERFKELLNE 842
|
.
gi 1532527591 670 R 670
Cdd:COG4913 843 N 843
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
356-536 |
3.60e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 356 ERLWEKEQEVAALRRSLEQSEAAVAQV----LEERQKAWE--RELAELRQGCSGKLQQVARRAQRAQQGLQLQVLRLQQd 429
Cdd:PRK03918 486 EKVLKKESELIKLKELAEQLKELEEKLkkynLEELEKKAEeyEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKK- 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 430 KKQLQEEAARLMRQ--------REELEDKVAACQKEQADFLpRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIV 501
Cdd:PRK03918 565 LDELEEELAELLKEleelgfesVEELEERLKELEPFYNEYL-ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1532527591 502 GLRSQLREGRASL-----REKEEQLLSLRDSFSSKQASLE 536
Cdd:PRK03918 644 ELRKELEELEKKYseeeyEELREEYLELSRELAGLRAELE 683
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
375-668 |
3.77e-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: 40.82 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 375 SEAAVAQVLEERQKAWERELAELRQgcsgklqQVARRAQRAqqglqlqvlrlqqdkKQLQEEAARLMRQREELEDKVAAC 454
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQS-------ELRRIENRL---------------DELSQELSDASRKIGEIEKEIEQL 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 455 QKEQADFLPRIEEtkwevcqKAGEISLLKQ-------QLKDSQADVSQKLSEIVGLRSQL-----REGRASLREKEEQLL 522
Cdd:TIGR02169 729 EQEEEKLKERLEE-------LEEDLSSLEQeienvksELKELEARIEELEEDLHKLEEALndleaRLSHSRIPEIQAELS 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 523 SLRDSFSSKQASLELGEGELPAACLKPALTPVDPAEPQDALATCESDEAKMRRQ--AGVAAAASLVSVDGEAEAGG---E 597
Cdd:TIGR02169 802 KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEieNLNGKKEELEEELEELEAALrdlE 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 598 SGTRALRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQL----------------QLSYVEMYQRNQ 661
Cdd:TIGR02169 882 SRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELseiedpkgedeeipeeELSLEDVQAELQ 961
|
....*..
gi 1532527591 662 QLERRLR 668
Cdd:TIGR02169 962 RVEEEIR 968
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
602-670 |
3.85e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 38.33 E-value: 3.85e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1532527591 602 ALRREVGRLQAELAAERRARERQGASFAEERRVWLEEK--EKVIEYQKQLQLSYVEMYQRNQQLERRLRER 670
Cdd:smart00935 29 KRQAELEKLEKELQKLKEKLQKDAATLSEAAREKKEKElqKKVQEFQRKQQKLQQDLQKRQQEELQKILDK 99
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
432-653 |
4.67e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 432 QLQEEAARLMRQREELEDkvaacQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDSQADVSQKLSEIvgLRSQLREGR 511
Cdd:COG4913 229 ALVEHFDDLERAHEALED-----AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 512 ASLREKEEQLLSLRDSFSSKQASLElgegELPAACLKPALTPVDPAEPQDALATCESDEAKMRRQAGVAAAASLvsvdGE 591
Cdd:COG4913 302 AELARLEAELERLEARLDALREELD----ELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL----GL 373
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1532527591 592 AEAGGESGTRALRREVGRLQAELAAER-RARERQGASFAEERRVW--LEEKEKVIEYQKQLQLSY 653
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEEELeALEEALAEAEAALRDLRreLRELEAEIASLERRKSNI 438
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
346-457 |
5.78e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 346 SPSALIQELEERLWEKEQEVAALRRSLEQSEAAVAQvLEERQKAWERELAELRQgcsgKLQQVARRAQRAQQGLQLQVLR 425
Cdd:COG4913 682 ASSDDLAALEEQLEELEAELEELEEELDELKGEIGR-LEKELEQAEEELDELQD----RLEAAEDLARLELRALLEERFA 756
|
90 100 110
....*....|....*....|....*....|..
gi 1532527591 426 LQQDKKQLQEEAARLMRQREELEDKVAACQKE 457
Cdd:COG4913 757 AALGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
360-539 |
6.42e-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: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 360 EKEQEVAALRRSLE----------QSEAAVAQVLEERQKAW----ERELAELRQGCSGKLQQV--ARRAQRAQQGLQLQV 423
Cdd:pfam12128 661 EKQSEKDKKNKALAerkdsanerlNSLEAQLKQLDKKHQAWleeqKEQKREARTEKQAYWQVVegALDAQLALLKAAIAA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 424 LRLQQDK--KQLQEEAAR--------------LMRQREELEDKVAACQKEQADFL--------------PRIEETKWEVC 473
Cdd:pfam12128 741 RRSGAKAelKALETWYKRdlaslgvdpdviakLKREIRTLERKIERIAVRRQEVLryfdwyqetwlqrrPRLATQLSNIE 820
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1532527591 474 QKAGEislLKQQLKDSQADVSQKLSEIVGLRSQLR-------EGRASLREKEEQLLSLRDSFSSKQASLELGE 539
Cdd:pfam12128 821 RAISE---LQQQLARLIADTKLRRAKLEMERKASEkqqvrlsENLRGLRCEMSKLATLKEDANSEQAQGSIGE 890
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
351-616 |
6.44e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 351 IQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELrqgcsgklqqvarraqraqqglqlqvlrlqqdK 430
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL-QAEIDKL--------------------------------Q 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 431 KQLQEEAARLMRQREELEDKVAACQKEQ---------------ADFLPRIEETKWEVCQKAGEISLL---KQQLKDSQAD 492
Cdd:COG3883 72 AEIAEAEAEIEERREELGERARALYRSGgsvsyldvllgsesfSDFLDRLSALSKIADADADLLEELkadKAELEAKKAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 493 VSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAACLKPALTPVDPAEPQDALATCESDEAK 572
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1532527591 573 MRRQAGVAAAASLVSVDGEAEAGGESGTRALRREVGRLQAELAA 616
Cdd:COG3883 232 AAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAG 275
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
344-447 |
6.60e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 39.93 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 344 PPSPSALIQELEerlwekeQEVAALRRSLEQ--SEAAVAQVLEERQKAWERELAELRQGCSGKLQQVARRAQRAQQGLQL 421
Cdd:PRK11448 137 PEDPENLLHALQ-------QEVLTLKQQLELqaREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAE 209
|
90 100
....*....|....*....|....*.
gi 1532527591 422 QVLRLQQDKKQLQEEAARLMRQREEL 447
Cdd:PRK11448 210 TSQERKQKRKEITDQAAKRLELSEEE 235
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
351-541 |
6.99e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 351 IQELEERLWEKEQEVAALRRSLEQSEAAVAQVLE-----ERQKAWERELAELRQGCSGKLQQVaRRAQRAQQGLQLQVLR 425
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEvmklyEEEKKMKAEEAKKAEEAKIKAEEL-KKAEEEKKKVEQLKKK 1641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 426 LQQDKKQLQE--EAARLMRQREELEDKVAACQKEQADFLPRIEETKwevcQKAGEISLLKQQLKDSQADVSQKLSEIVGL 503
Cdd:PTZ00121 1642 EAEEKKKAEElkKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE----KKAAEALKKEAEEAKKAEELKKKEAEEKKK 1717
|
170 180 190
....*....|....*....|....*....|....*...
gi 1532527591 504 RSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGE 541
Cdd:PTZ00121 1718 AEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
352-703 |
7.23e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 352 QELEERLWEKEQEVAALRRSLEQSEAAVA-QVLEERQKAWE-RELAELRQgcsgKLQQVARRAQRAQQGLQLQVLRLQQD 429
Cdd:PTZ00121 1434 DEAKKKAEEAKKADEAKKKAEEAKKAEEAkKKAEEAKKADEaKKKAEEAK----KADEAKKKAEEAKKKADEAKKAAEAK 1509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 430 KKQLQEEAARLMRQREELEDkvaACQKEQADFLPRIEET-KWEVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQ-L 507
Cdd:PTZ00121 1510 KKADEAKKAEEAKKADEAKK---AEEAKKADEAKKAEEKkKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEeA 1586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 508 REGRASLREKEEQLLSLRDSFSSKQASLElGEGELPAACLKPAltpVDPAEPQDALATCESDEAKMRRQAGVAAAASLVS 587
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMKAEEAKKA-EEAKIKAEELKKA---EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK 1662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 588 VDGEAEAGGESgtralRREVGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQLERRL 667
Cdd:PTZ00121 1663 AAEEAKKAEED-----KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737
|
330 340 350
....*....|....*....|....*....|....*.
gi 1532527591 668 RERGAAGGASTPTPQHGEEKKAWTPSRLERIESTEI 703
Cdd:PTZ00121 1738 EAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEI 1773
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
346-623 |
7.49e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 39.56 E-value: 7.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 346 SPSALIQELEERL--WEKEQEVAALRRSLEQSEAAVAQVLEERQKAWERELAELRQGCSGKLQQVARRaqraqqglqlqv 423
Cdd:COG5185 306 DIKKATESLEEQLaaAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELS------------ 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 424 lrlqQDKKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEI--------------SLLKQQLKDS 489
Cdd:COG5185 374 ----KSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELqrqieqatssneevSKLLNELISE 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 490 QADVSQKLSEIVGLRSQ------LREGRASLREKEEQLLSLRDSFSSKQASLE--LGEGELPAACLKPALTPVDPAE-PQ 560
Cdd:COG5185 450 LNKVMREADEESQSRLEeaydeiNRSVRSKKEDLNEELTQIESRVSTLKATLEklRAKLERQLEGVRSKLDQVAESLkDF 529
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1532527591 561 DALATCESDEAK-MRRQAGVAAAASLVSVDGEAEAggesgTRALRREVGRLQAELAAERRARER 623
Cdd:COG5185 530 MRARGYAHILALeNLIPASELIQASNAKTDGQAAN-----LRTAVIDELTQYLSTIESQQARED 588
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
352-542 |
7.75e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 352 QELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAWER---------ELAELRQ----------GCSGKLQQVARRA 412
Cdd:PRK02224 202 KDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVleeheerreELETLEAeiedlretiaETEREREELAEEV 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 413 --QRAQQGLQLQVLRLQQDKKQLQE-EAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAGEISLLKQQLKDS 489
Cdd:PRK02224 282 rdLRERLEELEEERDDLLAEAGLDDaDAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEEL 361
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1532527591 490 QADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGEL 542
Cdd:PRK02224 362 REEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL 414
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
349-533 |
8.32e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 38.35 E-value: 8.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 349 ALIQELEErlwekeqEVAALRRSLEQSEAAVAQVLEERQ------KAWERELAELRQgcsgKLQQVARRAQRAQQGLQLQ 422
Cdd:pfam13851 26 ELIKSLKE-------EIAELKKKEERNEKLMSEIQQENKrlteplQKAQEEVEELRK----QLENYEKDKQSLKNLKARL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532527591 423 vlrlqqdkKQLQEEAARLMRQREELEDKVAACQKEQADFLPRIEETKWEVCQKAG-EISLLKQQLKDSQADVSQK---LS 498
Cdd:pfam13851 95 --------KVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQKTGlKNLLLEKKLQALGETLEKKeaqLN 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 1532527591 499 EIVglrsqlreGRASLREKEEQLLS--LRDSFSSKQA 533
Cdd:pfam13851 167 EVL--------AAANLDPDALQAVTekLEDVLESKNQ 195
|
|
| |
