|
Name |
Accession |
Description |
Interval |
E-value |
| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
421-617 |
1.19e-70 |
|
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: 227.57 E-value: 1.19e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 421 VCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAAC----- 495
Cdd:pfam06818 5 VCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKneael 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 496 --------------LKPALTPVDPAEPQdalATCESDEAKMRRQAgvaaaaslvsvdgeaeaggESGTRALRREVGRLQA 561
Cdd:pfam06818 85 lrekvgkleeevsgLREALSDVSPSGYE---SVYESDEAKEQRQE-------------------EADLGSLRREVERLRA 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1917203328 562 ELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQLERRLR 617
Cdd:pfam06818 143 ELREERQRRERQASSFEQERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
321-593 |
5.32e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 5.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 321 IQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQGcSGKLQQVARRAQRAQQGLQLQVLRLQQDK 400
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA-EAELAEAEEE-LEELAEELLEALRAAAELAAQLEELEEAE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 401 KQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSK 480
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 481 QASLEL-----GEGELPAACLKPALTPVDPAEPQDALATCESDEAKMRRQAGVAAAASLVSVDGEAEAGGESGTRALRRE 555
Cdd:COG1196 490 AARLLLlleaeADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAA 569
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1917203328 556 ------------VGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIE 593
Cdd:COG1196 570 kagratflpldkIRARAALAAALARGAIGAAVDLVASDLREADARYYVLG 619
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
318-598 |
2.87e-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: 63.54 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 318 SALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQGCSGKLQQVARRAQRAQQGLQLQvlrlq 397
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL-SRQISALRKDLARLEAEVEQLEERIAQLSKEL----- 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 398 qdkKQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSF 477
Cdd:TIGR02168 757 ---TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 478 SSKQASLELGEGELpaaclkpALTPVDPAEPQDALATCESDEAKMRRQagVAAAASLVSVDGEAEAGGESGTRALRREVG 557
Cdd:TIGR02168 834 AATERRLEDLEEQI-------EELSEDIESLAAEIEELEELIEELESE--LEALLNERASLEEALALLRSELEELSEELR 904
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1917203328 558 RLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQL 598
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
319-473 |
1.76e-07 |
|
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: 52.62 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 319 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQ---GCSGKLQQVarRAQRAQQGLQLQVLR 395
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRL-ELEIEEVEArikKYEEQLGNV--RNNKEYEALQKEIES 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1917203328 396 LQQDKKQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREK-EEQLLSL 473
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKiPPELLAL 179
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
321-590 |
1.14e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 321 IQELEERLWEKEQEVAALRRSLEQSEAAvAQVLEERQKAWERELAELRQgcsgKLQQVARRAQRAQQ---GLQLQVLRLQ 397
Cdd:PRK02224 281 VRDLRERLEELEEERDDLLAEAGLDDAD-AEAVEARREELEDRDEELRD----RLEECRVAAQAHNEeaeSLREDADDLE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 398 QDKKQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQA---DVSQKLSEIVGLRSQLREGRASLREKEEqllSLR 474
Cdd:PRK02224 356 ERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRErfgDAPVDLGNAEDFLEELREERDELREREA---ELE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 475 DSFSSKQASLELGEGELPAACLKPALTPVDPAEPQDALATCESDEAKMRRQAGvAAAASLVSVDGEAEAGGESGTRALRR 554
Cdd:PRK02224 433 ATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELE-DLEEEVEEVEERLERAEDLVEAEDRI 511
|
250 260 270
....*....|....*....|....*....|....*.
gi 1917203328 555 EVGRLQAELAAERRARERQGasfAEERRVWLEEKEK 590
Cdd:PRK02224 512 ERLEERREDLEELIAERRET---IEEKRERAEELRE 544
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
324-470 |
4.54e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 324 LEERLWEKEQEVAALRRSLEQseaavaqvLEERQKAWERELAELRQgcsgKLQQVARR---AQRAQQGLQLQVLRLQQDK 400
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEE--------VDKEFAETRDELKDYRE----KLEKLKREineLKRELDRLQEELQRLSEEL 422
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 401 KQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQL 470
Cdd:TIGR02169 423 ADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
310-472 |
6.68e-05 |
|
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: 46.17 E-value: 6.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 310 AACSPPSPSALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQ------KAWERELAELRQGCSGKLQQVaRRAQ 383
Cdd:pfam05667 312 APAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKklessiKQVEEELEELKEQNEELEKQY-KVKK 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 384 RAQQGLQLQVLRLQQDKKQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASL 463
Cdd:pfam05667 391 KTLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEA 470
|
170
....*....|..
gi 1917203328 464 REKEE---QLLS 472
Cdd:pfam05667 471 KQKEElykQLVA 482
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
314-460 |
4.89e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.40 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 314 PPSPSALIQELEerlwekeQEVAALRRSLEQ--SEAAVAQVLEERQKAWERELAELRQGCSGKLQQVARRAQRAQQGLQL 391
Cdd:PRK11448 137 PEDPENLLHALQ-------QEVLTLKQQLELqaREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAE 209
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917203328 392 QVLRLQQDKKQLQEEAARLMRQREELEDKvcqkageisLLKQQLKDS--QADvSQKLSEIVGLRSQlrEGR 460
Cdd:PRK11448 210 TSQERKQKRKEITDQAAKRLELSEEETRI---------LIDQQLRKAgwEAD-SKTLRFSKGARPE--KGR 268
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
551-619 |
4.25e-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: 37.95 E-value: 4.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917203328 551 ALRREVGRLQAELAAERRARERQGASFAEERRVWLEEK--EKVIEYQKQLQLSYVEMYQRNQQLERRLRER 619
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 ... |
421-617 |
1.19e-70 |
|
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: 227.57 E-value: 1.19e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 421 VCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAAC----- 495
Cdd:pfam06818 5 VCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKneael 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 496 --------------LKPALTPVDPAEPQdalATCESDEAKMRRQAgvaaaaslvsvdgeaeaggESGTRALRREVGRLQA 561
Cdd:pfam06818 85 lrekvgkleeevsgLREALSDVSPSGYE---SVYESDEAKEQRQE-------------------EADLGSLRREVERLRA 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1917203328 562 ELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQLERRLR 617
Cdd:pfam06818 143 ELREERQRRERQASSFEQERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
321-593 |
5.32e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 5.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 321 IQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQGcSGKLQQVARRAQRAQQGLQLQVLRLQQDK 400
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA-EAELAEAEEE-LEELAEELLEALRAAAELAAQLEELEEAE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 401 KQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSK 480
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 481 QASLEL-----GEGELPAACLKPALTPVDPAEPQDALATCESDEAKMRRQAGVAAAASLVSVDGEAEAGGESGTRALRRE 555
Cdd:COG1196 490 AARLLLlleaeADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAA 569
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1917203328 556 ------------VGRLQAELAAERRARERQGASFAEERRVWLEEKEKVIE 593
Cdd:COG1196 570 kagratflpldkIRARAALAAALARGAIGAAVDLVASDLREADARYYVLG 619
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
319-646 |
2.14e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 319 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQvLEERQKAWERELAELRQgcsgKLQQVARRAQRAqqglQLQVLRLQQ 398
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEE-LRLELEELELELEEAQA----EEYELLAELARL----EQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 399 DKKQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFS 478
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 479 SKQASLELGEGELpaaclkpaltpvdpAEPQDALATCESDEAKMRRQAGVAAAASLVSVDGEAEAggESGTRALRREVGR 558
Cdd:COG1196 390 EALRAAAELAAQL--------------EELEEAEEALLERLERLEEELEELEEALAELEEEEEEE--EEALEEAAEEEAE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 559 LQAELAAERRARERQGASFAEERRVWLEEKEKVIEyQKQLQLSYVEMYQRNQQLERRLRERGAAGGASTPTPQHGEEkkA 638
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAE-AAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL--I 530
|
....*...
gi 1917203328 639 WTPSRLER 646
Cdd:COG1196 531 GVEAAYEA 538
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
318-598 |
2.87e-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: 63.54 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 318 SALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQGCSGKLQQVARRAQRAQQGLQLQvlrlq 397
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL-SRQISALRKDLARLEAEVEQLEERIAQLSKEL----- 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 398 qdkKQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSF 477
Cdd:TIGR02168 757 ---TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 478 SSKQASLELGEGELpaaclkpALTPVDPAEPQDALATCESDEAKMRRQagVAAAASLVSVDGEAEAGGESGTRALRREVG 557
Cdd:TIGR02168 834 AATERRLEDLEEQI-------EELSEDIESLAAEIEELEELIEELESE--LEALLNERASLEEALALLRSELEELSEELR 904
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1917203328 558 RLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQL 598
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
321-525 |
1.18e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 321 IQELEERLWEKEQEVAALRRSLEQSEAAVAQvLEERQKAWERELAELRQGcSGKLQQVARRAQRAQQGLQLQVLRLQQDK 400
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEQLKEELKA-LREALDELRAELTLLNEE-AANLRERLESLERRIAATERRLEDLEEQI 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 401 KQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSsk 480
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA-- 925
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1917203328 481 QASLELGEGELPAACLKPALTPVDPAEPQDALA---TCESDEAKMRRQ 525
Cdd:TIGR02168 926 QLELRLEGLEVRIDNLQERLSEEYSLTLEEAEAlenKIEDDEEEARRR 973
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
319-619 |
1.74e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 319 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAWERELAELRQGCSGKLQQVARRAQRAQQGLQLQVLRLQQ 398
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 399 DKKQLQEEAARLMRQREELEDKvcqkageiSLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFS 478
Cdd:COG1196 487 AEAAARLLLLLEAEADYEGFLE--------GVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEV 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 479 SKQASLELGE------GELPAACLKPALTPVDPAEPQD-----ALATCESDEAKMRRQAGVAAAASLVSVDGEAEAGGE- 546
Cdd:COG1196 559 AAAAIEYLKAakagraTFLPLDKIRARAALAAALARGAigaavDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRr 638
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1917203328 547 -SGTRALRREV-----GRLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQLERRLRER 619
Cdd:COG1196 639 aVTLAGRLREVtlegeGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERL 717
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
318-589 |
1.56e-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: 54.68 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 318 SALIQELEERLWEKEQEVAALRRSLEQSEAAVaQVLEERQKAWERELAELRQgcsgKLQQVARRAQRAQQGLQLQVLRLQ 397
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKEL-YALANEISRLEQQKQILRE----RLANLERQLEELEAQLEELESKLD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 398 QDKK---QLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLR 474
Cdd:TIGR02168 334 ELAEelaELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 475 DSFSSKQASLELGEGELPAACLKPALTPVDPAEPqdalatcESDEAKMRRQAGVAAAASLvsvdGEAEAGGESGTRALRR 554
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLEEAELKELQAELEELEE-------ELEELQEELERLEEALEEL----REELEEAEQALDAAER 482
|
250 260 270
....*....|....*....|....*....|....*
gi 1917203328 555 EVGRLQAELAAERRARERQGASFAEERRVWLEEKE 589
Cdd:TIGR02168 483 ELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
319-473 |
1.76e-07 |
|
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: 52.62 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 319 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQ---GCSGKLQQVarRAQRAQQGLQLQVLR 395
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRL-ELEIEEVEArikKYEEQLGNV--RNNKEYEALQKEIES 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1917203328 396 LQQDKKQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREK-EEQLLSL 473
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKiPPELLAL 179
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
320-618 |
3.85e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 320 LIQELEERLwekeqevAALRRsleQSEAAV-AQVLEERQKAWERELAELRqgcsgklqqvaRRAQRAqqglqlQVLRLQQ 398
Cdd:COG1196 194 ILGELERQL-------EPLER---QAEKAErYRELKEELKELEAELLLLK-----------LRELEA------ELEELEA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 399 DKKQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFS 478
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 479 SKQASLELGEGELPAACLKpaltpVDPAEPQDALATCESDEAKMRRQAGVAAAASLVSVDGEAEAGGESGTRALRREVGR 558
Cdd:COG1196 327 ELEEELEELEEELEELEEE-----LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 559 LQAELAAERRARERQgASFAEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQLERRLRE 618
Cdd:COG1196 402 LEELEEAEEALLERL-ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
321-480 |
1.06e-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: 50.31 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 321 IQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQgcsgKLQQVARRAQRAQQGLQLQVLRLqqDK 400
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDL-EKEIKRLEL----EIEEVEARIKKYEEQLGNVRNNK--EY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 401 KQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSK 480
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
325-619 |
3.06e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 325 EERLWEKEQEVAALRRSLEQSEAAVAQvLEERQKAWERELAELRQgcsgkLQQVARRaqraqqglqlqvlrlQQDKKQLQ 404
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEA-LEAELDALQERREALQR-----LAEYSWD---------------EIDVASAE 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 405 EEAARLMRQREELEDkvcqKAGEISLLKQQLKDSQADvsqkLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQASL 484
Cdd:COG4913 668 REIAELEAELERLDA----SSDDLAALEEQLEELEAE----LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 485 ELGEGELPAACLKPALtpvdPAEPQDALatcesdEAKMRRQAgvaaaaslvsvdgeaeaggESGTRALRREVGRLQAELa 564
Cdd:COG4913 740 EDLARLELRALLEERF----AAALGDAV------ERELRENL-------------------EERIDALRARLNRAEEEL- 789
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1917203328 565 aeRRARERQGASFAEERRVWLEEKEKVIEYQKQL-QLSYVEMYQRNQQLERRLRER 619
Cdd:COG4913 790 --ERAMRAFNREWPAETADLDADLESLPEYLALLdRLEEDGLPEYEERFKELLNEN 843
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
309-584 |
3.95e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 309 FAACSPPSPSALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQgcsgKLQQVARRAQRAQQG 388
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL-ERRIAALAR----RIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 389 LQLQvlrlqqdKKQLQEEAARLMRQREELED--KVCQKAGEISLLKQQLKDSQADVSQKLSEIVG-LRSQLREGRASLRE 465
Cdd:COG4942 85 LAEL-------EKEIAELRAELEAQKEELAEllRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKyLAPARREQAEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 466 KEEQLLSLRDSFSSKQASLELGEGELpaaclkpaltpvdpAEPQDALAtcesdEAKMRRQAGVAAAASLVSVDGEAEAGG 545
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAEL--------------EEERAALE-----ALKAERQKLLARLEKELAELAAELAEL 218
|
250 260 270
....*....|....*....|....*....|....*....
gi 1917203328 546 ESGTRALRREVGRLQAELAAerRARERQGASFAEERRVW 584
Cdd:COG4942 219 QQEAEELEALIARLEAEAAA--AAERTPAAGFAALKGKL 255
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
321-618 |
4.36e-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: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 321 IQELEERLWEKEQEVAALRRSLEQSEAAVAQ------VLEERQKAWERELAELRQGCSGKLQQVARRAQRaqqglqlqVL 394
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEElrlevsELEEEIEELQKELYALANEISRLEQQKQILRER--------LA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 395 RLQQDKKQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLkdsqADVSQKLSEivgLRSQLREGRASLREKEEQLLSLR 474
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL----ESLEAELEE---LEAELEELESRLEELEEQLETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 475 DSFSSKQASLELGEGELpaaclkpaltpvdpaEPQDALATCESDEAKMRRQAGVAAAASLVSVDGEAEAGGESGTRALRR 554
Cdd:TIGR02168 386 SKVAQLELQIASLNNEI---------------ERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELE 450
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1917203328 555 EvgrLQAELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQLQlSYVEMYQRNQQLERRLRE 618
Cdd:TIGR02168 451 E---LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD-SLERLQENLEGFSEGVKA 510
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
404-622 |
7.99e-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: 49.28 E-value: 7.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 404 QEEAARLMRQRE--ELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQ 481
Cdd:TIGR02168 667 KTNSSILERRREieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 482 ASLELGEGELPAACLKPALTPVDPAEPQDALATCESDEAKmrRQAGVAAAASLVSVDGEAEAGGESGTRALRREVGRLQA 561
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE--LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1917203328 562 ELAAERRARERQGASFAEERRVWLEEKEKVIEY--------------QKQLQLSYVEMYQRNQQLERRLRERGAA 622
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLaaeieeleelieelESELEALLNERASLEEALALLRSELEEL 899
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
321-590 |
1.14e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 321 IQELEERLWEKEQEVAALRRSLEQSEAAvAQVLEERQKAWERELAELRQgcsgKLQQVARRAQRAQQ---GLQLQVLRLQ 397
Cdd:PRK02224 281 VRDLRERLEELEEERDDLLAEAGLDDAD-AEAVEARREELEDRDEELRD----RLEECRVAAQAHNEeaeSLREDADDLE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 398 QDKKQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQA---DVSQKLSEIVGLRSQLREGRASLREKEEqllSLR 474
Cdd:PRK02224 356 ERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRErfgDAPVDLGNAEDFLEELREERDELREREA---ELE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 475 DSFSSKQASLELGEGELPAACLKPALTPVDPAEPQDALATCESDEAKMRRQAGvAAAASLVSVDGEAEAGGESGTRALRR 554
Cdd:PRK02224 433 ATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELE-DLEEEVEEVEERLERAEDLVEAEDRI 511
|
250 260 270
....*....|....*....|....*....|....*.
gi 1917203328 555 EVGRLQAELAAERRARERQGasfAEERRVWLEEKEK 590
Cdd:PRK02224 512 ERLEERREDLEELIAERRET---IEEKRERAEELRE 544
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
319-485 |
1.98e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 319 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQV----------------------LEERQKAWERELAELRQGcSGKLQ 376
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALqerrealqrlaeyswdeidvasAEREIAELEAELERLDAS-SDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 377 QVARRAQRAqqglqlqvlrlQQDKKQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQL 456
Cdd:COG4913 689 ALEEQLEEL-----------EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAA 757
|
170 180
....*....|....*....|....*....
gi 1917203328 457 REGRASLREKEEQLLSLRDSFSSKQASLE 485
Cdd:COG4913 758 ALGDAVERELRENLEERIDALRARLNRAE 786
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
314-619 |
2.06e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 314 PPSPSALIQELEERLWEKEQEVAALRRSLEQSEAavaqvLEERQKAWERELAELRQGCSGKLQQVARRAQRAqqglqlqv 393
Cdd:COG4717 66 PELNLKELKELEEELKEAEEKEEEYAELQEELEE-----LEEELEELEAELEELREELEKLEKLLQLLPLYQ-------- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 394 lrlqqDKKQLQEEAARLMRQREELEDKVC---QKAGEISLLKQQLKDSQADVSQKLSEI-VGLRSQLREGRASLREKEEQ 469
Cdd:COG4717 133 -----ELEALEAELAELPERLEELEERLEelrELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 470 LLSLRDSFSSKQASLELGEGELPAAclkpaltpvdpAEPQDALATCESDEAKMRRQAGVAAAASLVSVDGEAEAGGESGT 549
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQL-----------ENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 550 RALRREVG----------RLQAELAAERRARERQGASFAEERRVWLEEKEKV---IEYQKQLQLSYVEMYQRNQQLERRL 616
Cdd:COG4717 277 GVLFLVLGllallflllaREKASLGKEAEELQALPALEELEEEELEELLAALglpPDLSPEELLELLDRIEELQELLREA 356
|
...
gi 1917203328 617 RER 619
Cdd:COG4717 357 EEL 359
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
322-622 |
2.24e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 322 QELEERLWEKEQEVAALRRSLEQSEAAVAQvLEERQKAWE--RELAELRQgcsgKLQQVARRAQRAqQGLQLQVLRLQQD 399
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEK-LEKLLQLLPlyQELEALEA----ELAELPERLEEL-EERLEELRELEEE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 400 KKQLQEEAARLMRQREELEDKVC-QKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRD--- 475
Cdd:COG4717 165 LEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALeer 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 476 ---------------SFSSKQASLELGEGELPA---------ACLKPALTPVDPAEPQDALATCESDEAKMRRQAGVAAA 531
Cdd:COG4717 245 lkearlllliaaallALLGLGGSLLSLILTIAGvlflvlgllALLFLLLAREKASLGKEAEELQALPALEELEEEELEEL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 532 ASLVSVDGEAEAGGESG-------TRALRREVGRLQAELAAERRARERQ------GASFAEERRVWLEEKEKVIEYQKQL 598
Cdd:COG4717 325 LAALGLPPDLSPEELLElldrieeLQELLREAEELEEELQLEELEQEIAallaeaGVEDEEELRAALEQAEEYQELKEEL 404
|
330 340
....*....|....*....|....
gi 1917203328 599 QlsyvemyQRNQQLERRLRERGAA 622
Cdd:COG4717 405 E-------ELEEQLEELLGELEEL 421
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
324-470 |
4.54e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 324 LEERLWEKEQEVAALRRSLEQseaavaqvLEERQKAWERELAELRQgcsgKLQQVARR---AQRAQQGLQLQVLRLQQDK 400
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEE--------VDKEFAETRDELKDYRE----KLEKLKREineLKRELDRLQEELQRLSEEL 422
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 401 KQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQL 470
Cdd:TIGR02169 423 ADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
319-495 |
5.97e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 319 ALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAWERELAELRQGCSGKLQQVARRAQRAqqglqlqvlrlqq 398
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRR------------- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 399 dkKQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFS 478
Cdd:COG4913 362 --ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIP 439
|
170 180
....*....|....*....|....*
gi 1917203328 479 SKQ--------ASLELGEGELPAAC 495
Cdd:COG4913 440 ARLlalrdalaEALGLDEAELPFVG 464
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
310-472 |
6.68e-05 |
|
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: 46.17 E-value: 6.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 310 AACSPPSPSALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQ------KAWERELAELRQGCSGKLQQVaRRAQ 383
Cdd:pfam05667 312 APAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKklessiKQVEEELEELKEQNEELEKQY-KVKK 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 384 RAQQGLQLQVLRLQQDKKQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASL 463
Cdd:pfam05667 391 KTLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEA 470
|
170
....*....|..
gi 1917203328 464 REKEE---QLLS 472
Cdd:pfam05667 471 KQKEElykQLVA 482
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
315-625 |
1.13e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 315 PSPSALIQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQgcsgKLQQVARRAQRAQQGLQLQVL 394
Cdd:COG4372 20 PKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQL-EEELEQARS----ELEQLEEELEELNEQLQAAQA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 395 RLQQDKKQL---QEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLL 471
Cdd:COG4372 95 ELAQAQEELeslQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 472 SLRDSFSSKQASLELGEGELPAACLKPALTPVDPAEPQDALATCESDEAKMRRQAGVAAAASLVSVDGEAEAGGESGTRA 551
Cdd:COG4372 175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1917203328 552 LRREVGRLQAELAAERRARERQGASFAEERRVWLEEK--EKVIEYQKQLQLSYVEMYQRNQQLERRLRERGAAGGA 625
Cdd:COG4372 255 VILKEIEELELAILVEKDTEEEELEIAALELEALEEAalELKLLALLLNLAALSLIGALEDALLAALLELAKKLEL 330
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
400-593 |
1.40e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 400 KKQLQEEAARLMRQREELEdkvcqkagEISLLKQQLKDSQADVSQKLSEivglRSQLREgraSLREKEEQLLSLRDSFSS 479
Cdd:PRK02224 233 RETRDEADEVLEEHEERRE--------ELETLEAEIEDLRETIAETERE----REELAE---EVRDLRERLEELEEERDD 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 480 KQASLELGEGELPAAclkpaltpvdpAEPQDALATCESDEAKMRRQAGVAAAASLVSVDGEAEAGGESGTRA--LRREVG 557
Cdd:PRK02224 298 LLAEAGLDDADAEAV-----------EARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAeeLREEAA 366
|
170 180 190
....*....|....*....|....*....|....*.
gi 1917203328 558 RLQAELAAERRARerqgasfaEERRVWLEEKEKVIE 593
Cdd:PRK02224 367 ELESELEEAREAV--------EDRREEIEELEEEIE 394
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
321-491 |
1.75e-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: 45.06 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 321 IQELEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKAwERELAELRQgcsgKLQQVARRAQRAQqglqlqvlrlqqdk 400
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAEL-KEELEDLRA----ELEEVDKEFAETR-------------- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 401 kqlqeeaARLMRQREELEDkvcqkageislLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSK 480
Cdd:TIGR02169 385 -------DELKDYREKLEK-----------LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK 446
|
170
....*....|.
gi 1917203328 481 QASLELGEGEL 491
Cdd:TIGR02169 447 ALEIKKQEWKL 457
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
347-633 |
1.76e-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: 44.37 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 347 AAVAQVLEERQKAWERELAELRQgcsgKLQQVARRAQraqqglqlqvlrlqqdkkQLQEEAARLMRQREELEDKVCQKAG 426
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQ----EIAELEKELA------------------ALKKEEKALLKQLAALERRIAALAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 427 EISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREkeeqllSLRDSFSSKQASLelgegelpaacLKPALTPVDPA 506
Cdd:COG4942 70 RIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE------LLRALYRLGRQPP-----------LALLLSPEDFL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 507 EPQDALATCESDEAKMRRQAG--VAAAASLVSVDGEAEAGGESgTRALRREVGRLQAELAAERRARERQGASFAEERRVW 584
Cdd:COG4942 133 DAVRRLQYLKYLAPARREQAEelRADLAELAALRAELEAERAE-LEALLAELEEERAALEALKAERQKLLARLEKELAEL 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1917203328 585 LEEKEKVIEYQKQLQlsyvemyQRNQQLERRLRERGAAGGASTPTPQHG 633
Cdd:COG4942 212 AAELAELQQEAEELE-------ALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
314-570 |
2.07e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 314 PPSPSALIQELEE---RLWEKEQEVAALRRSLEQSEAAVAQVlEERQKAWEReLAELRQGCSGKLQQVARRAQRAQQGLQ 390
Cdd:COG4913 220 EPDTFEAADALVEhfdDLERAHEALEDAREQIELLEPIRELA-ERYAAARER-LAELEYLRAALRLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 391 LqvlrlqqdkkQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADvsqklsEIVGLRSQLREGRASLREKEEQL 470
Cdd:COG4913 298 E----------ELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD------RLEQLEREIERLERELEERERRR 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 471 LSLRDSFSSKQASLELGEGELPAAClkpaltpvdpAEPQDALATCESDEAKMRRQAGVAAAASlvsvdgeaeaggesgtR 550
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALR----------AEAAALLEALEEELEALEEALAEAEAAL----------------R 415
|
250 260
....*....|....*....|
gi 1917203328 551 ALRREVGRLQAELAAERRAR 570
Cdd:COG4913 416 DLRRELRELEAEIASLERRK 435
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
321-470 |
2.11e-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: 44.56 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 321 IQELEERLWEKEQEVAALRRSLEQ----SEAAVAQ---VLE---------ERQKAWERELAELRQGCSgkLQQVARRAQ- 383
Cdd:COG3096 439 AEDYLAAFRAKEQQATEEVLELEQklsvADAARRQfekAYElvckiagevERSQAWQTARELLRRYRS--QQALAQRLQq 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 384 -RAQQGLQLQVLRLQQDKKQLQEEAARlmRQREELEDkvcqkAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRAS 462
Cdd:COG3096 517 lRAQLAELEQRLRQQQNAERLLEEFCQ--RIGQQLDA-----AEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQ 589
|
....*...
gi 1917203328 463 LREKEEQL 470
Cdd:COG3096 590 LRARIKEL 597
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
322-612 |
2.79e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 322 QELEERLWEKEQEVAALRRSLEQSEAA-VAQVLEERQKAWE-RELAELRQGCSGKLQQVARRA---QRAQQGLQLQVLRL 396
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKAdEAKKAEEAKKADEaKKAEEAKKADEAKKAEEKKKAdelKKAEELKKAEEKKK 1565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 397 QQDKKQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRaSLREKEEQLLSLRDS 476
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE-EEKKKVEQLKKKEAE 1644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 477 FSSKQASLELGEGELPAACLKPALTPVDPAEPQDALATCESDEAK----MRRQAGVAAAASLVSVDGEAEAGGESGTRAl 552
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKaaeaLKKEAEEAKKAEELKKKEAEEKKKAEELKK- 1723
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 553 RREVGRLQAELAAERRARERQGAsfaEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQL 612
Cdd:PTZ00121 1724 AEEENKIKAEEAKKEAEEDKKKA---EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
314-460 |
4.89e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.40 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 314 PPSPSALIQELEerlwekeQEVAALRRSLEQ--SEAAVAQVLEERQKAWERELAELRQGCSGKLQQVARRAQRAQQGLQL 391
Cdd:PRK11448 137 PEDPENLLHALQ-------QEVLTLKQQLELqaREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAE 209
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917203328 392 QVLRLQQDKKQLQEEAARLMRQREELEDKvcqkageisLLKQQLKDS--QADvSQKLSEIVGLRSQlrEGR 460
Cdd:PRK11448 210 TSQERKQKRKEITDQAAKRLELSEEETRI---------LIDQQLRKAgwEAD-SKTLRFSKGARPE--KGR 268
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
402-616 |
7.45e-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: 42.74 E-value: 7.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 402 QLQEEAA-RLMRQREELEDKvcqkagEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSK 480
Cdd:TIGR02168 206 ERQAEKAeRYKELKAELREL------ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 481 QASLELGEGELPAACLKPALTPVDPAEPQDALATCESDEAKMRRQAGVAAAASLVSVDGEAEAGGESGTraLRREVGRLQ 560
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE--LKEELESLE 357
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917203328 561 AELAAERRARERQGASFAEERRVWLEEKEKVIEYQKQL-----QLSYVEmyQRNQQLERRL 616
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIaslnnEIERLE--ARLERLEDRR 416
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
401-618 |
1.15e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 401 KQLQEEAARLMRQREELEDKVcQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSK 480
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFI-KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 481 QASLELGEGELPAacLKPALtpvdpAEPQDALATCESDEAKMRRQAGvaaaaSLVSVDGEAEAGGE---------SGTRA 551
Cdd:PRK03918 244 EKELESLEGSKRK--LEEKI-----RELEERIEELKKEIEELEEKVK-----ELKELKEKAEEYIKlsefyeeylDELRE 311
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1917203328 552 LRREVGRLQAELAA-ERRARErqgASFAEERRVWLEEKEKVIEYQKQLQLSYVEMYQRNQQLERRLRE 618
Cdd:PRK03918 312 IEKRLSRLEEEINGiEERIKE---LEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELER 376
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
317-474 |
1.73e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 317 PSALIQELEERLWEKEQEVAALRRSLEQ--SEAAVAQVLEERQKAWER----ELAELRQGCSGKLQQVARRAQRA----- 385
Cdd:COG4717 331 PPDLSPEELLELLDRIEELQELLREAEEleEELQLEELEQEIAALLAEagveDEEELRAALEQAEEYQELKEELEeleeq 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 386 --QQGLQLQVLRLQQDKKQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADvsQKLSEivgLRSQLREGRASL 463
Cdd:COG4717 411 leELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED--GELAE---LLQELEELKAEL 485
|
170
....*....|.
gi 1917203328 464 REKEEQLLSLR 474
Cdd:COG4717 486 RELAEEWAALK 496
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
316-478 |
2.04e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 316 SPSALIQELEERLWEKEQEVAALRRSLEQSEAAVAQvLEERQKAWERELAELRQgcsgKLQQVARRAQRAQQGLQLQVLR 395
Cdd:COG4913 682 ASSDDLAALEEQLEELEAELEELEEELDELKGEIGR-LEKELEQAEEELDELQD----RLEAAEDLARLELRALLEERFA 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 396 LQQDKKQLQEEAARLMRQREELEDKVCQKAGEISLL----KQQLKDSQADVSQKLSEIVGLRSQLREGRAS-LREKEEQL 470
Cdd:COG4913 757 AALGDAVERELRENLEERIDALRARLNRAEEELERAmrafNREWPAETADLDADLESLPEYLALLDRLEEDgLPEYEERF 836
|
....*...
gi 1917203328 471 LSLRDSFS 478
Cdd:COG4913 837 KELLNENS 844
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
321-628 |
2.45e-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: 41.09 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 321 IQELEERLWEKEQEVAALRRSLEQSEAAvAQVLEERQKAWERELAELRQGC------SGKLQQVARRAQRAQQGLQLQVL 394
Cdd:COG3096 356 LEELTERLEEQEEVVEEAAEQLAEAEAR-LEAAEEEVDSLKSQLADYQQALdvqqtrAIQYQQAVQALEKARALCGLPDL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 395 rlqqDKKQLQEEAARLMRQREELEDKVCQkageislLKQQLKDSQADVSQ------KLSEIVG----------LRSQLRE 458
Cdd:COG3096 435 ----TPENAEDYLAAFRAKEQQATEEVLE-------LEQKLSVADAARRQfekayeLVCKIAGeversqawqtARELLRR 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 459 GRaSLREKEEQLLSLRDSFS------SKQASLElgegELPAACLKPALTPVDPAEpqdalatcESDEAKMRRQAGVAAAA 532
Cdd:COG3096 504 YR-SQQALAQRLQQLRAQLAeleqrlRQQQNAE----RLLEEFCQRIGQQLDAAE--------ELEELLAELEAQLEELE 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 533 SLVSVDGEAEAGGESGTRALRREVGRLQAE----LAAERRA---RERQGASFAEERRVwLEEKEKVIEYQKQLQLSYVEM 605
Cdd:COG3096 571 EQAAEAVEQRSELRQQLEQLRARIKELAARapawLAAQDALerlREQSGEALADSQEV-TAAMQQLLEREREATVERDEL 649
|
330 340
....*....|....*....|...
gi 1917203328 606 YQRNQQLERRLRERGAAGGASTP 628
Cdd:COG3096 650 AARKQALESQIERLSQPGGAEDP 672
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
318-551 |
2.75e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 318 SALIQELEERLWEKEQEVAALRRSLEQSEAAvaqvLEERQKAWERELAEL-RQGCSGK--------------------LQ 376
Cdd:COG3883 50 NEEYNELQAELEALQAEIDKLQAEIAEAEAE----IEERREELGERARALyRSGGSVSyldvllgsesfsdfldrlsaLS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 377 QVARRAQRAQQGLQLQVLRLQQDKKQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQL 456
Cdd:COG3883 126 KIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 457 REGRASLREKEEQLLSLRDSFSSKQASLELGEGELPAACLKPALTPVDPAEPQDALATCESDEAKMRRQAGVAAAASLVS 536
Cdd:COG3883 206 AAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGG 285
|
250
....*....|....*
gi 1917203328 537 VDGEAEAGGESGTRA 551
Cdd:COG3883 286 AGGAGGGGGGGGAAS 300
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
321-491 |
3.49e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 321 IQELEERLWEKEQEVAALRRSL------EQSEAAVAQV--LEERQKAWERELAELRQgcsgKLQQVarRAQRAQQGLQLQ 392
Cdd:COG3206 184 LPELRKELEEAEAALEEFRQKNglvdlsEEAKLLLQQLseLESQLAEARAELAEAEA----RLAAL--RAQLGSGPDALP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 393 VLRLQQDKKQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQAdvsQKLSEIVGLRSQLREGRASLREKEEQLLS 472
Cdd:COG3206 258 ELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRA---QLQQEAQRILASLEAELEALQAREASLQA 334
|
170
....*....|....*....
gi 1917203328 473 LRDSFSSKQASLELGEGEL 491
Cdd:COG3206 335 QLAQLEARLAELPELEAEL 353
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
317-616 |
4.16e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.26 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 317 PSALIqeLEERLWEKEQEVAALRRSLEQSEAAVAQVLEERQKA---WERELAELRQGCsGKLQQVARRAQRAQQGLQLQV 393
Cdd:pfam07888 27 PRAEL--LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDreqWERQRRELESRV-AELKEELRQSREKHEELEEKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 394 LRLQQDKKQLQEEAARLMRQRE-------ELED-------KVCQKAGEISLLKQQLK--------------DSQADVSQK 445
Cdd:pfam07888 104 KELSASSEELSEEKDALLAQRAahearirELEEdiktltqRVLERETELERMKERAKkagaqrkeeeaerkQLQAKLQQT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 446 LSEIVGLRSQLREGRASLREKEEQLLSLRDSFSSKQasLELGEGELPAACLKPALTPVDPAepQDALATCESDEAKMRRQ 525
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLT--QKLTTAHRKEAENEALLEELRSL--QERLNASERKVEGLGEE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 526 AGVAAA-------------------------ASLVSVDGEAEAGGESGT------------RALRREVGRLQAELAAERR 568
Cdd:pfam07888 260 LSSMAAqrdrtqaelhqarlqaaqltlqladASLALREGRARWAQERETlqqsaeadkdriEKLSAELQRLEERLQEERM 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1917203328 569 ARERQGASFAEER---RVWLEEKEKVIEYQK-----------QLQLSYVEMYQRNQQLERRL 616
Cdd:pfam07888 340 EREKLEVELGREKdcnRVQLSESRRELQELKaslrvaqkekeQLQAEKQELLEYIRQLEQRL 401
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
551-619 |
4.25e-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: 37.95 E-value: 4.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917203328 551 ALRREVGRLQAELAAERRARERQGASFAEERRVWLEEK--EKVIEYQKQLQLSYVEMYQRNQQLERRLRER 619
Cdd:smart00935 29 KRQAELEKLEKELQKLKEKLQKDAATLSEAAREKKEKElqKKVQEFQRKQQKLQQDLQKRQQEELQKILDK 99
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
400-616 |
4.55e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 400 KKQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLK--DSQADVSQKLSEIVGLRSQLREGRASLREKEEQLLSLrdsf 477
Cdd:COG3206 170 REEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL---- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 478 sskQASLELGEGELPAACLKPALtpvdpAEPQDALATCESDEAKMRRQAG------VAAAASLVSVDgeaeaggesgtRA 551
Cdd:COG3206 246 ---RAQLGSGPDALPELLQSPVI-----QQLRAQLAELEAELAELSARYTpnhpdvIALRAQIAALR-----------AQ 306
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1917203328 552 LRREVGRLQAELAAERRARERQGASFAEErrvwLEEKEKVIEYQKQLQLSYVEMyQRNQQLERRL 616
Cdd:COG3206 307 LQQEAQRILASLEAELEALQAREASLQAQ----LAQLEARLAELPELEAELRRL-EREVEVAREL 366
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
403-491 |
6.52e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 38.92 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 403 LQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQA------DVSQKLSEIVGLRSQLREGRASLREK---------- 466
Cdd:pfam15294 138 LKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKeqgakkDVKSNLKEISDLEEKMAALKSDLEKTlnastalqks 217
|
90 100
....*....|....*....|....*.
gi 1917203328 467 -EEQLLSLRDSFSSKQASLELGEGEL 491
Cdd:pfam15294 218 lEEDLASTKHELLKVQEQLEMAEKEL 243
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
310-483 |
8.22e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.51 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 310 AACSPPSPSALIQELEErlwekeqevAALRRSLEQSEAAVAQVLEERQ------KAWERELAELRQgcsgKLQQVARRAQ 383
Cdd:PRK11281 31 SNGDLPTEADVQAQLDA---------LNKQKLLEAEDKLVQQDLEQTLalldkiDRQKEETEQLKQ----QLAQAPAKLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 384 RAQQglqlqvlrlqqDKKQLQEEAARLMRQR------EELEDKVCQkageislLKQQLKDSQADVSQKLSEIVGLRSQLR 457
Cdd:PRK11281 98 QAQA-----------ELEALKDDNDEETRETlstlslRQLESRLAQ-------TLDQLQNAQNDLAEYNSQLVSLQTQPE 159
|
170 180
....*....|....*....|....*.
gi 1917203328 458 EGRASLREKEEQLLSLRDSFSSKQAS 483
Cdd:PRK11281 160 RAQAALYANSQRLQQIRNLLKGGKVG 185
|
|
| KASH_CCD |
pfam14662 |
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ... |
401-491 |
8.65e-03 |
|
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of KASH or Klarsicht/ANC-1/Syne/homology proteins. KASH are a meiosis-specific proteins that localize at telomeres and interact with SUN1, thus being implicated in meiotic chromosome dynamics and homolog pairing.
Pssm-ID: 405365 [Multi-domain] Cd Length: 191 Bit Score: 37.85 E-value: 8.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 401 KQLQEEAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQK------LSEIVGLRSQLREGRASLREKEEQLLSLR 474
Cdd:pfam14662 18 QKLLQENSKLKATVETREETNAKLLEENLNLRKQAKSQQQAVQKEklleeeLEDLKLIVNSLEEARRSLLAQNKQLEKEN 97
|
90
....*....|....*..
gi 1917203328 475 DSFSSKQASLELGEGEL 491
Cdd:pfam14662 98 QSLLQEIESLQEENKKN 114
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
320-619 |
9.33e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 39.34 E-value: 9.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 320 LIQELEERLWEKEQevaalRRSLEQSEAAvAQVLEERQKAWERELAELRQGCSGKLQQVaRRAQRAQQGLQLQVLRLQQD 399
Cdd:pfam17380 301 LRQEKEEKAREVER-----RRKLEEAEKA-RQAEMDRQAAIYAEQERMAMERERELERI-RQEERKRELERIRQEEIAME 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 400 KKQLQEeAARLMRQREELEDKVCQKAGEISLLKQQLKDSQADVSQKLSEIVGLRSQLREGRaslrekEEQLLSLRDSFSS 479
Cdd:pfam17380 374 ISRMRE-LERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEAR------QREVRRLEEERAR 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917203328 480 KQASLELGEgelpaaclkpaltpvdpAEPQDALATCESDEAKMRRQagvaaaaslvSVDGEAEAGGESGTRALRREVgrL 559
Cdd:pfam17380 447 EMERVRLEE-----------------QERQQQVERLRQQEEERKRK----------KLELEKEKRDRKRAEEQRRKI--L 497
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1917203328 560 QAELAAERRA---------------RERQGASFAEERRVWLEE---KEKVIEYQKQLQLSYVEMYQRNQQLERRLRER 619
Cdd:pfam17380 498 EKELEERKQAmieeerkrkllekemEERQKAIYEEERRREAEEerrKQQEMEERRRIQEQMRKATEERSRLEAMERER 575
|
|
| |
