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Conserved domains on  [gi|109715852|ref|NP_001035940|]
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centrosomal protein of 85 kDa-like isoform a [Homo sapiens]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000095)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 443-690 1.15e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.91  E-value: 1.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   443 EFEQKLASTEKEVLQLNEflkQRLSLFSEEKKKLEEKLKTRDRyISSLKKKCQKESEQNKEKQRRIETLEKYL----ADL 518
Cdd:TIGR02168  236 ELREELEELQEELKEAEE---ELEELTAELQELEEKLEELRLE-VSELEEEIEELQKELYALANEISRLEQQKqilrERL 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   519 PTLDDVQSQ-SLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERcLEDGIRL 597
Cdd:TIGR02168  312 ANLERQLEElEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET-LRSKVAQ 390

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   598 PMLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMM-----EELEKKERNVQRLTKAL 672
Cdd:TIGR02168  391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEleelqEELERLEEALEELREEL 470

                          250
                   ....*....|....*...
gi 109715852   673 LENQRQTDETCSLLDQGQ 690
Cdd:TIGR02168  471 EEAEQALDAAERELAQLQ 488
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 443-690 1.15e-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: 58.91  E-value: 1.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   443 EFEQKLASTEKEVLQLNEflkQRLSLFSEEKKKLEEKLKTRDRyISSLKKKCQKESEQNKEKQRRIETLEKYL----ADL 518
Cdd:TIGR02168  236 ELREELEELQEELKEAEE---ELEELTAELQELEEKLEELRLE-VSELEEEIEELQKELYALANEISRLEQQKqilrERL 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   519 PTLDDVQSQ-SLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERcLEDGIRL 597
Cdd:TIGR02168  312 ANLERQLEElEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET-LRSKVAQ 390

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   598 PMLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMM-----EELEKKERNVQRLTKAL 672
Cdd:TIGR02168  391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEleelqEELERLEEALEELREEL 470

                          250
                   ....*....|....*...
gi 109715852   673 LENQRQTDETCSLLDQGQ 690
Cdd:TIGR02168  471 EEAEQALDAAERELAQLQ 488
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 500-698 2.96e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 2.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 500 QNKEKQRRIETLEKYLADLptLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTT 579
Cdd:COG1196  219 KEELKELEAELLLLKLREL--EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 580 VQSLQQKVERCLEDGIRLPmLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELE 659
Cdd:COG1196  297 LARLEQDIARLEERRRELE-ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 109715852 660 KKERNVQRLTKALLENQRQTDETCSLLDQGQEPDQSRQQ 698
Cdd:COG1196  376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
443-663 3.16e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 54.30  E-value: 3.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 443 EFEQKLASTEKEVLQLNEfLKQRLSlfseekkKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTLD 522
Cdd:PRK03918 218 ELREELEKLEKEVKELEE-LKEEIE-------ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 523 DVQSQSLQL-----QILEEKNkNLQEALIDTEKKLEEIKKQCQDKETqlicQKKKEKELVTTVQSLQQKVERcLEDGIRL 597
Cdd:PRK03918 290 EKAEEYIKLsefyeEYLDELR-EIEKRLSRLEEEINGIEERIKELEE----KEERLEELKKKLKELEKRLEE-LEERHEL 363

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109715852 598 pMLDAKQLQNENDNLRQQ--NETASKI------IDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKER 663
Cdd:PRK03918 364 -YEEAKAKKEELERLKKRltGLTPEKLekeleeLEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKG 436
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 439-801 2.35e-05

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 48.04  E-value: 2.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   439 SQQGEFEQKLASTEKEVLQLNEFLKqRLSLFSEEKKKLEEKLKTRDRYIS------SLKKKCQKESEQNKEKQR---RIE 509
Cdd:pfam02463  139 VQGGKIEIIAMMKPERRLEIEEEAA-GSRLKRKKKEALKKLIEETENLAEliidleELKLQELKLKEQAKKALEyyqLKE 217

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   510 TLEKYLADLPTLDDVQSQSLQLQILEEKNKNLQEaLIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVER 589
Cdd:pfam02463  218 KLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE-EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEE 296

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   590 CLEDGIRLPMLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLT 669
Cdd:pfam02463  297 ELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELL 376

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   670 KALLENQRQTDETCSLLDQGQEPDQSRQQTVLSKRPLFDLTVIDQLFKEMSCCLFDLKALCSILNQRAQGKE--PNLSLL 747
Cdd:pfam02463  377 AKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEekEELEKQ 456

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 109715852   748 LGIRSMNCSAEETEND--HSTETLTKKLSDVCQLRRDIDELRTTiSDRYAQDMGDN 801
Cdd:pfam02463  457 ELKLLKDELELKKSEDllKETQLVKLQEQLELLLSRQKLEERSQ-KESKARSGLKV 511
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 601-688 2.94e-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: 38.72  E-value: 2.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   601 DAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTT-----QKMMEELEKKERNVQRLTKALLE- 674
Cdd:smart00935   5 DVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLseaarEKKEKELQKKVQEFQRKQQKLQQd 84

                           90
                   ....*....|....*
gi 109715852   675 -NQRQTDETCSLLDQ 688
Cdd:smart00935  85 lQKRQQEELQKILDK 99
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 443-690 1.15e-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: 58.91  E-value: 1.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   443 EFEQKLASTEKEVLQLNEflkQRLSLFSEEKKKLEEKLKTRDRyISSLKKKCQKESEQNKEKQRRIETLEKYL----ADL 518
Cdd:TIGR02168  236 ELREELEELQEELKEAEE---ELEELTAELQELEEKLEELRLE-VSELEEEIEELQKELYALANEISRLEQQKqilrERL 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   519 PTLDDVQSQ-SLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERcLEDGIRL 597
Cdd:TIGR02168  312 ANLERQLEElEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET-LRSKVAQ 390

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   598 PMLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMM-----EELEKKERNVQRLTKAL 672
Cdd:TIGR02168  391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEleelqEELERLEEALEELREEL 470

                          250
                   ....*....|....*...
gi 109715852   673 LENQRQTDETCSLLDQGQ 690
Cdd:TIGR02168  471 EEAEQALDAAERELAQLQ 488
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 500-698 2.96e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 2.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 500 QNKEKQRRIETLEKYLADLptLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTT 579
Cdd:COG1196  219 KEELKELEAELLLLKLREL--EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 580 VQSLQQKVERCLEDGIRLPmLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELE 659
Cdd:COG1196  297 LARLEQDIARLEERRRELE-ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 109715852 660 KKERNVQRLTKALLENQRQTDETCSLLDQGQEPDQSRQQ 698
Cdd:COG1196  376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
443-663 3.16e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 54.30  E-value: 3.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 443 EFEQKLASTEKEVLQLNEfLKQRLSlfseekkKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTLD 522
Cdd:PRK03918 218 ELREELEKLEKEVKELEE-LKEEIE-------ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 523 DVQSQSLQL-----QILEEKNkNLQEALIDTEKKLEEIKKQCQDKETqlicQKKKEKELVTTVQSLQQKVERcLEDGIRL 597
Cdd:PRK03918 290 EKAEEYIKLsefyeEYLDELR-EIEKRLSRLEEEINGIEERIKELEE----KEERLEELKKKLKELEKRLEE-LEERHEL 363

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109715852 598 pMLDAKQLQNENDNLRQQ--NETASKI------IDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKER 663
Cdd:PRK03918 364 -YEEAKAKKEELERLKKRltGLTPEKLekeleeLEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKG 436
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 440-706 3.29e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 3.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 440 QQGEFEQKLASTEKEVLQLN---EFLKQRLSLFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLA 516
Cdd:COG1196  247 ELEELEAELEELEAELAELEaelEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 517 DLptLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEikkqcqdketqlicQKKKEKELVTTVQSLQQKVERCLEDGIR 596
Cdd:COG1196  327 EL--EEELEELEEELEELEEELEEAEEELEEAEAELAE--------------AEEALLEAEAELAEAEEELEELAEELLE 390

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 597 LpMLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLTKALLENQ 676
Cdd:COG1196  391 A-LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469

                        250       260       270
                 ....*....|....*....|....*....|
gi 109715852 677 RQTDETCSLLDQGQEPDQSRQQTVLSKRPL 706
Cdd:COG1196  470 EEAALLEAALAELLEELAEAAARLLLLLEA 499
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 443-674 4.25e-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: 50.44  E-value: 4.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   443 EFEQKLASTEKEV---LQLNEFLKQRLSLFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADLp 519
Cdd:TIGR02168  688 ELEEKIAELEKALaelRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL- 766

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   520 tLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERCLEdgirlpm 599
Cdd:TIGR02168  767 -EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER------- 838

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   600 lDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQ-------SMQGKLSKEKLTTQKMMEELEKKERNVQRLTKAL 672
Cdd:TIGR02168  839 -RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEallneraSLEEALALLRSELEELSEELRELESKRSELRREL 917


                   ..
gi 109715852   673 LE 674
Cdd:TIGR02168  918 EE 919
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 487-681 4.61e-06

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 50.40  E-value: 4.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852  487 ISSLKKKCQKESEQNKEKQRRIETLEKYLADLptldDVQSQSLQLQILEEKN--KNLQEALIDTEKKLEEIKKQCQDKET 564
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQIKKLQQEKELL----EKEIERLKETIIKNNSeiKDLTNQDSVKELIIKNLDNTRESLET 468

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852  565 QLicqKKKEKELVTTVQSLQQKVERCLEDGIRLPMLDA--KQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQG 642
Cdd:TIGR04523 469 QL---KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEekKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLED 545

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 109715852  643 KLSKEK--LTTQKMMEELEKKERNVQRL---TKALLENQRQTDE 681
Cdd:TIGR04523 546 ELNKDDfeLKKENLEKEIDEKNKEIEELkqtQKSLKKKQEEKQE 589
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 500-698 4.73e-06

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.83  E-value: 4.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 500 QNKEKQRRIETLEKYLADLptLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLicqKKKEKELVTT 579
Cdd:COG3883   17 QIQAKQKELSELQAELEAA--QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI---EERREELGER 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 580 VQSLQQkvercleDGIRLPMLDAKQLQNENDNLRQQNETASKIIDSQQDEIDrmilEIQSMQGKLSKEKLTTQKMMEELE 659
Cdd:COG3883   92 ARALYR-------SGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLE----ELKADKAELEAKKAELEAKLAELE 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 109715852 660 KKERNVQRLTKALlenQRQTDETCSLLDQGQEPDQSRQQ 698
Cdd:COG3883  161 ALKAELEAAKAEL---EAQQAEQEALLAQLSAEEAAAEA 196
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 542-704 5.84e-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: 5.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 542 QEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERcLEDGIRLPMLDAKQLQNENDNLRQQNETASK 621
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA-LARRIRALEQELAALEAELAELEKEIAELRA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 622 IIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLTKA---LLENQRQTDETCSLLDQGQEPDQSRQQ 698
Cdd:COG4942   98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPArreQAEELRADLAELAALRAELEAERAELE 177


                 ....*.
gi 109715852 699 TVLSKR 704
Cdd:COG4942  178 ALLAEL 183
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 439-801 2.35e-05

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 48.04  E-value: 2.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   439 SQQGEFEQKLASTEKEVLQLNEFLKqRLSLFSEEKKKLEEKLKTRDRYIS------SLKKKCQKESEQNKEKQR---RIE 509
Cdd:pfam02463  139 VQGGKIEIIAMMKPERRLEIEEEAA-GSRLKRKKKEALKKLIEETENLAEliidleELKLQELKLKEQAKKALEyyqLKE 217

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   510 TLEKYLADLPTLDDVQSQSLQLQILEEKNKNLQEaLIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVER 589
Cdd:pfam02463  218 KLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE-EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEE 296

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   590 CLEDGIRLPMLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLT 669
Cdd:pfam02463  297 ELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELL 376

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   670 KALLENQRQTDETCSLLDQGQEPDQSRQQTVLSKRPLFDLTVIDQLFKEMSCCLFDLKALCSILNQRAQGKE--PNLSLL 747
Cdd:pfam02463  377 AKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEekEELEKQ 456

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 109715852   748 LGIRSMNCSAEETEND--HSTETLTKKLSDVCQLRRDIDELRTTiSDRYAQDMGDN 801
Cdd:pfam02463  457 ELKLLKDELELKKSEDllKETQLVKLQEQLELLLSRQKLEERSQ-KESKARSGLKV 511
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 487-682 2.99e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 47.71  E-value: 2.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852  487 ISSLKKKCQKESEQNKEKQRRIETLEKYLADlptlddvqsqslqlqiLEEKNKNLQEALIDTEKKLEEIKKQCQDKETQL 566
Cdd:TIGR04523 126 LNKLEKQKKENKKNIDKFLTEIKKKEKELEK----------------LNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852  567 ICQKKKEKELVTTVQSLQQKVERcledgirlpmldAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSK 646
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKIQK------------NKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ 257

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 109715852  647 EKLTTQKMMEELEKKERNVQRLTKAL--LENQRQTDET 682
Cdd:TIGR04523 258 LKDEQNKIKKQLSEKQKELEQNNKKIkeLEKQLNQLKS 295
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 355-665 4.21e-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: 47.37  E-value: 4.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   355 QDFSKWESMLKIKEGLLRQKEIVIDRQKQQITHLHERIRDNELRAqHAMLGHYVNCEDSYVASLQPQYENtslQTPFSEE 434
Cdd:TIGR02169  730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL-HKLEEALNDLEARLSHSRIPEIQA---ELSKLEE 805

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   435 SVShsqqgEFEQKLASTEKE---VLQLNEFLKQRLSLFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETL 511
Cdd:TIGR02169  806 EVS-----RIEARLREIEQKlnrLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL 880

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   512 EKYLADlptlddvqsqslqlqiLEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERCL 591
Cdd:TIGR02169  881 ESRLGD----------------LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109715852   592 EDGIRLPMLD--AKQLQNENDNLRQQNETASKIIDSQQDEIDRMiLEIQSMQGKLSKEKLTTQKMMEELEKKERNV 665
Cdd:TIGR02169  945 EIPEEELSLEdvQAELQRVEEEIRALEPVNMLAIQEYEEVLKRL-DELKEKRAKLEEERKAILERIEEYEKKKREV 1019
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 487-698 4.67e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 46.94  E-value: 4.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852  487 ISSLKKKCQKeseqNKEKQRRIETLEKYLADLPtlDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQL 566
Cdd:TIGR04523 203 LSNLKKKIQK----NKSLESQISELKKQNNQLK--DNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852  567 ICQKKKEKELVTTVQSLQQKVERcledgirlpmLDAKQLQNENDNLR---QQNETASKIIDSQQDEIDRMILEIQSMQGK 643
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISD----------LNNQKEQDWNKELKselKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 109715852  644 LSKEK----LTTQKMMEELEKKERNVQRLTKallENQRQTDETCSLLDQGQEPDQSRQQ 698
Cdd:TIGR04523 347 LKKELtnseSENSEKQRELEEKQNEIEKLKK---ENQSYKQEIKNLESQINDLESKIQN 402
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 516-704 6.67e-05

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 45.30  E-value: 6.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 516 ADLPTLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERcledgi 595
Cdd:COG1579    4 EDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK------ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 596 rlpmldakqlqnenDNLRQQNETASKIIDSQQDEIDRMILEIQsmqgKLSKEKLttqKMMEELEKKERNVQRLTKALLEN 675
Cdd:COG1579   78 --------------YEEQLGNVRNNKEYEALQKEIESLKRRIS----DLEDEIL---ELMERIEELEEELAELEAELAEL 136

                        170       180
                 ....*....|....*....|....*....
gi 109715852 676 QRQTDETCSLLDQGQEPDQSRQQTVLSKR 704
Cdd:COG1579  137 EAELEEKKAELDEELAELEAELEELEAER 165
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 364-672 1.59e-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: 45.43  E-value: 1.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   364 LKIKEGLLRQKEIVIDRQKQQITHLHERIRD------------NELRAQHAMLGHYVNCEDSYVASLQpqYENTSLQtpf 431
Cdd:TIGR02168  686 IEELEEKIAELEKALAELRKELEELEEELEQlrkeleelsrqiSALRKDLARLEAEVEQLEERIAQLS--KELTELE--- 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   432 SEESVSHSQQGEFEQKLASTEKEVLQLNEFLKQ---RLSLFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRI 508
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   509 ETLEKYLADLptlddvqsqSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVe 588
Cdd:TIGR02168  841 EDLEEQIEEL---------SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR- 910

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   589 rcledgirlpmldaKQLQNENDNLRQQNETAskiidsqQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKK------- 661
Cdd:TIGR02168  911 --------------SELRRELEELREKLAQL-------ELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKieddeee 969

                          330
                   ....*....|..
gi 109715852   662 -ERNVQRLTKAL 672
Cdd:TIGR02168  970 aRRRLKRLENKI 981
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
485-678 1.99e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 1.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 485 RYISSLKKKCQKESEQNKEKQRRIETLEKyladlpTLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKEt 564
Cdd:PRK03918 207 REINEISSELPELREELEKLEKEVKELEE------LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE- 279

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 565 qlicqkKKEKELvttvQSLQQKVERCLEDGirlpmldaKQLQNENDNLRQQNETASKIiDSQQDEIDRMILEIQSMQ--- 641
Cdd:PRK03918 280 ------EKVKEL----KELKEKAEEYIKLS--------EFYEEYLDELREIEKRLSRL-EEEINGIEERIKELEEKEerl 340

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 109715852 642 GKLSKEKLTTQKMMEELEKKERNVQRLtKALLENQRQ 678
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELYEEA-KAKKEELER 376
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
443-674 2.07e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 2.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 443 EFEQKLASTEKEVLQLNEFLKqRLSLFSEEKKKLEEKLKTRDRYISSLKKKCQKES-EQNKEKQRRIETLEKYLADLPTL 521
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLEL 607

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 522 DDVQSqslQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLicqkkKEKELVTTVQSLQQKVERCLEDGIRLPMLD 601
Cdd:PRK03918 608 KDAEK---ELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL-----EELEKKYSEEEYEELREEYLELSRELAGLR 679

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109715852 602 AKQLQNEndNLRQQNETASKIIDSQQDEIDRMILEIqsmqgklskEKLttQKMMEELEKKERNVQRLtKALLE 674
Cdd:PRK03918 680 AELEELE--KRREEIKKTLEKLKEELEEREKAKKEL---------EKL--EKALERVEELREKVKKY-KALLK 738
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
484-650 2.82e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 2.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 484 DRYISSLKKKCQKESEQnKEKQRRIETLEKYLADLPTLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKE 563
Cdd:COG4717   88 EEYAELQEELEELEEEL-EELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 564 TQLICQKKKEKELVTTVQSLQQKVERCLEDGIRlpmlDAKQLQNENDNLRQQNETASKIIDSQQDEIDRM--ILEIQSMQ 641
Cdd:COG4717  167 ELEAELAELQEELEELLEQLSLATEEELQDLAE----ELEELQQRLAELEEELEEAQEELEELEEELEQLenELEAAALE 242


                 ....*....
gi 109715852 642 GKLSKEKLT 650
Cdd:COG4717  243 ERLKEARLL 251
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 470-696 3.34e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.60  E-value: 3.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 470 SEEKKKLeeklktrdryisslKKKCQKESEQNKEKQRRIETLEKYLADLptLDDVQSQSLQLQILEEKNKNLQEALIDTE 549
Cdd:COG4942   19 ADAAAEA--------------EAELEQLQQEIAELEKELAALKKEEKAL--LKQLAALERRIAALARRIRALEQELAALE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 550 KKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQ--------KVERCLEDGIRLPMLDA--KQLQNENDNLRQQNETA 619
Cdd:COG4942   83 AELAELEKEIAELRAELEAQKEELAELLRALYRLGRqpplalllSPEDFLDAVRRLQYLKYlaPARREQAEELRADLAEL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 620 SKI---IDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLTKALLENQRQTDETCSLLDQGQEPDQSR 696
Cdd:COG4942  163 AALraeLEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 488-696 4.01e-04

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 43.96  E-value: 4.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852  488 SSLKKKCQKESEQNKEKQRRIETLEKYLADlptlddvQSQSLQLQIleEKNKNLQEALIDTEKKLEEIKKQCQDKETQLI 567
Cdd:pfam05557  37 SALKRQLDRESDRNQELQKRIRLLEKREAE-------AEEALREQA--ELNRLKKKYLEALNKKLNEKESQLADAREVIS 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852  568 CQKKKEKELVT-------TVQSLQQKVERCLEdgiRLPMLDAKqLQNENDnLRQQNETASKIIDSQQDEIDRMILEIQSM 640
Cdd:pfam05557 108 CLKNELSELRRqiqraelELQSTNSELEELQE---RLDLLKAK-ASEAEQ-LRQNLEKQQSSLAEAEQRIKELEFEIQSQ 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 109715852  641 qgklSKEKLTTQKMMEELE---KKERNVQRLtKALLENQRQTDETCSLLDQGQEPDQSR 696
Cdd:pfam05557 183 ----EQDSEIVKNSKSELAripELEKELERL-REHNKHLNENIENKLLLKEEVEDLKRK 236
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 364-680 4.63e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 4.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 364 LKIKEGLLRQKEIviDRQKQQITHLHERIRDNELRAQHAMLGhyvncedsyVASLQPQYENTSLQtpFSEESVSHSQQGE 443
Cdd:COG1196  222 LKELEAELLLLKL--RELEAELEELEAELEELEAELEELEAE---------LAELEAELEELRLE--LEELELELEEAQA 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 444 FEQKLASTEKEVLQLNEFLKQRLSLFSEEKKKLEEKlktrdryISSLKKKCQKESEQNKEKQRRIETLEKYLADLptldd 523
Cdd:COG1196  289 EEYELLAELARLEQDIARLEERRRELEERLEELEEE-------LAELEEELEELEEELEELEEELEEAEEELEEA----- 356

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 524 vqsqSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERCLEDGIRLpmldAK 603
Cdd:COG1196  357 ----EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL----EE 428

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109715852 604 QLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLtKALLENQRQTD 680
Cdd:COG1196  429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL-LLLLEAEADYE 504
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 487-589 9.12e-04

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: 41.83  E-value: 9.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 487 ISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQL 566
Cdd:COG1579   54 LEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAEL 133

                         90       100
                 ....*....|....*....|...
gi 109715852 567 icqKKKEKELVTTVQSLQQKVER 589
Cdd:COG1579  134 ---AELEAELEEKKAELDEELAE 153
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 500-648 1.34e-03

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 40.66  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852  500 QNKEKQRRIETLEKYLADLPTLddVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLicqKKKEK----- 574
Cdd:pfam15619  40 LQKRQEKALGKYEGTESELPQL--IARHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRDQL---KRLEKlsedk 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852  575 ------ELVTTVQSLQQKVERCLEDGIRLpmldAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLsKEK 648
Cdd:pfam15619 115 nlaereELQKKLEQLEAKLEDKDEKIQDL----ERKLELENKSFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKL-KEK 189
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 288-683 1.46e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 42.02  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852  288 VPIQPSVRTQMWLTEQLRTNplegrnTEDSYSLAPWQQQQIEDFRQGSETPMQVLTgssrqsyspgyqdfsKWESMLKIK 367
Cdd:pfam05483 303 MSLQRSMSTQKALEEDLQIA------TKTICQLTEEKEAQMEELNKAKAAHSFVVT---------------EFEATTCSL 361

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852  368 EGLLRQKEIVIDRQKQQIthlheRIRDNELRAQHAMLGHYVNCEDSYVASLQpqyentSLQTPFSEESVSHSQQGEFE-- 445
Cdd:pfam05483 362 EELLRTEQQRLEKNEDQL-----KIITMELQKKSSELEEMTKFKNNKEVELE------ELKKILAEDEKLLDEKKQFEki 430

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852  446 -QKLASTEKEVLQLNEFLKQRLSLFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKE------------KQRRIETLE 512
Cdd:pfam05483 431 aEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIEltahcdklllenKELTQEASD 510

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852  513 KYLADLPTLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERCLe 592
Cdd:pfam05483 511 MTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQM- 589

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852  593 dgirlpmldaKQLQNENDNLRQQNETASKIIDSQQDE---------------------IDRMILEIQSMQGKLSK----- 646
Cdd:pfam05483 590 ----------KILENKCNNLKKQIENKNKNIEELHQEnkalkkkgsaenkqlnayeikVNKLELELASAKQKFEEiidny 659

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 109715852  647 ------EKLTTQKMMEELEKKERNVQRLTKAllenQRQTDETC 683
Cdd:pfam05483 660 qkeiedKKISEEKLLEEVEKAKAIADEAVKL----QKEIDKRC 698
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 482-670 1.64e-03

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 40.43  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852  482 TRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTLDDVQSQSLQLQI---LEEKNKNLQEaLIDTEKKLEEIKKQ 558
Cdd:pfam05010  19 EKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIqkvLEEKDQALAD-LNSVEKSFSDLFKR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852  559 CQDKETQLICQKKKEKELVTTVQSLQQKVERcleDGIRLPMLDAKQLQNendnLRQQNETASKIIDSQQDEIdrmileiQ 638
Cdd:pfam05010  98 YEKQKEVISGYKKNEESLKKCAQDYLARIKK---EEQRYQALKAHAEEK----LDQANEEIAQVRSKAKAET-------A 163

                         170       180       190
                  ....*....|....*....|....*....|..
gi 109715852  639 SMQGKLSKEKLTTQKMMEELEKKERNVQRLTK 670
Cdd:pfam05010 164 ALQASLRKEQMKVQSLERQLEQKTKENEELTK 195
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 444-691 1.68e-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: 41.87  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 444 FEQKLASTEKEVLQLNEFLKQRLSLFSEEKKKLEEKLKTRDRYISSLKKKCQ-KESEQNKEKQRRIETLEKYLADLPTlD 522
Cdd:COG5185  266 RLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQlAAAEAEQELEESKRETETGIQNLTA-E 344

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 523 DVQSQSLQLQILEEKNKNLQEalIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERCLEDGIRLPMLDA 602
Cdd:COG5185  345 IEQGQESLTENLEAIKEEIEN--IVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQI 422

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 603 KQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQS-----MQGKLSKEKLTTQKMMEELEKK----ERNVQRLTKALL 673
Cdd:COG5185  423 EELQRQIEQATSSNEEVSKLLNELISELNKVMREADEesqsrLEEAYDEINRSVRSKKEDLNEEltqiESRVSTLKATLE 502

                        250       260
                 ....*....|....*....|..
gi 109715852 674 EN----QRQTDETCSLLDQGQE 691
Cdd:COG5185  503 KLraklERQLEGVRSKLDQVAE 524
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 483-641 1.99e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 41.55  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852  483 RDRYISSLKK---KCQKESEQNKEKQRRIETLEKYLADLPTLD--------DVQSQSLQLQILEEKNKNLQEALIdteKK 551
Cdd:pfam05667 358 IKKLESSIKQveeELEELKEQNEELEKQYKVKKKTLDLLPDAEeniaklqaLVDASAQRLVELAGQWEKHRVPLI---EE 434

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852  552 LEEIKKQCQDKETQliCQKKKEKelvttVQSLQQKVERCLEDgIRLPMLDAKQLQNENDNLRQQ---NETASKI------ 622
Cdd:pfam05667 435 YRALKEAKSNKEDE--SQRKLEE-----IKELREKIKEVAEE-AKQKEELYKQLVAEYERLPKDvsrSAYTRRIleivkn 506

                         170
                  ....*....|....*....
gi 109715852  623 IDSQQDEIDRMILEIQSMQ 641
Cdd:pfam05667 507 IKKQKEEITKILSDTKSLQ 525
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 361-658 2.31e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.54  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852  361 ESMLKIKEGLLRQKEIVIDRQKQQITHLHERIRDneLRAQHAMLGHYVNCEDSYVASLQPQYENTSLQTPfSEESVSHSQ 440
Cdd:TIGR04523 411 DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD--LTNQDSVKELIIKNLDNTRESLETQLKVLSRSIN-KIKQNLEQK 487

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852  441 QGEFEQKlastEKEVLQLNEFLKQrlslfseekkkLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKylaDLPT 520
Cdd:TIGR04523 488 QKELKSK----EKELKKLNEEKKE-----------LEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLED---ELNK 549

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852  521 LDDVQSQSLQLQILEEKNKNL------QEALIDTEKKLEEIKKQCQDKETQLIcqkKKEKELVTTVQSLQQKVERCLEDG 594
Cdd:TIGR04523 550 DDFELKKENLEKEIDEKNKEIeelkqtQKSLKKKQEEKQELIDQKEKEKKDLI---KEIEEKEKKISSLEKELEKAKKEN 626

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109715852  595 IRLpMLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEEL 658
Cdd:TIGR04523 627 EKL-SSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKEL 689
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 529-681 2.79e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.35  E-value: 2.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 529 LQLQILEEKNKNLQEaliDTEKkLEEIKKQCQDKETQlicQKKKEKELvttvQSLQQKVERCLEDGIRLpmldAKQLQNE 608
Cdd:PRK00409 499 LPENIIEEAKKLIGE---DKEK-LNELIASLEELERE---LEQKAEEA----EALLKEAEKLKEELEEK----KEKLQEE 563

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109715852 609 NDNLRQ-QNETASKIIDSQQDEIDRMILEIQSMQgKLSKEKLTTQKMMEELEKKERNVQRLTKALLENQRQTDE 681
Cdd:PRK00409 564 EDKLLEeAEKEAQQAIKEAKKEADEIIKELRQLQ-KGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 601-688 2.94e-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: 38.72  E-value: 2.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   601 DAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTT-----QKMMEELEKKERNVQRLTKALLE- 674
Cdd:smart00935   5 DVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLseaarEKKEKELQKKVQEFQRKQQKLQQd 84

                           90
                   ....*....|....*
gi 109715852   675 -NQRQTDETCSLLDQ 688
Cdd:smart00935  85 lQKRQQEELQKILDK 99
PRK11281 PRK11281
mechanosensitive channel MscK;
516-704 3.04e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 41.05  E-value: 3.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852  516 ADLPTLDDVQSQSLQLQ---ILEEKNKNLQEALIDT----------EKKLEEIKKQCQDKETQLicqKKKEKELVTTVQS 582
Cdd:PRK11281   33 GDLPTEADVQAQLDALNkqkLLEAEDKLVQQDLEQTlalldkidrqKEETEQLKQQLAQAPAKL---RQAQAELEALKDD 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852  583 LQQKVERCLEDgIRLPMLDAK------QLQNENDNLrqqNETASKIIDSQ------QDEIDRMILEIQSMQ-----GKLS 645
Cdd:PRK11281  110 NDEETRETLST-LSLRQLESRlaqtldQLQNAQNDL---AEYNSQLVSLQtqperaQAALYANSQRLQQIRnllkgGKVG 185

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109715852  646 KEKLT-TQKMMEELEKKERNVQ-RLTKALLEN--------QRQTDETCSLLDQGQEPDQSRQQTVLSKR 704
Cdd:PRK11281  186 GKALRpSQRVLLQAEQALLNAQnDLQRKSLEGntqlqdllQKQRDYLTARIQRLEHQLQLLQEAINSKR 254
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 496-681 3.13e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 3.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   496 KESEQNKEKQRRIETLEKYLADLptLDDVQSQslqlqilEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKE 575
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSL--QSELRRI-------ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   576 LVTTVQSLQQK---VERCLEDGI-RLPMLDAK--QLQNENDNL-----RQQNETASKIIDSQQDEIDRMILEIQSMQGKL 644
Cdd:TIGR02169  742 LEEDLSSLEQEienVKSELKELEaRIEELEEDlhKLEEALNDLearlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKL 821

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 109715852   645 SKEKLTTQKMMEELEKKERNVQRLTKALLENQRQTDE 681
Cdd:TIGR02169  822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN 858
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 439-681 3.21e-03

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: 40.52  E-value: 3.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 439 SQQGEFEQKLASTEKEVLQLNEFLKQRlslfSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKyladl 518
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAAL----KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK----- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 519 ptlddvqsqslQLQILEEKNKNLQEALidtEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERCLEDGIRLp 598
Cdd:COG4942   91 -----------EIAELRAELEAQKEEL---AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 599 MLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEI---QSMQGKLSKEKLTTQKMMEELEKKERNVQRLTKALLEN 675
Cdd:COG4942  156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKaerQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235


                 ....*.
gi 109715852 676 QRQTDE 681
Cdd:COG4942  236 AAAAAE 241
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 496-735 3.66e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.11  E-value: 3.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   496 KESEQNKEKQRRIETLEKYLADLPTLDDVQSQSLQLQILEeknknlqealiDTEKKLEEIKKQCQDKETQLICQKKKEKE 575
Cdd:TIGR00618  186 FAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLE-----------KELKHLREALQQTQQSHAYLTQKREAQEE 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   576 LVTTVQSLQQKVERCLEDGIRLPMLdakQLQNENDNLRQQNE---TASKIIDSQQDEIDRMILEIQSMQGKLSKE---KL 649
Cdd:TIGR00618  255 QLKKQQLLKQLRARIEELRAQEAVL---EETQERINRARKAAplaAHIKAVTQIEQQAQRIHTELQSKMRSRAKLlmkRA 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   650 TTQKMMEELEKKERNVQRLTKALLENQRQTDETCSLLdqgqepDQSRQQTVLSKRplfdltvIDQLFKEMSCCLFDLKAL 729
Cdd:TIGR00618  332 AHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIR------EISCQQHTLTQH-------IHTLQQQKTTLTQKLQSL 398


                   ....*.
gi 109715852   730 CSILNQ 735
Cdd:TIGR00618  399 CKELDI 404
PRK12705 PRK12705
hypothetical protein; Provisional
 532-686 4.36e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 40.46  E-value: 4.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 532 QILEEKNKNLQEALIDTEKKLEEIkkQCQDKETQLICQKKKEKELVTTVQSLQQKVERCLEdgiRLPMLDAKQlqNENDN 611
Cdd:PRK12705  30 RLAKEAERILQEAQKEAEEKLEAA--LLEAKELLLRERNQQRQEARREREELQREEERLVQ---KEEQLDARA--EKLDN 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 612 LRQQNETASKIIDSQQDEID------RMILE--------------IQSMQGKLSKEKLTTQKMMEE---LEKKERNVQRL 668
Cdd:PRK12705 103 LENQLEEREKALSARELELEelekqlDNELYrvagltpeqarkllLKLLDAELEEEKAQRVKKIEEeadLEAERKAQNIL 182

                        170
                 ....*....|....*...
gi 109715852 669 TKALlenQRQTDETCSLL 686
Cdd:PRK12705 183 AQAM---QRIASETASDL 197
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 621-688 5.30e-03

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 38.66  E-value: 5.30e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109715852 621 KIIDSQQDEIDRMILEIQSMQGKLSKEKLTT-----QKMMEELEKKERNVQRLTKALLE--NQRQTDETCSLLDQ 688
Cdd:COG2825   50 KEFKKRQAELQKLEKELQALQEKLQKEAATLseeerQKKERELQKKQQELQRKQQEAQQdlQKRQQELLQPILEK 124
Spc42p pfam11544
Spindle pole body component Spc42p; Spc42p is a 42-kD component of the S.cerevisiae spindle ...
 612-671 5.70e-03

Spindle pole body component Spc42p; Spc42p is a 42-kD component of the S.cerevisiae spindle body that localizes to the electron dense central region of the SPB.Spc42p is a phosphoprotein which forms a polymeric layer at the periphery of the SPB central plaque. This functions during SPB duplication and also facilitates the attachment of the SPB to the nuclear membrane.


Pssm-ID: 402925  Cd Length: 72  Bit Score: 36.27  E-value: 5.70e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852  612 LRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLTKA 671
Cdd:pfam11544   3 LIKQNKELQNKLDEKQEEIDRLNVLVGSLRAKLIKYTELNKKLEDELQQSERSSSSGNSR 62
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 483-662 5.81e-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: 40.44  E-value: 5.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   483 RDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTLddvqsqslqlqiLEEKNKNLQEAlidtEKKLEEIKKQCQDK 562
Cdd:TIGR02169  221 REYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEE------------ISELEKRLEEI----EQLLEELNKKIKDL 284

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852   563 ETQLICQKKKEkelvttVQSLQQKVERClEDGIRLPMLDAKQLQNEndnlRQQNETaskiidsqqdEIDRMILEIQSMQG 642
Cdd:TIGR02169  285 GEEEQLRVKEK------IGELEAEIASL-ERSIAEKERELEDAEER----LAKLEA----------EIDKLLAEIEELER 343

                          170       180
                   ....*....|....*....|
gi 109715852   643 KLSKEKLTTQKMMEELEKKE 662
Cdd:TIGR02169  344 EIEEERKRRDKLTEEYAELK 363
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
487-681 6.31e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 6.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 487 ISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTLDDVQSQSLQLQILEEKNK---------------NLQEALIDTEKK 551
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKkynleelekkaeeyeKLKEKLIKLKGE 540

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 552 LEEIKKQCQDKETQlicqKKKEKELVTTVQSLQQKVERCLEDGIRLPMLDAKQLQNENDNLRQQNETASKIIDSQQdeid 631
Cdd:PRK03918 541 IKSLKKELEKLEEL----KKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEK---- 612

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 109715852 632 rmilEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLTKALLENQRQTDE 681
Cdd:PRK03918 613 ----ELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE 658
PRK12704 PRK12704
phosphodiesterase; Provisional
 489-662 6.34e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 6.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 489 SLKKKcqKESEQNKEKQRRIETLEKyladlptldDVQSQSLQLQILEEKNKNLQEALidtEKKLEEIKKqcqdKETQLic 568
Cdd:PRK12704  53 AIKKE--ALLEAKEEIHKLRNEFEK---------ELRERRNELQKLEKRLLQKEENL---DRKLELLEK----REEEL-- 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 569 qKKKEKELVTTVQSLQQKVERCledgirlpmldaKQLQNEndnlrqQNETASKIIDSQQDEIDRMILEiqSMQGKLSKEK 648
Cdd:PRK12704 113 -EKKEKELEQKQQELEKKEEEL------------EELIEE------QLQELERISGLTAEEAKEILLE--KVEEEARHEA 171

                        170
                 ....*....|....
gi 109715852 649 LTTQKMMEELEKKE 662
Cdd:PRK12704 172 AVLIKEIEEEAKEE 185
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
485-663 6.47e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.51  E-value: 6.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 485 RYISSLKKKCQKESEQNKEKQRRIETLEKYLadlptlddvQSQSLQLQ---ILEEKNKNLqEALIDTEKKLEEIKKQCQD 561
Cdd:COG1340   95 DELRKELAELNKAGGSIDKLRKEIERLEWRQ---------QTEVLSPEeekELVEKIKEL-EKELEKAKKALEKNEKLKE 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 562 KETQLICQKKKEKELVTTVQSLQQKVERCLEDgirlpMLDAKQ----LQNENDNLRQQNETASKIIDSQQDEIDRMILEI 637
Cdd:COG1340  165 LRAELKELRKEAEEIHKKIKELAEEAQELHEE-----MIELYKeadeLRKEADELHKEIVEAQEKADELHEEIIELQKEL 239

                        170       180
                 ....*....|....*....|....*...
gi 109715852 638 QSMQGKLS--KEKLTTQKMMEELEKKER 663
Cdd:COG1340  240 RELRKELKklRKKQRALKREKEKEELEE 267
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
424-593 6.79e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 6.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 424 NTSLQTPFSEESVSHSQQGEFEQKLASTEKEVLQLNEFLKQRLSLFseekkkLEEKLKTRDRYISSLKKKcqkesEQNKE 503
Cdd:COG4717  331 PPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALL------AEAGVEDEEELRAALEQA-----EEYQE 399

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852 504 KQRRIETLEKYLADLPTLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLicqkkKEKELVTTVQSL 583
Cdd:COG4717  400 LKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAEL-----EQLEEDGELAEL 474

                        170
                 ....*....|
gi 109715852 584 QQKVERCLED 593
Cdd:COG4717  475 LQELEELKAE 484
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 486-671 6.99e-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: 38.73  E-value: 6.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852  486 YISSLKkkcqkesEQNKEKQRRIETLEKYLADLptlddvqsqslqlqilEEKNKNLQEALIDTEKKLEEIKKQCQDKETq 565
Cdd:pfam13851  27 LIKSLK-------EEIAELKKKEERNEKLMSEI----------------QQENKRLTEPLQKAQEEVEELRKQLENYEK- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852  566 licQKKKEKELVTTVQSLQQKVercledgirlpmldaKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQ---SMQG 642
Cdd:pfam13851  83 ---DKQSLKNLKARLKVLEKEL---------------KDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQqktGLKN 144

                         170       180
                  ....*....|....*....|....*....
gi 109715852  643 KLSKEKLttQKMMEELEKKERNVQRLTKA 671
Cdd:pfam13851 145 LLLEKKL--QALGETLEKKEAQLNEVLAA 171
CAGE1 pfam15066
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ...
 533-660 9.25e-03

Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.


Pssm-ID: 464481  Cd Length: 528  Bit Score: 39.43  E-value: 9.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715852  533 ILEEKN------KNLQEALIDTEKKLEEIKKqcqDKETqLICQKKKEK--------ELVTTVQSLQQKVERCLEDGIRLP 598
Cdd:pfam15066 382 VILEKNdinktlQNLQEILANTQKHLQESRK---EKET-LQLELKKIKvnyvhlqeRYITEMQQKNKSVSQCLEMDKTLS 457

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109715852  599 MLD--AKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLT-TQKMMEELEK 660
Cdd:pfam15066 458 KKEeeVERLQQLKGELEKATTSALDLLKREKETREQEFLSLQEEFQKHEKENLEeRQKLKSRLEK 522
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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