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Conserved domains on  [gi|3093476|gb|AAC16031|]
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EVI-5 homolog [Homo sapiens]

Protein Classification

TBC domain-containing protein( domain architecture ID 13892437)

TBC (Tre-2, BUB2p, Cdc16p) domain-containing protein possibly performs a GTP-activator activity on Rab-like GTPases, similar to Human ecotropic viral integration site 5 protein homolog isoform 6

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
160-368 2.36e-83

Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases.


:

Pssm-ID: 214540 [Multi-domain]  Cd Length: 216  Bit Score: 264.94  E-value: 2.36e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     160 VHKGIPHHFRAIVWQLLCSAQSMPI---KDQYSELLKMTSPCEKL----IRRDIARTYPEHNFFKEKDSLGQEVLFNVMK 232
Cdd:smart00164   1 VRKGVPPSLRGVVWKLLLNAQPMDTsadKDLYSRLLKETAPDDKSivhqIEKDLRRTFPEHSFFQDKEGPGQESLRRVLK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     233 AYSLVDREVGYCQGSAFIVGLLLMQMP-EEEAFCVFVKLMQDYRLReLFKPSMAELGLCMYQFECMIQEHLPELFVHFQS 311
Cdd:smart00164  81 AYALYNPEVGYCQGMNFLAAPLLLVMEdEEDAFWCLVKLMERYGPN-FYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKD 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 3093476     312 QSFHTSMYASSWFLTIFLTTFPLPVATRIFDIFMSEGLEIVFRVGLALLQMNQAELM 368
Cdd:smart00164 160 LGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
400-707 2.02e-09

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 61.23  E-value: 2.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     400 QVQYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETL-----EKHKCSSNYNEDFVlQLEKELVQARLSE 474
Cdd:TIGR02168  671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLrkeleELSRQISALRKDLA-RLEAEVEQLEERI 749
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     475 AESQCALKEMQDKVLDIEKRNNSLPD-----ENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARTTGR 549
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEelaeaEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     550 WKD-PPKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQ 628
Cdd:TIGR02168  830 ERRiAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK 909
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3093476     629 LSEAKRKQaeIECKNKEEVMAVRLREADsiAAVAELRQHIAELEIQKEEGKLQGQLNKSDSNQyigELKDQIAELNHEL 707
Cdd:TIGR02168  910 RSELRREL--EELREKLAQLELRLEGLE--VRIDNLQERLSEEYSLTLEEAEALENKIEDDEE---EARRRLKRLENKI 981
 
Name Accession Description Interval E-value
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
160-368 2.36e-83

Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases.


Pssm-ID: 214540 [Multi-domain]  Cd Length: 216  Bit Score: 264.94  E-value: 2.36e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     160 VHKGIPHHFRAIVWQLLCSAQSMPI---KDQYSELLKMTSPCEKL----IRRDIARTYPEHNFFKEKDSLGQEVLFNVMK 232
Cdd:smart00164   1 VRKGVPPSLRGVVWKLLLNAQPMDTsadKDLYSRLLKETAPDDKSivhqIEKDLRRTFPEHSFFQDKEGPGQESLRRVLK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     233 AYSLVDREVGYCQGSAFIVGLLLMQMP-EEEAFCVFVKLMQDYRLReLFKPSMAELGLCMYQFECMIQEHLPELFVHFQS 311
Cdd:smart00164  81 AYALYNPEVGYCQGMNFLAAPLLLVMEdEEDAFWCLVKLMERYGPN-FYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKD 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 3093476     312 QSFHTSMYASSWFLTIFLTTFPLPVATRIFDIFMSEGLEIVFRVGLALLQMNQAELM 368
Cdd:smart00164 160 LGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
RabGAP-TBC pfam00566
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ...
200-368 1.82e-55

Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are GTPase activator proteins of yeast Ypt6 and Ypt7, implies that these domains are GTPase activator proteins of Rab-like small GTPases.


Pssm-ID: 459855  Cd Length: 178  Bit Score: 188.62  E-value: 1.82e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    200 KLIRRDIARTYPEHNFFKEKDslGQEVLFNVMKAYSLVDREVGYCQGSAFIVGLLLMQ-MPEEEAFCVFVKLMQDYRLRE 278
Cdd:pfam00566  10 EQIEKDVPRTFPHSFFFDNGP--GQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLVyLDEEDAFWCFVSLLENYLLRD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    279 LFKPSMAELGLCMYQFECMIQEHLPELFVHFQSQSFHTSMYASSWFLTIFLTTFPLPVATRIFDIFMSEGLEIV-FRVGL 357
Cdd:pfam00566  88 FYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVlFRVAL 167
                         170
                  ....*....|.
gi 3093476    358 ALLQMNQAELM 368
Cdd:pfam00566 168 AILKRFREELL 178
COG5210 COG5210
GTPase-activating protein [General function prediction only];
131-377 1.99e-43

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 164.59  E-value: 1.99e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  131 EEDSWILWGRIVN-EWEDVRKKKEKQVKELVHKGIPHHFRAIVWQLLcsAQSMPIKDQ----YSELLKM-------TSPC 198
Cdd:COG5210 179 ELAADKLWISYLDpNPLSFLPVQLSKLRELIRKGIPNELRGDVWEFL--LGIGFDLDKnpglYERLLNLhreakipTQEI 256
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  199 EKLIRRDIARTYPEHNFFKEKDSLGQEVLFNVMKAYSLVDREVGYCQGSAFIVGLLLMQMPEEE-AFCVFVKLMQDYRLR 277
Cdd:COG5210 257 ISQIEKDLSRTFPDNSLFQTEISIRAENLRRVLKAYSLYNPEVGYVQGMNFLAAPLLLVLESEEqAFWCLVKLLKNYGLP 336
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  278 ELFKPSMAELGLCMYQFECMIQEHLPELFVHFQSQSFHTSMYASSWFLTIFLTTFPLPVATRIFDIFMSEGLEIVFRVGL 357
Cdd:COG5210 337 GYFLKNLSGLHRDLKVLDDLVEELDPELYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLAL 416
                       250       260
                ....*....|....*....|
gi 3093476  358 ALLQMNQAELMQLDMEGMLQ 377
Cdd:COG5210 417 AILKLLRDKLLKLDSDELLD 436
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
400-707 2.02e-09

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 61.23  E-value: 2.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     400 QVQYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETL-----EKHKCSSNYNEDFVlQLEKELVQARLSE 474
Cdd:TIGR02168  671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLrkeleELSRQISALRKDLA-RLEAEVEQLEERI 749
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     475 AESQCALKEMQDKVLDIEKRNNSLPD-----ENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARTTGR 549
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEelaeaEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     550 WKD-PPKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQ 628
Cdd:TIGR02168  830 ERRiAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK 909
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3093476     629 LSEAKRKQaeIECKNKEEVMAVRLREADsiAAVAELRQHIAELEIQKEEGKLQGQLNKSDSNQyigELKDQIAELNHEL 707
Cdd:TIGR02168  910 RSELRREL--EELREKLAQLELRLEGLE--VRIDNLQERLSEEYSLTLEEAEALENKIEDDEE---EARRRLKRLENKI 981
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
361-675 2.61e-08

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 57.82  E-value: 2.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     361 QMNQAELMQLDMEGMLQHFQKVIphqfdgvpdkliqaayqVQYNSKKMKKLEKE--YTTIKTKEMEEQVE--IKRLRTEN 436
Cdd:pfam15921  171 QIEQLRKMMLSHEGVLQEIRSIL-----------------VDFEEASGKKIYEHdsMSTMHFRSLGSAISkiLRELDTEI 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     437 RLLKQRI----ETLEKHKCSSNYNEDFVLQLEKELVQARLSEAESQcaLKEMQDKVLDIEKRNNSLPDENNI----ARLQ 508
Cdd:pfam15921  234 SYLKGRIfpveDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVE--ITGLTEKASSARSQANSIQSQLEIiqeqARNQ 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     509 EELIAVKLREAEAIMG-----LKELRQQVKDLEEHWQRHL---------ARTTGRWKDPPKKNAMNELQDELMTIRLREA 574
Cdd:pfam15921  312 NSMYMRQLSDLESTVSqlrseLREAKRMYEDKIEELEKQLvlanselteARTERDQFSQESGNLDDQLQKLLADLHKREK 391
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     575 ETQAEiREIKQRMMEMETQNQINSNHLRRaeqEVISLQEKVQYLSAQNKGLLTQLS-EAKRKQAEIECKNKEevmavrLR 653
Cdd:pfam15921  392 ELSLE-KEQNKRLWDRDTGNSITIDHLRR---ELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNES------LE 461
                          330       340
                   ....*....|....*....|....*..
gi 3093476     654 EADSIAAVAE-----LRQHIAELEIQK 675
Cdd:pfam15921  462 KVSSLTAQLEstkemLRKVVEELTAKK 488
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
406-708 3.76e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.25  E-value: 3.76e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  406 KKMKKLEKE------YTTIKTKEMEEQVE-----IKRLRTENRLLKQRIETLEKHKCSSNYNEDfvlQLEKELVQARLSE 474
Cdd:COG1196 200 RQLEPLERQaekaerYRELKEELKELEAEllllkLRELEAELEELEAELEELEAELEELEAELA---ELEAELEELRLEL 276
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  475 AESQCALKEMQDKVLDIEKRNNSLpdENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEhwqrhlarttgrwkdpp 554
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARL--EQDIARLEERRRELEERLEELEEELAELEEELEELEE----------------- 337
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  555 kknAMNELQDELMTIRLREAETQAEIREIKQRmmemetqnqinsnhLRRAEQEVISLQEKvqyLSAQNKGLLTQLSEAKR 634
Cdd:COG1196 338 ---ELEELEEELEEAEEELEEAEAELAEAEEA--------------LLEAEAELAEAEEE---LEELAEELLEALRAAAE 397
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3093476  635 KQAEIEckNKEEVMAVRLREADSI-AAVAELRQHIAELEIQKEEGKLQGQLNKSDSNQYIGELKDQIAELNHELR 708
Cdd:COG1196 398 LAAQLE--ELEEAEEALLERLERLeEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
393-715 5.84e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.14  E-value: 5.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476   393 KLIQAAYQVQynsKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKHKCSSNYNEDFVLQLEKElvqarl 472
Cdd:PRK03918 183 KFIKRTENIE---ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS------ 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476   473 seaesqcaLKEMQDKVLDIEKRnnslpdennIARLQEEliavklreaeaimgLKELRQQVKDLEE-HWQRHLARTTGRWK 551
Cdd:PRK03918 254 --------KRKLEEKIRELEER---------IEELKKE--------------IEELEEKVKELKElKEKAEEYIKLSEFY 302
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476   552 DppkknamnELQDELMTIRLREAETQAEIREIKQRMMEMETQNqinsNHLRRAEQEVISLQEKVQYLsaqnKGLLTQLSE 631
Cdd:PRK03918 303 E--------EYLDELREIEKRLSRLEEEINGIEERIKELEEKE----ERLEELKKKLKELEKRLEEL----EERHELYEE 366
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476   632 AKRKQAEIEcknkeevmavRLREADSIAAVAELRQHIAELEIQKEEgkLQGQLNKsdSNQYIGELKDQIAELNHELRCLK 711
Cdd:PRK03918 367 AKAKKEELE----------RLKKRLTGLTPEKLEKELEELEKAKEE--IEEEISK--ITARIGELKKEIKELKKAIEELK 432

                 ....
gi 3093476   712 GQKG 715
Cdd:PRK03918 433 KAKG 436
 
Name Accession Description Interval E-value
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
160-368 2.36e-83

Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases.


Pssm-ID: 214540 [Multi-domain]  Cd Length: 216  Bit Score: 264.94  E-value: 2.36e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     160 VHKGIPHHFRAIVWQLLCSAQSMPI---KDQYSELLKMTSPCEKL----IRRDIARTYPEHNFFKEKDSLGQEVLFNVMK 232
Cdd:smart00164   1 VRKGVPPSLRGVVWKLLLNAQPMDTsadKDLYSRLLKETAPDDKSivhqIEKDLRRTFPEHSFFQDKEGPGQESLRRVLK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     233 AYSLVDREVGYCQGSAFIVGLLLMQMP-EEEAFCVFVKLMQDYRLReLFKPSMAELGLCMYQFECMIQEHLPELFVHFQS 311
Cdd:smart00164  81 AYALYNPEVGYCQGMNFLAAPLLLVMEdEEDAFWCLVKLMERYGPN-FYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKD 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 3093476     312 QSFHTSMYASSWFLTIFLTTFPLPVATRIFDIFMSEGLEIVFRVGLALLQMNQAELM 368
Cdd:smart00164 160 LGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
RabGAP-TBC pfam00566
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ...
200-368 1.82e-55

Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are GTPase activator proteins of yeast Ypt6 and Ypt7, implies that these domains are GTPase activator proteins of Rab-like small GTPases.


Pssm-ID: 459855  Cd Length: 178  Bit Score: 188.62  E-value: 1.82e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    200 KLIRRDIARTYPEHNFFKEKDslGQEVLFNVMKAYSLVDREVGYCQGSAFIVGLLLMQ-MPEEEAFCVFVKLMQDYRLRE 278
Cdd:pfam00566  10 EQIEKDVPRTFPHSFFFDNGP--GQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLVyLDEEDAFWCFVSLLENYLLRD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    279 LFKPSMAELGLCMYQFECMIQEHLPELFVHFQSQSFHTSMYASSWFLTIFLTTFPLPVATRIFDIFMSEGLEIV-FRVGL 357
Cdd:pfam00566  88 FYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVlFRVAL 167
                         170
                  ....*....|.
gi 3093476    358 ALLQMNQAELM 368
Cdd:pfam00566 168 AILKRFREELL 178
COG5210 COG5210
GTPase-activating protein [General function prediction only];
131-377 1.99e-43

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 164.59  E-value: 1.99e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  131 EEDSWILWGRIVN-EWEDVRKKKEKQVKELVHKGIPHHFRAIVWQLLcsAQSMPIKDQ----YSELLKM-------TSPC 198
Cdd:COG5210 179 ELAADKLWISYLDpNPLSFLPVQLSKLRELIRKGIPNELRGDVWEFL--LGIGFDLDKnpglYERLLNLhreakipTQEI 256
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  199 EKLIRRDIARTYPEHNFFKEKDSLGQEVLFNVMKAYSLVDREVGYCQGSAFIVGLLLMQMPEEE-AFCVFVKLMQDYRLR 277
Cdd:COG5210 257 ISQIEKDLSRTFPDNSLFQTEISIRAENLRRVLKAYSLYNPEVGYVQGMNFLAAPLLLVLESEEqAFWCLVKLLKNYGLP 336
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  278 ELFKPSMAELGLCMYQFECMIQEHLPELFVHFQSQSFHTSMYASSWFLTIFLTTFPLPVATRIFDIFMSEGLEIVFRVGL 357
Cdd:COG5210 337 GYFLKNLSGLHRDLKVLDDLVEELDPELYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLAL 416
                       250       260
                ....*....|....*....|
gi 3093476  358 ALLQMNQAELMQLDMEGMLQ 377
Cdd:COG5210 417 AILKLLRDKLLKLDSDELLD 436
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
400-707 2.02e-09

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 61.23  E-value: 2.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     400 QVQYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETL-----EKHKCSSNYNEDFVlQLEKELVQARLSE 474
Cdd:TIGR02168  671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLrkeleELSRQISALRKDLA-RLEAEVEQLEERI 749
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     475 AESQCALKEMQDKVLDIEKRNNSLPD-----ENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARTTGR 549
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEelaeaEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     550 WKD-PPKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQ 628
Cdd:TIGR02168  830 ERRiAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK 909
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3093476     629 LSEAKRKQaeIECKNKEEVMAVRLREADsiAAVAELRQHIAELEIQKEEGKLQGQLNKSDSNQyigELKDQIAELNHEL 707
Cdd:TIGR02168  910 RSELRREL--EELREKLAQLELRLEGLE--VRIDNLQERLSEEYSLTLEEAEALENKIEDDEE---EARRRLKRLENKI 981
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
492-707 3.44e-09

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.84  E-value: 3.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     492 EKRNNSLPDENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEhwQRHLARTTGRWKDPPKKNAMNELQDELMTIRL 571
Cdd:TIGR02168  667 KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEE--ELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     572 RE---AETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIecknKEEVM 648
Cdd:TIGR02168  745 LEeriAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL----NEEAA 820
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 3093476     649 AVRLREADSIAAVAELRQHIAELEIQKEEGKLQGQLNksdsNQYIGELKDQIAELNHEL 707
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESL----AAEIEELEELIEELESEL 875
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
361-675 2.61e-08

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 57.82  E-value: 2.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     361 QMNQAELMQLDMEGMLQHFQKVIphqfdgvpdkliqaayqVQYNSKKMKKLEKE--YTTIKTKEMEEQVE--IKRLRTEN 436
Cdd:pfam15921  171 QIEQLRKMMLSHEGVLQEIRSIL-----------------VDFEEASGKKIYEHdsMSTMHFRSLGSAISkiLRELDTEI 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     437 RLLKQRI----ETLEKHKCSSNYNEDFVLQLEKELVQARLSEAESQcaLKEMQDKVLDIEKRNNSLPDENNI----ARLQ 508
Cdd:pfam15921  234 SYLKGRIfpveDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVE--ITGLTEKASSARSQANSIQSQLEIiqeqARNQ 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     509 EELIAVKLREAEAIMG-----LKELRQQVKDLEEHWQRHL---------ARTTGRWKDPPKKNAMNELQDELMTIRLREA 574
Cdd:pfam15921  312 NSMYMRQLSDLESTVSqlrseLREAKRMYEDKIEELEKQLvlanselteARTERDQFSQESGNLDDQLQKLLADLHKREK 391
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     575 ETQAEiREIKQRMMEMETQNQINSNHLRRaeqEVISLQEKVQYLSAQNKGLLTQLS-EAKRKQAEIECKNKEevmavrLR 653
Cdd:pfam15921  392 ELSLE-KEQNKRLWDRDTGNSITIDHLRR---ELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNES------LE 461
                          330       340
                   ....*....|....*....|....*..
gi 3093476     654 EADSIAAVAE-----LRQHIAELEIQK 675
Cdd:pfam15921  462 KVSSLTAQLEstkemLRKVVEELTAKK 488
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
406-708 3.76e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.25  E-value: 3.76e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  406 KKMKKLEKE------YTTIKTKEMEEQVE-----IKRLRTENRLLKQRIETLEKHKCSSNYNEDfvlQLEKELVQARLSE 474
Cdd:COG1196 200 RQLEPLERQaekaerYRELKEELKELEAEllllkLRELEAELEELEAELEELEAELEELEAELA---ELEAELEELRLEL 276
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  475 AESQCALKEMQDKVLDIEKRNNSLpdENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEhwqrhlarttgrwkdpp 554
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARL--EQDIARLEERRRELEERLEELEEELAELEEELEELEE----------------- 337
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  555 kknAMNELQDELMTIRLREAETQAEIREIKQRmmemetqnqinsnhLRRAEQEVISLQEKvqyLSAQNKGLLTQLSEAKR 634
Cdd:COG1196 338 ---ELEELEEELEEAEEELEEAEAELAEAEEA--------------LLEAEAELAEAEEE---LEELAEELLEALRAAAE 397
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3093476  635 KQAEIEckNKEEVMAVRLREADSI-AAVAELRQHIAELEIQKEEGKLQGQLNKSDSNQYIGELKDQIAELNHELR 708
Cdd:COG1196 398 LAAQLE--ELEEAEEALLERLERLeEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
406-664 1.48e-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: 55.45  E-value: 1.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     406 KKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKHKCSSNYNEDFV------LQLEKELVQARLSEAESQC 479
Cdd:TIGR02168  274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELeskldeLAEELAELEEKLEELKEEL 353
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     480 A-----LKEMQDKVLDIEKRNNSLpdENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARTTGRWKDpP 554
Cdd:TIGR02168  354 EsleaeLEELEAELEELESRLEEL--EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK-L 430
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     555 KKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMETQnqinsnhLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKR 634
Cdd:TIGR02168  431 EEAELKELQAELEELEEELEELQEELERLEEALEELREE-------LEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
                          250       260       270
                   ....*....|....*....|....*....|
gi 3093476     635 KQAEIecknkEEVMAVRLREADSIAAVAEL 664
Cdd:TIGR02168  504 FSEGV-----KALLKNQSGLSGILGVLSEL 528
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
503-714 1.51e-07

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.31  E-value: 1.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476   503 NIARLQEELIavKLREAEAIMglKELRQQVKDLE---EHWQRHLArttgrwkdppKKNAMNELQDELMTIRLREAET--- 576
Cdd:COG4913  226 AADALVEHFD--DLERAHEAL--EDAREQIELLEpirELAERYAA----------ARERLAELEYLRAALRLWFAQRrle 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476   577 --QAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEiECKNKEEVMAVRLRE 654
Cdd:COG4913  292 llEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELE-ERERRRARLEALLAA 370
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3093476   655 -----ADSIAAVAELRQHIAEL--EIQKEEGKLQGQLNKSDSNQYigELKDQIAELNHELRCLKGQK 714
Cdd:COG4913  371 lglplPASAEEFAALRAEAAALleALEEELEALEEALAEAEAALR--DLRRELRELEAEIASLERRK 435
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
501-708 2.05e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 2.05e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  501 ENNIARLQEEliAVKLREAeaimglKELRQQVKDLE-EHWQRHLARTTGRWKDppKKNAMNELQDELMTIRLREAETQAE 579
Cdd:COG1196 199 ERQLEPLERQ--AEKAERY------RELKEELKELEaELLLLKLRELEAELEE--LEAELEELEAELEELEAELAELEAE 268
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  580 IREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIEckNKEEVMAVRLREADSIA 659
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE--EELEELEEELEELEEEL 346
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 3093476  660 AVAELRQHIAELEIQKEEGKLQGQLNKSDSNQyiGELKDQIAELNHELR 708
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAE--EELEELAEELLEALR 393
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
423-633 4.79e-07

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 53.48  E-value: 4.79e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  423 MEEQVEIKRLRTENRL--LKQRIETLE---------------KHKCSS-----NYNEDFVLQLEKELVQARLSEAESQCA 480
Cdd:COG3206 162 LEQNLELRREEARKALefLEEQLPELRkeleeaeaaleefrqKNGLVDlseeaKLLLQQLSELESQLAEARAELAEAEAR 241
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  481 LKEMQDKVLDIEKRNNSLPDENNIARLQEELIAVKLREAEAIMGL-------KELRQQVKDLEEHWQRHLARttgrwkdp 553
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAALRAQLQQEAQR-------- 313
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  554 pkknAMNELQDELMTIRLREAETQAEIREIKQRMMEmetqnqinsnhLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAK 633
Cdd:COG3206 314 ----ILASLEAELEALQAREASLQAQLAQLEARLAE-----------LPELEAELRRLEREVEVARELYESLLQRLEEAR 378
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
393-715 5.84e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.14  E-value: 5.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476   393 KLIQAAYQVQynsKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKHKCSSNYNEDFVLQLEKElvqarl 472
Cdd:PRK03918 183 KFIKRTENIE---ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS------ 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476   473 seaesqcaLKEMQDKVLDIEKRnnslpdennIARLQEEliavklreaeaimgLKELRQQVKDLEE-HWQRHLARTTGRWK 551
Cdd:PRK03918 254 --------KRKLEEKIRELEER---------IEELKKE--------------IEELEEKVKELKElKEKAEEYIKLSEFY 302
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476   552 DppkknamnELQDELMTIRLREAETQAEIREIKQRMMEMETQNqinsNHLRRAEQEVISLQEKVQYLsaqnKGLLTQLSE 631
Cdd:PRK03918 303 E--------EYLDELREIEKRLSRLEEEINGIEERIKELEEKE----ERLEELKKKLKELEKRLEEL----EERHELYEE 366
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476   632 AKRKQAEIEcknkeevmavRLREADSIAAVAELRQHIAELEIQKEEgkLQGQLNKsdSNQYIGELKDQIAELNHELRCLK 711
Cdd:PRK03918 367 AKAKKEELE----------RLKKRLTGLTPEKLEKELEELEKAKEE--IEEEISK--ITARIGELKKEIKELKKAIEELK 432

                 ....
gi 3093476   712 GQKG 715
Cdd:PRK03918 433 KAKG 436
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
396-671 7.26e-07

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.14  E-value: 7.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     396 QAAYQVQYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKHKCSsnyNEDFVLQLEKELVQARLSEA 475
Cdd:TIGR02168  793 QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE---LSEDIESLAAEIEELEELIE 869
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     476 ESQCALKEMQDKVldiekrnnslpdenniARLQEELIAVKLREAEAIMGLKELRQQVKDLEEhwqrhlarttgrwkdppk 555
Cdd:TIGR02168  870 ELESELEALLNER----------------ASLEEALALLRSELEELSEELRELESKRSELRR------------------ 915
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     556 knAMNELQDELMTIRLREAETQAEIREIKQR--------MMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLT 627
Cdd:TIGR02168  916 --ELEELREKLAQLELRLEGLEVRIDNLQERlseeysltLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIE 993
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 3093476     628 QLSEAKRKQAEIEcKNKEevmavrlreaDSIAAVAELRQHIAEL 671
Cdd:TIGR02168  994 EYEELKERYDFLT-AQKE----------DLTEAKETLEEAIEEI 1026
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
396-677 1.10e-06

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: 52.43  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    396 QAAYQVQYNSKKMKKLEKEytTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKHKCSSNYNEDFVLQLEKELVQARLSEA 475
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQE--RLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEER 358
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    476 ESQCALKEMQDKVLDIEKRNNslpdennIARLQEEliavKLREAEAIMGLKELRQQVKDLEEHWQRHLARTTGRWKDPPK 555
Cdd:pfam17380 359 KRELERIRQEEIAMEISRMRE-------LERLQME----RQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRA 427
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    556 KnamnelQDELMTIRLREAETQAEIREIKQRMMEMETQNQI-----NSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLS 630
Cdd:pfam17380 428 E------QEEARQREVRRLEEERAREMERVRLEEQERQQQVerlrqQEEERKRKKLELEKEKRDRKRAEEQRRKILEKEL 501
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 3093476    631 EAkRKQAEIECKNKEEVMAVRLREADSiAAVAELRQHIAELEIQKEE 677
Cdd:pfam17380 502 EE-RKQAMIEEERKRKLLEKEMEERQK-AIYEEERRREAEEERRKQQ 546
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
506-713 2.93e-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: 51.21  E-value: 2.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     506 RLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHlarttgRWKDPPKKNAMNELQDELMTIRLREAETQAEIREIKQ 585
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEEL------RLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     586 RM-------MEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIECKNK---EEVMAVRLREA 655
Cdd:TIGR02168  310 RLanlerqlEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEeleEQLETLRSKVA 389
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3093476     656 DSIAAVAELRQHIAELEIQKEEGKL--------QGQLNKSDSNQYIGELKDQIAELNHELRCLKGQ 713
Cdd:TIGR02168  390 QLELQIASLNNEIERLEARLERLEDrrerlqqeIEELLKKLEEAELKELQAELEELEEELEELQEE 455
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
504-708 1.14e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476   504 IARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARTTGRWKD---PPKKNAMNELQDE----------LMTIR 570
Cdd:COG4913  612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEidvASAEREIAELEAElerldassddLAALE 691
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476   571 LREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIEC--------- 641
Cdd:COG4913  692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAverelrenl 771
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476   642 ----------KNKEEVMAVRLREA-------------DSIAAVAELRQHIAELE----IQKEEgKLQGQLNKSdSNQYIG 694
Cdd:COG4913  772 eeridalrarLNRAEEELERAMRAfnrewpaetadldADLESLPEYLALLDRLEedglPEYEE-RFKELLNEN-SIEFVA 849
                        250       260
                 ....*....|....*....|....*
gi 3093476   695 EL-----------KDQIAELNHELR 708
Cdd:COG4913  850 DLlsklrraireiKERIDPLNDSLK 874
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
405-647 1.82e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.53  E-value: 1.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     405 SKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKhkcssnynedfvlqlEKELVQARLSEAESQcaLKEM 484
Cdd:TIGR02169  715 SRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS---------------ELKELEARIEELEED--LHKL 777
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     485 QDKVLDIEKRnnslPDENNIARLQEELIAVK---------LREAEAIMGLKEL-RQQVKDLEEHWQRHLARTTGRWKDpp 554
Cdd:TIGR02169  778 EEALNDLEAR----LSHSRIPEIQAELSKLEeevsriearLREIEQKLNRLTLeKEYLEKEIQELQEQRIDLKEQIKS-- 851
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     555 KKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKR 634
Cdd:TIGR02169  852 IEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
                          250
                   ....*....|...
gi 3093476     635 KQAEIECKNKEEV 647
Cdd:TIGR02169  932 ELSEIEDPKGEDE 944
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
406-714 3.90e-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: 47.32  E-value: 3.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    406 KKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKHKcssNYNEDFVLQLEKELVQARLSEAESQCAL---- 481
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENEL---NLLEKEKLNIQKNIDKIKNKLLKLELLLsnlk 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    482 ------KEMQDKVLDIEKRNNSLpdENNIARLQEELIAVKL---REAEAIMGLKELRQQVKDLEEHWQRHLARTTGRWKD 552
Cdd:TIGR04523 208 kkiqknKSLESQISELKKQNNQL--KDNIEKKQQEINEKTTeisNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE 285
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    553 ppKKNAMNELQDELMTIRLREA-----ETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLT 627
Cdd:TIGR04523 286 --LEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQR 363
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    628 QLSEaKRKQAEIECKNKEEVMAVRLREADSIAAVAELRQHIAELEIQKEEGKLQGQLNKSDSNQYIGELKDQIAELNHEL 707
Cdd:TIGR04523 364 ELEE-KQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEI 442

                  ....*..
gi 3093476    708 RCLKGQK 714
Cdd:TIGR04523 443 KDLTNQD 449
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
504-714 4.17e-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: 4.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     504 IARLQEELIAVKLREAEAIMGLKELRQQVKDLEehwqrhlarttgrwKDPPKKNAMNELQDElmtirLREAETQAEIREI 583
Cdd:TIGR02169  172 KEKALEELEEVEENIERLDLIIDEKRQQLERLR--------------REREKAERYQALLKE-----KREYEGYELLKEK 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     584 KqrmmEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKqaeIECKNKEEVMAVRLREADSIAAVAE 663
Cdd:TIGR02169  233 E----ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKK---IKDLGEEEQLRVKEKIGELEAEIAS 305
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 3093476     664 LRQHIAELEIQKEEgkLQGQLNKSDSNqyIGELKDQIAELNHELRCLKGQK 714
Cdd:TIGR02169  306 LERSIAEKERELED--AEERLAKLEAE--IDKLLAEIEELEREIEEERKRR 352
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
392-711 4.47e-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: 4.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    392 DKLIQAAYQVQYNSKKMKKLEKEYTTIKT-----KEMEEQVEIKRLRTENRLLKQRIETLEKHKCSSNYN----EDFVLQ 462
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSeisdlNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIisqlNEQISQ 346
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    463 LEKELVQARLSEAESQCALKEMQDKVLDIEKRNNSLPDE-----NNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEE 537
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEiknleSQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    538 HWQRHLARTT---GRWKDPPKKNAMNELQDELMTIRLREAETQAEIREIKQRmmEMETQNQINSNHLRRAEQEVISLQEK 614
Cdd:TIGR04523 427 EIERLKETIIknnSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSIN--KIKQNLEQKQKELKSKEKELKKLNEE 504
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    615 VQYLSAQNKGLLTQLSEAKRKQAEIECKNKeevmavrlreadsiaavaelrqhiaelEIQKEEGKLQGQLNKSDSNQYIG 694
Cdd:TIGR04523 505 KKELEEKVKDLTKKISSLKEKIEKLESEKK---------------------------EKESKISDLEDELNKDDFELKKE 557
                         330
                  ....*....|....*..
gi 3093476    695 ELKDQIAELNHELRCLK 711
Cdd:TIGR04523 558 NLEKEIDEKNKEIEELK 574
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
462-689 4.50e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 46.68  E-value: 4.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  462 QLEKELVQARLSEAESQCALKEMQDKVLDIEKRNNSLpdENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLeehwQR 541
Cdd:COG4942  24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL--ERRIAALARRIRALEQELAALEAELAELEKEIAEL----RA 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  542 HLARTTGRWKDPPKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSnhLRRAEQEVISLQEKVQYLSAQ 621
Cdd:COG4942  98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE--LRADLAELAALRAELEAERAE 175
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  622 NKGLLTQLSEAKRKQAEIECKNKEEVMAVRLREADSIAAVAELRQHIAELE--IQKEEGKLQGQLNKSDS 689
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEalIARLEAEAAAAAERTPA 245
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
475-668 6.03e-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: 6.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  475 AESQCALKEMQD---KVLDIEKRNNSLPDEnnIARLQEELIAVKLREAEAIMGLKELRQQVKDLE---EHWQRHLARTTG 548
Cdd:COG1579   3 PEDLRALLDLQEldsELDRLEHRLKELPAE--LAELEDELAALEARLEAAKTELEDLEKEIKRLEleiEEVEARIKKYEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  549 RWKDPPKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQEvisLQEKVQYLSAQNKGLLTQ 628
Cdd:COG1579  81 QLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAE---LEEKKAELDEELAELEAE 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 3093476  629 LSEAKRKQAEIECKNKEEVMAV--RLREADSIAAVAELRQHI 668
Cdd:COG1579 158 LEELEAEREELAAKIPPELLALyeRIRKRKNGLAVVPVEGGA 199
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
525-708 6.03e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.68  E-value: 6.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  525 LKELRQQVKDLEEHWQRHlarttgrwkdppkknamNELQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSNH--LR 602
Cdd:COG4717  73 LKELEEELKEAEEKEEEY-----------------AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYqeLE 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  603 RAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIECKNKEevmAVRLREADSIAAVAELRQHIAELE-IQKEEGKLQ 681
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEE---LEELLEQLSLATEEELQDLAEELEeLQQRLAELE 212
                       170       180
                ....*....|....*....|....*..
gi 3093476  682 GQLNKSDsnQYIGELKDQIAELNHELR 708
Cdd:COG4717 213 EELEEAQ--EELEELEEELEQLENELE 237
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
410-714 1.28e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 45.88  E-value: 1.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     410 KLEKEYTTIKTK-EMEEQVE--IKRLRTENRLLKQRIETLEKHKCSSNYNEDFVLQLEKELVQARLSEAESQCALKEMQD 486
Cdd:pfam15921  445 QMERQMAAIQGKnESLEKVSslTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRS 524
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     487 KV-LDIEKRNNSLPDENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHlARTTG--RWKDPPKKNAMNELQ 563
Cdd:pfam15921  525 RVdLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQH-GRTAGamQVEKAQLEKEINDRR 603
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     564 DELMTIRLREAETQAEIREIKQRM--MEMETQNQINSNHLR-RAEQEVisLQEKVQYLS--AQNKGLLTQLSEA------ 632
Cdd:pfam15921  604 LELQEFKILKDKKDAKIRELEARVsdLELEKVKLVNAGSERlRAVKDI--KQERDQLLNevKTSRNELNSLSEDyevlkr 681
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     633 --KRKQAEIECKNKEevMAVRLREADSiaAVAELRQHIAELE------------IQKEEGKLQGQLNKSDSNqyIGELKD 698
Cdd:pfam15921  682 nfRNKSEEMETTTNK--LKMQLKSAQS--ELEQTRNTLKSMEgsdghamkvamgMQKQITAKRGQIDALQSK--IQFLEE 755
                          330
                   ....*....|....*.
gi 3093476     699 QIAELNHELRCLKGQK 714
Cdd:pfam15921  756 AMTNANKEKHFLKEEK 771
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
406-713 1.37e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 1.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  406 KKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKHKcssnynEDFVLQLEKELVQARLSEAESQcaLKEMQ 485
Cdd:COG4717  81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL------QLLPLYQELEALEAELAELPER--LEELE 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  486 DKVLDIEKRNNSLPD-ENNIARLQEELiaVKLREAEAIMGLKELRQQVKDLEEHWQRhlarttgrwkdppkknaMNELQD 564
Cdd:COG4717 153 ERLEELRELEEELEElEAELAELQEEL--EELLEQLSLATEEELQDLAEELEELQQR-----------------LAELEE 213
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  565 ELMTIRLREAETQAEIREIKQRMMEMETQNQINSN-------------------------------------------HL 601
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELEAAALEERLKEArlllliaaallallglggsllsliltiagvlflvlgllallflLL 293
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  602 RRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIECKNKEEVMAVRLREADSIAAVAELRQHIAELEIQKEEGKLQ 681
Cdd:COG4717 294 AREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA 373
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 3093476  682 GQLNKSDSN-----QYIGELKDQIAELNHELRCLKGQ 713
Cdd:COG4717 374 ALLAEAGVEdeeelRAALEQAEEYQELKEELEELEEQ 410
PTZ00121 PTZ00121
MAEBL; Provisional
392-702 1.56e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    392 DKLIQAAYQVQYNSKKMKKLEKEYttiKTKEMEEQVEIKRlRTENrlLKQRIEtlEKHKCSsnynedfvlQLEKELVQAR 471
Cdd:PTZ00121 1421 DEAKKKAEEKKKADEAKKKAEEAK---KADEAKKKAEEAK-KAEE--AKKKAE--EAKKAD---------EAKKKAEEAK 1483
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    472 LSEaESQCALKEMQDKVLDIEKRNNSLPDENNIARLQEELIAVKLREAEAIMGLKELR--QQVKDLEEHWQRHLARTTGR 549
Cdd:PTZ00121 1484 KAD-EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKkaEEKKKADELKKAEELKKAEE 1562
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    550 WKDPPKKNAMNElqDELMTIRLREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQL 629
Cdd:PTZ00121 1563 KKKAEEAKKAEE--DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3093476    630 SEAKRKQAEIECKNKEEVMAVRlreADSIAAVAELRQHIAElEIQKEE----GKLQGQLNKSDSNQYIGELKDQIAE 702
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKIK---AAEEAKKAEEDKKKAE-EAKKAEedekKAAEALKKEAEEAKKAEELKKKEAE 1713
PRK11281 PRK11281
mechanosensitive channel MscK;
439-682 1.89e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 45.29  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    439 LKQRIETLEKHKcssnynedfVLQLEKELVQARLSEAESQCALKEMQDKVLD-IEKRNNSLPDE-----NNIARLQEELI 512
Cdd:PRK11281   41 VQAQLDALNKQK---------LLEAEDKLVQQDLEQTLALLDKIDRQKEETEqLKQQLAQAPAKlrqaqAELEALKDDND 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    513 AVkLREAEAIMGLKELRQQVKDLEEHWQRhlarttgrwkdppKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMET 592
Cdd:PRK11281  112 EE-TRETLSTLSLRQLESRLAQTLDQLQN-------------AQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRN 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    593 Q---NQINSNHLR-------RAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAeIECKNKEEVMAVRLREADSIAAVA 662
Cdd:PRK11281  178 LlkgGKVGGKALRpsqrvllQAEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYL-TARIQRLEHQLQLLQEAINSKRLT 256
                         250       260
                  ....*....|....*....|
gi 3093476    663 ELRQHIAELEIQKEEGKLQG 682
Cdd:PRK11281  257 LSEKTVQEAQSQDEAARIQA 276
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
408-610 4.25e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 4.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  408 MKKLEKEYTTI-KTKEMEEQVEIKRLRTENRLLKQRIETLEKHKcssnynedfvlQLEKELVQARLSEAESQCALKEMQD 486
Cdd:COG4717  48 LERLEKEADELfKPQGRKPELNLKELKELEEELKEAEEKEEEYA-----------ELQEELEELEEELEELEAELEELRE 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  487 KVLDIEKRNNSLPDENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLE------EHWQRHLARTTGRWkDPPKKNAMN 560
Cdd:COG4717 117 ELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEeleaelAELQEELEELLEQL-SLATEEELQ 195
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 3093476  561 ELQDELMTIRLREAETQAEIREIKQRMMEMETQ-NQINSNHLRRAEQEVIS 610
Cdd:COG4717 196 DLAEELEELQQRLAELEEELEEAQEELEELEEElEQLENELEAAALEERLK 246
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
407-714 4.92e-04

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: 43.81  E-value: 4.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     407 KMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLK---QRIETLEKHKCSsnynEDFVLQLEKELVQARLSEAESQcaLKE 483
Cdd:pfam02463  168 KRKKKEALKKLIEETENLAELIIDLEELKLQELKlkeQAKKALEYYQLK----EKLELEEEYLLYLDYLKLNEER--IDL 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     484 MQDKVLDIEKRNNSLPDENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARTTGRwkdpPKKNAMNELQ 563
Cdd:pfam02463  242 LQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER----RKVDDEEKLK 317
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     564 DELMTIRLREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQeviSLQEKVQYLSAQNKGLLTQLSEAKRKQAEIECKN 643
Cdd:pfam02463  318 ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEE---LEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE 394
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3093476     644 KE-EVMAVRLREADSIAAVAELRQHIAELEIQKEEGKLQGQLNKSDSNQ-YIGELKDQIAELNHELRCLKGQK 714
Cdd:pfam02463  395 EElELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQgKLTEEKEELEKQELKLLKDELEL 467
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
412-586 6.95e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 6.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476   412 EKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKHkcssnynedfVLQLEKELVQA---RLSEAEsqcalKEMQDKV 488
Cdd:COG4913  287 QRRLELLEAELEELRAELARLEAELERLEARLDALREE----------LDELEAQIRGNggdRLEQLE-----REIERLE 351
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476   489 LDIEKRnnslpdENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARTTgrwkdppkkNAMNELQDELMT 568
Cdd:COG4913  352 RELEER------ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALE---------EALAEAEAALRD 416
                        170
                 ....*....|....*...
gi 3093476   569 IRLREAETQAEIREIKQR 586
Cdd:COG4913  417 LRRELRELEAEIASLERR 434
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
502-708 9.60e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.70  E-value: 9.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  502 NNIARL-QEELIAVKLREAEAIMG-----LKELRQQVKDLEEHWQRHLARTTGRwkDPPKK-----NAMNELQDELMTIR 570
Cdd:COG3206 155 NALAEAyLEQNLELRREEARKALEfleeqLPELRKELEEAEAALEEFRQKNGLV--DLSEEaklllQQLSELESQLAEAR 232
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  571 LREAETQAEIREIKQRmmemetqnqinsnhLRRAEQEVISLQEkvqylSAQNKGLLTQLSEAKRKQAEiecknkeevMAV 650
Cdd:COG3206 233 AELAEAEARLAALRAQ--------------LGSGPDALPELLQ-----SPVIQQLRAQLAELEAELAE---------LSA 284
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3093476  651 RLREADSiaAVAELRQHIAELE--IQKEEGKLQGQL--NKSDSNQYIGELKDQIAELNHELR 708
Cdd:COG3206 285 RYTPNHP--DVIALRAQIAALRaqLQQEAQRILASLeaELEALQAREASLQAQLAQLEARLA 344
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
556-713 1.15e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.31  E-value: 1.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  556 KNAMNELQDELMTIR--LREAEtqAEIREIKQR--MMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSE 631
Cdd:COG3206 174 RKALEFLEEQLPELRkeLEEAE--AALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  632 AKRKQAEIecKNKEEVMAVRLREADSIAAVAELRQ-----HIAELEIQKEEGKLQGQLnKSDSNQYIGELKDQIAELNHE 706
Cdd:COG3206 252 GPDALPEL--LQSPVIQQLRAQLAELEAELAELSArytpnHPDVIALRAQIAALRAQL-QQEAQRILASLEAELEALQAR 328

                ....*..
gi 3093476  707 LRCLKGQ 713
Cdd:COG3206 329 EASLQAQ 335
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
501-714 1.37e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 1.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  501 ENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARTTGrwkdppKKNAMNELQDELmtirlreAETQAEI 580
Cdd:COG3883  15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEA------LQAEIDKLQAEI-------AEAEAEI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  581 REIKQRMMEMETQNQINSNHLRRAE--------QEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEiecknkeevmavrl 652
Cdd:COG3883  82 EERREELGERARALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEA-------------- 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3093476  653 READSIAAVAELRQHIAELEIQKEEgkLQGQlnKSDSNQYIGELKDQIAELNHELRCLKGQK 714
Cdd:COG3883 148 KKAELEAKLAELEALKAELEAAKAE--LEAQ--QAEQEALLAQLSAEEAAAEAQLAELEAEL 205
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
405-717 1.76e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476   405 SKKMKKLEKEYTTIKTKEMEEQvEIKRLRTENRLLKQRIETLEKHKcssnynedfvlqLEKELvqarlSEAESqcALKEM 484
Cdd:PRK03918 344 KKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPEK------------LEKEL-----EELEK--AKEEI 403
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476   485 QDKVLDIEKRNNSLpdENNIARLQEELIAVKLREAEAIMGLKELRqqvkdlEEHwqrhlarttgrwkdppKKNAMNELQD 564
Cdd:PRK03918 404 EEEISKITARIGEL--KKEIKELKKAIEELKKAKGKCPVCGRELT------EEH----------------RKELLEEYTA 459
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476   565 ELMTIRLREAETQAEIREIKQRMMEMETqnqinsnhLRRAEQEVISLQEKVQYL-SAQNKGLLTQLSEAKRKQAEIEcKN 643
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEK--------VLKKESELIKLKELAEQLkELEEKLKKYNLEELEKKAEEYE-KL 530
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3093476   644 KEEVMAVR---LREADSIAAVAELRQHIAELEIQkeegklqgqlnksdsnqyIGELKDQIAELNHELRclkgQKGFS 717
Cdd:PRK03918 531 KEKLIKLKgeiKSLKKELEKLEELKKKLAELEKK------------------LDELEEELAELLKELE----ELGFE 585
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
391-640 1.99e-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: 41.29  E-value: 1.99e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  391 PDKLIQAAYQVQYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKHkcssnynedfVLQLEKELVQA 470
Cdd:COG4942  19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE----------LAALEAELAEL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  471 RLSEAESQCALKEMQDkvlDIEKRNNSLPDENNIARLQEELIAVKLREAE-AIMGLKELRQQVKDLEEHWQRHLArttgr 549
Cdd:COG4942  89 EKEIAELRAELEAQKE---ELAELLRALYRLGRQPPLALLLSPEDFLDAVrRLQYLKYLAPARREQAEELRADLA----- 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  550 wkdppkknamnELQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQL 629
Cdd:COG4942 161 -----------ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
                       250
                ....*....|.
gi 3093476  630 SEAKRKQAEIE 640
Cdd:COG4942 230 ARLEAEAAAAA 240
Fibrinogen_BP pfam08017
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ...
433-695 2.19e-03

Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.


Pssm-ID: 311808 [Multi-domain]  Cd Length: 393  Bit Score: 41.39  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    433 RTENRLLKQRIETLEkHKCSSNYNE----DFVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKRN--NSLPDENNIAR 506
Cdd:pfam08017  41 RSQGNVLERRQRDAE-NRSQGNVLErrqrDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSqgNVLERRQRDAE 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    507 LQEELIAVKLREAEAimglkELRQQVKDLEEHWQRHLARTTGRWKDPPKKNAMNELQDELMTIRLREAE--TQAEIREIK 584
Cdd:pfam08017 120 NKSQGNVLERRQRDA-----ENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAEnkSQGNVLERR 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    585 QRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKgllTQLSEAKRKQAEIECKNKEEVMAVRLREAD--SIAAVA 662
Cdd:pfam08017 195 QRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENR---SQGNVLERRQRDAENKSQGNVLERRQRDAEnrSQGNVL 271
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 3093476    663 ELRQHIAELEIQKE--EGKLQGQLNKSDSNQYIGE 695
Cdd:pfam08017 272 ERRQRDAENRSQGNvlERRQRDAENKSQVGQLIGK 306
mukB PRK04863
chromosome partition protein MukB;
408-686 2.20e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.87  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    408 MKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKHKCSSNYNEDFVLQLEKELVQARLSEAESQCA-LKEMQD 486
Cdd:PRK04863  839 LRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLADRVEEIREQLDEAEEAKRfVQQHGN 918
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    487 KVLDIEKRNNSL-PDENNIARLQEELiavklreAEAIMGLKELRQQVKDLEEHWQR--HLArttgrWKDPPKK-NAMNEL 562
Cdd:PRK04863  919 ALAQLEPIVSVLqSDPEQFEQLKQDY-------QQAQQTQRDAKQQAFALTEVVQRraHFS-----YEDAAEMlAKNSDL 986
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    563 QDELMTiRLREAETQAeiREIKQRMMEMETQnqinsnhLRRAEQEVISLQEkvqylSAQNKglLTQLSEAKRKQAEI--- 639
Cdd:PRK04863  987 NEKLRQ-RLEQAEQER--TRAREQLRQAQAQ-------LAQYNQVLASLKS-----SYDAK--RQMLQELKQELQDLgvp 1049
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 3093476    640 ECKNKEEVMAVRLREADSIAAVAELRQHIAELEIQKEEGKLQGQLNK 686
Cdd:PRK04863 1050 ADSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKK 1096
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
392-707 2.45e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 2.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476   392 DKLIQAAYQVQYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKHKCSSNYNEDFVLQLE----KEL 467
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelkeKAE 293
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476   468 VQARLSEaesqcALKEMQDKVLDIEKRNNSLpdENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARTT 547
Cdd:PRK03918 294 EYIKLSE-----FYEEYLDELREIEKRLSRL--EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEE 366
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476   548 GRwkdpPKKNAMNELQDELMTIRLREAEtqAEIREIKQRMMEMETQnqinsnhLRRAEQEVISLQEKVqylsAQNKGLLT 627
Cdd:PRK03918 367 AK----AKKEELERLKKRLTGLTPEKLE--KELEELEKAKEEIEEE-------ISKITARIGELKKEI----KELKKAIE 429
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476   628 QLSEAKRK----QAEIECKNKEEVMAVRLREADSIAA-VAELRQHIAELEiqKEEGKLQGQLNKSDSNQYIGELKDQIAE 702
Cdd:PRK03918 430 ELKKAKGKcpvcGRELTEEHRKELLEEYTAELKRIEKeLKEIEEKERKLR--KELRELEKVLKKESELIKLKELAEQLKE 507

                 ....*
gi 3093476   703 LNHEL 707
Cdd:PRK03918 508 LEEKL 512
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
419-621 2.65e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 2.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  419 KTKEMEEQVEIKRLRTENRLLKQRI-ETLEKHKCSSNYNEDFVLQLEKELVQARLSEAESQCALKEMQdkVLDIEKRNNS 497
Cdd:COG4717 297 KASLGKEAEELQALPALEELEEEELeELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAA 374
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  498 LPDENNIArlQEELIAVKLREAEAimgLKELRQQVKDLEEHWQRHLARTTGRWKDPPKKNAMNELQDELMTIRLREAET- 576
Cdd:COG4717 375 LLAEAGVE--DEEELRAALEQAEE---YQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELe 449
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 3093476  577 --QAEIREIKQRMMEMETQNQinsnhLRRAEQEVISLQEKVQYLSAQ 621
Cdd:COG4717 450 elREELAELEAELEQLEEDGE-----LAELLQELEELKAELRELAEE 491
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
402-666 3.71e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 40.96  E-value: 3.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    402 QYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIEtLEKHKcssnyneDFVLQLEKELVQARLSEAESQcAL 481
Cdd:pfam10174 483 KVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIA-VEQKK-------EECSKLENQLKKAHNAEEAVR-TN 553
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    482 KEMQDKVLDIEKRNNSLPDENNIARLQEELIAVKLREAEAIMGLKElrQQVKDLEEHWQRHLarttgrwKDPPKKNAMNE 561
Cdd:pfam10174 554 PEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKD--KKIAELESLTLRQM-------KEQNKKVANIK 624
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    562 LQDELMtiRLREAETQAEIREIKQRMMEMETQNQINS--NHLRRAEQEVISLQEKV---QYLSAQNKGLLTQLSEAKRKQ 636
Cdd:pfam10174 625 HGQQEM--KKKGAQLLEEARRREDNLADNSQQLQLEElmGALEKTRQELDATKARLsstQQSLAEKDGHLTNLRAERRKQ 702
                         250       260       270
                  ....*....|....*....|....*....|
gi 3093476    637 AEIECKNKEEVMAVRLREADSIAAVAELRQ 666
Cdd:pfam10174 703 LEEILEMKQEALLAAISEKDANIALLELSS 732
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
405-714 4.60e-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: 40.39  E-value: 4.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    405 SKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLekhkcsSNYNEDFVLQLE---KELVQA--RLSEAESQC 479
Cdd:TIGR04523 217 ESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQL------KDEQNKIKKQLSekqKELEQNnkKIKELEKQL 290
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    480 ALKEMQDKVLDIEKRNNSLPD-ENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHwqrhlaRTTGRWKDPPKKNA 558
Cdd:TIGR04523 291 NQLKSEISDLNNQKEQDWNKElKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKE------LTNSESENSEKQRE 364
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    559 MNELQDELMTIRLREAETQAEIREIKQRMMEMETQ-------NQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSE 631
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKiqnqeklNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    632 AKRKQAEIECKNK---------EEVMAVRLREADSIAAvaELRQHIAELEIQKEEGKlqgQLN--KSDSNQYIGELKDQI 700
Cdd:TIGR04523 445 LTNQDSVKELIIKnldntreslETQLKVLSRSINKIKQ--NLEQKQKELKSKEKELK---KLNeeKKELEEKVKDLTKKI 519
                         330
                  ....*....|....
gi 3093476    701 AELNHELRCLKGQK 714
Cdd:TIGR04523 520 SSLKEKIEKLESEK 533
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
402-713 4.71e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 4.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476   402 QYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIE----TLEKHKcsSNYNEDFVLQLEKELVQARLSEAES 477
Cdd:PRK02224 195 QIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDeadeVLEEHE--ERREELETLEAEIEDLRETIAETER 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476   478 QC-----ALKEMQDKVLDIEKRNNSLPDENNIARLQEELIAVKLREAEAimGLKELRQQVKDLEEHWQRHlarttgrwkd 552
Cdd:PRK02224 273 EReelaeEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELED--RDEELRDRLEECRVAAQAH---------- 340
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476   553 ppkknamnELQDELMTIRLREAETQAEirEIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEA 632
Cdd:PRK02224 341 --------NEEAESLREDADDLEERAE--ELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476   633 KRKQAEIEcknkEEVMAVRLREADSIAAVAELRQHIAELEIQKEEGKLQ--GQ-LNKSDSNQYIGELKDQIAELNHELRC 709
Cdd:PRK02224 411 EDFLEELR----EERDELREREAELEATLRTARERVEEAEALLEAGKCPecGQpVEGSPHVETIEEDRERVEELEAELED 486

                 ....
gi 3093476   710 LKGQ 713
Cdd:PRK02224 487 LEEE 490
DUF1129 pfam06570
Protein of unknown function (DUF1129); This family consists of several hypothetical bacterial ...
453-493 5.22e-03

Protein of unknown function (DUF1129); This family consists of several hypothetical bacterial proteins of unknown function.


Pssm-ID: 429008  Cd Length: 200  Bit Score: 39.18  E-value: 5.22e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 3093476    453 SNYNEDFVLQLEKELVQARLSEAESQCALKEMQDKVLDIEK 493
Cdd:pfam06570   3 TKKNQDYIFRLTKQLIKDGKSDEEIKEILDEMLPEILEGQK 43
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
462-704 6.25e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 40.21  E-value: 6.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     462 QLEKELVQARLSEAESQCALKEMQDKVLDIEKRNNSLpdENNIARLQ---------EELIAVKLREAEAimGLKELRQQV 532
Cdd:pfam12128  217 RLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTL--ESAELRLShlhfgyksdETLIASRQEERQE--TSAELNQLL 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     533 KDLEEHWQRHLARTTGRWKDPPKKNAMNELQDELMTIRLReaetQAEIREIKQRMMEMETQNQINSNhlrraeqevISLQ 612
Cdd:pfam12128  293 RTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHG----AFLDADIETAAADQEQLPSWQSE---------LENL 359
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476     613 EKVQYLSAQNKGLLTQLSEAKRKQAEIECKNKEEVMAVRLreaDSIAAVAELRQHIAELEIQKEEGKLQGQLNKSDSNQY 692
Cdd:pfam12128  360 EERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKL---AKIREARDRQLAVAEDDLQALESELREQLEAGKLEFN 436
                          250
                   ....*....|....
gi 3093476     693 IGE--LKDQIAELN 704
Cdd:pfam12128  437 EEEyrLKSRLGELK 450
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
572-685 7.67e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 38.01  E-value: 7.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476   572 REAETQAEIREIKQRMMEMETQnqinsnhLRRAEQEVISLQEKVQYLSAQNKglltqlSEAKRKQAEIECKNKEEVMAVR 651
Cdd:PRK07352  51 RREAILQALKEAEERLRQAAQA-------LAEAQQKLAQAQQEAERIRADAK------ARAEAIRAEIEKQAIEDMARLK 117
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 3093476   652 ---LREADSIA--AVAELRQHIAELEIQKEEGKLQGQLN 685
Cdd:PRK07352 118 qtaAADLSAEQerVIAQLRREAAELAIAKAESQLPGRLD 156
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
501-708 9.48e-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: 38.98  E-value: 9.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  501 ENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEhwqrhLARTTgrwkdppkKNAMNELQDELMTIRLREAETQAEI 580
Cdd:COG4942  33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALAR-----RIRAL--------EQELAALEAELAELEKEIAELRAEL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476  581 REIKQRMMEMETQNQINSNH----LRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIEcknkeevmavrlread 656
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQpplaLLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA---------------- 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 3093476  657 siaavaELRQHIAELEIQKEEGKLQGQLNKSDSNQYIGELKDQIAELNHELR 708
Cdd:COG4942 164 ------ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA 209
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
419-667 9.63e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 39.42  E-value: 9.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    419 KTKEMEEQVEIKR---LRTENRLLK-QRIETLEKHKCSSNyneDFVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKR 494
Cdd:pfam10174 518 KLKSLEIAVEQKKeecSKLENQLKKaHNAEEAVRTNPEIN---DRIRLLEQEVARYKEESGKAQAEVERLLGILREVENE 594
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    495 NNSlpDENNIARLqEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARttgRWKDPPKKNAMNELQDELMTIRLRea 574
Cdd:pfam10174 595 KND--KDKKIAEL-ESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEAR---RREDNLADNSQQLQLEELMGALEK-- 666
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3093476    575 eTQAEIREIKQRMMEMETQNQINSNHL------RRAEQEVIsLQEKVQYLSA------QNKGLLtQLSEAKRKqaeiecK 642
Cdd:pfam10174 667 -TRQELDATKARLSSTQQSLAEKDGHLtnlraeRRKQLEEI-LEMKQEALLAaisekdANIALL-ELSSSKKK------K 737
                         250       260
                  ....*....|....*....|....*
gi 3093476    643 NKEEVMAVRlREADSIaaVAELRQH 667
Cdd:pfam10174 738 TQEEVMALK-REKDRL--VHQLKQQ 759
 
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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