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Conserved domains on  [gi|23271084|gb|AAH23296|]
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Leucine rich repeat containing 45 [Mus musculus]

Protein Classification

leucine-rich repeat domain-containing protein( domain architecture ID 1905305)

leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
12-257 1.81e-30

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


The actual alignment was detected with superfamily member COG5238:

Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 124.52  E-value: 1.81e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  12 CEESGAEPQEAVLQQLHQLPK-GGLDLTTQSLTVETCRALGKLLHKETLLKELVLSDCMLSEEGSTLLFQGLCANTSVQH 90
Cdd:COG5238 189 CNQIGDEGIEELAEALTQNTTvTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVET 268
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  91 LDLKGNNLRATGAEALGKLLRQNKSIQSLTLEWNNLGtwEDAFATFCGGLAANSALRQLDLRNNQISHKGAEELALALKG 170
Cdd:COG5238 269 LYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIG--DEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQE 346
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 171 NTTLQQLDLRWNNIGLLGGRALVNCLPSNRTLWKLDLAGNNIPGDILRAVEQAMDHNQDRLTAFRENQARTKILSKEVQH 250
Cdd:COG5238 347 NTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNRLHTLILDGNLIGAEAQQRLEQL 426

                ....*..
gi 23271084 251 LQEEKSK 257
Cdd:COG5238 427 LERIKSV 433
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
372-665 3.87e-14

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 76.13  E-value: 3.87e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 372 LRSQVDELERKARsQQEQLFLTKQELTNTSAELKIRAIQ-AEERLDVEKRRAKQNMEDLEKLhSKEVDHMTRHLEESERA 450
Cdd:COG1196 198 LERQLEPLERQAE-KAERYRELKEELKELEAELLLLKLReLEAELEELEAELEELEAELEEL-EAELAELEAELEELRLE 275
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 451 MQERVQRLEALRLSLEEELSRmkAAVLSERGQAEEELIKARNQARLEEQHRLAHLEEKIRLLAQARDEAQGTCVQQKQMV 530
Cdd:COG1196 276 LEELELELEEAQAEEYELLAE--LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 531 AESQARVSQLNLQMEGQQRRLEELQQELINKDQEKVAEVARVRVELQEQmgrmQADLVAQEALREKVAALERQMKVIGSE 610
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL----EELEEAEEALLERLERLEEELEELEEA 429
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 23271084 611 HREALLDRESENASLREKLRLKEAEISRIRDEEAQRASFLQNAVLAYVQGSPLRA 665
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
216-405 6.24e-04

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 6.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    216 ILRAVEQAMDHNQDRLTAFRENQARTKILSKEVQHLQEEKSKQFLDLMETIDKQREEMARDSRASAVRVGQLQEALNERQ 295
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    296 SIINALKAKLQMTEAALALSEQKVRDLGELLVAGDQERQSLSQRHEKERKLERQEAADRESKLLRDlsaaneknllLRSQ 375
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEE----------LQEE 455
                          170       180       190
                   ....*....|....*....|....*....|
gi 23271084    376 VDELERKARSQQEQLFLTKQELTNTSAELK 405
Cdd:TIGR02168  456 LERLEEALEELREELEEAEQALDAAERELA 485
 
Name Accession Description Interval E-value
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
12-257 1.81e-30

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 124.52  E-value: 1.81e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  12 CEESGAEPQEAVLQQLHQLPK-GGLDLTTQSLTVETCRALGKLLHKETLLKELVLSDCMLSEEGSTLLFQGLCANTSVQH 90
Cdd:COG5238 189 CNQIGDEGIEELAEALTQNTTvTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVET 268
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  91 LDLKGNNLRATGAEALGKLLRQNKSIQSLTLEWNNLGtwEDAFATFCGGLAANSALRQLDLRNNQISHKGAEELALALKG 170
Cdd:COG5238 269 LYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIG--DEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQE 346
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 171 NTTLQQLDLRWNNIGLLGGRALVNCLPSNRTLWKLDLAGNNIPGDILRAVEQAMDHNQDRLTAFRENQARTKILSKEVQH 250
Cdd:COG5238 347 NTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNRLHTLILDGNLIGAEAQQRLEQL 426

                ....*..
gi 23271084 251 LQEEKSK 257
Cdd:COG5238 427 LERIKSV 433
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
35-229 2.60e-24

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 104.36  E-value: 2.60e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  35 LDLTTQSLTVETCRALGKLLHKETLlKELVLSDCMLSEEGSTLLFQGLCANT-SVQHLDLKGNNLRATGAEALGKLLRQN 113
Cdd:cd00116  86 LDLSDNALGPDGCGVLESLLRSSSL-QELKLNNNGLGDRGLRLLAKGLKDLPpALEKLVLGRNRLEGASCEALAKALRAN 164
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 114 KSIQSLTLEWNNLGtwEDAFATFCGGLAANSALRQLDLRNNQISHKGAEELALALKGNTTLQQLDLRWNNIGLLGGRALV 193
Cdd:cd00116 165 RDLKELNLANNGIG--DAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALA 242
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 23271084 194 NCLPS-NRTLWKLDLAGNNIPGDILRAVEQAMDHNQD 229
Cdd:cd00116 243 SALLSpNISLLTLSLSCNDITDDGAKDLAEVLAEKES 279
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
372-665 3.87e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 76.13  E-value: 3.87e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 372 LRSQVDELERKARsQQEQLFLTKQELTNTSAELKIRAIQ-AEERLDVEKRRAKQNMEDLEKLhSKEVDHMTRHLEESERA 450
Cdd:COG1196 198 LERQLEPLERQAE-KAERYRELKEELKELEAELLLLKLReLEAELEELEAELEELEAELEEL-EAELAELEAELEELRLE 275
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 451 MQERVQRLEALRLSLEEELSRmkAAVLSERGQAEEELIKARNQARLEEQHRLAHLEEKIRLLAQARDEAQGTCVQQKQMV 530
Cdd:COG1196 276 LEELELELEEAQAEEYELLAE--LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 531 AESQARVSQLNLQMEGQQRRLEELQQELINKDQEKVAEVARVRVELQEQmgrmQADLVAQEALREKVAALERQMKVIGSE 610
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL----EELEEAEEALLERLERLEEELEELEEA 429
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 23271084 611 HREALLDRESENASLREKLRLKEAEISRIRDEEAQRASFLQNAVLAYVQGSPLRA 665
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
267-608 8.46e-13

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: 72.01  E-value: 8.46e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    267 DKQREEMARDSRASAVRVGQLQEALNERQSIINALKAKLQMTEAALALSEQKVRDLGELLVAGDQERQSLSQRHEKERKl 346
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK- 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    347 ERQEAADRESKLLRDLSAANEKNLLLRSQVDELERKARSQQEQLFLTKQELTNTSAELKiraiqaeeRLDVEKRRAKQNM 426
Cdd:TIGR02168  755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT--------LLNEEAANLRERL 826
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    427 EDLEKLHSKEVDHMTRHLEESERaMQERVQRLEALRLSLEEELSRMKAAVlsergQAEEELIKARNQARLEEQHRLAHLE 506
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEE-LSEDIESLAAEIEELEELIEELESEL-----EALLNERASLEEALALLRSELEELS 900
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    507 EKIRLLAQARDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQelinkdqekvaevarvrVELQEQMGRMQAD 586
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYS-----------------LTLEEAEALENKI 963
                          330       340
                   ....*....|....*....|..
gi 23271084    587 LVAQEALREKVAALERQMKVIG 608
Cdd:TIGR02168  964 EDDEEEARRRLKRLENKIKELG 985
PTZ00121 PTZ00121
MAEBL; Provisional
215-646 3.70e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.15  E-value: 3.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   215 DILRAVEQAMDHNQDRLTAFRENQARTkilSKEVQHLQEEKSKQflDLMETIDKQREEMARDSRASAVRVGQLQEALNER 294
Cdd:PTZ00121 1253 EIRKFEEARMAHFARRQAAIKAEEARK---ADELKKAEEKKKAD--EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA 1327
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   295 QSIINALKAKLQMTEAALALSEQKVRDLGELLVAGDQERQSLSQRHEKERKleRQEAADRESKLLRDLSAANEKNLLLRS 374
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK--KADAAKKKAEEKKKADEAKKKAEEDKK 1405
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   375 QVDELERKARSQQEQLFLTKQ-ELTNTSAELKIRAIQAEERLDVEKR-RAKQNMEDLEKL--HSKEVDHMTRHLEESERA 450
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKKaEEKKKADEAKKKAEEAKKADEAKKKaEEAKKAEEAKKKaeEAKKADEAKKKAEEAKKA 1485
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   451 ------MQERVQRLEALRLSLEEELSRMKAAVLSERGQAEE----------------------------------ELIKA 490
Cdd:PTZ00121 1486 deakkkAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEakkaeeakkadeakkaeekkkadelkkaeelkkaEEKKK 1565
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   491 RNQARLEEQHRLAHLE--EKIRLLAQARDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQ---ELINKDQEK 565
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRkaEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKkveQLKKKEAEE 1645
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   566 VAEVARVRVElqEQMGRMQADLVAQEALREKVAALERQMKVIGSEHREALLDRESENASLREKLRLKEAEISR----IRD 641
Cdd:PTZ00121 1646 KKKAEELKKA--EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKkaeeLKK 1723

                  ....*
gi 23271084   642 EEAQR 646
Cdd:PTZ00121 1724 AEEEN 1728
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
248-605 3.41e-08

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: 56.67  E-value: 3.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   248 VQHLQEEKSKQFLDLMETIDKQREEMARDSRASAV-RVGQLQEALNERQSIINALKAklqmteaalalseqkvrdlgell 326
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVeRRRKLEEAEKARQAEMDRQAA----------------------- 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   327 VAGDQERQSLsqrhEKERKLER--QEAADRESKLLRDLSAANEKnlllrSQVDELERKARSQQEQLFLTKQELtntSAEL 404
Cdd:pfam17380 335 IYAEQERMAM----ERERELERirQEERKRELERIRQEEIAMEI-----SRMRELERLQMERQQKNERVRQEL---EAAR 402
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   405 KIRaIQAEERldveKRRAKQNMEDLEKLHSKEVDHMTRHLEESEramQERVQRLEALRlslEEELSRMKAAvlsERGQAE 484
Cdd:pfam17380 403 KVK-ILEEER----QRKIQQQKVEMEQIRAEQEEARQREVRRLE---EERAREMERVR---LEEQERQQQV---ERLRQQ 468
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   485 EELIKARNQARLEEQHRLAHLEEKIRLLAQARDEAQgtcvqqKQMVAESQARVSQLNLQMEGQQRRLEELQQELINKDQE 564
Cdd:pfam17380 469 EEERKRKKLELEKEKRDRKRAEEQRRKILEKELEER------KQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEER 542
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 23271084   565 KVAEVARVRVELQEQMGRMQADLVAQEALrEKVAALERQMK 605
Cdd:pfam17380 543 RKQQEMEERRRIQEQMRKATEERSRLEAM-EREREMMRQIV 582
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
244-493 3.13e-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: 3.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    244 LSKEVQHLQEEKSKQFLDLMETIDKQREEMARDSRASAVRVGQLQEALNERQSIINALKAKLQMTEAALALSEQKVRDLG 323
Cdd:TIGR02169  277 LNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT 356
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    324 ELLVAGDQERQSLSQRHEKERKlERQEAADRESKLLRDLSAAN-EKNLLLRSQVDELERKARSQQEQLFLtKQELTNTSA 402
Cdd:TIGR02169  357 EEYAELKEELEDLRAELEEVDK-EFAETRDELKDYREKLEKLKrEINELKRELDRLQEELQRLSEELADL-NAAIAGIEA 434
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    403 ---ELKIRAIQAEERLDVEKRRAKQNMEDLEKLhskevdhmtrhlEESERAMQERVQRLEALRLSLEEELSRMKAAVLSE 479
Cdd:TIGR02169  435 kinELEEEKEDKALEIKKQEWKLEQLAADLSKY------------EQELYDLKEEYDRVEKELSKLQRELAEAEAQARAS 502
                          250
                   ....*....|....*....
gi 23271084    480 R-----GQAEEELIKARNQ 493
Cdd:TIGR02169  503 EervrgGRAVEEVLKASIQ 521
LRR_8 pfam13855
Leucine rich repeat;
146-212 2.06e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 39.82  E-value: 2.06e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23271084   146 LRQLDLRNNQISHKGAEelalALKGNTTLQQLDLRWNNIGLLGGRALVnCLPSnrtLWKLDLAGNNI 212
Cdd:pfam13855   3 LRSLDLSNNRLTSLDDG----AFKGLSNLKVLDLSNNLLTTLSPGAFS-GLPS---LRYLDLSGNRL 61
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
216-405 6.24e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 6.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    216 ILRAVEQAMDHNQDRLTAFRENQARTKILSKEVQHLQEEKSKQFLDLMETIDKQREEMARDSRASAVRVGQLQEALNERQ 295
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    296 SIINALKAKLQMTEAALALSEQKVRDLGELLVAGDQERQSLSQRHEKERKLERQEAADRESKLLRDlsaaneknllLRSQ 375
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEE----------LQEE 455
                          170       180       190
                   ....*....|....*....|....*....|
gi 23271084    376 VDELERKARSQQEQLFLTKQELTNTSAELK 405
Cdd:TIGR02168  456 LERLEEALEELREELEEAEQALDAAERELA 485
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
218-487 9.72e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 9.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  218 RAVEQAMDHNQDRLTAFRENQARTKILSKEVQHLQ--EEKSKQFLDLMETIDKQREEMAR-DSRASAVRVGQLQEALNER 294
Cdd:COG4913  221 PDTFEAADALVEHFDDLERAHEALEDAREQIELLEpiRELAERYAAARERLAELEYLRAAlRLWFAQRRLELLEAELEEL 300
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  295 QSIINALKAKLQMTEAALALSEQKVRDLGELLvagdqerqslsqrhekerkleRQEAADRESKLLRDLSAANEknlllrs 374
Cdd:COG4913  301 RAELARLEAELERLEARLDALREELDELEAQI---------------------RGNGGDRLEQLEREIERLER------- 352
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  375 QVDELERKARSQQEQLFLTKQELTNTSAELKIRAIQAEERLDVEKRRAKQNMEDLEKLHSKEVDhmtrhLEESERAMQER 454
Cdd:COG4913  353 ELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD-----LRRELRELEAE 427
                        250       260       270
                 ....*....|....*....|....*....|...
gi 23271084  455 VQRLEALRLSLEEELSRMKAAVLSERGQAEEEL 487
Cdd:COG4913  428 IASLERRKSNIPARLLALRDALAEALGLDEAEL 460
 
Name Accession Description Interval E-value
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
12-257 1.81e-30

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 124.52  E-value: 1.81e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  12 CEESGAEPQEAVLQQLHQLPK-GGLDLTTQSLTVETCRALGKLLHKETLLKELVLSDCMLSEEGSTLLFQGLCANTSVQH 90
Cdd:COG5238 189 CNQIGDEGIEELAEALTQNTTvTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVET 268
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  91 LDLKGNNLRATGAEALGKLLRQNKSIQSLTLEWNNLGtwEDAFATFCGGLAANSALRQLDLRNNQISHKGAEELALALKG 170
Cdd:COG5238 269 LYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIG--DEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQE 346
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 171 NTTLQQLDLRWNNIGLLGGRALVNCLPSNRTLWKLDLAGNNIPGDILRAVEQAMDHNQDRLTAFRENQARTKILSKEVQH 250
Cdd:COG5238 347 NTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNRLHTLILDGNLIGAEAQQRLEQL 426

                ....*..
gi 23271084 251 LQEEKSK 257
Cdd:COG5238 427 LERIKSV 433
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
35-229 2.60e-24

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 104.36  E-value: 2.60e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  35 LDLTTQSLTVETCRALGKLLHKETLlKELVLSDCMLSEEGSTLLFQGLCANT-SVQHLDLKGNNLRATGAEALGKLLRQN 113
Cdd:cd00116  86 LDLSDNALGPDGCGVLESLLRSSSL-QELKLNNNGLGDRGLRLLAKGLKDLPpALEKLVLGRNRLEGASCEALAKALRAN 164
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 114 KSIQSLTLEWNNLGtwEDAFATFCGGLAANSALRQLDLRNNQISHKGAEELALALKGNTTLQQLDLRWNNIGLLGGRALV 193
Cdd:cd00116 165 RDLKELNLANNGIG--DAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALA 242
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 23271084 194 NCLPS-NRTLWKLDLAGNNIPGDILRAVEQAMDHNQD 229
Cdd:cd00116 243 SALLSpNISLLTLSLSCNDITDDGAKDLAEVLAEKES 279
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
28-185 1.09e-17

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 84.71  E-value: 1.09e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  28 HQLPKGGLDLTTQSLTVETCRALGKLLHKETLLKELVLSDCMLSEEGSTLLFQGLCANTSVQHLDLKGNNLRATGAEALG 107
Cdd:cd00116 135 LPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALA 214
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23271084 108 KLLRQNKSIQSLTLEWNNLGTWedAFATFCGGL-AANSALRQLDLRNNQISHKGAEELALALKGNTTLQQLDLRWNNIG 185
Cdd:cd00116 215 ETLASLKSLEVLNLGDNNLTDA--GAAALASALlSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFG 291
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
48-231 3.26e-16

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 80.09  E-value: 3.26e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  48 RALGKLLHKETLLKELVLSDCMLSEEGSTLlFQGLCANTSVQHLDLKGNNLRATGAEALGKLLRQNK-SIQSLTLEWNNL 126
Cdd:cd00116  71 QSLLQGLTKGCGLQELDLSDNALGPDGCGV-LESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPpALEKLVLGRNRL 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 127 gTWEDAFATfCGGLAANSALRQLDLRNNQISHKGAEELALALKGNTTLQQLDLRWNNIGLLGGRALVNCLPSNRTLWKLD 206
Cdd:cd00116 150 -EGASCEAL-AKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLN 227
                       170       180
                ....*....|....*....|....*
gi 23271084 207 LAGNNIPGDILRAVEQAMDHNQDRL 231
Cdd:cd00116 228 LGDNNLTDAGAAALASALLSPNISL 252
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
372-665 3.87e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 76.13  E-value: 3.87e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 372 LRSQVDELERKARsQQEQLFLTKQELTNTSAELKIRAIQ-AEERLDVEKRRAKQNMEDLEKLhSKEVDHMTRHLEESERA 450
Cdd:COG1196 198 LERQLEPLERQAE-KAERYRELKEELKELEAELLLLKLReLEAELEELEAELEELEAELEEL-EAELAELEAELEELRLE 275
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 451 MQERVQRLEALRLSLEEELSRmkAAVLSERGQAEEELIKARNQARLEEQHRLAHLEEKIRLLAQARDEAQGTCVQQKQMV 530
Cdd:COG1196 276 LEELELELEEAQAEEYELLAE--LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 531 AESQARVSQLNLQMEGQQRRLEELQQELINKDQEKVAEVARVRVELQEQmgrmQADLVAQEALREKVAALERQMKVIGSE 610
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL----EELEEAEEALLERLERLEEELEELEEA 429
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 23271084 611 HREALLDRESENASLREKLRLKEAEISRIRDEEAQRASFLQNAVLAYVQGSPLRA 665
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
261-616 6.00e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 75.74  E-value: 6.00e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 261 DLMETIDKQREEMARDSRAsAVRVGQLQEALNERQsiINALKAKLQMTEAALALSEQKVRDLGELLVAGDQERQSLSQRH 340
Cdd:COG1196 193 DILGELERQLEPLERQAEK-AERYRELKEELKELE--AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL 269
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 341 EKERkLERQEAADReskllrdLSAANEKNLLLRSQVDELERKARSQQEQLfltkQELTNTSAELKIRAIQAEERLDVEKR 420
Cdd:COG1196 270 EELR-LELEELELE-------LEEAQAEEYELLAELARLEQDIARLEERR----RELEERLEELEEELAELEEELEELEE 337
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 421 RAKQNMEDLEKLHSKEvdhmtRHLEESERAMQERVQRLEALRLSLEEELSRMKAAVLSERgqaeeelikarnQARLEEQH 500
Cdd:COG1196 338 ELEELEEELEEAEEEL-----EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL------------RAAAELAA 400
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 501 RLAHLEEKIRLLAQARDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQELInKDQEKVAEVARVRVELQEQM 580
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE-ALLELLAELLEEAALLEAAL 479
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 23271084 581 GRMQADLVAQEALREKVAALERQMKVIGSEHREALL 616
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
230-648 1.65e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 74.20  E-value: 1.65e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 230 RLTAFRENQARTKILSKEVQHLQEEKskqfldlmETIDKQREEMARDSRASAVRVGQLQEALNERQSIINALKAKLQMTE 309
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAEL--------EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 310 AALALSEQKVRDLGELLVAGDQERQSLSQRHEKERKlERQEAADRESKLLRDLSAANEKNLLLRSQVDELERKARSQQEQ 389
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEE-ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 390 LfltkQELTNTSAELKIRAIQAEERLDVEKRRAKQNMEDLEKLHSKEVDHMTRHLEESERAMQERVQRLEALRLSLEEEL 469
Cdd:COG1196 381 L----EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 470 SRMKAAVLSERGQAEEELIKARNQARLEEQHRLAhLEEKIRLLAQARDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQR 549
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAA-ARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAA 535
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 550 RLEELQQELINKDQEKVAEVARVRVEL-----QEQMGRMQADLVAQEALREKVAALERQMKVIGSEHREALLDRESENAS 624
Cdd:COG1196 536 YEAALEAALAAALQNIVVEDDEVAAAAieylkAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARY 615
                       410       420
                ....*....|....*....|....
gi 23271084 625 LREKLRLKEAEISRIRDEEAQRAS 648
Cdd:COG1196 616 YVLGDTLLGRTLVAARLEAALRRA 639
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
267-608 8.46e-13

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: 72.01  E-value: 8.46e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    267 DKQREEMARDSRASAVRVGQLQEALNERQSIINALKAKLQMTEAALALSEQKVRDLGELLVAGDQERQSLSQRHEKERKl 346
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK- 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    347 ERQEAADRESKLLRDLSAANEKNLLLRSQVDELERKARSQQEQLFLTKQELTNTSAELKiraiqaeeRLDVEKRRAKQNM 426
Cdd:TIGR02168  755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT--------LLNEEAANLRERL 826
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    427 EDLEKLHSKEVDHMTRHLEESERaMQERVQRLEALRLSLEEELSRMKAAVlsergQAEEELIKARNQARLEEQHRLAHLE 506
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEE-LSEDIESLAAEIEELEELIEELESEL-----EALLNERASLEEALALLRSELEELS 900
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    507 EKIRLLAQARDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQelinkdqekvaevarvrVELQEQMGRMQAD 586
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYS-----------------LTLEEAEALENKI 963
                          330       340
                   ....*....|....*....|..
gi 23271084    587 LVAQEALREKVAALERQMKVIG 608
Cdd:TIGR02168  964 EDDEEEARRRLKRLENKIKELG 985
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
230-563 2.62e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 63.92  E-value: 2.62e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    230 RLTAFRENQARTKILSKEVQ------HLQEEKSKQFLDLMETI-DKQREEMARDSRASAVRVGQLQEALNERQSIINALK 302
Cdd:TIGR02168  180 KLERTRENLDRLEDILNELErqlkslERQAEKAERYKELKAELrELELALLVLRLEELREELEELQEELKEAEEELEELT 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    303 AKLQMTEAALALSEQKVRDLGELLVAGDQERQSLSQR-HEKERKLERQEAadRESKLLRDLSAANEKNLLLRSQVDELER 381
Cdd:TIGR02168  260 AELQELEEKLEELRLEVSELEEEIEELQKELYALANEiSRLEQQKQILRE--RLANLERQLEELEAQLEELESKLDELAE 337
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    382 KARSQQEQLFLTKQELTNTSAELKIRAIQAEERldveKRRAKQNMEDLEKLHSKEVDHmtRHLEESERA----MQERVQR 457
Cdd:TIGR02168  338 ELAELEEKLEELKEELESLEAELEELEAELEEL----ESRLEELEEQLETLRSKVAQL--ELQIASLNNeierLEARLER 411
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    458 LEALRLSLEEELSRMKAAVLSERGQAEEELIKARNQARLEEQHRLAHLEEKIRLLAQARDEAQGTCVQQKQMVAESQARV 537
Cdd:TIGR02168  412 LEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
                          330       340
                   ....*....|....*....|....*.
gi 23271084    538 SQLNLQMEGQQRRLEELQQELINKDQ 563
Cdd:TIGR02168  492 DSLERLQENLEGFSEGVKALLKNQSG 517
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
338-651 1.18e-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: 61.61  E-value: 1.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    338 QRHEKERKLER-QEAADRESKLLRDlsaaneknllLRSQVDELERKARSQQEQLFLtKQELTNTSAEL-KIRAIQAEERL 415
Cdd:TIGR02168  173 RRKETERKLERtRENLDRLEDILNE----------LERQLKSLERQAEKAERYKEL-KAELRELELALlVLRLEELREEL 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    416 DvEKRRAKQNMEDLEKLHSKEVDHMTRHLEESERAMQERVQRLEALR---LSLEEELSRMKA--AVLSERGQAEEELIKA 490
Cdd:TIGR02168  242 E-ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQkelYALANEISRLEQqkQILRERLANLERQLEE 320
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    491 RNQARLEEQHRLAHLEEKIRLLAQARDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQELINKDQEKVAEVA 570
Cdd:TIGR02168  321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    571 RVRV------ELQEQMGRMQADLVAQEALREKVAALERQMKVigSEHREALLDRESENASLREKLRLKEAEISRIRDEEA 644
Cdd:TIGR02168  401 EIERlearleRLEDRRERLQQEIEELLKKLEEAELKELQAEL--EELEEELEELQEELERLEEALEELREELEEAEQALD 478

                   ....*..
gi 23271084    645 QRASFLQ 651
Cdd:TIGR02168  479 AAERELA 485
PTZ00121 PTZ00121
MAEBL; Provisional
215-646 3.70e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.15  E-value: 3.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   215 DILRAVEQAMDHNQDRLTAFRENQARTkilSKEVQHLQEEKSKQflDLMETIDKQREEMARDSRASAVRVGQLQEALNER 294
Cdd:PTZ00121 1253 EIRKFEEARMAHFARRQAAIKAEEARK---ADELKKAEEKKKAD--EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA 1327
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   295 QSIINALKAKLQMTEAALALSEQKVRDLGELLVAGDQERQSLSQRHEKERKleRQEAADRESKLLRDLSAANEKNLLLRS 374
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK--KADAAKKKAEEKKKADEAKKKAEEDKK 1405
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   375 QVDELERKARSQQEQLFLTKQ-ELTNTSAELKIRAIQAEERLDVEKR-RAKQNMEDLEKL--HSKEVDHMTRHLEESERA 450
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKKaEEKKKADEAKKKAEEAKKADEAKKKaEEAKKAEEAKKKaeEAKKADEAKKKAEEAKKA 1485
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   451 ------MQERVQRLEALRLSLEEELSRMKAAVLSERGQAEE----------------------------------ELIKA 490
Cdd:PTZ00121 1486 deakkkAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEakkaeeakkadeakkaeekkkadelkkaeelkkaEEKKK 1565
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   491 RNQARLEEQHRLAHLE--EKIRLLAQARDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQ---ELINKDQEK 565
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRkaEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKkveQLKKKEAEE 1645
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   566 VAEVARVRVElqEQMGRMQADLVAQEALREKVAALERQMKVIGSEHREALLDRESENASLREKLRLKEAEISR----IRD 641
Cdd:PTZ00121 1646 KKKAEELKKA--EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKkaeeLKK 1723

                  ....*
gi 23271084   642 EEAQR 646
Cdd:PTZ00121 1724 AEEEN 1728
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
217-608 5.38e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.57  E-value: 5.38e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 217 LRAVEQAMDHNQDRLTAFRENQARTKILSKEVQHLQEEKSKQFLDLMETIDKQREEMAR---DSRASAVRVGQLQEALNE 293
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEleeALAELEEEEEEEEEALEE 446
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 294 RQSIINALKAKLQMTEAALALSEQKVRDLGELLVAGDQERQSLSQRHEKERKLERQEAADRESKLLRDLSAANEKNLLL- 372
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAv 526
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 373 --------RSQVDELERKARSQQEQLFLTKQELTNTSAELKIRAIQAEERLDVEKRRAKQNMEDLEKLHSKEVDHMTRHL 444
Cdd:COG1196 527 avligveaAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVAS 606
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 445 EESERAMQERVQRLEALRLSLEEELSRMKAAVLSERGQAEEELIKAR---NQARLEEQHRLAHLEEKIRLLAQARDEAQG 521
Cdd:COG1196 607 DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGeggSAGGSLTGGSRRELLAALLEAEAELEELAE 686
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 522 TCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQELINKDQEKVAEVARVRVELQEQMGRMQADLVAQ-------EALR 594
Cdd:COG1196 687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEElpeppdlEELE 766
                       410
                ....*....|....
gi 23271084 595 EKVAALERQMKVIG 608
Cdd:COG1196 767 RELERLEREIEALG 780
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
88-228 3.07e-08

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 55.82  E-value: 3.07e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  88 VQHLDLKGNNLRATGAEALGKLLRQNKSIQSLTLEWNNLGTWEDAFATFCGGLAANSALRQLDLRNNQISHKGAEELALA 167
Cdd:cd00116  25 LQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRIPRGLQSLLQGLTKGCGLQELDLSDNALGPDGCGVLESL 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 168 LKgNTTLQQLDLRWNNIGLLGGR-----------------------------ALVNCLPSNRTLWKLDLAGNNIPGDILR 218
Cdd:cd00116 105 LR-SSSLQELKLNNNGLGDRGLRllakglkdlppaleklvlgrnrlegasceALAKALRANRDLKELNLANNGIGDAGIR 183
                       170
                ....*....|
gi 23271084 219 AVEQAMDHNQ 228
Cdd:cd00116 184 ALAEGLKANC 193
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
248-605 3.41e-08

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: 56.67  E-value: 3.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   248 VQHLQEEKSKQFLDLMETIDKQREEMARDSRASAV-RVGQLQEALNERQSIINALKAklqmteaalalseqkvrdlgell 326
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVeRRRKLEEAEKARQAEMDRQAA----------------------- 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   327 VAGDQERQSLsqrhEKERKLER--QEAADRESKLLRDLSAANEKnlllrSQVDELERKARSQQEQLFLTKQELtntSAEL 404
Cdd:pfam17380 335 IYAEQERMAM----ERERELERirQEERKRELERIRQEEIAMEI-----SRMRELERLQMERQQKNERVRQEL---EAAR 402
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   405 KIRaIQAEERldveKRRAKQNMEDLEKLHSKEVDHMTRHLEESEramQERVQRLEALRlslEEELSRMKAAvlsERGQAE 484
Cdd:pfam17380 403 KVK-ILEEER----QRKIQQQKVEMEQIRAEQEEARQREVRRLE---EERAREMERVR---LEEQERQQQV---ERLRQQ 468
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   485 EELIKARNQARLEEQHRLAHLEEKIRLLAQARDEAQgtcvqqKQMVAESQARVSQLNLQMEGQQRRLEELQQELINKDQE 564
Cdd:pfam17380 469 EEERKRKKLELEKEKRDRKRAEEQRRKILEKELEER------KQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEER 542
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 23271084   565 KVAEVARVRVELQEQMGRMQADLVAQEALrEKVAALERQMK 605
Cdd:pfam17380 543 RKQQEMEERRRIQEQMRKATEERSRLEAM-EREREMMRQIV 582
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
229-645 3.93e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 56.59  E-value: 3.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  229 DRLTAFRENQARTKILSKEVQHLQEEKSKQFLDLMETIDKQREEMARDSR---ASAVRVGQLQEALNERQSIINALKAKL 305
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETERereELAEEVRDLRERLEELEEERDDLLAEA 302
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  306 QMTEAALALSEQKVRDLG----ELLVAGDQERQSLsQRHEKERKLERQEAADRESKLLRDLSAANEknllLRSQVDELER 381
Cdd:PRK02224 303 GLDDADAEAVEARREELEdrdeELRDRLEECRVAA-QAHNEEAESLREDADDLEERAEELREEAAE----LESELEEARE 377
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  382 KARSQQEQLfltkQELTNTSAELKIRAIQAEERLDVEKRRAKQNMEDLEKLHSKEVDhmtrhLEESERAMQERVQRLEAL 461
Cdd:PRK02224 378 AVEDRREEI----EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAE-----LEATLRTARERVEEAEAL 448
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  462 R-----------------LSLEEELSRMKAAVLSERGQAEEELikARNQARLEEQHRLAHLEEKIRLLAQARDEAQGTCV 524
Cdd:PRK02224 449 LeagkcpecgqpvegsphVETIEEDRERVEELEAELEDLEEEV--EEVEERLERAEDLVEAEDRIERLEERREDLEELIA 526
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  525 QQKQMVAESQARVSQLNLQMEGQQRRLEElQQELINKDQEKVAEVARVRVELQEQMGRMQADLVAQEALREKVAALERQM 604
Cdd:PRK02224 527 ERRETIEEKRERAEELRERAAELEAEAEE-KREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAE 605
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 23271084  605 KVIGS--EHREALLDRESEN----ASLREKLRLKEAEISRIRDEEAQ 645
Cdd:PRK02224 606 DEIERlrEKREALAELNDERrerlAEKRERKRELEAEFDEARIEEAR 652
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
439-646 3.94e-08

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: 56.67  E-value: 3.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   439 HMTRHLEE-SERAMQERVQRLEALRLSLEEElsrMKAAVLSERGQAEEElikarnqarleEQHRLAHLEEKIRLLAQard 517
Cdd:pfam17380 276 HIVQHQKAvSERQQQEKFEKMEQERLRQEKE---EKAREVERRRKLEEA-----------EKARQAEMDRQAAIYAE--- 338
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   518 eaqgtcvqQKQMVAESQARVSQLnlQMEGQQRRLEELQQELINKDQEKVAEVARVRVELQEQMGRMQADLVAqeALREKV 597
Cdd:pfam17380 339 --------QERMAMERERELERI--RQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEA--ARKVKI 406
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 23271084   598 AALERQMKVIGSEHREALLDRESENASLREKLRLKEA---EISRIRDEEAQR 646
Cdd:pfam17380 407 LEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEErarEMERVRLEEQER 458
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
437-640 5.19e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.46  E-value: 5.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  437 VDHMtRHLEESERAMQERVQRLEALRlSLEEELSRMKAAVlsergQAEEELIKARNQARLEE-QHRLAHLEEKIRLLAQA 515
Cdd:COG4913  231 VEHF-DDLERAHEALEDAREQIELLE-PIRELAERYAAAR-----ERLAELEYLRAALRLWFaQRRLELLEAELEELRAE 303
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  516 RDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQ-RRLEELQQELINKDQEKvAEVARVRVELQEQMGRMQADLVAQE--- 591
Cdd:COG4913  304 LARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLEREL-EERERRRARLEALLAALGLPLPASAeef 382
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 23271084  592 -ALREKVAALERQMKVIGSEHREALLDRESENASLREKLRLKEAEISRIR 640
Cdd:COG4913  383 aALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
84-227 8.36e-08

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 55.18  E-value: 8.36e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  84 ANTSVQHLDLKGNNLRATGAEALGKLLRQNKSIQSLTLEWNNLGTwedaFATFCGGLAANSALRQLDLRNNQISHKGAEE 163
Cdd:COG5238 124 AKTLEDSLILYLALPRRINLIQVLKDPLGGNAVHLLGLAARLGLL----AAISMAKALQNNSVETVYLGCNQIGDEGIEE 199
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23271084 164 LALALKGNTTLQQLDLRWNNIGLLGGRALVNCLPSNRTLWKLDLAGNNIPGDILRAVEQAMDHN 227
Cdd:COG5238 200 LAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNN 263
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
35-212 1.56e-07

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 54.17  E-value: 1.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  35 LDLTTQSLTVETCRALGKLLHKETLLKELVLSDCmlseegstllfQGLCANTSVQHLDLKGNNLratgaEALGKLLRQNK 114
Cdd:COG4886  73 LLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGN-----------EELSNLTNLESLDLSGNQL-----TDLPEELANLT 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 115 SIQSLTLEWNNLgtwedafATFCGGLAANSALRQLDLRNNQIShkgaeELALALKGNTTLQQLDLRWNNIGLLGgralvN 194
Cdd:COG4886 137 NLKELDLSNNQL-------TDLPEPLGNLTNLKSLDLSNNQLT-----DLPEELGNLTNLKELDLSNNQITDLP-----E 199
                       170
                ....*....|....*...
gi 23271084 195 CLPSNRTLWKLDLAGNNI 212
Cdd:COG4886 200 PLGNLTNLEELDLSGNQL 217
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
219-630 1.97e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 54.28  E-value: 1.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  219 AVEQAMDHNQDRLTAFREN--QARTKILSKEVQhlQEEKSKQFLDLMETIDKQREEMAR-DSRASAVRvgqlqEALNERQ 295
Cdd:PRK02224 311 AVEARREELEDRDEELRDRleECRVAAQAHNEE--AESLREDADDLEERAEELREEAAElESELEEAR-----EAVEDRR 383
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  296 SIINALKAKLQMTEAALALSEQKVRDLGELLVAGDQERQSLSQRhEKERKLERQEAADRESKLLRDLSAAN----EKNLL 371
Cdd:PRK02224 384 EEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRER-EAELEATLRTARERVEEAEALLEAGKcpecGQPVE 462
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  372 LRSQVDELERKaRSQQEQLFLTKQELTNTSAELKIRAIQAEERLDVEKR--RAKQNMEDLEKLHSkevDHMTRHLEESER 449
Cdd:PRK02224 463 GSPHVETIEED-RERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRieRLEERREDLEELIA---ERRETIEEKRER 538
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  450 A--MQERVQRLEAlrlslEEELSRMKAAVLSERGQAEEELIKARNQARLE---EQHRLAHLEEKIRLLAQARDEAQGTCV 524
Cdd:PRK02224 539 AeeLRERAAELEA-----EAEEKREAAAEAEEEAEEAREEVAELNSKLAElkeRIESLERIRTLLAAIADAEDEIERLRE 613
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  525 QQKQM----------VAESQARVSQLNLQMEGQqrRLEELQQELINKDQ------EKVAEVARVRVELQEQMGRMQADLV 588
Cdd:PRK02224 614 KREALaelnderrerLAEKRERKRELEAEFDEA--RIEEAREDKERAEEyleqveEKLDELREERDDLQAEIGAVENELE 691
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 23271084  589 AQEALREKVAALERQMKVIGSEHREAlLDRESENASLREKLR 630
Cdd:PRK02224 692 ELEELRERREALENRVEALEALYDEA-EELESMYGDLRAELR 732
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
347-643 3.59e-07

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: 53.53  E-value: 3.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    347 ERQEAADRESKLLRDLSAANEKNLLLRSQVDELERKARSQQEQLfltkqeltntsAELKIRAIQAEERLDVEKRRAKQNM 426
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKI-----------GEIEKEIEQLEQEEEKLKERLEELE 743
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    427 EDLEKLhskevdhmTRHLEESERAMQERVQRLEALRL---SLEEELSRMKAAVLSERGQAEEELIKARNQARLEEQHRLA 503
Cdd:TIGR02169  744 EDLSSL--------EQEIENVKSELKELEARIEELEEdlhKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLR 815
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    504 HLEEKIRLLAQARDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQELINKdQEKVAEVARVRVELQEQMGRM 583
Cdd:TIGR02169  816 EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEL-EAALRDLESRLGDLKKERDEL 894
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    584 QADLVAQEALREKVAALERQMKVIGSEHREALLDRESENASLREKLRLKEAEISRIRDEE 643
Cdd:TIGR02169  895 EAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLE 954
PTZ00121 PTZ00121
MAEBL; Provisional
236-596 4.38e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.61  E-value: 4.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   236 ENQARTKILSKEVQHLQEEKSKQfldlmETIDKQREEMARDSRASAvrvgQLQEALNERQSIINALKAKLQMTEAALALS 315
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKKAEEAKKA-----EEAKKKAEEAKKADEAKK----KAEEAKKADEAKKKAEEAKKKADEAKKAAE 1507
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   316 EQKVRDlgELLVAGDQERQSLSQRHEKERKLERQEAADrESKLLRDLSAANEknLLLRSQVDELERKARSQQEQ-LFLTK 394
Cdd:PTZ00121 1508 AKKKAD--EAKKAEEAKKADEAKKAEEAKKADEAKKAE-EKKKADELKKAEE--LKKAEEKKKAEEAKKAEEDKnMALRK 1582
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   395 QELTNTSAELKIRAIQAEERLDVEKRRAKQNMEDLEKLHSKEV---DHMTRHLEESERAMQERVQRLEALRLslEEELSR 471
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELkkaEEEKKKVEQLKKKEAEEKKKAEELKK--AEEENK 1660
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   472 MKAAVLSERGQAE----EELIKARNQARLEEQHRLAHLEE--KIRLLAQARDEAQGTCVQQKQMVAESQARVSQLNLQME 545
Cdd:PTZ00121 1661 IKAAEEAKKAEEDkkkaEEAKKAEEDEKKAAEALKKEAEEakKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE 1740
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 23271084   546 GQQRRLEELQQEliNKDQEKVAEVARVRVELQEQMgRMQADLVAQEALREK 596
Cdd:PTZ00121 1741 EDKKKAEEAKKD--EEEKKKIAHLKKEEEKKAEEI-RKEKEAVIEEELDEE 1788
PTZ00121 PTZ00121
MAEBL; Provisional
236-653 7.36e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.84  E-value: 7.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   236 ENQARTKILSKEVQHLQEEKSKQFLDLMETIDKQREEMARDS----RASAVRVGQLQEALNERQSIINALKAKlQMTEAA 311
Cdd:PTZ00121 1101 EEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAeearKAEDAKRVEIARKAEDARKAEEARKAE-DAKKAE 1179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   312 LALSEQKVRDLGELLVAGDQERQSLSQRHEKERKLERQEAADRESKlLRDLSAANEknllLRSQVDELERKARSQQEQLF 391
Cdd:PTZ00121 1180 AARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKK-AEAVKKAEE----AKKDAEEAKKAEEERNNEEI 1254
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   392 LTKQELTNTSAELKIRAIQAEERL---DVEKRRAKQNMEDLEKLHS-KEVDHMTRHLEESERA------MQERVQRLEAL 461
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKAEEARkadELKKAEEKKKADEAKKAEEkKKADEAKKKAEEAKKAdeakkkAEEAKKKADAA 1334
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   462 RLSLEE-----ELSRMKAAVLSERGQAEEELIKARNQARLEEQHRLAHLEEKIRLLAQArDEAQGTCVQQKQMvAESQAR 536
Cdd:PTZ00121 1335 KKKAEEakkaaEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA-DEAKKKAEEDKKK-ADELKK 1412
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   537 VSQLNLQMEGQQRRLEELQQElinKDQEKVAEVARVRVELQEQMGRMQADLVAQEALREKVAALERQMKVIGSEHREALL 616
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEKKKA---DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAK 1489
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 23271084   617 DRESENASLREKLRLKEAEISRIRD----EEAQRASFLQNA 653
Cdd:PTZ00121 1490 KKAEEAKKKADEAKKAAEAKKKADEakkaEEAKKADEAKKA 1530
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
396-642 7.49e-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: 52.75  E-value: 7.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    396 ELTNTSAELKIRAIQAEERLDvEKRRAKQNMEDLEKLHSKEVDHMTRHLeeseRAMQERVQRLEALRLSLEEELSRMKAA 475
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALA-ELRKELEELEEELEQLRKELEELSRQI----SALRKDLARLEAEVEQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    476 VLSERGQAEEELikarnQARLEEQHRLAHLEEKIRLLAQARDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQ 555
Cdd:TIGR02168  756 LTELEAEIEELE-----ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    556 QElinkdqekVAEVARVRVELQEQMGRMQADLV----AQEALREKVAALERQMKVIG---SEHREALLDRESENASLREK 628
Cdd:TIGR02168  831 RR--------IAATERRLEDLEEQIEELSEDIEslaaEIEELEELIEELESELEALLnerASLEEALALLRSELEELSEE 902
                          250
                   ....*....|....
gi 23271084    629 LRLKEAEISRIRDE 642
Cdd:TIGR02168  903 LRELESKRSELRRE 916
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
286-648 1.40e-06

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 51.89  E-value: 1.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    286 QLQEALNERQSIINALKAKLQMTEAALALSEQKVRDLGELLVAGDQERQSLSQRHEKERKLERQEAADRESKLLRDLSAA 365
Cdd:TIGR00618  212 CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARK 291
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    366 NEKNLLLRSQVDELERKARSQQEQLFLTKQELtnTSAELKIRAIQAEERLDVEKRRAKQNMEDLEKLHSKEVDHMTRHLE 445
Cdd:TIGR00618  292 AAPLAAHIKAVTQIEQQAQRIHTELQSKMRSR--AKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIRE 369
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    446 ESERAMQERvQRLEALRLSLEEELSRMKAAV-LSERGQAEEELIKARNQARLEEQHRLAHL--EEKIRLLAQARDEAQGT 522
Cdd:TIGR00618  370 ISCQQHTLT-QHIHTLQQQKTTLTQKLQSLCkELDILQREQATIDTRTSAFRDLQGQLAHAkkQQELQQRYAELCAAAIT 448
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    523 CVQQKQMVAESQARVSQLNLQMEGQQrrlEELQQELINKDQEKVAEVARVRVELQEQMGRMQADLVAQEALREKVAALE- 601
Cdd:TIGR00618  449 CTAQCEKLEKIHLQESAQSLKEREQQ---LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGp 525
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 23271084    602 RQMKVIGSEHREALLDRESENA-----SLREKLRLKEAEISRIRDEEAQRAS 648
Cdd:TIGR00618  526 LTRRMQRGEQTYAQLETSEEDVyhqltSERKQRASLKEQMQEIQQSFSILTQ 577
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
374-645 1.76e-06

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: 51.61  E-value: 1.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    374 SQVDELERKARSQQEQLFLTKQELTNTSAELKIRAIQ----AEERLDVEK----RRAKQNMEDLEKLHSK---------- 435
Cdd:TIGR02169  163 AGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQlerlRREREKAERyqalLKEKREYEGYELLKEKealerqkeai 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    436 --EVDHMTRHLEESERAMQERVQRLEALRLSLEEELSRMKAAVLSERGQAEEELikarnqarLEEQHRLAHLEEKIRLLA 513
Cdd:TIGR02169  243 erQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKI--------GELEAEIASLERSIAEKE 314
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    514 QARDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQELinkdQEKVAEVARVRVELQEQMGRMQADLVAQEAL 593
Cdd:TIGR02169  315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEY----AELKEELEDLRAELEEVDKEFAETRDELKDY 390
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 23271084    594 REKVAALERQMkvigSEHREALLDRESENASLREKLRLKEAEISRIRDEEAQ 645
Cdd:TIGR02169  391 REKLEKLKREI----NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE 438
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
331-567 2.09e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 50.53  E-value: 2.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 331 QERQSLSQRHEKERKlERQEAADRESKLLRDLSAANEKNLLLRSQVDELERKARSQQEQLFLTKQELTNTSAELKIRAIQ 410
Cdd:COG4942  27 AELEQLQQEIAELEK-ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 411 AEERLDVEKRRAKQNMEDLeKLHSKEVDHMTRHLEESERAMQERVQRLEALRLSLEEelsrmkaavlsergqaEEELIKA 490
Cdd:COG4942 106 LAELLRALYRLGRQPPLAL-LLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE----------------LAALRAE 168
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23271084 491 RNQARLEEQHRLAHLEEKIRLLAQARDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQELINKDQEKVA 567
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
324-645 2.99e-06

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 50.89  E-value: 2.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    324 ELLVAGDQERQS--LSQRHEKERKLE--RQEAADRESKLLRDLSAANEKNLLLRSQVDELER----KARSQQEQLFLTKQ 395
Cdd:pfam15921  277 EVEITGLTEKASsaRSQANSIQSQLEiiQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRmyedKIEELEKQLVLANS 356
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    396 ELTNTSAE-----------------LKIRAIQAEERLDVEKRRAKQnMEDLEKLHSKEVDHMTRHLEesERAMQerVQRL 458
Cdd:pfam15921  357 ELTEARTErdqfsqesgnlddqlqkLLADLHKREKELSLEKEQNKR-LWDRDTGNSITIDHLRRELD--DRNME--VQRL 431
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    459 EALRLSLEEELsrmkaavlseRGQAEEEL--IKARNQARLEEQHRLAHLEEKIRLLAQARDEaqgtcVQQKQMVAESQAR 536
Cdd:pfam15921  432 EALLKAMKSEC----------QGQMERQMaaIQGKNESLEKVSSLTAQLESTKEMLRKVVEE-----LTAKKMTLESSER 496
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    537 -VSQLNLQMEGQQRRLEELQQE---LINKDQEKVAEVARVRVElQEQMGRMQAD---LVAQEALREKVAALERQ-----M 604
Cdd:pfam15921  497 tVSDLTASLQEKERAIEATNAEitkLRSRVDLKLQELQHLKNE-GDHLRNVQTEceaLKLQMAEKDKVIEILRQqienmT 575
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 23271084    605 KVIGSEHR--------EALLDRE--SENASLREKLRLKEAEISRIRDEEAQ 645
Cdd:pfam15921  576 QLVGQHGRtagamqveKAQLEKEinDRRLELQEFKILKDKKDAKIRELEAR 626
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
235-605 3.75e-06

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: 50.45  E-value: 3.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    235 RENQARTKILSKEVQHLQEEKSKQFLDLMETIDKQREEMARDSRASAvRVGQLQEALNERQSIINALKAKLQMTEAALAL 314
Cdd:TIGR02169  677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEK-EIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    315 SEQKVRDLGELLvagDQERQSLSQRHEKERKLERQEAADRESKLLRDLSAANEKNLLLRSQVDELERKARSQQeqlfLTK 394
Cdd:TIGR02169  756 VKSELKELEARI---EELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT----LEK 828
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    395 QELTNTSAELKIRAIQAEERLDVEKRRAKQNMEDLEKLHSKEVDHmtrhlEESERAMQERVQRLEALRLSLEEELSRMKa 474
Cdd:TIGR02169  829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEL-----EAALRDLESRLGDLKKERDELEAQLRELE- 902
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    475 avlSERGQAEEELIKARnqarleeqHRLAHLEEKIRLLAQARDEAqGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEEL 554
Cdd:TIGR02169  903 ---RKIEELEAQIEKKR--------KRLSELKAKLEALEEELSEI-EDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 23271084    555 qQELINKDQEKVAEVARVRVELQEQMGRMQADlvaQEALREKVAALERQMK 605
Cdd:TIGR02169  971 -EPVNMLAIQEYEEVLKRLDELKEKRAKLEEE---RKAILERIEEYEKKKR 1017
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
343-605 4.89e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.06  E-value: 4.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    343 ERKLERQEAADRESKLLRDLSAANEKNLLLRSQVDELERKARSQQEQLFLTKQELTNTSAELKiRAIQAEERLdvEKRRA 422
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA-RLEAEVEQL--EERIA 750
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    423 KQNMEDLEKLHSKEVDHMTRHLEESERAmqervqRLEALRLSLEEELSRMKaavlSERGQAEEELIKARNQARLEEQhRL 502
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERLEEAEEELA------EAEAEIEELEAQIEQLK----EELKALREALDELRAELTLLNE-EA 819
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    503 AHLEEKIRLLAQARDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQELINKDQEKvAEVARVRVELQEQMGR 582
Cdd:TIGR02168  820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER-ASLEEALALLRSELEE 898
                          250       260
                   ....*....|....*....|...
gi 23271084    583 MQADLvaqEALREKVAALERQMK 605
Cdd:TIGR02168  899 LSEEL---RELESKRSELRRELE 918
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
409-646 9.01e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.91  E-value: 9.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  409 IQAEErlDVEKRRAKQNMEDLEKLHS-KEVDHMTRHLEESERAMQERVQRLEALRLSLEEelSRMKAAVLSERGQAEEEL 487
Cdd:PRK03918 185 IKRTE--NIEELIKEKEKELEEVLREiNEISSELPELREELEKLEKEVKELEELKEEIEE--LEKELESLEGSKRKLEEK 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  488 IKARNQARLEEQHRLAHLEEKIRLLAQARDEAQ------GTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELqqeliNK 561
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELKELKEKAEeyiklsEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL-----EE 335
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  562 DQEKVAEVARVRVELQEQMGRMQADLVAQEALREKVAALERQMKVIGSEHREAlLDRESENAS-----LREKLRLKEAEI 636
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEK-LEKELEELEkakeeIEEEISKITARI 414
                        250
                 ....*....|
gi 23271084  637 SRIRDEEAQR 646
Cdd:PRK03918 415 GELKKEIKEL 424
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
351-592 9.75e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.22  E-value: 9.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 351 AADRESKLLRDLSAANEKNLLLRSQVDELERKARSQQEQLFLTKQELTNTSAELKiraiQAEERLDVEKRRAKQNMEDLE 430
Cdd:COG4942  18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIR----ALEQELAALEAELAELEKEIA 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 431 KLHsKEVDHMTRHLEESERAMQERVQRLEALRLsleeeLSRMKAAVLSERGQAEEELIKARNQARLEEQHRLAHLEEKIR 510
Cdd:COG4942  94 ELR-AELEAQKEELAELLRALYRLGRQPPLALL-----LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 511 LLAQARDeaqgtcvQQKQMVAESQARVSQLNLQMEGQQRRLEELQQElINKDQEKVAEVARVRVELQEQMGRMQADLVAQ 590
Cdd:COG4942 168 ELEAERA-------ELEALLAELEEERAALEALKAERQKLLARLEKE-LAELAAELAELQQEAEELEALIARLEAEAAAA 239

                ..
gi 23271084 591 EA 592
Cdd:COG4942 240 AE 241
PLN02939 PLN02939
transferase, transferring glycosyl groups
225-536 1.10e-05

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 48.74  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  225 DHNQDRLTAFRENQARTKILSKEVQHLQEEKSKQFLDLMETIDKQREEMARDSRASAVRVGQLQEALNERQSI---INAL 301
Cdd:PLN02939  96 DHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALqgkINIL 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  302 KAKLQMTEAALALSEQKVRDLGELLVAGDQERQSLSQRHEKERKLerqeaadrESKLLRDLSAANEKNLLLRSQVDELER 381
Cdd:PLN02939 176 EMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLC--------VHSLSKELDVLKEENMLLKDDIQFLKA 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  382 K---ARSQQEQLFLTKQE---LTNTSAELKIRAIQAEErlDVEKRRAKQ---------NMEDLEKLHSKEVDHMTRHLEE 446
Cdd:PLN02939 248 ElieVAETEERVFKLEKErslLDASLRELESKFIVAQE--DVSKLSPLQydcwwekveNLQDLLDRATNQVEKAALVLDQ 325
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  447 SeRAMQERVQRLEAlrlSLEE----ELSRMKAAVLSERGQAEEElikaRNQARLEEQHrlahleEKIRLLAQARDEAQGT 522
Cdd:PLN02939 326 N-QDLRDKVDKLEA---SLKEanvsKFSSYKVELLQQKLKLLEE----RLQASDHEIH------SYIQLYQESIKEFQDT 391
                        330
                 ....*....|....
gi 23271084  523 CvqqKQMVAESQAR 536
Cdd:PLN02939 392 L---SKLKEESKKR 402
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
302-497 1.32e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.76  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  302 KAKLQMTEAALALSEQKVRDLGELLVAGDQERQSLSQRHEKERKLERQEAADRESK-LLRDLSAANEKNLLLRSQVDELE 380
Cdd:COG4913  609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAsAEREIAELEAELERLDASSDDLA 688
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  381 RkARSQQEQLFLTKQELTNTSAELKIRAIQAEERLDVEKRRAKQNMEDLEKLHSKEVDHMTRHLEE-SERAMQERVQRle 459
Cdd:COG4913  689 A-LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEErFAAALGDAVER-- 765
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 23271084  460 ALRLSLEEELSRMKAavlsERGQAEEELIKARNQARLE 497
Cdd:COG4913  766 ELRENLEERIDALRA----RLNRAEEELERAMRAFNRE 799
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
444-656 1.35e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.51  E-value: 1.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    444 LEESERAMQERVQRLEALRLSLEEELSRMKAAVLSERGQ---AEEELIKARNQARLEEQ------HRLAHLEEKIRLLAQ 514
Cdd:TIGR02168  689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQisaLRKDLARLEAEVEQLEEriaqlsKELTELEAEIEELEE 768
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    515 ARDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQqelinkdqekvAEVARVRVELQEQMGRMqadlvaqEALR 594
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR-----------AELTLLNEEAANLRERL-------ESLE 830
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23271084    595 EKVAALERQMKVIGSEHREALLDRESENASLREKLRLKEAEISRIRDEEAQRASFLQNAVLA 656
Cdd:TIGR02168  831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL 892
PTZ00121 PTZ00121
MAEBL; Provisional
215-647 1.42e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   215 DILRAVEQAMDHNQDRLTAFRENQARTKIlsKEVQHLQEEKSKQFLDLMETIDKQREEMardSRASAVRVGQlqealnER 294
Cdd:PTZ00121 1186 EVRKAEELRKAEDARKAEAARKAEEERKA--EEARKAEDAKKAEAVKKAEEAKKDAEEA---KKAEEERNNE------EI 1254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   295 QSIINALKAKLQMTEAALALSEQKVRDlgELLVAGDQERQSLSQRHEKERKLERQEAADRESKLLRDLSAANEKNlllRS 374
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKAEEARKAD--ELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA---KK 1329
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   375 QVDELERKARSQQEQLFLTKQELTNTSAELKI---RAIQAEERLDVEKRRA---KQNMEDLEKLHS--KEVDHMTRHLEE 446
Cdd:PTZ00121 1330 KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAaeeKAEAAEKKKEEAKKKAdaaKKKAEEKKKADEakKKAEEDKKKADE 1409
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   447 SERAMQERVQRLEALRLSLEEELSRMKAAVLSERGQAEE------ELIKARNQARLEEQHRLAHLEEKIRLLAQARDEAQ 520
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEakkkaeEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAK 1489
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   521 GTCVQQKQMVAESQarvsqlnlQMEGQQRRLEELQ--QELINKDQEKVAEVARVRVELQEQMGRMQADLVAQEALREKVA 598
Cdd:PTZ00121 1490 KKAEEAKKKADEAK--------KAAEAKKKADEAKkaEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE 1561
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 23271084   599 ALERQMKVIGSEHREALLDRESENASLREKLRLKEA-----EISRIRDEEAQRA 647
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVmklyeEEKKMKAEEAKKA 1615
PTZ00121 PTZ00121
MAEBL; Provisional
268-571 1.72e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 1.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   268 KQREEMARDSRASAVRVGQLQEALNERQSiiNALKAKLQMTEAALALSEQKVRDLGELLVAGD-QERQSLSQRHEKERKL 346
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKADEAKKAEEAKKA--DEAKKAEEAKKADEAKKAEEKKKADELKKAEElKKAEEKKKAEEAKKAE 1573
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   347 ERQEAADRESKLLRDLSAANEKNLLLRSQVDELERKARSQQEQLFLTKQELTNTSAELKIRAIQAEERLDVEKRRAKQNM 426
Cdd:PTZ00121 1574 EDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   427 EDLEKLH------SKEVDHMTRHLEESERAMQERVQRLEALRLSLEEelsrmkAAVLSERGQAEEELIKARNQARLEEQH 500
Cdd:PTZ00121 1654 KAEEENKikaaeeAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE------AKKAEELKKKEAEEKKKAEELKKAEEE 1727
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23271084   501 RLAHLEEKIRLLAQARDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQELINKDQEKVAEVAR 571
Cdd:PTZ00121 1728 NKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
358-605 2.67e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.07  E-value: 2.67e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 358 LLRDLSAANEKNLLLRSQVDELERKARSQQEQLFLTKQELTNTSAELKiraiQAEERLDVEKRRAKQNMEDLEKLhskev 437
Cdd:COG4942  11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA----ALERRIAALARRIRALEQELAAL----- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 438 dhmtrhlEESERAMQERVQRLEALRLSLEEELSRMkAAVLSERGQAEEELIKARNQARLEEQHRLAHLEEkirlLAQARD 517
Cdd:COG4942  82 -------EAELAELEKEIAELRAELEAQKEELAEL-LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKY----LAPARR 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 518 EAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQELINKDQEKVAEVARVRVELQEQMGRMQADLVAQEALREKV 597
Cdd:COG4942 150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229

                ....*...
gi 23271084 598 AALERQMK 605
Cdd:COG4942 230 ARLEAEAA 237
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
244-493 3.13e-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: 3.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    244 LSKEVQHLQEEKSKQFLDLMETIDKQREEMARDSRASAVRVGQLQEALNERQSIINALKAKLQMTEAALALSEQKVRDLG 323
Cdd:TIGR02169  277 LNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT 356
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    324 ELLVAGDQERQSLSQRHEKERKlERQEAADRESKLLRDLSAAN-EKNLLLRSQVDELERKARSQQEQLFLtKQELTNTSA 402
Cdd:TIGR02169  357 EEYAELKEELEDLRAELEEVDK-EFAETRDELKDYREKLEKLKrEINELKRELDRLQEELQRLSEELADL-NAAIAGIEA 434
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    403 ---ELKIRAIQAEERLDVEKRRAKQNMEDLEKLhskevdhmtrhlEESERAMQERVQRLEALRLSLEEELSRMKAAVLSE 479
Cdd:TIGR02169  435 kinELEEEKEDKALEIKKQEWKLEQLAADLSKY------------EQELYDLKEEYDRVEKELSKLQRELAEAEAQARAS 502
                          250
                   ....*....|....*....
gi 23271084    480 R-----GQAEEELIKARNQ 493
Cdd:TIGR02169  503 EervrgGRAVEEVLKASIQ 521
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
217-635 4.49e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.98  E-value: 4.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  217 LRAVEQAMDHNQDRLTAFRENQARTKILSKEVQHLQEEKSKQFLDLMETIDKQREEMARDSR------ASAVRVGQLQEA 290
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKevkeleELKEEIEELEKE 246
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  291 LNERQSIINALKAKLQMTEAALALSEQKVRDLGELlVAGDQERQSLSQRHEKERKLeRQEAADRESKLLRDLSAANEKNL 370
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEK-VKELKELKEKAEEYIKLSEF-YEEYLDELREIEKRLSRLEEEIN 324
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  371 LLRSQVDELERKaRSQQEQLFLTKQELTNTSAELKIRAIQAEErldvekrrAKQNMEDLEKLHSKEVDHMTRHLEESERA 450
Cdd:PRK03918 325 GIEERIKELEEK-EERLEELKKKLKELEKRLEELEERHELYEE--------AKAKKEELERLKKRLTGLTPEKLEKELEE 395
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  451 MQERVQRLEALRLSLEEELSRMKAAVlSERGQAEEELIKARNQ-----ARLEEQHRLAHLEEKIRLLAQARDEAQGTCVQ 525
Cdd:PRK03918 396 LEKAKEEIEEEISKITARIGELKKEI-KELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAELKRIEKELKEIEEK 474
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  526 QKQMVAESQ------------ARVSQLNLQMEGQQRRLEELQQELINKDQEKVAEVARVRVELQEQMGRMQADLVAQEAL 593
Cdd:PRK03918 475 ERKLRKELRelekvlkkeselIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEEL 554
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 23271084  594 REKVAALERQMKVIGSEHREALLDRESENASLREKL--RLKEAE 635
Cdd:PRK03918 555 KKKLAELEKKLDELEEELAELLKELEELGFESVEELeeRLKELE 598
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
336-516 5.45e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 5.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  336 LSQRHEKERKLERQEAADRESKLLRDLSAANEKNLLLRSQVDELERKARSQQEQLfltkqeltntsAELKIRAIQAEERL 415
Cdd:COG4913  257 IRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAEL-----------ERLEARLDALREEL 325
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  416 D-VEKRRAKQNMEDLEKLhSKEVDHMTRHLEESERAMQERVQRLEALRLSLE----------EELSRMKAAVLSERGQAE 484
Cdd:COG4913  326 DeLEAQIRGNGGDRLEQL-EREIERLERELEERERRRARLEALLAALGLPLPasaeefaalrAEAAALLEALEEELEALE 404
                        170       180       190
                 ....*....|....*....|....*....|..
gi 23271084  485 EELIKARNQARlEEQHRLAHLEEKIRLLAQAR 516
Cdd:COG4913  405 EALAEAEAALR-DLRRELRELEAEIASLERRK 435
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
339-569 1.72e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 1.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  339 RHEK--ERKLERQ-----EAADRESKLLRDLSAANEKNLLLRSQVDELERKARSQQEQLFLTKQELTNTSAELKIRAIQA 411
Cdd:COG4913  589 RHEKddRRRIRSRyvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAER 668
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  412 E-ERLDVEKRRAKQNMEDLEKlhskevdhmtrhLEESERAMQERVQRLEALRLSLEEELSRMKaavlSERGQAEEELikA 490
Cdd:COG4913  669 EiAELEAELERLDASSDDLAA------------LEEQLEELEAELEELEEELDELKGEIGRLE----KELEQAEEEL--D 730
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23271084  491 RNQARLEEQHRLAHLEEkiRLLAQARDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQELINKDQEKVAEV 569
Cdd:COG4913  731 ELQDRLEAAEDLARLEL--RALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADL 807
LRR_8 pfam13855
Leucine rich repeat;
146-212 2.06e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 39.82  E-value: 2.06e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23271084   146 LRQLDLRNNQISHKGAEelalALKGNTTLQQLDLRWNNIGLLGGRALVnCLPSnrtLWKLDLAGNNI 212
Cdd:pfam13855   3 LRSLDLSNNRLTSLDDG----AFKGLSNLKVLDLSNNLLTTLSPGAFS-GLPS---LRYLDLSGNRL 61
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
315-613 2.51e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 44.56  E-value: 2.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  315 SEQKVRDLGELLVAGDQERQSLSQRHEKERKLER-----QEAADRESKLLRDLSAANEK-NLLL------------RSQV 376
Cdd:COG3096  277 ANERRELSERALELRRELFGARRQLAEEQYRLVEmarelEELSARESDLEQDYQAASDHlNLVQtalrqqekieryQEDL 356
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  377 DELERKARSQQEQLfltkQELTNTSAELKIRAIQAEERLDvekrRAKQNMEDLEklhskevdhmtRHLEESE-RAMQER- 454
Cdd:COG3096  357 EELTERLEEQEEVV----EEAAEQLAEAEARLEAAEEEVD----SLKSQLADYQ-----------QALDVQQtRAIQYQq 417
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  455 -VQRLE-ALRLSLEEELSRMKAAVLSERGQAEEELIkarNQARLEEQHRLAHLEEKIRLLAQA------------RDEAQ 520
Cdd:COG3096  418 aVQALEkARALCGLPDLTPENAEDYLAAFRAKEQQA---TEEVLELEQKLSVADAARRQFEKAyelvckiageveRSQAW 494
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  521 GTCVQQKQMVAESQA---RVSQLNLQM------EGQQRRLEELQQELINKDQEKVAEVARVRVELQEQMGRMQADLVAQE 591
Cdd:COG3096  495 QTARELLRRYRSQQAlaqRLQQLRAQLaeleqrLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAA 574
                        330       340
                 ....*....|....*....|..
gi 23271084  592 ALREKVAALERQMKVIGSEHRE 613
Cdd:COG3096  575 EAVEQRSELRQQLEQLRARIKE 596
Macoilin pfam09726
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ...
357-572 4.01e-04

Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.


Pssm-ID: 462859 [Multi-domain]  Cd Length: 670  Bit Score: 43.69  E-value: 4.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   357 KLLRDLSAANEKNLLLRSQVDEL---ERKARSQQEQLfltKQEltNTSAELKIR-AIQAeerldveKRRAKQNMEDLEKL 432
Cdd:pfam09726 406 KLKAELQASRQTEQELRSQISSLtslERSLKSELGQL---RQE--NDLLQTKLHnAVSA-------KQKDKQTVQQLEKR 473
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   433 HSKEVDHmtRHLEESERAMQERVQRLEalrlslEEELSRMKAAVLSERGQAEEELIKARNQARLE----------EQHRL 502
Cdd:pfam09726 474 LKAEQEA--RASAEKQLAEEKKRKKEE------EATAARAVALAAASRGECTESLKQRKRELESEikklthdiklKEEQI 545
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   503 AHLEEKIRLLAQARDEAQGTCV--------QQK-QMVAESQARVSQLNLQ----MEGQQRRLEELQQELINKDQE----- 564
Cdd:pfam09726 546 RELEIKVQELRKYKESEKDTEVlmsalsamQDKnQHLENSLSAETRIKLDlfsaLGDAKRQLEIAQGQIYQKDQEikdlk 625

                  ....*....
gi 23271084   565 -KVAEVARV 572
Cdd:pfam09726 626 qKIAEVMAV 634
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
75-212 4.55e-04

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 43.00  E-value: 4.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  75 STLLFQGLCANTSVQHLDLKGNNLRATGAEALGKLLRQNKSIQSLTLEWNNLGTWEDAFATFCGGLAANSALRQLDLRNN 154
Cdd:COG4886  44 SLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSNLTNLESLDLSGN 123
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 23271084 155 QIShkgaeELALALKGNTTLQQLDLRWNNIgllggRALVNCLPSNRTLWKLDLAGNNI 212
Cdd:COG4886 124 QLT-----DLPEELANLTNLKELDLSNNQL-----TDLPEPLGNLTNLKSLDLSNNQL 171
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
216-405 6.24e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 6.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    216 ILRAVEQAMDHNQDRLTAFRENQARTKILSKEVQHLQEEKSKQFLDLMETIDKQREEMARDSRASAVRVGQLQEALNERQ 295
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    296 SIINALKAKLQMTEAALALSEQKVRDLGELLVAGDQERQSLSQRHEKERKLERQEAADRESKLLRDlsaaneknllLRSQ 375
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEE----------LQEE 455
                          170       180       190
                   ....*....|....*....|....*....|
gi 23271084    376 VDELERKARSQQEQLFLTKQELTNTSAELK 405
Cdd:TIGR02168  456 LERLEEALEELREELEEAEQALDAAERELA 485
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
236-508 6.75e-04

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 42.79  E-value: 6.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   236 ENQARTKILSKEVQHLQEEKSKQFLDL------METIDKQREEMARDSRASAVRVGQLQealNERQSIINALKAKLQMTE 309
Cdd:pfam05483 489 ELTAHCDKLLLENKELTQEASDMTLELkkhqedIINCKKQEERMLKQIENLEEKEMNLR---DELESVREEFIQKGDEVK 565
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   310 AALALSEQKVRDLGELLVAGDQERQSLSQ-----RHEKERKLERQEAADRESKLLRDLSAANEKNL-LLRSQVDELERKA 383
Cdd:pfam05483 566 CKLDKSEENARSIEYEVLKKEKQMKILENkcnnlKKQIENKNKNIEELHQENKALKKKGSAENKQLnAYEIKVNKLELEL 645
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   384 RSQQEQLfltkQELTNT-SAELKIRAIqAEERLDVEKRRAKQNMEDLEKLHsKEVDH------------MTRHLEESERA 450
Cdd:pfam05483 646 ASAKQKF----EEIIDNyQKEIEDKKI-SEEKLLEEVEKAKAIADEAVKLQ-KEIDKrcqhkiaemvalMEKHKHQYDKI 719
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23271084   451 MQER----------VQRLEALRLSLEEELSRMKAAVLSERGQAEEELiKARNQARLEEQHRLAHLEEK 508
Cdd:pfam05483 720 IEERdselglyknkEQEQSSAKAALEIELSNIKAELLSLKKQLEIEK-EEKEKLKMEAKENTAILKDK 786
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
217-640 6.84e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 6.84e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 217 LRAVEQAMDHNQDRLTAFRENQARTKILSKEVQHLQEEKSKQfldlmeTIDKQREEMARDSRASAVRVGQLQEALNERQS 296
Cdd:COG4717  73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEEL------REELEKLEKLLQLLPLYQELEALEAELAELPE 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 297 IINALKAKLQMTEAALALSEQKVRDLGELLVAGDQERQSLSQRHEKE---RKLERQEAADRESKLLRDLSAANEKNLLLR 373
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElqdLAEELEELQQRLAELEEELEEAQEELEELE 226
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 374 SQVDELERKARSQQEQLFLTKQELTNTSAELKIRAIQAEERLDVEKRRAKQNMEDLEKLHSKEVDHMTRHLEESERAMQE 453
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEE 306
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 454 RVQRLEALRLSLEEELSRMKAAVLSERGQAEEELIKARNQARLEEQHRLAHLEEKIRLLAQARDEAQGTCVQQKQMVAES 533
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEE 386
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 534 QARVSQLNLQMEGQQRRLEELQQELINKDQEKVAEVA-----RVRVELQEQMGRMQADLVAQEALREKVAALERQMKVIG 608
Cdd:COG4717 387 LRAALEQAEEYQELKEELEELEEQLEELLGELEELLEaldeeELEEELEELEEELEELEEELEELREELAELEAELEQLE 466
                       410       420       430
                ....*....|....*....|....*....|..
gi 23271084 609 SEHReaLLDRESENASLREKLRLKEAEISRIR 640
Cdd:COG4717 467 EDGE--LAELLQELEELKAELRELAEEWAALK 496
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
490-647 8.91e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.75  E-value: 8.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    490 ARNQARLEEQHR-LAHLEEKIRLLAQARDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQELINKDQE---- 564
Cdd:TIGR02169  677 QRLRERLEGLKReLSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEienv 756
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    565 --KVAEVARVRVELQEQMGRMQADLVAQEA--LREKVAALERQMKVIGSEHREALLDRESENASLREKLRLKEAEISRIR 640
Cdd:TIGR02169  757 ksELKELEARIEELEEDLHKLEEALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ 836

                   ....*..
gi 23271084    641 DEEAQRA 647
Cdd:TIGR02169  837 ELQEQRI 843
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
218-487 9.72e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 9.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  218 RAVEQAMDHNQDRLTAFRENQARTKILSKEVQHLQ--EEKSKQFLDLMETIDKQREEMAR-DSRASAVRVGQLQEALNER 294
Cdd:COG4913  221 PDTFEAADALVEHFDDLERAHEALEDAREQIELLEpiRELAERYAAARERLAELEYLRAAlRLWFAQRRLELLEAELEEL 300
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  295 QSIINALKAKLQMTEAALALSEQKVRDLGELLvagdqerqslsqrhekerkleRQEAADRESKLLRDLSAANEknlllrs 374
Cdd:COG4913  301 RAELARLEAELERLEARLDALREELDELEAQI---------------------RGNGGDRLEQLEREIERLER------- 352
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  375 QVDELERKARSQQEQLFLTKQELTNTSAELKIRAIQAEERLDVEKRRAKQNMEDLEKLHSKEVDhmtrhLEESERAMQER 454
Cdd:COG4913  353 ELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD-----LRRELRELEAE 427
                        250       260       270
                 ....*....|....*....|....*....|...
gi 23271084  455 VQRLEALRLSLEEELSRMKAAVLSERGQAEEEL 487
Cdd:COG4913  428 IASLERRKSNIPARLLALRDALAEALGLDEAEL 460
Caldesmon pfam02029
Caldesmon;
328-591 1.13e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 42.16  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   328 AGDQERQSLS---QRHEKERKLERQEAADRESKLLRDLSAANE-----------------------KNLLLRSQVDELER 381
Cdd:pfam02029  56 GGLDEEEAFLdrtAKREERRQKRLQEALERQKEFDPTIADEKEsvaerkenneeeensswekeekrDSRLGRYKEEETEI 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   382 KARSQQEQLFLTKQELTNTSAELKIRAIQAEERLDvEKRRAKQNMEDLEKLHSKEVDHMTRHLEESERAMQER-VQRLEA 460
Cdd:pfam02029 136 REKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVP-TENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVkSQNGEE 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   461 LRLSLEEELSRMKAAVLSERGQAEEElikarnQARLEEQHRLahleEKIRLLAQARDEAQGTCVQQKQmvAESQARVSQL 540
Cdd:pfam02029 215 EVTKLKVTTKRRQGGLSQSQEREEEA------EVFLEAEQKL----EELRRRRQEKESEEFEKLRQKQ--QEAELELEEL 282
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23271084   541 NLQME--------GQQRRLEELQQELINKDQEK---VAEVARVRVELQEQMGRMQADLVAQE 591
Cdd:pfam02029 283 KKKREerrklleeEEQRRKQEEAERKLREEEEKrrmKEEIERRRAEAAEKRQKLPEDSSSEG 344
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
444-661 1.27e-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: 41.67  E-value: 1.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 444 LEESERAMQERVQRLEALRLSLEEELSRmKAAVLSERGQAEEELIKARNQARLEEQhRLAHLEEKIRLLAQARDEAQGTC 523
Cdd:COG4942  22 AAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQ-ELAALEAELAELEKEIAELRAEL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 524 VQQKQMVAE------SQARVSQLNLQMEGQQ-----------RRLEELQQELINKDQEKVAEVARVRVELQEQMGRMQAD 586
Cdd:COG4942 100 EAQKEELAEllralyRLGRQPPLALLLSPEDfldavrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 587 LVAQEALREK-----------VAALERQMKvigsehreallDRESENASLREKLRLKEAEISRIRDEEAQRASFLQNAVL 655
Cdd:COG4942 180 LAELEEERAAlealkaerqklLARLEKELA-----------ELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248

                ....*.
gi 23271084 656 AYVQGS 661
Cdd:COG4942 249 AALKGK 254
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
448-645 1.36e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.93  E-value: 1.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 448 ERAMQERVQRLEALRLSLEEELSRMKAAVLsergQAEEELikarnqARLEEQHRLAHLEEKIRLLAQARDEAQGTCVQQK 527
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELE----EAEAAL------EEFRQKNGLVDLSEEAKLLLQQLSELESQLAEAR 232
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 528 QMVAESQARVSQLNLQMEGQQRRLEELQQELINkdQEKVAEVARVRVELQEQMGRMQADLVAQEALREKVAALERQMKvi 607
Cdd:COG3206 233 AELAEAEARLAALRAQLGSGPDALPELLQSPVI--QQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQ-- 308
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 23271084 608 gSEHREALLDRESEN-------ASLREKLRLKEAEISRIRDEEAQ 645
Cdd:COG3206 309 -QEAQRILASLEAELealqareASLQAQLAQLEARLAELPELEAE 352
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
341-476 1.46e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.77  E-value: 1.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 341 EKERKLERQEAADRESKLLRDLSAANEKNLLLRSQVDELERKARSQQEQlfLTKQELTNTSAELKIRAIQAEERLDVEKR 420
Cdd:COG2433 387 EKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAE--LEEKDERIERLERELSEARSEERREIRKD 464
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 23271084 421 RAKQNMEdleklhsKEVDHMTRHLEESERAMQERVQRLEALRLSLEEELSRMKAAV 476
Cdd:COG2433 465 REISRLD-------REIERLERELEEERERIEELKRKLERLKELWKLEHSGELVPV 513
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
60-227 1.69e-03

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 41.46  E-value: 1.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  60 LKELVLSDCMLSEegstlLFQGLCANTSVQHLDLKGNNLraTGAEALGKLlrqnKSIQSLTLEWNNLGTWEDafatfcgg 139
Cdd:COG4886 207 LEELDLSGNQLTD-----LPEPLANLTNLETLDLSNNQL--TDLPELGNL----TNLEELDLSNNQLTDLPP-------- 267
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 140 LAANSALRQLDLRNNQISHKGAEELALALKGNTTLQQLDLRWNNIGLLGGRALVNCLPSNRTLWKLDLAGNNIPGDILRA 219
Cdd:COG4886 268 LANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLL 347

                ....*...
gi 23271084 220 VEQAMDHN 227
Cdd:COG4886 348 ALLTLLLL 355
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
254-605 1.77e-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: 41.75  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    254 EKSKQFLDLMETIDKQREEMARDSRASAVRVGQLQEALNERQSIINA-LKAKLQMTEAALALS-EQKVRDLGELLVAGDQ 331
Cdd:pfam12128  340 ETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEqNNRDIAGIKDKLAKIrEARDRQLAVAEDDLQA 419
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    332 ERQSLSQRHE------KERKLERQEAADRESKLLRDLSAANEKNLLLRSQVDELERkARSQQEQLFLTKQELTNTSAELK 405
Cdd:pfam12128  420 LESELREQLEagklefNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIER-AREEQEAANAEVERLQSELRQAR 498
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    406 IRAIQAEERLDVEKRRAKQNMEDLEKLHSK---------------------------------------EVDHMTRHLEE 446
Cdd:pfam12128  499 KRRDQASEALRQASRRLEERQSALDELELQlfpqagtllhflrkeapdweqsigkvispellhrtdldpEVWDGSVGGEL 578
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    447 SERAMQERVQRLE-----ALRLSLEEELSRMKAAVLSER---GQAEEELIKARNQ---ARLEEQHRLAHLEEKIRLLAQA 515
Cdd:pfam12128  579 NLYGVKLDLKRIDvpewaASEEELRERLDKAEEALQSARekqAAAEEQLVQANGElekASREETFARTALKNARLDLRRL 658
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084    516 RDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQELINKDQEKVAEvarVRVELQEQMGRMQADLVAQEA-LR 594
Cdd:pfam12128  659 FDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKRE---ARTEKQAYWQVVEGALDAQLAlLK 735
                          410
                   ....*....|.
gi 23271084    595 EKVAALERQMK 605
Cdd:pfam12128  736 AAIAARRSGAK 746
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
235-478 2.17e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 2.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 235 RENQARTKILSKEVQHLQEEKSKQfldlmetiDKQREEMARDSRASAVRVGQLQEALNERQSIINALKAKLQMTEAALAL 314
Cdd:COG4942  23 AEAEAELEQLQQEIAELEKELAAL--------KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 315 SEQKVRDLGELLVAGDQERQSLSQRHEKERKLERQEAAD--RESKLLRDLSAANEKNLL-LRSQVDELERKARSQQEQlf 391
Cdd:COG4942  95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDavRRLQYLKYLAPARREQAEeLRADLAELAALRAELEAE-- 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 392 ltKQELTNTSAELKiraiQAEERLDVEKRRAKQNMEDLEKLHSKEvdhmtrhlEESERAMQERVQRLEALRLSLEEELSR 471
Cdd:COG4942 173 --RAELEALLAELE----EERAALEALKAERQKLLARLEKELAEL--------AAELAELQQEAEELEALIARLEAEAAA 238

                ....*..
gi 23271084 472 MKAAVLS 478
Cdd:COG4942 239 AAERTPA 245
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
234-643 2.61e-03

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 40.86  E-value: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   234 FRENQARTKILSKEVQHLQEEKSKQFLDLMETIDK--------------QREEMARDSRASAVRVGQLQEalnERQSIIN 299
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKmilafeelrvqaenARLEMHFKLKEDHEKIQHLEE---EYKKEIN 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   300 ALKAKLQMTEAALALSEQKVRDLGELLvagDQERQSLSQRHEK-----ERKLERQEAADRESKLLRDLSAANEKNLLLRS 374
Cdd:pfam05483 237 DKEKQVSLLLIQITEKENKMKDLTFLL---EESRDKANQLEEKtklqdENLKELIEKKDHLTKELEDIKMSLQRSMSTQK 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   375 QVDE-----------LERKARSQQEQLFLTKQELTNTSAELKIRAIQAEERLDVEKRRAKQNmEDLEKLHSKEVDHMTRH 443
Cdd:pfam05483 314 ALEEdlqiatkticqLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKN-EDQLKIITMELQKKSSE 392
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   444 LEESERAMQERVQRLEALRLSLEEELSRM----KAAVLSERGQAEEELIKARNQARLEEQHRLahleeKIRLLAQARDEa 519
Cdd:pfam05483 393 LEEMTKFKNNKEVELEELKKILAEDEKLLdekkQFEKIAEELKGKEQELIFLLQAREKEIHDL-----EIQLTAIKTSE- 466
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   520 QGTCVQQKQMVAESQARVSQlNLQMEGQQRRLEELQQELINKDQEKVAEVARVRVELQEQMGRMQADLVAQEALREKVAA 599
Cdd:pfam05483 467 EHYLKEVEDLKTELEKEKLK-NIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMN 545
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 23271084   600 LERQMKVIGSEHRE------ALLDRESENASLREKLRLKEAEISRIRDEE 643
Cdd:pfam05483 546 LRDELESVREEFIQkgdevkCKLDKSEENARSIEYEVLKKEKQMKILENK 595
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
286-480 3.02e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 3.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 286 QLQEALNERQSIINALKAKLQMTEAALALSEQKVRDLGELLVAGDQERQSLSQR----HEKERKLERQEAADRE--SKLL 359
Cdd:COG4942  31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElaelEKEIAELRAELEAQKEelAELL 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 360 RDL---SAANEKNLLLRSQ-----------VDELERKARSQQEQLFLTKQELTNTSAELKiraiQAEERLDVEKRRAKQN 425
Cdd:COG4942 111 RALyrlGRQPPLALLLSPEdfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELE----AERAELEALLAELEEE 186
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 23271084 426 MEDLEKLHSKEVDHMTRhLEESERAMQERVQRLEALRLSLEEELSRMKAAVLSER 480
Cdd:COG4942 187 RAALEALKAERQKLLAR-LEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
506-657 3.04e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 3.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  506 EEKIRLLAQARDEAQgtcvqqkQMVAESQARVSQLNLQMEGQQRRLEELQQ-ELINKDQEKVAEVARVRVELQEQMGRMQ 584
Cdd:COG4913  609 RAKLAALEAELAELE-------EELAEAEERLEALEAELDALQERREALQRlAEYSWDEIDVASAEREIAELEAELERLD 681
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23271084  585 ADLVAQEALREKVAALERQMKvigsEHREALLDRESENASLREKLRLKEAEISRIRDEEAQRASFLQNAVLAY 657
Cdd:COG4913  682 ASSDDLAALEEQLEELEAELE----ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
308-475 3.89e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 40.71  E-value: 3.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  308 TEAALALSEQKVRDLGELLVAGDQERQSLSQRHEKERKLERQEAADRESKLL-----RDLSAANEKNLL---LRSQVDEL 379
Cdd:COG3096  490 RSQAWQTARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFcqrigQQLDAAEELEELlaeLEAQLEEL 569
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  380 ERKARSQQEQLFLTKQELTNTSAELKIRAIQAEERLDVEKRRAK-QNMEDLEKLHSKEVDHMTRHLEESERAMQERVQRL 458
Cdd:COG3096  570 EEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERlREQSGEALADSQEVTAAMQQLLEREREATVERDEL 649
                        170
                 ....*....|....*..
gi 23271084  459 EALRLSLEEELSRMKAA 475
Cdd:COG3096  650 AARKQALESQIERLSQP 666
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
347-557 4.21e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 39.74  E-value: 4.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   347 ERQEAADRESKLLRDLSAANEKNLLLrsqvDELERKARSQQEQLFLTKQELTNTSAELKiraiQAEERLDVEKRRAKQNM 426
Cdd:pfam09787  24 EKLIASLKEGSGVEGLDSSTALTLEL----EELRQERDLLREEIQKLRGQIQQLRTELQ----ELEAQQQEEAESSREQL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084   427 EDLEKLHSKEvdhmtrhlEESERAMQERVQRLEALRLSLEEELSRMKAAVLSERGQAEEELIKARNQARLEEQHRL--AH 504
Cdd:pfam09787  96 QELEEQLATE--------RSARREAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKSQSSSsqSE 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 23271084   505 LEEKIRLLAQardeaqgTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQE 557
Cdd:pfam09787 168 LENRLHQLTE-------TLIQKQTMLEALSTEKNSLVLQLERMEQQIKELQGE 213
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
372-574 5.99e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 5.99e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 372 LRSQVDELERKARSQQEQL--FLTKQELTNTSAELKIRAIQAEE------RLDVEKRRAKQNMEDLEKLHSKEVDHMTRH 443
Cdd:COG3206 180 LEEQLPELRKELEEAEAALeeFRQKNGLVDLSEEAKLLLQQLSElesqlaEARAELAEAEARLAALRAQLGSGPDALPEL 259
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 444 LEESerAMQERVQRLEALRLSLEEELSRMKA------AVLSERGQAEEELIKARNQARLEEQHRLAHLEEKIRLLAQARD 517
Cdd:COG3206 260 LQSP--VIQQLRAQLAELEAELAELSARYTPnhpdviALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLA 337
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 23271084 518 EAQgtcvQQKQMVAESQARVSQLNLQMEGQQRRLEELQQELINKDQEKVAEVARVRV 574
Cdd:COG3206 338 QLE----ARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRV 390
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
400-571 6.08e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 39.68  E-value: 6.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 400 TSAELKIRAIQAEERLDVEKRRAKQNMEDLEKLhskevdhmtrhLEESERAMQERVQRLEALRLSLEEELSRMKAAVLSE 479
Cdd:COG0542 398 AAARVRMEIDSKPEELDELERRLEQLEIEKEAL-----------KKEQDEASFERLAELRDELAELEEELEALKARWEAE 466
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 480 RGQAEEELikaRNQARLEEQHRLAHLEEKIRLLAQARDEAQGTCVQQ---KQMVAESQAR-----VSQLnlqMEGQQRRL 551
Cdd:COG0542 467 KELIEEIQ---ELKEELEQRYGKIPELEKELAELEEELAELAPLLREevtEEDIAEVVSRwtgipVGKL---LEGEREKL 540
                       170       180
                ....*....|....*....|....
gi 23271084 552 ----EELQQELINKDqEKVAEVAR 571
Cdd:COG0542 541 lnleEELHERVIGQD-EAVEAVAD 563
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
403-522 6.36e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.84  E-value: 6.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 403 ELKIRAIQA---EERLDVEKRRAKQNMEDLEKLHSKEVDHMTRHLEESERAMQERVQRLEALRLSLEEELSRMKAAVlsE 479
Cdd:COG2433 367 EVKARVIRGlsiEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERI--E 444
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 23271084 480 RGQAEEELIKARNQARLEEQHRLAHLEEKIRLLAQARDEAQGT 522
Cdd:COG2433 445 RLERELSEARSEERREIRKDREISRLDREIERLERELEEERER 487
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
268-645 7.42e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 7.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 268 KQREEMARDSRASAVRVGQLQEALNERQSiinaLKAKLQMTEAALALSEQKVRDLGELLVAGDQERQSLSQRHEKERKLE 347
Cdd:COG4717  71 KELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPE 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 348 RQEAADRESKLLRDLsaaneknlllRSQVDELERKARSQQEQLFLTKQELTNTSAELKIRAIQAEERLDVEKRRAKQNME 427
Cdd:COG4717 147 RLEELEERLEELREL----------EEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 428 DL-EKLHSKEVDHMTRHLEESERAMQERVQRLEALRLSL--------------EEELSRMKAAVLSERGQAEEELIKARN 492
Cdd:COG4717 217 EAqEELEELEEELEQLENELEAAALEERLKEARLLLLIAaallallglggsllSLILTIAGVLFLVLGLLALLFLLLARE 296
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 493 QARLEEQHRLAHLEEKIRLLAQAR-----DEAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQELINkdQEKVA 567
Cdd:COG4717 297 KASLGKEAEELQALPALEELEEEEleellAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELE--QEIAA 374
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084 568 EVARVRVELQEQMGRMQADLVAQEALREKVAALERQMKVIGSEHREALLDRESEN-----ASLREKLRLKEAEISRIRDE 642
Cdd:COG4717 375 LLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEleeelEELEEELEELEEELEELREE 454

                ...
gi 23271084 643 EAQ 645
Cdd:COG4717 455 LAE 457
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
54-159 8.90e-03

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 38.23  E-value: 8.90e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23271084  54 LHKETLLKELVLSDCMLsEEGSTLLFQGLCANT---SVQHLDLKGNNLRATgaEALGKLlrqnKSIQSLTLEWNNLGTWE 130
Cdd:cd21340  86 LENLTNLEELHIENQRL-PPGEKLTFDPRSLAAlsnSLRVLNISGNNIDSL--EPLAPL----RNLEQLDASNNQISDLE 158
                        90       100
                ....*....|....*....|....*....
gi 23271084 131 DAFATfcggLAANSALRQLDLRNNQISHK 159
Cdd:cd21340 159 ELLDL----LSSWPSLRELDLTGNPVCKK 183
 
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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