|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
398-506 |
1.27e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 398 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 477
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
90 100
....*....|....*....|....*....
gi 1907166730 478 REEKNSfVAVTHEKREAALDEAATVLQAA 506
Cdd:COG1196 340 EELEEE-LEEAEEELEEAEAELAEAEEAL 367
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
149-506 |
1.02e-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: 52.37 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 149 EIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpsrgpdfvrtlaeKKPDTGWVITGLKQRIFRLEQQCKE 228
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK-------------ELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 229 KDNTINKLQTdmkttNLEEMRIAMETYYEEIHRLQTLLASSEATGKKpmVEKKLgvkrqKKMSSALLNLTRSVQELTEEN 308
Cdd:TIGR02168 745 LEERIAQLSK-----ELTELEAEIEELEERLEEAEEELAEAEAEIEE--LEAQI-----EQLKEELKALREALDELRAEL 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 309 QSLKEDLDRMLSNSPTISKIKGYGDWSKPRLLRRIAELEKKVSS--------SESPKQSTSELVnpnplvrSPSNISVQK 380
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESlaaeieelEELIEELESELE-------ALLNERASL 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 381 QPKGDQSPEDLPKVApcEEQEHLQGTVKSLREELGALQEQLLEKDLEMKQL------LQSKI--DLEKELETAREGEKGR 452
Cdd:TIGR02168 886 EEALALLRSELEELS--EELRELESKRSELRRELEELREKLAQLELRLEGLevridnLQERLseEYSLTLEEAEALENKI 963
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907166730 453 QEQEQALREEVEALTKKCQEL-------EEAKREEKNSFVAVTHEKREaaLDEAATVLQAA 506
Cdd:TIGR02168 964 EDDEEEARRRLKRLENKIKELgpvnlaaIEEYEELKERYDFLTAQKED--LTEAKETLEEA 1022
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
138-681 |
3.04e-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: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 138 SVYREKEDMY-DEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPSRGPDFVRTLAEKKPDTGW-VITGL 215
Cdd:pfam15921 331 SELREAKRMYeDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWdRDTGN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 216 KQRIFRLEQQCKEKDNTINKLQTDMKTT------NLEEMRIAMETYYEEIHRLQTLLASSEATgkKPMVEKKLGVKRQKK 289
Cdd:pfam15921 411 SITIDHLRRELDDRNMEVQRLEALLKAMksecqgQMERQMAAIQGKNESLEKVSSLTAQLEST--KEMLRKVVEELTAKK 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 290 MS-----SALLNLTRSVQELT---------------------EENQSLKEDLDRmLSNSPT------------------- 324
Cdd:pfam15921 489 MTlesseRTVSDLTASLQEKEraieatnaeitklrsrvdlklQELQHLKNEGDH-LRNVQTecealklqmaekdkvieil 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 325 ------ISKIKGYGDWSKPRLLRRIAELEKKVSSSESPKQSTSELVNPN-----PLVRSPSNISVQKQPKGDQSPEDLPK 393
Cdd:pfam15921 568 rqqienMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKdakirELEARVSDLELEKVKLVNAGSERLRA 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 394 VAPC-EEQEHLQGTVKSLREELGALQE--QLLEKDLEMK-------------QLLQSKIDLEKELETAREGEK------- 450
Cdd:pfam15921 648 VKDIkQERDQLLNEVKTSRNELNSLSEdyEVLKRNFRNKseemetttnklkmQLKSAQSELEQTRNTLKSMEGsdghamk 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 451 ---GRQEQEQALREEVEALTKKCQELEEAK----------REEKNSF-------------------VAVTHEKR------ 492
Cdd:pfam15921 728 vamGMQKQITAKRGQIDALQSKIQFLEEAMtnankekhflKEEKNKLsqelstvateknkmageleVLRSQERRlkekva 807
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 493 --EAALDEAAtvLQAA------FRGHLARSKLVRSKVPDSRSPSLPGLLSplnQSSPAPRVLSPISPAEENPTqeeaviv 564
Cdd:pfam15921 808 nmEVALDKAS--LQFAecqdiiQRQEQESVRLKLQHTLDVKELQGPGYTS---NSSMKPRLLQPASFTRTHSN------- 875
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 565 iqsilrgylaqarfiasccreiaASSQRETVSLTPSGSASPPSLRASPGVIRKELCasEELRETSASEPAPSVPYSAQGG 644
Cdd:pfam15921 876 -----------------------VPSSQSTASFLSHHSRKTNALKEDPTRDLKQLL--QELRSVINEEPTVQLSKAEDKG 930
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1907166730 645 HG-------DCPSSSSLEAvpSMKDAMCEERSSSPRSAGPSLAE 681
Cdd:pfam15921 931 RApslgaldDRVRDCIIES--SLRSDICHSSSNSLQTEGSKSSE 972
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
141-501 |
6.08e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 141 REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpsRGPDFVRTLAEKKPDTGWV---ITGLKQ 217
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELED--RDEELRDRLEECRVAAQAHneeAESLRE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 218 RIFRLEQQCKEKDNTINKLQTDmkttnLEEMRIAMETYYEEIHRLQTLLASSEAtgkkpmvekklgvkrqkkmssALLNL 297
Cdd:PRK02224 350 DADDLEERAEELREEAAELESE-----LEEAREAVEDRREEIEELEEEIEELRE---------------------RFGDA 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 298 TRSVQELTEENQSLKEDLDRmlsnsptiskikgygdwskprLLRRIAELEKKVSSSESPKQSTSELVNPNplvrspsnis 377
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDE---------------------LREREAELEATLRTARERVEEAEALLEAG---------- 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 378 vqKQPKGDQSPEDLPKVAPCEEQEhlqGTVKSLREELGALQEQL--LEKDLE-----------MKQLLQSKIDLEKELET 444
Cdd:PRK02224 453 --KCPECGQPVEGSPHVETIEEDR---ERVEELEAELEDLEEEVeeVEERLEraedlveaedrIERLEERREDLEELIAE 527
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907166730 445 AREGEKGRQEQEQALREEVEALTKKCQELEEAKREEknsfvavtHEKREAALDEAAT 501
Cdd:PRK02224 528 RRETIEEKRERAEELRERAAELEAEAEEKREAAAEA--------EEEAEEAREEVAE 576
|
|
| IQCD |
cd23767 |
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ... |
490-520 |
3.02e-04 |
|
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.
Pssm-ID: 467745 [Multi-domain] Cd Length: 37 Bit Score: 38.68 E-value: 3.02e-04
10 20 30
....*....|....*....|....*....|.
gi 1907166730 490 EKREAALDEAATVLQAAFRGHLARSKLVRSK 520
Cdd:cd23767 2 EEELQRMNRAATLIQALWRGYKVRKELKKKK 32
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
140-529 |
5.77e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 140 YREKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLD--PSRGPDFVRTLAEKkpdtgwvITGLKQ 217
Cdd:COG4717 134 LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEqlSLATEEELQDLAEE-------LEELQQ 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 218 RIFRLEQQCKEKDNTINKLQTDMKTTNLEEMRIAMETYYEEIHRLQTLLA-----SSEATGKKPMVEKKLGV-------- 284
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAallalLGLGGSLLSLILTIAGVlflvlgll 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 285 -------KRQKKMSSALLNLTRSVQELTE-ENQSLKEDLDR-MLSNSPTISKIKGYGDW--SKPRLLRRIAELEKKVSSS 353
Cdd:COG4717 287 allflllAREKASLGKEAEELQALPALEElEEEELEELLAAlGLPPDLSPEELLELLDRieELQELLREAEELEEELQLE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 354 ESPKQSTSELvnpnplvrspsnisvqkQPKGDQSPEDLpkVAPCEEQEHLQgtvkSLREELGALQEQLLEKDLEMKQLLQ 433
Cdd:COG4717 367 ELEQEIAALL-----------------AEAGVEDEEEL--RAALEQAEEYQ----ELKEELEELEEQLEELLGELEELLE 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 434 --SKIDLEKELETAregekgrQEQEQALREEVEALTKKCQELEEAKRE-EKNSFVAVTHEKREAALDEAATVLQAAFRGH 510
Cdd:COG4717 424 alDEEELEEELEEL-------EEELEELEEELEELREELAELEAELEQlEEDGELAELLQELEELKAELRELAEEWAALK 496
|
410 420
....*....|....*....|.
gi 1907166730 511 LARSKL--VRSKVPDSRSPSL 529
Cdd:COG4717 497 LALELLeeAREEYREERLPPV 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
398-506 |
8.35e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 8.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 398 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQL-------------LQSKI-DLEKELETAREGEKGRQEQEQALREEV 463
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSELeeeieelqkelyaLANEIsRLEQQKQILRERLANLERQLEELEAQL 325
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1907166730 464 EALTKKCQELEE--AKREEKNSFVAVTHEKREAALDEAATVLQAA 506
Cdd:TIGR02168 326 EELESKLDELAEelAELEEKLEELKEELESLEAELEELEAELEEL 370
|
|
| IQ |
smart00015 |
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
496-516 |
2.65e-03 |
|
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.
Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 35.76 E-value: 2.65e-03
|
| IQ |
pfam00612 |
IQ calmodulin-binding motif; Calmodulin-binding motif. |
498-516 |
5.06e-03 |
|
IQ calmodulin-binding motif; Calmodulin-binding motif.
Pssm-ID: 459869 Cd Length: 21 Bit Score: 34.99 E-value: 5.06e-03
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
336-481 |
5.53e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.11 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 336 KPRLLRRIAELEKKvssSESPKQSTSELVNPNPLVRSPSNISVQKQPKGDQSPEDL--PKVAPCEEQEHLQGTVKSLREE 413
Cdd:pfam17380 346 RERELERIRQEERK---RELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELeaARKVKILEEERQRKIQQQKVEM 422
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907166730 414 LGALQEQLLEKDLEMKQLLQSKidlEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKREEK 481
Cdd:pfam17380 423 EQIRAEQEEARQREVRRLEEER---AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRK 487
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
418-504 |
7.63e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.81 E-value: 7.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 418 QEQLLEKDLEMKQLLQSKIDLEKELET-AREGEKGRQEQEQaLREEVEaltKKCQELEEAKREEKNSFVAVTHEKREAAL 496
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQkAEEAEALLKEAEK-LKEELE---EKKEKLQEEEDKLLEEAEKEAQQAIKEAK 583
|
....*...
gi 1907166730 497 DEAATVLQ 504
Cdd:PRK00409 584 KEADEIIK 591
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
398-506 |
1.27e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 398 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 477
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
90 100
....*....|....*....|....*....
gi 1907166730 478 REEKNSfVAVTHEKREAALDEAATVLQAA 506
Cdd:COG1196 340 EELEEE-LEEAEEELEEAEAELAEAEEAL 367
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
149-506 |
1.02e-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: 52.37 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 149 EIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpsrgpdfvrtlaeKKPDTGWVITGLKQRIFRLEQQCKE 228
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK-------------ELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 229 KDNTINKLQTdmkttNLEEMRIAMETYYEEIHRLQTLLASSEATGKKpmVEKKLgvkrqKKMSSALLNLTRSVQELTEEN 308
Cdd:TIGR02168 745 LEERIAQLSK-----ELTELEAEIEELEERLEEAEEELAEAEAEIEE--LEAQI-----EQLKEELKALREALDELRAEL 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 309 QSLKEDLDRMLSNSPTISKIKGYGDWSKPRLLRRIAELEKKVSS--------SESPKQSTSELVnpnplvrSPSNISVQK 380
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESlaaeieelEELIEELESELE-------ALLNERASL 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 381 QPKGDQSPEDLPKVApcEEQEHLQGTVKSLREELGALQEQLLEKDLEMKQL------LQSKI--DLEKELETAREGEKGR 452
Cdd:TIGR02168 886 EEALALLRSELEELS--EELRELESKRSELRRELEELREKLAQLELRLEGLevridnLQERLseEYSLTLEEAEALENKI 963
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907166730 453 QEQEQALREEVEALTKKCQEL-------EEAKREEKNSFVAVTHEKREaaLDEAATVLQAA 506
Cdd:TIGR02168 964 EDDEEEARRRLKRLENKIKELgpvnlaaIEEYEELKERYDFLTAQKED--LTEAKETLEEA 1022
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
398-506 |
1.08e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 398 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 477
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
90 100
....*....|....*....|....*....
gi 1907166730 478 REEKNSFVAVTHEKREAALDEAATVLQAA 506
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLE 403
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
398-508 |
1.79e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 398 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 477
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
90 100 110
....*....|....*....|....*....|.
gi 1907166730 478 REEKNSFVAVThEKREAALDEAATVLQAAFR 508
Cdd:COG1196 361 AEAEEALLEAE-AELAEAEEELEELAEELLE 390
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
138-681 |
3.04e-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: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 138 SVYREKEDMY-DEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPSRGPDFVRTLAEKKPDTGW-VITGL 215
Cdd:pfam15921 331 SELREAKRMYeDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWdRDTGN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 216 KQRIFRLEQQCKEKDNTINKLQTDMKTT------NLEEMRIAMETYYEEIHRLQTLLASSEATgkKPMVEKKLGVKRQKK 289
Cdd:pfam15921 411 SITIDHLRRELDDRNMEVQRLEALLKAMksecqgQMERQMAAIQGKNESLEKVSSLTAQLEST--KEMLRKVVEELTAKK 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 290 MS-----SALLNLTRSVQELT---------------------EENQSLKEDLDRmLSNSPT------------------- 324
Cdd:pfam15921 489 MTlesseRTVSDLTASLQEKEraieatnaeitklrsrvdlklQELQHLKNEGDH-LRNVQTecealklqmaekdkvieil 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 325 ------ISKIKGYGDWSKPRLLRRIAELEKKVSSSESPKQSTSELVNPN-----PLVRSPSNISVQKQPKGDQSPEDLPK 393
Cdd:pfam15921 568 rqqienMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKdakirELEARVSDLELEKVKLVNAGSERLRA 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 394 VAPC-EEQEHLQGTVKSLREELGALQE--QLLEKDLEMK-------------QLLQSKIDLEKELETAREGEK------- 450
Cdd:pfam15921 648 VKDIkQERDQLLNEVKTSRNELNSLSEdyEVLKRNFRNKseemetttnklkmQLKSAQSELEQTRNTLKSMEGsdghamk 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 451 ---GRQEQEQALREEVEALTKKCQELEEAK----------REEKNSF-------------------VAVTHEKR------ 492
Cdd:pfam15921 728 vamGMQKQITAKRGQIDALQSKIQFLEEAMtnankekhflKEEKNKLsqelstvateknkmageleVLRSQERRlkekva 807
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 493 --EAALDEAAtvLQAA------FRGHLARSKLVRSKVPDSRSPSLPGLLSplnQSSPAPRVLSPISPAEENPTqeeaviv 564
Cdd:pfam15921 808 nmEVALDKAS--LQFAecqdiiQRQEQESVRLKLQHTLDVKELQGPGYTS---NSSMKPRLLQPASFTRTHSN------- 875
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 565 iqsilrgylaqarfiasccreiaASSQRETVSLTPSGSASPPSLRASPGVIRKELCasEELRETSASEPAPSVPYSAQGG 644
Cdd:pfam15921 876 -----------------------VPSSQSTASFLSHHSRKTNALKEDPTRDLKQLL--QELRSVINEEPTVQLSKAEDKG 930
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1907166730 645 HG-------DCPSSSSLEAvpSMKDAMCEERSSSPRSAGPSLAE 681
Cdd:pfam15921 931 RApslgaldDRVRDCIIES--SLRSDICHSSSNSLQTEGSKSSE 972
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
194-476 |
3.34e-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: 50.83 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 194 GPDFVRTLAEKKPDTGwvITGLKQRIFRLEQQCKEKDNTINKLQTdmkttNLEEMRIAMETYYEEIHRLQTLLASSEatg 273
Cdd:TIGR02168 656 RPGGVITGGSAKTNSS--ILERRREIEELEEKIEELEEKIAELEK-----ALAELRKELEELEEELEQLRKELEELS--- 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 274 KKPMVEKKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISkikgygdwskpRLLRRIAELEKKVS-S 352
Cdd:TIGR02168 726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA-----------EAEAEIEELEAQIEqL 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 353 SESPKQSTSELVNPNPLVRSpSNISVQKQPKGDQSPEDlpKVAPCEEQ--------EHLQGTVKSLREELGALQEQLLEK 424
Cdd:TIGR02168 795 KEELKALREALDELRAELTL-LNEEAANLRERLESLER--RIAATERRledleeqiEELSEDIESLAAEIEELEELIEEL 871
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1907166730 425 DLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEA 476
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
215-503 |
3.66e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 215 LKQRIFRLEQQC------KEKDNTINKLQTDMKTTNLEEMRIAMETYYEEIHRLQTLLAssEATGKKPMVEKKLGVKRqk 288
Cdd:TIGR02168 198 LERQLKSLERQAekaeryKELKAELRELELALLVLRLEELREELEELQEELKEAEEELE--ELTAELQELEEKLEELR-- 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 289 kmsSALLNLTRSVQELTEENQSLKEDLDRmlsnsptiskikgygdwskprLLRRIAELEKKVSSsespkqstselvnpnp 368
Cdd:TIGR02168 274 ---LEVSELEEEIEELQKELYALANEISR---------------------LEQQKQILRERLAN---------------- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 369 LVRSPSNISVQKQPKGDQSPEDLPKVAPCEEQehlqgtVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREG 448
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEK------LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1907166730 449 EKGRQEQEQALREEVEALTKKCQELEEAKREEKNSFVAVTHEKREAALDEAATVL 503
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL 442
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
398-523 |
3.76e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.77 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 398 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQL------LQSKID-----------------LEKELETAREGEKGRQE 454
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLeleieeVEARIKkyeeqlgnvrnnkeyeaLQKEIESLKRRISDLED 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907166730 455 QEQALREEVEALTKKCQELEEAKREEKNSFvavthEKREAALDEAATVLQAAFRGHLARSKLVRSKVPD 523
Cdd:COG1579 111 EILELMERIEELEEELAELEAELAELEAEL-----EEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
398-506 |
7.50e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 7.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 398 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 477
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
90 100
....*....|....*....|....*....
gi 1907166730 478 REEKNSFVAVTHEKREAALDEAATVLQAA 506
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
398-506 |
7.96e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 7.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 398 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKkcQELEEAK 477
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR--AAAELAA 400
|
90 100
....*....|....*....|....*....
gi 1907166730 478 REEKNSFVAVTHEKREAALDEAATVLQAA 506
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEA 429
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
381-479 |
1.19e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 48.70 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 381 QPKGDQSPEDLPKVAPCEEQEH------LQGTVKSLREELGALQEQLLEKDLEMKqllqskiDLEKELETAR--EGEKGR 452
Cdd:COG2433 390 LPEEEPEAEREKEHEERELTEEeeeirrLEEQVERLEAEVEELEAELEEKDERIE-------RLERELSEARseERREIR 462
|
90 100
....*....|....*....|....*...
gi 1907166730 453 QEQE-QALREEVEALTKKCQELEEAKRE 479
Cdd:COG2433 463 KDREiSRLDREIERLERELEEERERIEE 490
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
398-506 |
1.84e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 398 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 477
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
90 100
....*....|....*....|....*....
gi 1907166730 478 REEKNSFVAVTHEKREAALDEAATVLQAA 506
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEE 410
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
398-494 |
5.94e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 5.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 398 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 477
Cdd:COG4372 59 EELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQI 138
|
90
....*....|....*..
gi 1907166730 478 REEKNSFVAVTHEKREA 494
Cdd:COG4372 139 AELQSEIAEREEELKEL 155
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
141-501 |
6.08e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 141 REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpsRGPDFVRTLAEKKPDTGWV---ITGLKQ 217
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELED--RDEELRDRLEECRVAAQAHneeAESLRE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 218 RIFRLEQQCKEKDNTINKLQTDmkttnLEEMRIAMETYYEEIHRLQTLLASSEAtgkkpmvekklgvkrqkkmssALLNL 297
Cdd:PRK02224 350 DADDLEERAEELREEAAELESE-----LEEAREAVEDRREEIEELEEEIEELRE---------------------RFGDA 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 298 TRSVQELTEENQSLKEDLDRmlsnsptiskikgygdwskprLLRRIAELEKKVSSSESPKQSTSELVNPNplvrspsnis 377
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDE---------------------LREREAELEATLRTARERVEEAEALLEAG---------- 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 378 vqKQPKGDQSPEDLPKVAPCEEQEhlqGTVKSLREELGALQEQL--LEKDLE-----------MKQLLQSKIDLEKELET 444
Cdd:PRK02224 453 --KCPECGQPVEGSPHVETIEEDR---ERVEELEAELEDLEEEVeeVEERLEraedlveaedrIERLEERREDLEELIAE 527
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907166730 445 AREGEKGRQEQEQALREEVEALTKKCQELEEAKREEknsfvavtHEKREAALDEAAT 501
Cdd:PRK02224 528 RRETIEEKRERAEELRERAAELEAEAEEKREAAAEA--------EEEAEEAREEVAE 576
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
141-466 |
8.28e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.97 E-value: 8.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 141 REKEDMYDEIIELKKSLHMQKSDVDlmrTKLRRLEEENSRKDRQIEQLLDPSRGPDfvRTLAEKKPDTGWVITGLKQRIF 220
Cdd:pfam10174 411 RDKDKQLAGLKERVKSLQTDSSNTD---TALTTLEEALSEKERIIERLKEQRERED--RERLEELESLKKENKDLKEKVS 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 221 RLEQQCKEKDNTINKLQTDM---------KTTNLEEMRIAMETYYEEIHRLQTLLASSEatgkkpmvEKKLGVKRQKKMS 291
Cdd:pfam10174 486 ALQPELTEKESSLIDLKEHAsslassglkKDSKLKSLEIAVEQKKEECSKLENQLKKAH--------NAEEAVRTNPEIN 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 292 SALLNLTRSVQELTEENQSLKEDLDRML-----SNSPTISKIKGYGDWSKpRLLRRIAELEKKVSS-----SESPKQSTS 361
Cdd:pfam10174 558 DRIRLLEQEVARYKEESGKAQAEVERLLgilreVENEKNDKDKKIAELES-LTLRQMKEQNKKVANikhgqQEMKKKGAQ 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 362 ELVNPNPLVRSPSNISVQKQPkgdqspEDLPKVAPCEEQE------HLQGTVKSLREELGAL------QEQLLEKDLEMK 429
Cdd:pfam10174 637 LLEEARRREDNLADNSQQLQL------EELMGALEKTRQEldatkaRLSSTQQSLAEKDGHLtnlraeRRKQLEEILEMK 710
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1907166730 430 Q-LLQSKIDlEKE-----LETAREGEKGRQEQEQALREEVEAL 466
Cdd:pfam10174 711 QeALLAAIS-EKDanialLELSSSKKKKTQEEVMALKREKDRL 752
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
407-515 |
8.68e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 8.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 407 VKSLREELGALQEQL--LEK-DLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKREEKNS 483
Cdd:COG4913 663 VASAEREIAELEAELerLDAsSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
90 100 110
....*....|....*....|....*....|....*..
gi 1907166730 484 FVAVTHEK-----REAALDEAATVLQAAFRGHLARSK 515
Cdd:COG4913 743 ARLELRALleerfAAALGDAVERELRENLEERIDALR 779
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
134-493 |
9.45e-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: 45.83 E-value: 9.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 134 VSGTSVY-REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEqLLDPSRGPDFVRTLAEKK------- 205
Cdd:TIGR02169 162 IAGVAEFdRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQA-LLKEKREYEGYELLKEKEalerqke 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 206 ------PDTGWVITGLKQRIFRLEQQCKEKDNTINKLQTDMKTTNLEEMRiameTYYEEIHRLQTLLASSEATGKKPMVE 279
Cdd:TIGR02169 241 aierqlASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL----RVKEKIGELEAEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 280 KKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNspTISKIKGYGDwskprLLRRIAELEKK----VSSSES 355
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEE--YAELKEELED-----LRAELEEVDKEfaetRDELKD 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 356 PKQSTSELVNP-NPLVRSPSNISVQKQPKGdqspedlpkvapcEEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQS 434
Cdd:TIGR02169 390 YREKLEKLKREiNELKRELDRLQEELQRLS-------------EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWK 456
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907166730 435 KIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELE---EAKREEKNSFVAVTHEKRE 493
Cdd:TIGR02169 457 LEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEaqaRASEERVRGGRAVEEVLKA 518
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
147-482 |
9.87e-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: 45.82 E-value: 9.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 147 YDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpsrgpdFVRTLAEKKPDTGWVITGLKQRIFRLEQQC 226
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL------EVSELEEEIEELQKELYALANEISRLEQQK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 227 KEKDNTINKLQTDMKTTN--LEEMRIAMETYYEEIHRLQTLLASSEatgkkpmVEKKLGVKRQKKMSSALLNLTRSVQEL 304
Cdd:TIGR02168 305 QILRERLANLERQLEELEaqLEELESKLDELAEELAELEEKLEELK-------EELESLEAELEELEAELEELESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 305 TEENQSLKEDLDRMLSNSPTISKikgygdwskprllrRIAELEKKVSSSESpkqstselvnpnplvrspsnisvqKQPKG 384
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNN--------------EIERLEARLERLED------------------------RRERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 385 DQSPEDLPKVAPCEEQEHLQGTVKSLREELGALQEQLlekdlemKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVE 464
Cdd:TIGR02168 420 QQEIEELLKKLEEAELKELQAELEELEEELEELQEEL-------ERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
|
330
....*....|....*...
gi 1907166730 465 ALTKKCQELEEAKREEKN 482
Cdd:TIGR02168 493 SLERLQENLEGFSEGVKA 510
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
398-506 |
1.01e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 398 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 477
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
90 100
....*....|....*....|....*....
gi 1907166730 478 REEKNSFVAVTHEKREAALDEAATVLQAA 506
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELE 382
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
338-487 |
1.38e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 338 RLLRRIAELEKKVSSSESPKQSTSELVNPNPLVRSPSNISVQKQPKGDQSPEDLPKVAP----CEEQEHLQGTVKSLREE 413
Cdd:COG4717 99 ELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEElrelEEELEELEAELAELQEE 178
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907166730 414 LGALQEQL-LEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKREEKNSFVAV 487
Cdd:COG4717 179 LEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL 253
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
398-506 |
1.96e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 398 EEQEHLQGTV-----KSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQE 472
Cdd:COG1196 220 EELKELEAELlllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299
|
90 100 110
....*....|....*....|....*....|....*.
gi 1907166730 473 LEEAKR--EEKNSFVAVTHEKREAALDEAATVLQAA 506
Cdd:COG1196 300 LEQDIArlEERRRELEERLEELEEELAELEEELEEL 335
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
398-508 |
2.98e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 398 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEE-- 475
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEErl 318
|
90 100 110
....*....|....*....|....*....|....*.
gi 1907166730 476 ---AKREEKNSFVAVTHEKREAALDEAATVLQAAFR 508
Cdd:COG1196 319 eelEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
|
| IQCD |
cd23767 |
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ... |
490-520 |
3.02e-04 |
|
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.
Pssm-ID: 467745 [Multi-domain] Cd Length: 37 Bit Score: 38.68 E-value: 3.02e-04
10 20 30
....*....|....*....|....*....|.
gi 1907166730 490 EKREAALDEAATVLQAAFRGHLARSKLVRSK 520
Cdd:cd23767 2 EEELQRMNRAATLIQALWRGYKVRKELKKKK 32
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
212-483 |
3.28e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 212 ITGLKQRIFRLEQQCKEKDNTINKLQTDMKTTNLEEmriamETYYEEIHRLQTLLASSEATGKKPMVEKKLGVKRQKKMS 291
Cdd:TIGR04523 77 IKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEI-----KNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 292 SALLNLTRSVQELTEENQSLKEDLDRMLSNsptISKIKGYGDWSKPRLLRriaeLEKKVSSSESPKQSTSELVNP-NPLV 370
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKE---KLNIQKNIDKIKNKLLK----LELLLSNLKKKIQKNKSLESQiSELK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 371 RSPSNISVQKQPKGDQSPEDLPKVAPCEEQehlqgtVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAR-EGE 449
Cdd:TIGR04523 225 KQNNQLKDNIEKKQQEINEKTTEISNTQTQ------LNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKsEIS 298
|
250 260 270
....*....|....*....|....*....|....*
gi 1907166730 450 KGRQEQEQALREEV-EALTKKCQELEEAKREEKNS 483
Cdd:TIGR04523 299 DLNNQKEQDWNKELkSELKNQEKKLEEIQNQISQN 333
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
141-481 |
3.86e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.86 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 141 REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPsrgpdfVRTLAEKKPDTGWVITGLKQRIF 220
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNE------IEKLKKENQSYKQEIKNLESQIN 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 221 RLEQQCKEKDNTINKLQTDMKTTNLEEmriamETYYEEIHRLQTLLASSEATGK---KPMVEKKLGVKRqkkmssalLNL 297
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKDEQIKKLQQEK-----ELLEKEIERLKETIIKNNSEIKdltNQDSVKELIIKN--------LDN 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 298 TRSVQElteenQSLKEdldrmLSNSptISKIKGYGDWSKprllrriAELEKKVSSSESPKQSTSELVNPNPLVRSPSNIS 377
Cdd:TIGR04523 462 TRESLE-----TQLKV-----LSRS--INKIKQNLEQKQ-------KELKSKEKELKKLNEEKKELEEKVKDLTKKISSL 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 378 VQKQpkgdqspEDLPKVAPCEEQE--HLQGTVKSLREEL--GALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQ 453
Cdd:TIGR04523 523 KEKI-------EKLESEKKEKESKisDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKE 595
|
330 340 350
....*....|....*....|....*....|..
gi 1907166730 454 EQEQALREEVEALTKKC----QELEEAKREEK 481
Cdd:TIGR04523 596 KEKKDLIKEIEEKEKKIssleKELEKAKKENE 627
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
427-521 |
5.34e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 427 EMKQLLQSKIDLEKELETA-REGEKGRQEQEQALREEVEALTKKCQELEEAKREEKNSFVAVTH-----EKREAALDEAA 500
Cdd:COG0542 412 ELDELERRLEQLEIEKEALkKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQElkeelEQRYGKIPELE 491
|
90 100
....*....|....*....|.
gi 1907166730 501 TVLQAAFRGHLARSKLVRSKV 521
Cdd:COG0542 492 KELAELEEELAELAPLLREEV 512
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
140-529 |
5.77e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 140 YREKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLD--PSRGPDFVRTLAEKkpdtgwvITGLKQ 217
Cdd:COG4717 134 LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEqlSLATEEELQDLAEE-------LEELQQ 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 218 RIFRLEQQCKEKDNTINKLQTDMKTTNLEEMRIAMETYYEEIHRLQTLLA-----SSEATGKKPMVEKKLGV-------- 284
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAallalLGLGGSLLSLILTIAGVlflvlgll 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 285 -------KRQKKMSSALLNLTRSVQELTE-ENQSLKEDLDR-MLSNSPTISKIKGYGDW--SKPRLLRRIAELEKKVSSS 353
Cdd:COG4717 287 allflllAREKASLGKEAEELQALPALEElEEEELEELLAAlGLPPDLSPEELLELLDRieELQELLREAEELEEELQLE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 354 ESPKQSTSELvnpnplvrspsnisvqkQPKGDQSPEDLpkVAPCEEQEHLQgtvkSLREELGALQEQLLEKDLEMKQLLQ 433
Cdd:COG4717 367 ELEQEIAALL-----------------AEAGVEDEEEL--RAALEQAEEYQ----ELKEELEELEEQLEELLGELEELLE 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 434 --SKIDLEKELETAregekgrQEQEQALREEVEALTKKCQELEEAKRE-EKNSFVAVTHEKREAALDEAATVLQAAFRGH 510
Cdd:COG4717 424 alDEEELEEELEEL-------EEELEELEEELEELREELAELEAELEQlEEDGELAELLQELEELKAELRELAEEWAALK 496
|
410 420
....*....|....*....|.
gi 1907166730 511 LARSKL--VRSKVPDSRSPSL 529
Cdd:COG4717 497 LALELLeeAREEYREERLPPV 517
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
168-515 |
7.44e-04 |
|
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: 43.03 E-value: 7.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 168 RTKLRRLEEENSRKDRQIEQLLDPSRGpdfvRTLAEKKPDTGWVITGLKQ-------RIFRLEQ-QCKE--KDNTINKLQ 237
Cdd:TIGR00618 92 RTLRCTRSHRKTEQPEQLYLEQKKGRG----RILAAKKSETEEVIHDLLKldyktftRVVLLPQgEFAQflKAKSKEKKE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 238 TDMKTTNLEEMR-IAMETYyeEIHRlqTLLASSEATGKKPMVEKKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEdld 316
Cdd:TIGR00618 168 LLMNLFPLDQYTqLALMEF--AKKK--SLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQ--- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 317 rmlsnsptiskikgygdwSKPRLLRRIAELEKKVSSSESPKQSTSELVNPNPLVRSPSNisvqKQPKGDQSPEDLP---- 392
Cdd:TIGR00618 241 ------------------SHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEE----TQERINRARKAAPlaah 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 393 --KVAPCEEQEH-----LQGTVKSLREEL---GALQEQLLEKDlEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREE 462
Cdd:TIGR00618 299 ikAVTQIEQQAQrihteLQSKMRSRAKLLmkrAAHVKQQSSIE-EQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTL 377
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1907166730 463 VEALTKKCQELEEAKREEKNSFVAVTHEKREAALDEAATVLQAAFRGHLARSK 515
Cdd:TIGR00618 378 TQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAK 430
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
398-506 |
8.35e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 8.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 398 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQL-------------LQSKI-DLEKELETAREGEKGRQEQEQALREEV 463
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSELeeeieelqkelyaLANEIsRLEQQKQILRERLANLERQLEELEAQL 325
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1907166730 464 EALTKKCQELEE--AKREEKNSFVAVTHEKREAALDEAATVLQAA 506
Cdd:TIGR02168 326 EELESKLDELAEelAELEEKLEELKEELESLEAELEELEAELEEL 370
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
143-479 |
1.02e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 143 KEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQL-----------LDPSRGPDFVRTLAEKKPDTGWV 211
Cdd:PRK03918 188 TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELeelkeeieeleKELESLEGSKRKLEEKIRELEER 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 212 ITGLKQRIFRLEQQCKEkdntINKLQTDMKTtnLEEMRIAMETYYEEIHRLQTLLASSEATGKKpmVEKKLgvKRQKKMS 291
Cdd:PRK03918 268 IEELKKEIEELEEKVKE----LKELKEKAEE--YIKLSEFYEEYLDELREIEKRLSRLEEEING--IEERI--KELEEKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 292 SALLNLTRSVQELTEENQSLKED---LDRMLSNSPTISKIKG-YGDWSKPRLLRRIAELEK-KVSSSESPKQSTSELVNP 366
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERhelYEEAKAKKEELERLKKrLTGLTPEKLEKELEELEKaKEEIEEEISKITARIGEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 367 NPLVRS-PSNISVQKQPKGdqspedlpKVAPCE---EQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKEL 442
Cdd:PRK03918 418 KKEIKElKKAIEELKKAKG--------KCPVCGrelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVL 489
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1907166730 443 ETAREGEKGRQ--EQEQALREE-----VEALTKKCQELEEAKRE 479
Cdd:PRK03918 490 KKESELIKLKElaEQLKELEEKlkkynLEELEKKAEEYEKLKEK 533
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
279-505 |
1.30e-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: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 279 EKKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISKIKGYGDwskprLLRRIAELEkkvsssespkq 358
Cdd:COG3206 213 EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ-----LRAQLAELE----------- 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 359 stselvnpnplvrspSNISVQKQPKGDQSPEdlpkvapceeqehlqgtVKSLREELGALQEQLLEkdlEMKQLLQSkidL 438
Cdd:COG3206 277 ---------------AELAELSARYTPNHPD-----------------VIALRAQIAALRAQLQQ---EAQRILAS---L 318
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 439 EKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKRE---EKNSFVAVTHEKREAALDEAATVLQA 505
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREvevARELYESLLQRLEEARLAEALTVGNV 388
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
403-513 |
1.38e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 403 LQGTVKSLREELGALQEQL--LEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKREe 480
Cdd:COG4717 93 LQEELEELEEELEELEAELeeLREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE- 171
|
90 100 110
....*....|....*....|....*....|...
gi 1907166730 481 knsfvavtHEKREAALDEAATVLQAAFRGHLAR 513
Cdd:COG4717 172 --------LAELQEELEELLEQLSLATEEELQD 196
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
141-484 |
1.72e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 141 REKEDMYDEIielkKSLHMQKSDvdlMRTKLRRLEEENSRKDRQIEQLLDPSRgpdfvrtLAEKKpdtgwvITGLKQRIF 220
Cdd:TIGR04523 377 KENQSYKQEI----KNLESQIND---LESKIQNQEKLNQQKDEQIKKLQQEKE-------LLEKE------IERLKETII 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 221 RLEQQCKEKDNTINKLQTDMKttNLEEMRIAMETYYEEIHRlqtllasSEATGKKPMVEKKLGVKRQKKMssaLLNLTRS 300
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIK--NLDNTRESLETQLKVLSR-------SINKIKQNLEQKQKELKSKEKE---LKKLNEE 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 301 VQELTEENQSLKEDldrmlsNSPTISKIKgygdwskpRLLRRIAELEKKVSSSESPKQSTSELVNPNPLVRSPSNISvQK 380
Cdd:TIGR04523 505 KKELEEKVKDLTKK------ISSLKEKIE--------KLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKN-KE 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 381 QPKGDQSPEDLPKvapceEQEHLQGTVKSLREELGALQEQLLEKDlemkqllQSKIDLEKELETAREGEKGRQEQEQALR 460
Cdd:TIGR04523 570 IEELKQTQKSLKK-----KQEEKQELIDQKEKEKKDLIKEIEEKE-------KKISSLEKELEKAKKENEKLSSIIKNIK 637
|
330 340
....*....|....*....|....
gi 1907166730 461 EEVEALTKKCQELEEAKREEKNSF 484
Cdd:TIGR04523 638 SKKNKLKQEVKQIKETIKEIRNKW 661
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
220-428 |
2.07e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 41.38 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 220 FRLEQQCKEKDNTINKLQTDMKTTNLEEMRIAMETYYEEIHRLQTLL-ASSEAtgkKPMVEKKLGvkrqkkmssallNLT 298
Cdd:pfam06160 233 LNVDKEIQQLEEQLEENLALLENLELDEAEEALEEIEERIDQLYDLLeKEVDA---KKYVEKNLP------------EIE 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 299 RSVQELTEENQSLKEDLDRM-----LSNSpTISKIKGYGDWSKpRLLRRIAELEKKVsssESPKQSTSELvnpnplvrsp 373
Cdd:pfam06160 298 DYLEHAEEQNKELKEELERVqqsytLNEN-ELERVRGLEKQLE-ELEKRYDEIVERL---EEKEVAYSEL---------- 362
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907166730 374 snISVQKQPKgdqspEDLPKVApcEEQEHLQGTVKSLREELGALQEQLLEKDLEM 428
Cdd:pfam06160 363 --QEELEEIL-----EQLEEIE--EEQEEFKESLQSLRKDELEAREKLDEFKLEL 408
|
|
| IQ |
smart00015 |
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
496-516 |
2.65e-03 |
|
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.
Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 35.76 E-value: 2.65e-03
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
401-506 |
3.70e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 401 EHLQGTVKSLREELGALQEQLLEKDLEMKQlLQSKIDLEKELETAREGE---KGRQEQEQALREEVEALTKKCQELEEAK 477
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDA-LQERREALQRLAEYSWDEidvASAEREIAELEAELERLDASSDDLAALE 691
|
90 100
....*....|....*....|....*....
gi 1907166730 478 REEknsfvavthEKREAALDEAATVLQAA 506
Cdd:COG4913 692 EQL---------EELEAELEELEEELDEL 711
|
|
| IQ |
pfam00612 |
IQ calmodulin-binding motif; Calmodulin-binding motif. |
498-516 |
5.06e-03 |
|
IQ calmodulin-binding motif; Calmodulin-binding motif.
Pssm-ID: 459869 Cd Length: 21 Bit Score: 34.99 E-value: 5.06e-03
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
398-505 |
5.39e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 398 EEQEHLQGTVKSLREELGAL--QEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQ---ALREEVEALTKKCQE 472
Cdd:COG4717 102 EELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEeleELEAELAELQEELEE 181
|
90 100 110
....*....|....*....|....*....|...
gi 1907166730 473 LEEAKREEKNSFVAVTHEKREAALDEAATVLQA 505
Cdd:COG4717 182 LLEQLSLATEEELQDLAEELEELQQRLAELEEE 214
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
336-481 |
5.53e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.11 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 336 KPRLLRRIAELEKKvssSESPKQSTSELVNPNPLVRSPSNISVQKQPKGDQSPEDL--PKVAPCEEQEHLQGTVKSLREE 413
Cdd:pfam17380 346 RERELERIRQEERK---RELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELeaARKVKILEEERQRKIQQQKVEM 422
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907166730 414 LGALQEQLLEKDLEMKQLLQSKidlEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKREEK 481
Cdd:pfam17380 423 EQIRAEQEEARQREVRRLEEER---AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRK 487
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
296-477 |
5.90e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 296 NLTRSVQELTEENQSLKEDLDrmlsnspTISKIKGYGDWSKPRLLRRIAELEKKVSSSESPKQSTSELVNPNPL-VRSPS 374
Cdd:pfam01576 374 NLEKAKQALESENAELQAELR-------TLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSeLESVS 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 375 NISVQKQPKGDQSPEDLPKVAPC--EEQEHLQ----------GTVKSLREELGALQEQL---------LEKDLEM--KQL 431
Cdd:pfam01576 447 SLLNEAEGKNIKLSKDVSSLESQlqDTQELLQeetrqklnlsTRLRQLEDERNSLQEQLeeeeeakrnVERQLSTlqAQL 526
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907166730 432 LQSKIDLEKELETAREGEKGRQEqeqaLREEVEALTKKCQELEEAK 477
Cdd:pfam01576 527 SDMKKKLEEDAGTLEALEEGKKR----LQRELEALTQQLEEKAAAY 568
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
399-476 |
6.20e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 6.20e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907166730 399 EQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAregekgrQEQEQALREEVEALTKKCQELEEA 476
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL-------QAEIDKLQAEIAEAEAEIEERREE 87
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
142-477 |
6.46e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 39.81 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 142 EKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQL--------LDPSRGPDFVRTLAEKKPDTGWVIT 213
Cdd:pfam10174 374 EKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLkervkslqTDSSNTDTALTTLEEALSEKERIIE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 214 GLKQRIFRLEQQCKEKDNTINKLQTDMKTTnLEEMRIAMETYYEEIHRLQTLlASSEATGkkpmvekklGVKRQKKMSSA 293
Cdd:pfam10174 454 RLKEQREREDRERLEELESLKKENKDLKEK-VSALQPELTEKESSLIDLKEH-ASSLASS---------GLKKDSKLKSL 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 294 LLNLTRSVQELTE-ENQSLK----EDLDRMlsnsptiskikgygdwsKPRLLRRIAELEKKVSS-SESPKQSTSELVNPN 367
Cdd:pfam10174 523 EIAVEQKKEECSKlENQLKKahnaEEAVRT-----------------NPEINDRIRLLEQEVARyKEESGKAQAEVERLL 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 368 PLVRSPSNisvQKQPKgDQSPEDLPKVAP--CEEQEHLQGTVKSLREELGALQEQLLEKDLEmkqllqskidlekeleta 445
Cdd:pfam10174 586 GILREVEN---EKNDK-DKKIAELESLTLrqMKEQNKKVANIKHGQQEMKKKGAQLLEEARR------------------ 643
|
330 340 350
....*....|....*....|....*....|..
gi 1907166730 446 REGEKGRQEQEQALREEVEALTKKCQELEEAK 477
Cdd:pfam10174 644 REDNLADNSQQLQLEELMGALEKTRQELDATK 675
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
216-494 |
7.42e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.67 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 216 KQRIFRLEQQCKEKDNTINKLQTDmkttnleemRIAMETYYEEIHRLQTLLASSEATGKKPMVEKKLGVKRQkkmssaLL 295
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRRE---------REKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQ------LA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 296 NLTRSVQELTEENQSLKEDLDRMLSNSPTIS-KIKGYGDWSKPRLLRRIAELEKKVSSSESP--------KQSTSELVNP 366
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKRLEEIEQLLEELNkKIKDLGEEEQLRVKEKIGELEAEIASLERSiaekerelEDAEERLAKL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 367 NPLVRSpsnisvqKQPKGDQSPEDLPKVApcEEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAR 446
Cdd:TIGR02169 328 EAEIDK-------LLAEIEELEREIEEER--KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK 398
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1907166730 447 EGEKGRQEQEQALREEVEALTKKCQELE---EAKREEKNSFVAVTHEKREA 494
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNaaiAGIEAKINELEEEKEDKALE 449
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
418-504 |
7.63e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.81 E-value: 7.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166730 418 QEQLLEKDLEMKQLLQSKIDLEKELET-AREGEKGRQEQEQaLREEVEaltKKCQELEEAKREEKNSFVAVTHEKREAAL 496
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQkAEEAEALLKEAEK-LKEELE---EKKEKLQEEEDKLLEEAEKEAQQAIKEAK 583
|
....*...
gi 1907166730 497 DEAATVLQ 504
Cdd:PRK00409 584 KEADEIIK 591
|
|
| |
