|
Name |
Accession |
Description |
Interval |
E-value |
| C2-C2_1 |
pfam11618 |
First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 ... |
597-738 |
1.32e-77 |
|
First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 domain on X-linked retinitis pigmentosa GTPase regulator-interacting proteins, or RPGR-interacting proteins.
Pssm-ID: 463310 Cd Length: 143 Bit Score: 252.17 E-value: 1.32e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 597 TIHLERGENLFEIHINKVTFSSEVLQASGDKEPVTFCTYAFYDFELQTTPVVRGLHPEYNFTSQYLVHVNDLFLQYIQKN 676
Cdd:pfam11618 1 TVELERGENLFELHIGGVTFSPEALRALGDKEPSTFCTYDFYDFETQTTPVVRGLNPFYDFTSQYKVTVDDLFLQYLQTN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 816197642 677 TITLEVHQAYSTEYETIAACQLKFHEILEK-SGRIFCTASLIGTKGDIPNFGTVEYWFRLRVP 738
Cdd:pfam11618 81 SLTLELHQALGVDFKTLAAAQLRLHGLLEDrGGRIHGTVTLTGVEGEIQIIGTLEYWIRLRVP 143
|
|
| RPGR1_C |
pfam18111 |
Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain ... |
1099-1262 |
7.25e-71 |
|
Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain of retinitis pigmentosa G-protein regulator (RPGR) interacting protein-1 present in Homo sapiens. A mutation in RPGR interacting protein-1 can be observed in the eye disease Leber congenital amaurosis. The domain is commonly known as the RPGR-interacting domain (RID) and is thought to have a C2-like fold.
Pssm-ID: 465655 Cd Length: 166 Bit Score: 233.85 E-value: 7.25e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 1099 PSEKIRIEIIALSL-NDSQVTMDDTIQRLFVECRFYSLPAE--ETPVSLPKPKSGQWVYYNYSNVIYVDKENNKAKRDIL 1175
Cdd:pfam18111 1 DSDTIRIEIISLQLlNESEVMQDDNIQQLFVEYRFLGRPEEetETPVSLPKPKTGQELYYNFSKVIDVDKEKNSARREIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 1176 KAILQKQEMPNRSLRFTVVSDPPeDEQDLECEDIGVAHVDLADMFQEGRDLIEQNIDVFDARADGEGIGKLRVTVEALHA 1255
Cdd:pfam18111 81 RSMLLPEDPNQGNLKFTVVSEPL-DTEDGECEEIGYAYVDLKQILQSGRDIIEQDLDVKDARDENEQIGKLKVSVEALAA 159
|
....*..
gi 816197642 1256 LQSVYKQ 1262
Cdd:pfam18111 160 LRAIYSE 166
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
201-543 |
4.96e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.83 E-value: 4.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEI------LKTQLRRKEneIELSLLQLREQQATDQRsnirdnvemikLHKQ 274
Cdd:COG1196 181 LEATEENLERLEDILGELERQLEPLERQAEKaeryreLKEELKELE--AELLLLKLRELEAELEE-----------LEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 275 LVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHS----MKFSERRIEELQDRIND 350
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARleerRRELEERLEELEEELAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 351 LEKERELLKENYDKLydsafsAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQ 430
Cdd:COG1196 328 LEEELEELEEELEEL------EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 431 YLEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEIN------KDLERSMRELQATHAE 504
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEallellAELLEEAALLEAALAE 481
|
330 340 350
....*....|....*....|....*....|....*....
gi 816197642 505 TVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQD 543
Cdd:COG1196 482 LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
201-445 |
8.98e-16 |
|
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: 83.18 E-value: 8.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIElsllQLREQQATDQRSNIRDNVEMIKLHKQLVEKSN 280
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE----QLEERIAQLSKELTELEAEIEELEERLEEAEE 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 281 ALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKE-------QRLKCCSLEKQLHSmkfSERRIEELQDRINDLEK 353
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanLRERLESLERRIAA---TERRLEDLEEQIEELSE 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 354 ERELLKENYDKLydSAFSAAHEEQWKLKEQQLKVQIAQLEtALKSDLTDKTEILDRLKTERDQNEKLVQENRE----LQL 429
Cdd:TIGR02168 853 DIESLAAEIEEL--EELIEELESELEALLNERASLEEALA-LLRSELEELSEELRELESKRSELRRELEELREklaqLEL 929
|
250
....*....|....*.
gi 816197642 430 QYLEQKQQLDELKKRI 445
Cdd:TIGR02168 930 RLEGLEVRIDNLQERL 945
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
198-572 |
2.75e-15 |
|
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: 81.64 E-value: 2.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 198 NSLLEEARgEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIElsllqlreqqatdqrsnirdnvemiKLHKQLVE 277
Cdd:TIGR02168 670 SSILERRR-EIEELEEKIEELEEKIAELEKALAELRKELEELEEELE-------------------------QLRKELEE 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 278 KSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSmkfSERRIEELQDRINDLEKEREL 357
Cdd:TIGR02168 724 LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE---AEAEIEELEAQIEQLKEELKA 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 358 LKENYDKLydsafSAAHEEQwKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQ 437
Cdd:TIGR02168 801 LREALDEL-----RAELTLL-NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 438 LDELKKRIklynqendinaDELSEALLLIKAQKEQKNGDLsflvKVDSEINKDLERSMRELQATHAETVQELEKTRNMLI 517
Cdd:TIGR02168 875 LEALLNER-----------ASLEEALALLRSELEELSEEL----RELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 816197642 518 -MQHKINKDYQMEVEAVTRKMENLqQDYELKVEQyvhlldiraaRIHKLEAQLKDI 572
Cdd:TIGR02168 940 nLQERLSEEYSLTLEEAEALENKI-EDDEEEARR----------RLKRLENKIKEL 984
|
|
| C2 |
cd00030 |
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ... |
792-891 |
4.89e-13 |
|
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.
Pssm-ID: 175973 [Multi-domain] Cd Length: 102 Bit Score: 66.32 E-value: 4.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 792 LHITIRCCNHLQSRASHLQPHPYVVYKFFDFADHDTAIIPSSNDPQFDDHMYFPVPMNMdldrylkSESLSFYVFDDSDT 871
Cdd:cd00030 1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQKFKTKVVKNTLNPVWNETFEFPVLDPE-------SDTLTVEVWDKDRF 73
|
90 100
....*....|....*....|
gi 816197642 872 QENIYIGKVNVPLISLAHDR 891
Cdd:cd00030 74 SKDDFLGEVEIPLSELLDSG 93
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
106-492 |
1.53e-12 |
|
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: 72.40 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 106 VEMEEMIEQLQEKVHELEKQNETLKnrlisaKQQLQTQGYR--QTPYNNVQSRINTGRRKANenaglqecpRKGIKFQDA 183
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQLKSLE------RQAEKAERYKelKAELRELELALLVLRLEEL---------REELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 184 DVAETphpmftkygNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKT---QLRRKENEIELSLLQLREQQATDQRS 260
Cdd:TIGR02168 247 ELKEA---------EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKelyALANEISRLEQQKQILRERLANLERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 261 NIRDNVEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSER- 339
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAs 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 340 ---RIEELQDRINDLEKERELLKENydklydsafsaAHEEQWKLKEQQLKVQIAQLETaLKSDLTDKTEILDRLkteRDQ 416
Cdd:TIGR02168 398 lnnEIERLEARLERLEDRRERLQQE-----------IEELLKKLEEAELKELQAELEE-LEEELEELQEELERL---EEA 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 417 NEKLVQENRELQLQYLEQKQQLDELKKRIK-LYNQENdiNADELSEALLLIKAQKEQKNGD---LSFLVKVDSEINKDLE 492
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDsLERLQE--NLEGFSEGVKALLKNQSGLSGIlgvLSELISVDEGYEAAIE 540
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-498 |
1.83e-12 |
|
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: 72.40 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 101 RLGRDVEmeemIEQLQEKVHELEKQNETLKNRLISAKQQLQT---------QGYRQTPYNNVQSRINTGRRKANENAGLQ 171
Cdd:TIGR02168 672 ILERRRE----IEELEEKIEELEEKIAELEKALAELRKELEEleeeleqlrKELEELSRQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 172 ECPRKGIKFQDADVAETPHpmftkygNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENeiELSLLQLR 251
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEEL-------EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA--ELTLLNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 252 EQQATDQRSNIRDNVEMIK-----LHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRlkccs 326
Cdd:TIGR02168 819 AANLRERLESLERRIAATErrledLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR----- 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 327 lekqlhsmkfseRRIEELQDRINDLEKERELLKENYDKLydsafsAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEI 406
Cdd:TIGR02168 894 ------------SELEELSEELRELESKRSELRRELEEL------REKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE 955
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 407 LDRLkterdqneklvQENRELQLQYLEQKqqLDELKKRIKlynQENDINADELSEAlllikaqkEQKNGDLSFLVKVDSE 486
Cdd:TIGR02168 956 AEAL-----------ENKIEDDEEEARRR--LKRLENKIK---ELGPVNLAAIEEY--------EELKERYDFLTAQKED 1011
|
410
....*....|....*
gi 816197642 487 INK---DLERSMREL 498
Cdd:TIGR02168 1012 LTEakeTLEEAIEEI 1026
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
114-600 |
2.94e-11 |
|
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: 68.12 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 114 QLQEKVHELEKQNETLKNRLISAKQQLQTQgyrQTPYNNVQSRINTGRRKANEnaglqecprkgIKFQDADvaetphpmf 193
Cdd:TIGR04523 215 SLESQISELKKQNNQLKDNIEKKQQEINEK---TTEISNTQTQLNQLKDEQNK-----------IKKQLSE--------- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 194 tkyGNSLLEEARGEIRNLENVIQSQRGQIEEL-----EHLAEILKTQLRRKENEIELSLLQLRE-----QQATDQRSNIR 263
Cdd:TIGR04523 272 ---KQKELEQNNKKIKELEKQLNQLKSEISDLnnqkeQDWNKELKSELKNQEKKLEEIQNQISQnnkiiSQLNEQISQLK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 264 D-----NVEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDAL---MANGDELNmQLKEQRLKCCSLEKQLhsmk 335
Cdd:TIGR04523 349 KeltnsESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLeskIQNQEKLN-QQKDEQIKKLQQEKEL---- 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 336 fSERRIEELQDRINDLEKE-RELLKENYDK--LYDSAFSAAHEEQWKLKEqqLKVQIAQLETAL---KSDLTDKTEILDR 409
Cdd:TIGR04523 424 -LEKEIERLKETIIKNNSEiKDLTNQDSVKelIIKNLDNTRESLETQLKV--LSRSINKIKQNLeqkQKELKSKEKELKK 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 410 LKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRI--KLYNQENDINADELSEALLLIKAQKEQKNGDLSFLvkvdSEI 487
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKesKISDLEDELNKDDFELKKENLEKEIDEKNKEIEEL----KQT 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 488 NKDLERSMRELQathaETVQELEKTRNMLIMQHKInkdYQMEVEAVTRKMENLQQDYElKVEQYVHLLDIRAARIHKLEA 567
Cdd:TIGR04523 577 QKSLKKKQEEKQ----ELIDQKEKEKKDLIKEIEE---KEKKISSLEKELEKAKKENE-KLSSIIKNIKSKKNKLKQEVK 648
|
490 500 510
....*....|....*....|....*....|....*
gi 816197642 568 QLKDIAYGTKQYkfKPEIMPD--DSVDEFDETIHL 600
Cdd:TIGR04523 649 QIKETIKEIRNK--WPEIIKKikESKTKIDDIIEL 681
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
107-570 |
6.26e-11 |
|
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: 67.07 E-value: 6.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 107 EMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQGyrqtpyNNVQSRINTGRRKANENAGLQECprkgikfQDADVA 186
Cdd:pfam15921 257 KIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQA------NSIQSQLEIIQEQARNQNSMYMR-------QLSDLE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 187 ETphpmftkygnslLEEARGEIRNLENVIQSQrgqIEELEHLAEILKTQLRRKENEielsllqlrEQQATDQRSNIRDNV 266
Cdd:pfam15921 324 ST------------VSQLRSELREAKRMYEDK---IEELEKQLVLANSELTEARTE---------RDQFSQESGNLDDQL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 267 E--MIKLHKQlvEKSNALSAMEGKfiQLQEKQRTLRISHDALMANGDELNMQ-------LKEQRLKC-CSLEKQLHSMKF 336
Cdd:pfam15921 380 QklLADLHKR--EKELSLEKEQNK--RLWDRDTGNSITIDHLRRELDDRNMEvqrlealLKAMKSECqGQMERQMAAIQG 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 337 SERRIEELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQW------KLKEQQLKVQIAQLE-TALKSDLTDKTEILDR 409
Cdd:pfam15921 456 KNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTvsdltaSLQEKERAIEATNAEiTKLRSRVDLKLQELQH 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 410 LKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQENDINAdELSEALLLIKAQKEQKNGDLSFLVKvDSEINK 489
Cdd:pfam15921 536 LKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHG-RTAGAMQVEKAQLEKEINDRRLELQ-EFKILK 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 490 DLERS-MRELQATHAETvqELEKT--------RNMLIMQHKINKDYQM-EVEAVTRKMENLQQDYELKVEQYVHLLDIRA 559
Cdd:pfam15921 614 DKKDAkIRELEARVSDL--ELEKVklvnagseRLRAVKDIKQERDQLLnEVKTSRNELNSLSEDYEVLKRNFRNKSEEME 691
|
490
....*....|.
gi 816197642 560 ARIHKLEAQLK 570
Cdd:pfam15921 692 TTTNKLKMQLK 702
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
368-572 |
1.46e-10 |
|
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: 64.79 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 368 SAFSAAHEEQWKLKEQ--QLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRI 445
Cdd:COG4942 13 LAAAAQADAAAEAEAEleQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 446 KLYNQENDINADELSEalLLIKAQKEQKNGDLSFLVKVDS--------EINKDLERSMRELQATHAETVQELEKTRNMLI 517
Cdd:COG4942 93 AELRAELEAQKEELAE--LLRALYRLGRQPPLALLLSPEDfldavrrlQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 816197642 518 MQHKINKDYQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDI 572
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
201-512 |
1.56e-09 |
|
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: 62.78 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLR--EQQATDQRSNIRDNVEMI-----KLHK 273
Cdd:TIGR02169 697 LRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSslEQEIENVKSELKELEARIeeleeDLHK 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 274 qLVEKSNALSAMEG--KFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKqlhSMKFSERRIEELQDRINDL 351
Cdd:TIGR02169 777 -LEEALNDLEARLShsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEK---EIQELQEQRIDLKEQIKSI 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 352 EKERELLKenydklydsafsaAHEEQWKLKEQQLKVQIAQLETALKSdltdkteildrLKTERDQNEKlvqENRELQLQY 431
Cdd:TIGR02169 853 EKEIENLN-------------GKKEELEEELEELEAALRDLESRLGD-----------LKKERDELEA---QLRELERKI 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 432 LEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSfLVKVDSEINKdLERSMRELQATHAETVQELEK 511
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQR-VEEEIRALEPVNMLAIQEYEE 983
|
.
gi 816197642 512 T 512
Cdd:TIGR02169 984 V 984
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
39-572 |
1.82e-09 |
|
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: 62.44 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 39 RQAVSRVSRE---ELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLvndkkRYERVGGGPKRLGRDVEMEEMIEQL 115
Cdd:pfam15921 73 KEHIERVLEEyshQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEM-----QMERDAMADIRRRESQSQEDLRNQL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 116 QEKVHELEKQNETLKNRLISAKQQLQTQGYRQTPYNNVQSRINTGRRKANENAGlqecprKGIKFQDAdvaetphpMFTK 195
Cdd:pfam15921 148 QNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASG------KKIYEHDS--------MSTM 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 196 YGNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRK-----------------ENEIELSLLQLREQQATDQ 258
Cdd:pfam15921 214 HFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKielllqqhqdrieqlisEHEVEITGLTEKASSARSQ 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 259 RSNIRDNVEMIKlhkQLVEKSNA-----LSAMEGKFIQLQEKQRTL-RISHDALmangDELNMQL--KEQRLKCCSLEKQ 330
Cdd:pfam15921 294 ANSIQSQLEIIQ---EQARNQNSmymrqLSDLESTVSQLRSELREAkRMYEDKI----EELEKQLvlANSELTEARTERD 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 331 LHSMKfSERRIEELQDRINDL---EKERELLKENYDKLYD----SAFSAAHEEQwKLKEQQLKVQ-IAQLETALKSDLTD 402
Cdd:pfam15921 367 QFSQE-SGNLDDQLQKLLADLhkrEKELSLEKEQNKRLWDrdtgNSITIDHLRR-ELDDRNMEVQrLEALLKAMKSECQG 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 403 KTEilDRLKTERDQNEKLvQENRELQLQYLEQKQQL----DELK-KRIKLYNQENDINadELSEALLLIKAQKEQKNGDL 477
Cdd:pfam15921 445 QME--RQMAAIQGKNESL-EKVSSLTAQLESTKEMLrkvvEELTaKKMTLESSERTVS--DLTASLQEKERAIEATNAEI 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 478 SFL-VKVDSEIN-----KDLERSMRELQAT-HAETVQELEKTRNMLIMQHKINKDYQ-----------MEVEAVtrKMEN 539
Cdd:pfam15921 520 TKLrSRVDLKLQelqhlKNEGDHLRNVQTEcEALKLQMAEKDKVIEILRQQIENMTQlvgqhgrtagaMQVEKA--QLEK 597
|
570 580 590
....*....|....*....|....*....|...
gi 816197642 540 LQQDYELKVEQYVHLLDIRAARIHKLEAQLKDI 572
Cdd:pfam15921 598 EINDRRLELQEFKILKDKKDAKIRELEARVSDL 630
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
211-569 |
2.16e-09 |
|
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: 62.11 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 211 LENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQrsnirdnvemiKLHKQLVEKSNALSAMEGKFI 290
Cdd:pfam01576 73 LEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQ-----------KLQLEKVTTEAKIKKLEEDIL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 291 QLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSmkfSERRIEELQDRINDLEKERELLKENYDKLyDSAF 370
Cdd:pfam01576 142 LLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNK---HEAMISDLEERLKKEEKGRQELEKAKRKL-EGES 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 371 SAAHEEQWKLKEQ--QLKVQIAQLETALKSdltdkteILDRLKTERDQNEKLVQENRELQLQYLEQKQQLD-ELKKRIKL 447
Cdd:pfam01576 218 TDLQEQIAELQAQiaELRAQLAKKEEELQA-------ALARLEEETAQKNNALKKIRELEAQISELQEDLEsERAARNKA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 448 YNQENDINAD------ELSEALLLIKAQKE---QKNGDLSFLVKVDSEINKDLERSMRELQATHAETVQE---------- 508
Cdd:pfam01576 291 EKQRRDLGEElealktELEDTLDTTAAQQElrsKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEElteqleqakr 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 816197642 509 -----------LEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQL 569
Cdd:pfam01576 371 nkanlekakqaLESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSEL 442
|
|
| C2 |
smart00239 |
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ... |
792-887 |
2.28e-09 |
|
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.
Pssm-ID: 214577 [Multi-domain] Cd Length: 101 Bit Score: 55.96 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 792 LHITIRCCNHLQSRASHLQPHPYVVYKFFDFADHD--TAIIPSSNDPQFDDHMYFPVPmnmdldrYLKSESLSFYVFDDS 869
Cdd:smart00239 2 LTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKkkTKVVKNTLNPVWNETFEFEVP-------PPELAELEIEVYDKD 74
|
90
....*....|....*...
gi 816197642 870 DTQENIYIGKVNVPLISL 887
Cdd:smart00239 75 RFGRDDFIGQVTIPLSDL 92
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
64-542 |
3.06e-09 |
|
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: 61.57 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 64 LKQHARKQEDKIKRMATKLIRLVND-KKRYERVGGGPKRLGRDvemEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQT 142
Cdd:TIGR04523 24 YKNIANKQDTEEKQLEKKLKTIKNElKNKEKELKNLDKNLNKD---EEKINNSNNKIKILEQQIKDLNDKLKKNKDKINK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 143 QGYRQTPYNN-VQSRINTGRRKANENAGLQECPRKGIKFQDADVAE-TPHPMFTKYGNSLLEEARGEIRNLENVIQSQRG 220
Cdd:TIGR04523 101 LNSDLSKINSeIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEiKKKEKELEKLNNKYNDLKKQKEELENELNLLEK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 221 QIEELEHLAEILKTQLRRKE-------------NEIELSLLQLREQQATDQRSNIRDNVEM------------------- 268
Cdd:TIGR04523 181 EKLNIQKNIDKIKNKLLKLElllsnlkkkiqknKSLESQISELKKQNNQLKDNIEKKQQEInektteisntqtqlnqlkd 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 269 --IKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGD-----ELNMQLKEQRLKCCSLEKQLHSmkfSERRI 341
Cdd:TIGR04523 261 eqNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQ---NNKII 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 342 EELQDRINDLEKERELLKENYDKLydsafsaahEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDrLKTERDQNEKLv 421
Cdd:TIGR04523 338 SQLNEQISQLKKELTNSESENSEK---------QRELEEKQNEIEKLKKENQSYKQEIKNLESQIND-LESKIQNQEKL- 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 422 qeNRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEaLLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQAT 501
Cdd:TIGR04523 407 --NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD-LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN 483
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 816197642 502 HAETVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQ 542
Cdd:TIGR04523 484 LEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKE 524
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
216-572 |
4.45e-09 |
|
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: 61.24 E-value: 4.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 216 QSQRGQIEELEHLAEILKTQLRRKENEIElsllqlreqQATDQRSNirdnvemikLHKQLVEKSNALSAMEGKFIQLQEK 295
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLD---------ELSQELSD---------ASRKIGEIEKEIEQLEQEEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 296 ----QRTLRISHDALMANGDE---LNMQLKEQRLKCCSLEKQLHSMK--FSERRIEELQDRINDLEKER--------ELL 358
Cdd:TIGR02169 739 leelEEDLSSLEQEIENVKSElkeLEARIEELEEDLHKLEEALNDLEarLSHSRIPEIQAELSKLEEEVsriearlrEIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 359 KENYDKLYDSAFsaAHEEQWKLKEQQ--LKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQ 436
Cdd:TIGR02169 819 QKLNRLTLEKEY--LEKEIQELQEQRidLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 437 QLDELKKRIklynQENDINADELSEALLLIKAQKEQKNGDLSflvkvdseinkDLERSMRELQATHAETVQElektrnml 516
Cdd:TIGR02169 897 QLRELERKI----EELEAQIEKKRKRLSELKAKLEALEEELS-----------EIEDPKGEDEEIPEEELSL-------- 953
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 816197642 517 imqhkinKDYQMEVEAVTRKMENLQ-------QDYELKVEQYVHLLDIRAarihKLEAQLKDI 572
Cdd:TIGR02169 954 -------EDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRA----KLEEERKAI 1005
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
201-446 |
5.77e-09 |
|
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: 59.78 E-value: 5.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIelsllQLREQQATDQRSNIRDN-VEMIKLHKQLVEKS 279
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI-----RALEQELAALEAELAELeKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 280 NALSAMegkfiqLQEKQRTLRISHDALMANGDELNMQLKEQRlkccsLEKQLhsMKFSERRIEELQDRINDLEKERELLK 359
Cdd:COG4942 104 EELAEL------LRALYRLGRQPPLALLLSPEDFLDAVRRLQ-----YLKYL--APARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 360 ENYDKLydsafsaaheeqwklkeQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEklvQENRELQLQYLEQKQQLD 439
Cdd:COG4942 171 AERAEL-----------------EALLAELEEERAALEALKAERQKLLARLEKELAELA---AELAELQQEAEELEALIA 230
|
....*..
gi 816197642 440 ELKKRIK 446
Cdd:COG4942 231 RLEAEAA 237
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
341-573 |
6.83e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 6.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 341 IEELQDRINDLEKEREL------LKENYdKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTER 414
Cdd:COG1196 195 LGELERQLEPLERQAEKaeryreLKEEL-KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 415 DQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEInKDLERS 494
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL-EEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 495 MRELQATHAETVQEL-EKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDIA 573
Cdd:COG1196 353 LEEAEAELAEAEEALlEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
107-566 |
8.17e-09 |
|
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: 60.37 E-value: 8.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 107 EMEEMIEQLQEKVHELEKQNETL--KNRLISAKQQLQTQGYRQTP----YNNVQSRINTGRRKAN---ENAGLQECpRKG 177
Cdd:TIGR00618 230 HLREALQQTQQSHAYLTQKREAQeeQLKKQQLLKQLRARIEELRAqeavLEETQERINRARKAAPlaaHIKAVTQI-EQQ 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 178 IKFQDADVAETphpmftkygnsllEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQ--LRRKENEIELSLLQLREQQA 255
Cdd:TIGR00618 309 AQRIHTELQSK-------------MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQeiHIRDAHEVATSIREISCQQH 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 256 TDqRSNIRDNVEMIKLhkqLVEKSNALSAMEGKFIQLQEKQRTLRISHDAL----MANGDELNMQLKEQRLKCCSLEKQL 331
Cdd:TIGR00618 376 TL-TQHIHTLQQQKTT---LTQKLQSLCKELDILQREQATIDTRTSAFRDLqgqlAHAKKQQELQQRYAELCAAAITCTA 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 332 HSMKFSERRIEELQDRInDLEKERELLKENYDKLYdsafsaahEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLK 411
Cdd:TIGR00618 452 QCEKLEKIHLQESAQSL-KEREQQLQTKEQIHLQE--------TRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDN 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 412 TERDQNEKLVQENRELQLQYLEQK--QQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEINK 489
Cdd:TIGR00618 523 PGPLTRRMQRGEQTYAQLETSEEDvyHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEK 602
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 816197642 490 DLERSMRELQATHAETVQELEKTRNMLIMQH--KINKDYQMEVEAVTRKMENLQQDyelkvEQYVHLLDIRAARIHKLE 566
Cdd:TIGR00618 603 LSEAEDMLACEQHALLRKLQPEQDLQDVRLHlqQCSQELALKLTALHALQLTLTQE-----RVREHALSIRVLPKELLA 676
|
|
| C2 |
pfam00168 |
C2 domain; |
792-899 |
8.32e-09 |
|
C2 domain;
Pssm-ID: 425499 [Multi-domain] Cd Length: 104 Bit Score: 54.25 E-value: 8.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 792 LHITIRCCNHLQSRASHLQPHPYV-VYKFFDFADHDTAIIPSSNDPQFDDHMYFPVPMNMDldrylksESLSFYVFDDSD 870
Cdd:pfam00168 3 LTVTVIEAKNLPPKDGNGTSDPYVkVYLLDGKQKKKTKVVKNTLNPVWNETFTFSVPDPEN-------AVLEIEVYDYDR 75
|
90 100
....*....|....*....|....*....
gi 816197642 871 TQENIYIGKVNVPLISLAHDRCISGIFEL 899
Cdd:pfam00168 76 FGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
273-473 |
1.20e-08 |
|
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: 58.62 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 273 KQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLhsmKFSERRIEELQDRINDLE 352
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL---AALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 353 KERELLKENYDKLYDSAFSAAHEEQWKLK---------------EQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQN 417
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPLALLlspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 816197642 418 EKLVQEN----RELQLQYLEQKQQLDELKKRIKLYNQENDI---NADELSEALLLIKAQKEQK 473
Cdd:COG4942 177 EALLAELeeerAALEALKAERQKLLARLEKELAELAAELAElqqEAEELEALIARLEAEAAAA 239
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
229-572 |
1.19e-07 |
|
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: 56.34 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 229 AEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNV-----------EM-IKLHKQLVEKSNALSAMEGKFIQLQEKQ 296
Cdd:pfam01576 12 EELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLqaetelcaeaeEMrARLAARKQELEEILHELESRLEEEEERS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 297 RTLRISHDALMANGDELNMQLKE-----QRLKccsLEKQL--HSMKFSERRIEELQDRINDLEKERELLKEnydKLYDSA 369
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLEEQLDEeeaarQKLQ---LEKVTteAKIKKLEEDILLLEDQNSKLSKERKLLEE---RISEFT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 370 FSAAHEEQWKLKEQQLKVQiaqlETALKSDLTDkteildRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYN 449
Cdd:pfam01576 166 SNLAEEEEKAKSLSKLKNK----HEAMISDLEE------RLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 450 QENDINADELSEALLLIKAQKEQKNgdlsflvkvdseinkDLERSMRELQATHAETVQELEKTRNMLIMQHKINKDYQME 529
Cdd:pfam01576 236 AQLAKKEEELQAALARLEEETAQKN---------------NALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEE 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 816197642 530 VEAVTRKME------NLQQDYELKVEQYVHLLDiRA----ARIHklEAQLKDI 572
Cdd:pfam01576 301 LEALKTELEdtldttAAQQELRSKREQEVTELK-KAleeeTRSH--EAQLQEM 350
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
49-558 |
1.37e-07 |
|
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: 56.28 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 49 ELEDRFLRLHDEnilLKQHARKQEDKIKRMATKLIrLVNDK---KRYERVGGGPKRLGRDVEMEEMIEQLQEKVHEL--- 122
Cdd:pfam15921 321 DLESTVSQLRSE---LREAKRMYEDKIEELEKQLV-LANSElteARTERDQFSQESGNLDDQLQKLLADLHKREKELsle 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 123 EKQNETLKNR----------------------------LISAKQQLQTQGYRQTPynNVQSRINTGRRKANENAGLQ--- 171
Cdd:pfam15921 397 KEQNKRLWDRdtgnsitidhlrrelddrnmevqrlealLKAMKSECQGQMERQMA--AIQGKNESLEKVSSLTAQLEstk 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 172 ECPRKGIKFQDAD--VAETPHPMFTKYGNSLLEEARG-EIRNLEnvIQSQRGQI----EELEHLAEiLKTQLRRKENEIE 244
Cdd:pfam15921 475 EMLRKVVEELTAKkmTLESSERTVSDLTASLQEKERAiEATNAE--ITKLRSRVdlklQELQHLKN-EGDHLRNVQTECE 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 245 LSLLQLREQQATDQ--RSNIRDNVEMIKLHKQ-----LVEKSNALSAMEGKFIQLQEkqrtLRISHDALMANGDELNMQL 317
Cdd:pfam15921 552 ALKLQMAEKDKVIEilRQQIENMTQLVGQHGRtagamQVEKAQLEKEINDRRLELQE----FKILKDKKDAKIRELEARV 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 318 KEQRLKCCSL----EKQLHSMKFSERRIEELQDRINDLEKERELLKENYDKLydsafsaahEEQWKLKEQQLKVQIAQLE 393
Cdd:pfam15921 628 SDLELEKVKLvnagSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVL---------KRNFRNKSEEMETTTNKLK 698
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 394 TALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKlYNQENDINADELSEALllikaqKEQK 473
Cdd:pfam15921 699 MQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQ-FLEEAMTNANKEKHFL------KEEK 771
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 474 NGDLSFLVKVDSEINKdlerSMRELQATHAETVQELEKTRNMLIMQHKINKDYQmEVEAVTRKMEnlQQDYELKVEqyvH 553
Cdd:pfam15921 772 NKLSQELSTVATEKNK----MAGELEVLRSQERRLKEKVANMEVALDKASLQFA-ECQDIIQRQE--QESVRLKLQ---H 841
|
....*
gi 816197642 554 LLDIR 558
Cdd:pfam15921 842 TLDVK 846
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
201-573 |
2.27e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNVEMIKLH-KQLVEKS 279
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERlEELRELE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 280 NALSAMEGKFIQLQEKQRTLRISHDALMANgdelnmqlkeqrlkccSLEKQLHSMKFSERRIEELQDRINDLEKERELLK 359
Cdd:COG4717 163 EELEELEAELAELQEELEELLEQLSLATEE----------------ELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 360 ENYDKLYDSAFSAAHEEQWKLKEQQLKV--QIAQLETALKSDLTDKTEILDRLKT---------ERDQNEKLVQENRELQ 428
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARLLLLIaaALLALLGLGGSLLSLILTIAGVLFLvlgllallfLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 429 LQYLEQKQQLD--ELKKRIKLYNQENDINADELSEALLLIKAQKEQkngdLSFLVKVDSEInkDLERSMRELQATHAETV 506
Cdd:COG4717 307 LQALPALEELEeeELEELLAALGLPPDLSPEELLELLDRIEELQEL----LREAEELEEEL--QLEELEQEIAALLAEAG 380
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 816197642 507 QELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLqqDYELKVEQYVHLLDIRAARIHKLEAQLKDIA 573
Cdd:COG4717 381 VEDEEELRAALEQAEEYQELKEELEELEEQLEEL--LGELEELLEALDEEELEEELEELEEELEELE 445
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
219-580 |
3.02e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 219 RGQIEELehlAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNVEmiKLHKQlveKSNALsamegKFIQLQEKQRT 298
Cdd:COG1196 158 RAIIEEA---AGISKYKERKEEAERKLEATEENLERLEDILGELERQLE--PLERQ---AEKAE-----RYRELKEELKE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 299 LRISHDALmangdelnmQLKEQRLKccsLEKQLHSMKFSERRIEELQDRINDLEKERELLKENYDKLyDSAFSAAHEEqw 378
Cdd:COG1196 225 LEAELLLL---------KLRELEAE---LEELEAELEELEAELEELEAELAELEAELEELRLELEEL-ELELEEAQAE-- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 379 klkEQQLKVQIAQLETALKSDLTDKTEILDRLkterdqnEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQEndinADE 458
Cdd:COG1196 290 ---EYELLAELARLEQDIARLEERRRELEERL-------EELEEELAELEEELEELEEELEELEEELEEAEEE----LEE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 459 LSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQATHAEtVQELEKTRNMLIMQHKINKDYQMEVEAVTRKME 538
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ-LEELEEAEEALLERLERLEEELEELEEALAELE 434
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 816197642 539 NLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDIAYGTKQYK 580
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
338-594 |
3.49e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 338 ERRIEELQDRINDLEKERELLKENYDKL---------YDSAFSAAHEEQWKLKE-QQLKVQIAQLETALKsDLTDKTEIL 407
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALeaeldalqeRREALQRLAEYSWDEIDvASAEREIAELEAELE-RLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 408 DRLKTERDQNEK----LVQENRELQLQYLEQKQQLDELKKRIK-LYNQENDINADELSEALLLIKAQKEQKNGDlsflvK 482
Cdd:COG4913 688 AALEEQLEELEAeleeLEEELDELKGEIGRLEKELEQAEEELDeLQDRLEAAEDLARLELRALLEERFAAALGD-----A 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 483 VDSEINKDLERSMRELQATHAETVQELEKTRnmlimqHKINKDYQMEVEAVT----------RKMENLQQD----YELK- 547
Cdd:COG4913 763 VERELRENLEERIDALRARLNRAEEELERAM------RAFNREWPAETADLDadleslpeylALLDRLEEDglpeYEERf 836
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 816197642 548 -----------VEQYVHLLD--IRAA--RIHKLEAQLKDIAYGT-KQYKFKPEIMPDDSVDEF 594
Cdd:COG4913 837 kellnensiefVADLLSKLRraIREIkeRIDPLNDSLKRIPFGPgRYLRLEARPRPDPEVREF 899
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
148-511 |
4.62e-07 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 54.52 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 148 TPYNNVQSRINTGRRKANENAGLQECPRKGIKFQDADVAetphpmftkygnslLEEARGEIRNLE-NVIQSQRGQIEELE 226
Cdd:PLN02939 91 TSSDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQ--------------LEDLVGMIQNAEkNILLLNQARLQALE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 227 HLAEIL--KTQLRRKENEIELSLLQLREQQATDQRSNIRDNVEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRishd 304
Cdd:PLN02939 157 DLEKILteKEALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLK---- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 305 almangdELNMQLKEqrlkccslEKQLHSMKFSErrIEELQDRINDLEKERELLKENYDKLyDSAFSAAHEEQWKLKEQQ 384
Cdd:PLN02939 233 -------EENMLLKD--------DIQFLKAELIE--VAETEERVFKLEKERSLLDASLREL-ESKFIVAQEDVSKLSPLQ 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 385 LKVQIAQLETalksdLTDkteILDRLKTERDQNEKLVQENRELqlqyleqKQQLDELKKRIKlynqenDINADELSEALL 464
Cdd:PLN02939 295 YDCWWEKVEN-----LQD---LLDRATNQVEKAALVLDQNQDL-------RDKVDKLEASLK------EANVSKFSSYKV 353
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 816197642 465 LIKAQK----EQKngdlsfLVKVDSEINKDL---ERSMRELQATHAETVQELEK 511
Cdd:PLN02939 354 ELLQQKlkllEER------LQASDHEIHSYIqlyQESIKEFQDTLSKLKEESKK 401
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
206-446 |
5.73e-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: 54.30 E-value: 5.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 206 GEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIElSLLQLREQQA---------------------TDQRSNIRD 264
Cdd:TIGR02169 230 KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLE-EIEQLLEELNkkikdlgeeeqlrvkekigelEAEIASLER 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 265 NV-----EMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKqlhsmKFSER 339
Cdd:TIGR02169 309 SIaekerELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDK-----EFAET 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 340 RIE--ELQDRINDLEKERELLKENYDKLYDSAfsaaheEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQN 417
Cdd:TIGR02169 384 RDElkDYREKLEKLKREINELKRELDRLQEEL------QRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
250 260
....*....|....*....|....*....
gi 816197642 418 EKLVQENRELQLQYLEQKQQLDELKKRIK 446
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKELS 486
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
48-569 |
7.16e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 7.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 48 EELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRL-GRDVEMEEMIEQLQEKVHELEKQN 126
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLeEKIRELEERIEELKKEIEELEEKV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 127 ETLKN---------RLISAKQQLQTQGYR--------QTPYNNVQSRINTGRRKANENAGLQEcPRKGIKfQDADVAETP 189
Cdd:PRK03918 283 KELKElkekaeeyiKLSEFYEEYLDELREiekrlsrlEEEINGIEERIKELEEKEERLEELKK-KLKELE-KRLEELEER 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 190 HpmftkygnSLLEEARGEIRNLENViqSQRGQIEELEHLAEILKTQLRRKEnEIELSLLQLREQQAT--DQRSNIRDNVE 267
Cdd:PRK03918 361 H--------ELYEEAKAKKEELERL--KKRLTGLTPEKLEKELEELEKAKE-EIEEEISKITARIGElkKEIKELKKAIE 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 268 MIKLHK----------------QLVEKSNA-LSAMEGKFIQLQEKQRTLRishdalmANGDELNMQLKEQR--LKCCSLE 328
Cdd:PRK03918 430 ELKKAKgkcpvcgrelteehrkELLEEYTAeLKRIEKELKEIEEKERKLR-------KELRELEKVLKKESelIKLKELA 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 329 KQLHSM--KFSERRIEELQDRindlEKERELLKENYDKLyDSAFSAAHEEQWKLKEqqLKVQIAQLETALKSDLTDKTEI 406
Cdd:PRK03918 503 EQLKELeeKLKKYNLEELEKK----AEEYEKLKEKLIKL-KGEIKSLKKELEKLEE--LKKKLAELEKKLDELEEELAEL 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 407 LDRLKTE----RDQNEKLVQENRELQLQYLEQK---QQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNgdlSF 479
Cdd:PRK03918 576 LKELEELgfesVEELEERLKELEPFYNEYLELKdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE---EL 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 480 LVKVDSEINKDLERSMRELQATHA----------ETVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQDYElKVE 549
Cdd:PRK03918 653 EKKYSEEEYEELREEYLELSRELAglraeleeleKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELRE-KVK 731
|
570 580
....*....|....*....|.
gi 816197642 550 QYVHLLDIRA-ARIHKLEAQL 569
Cdd:PRK03918 732 KYKALLKERAlSKVGEIASEI 752
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
65-549 |
7.48e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 7.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 65 KQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELEKQNEtLKNRLISAKqqlqtqg 144
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADE-AKKKAEEAK------- 1444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 145 yrqtpynnvqsRINTGRRKANENAGLQECPRKGIKFQDADVAETPHPMFTKygnslLEEARGEIRNLENVIQSQRGQIEE 224
Cdd:PTZ00121 1445 -----------KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK-----ADEAKKKAEEAKKKADEAKKAAEA 1508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 225 LEHLAEILKTQLRRKENEIElsllQLREQQATDQRSNIRDNVEMIKLHK-QLVEKSNALSAMEGKFIQLQEKQRTLRish 303
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAK----KAEEAKKADEAKKAEEKKKADELKKaEELKKAEEKKKAEEAKKAEEDKNMALR--- 1581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 304 dalmaNGDELNMQLKEQRLKCCSLEKQLHSMKFSE-RRIEELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQWKLKE 382
Cdd:PTZ00121 1582 -----KAEEAKKAEEARIEEVMKLYEEEKKMKAEEaKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE 1656
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 383 QQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKK--RIKLYNQENDINADELS 460
Cdd:PTZ00121 1657 EENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKaeELKKAEEENKIKAEEAK 1736
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 461 EallliKAQKEQKNGDlsfLVKVDSEINKDLERSMRELQATHAETVQELEKtrnmlIMQHKINKDYQMEVEAVTRKMENL 540
Cdd:PTZ00121 1737 K-----EAEEDKKKAE---EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA-----VIEEELDEEDEKRRMEVDKKIKDI 1803
|
....*....
gi 816197642 541 QQDYELKVE 549
Cdd:PTZ00121 1804 FDNFANIIE 1812
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
47-571 |
9.70e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 9.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 47 REELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDV-EMEEMIEQLQEKVHELEKQ 125
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIsRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 126 NETLKNRLISAKQQLQTQGYR----QTPYNNVQSRINTGRRKANENAGLQECPRKGIKFQDAdvaetphpmftkygnsLL 201
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEElaelEEKLEELKEELESLEAELEELEAELEELESRLEELEE----------------QL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 202 EEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNVEMI------------ 269
Cdd:TIGR02168 382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELeelqeelerlee 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 270 ---KLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFS---ERRIEE 343
Cdd:TIGR02168 462 aleELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDegyEAAIEA 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 344 -LQDRINDLEKER--------ELLKEN---------YDKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALK-----SDL 400
Cdd:TIGR02168 542 aLGGRLQAVVVENlnaakkaiAFLKQNelgrvtflpLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKlrkalSYL 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 401 TDKTEILDRLKTERDQNEKLVQENR--------------------ELQLQYLEQKQQLDELKKRIKLynQENDINA---- 456
Cdd:TIGR02168 622 LGGVLVVDDLDNALELAKKLRPGYRivtldgdlvrpggvitggsaKTNSSILERRREIEELEEKIEE--LEEKIAEleka 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 457 -DELSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQaTHAETVQELEKTRNMLIMQHKINKDY----QMEVE 531
Cdd:TIGR02168 700 lAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE-QLEERIAQLSKELTELEAEIEELEERleeaEEELA 778
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 816197642 532 AVTRKMENLQQDyelkVEQYVHLLDIRAARIHKLEAQLKD 571
Cdd:TIGR02168 779 EAEAEIEELEAQ----IEQLKEELKALREALDELRAELTL 814
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
201-463 |
1.19e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 201 LEEARGEIRNLEnviqsqrgqiEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRdnvemIKLHKQLVEKSN 280
Cdd:COG4913 237 LERAHEALEDAR----------EQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRR-----LELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 281 ALSAmegkfiQLQEKQRTLRISHDALMANGDELNMQLKEQRLkccslekqlhsmkfseRRIEELQDRINDLEKERELLKE 360
Cdd:COG4913 302 AELA------RLEAELERLEARLDALREELDELEAQIRGNGG----------------DRLEQLEREIERLERELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 361 NYDKlYDSAFSAAHEEqWKLKEQQLKVQIAQLETALksdlTDKTEILDRLKTERDQnekLVQENRELQLQYLEQKQQLDE 440
Cdd:COG4913 360 RRAR-LEALLAALGLP-LPASAEEFAALRAEAAALL----EALEEELEALEEALAE---AEAALRDLRRELRELEAEIAS 430
|
250 260
....*....|....*....|...
gi 816197642 441 LKKRIKLYNQENDINADELSEAL 463
Cdd:COG4913 431 LERRKSNIPARLLALRDALAEAL 453
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
341-578 |
1.35e-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: 53.15 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 341 IEELQDRINDLEKERELlKENYDKLydsafsaaheeQWKLKEQQLKVQIAQLETALKSdltdKTEILDRLKTERDQNEKL 420
Cdd:TIGR02169 193 IDEKRQQLERLRREREK-AERYQAL-----------LKEKREYEGYELLKEKEALERQ----KEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 421 VQENRELQLQYLEQKQQLDELKKRIKlynQENDINADELSEALLLIKAQKEQKNGDLSF-----------LVKVDSEINK 489
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEELNKKIK---DLGEEEQLRVKEKIGELEAEIASLERSIAEkereledaeerLAKLEAEIDK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 490 ------DLERSMRELQATHA---ETVQELEKTRNMLIMQ-------HKI----NKDYQMEVEAVTRKMENLQQDY----E 545
Cdd:TIGR02169 334 llaeieELEREIEEERKRRDkltEEYAELKEELEDLRAEleevdkeFAEtrdeLKDYREKLEKLKREINELKRELdrlqE 413
|
250 260 270
....*....|....*....|....*....|....*....
gi 816197642 546 LKVEQYVHLLDIRA------ARIHKLEAQLKDIAYGTKQ 578
Cdd:TIGR02169 414 ELQRLSEELADLNAaiagieAKINELEEEKEDKALEIKK 452
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
47-365 |
1.96e-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: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 47 REELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVN-DKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELEKQ 125
Cdd:TIGR02168 718 RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTElEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 126 NETLKNRLISAKQQLQTQgyrqtpynnvqsrintgrrkaNENAGLQECPRKGIKFQDADVAETphpmftkygnslLEEAR 205
Cdd:TIGR02168 798 LKALREALDELRAELTLL---------------------NEEAANLRERLESLERRIAATERR------------LEDLE 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 206 GEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIE-----LSLLQLREQQATDQRSNIRDNV-----EMIKLHKQL 275
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERAsleeaLALLRSELEELSEELRELESKRselrrELEELREKL 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 276 VEKSNALSAMEGKFIQLQEKQRTL-RISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMK----FSERRIEELQDRIND 350
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGpvnlAAIEEYEELKERYDF 1004
|
330
....*....|....*
gi 816197642 351 LEKERELLKENYDKL 365
Cdd:TIGR02168 1005 LTAQKEDLTEAKETL 1019
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
200-569 |
2.24e-06 |
|
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: 52.03 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 200 LLEEARGEIRNLENVIQSQ----RGQIEELEHLA---EILKTQLRR-----KENEIELSLLQLREQQATDQRSnirdnVE 267
Cdd:pfam05483 262 LLEESRDKANQLEEKTKLQdenlKELIEKKDHLTkelEDIKMSLQRsmstqKALEEDLQIATKTICQLTEEKE-----AQ 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 268 MIKLHKQLVEKSNALSAMEGKFIQLQEkqrTLRISHDALMANGDELNMQLKEQRLKCCSLEKQlhsMKFSERRIEELQDR 347
Cdd:pfam05483 337 MEELNKAKAAHSFVVTEFEATTCSLEE---LLRTEQQRLEKNEDQLKIITMELQKKSSELEEM---TKFKNNKEVELEEL 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 348 INDLEKERELLKEN--YDKLYDSAFSAAHEEQWKLKEQQ-----LKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKL 420
Cdd:pfam05483 411 KKILAEDEKLLDEKkqFEKIAEELKGKEQELIFLLQAREkeihdLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIEL 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 421 VQENRELQLQYLEQKQQLDELKkrIKLYNQENDINADELSEALLL-----IKAQKEQKNGDLSF----LVKVDSEINKDL 491
Cdd:pfam05483 491 TAHCDKLLLENKELTQEASDMT--LELKKHQEDIINCKKQEERMLkqienLEEKEMNLRDELESvreeFIQKGDEVKCKL 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 492 ERSMRELQATHAETvqeLEKTRNMLIMQHKINkDYQMEVEAVTRKMENLQQD---YELKVEQYVHLLDIRAARIHKLEAQ 568
Cdd:pfam05483 569 DKSEENARSIEYEV---LKKEKQMKILENKCN-NLKKQIENKNKNIEELHQEnkaLKKKGSAENKQLNAYEIKVNKLELE 644
|
.
gi 816197642 569 L 569
Cdd:pfam05483 645 L 645
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
339-514 |
2.37e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 339 RRIEELQDRINDLEKERELLkenydklyDSAFSAAHEEQWKLKEQQLKVQIAQLETA---LKSDLTDKTEILDRLKTERD 415
Cdd:COG4913 262 ERYAAARERLAELEYLRAAL--------RLWFAQRRLELLEAELEELRAELARLEAElerLEARLDALREELDELEAQIR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 416 QN-----EKLVQENRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEINKD 490
Cdd:COG4913 334 GNggdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAA 413
|
170 180
....*....|....*....|....
gi 816197642 491 LERSMRELQATHAEtVQELEKTRN 514
Cdd:COG4913 414 LRDLRRELRELEAE-IASLERRKS 436
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
225-586 |
4.52e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 225 LEHLAEILKTQLRRKEneielSLLQLREQQA-----TDQRSNIRDNVEMIKLHKQLVEKSNALSAmegkfiQLQEKQRTL 299
Cdd:TIGR02168 161 FEEAAGISKYKERRKE-----TERKLERTREnldrlEDILNELERQLKSLERQAEKAERYKELKA------ELRELELAL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 300 RISH-DALMANGDELNMQLKEQRLKCCSLEKQLHSmkfSERRIEELQDRINDLEKERELLKENYDKLydsafsaaheeqw 378
Cdd:TIGR02168 230 LVLRlEELREELEELQEELKEAEEELEELTAELQE---LEEKLEELRLEVSELEEEIEELQKELYAL------------- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 379 klkeqqlkvqiaqleTALKSDLTDKTEILDrlktERDQNekLVQENRELQLQYLEQKQQLDELKKRI-----KLYNQEND 453
Cdd:TIGR02168 294 ---------------ANEISRLEQQKQILR----ERLAN--LERQLEELEAQLEELESKLDELAEELaeleeKLEELKEE 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 454 INA--DELSEALLLIKAQK----------EQKNGDLSFLVKVDSEINKDLER---SMRELQATHAETVQELEKTRNMLIM 518
Cdd:TIGR02168 353 LESleAELEELEAELEELEsrleeleeqlETLRSKVAQLELQIASLNNEIERleaRLERLEDRRERLQQEIEELLKKLEE 432
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 816197642 519 QHKinKDYQMEVEAVTRKMENLQQDYELKVEQyvhlLDIRAARIHKLEAQLKDIAYGTKQYKFKPEIM 586
Cdd:TIGR02168 433 AEL--KELQAELEELEEELEELQEELERLEEA----LEELREELEEAEQALDAAERELAQLQARLDSL 494
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
107-463 |
5.08e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 107 EMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTqgyrqtpynnvqsrINTGRRKANENAGLQECPRKGIKFQDADVA 186
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEE--------------LEEERDDLLAEAGLDDADAEAVEARREELE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 187 ETphpmftkygnslLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQ---LRRKENEIElSLLQLREQQATDQRSNIR 263
Cdd:PRK02224 321 DR------------DEELRDRLEECRVAAQAHNEEAESLREDADDLEERaeeLREEAAELE-SELEEAREAVEDRREEIE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 264 DnvemikLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKE--------QRL----KC--C--SL 327
Cdd:PRK02224 388 E------LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTarerveeaEALleagKCpeCgqPV 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 328 EKQLHSMKFSERR--IEELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDltdkte 405
Cdd:PRK02224 462 EGSPHVETIEEDRerVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEK------ 535
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 816197642 406 iLDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQENDINADELsEAL 463
Cdd:PRK02224 536 -RERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERI-ESL 591
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
63-474 |
5.63e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 63 LLKQHARKQEDKI--KRMATKLIRLVNDKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELEKQNETLKNRLISAKQQL 140
Cdd:COG4717 46 MLLERLEKEADELfkPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 141 QTQGYRQTP------YNNVQSRINTGRRKANENAGLQEcprkGIKFQDADVAETpHPMFTKYGNSLLEEARGEIRNLENV 214
Cdd:COG4717 126 QLLPLYQELealeaeLAELPERLEELEERLEELRELEE----ELEELEAELAEL-QEELEELLEQLSLATEEELQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 215 IQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQrsnIRDNVEMIKLHKQLVEKSNALSAMEGKFIQLQE 294
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER---LKEARLLLLIAAALLALLGLGGSLLSLILTIAG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 295 KQRT-----------LRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSE--------------RRIEELQDRIN 349
Cdd:COG4717 278 VLFLvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPdlspeellelldriEELQELLREAE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 350 DLEKEREL--LKENYDKLYDSAFSAAHEE-----QWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTE--RDQNEKL 420
Cdd:COG4717 358 ELEEELQLeeLEQEIAALLAEAGVEDEEElraalEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEEL 437
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 816197642 421 VQENRELQLQYLEQKQQLDELKKRIKlyNQENDinaDELSEALLLIKAQKEQKN 474
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELE--QLEED---GELAELLQELEELKAELR 486
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
223-588 |
1.09e-05 |
|
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: 49.72 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 223 EELEHLAEILKTQLRRKENEIELSLLQLREQQAT---------DQRSNIRDNVEMIKLH----KQLVEKSNAL-SAMEGK 288
Cdd:pfam05483 222 EKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKmkdltflleESRDKANQLEEKTKLQdenlKELIEKKDHLtKELEDI 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 289 FIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSerrIEELQDRINDLEkerELLKENYDKLYDS 368
Cdd:pfam05483 302 KMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFV---VTEFEATTCSLE---ELLRTEQQRLEKN 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 369 afsaahEEQWKLKEQQLKVQIAQLETALKsdLTDKTEI-LDRLKTERDQNEKLVQENRELQLQYLEQKQQLDEL-----K 442
Cdd:pfam05483 376 ------EDQLKIITMELQKKSSELEEMTK--FKNNKEVeLEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELifllqA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 443 KRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEINKD-LERSMRELQATHAETVQELEKTRNMLIMQHK 521
Cdd:pfam05483 448 REKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDkLLLENKELTQEASDMTLELKKHQEDIINCKK 527
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 816197642 522 INKDYQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDIAYGTKQYKFKPEIMPD 588
Cdd:pfam05483 528 QEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILEN 594
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
37-572 |
1.47e-05 |
|
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: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 37 KSRQAVSRVSREELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERvgggpkrlgRDVEMEEMIEQLQ 116
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE---------RRRELEERLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 117 EKVHELEKQNETLKNRLISAKQQLQTQGYRQTpyNNVQSRINTGRRKANENAGLQECPRKGIKFQDADVAETphpmftky 196
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELE--EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL-------- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 197 gnSLLEEARGEIRNLENVIQSQRGQIEELEHLAEilktQLRRKENEIELSLLQLREQQATDQRSNIRDNVEMIKLHKQLV 276
Cdd:COG1196 393 --RAAAELAAQLEELEEAEEALLERLERLEEELE----ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 277 EKSNALSAMEGKFIQLQEKQRTLRISHDALMA--------NGDELNMQLKEQRLKCCSLEKQLHSMKFSERRIEE----- 343
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLLLEaeadyegfLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEaalaa 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 344 -LQDRIN----DLEKERELLKEN---------YDKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDR 409
Cdd:COG1196 547 aLQNIVVeddeVAAAAIEYLKAAkagratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 410 LKTERDQNEKLVQenRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQkngdlsflvkVDSEINK 489
Cdd:COG1196 627 LVAARLEAALRRA--VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAER----------LAEEELE 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 490 DLERSMRELQATHAETVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRA--ARIHKLEA 567
Cdd:COG1196 695 LEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEleRELERLER 774
|
....*
gi 816197642 568 QLKDI 572
Cdd:COG1196 775 EIEAL 779
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
221-499 |
1.67e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 221 QIEELEHLAEILKTQLRRKENEIElsllqlREQQATDQRSNIRDNVEMIKlhKQLVEKSNALSAMEGKFIQLQEKQRTLR 300
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIE------RLEKFIKRTENIEELIKEKE--KELEEVLREINEISSELPELREELEKLE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 301 ISHDALmangDELNMQLKEQRLKCCSLEKqlhSMKFSERRIEELQDRINDLEKERELLKENYDKL-----YDSAFSAAHE 375
Cdd:PRK03918 228 KEVKEL----EELKEEIEELEKELESLEG---SKRKLEEKIRELEERIEELKKEIEELEEKVKELkelkeKAEEYIKLSE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 376 --EQWKLKEQQLKVQIAQLETALK------SDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQ---QLDELKKR 444
Cdd:PRK03918 301 fyEEYLDELREIEKRLSRLEEEINgieeriKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAkkeELERLKKR 380
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 816197642 445 IKLYNQEndinadELSEALLLIKAQKEQKNGDLSFLVKVDSEIN---KDLERSMRELQ 499
Cdd:PRK03918 381 LTGLTPE------KLEKELEELEKAKEEIEEEISKITARIGELKkeiKELKKAIEELK 432
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
201-451 |
2.03e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIR-DNVEMIKLHKQLVEKS 279
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDaSSDDLAALEEQLEELE 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 280 NALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLkEQRLKCCSLEKQLHsmkFSERRIEELQDRI-----NDLEKE 354
Cdd:COG4913 699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL-EAAEDLARLELRAL---LEERFAAALGDAVerelrENLEER 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 355 RELLKENYDKLYDSAFSAAHE--EQWKLKEQQLKVQIAqletalksDLTDKTEILDRLKTE-----RDQNEKLVQEN-RE 426
Cdd:COG4913 775 IDALRARLNRAEEELERAMRAfnREWPAETADLDADLE--------SLPEYLALLDRLEEDglpeyEERFKELLNENsIE 846
|
250 260
....*....|....*....|....*.
gi 816197642 427 LQLQYLEQ-KQQLDELKKRIKLYNQE 451
Cdd:COG4913 847 FVADLLSKlRRAIREIKERIDPLNDS 872
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
201-443 |
2.06e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILK------TQLRRKENEIELSLLQLREqqatdQRSNIRDNVEMIKLH-K 273
Cdd:PRK03918 202 LEEVLREINEISSELPELREELEKLEKEVKELEelkeeiEELEKELESLEGSKRKLEE-----KIRELEERIEELKKEiE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 274 QLVEKSNALSAMEGKfiqlQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSERRIEELQDRINDLEK 353
Cdd:PRK03918 277 ELEEKVKELKELKEK----AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 354 ERELLKEnYDKLYDSAfSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKterdqneKLVQENRELQLQYLE 433
Cdd:PRK03918 353 RLEELEE-RHELYEEA-KAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEIS-------KITARIGELKKEIKE 423
|
250
....*....|
gi 816197642 434 QKQQLDELKK 443
Cdd:PRK03918 424 LKKAIEELKK 433
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
201-365 |
2.36e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 201 LEEARGEIR---------NLENVIQSQRGQIEELEhlAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNVEMIKL 271
Cdd:COG3206 191 LEEAEAALEefrqknglvDLSEEAKLLLQQLSELE--SQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQL 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 272 HKQLVEKSNALSAMEGKF-------IQLQEKQRTLRISHDALMANG-DELNMQLKEQRLKCCSLEKQLHSMKFSERRIEE 343
Cdd:COG3206 269 RAQLAELEAELAELSARYtpnhpdvIALRAQIAALRAQLQQEAQRIlASLEAELEALQAREASLQAQLAQLEARLAELPE 348
|
170 180
....*....|....*....|..
gi 816197642 344 LQDRINDLEKERELLKENYDKL 365
Cdd:COG3206 349 LEAELRRLEREVEVARELYESL 370
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
39-375 |
3.03e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 39 RQAVSRVSRE--ELEDRFLRLHDE----NILLKQHARKQ---EDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDVEME 109
Cdd:TIGR02169 708 SQELSDASRKigEIEKEIEQLEQEeeklKERLEELEEDLsslEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 110 EMIEQLQEKVHELEKQNETLKN---RLISAKQQLQTQGYR----QTPYNNVQSRINTGRRKANENaglqecpRKGIKFQD 182
Cdd:TIGR02169 788 LSHSRIPEIQAELSKLEEEVSRieaRLREIEQKLNRLTLEkeylEKEIQELQEQRIDLKEQIKSI-------EKEIENLN 860
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 183 ADVAETphpmftkygNSLLEEARGEIRNLENVIQSQRGQIEELEhlAEIlkTQLRRKENEIELSLLQLREQQA--TDQRS 260
Cdd:TIGR02169 861 GKKEEL---------EEELEELEAALRDLESRLGDLKKERDELE--AQL--RELERKIEELEAQIEKKRKRLSelKAKLE 927
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 261 NIRDNVEMI-KLHKQLVEKSNALSAMEGKFIQLQEKQRtlrishdALMANGDeLNMQLKEQrlkccslekqlhsMKFSER 339
Cdd:TIGR02169 928 ALEEELSEIeDPKGEDEEIPEEELSLEDVQAELQRVEE-------EIRALEP-VNMLAIQE-------------YEEVLK 986
|
330 340 350
....*....|....*....|....*....|....*....
gi 816197642 340 RIEELQDRINDLEKERELLK---ENYDKLYDSAFSAAHE 375
Cdd:TIGR02169 987 RLDELKEKRAKLEEERKAILeriEEYEKKKREVFMEAFE 1025
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
208-460 |
4.11e-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: 47.89 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 208 IRNLENVIQSQRGQIEELEHLAEILKTQ--------------LRRKENEIElsllQLREQQATDQRSNIRDNVEMIKLHK 273
Cdd:pfam10174 403 IENLQEQLRDKDKQLAGLKERVKSLQTDssntdtalttleeaLSEKERIIE----RLKEQREREDRERLEELESLKKENK 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 274 QLVEKSNAL----SAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQL---HSMKFSERRIEELQD 346
Cdd:pfam10174 479 DLKEKVSALqpelTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLkkaHNAEEAVRTNPEIND 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 347 RINDLEKERELLKE-------NYDKLYDSAFSAAHEEQWKLKeqqlkvQIAQLETALKSDLTDKTEILDRLKT----ERD 415
Cdd:pfam10174 559 RIRLLEQEVARYKEesgkaqaEVERLLGILREVENEKNDKDK------KIAELESLTLRQMKEQNKKVANIKHgqqeMKK 632
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 816197642 416 QNEKLVQENRELQLQYLE--QKQQLDELKKRIKLYNQENDINADELS 460
Cdd:pfam10174 633 KGAQLLEEARRREDNLADnsQQLQLEELMGALEKTRQELDATKARLS 679
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
311-512 |
4.52e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 311 DELNMQLKEQRLKCCSLEKQLHSMkfsERRIEELQDRINDLEKERELLKENYDKLYDSAfsAAHEEQWKLKEQQLKVQIA 390
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDAL---QAELEELNEEYNELQAELEALQAEIDKLQAEI--AEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 391 Q----------LETALKS-DLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLynqendiNADEL 459
Cdd:COG3883 94 AlyrsggsvsyLDVLLGSeSFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEA-------LKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 816197642 460 SEALLLIKAQKEQKNGDLSFLvkvdSEINKDLERSMRELQATHAETVQELEKT 512
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQL----SAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
316-517 |
4.87e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 316 QLKEQRLKCCSLEKQLHSMKFSERRIEELQDRINDLEKERELLKENYDKLydsafsaaheeqwkLKEQQLKVQIAQLEtA 395
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL--------------EKLLQLLPLYQELE-A 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 396 LKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQEndiNADELSEALLLIKAQKEQKNG 475
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE---ELQDLAEELEELQQRLAELEE 213
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 816197642 476 DLSFLVKVDSEINKDLERsmRELQATHAETVQELEKTRNMLI 517
Cdd:COG4717 214 ELEEAQEELEELEEELEQ--LENELEAAALEERLKEARLLLL 253
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
335-562 |
5.53e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 335 KFSERRIEELQDRINDLEKERELLKENYDkLYDSafsaahEEQWKLKEQQLkVQIAQLETALKSDLTDKTEILDRLKTER 414
Cdd:COG3206 178 EFLEEQLPELRKELEEAEAALEEFRQKNG-LVDL------SEEAKLLLQQL-SELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 415 DQNEKLVQEN------RELQLQYLEQKQQLDELKKRiklYNQENDInadelsealllIKAQKEQKNGDLSFLVKVDSEIN 488
Cdd:COG3206 250 GSGPDALPELlqspviQQLRAQLAELEAELAELSAR---YTPNHPD-----------VIALRAQIAALRAQLQQEAQRIL 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 816197642 489 KDLERSMRELQATHAETVQELEKTRNMLimqhkinkdyqMEVEAVTRKMENLQQDYELKVEQYVHLLD-IRAARI 562
Cdd:COG3206 316 ASLEAELEALQAREASLQAQLAQLEARL-----------AELPELEAELRRLEREVEVARELYESLLQrLEEARL 379
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
209-446 |
5.97e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 209 RNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIE-------LSLLQLREQQATDQRSNIRDnvemiklhkQLVEKSNA 281
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEefrqkngLVDLSEEAKLLLQQLSELES---------QLAEARAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 282 LSAMEGKFIQLQEKQRTLRISHDALMAngDELNMQLKEQRLKccsLEKQLHSM--KFSER--RIEELQDRINDLekeREL 357
Cdd:COG3206 235 LAEAEARLAALRAQLGSGPDALPELLQ--SPVIQQLRAQLAE---LEAELAELsaRYTPNhpDVIALRAQIAAL---RAQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 358 LKENYDKLYDSAFSAAheeqwklkeQQLKVQIAQLETALksdltdkteilDRLKTERDQNEKLVQENRELQLQYLEQKQQ 437
Cdd:COG3206 307 LQQEAQRILASLEAEL---------EALQAREASLQAQL-----------AQLEARLAELPELEAELRRLEREVEVAREL 366
|
....*....
gi 816197642 438 LDELKKRIK 446
Cdd:COG3206 367 YESLLQRLE 375
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
191-533 |
6.21e-05 |
|
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: 47.66 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 191 PMFTKYGNSLLEEARGEIRNLENVIQSQR-----GQIEELEHLAEILKTQLRRK--ENEIELSLLQLREQQATDQRSNIR 263
Cdd:TIGR00618 601 EKLSEAEDMLACEQHALLRKLQPEQDLQDvrlhlQQCSQELALKLTALHALQLTltQERVREHALSIRVLPKELLASRQL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 264 DNVEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLR--------ISHDA---LMANGDELNMQLKE----QRLKCCSLE 328
Cdd:TIGR00618 681 ALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDrefneienASSSLgsdLAAREDALNQSLKElmhqARTVLKART 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 329 KQlHSMKFSERRIE-----ELQDRINDLEKERELLKENYdklydsafsaaheeqwklkeQQLKVQIAQLETALKSDLTDK 403
Cdd:TIGR00618 761 EA-HFNNNEEVTAAlqtgaELSHLAAEIQFFNRLREEDT--------------------HLLKTLEAEIGQEIPSDEDIL 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 404 TEILDRLKTERDQNEKLVQEN-------RELQLQYLEQKQQLDELKKRIKLYNQendinadeLSEALLLIKAQKEQKNGD 476
Cdd:TIGR00618 820 NLQCETLVQEEEQFLSRLEEKsatlgeiTHQLLKYEECSKQLAQLTQEQAKIIQ--------LSDKLNGINQIKIQFDGD 891
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 816197642 477 LsfLVKVDSEINKDLERSMRELQATHAETVQELektrnmlimQHKINKDYQMEVEAV 533
Cdd:TIGR00618 892 A--LIKFLHEITLYANVRLANQSEGRFHGRYAD---------SHVNARKYQGLALLV 937
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
388-569 |
6.28e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 388 QIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEAlllik 467
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 468 AQKEQKNGD----LSFLVKVDSeINKDLERS--MRELQATHAETVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQ 541
Cdd:COG3883 92 ARALYRSGGsvsyLDVLLGSES-FSDFLDRLsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180
....*....|....*....|....*...
gi 816197642 542 QDYELKVEQYVHLLDIRAARIHKLEAQL 569
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQL 198
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
372-513 |
7.96e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 372 AAHEEQWKLKE-QQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQ 450
Cdd:COG1579 1 AMPEDLRALLDlQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 451 -------ENDINA------------DELSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQATHAETVQELEK 511
Cdd:COG1579 81 qlgnvrnNKEYEAlqkeieslkrriSDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
..
gi 816197642 512 TR 513
Cdd:COG1579 161 LE 162
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
201-492 |
8.08e-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: 8.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIElsllQLREQQATDQRSNIRDNVEMIKLHKQlveksn 280
Cdd:TIGR02169 296 IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE----ELEREIEEERKRRDKLTEEYAELKEE------ 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 281 alsaMEGKFIQLQEKQRTLRISHDALMAngdelnmqlkeqrlkccslekqlhsmkfSERRIEELQDRINDLEKERELLKE 360
Cdd:TIGR02169 366 ----LEDLRAELEEVDKEFAETRDELKD----------------------------YREKLEKLKREINELKRELDRLQE 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 361 NYDKLydSAFSAAHEEQWKLKEQQLKVQIAQLETA---LKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQ 437
Cdd:TIGR02169 414 ELQRL--SEELADLNAAIAGIEAKINELEEEKEDKaleIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 816197642 438 LDELKKRIKLYNQENDINADelseALLLIKAQKEQKNGDLSFLVKVDSEINKDLE 492
Cdd:TIGR02169 492 LAEAEAQARASEERVRGGRA----VEEVLKASIQGVHGTVAQLGSVGERYATAIE 542
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
201-477 |
8.50e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 8.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQAtdqrsnirdnvEMIKLHKQLVEKSN 280
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQA-----------ELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 281 ALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSERRIEELQDRINDLEKERELlke 360
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL--- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 361 nyDKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDE 440
Cdd:COG4372 186 --DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
|
250 260 270
....*....|....*....|....*....|....*..
gi 816197642 441 LKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDL 477
Cdd:COG4372 264 ELAILVEKDTEEEELEIAALELEALEEAALELKLLAL 300
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
109-464 |
9.23e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 9.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 109 EEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQGYRQTPYNNVQSRINTGRRKANENAGLQECPRKGIKFQDADVAet 188
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEE-- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 189 phpmftkygnslLEEARGEIRNLENVIQSQRGQ--IEELEHLAEILKT----QLRRKENEIELSLLQLREQQATDQRSNI 262
Cdd:COG4717 165 ------------LEELEAELAELQEELEELLEQlsLATEEELQDLAEEleelQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 263 RDNVEMIKLHKQLVEKSN------ALSAMEGKFIQLQEKQRT------------------LRISHDALMANGDELNMQLK 318
Cdd:COG4717 233 ENELEAAALEERLKEARLllliaaALLALLGLGGSLLSLILTiagvlflvlgllallfllLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 319 EQRLKCCSLEKQLHSMKFSE--------------RRIEELQDRINDLEKEREL--LKENYDKLYDSAFSAAHEE-----Q 377
Cdd:COG4717 313 LEELEEEELEELLAALGLPPdlspeellelldriEELQELLREAEELEEELQLeeLEQEIAALLAEAGVEDEEElraalE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 378 WKLKEQQLKVQIAQLETALKS---------DLTDKTEI---LDRLKTERDQNEKLVQENRE------LQLQYLEQKQQLD 439
Cdd:COG4717 393 QAEEYQELKEELEELEEQLEEllgeleellEALDEEELeeeLEELEEELEELEEELEELREelaeleAELEQLEEDGELA 472
|
410 420 430
....*....|....*....|....*....|
gi 816197642 440 ELKKRI-----KLYNQENDINADELSEALL 464
Cdd:COG4717 473 ELLQELeelkaELRELAEEWAALKLALELL 502
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
69-552 |
9.30e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 9.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 69 RKQEDKIKRMATKL---IRLVNDKKRYERvgggpkrlGRDVEMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQGY 145
Cdd:PTZ00121 1194 RKAEDARKAEAARKaeeERKAEEARKAED--------AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHF 1265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 146 --RQTPYNNVQSRINTGRRKANENAGLQECpRKGIKFQDADVAETPHPMFTKygnslLEEARGEIRNLENVIQSQRGQIE 223
Cdd:PTZ00121 1266 arRQAAIKAEEARKADELKKAEEKKKADEA-KKAEEKKKADEAKKKAEEAKK-----ADEAKKKAEEAKKKADAAKKKAE 1339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 224 ELEHLAEILKTQLRRKENEIELSllQLREQQATDQRSNIRDNVEMIKLHKQLVEKSNALsamEGKFIQLQEKQRTLRISH 303
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEAA--EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEA---KKKAEEDKKKADELKKAA 1414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 304 DAlMANGDELNMQLKEQRlKCCSLEKQLHSmkfsERRIEELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQWKLKEQ 383
Cdd:PTZ00121 1415 AA-KKKADEAKKKAEEKK-KADEAKKKAEE----AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEA 1488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 384 QLKVQiaqlETALKSDLTDKTEildRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKriklynQENDINADELSEAL 463
Cdd:PTZ00121 1489 KKKAE----EAKKKADEAKKAA---EAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK------AEEKKKADELKKAE 1555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 464 LLIKAQKEQKNgdlsflvkvdSEINKDLERsmRELQATHAETVQELEKTRNMLIMQhKINKDYQMEVEAVTRKMENLQQD 543
Cdd:PTZ00121 1556 ELKKAEEKKKA----------EEAKKAEED--KNMALRKAEEAKKAEEARIEEVMK-LYEEEKKMKAEEAKKAEEAKIKA 1622
|
....*....
gi 816197642 544 YELKVEQYV 552
Cdd:PTZ00121 1623 EELKKAEEE 1631
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
109-321 |
1.32e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 109 EEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQ----GYRQTPYNNVQSRINTGRRKANENAGLQECPRKGIKFQDAD 184
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALerriAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 185 VAE----------TPHPMFTKYGNSLLEEARGeIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIElSLLQLREQQ 254
Cdd:COG4942 106 LAEllralyrlgrQPPLALLLSPEDFLDAVRR-LQYLKYLAPARREQAEELRADLAELAALRAELEAERA-ELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 816197642 255 ATDQRsnirdnvemiKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQR 321
Cdd:COG4942 184 EEERA----------ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
202-462 |
1.35e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.04 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 202 EEARGEIRNLENVIQSQRGQIEELEhlaeilkTQLRRKENEIELSLLQLREQQATDQRSNIR---DNVEMIKLHKQLVEK 278
Cdd:pfam07888 125 AAHEARIRELEEDIKTLTQRVLERE-------TELERMKERAKKAGAQRKEEEAERKQLQAKlqqTEEELRSLSKEFQEL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 279 SNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRlkccSLEKQLHSmkfSERRIEELQDRINDLEKERell 358
Cdd:pfam07888 198 RNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELR----SLQERLNA---SERKVEGLGEELSSMAAQR--- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 359 kenydklyDSAFSAAHeeQWKLKEQQLKVQIAQLETALKSDLT----DKTEILDRLKTERDQNEKLvqeNRELQ-LQYLE 433
Cdd:pfam07888 268 --------DRTQAELH--QARLQAAQLTLQLADASLALREGRArwaqERETLQQSAEADKDRIEKL---SAELQrLEERL 334
|
250 260
....*....|....*....|....*....
gi 816197642 434 QKQQLDELKKRIKLyNQENDINADELSEA 462
Cdd:pfam07888 335 QEERMEREKLEVEL-GREKDCNRVQLSES 362
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
221-504 |
1.57e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 221 QIEELEHLAEILKT---QLRRKENEIELSLLQLREQqatdqrsniRDnvemiKLHKQLVEKSNALSAMEGKFIQLQEKQR 297
Cdd:COG1340 9 SLEELEEKIEELREeieELKEKRDELNEELKELAEK---------RD-----ELNAQVKELREEAQELREKRDELNEKVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 298 TLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSERRIEELQDRIN----DLEKERELLKE--NYDKLYDSAfs 371
Cdd:COG1340 75 ELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQtevlSPEEEKELVEKikELEKELEKA-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 372 aaheeqwkLKEQQLKVQIAQLETALKsdltdktEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQE 451
Cdd:COG1340 153 --------KKALEKNEKLKELRAELK-------ELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKE 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 816197642 452 ND---INADELSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQATHAE 504
Cdd:COG1340 218 IVeaqEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIF 273
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
43-442 |
1.65e-04 |
|
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: 45.98 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 43 SRVSREELEdRFLRLHD-----ENIllKQHARKQEDKIKRMATKLIRLVNDKKRYervgggpkrlgrdVEMEEMIEQLQE 117
Cdd:pfam12128 216 SRLNRQQVE-HWIRDIQaiagiMKI--RPEFTKLQQEFNTLESAELRLSHLHFGY-------------KSDETLIASRQE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 118 KVHELEKQnetLKNRLISAKQQLQtqgyrqtpynnvQSRINTGRRKANENAGLQECPrkgikfQDADVAETPHPMFTKYG 197
Cdd:pfam12128 280 ERQETSAE---LNQLLRTLDDQWK------------EKRDELNGELSAADAAVAKDR------SELEALEDQHGAFLDAD 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 198 nslLEEARGEIRNLENViqsqRGQIEELEHLAEILKTQLRRKENEIElSLLQLREQQATDQRSNIRDNVEMIK--LHKQL 275
Cdd:pfam12128 339 ---IETAAADQEQLPSW----QSELENLEERLKALTGKHQDVTAKYN-RRRSKIKEQNNRDIAGIKDKLAKIReaRDRQL 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 276 VEKSNALSAMEGKfiqlqekqrtLRISHDALMANGDELNMQLKEqrlkccslekqlhsmkfserRIEELQDRINDLEKER 355
Cdd:pfam12128 411 AVAEDDLQALESE----------LREQLEAGKLEFNEEEYRLKS--------------------RLGELKLRLNQATATP 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 356 ELLKENydKLYDSAFSAAHEEQWKLKEQQLkvqiaqletALKSDLTdkteildRLKTERDQ-NEKLVQENRELQlqylEQ 434
Cdd:pfam12128 461 ELLLQL--ENFDERIERAREEQEAANAEVE---------RLQSELR-------QARKRRDQaSEALRQASRRLE----ER 518
|
....*...
gi 816197642 435 KQQLDELK 442
Cdd:pfam12128 519 QSALDELE 526
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
232-511 |
2.22e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.39 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 232 LKTQLRRK--ENEIELSLL---------QLRE--QQATDQRSNIRDNVEMIKLHKQLVEKSNALSAMEgkfiqLQEKQRT 298
Cdd:PHA02562 147 LSAPARRKlvEDLLDISVLsemdklnkdKIRElnQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGEN-----IARKQNK 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 299 LrishdalmangDELnmqLKEqrlkccslEKQLHSmkfserRIEELQDRINDLEKERELLKENYDKLYDSAFsaaheeqw 378
Cdd:PHA02562 222 Y-----------DEL---VEE--------AKTIKA------EIEELTDELLNLVMDIEDPSAALNKLNTAAA-------- 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 379 klkeqQLKVQIAQLETALKSdLTDKTEI---LDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNqendin 455
Cdd:PHA02562 266 -----KIKSKIEQFQKVIKM-YEKGGVCptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFN------ 333
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 816197642 456 adELSEALLLIKAQKEQKNGDLSFLVKVdseiNKDLERSMRELQATHAETVQELEK 511
Cdd:PHA02562 334 --EQSKKLLELKNKISTNKQSLITLVDK----AKKVKAAIEELQAEFVDNAEELAK 383
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
208-561 |
2.52e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 208 IRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIElsllQLREQQATDQRSNIRDNVEMIKLHKQLVEKSNALSAMEG 287
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELE----QLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 288 KFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLhsmKFSERRIEELQDRINDLEKERELLKENYDKLYD 367
Cdd:COG4372 102 ELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI---AEREEELKELEEQLESLQEELAALEQELQALSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 368 safSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKL 447
Cdd:COG4372 179 ---AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 448 YNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQATHAETVQELEKTRNMLIMQHKINKDYQ 527
Cdd:COG4372 256 ILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
|
330 340 350
....*....|....*....|....*....|....
gi 816197642 528 MEVEAVTRKMENLQQDYELKVEQYVHLLDIRAAR 561
Cdd:COG4372 336 LAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
264-552 |
2.67e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 264 DNVEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKE---QRLKccSLEKQLHSMKFSERR 340
Cdd:PRK04863 835 PEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADEtlaDRVE--EIREQLDEAEEAKRF 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 341 IEELQDRINDLEKERELLK---ENYDKLYDSAFSAahEEQWKLKEQQLK--VQIAQLETALK-----SDLTDKTEILDRL 410
Cdd:PRK04863 913 VQQHGNALAQLEPIVSVLQsdpEQFEQLKQDYQQA--QQTQRDAKQQAFalTEVVQRRAHFSyedaaEMLAKNSDLNEKL 990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 411 KTERDQNEklvQENRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEAlllikaqkEQKNGDLSflVKVDSEINKD 490
Cdd:PRK04863 991 RQRLEQAE---QERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQEL--------KQELQDLG--VPADSGAEER 1057
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 816197642 491 LERSMRELQA---THAETVQELEKTRNMLimqhkinkdyQMEVEAVTRKMENLQQDYELKVEQYV 552
Cdd:PRK04863 1058 ARARRDELHArlsANRSRRNQLEKQLTFC----------EAEMDNLTKKLRKLERDYHEMREQVV 1112
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
341-454 |
3.29e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.07 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 341 IEELQDRINDLEKERELLKENYDKLydsafSAAHEEQWKLKEQQLKVQIAQLETALKSDltdkTEILDRLKTERDQNEKL 420
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEA-----SFERLAELRDELAELEEELEALKARWEAE----KELIEEIQELKEELEQR 483
|
90 100 110
....*....|....*....|....*....|....
gi 816197642 421 VQENRELQLQYLEQKQQLDELKKRIKLYNQENDI 454
Cdd:COG0542 484 YGKIPELEKELAELEEELAELAPLLREEVTEEDI 517
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
207-323 |
4.87e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 207 EIRNLENVIQSQRGQIEELEHLAEILK--TQLRRKENEIELSLLQLRE--QQATDQRSNIRDNVEMIK-----LHKQLVE 277
Cdd:COG1340 141 KIKELEKELEKAKKALEKNEKLKELRAelKELRKEAEEIHKKIKELAEeaQELHEEMIELYKEADELRkeadeLHKEIVE 220
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 816197642 278 KSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLK 323
Cdd:COG1340 221 AQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
198-360 |
5.36e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 198 NSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIElsllQLREQQATDQR--SNIRDNVEMIKLHKQL 275
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE----EVEARIKKYEEqlGNVRNNKEYEALQKEI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 276 VEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEqrlkccsLEKQLhsmkfsERRIEELQDRINDLEKER 355
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEE-------KKAEL------DEELAELEAELEELEAER 165
|
....*
gi 816197642 356 ELLKE 360
Cdd:COG1579 166 EELAA 170
|
|
| C2A_Tricalbin-like |
cd04044 |
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ... |
792-916 |
7.54e-04 |
|
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are present in Tricalbin, a yeast homolog of Synaptotagmin, which is involved in membrane trafficking and sorting. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-II topology.
Pssm-ID: 176009 [Multi-domain] Cd Length: 124 Bit Score: 40.62 E-value: 7.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 792 LHITIRCCNHLQSRASHLQ-PHPYVVYKFFDFADHD-TAIIPSSNDPQFDDHMYFPVpmNMDldrylkSESLSFYVFDDS 869
Cdd:cd04044 4 LAVTIKSARGLKGSDIIGGtVDPYVTFSISNRRELArTKVKKDTSNPVWNETKYILV--NSL------TEPLNLTVYDFN 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 816197642 870 DTQENIYIGKVNVPLISLAHDRCISGI-FELTDHQKhPAGTIHVILKW 916
Cdd:cd04044 76 DKRKDKLIGTAEFDLSSLLQNPEQENLtKNLLRNGK-PVGELNYDLRF 122
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
107-363 |
8.97e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 8.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 107 EMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQGYRQTPYNN---VQSRINTGRRKANENAGLQECPRKGIKFQDA 183
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERredLEELIAERRETIEEKRERAEELRERAAELEA 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 184 DVAETPHPMFTKYGNSllEEARGEIRNLENVIQSQRGQIEELEHLAEILKtqlRRKENEIELSLLQLREQQATDQRSNIR 263
Cdd:PRK02224 552 EAEEKREAAAEAEEEA--EEAREEVAELNSKLAELKERIESLERIRTLLA---AIADAEDEIERLREKREALAELNDERR 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 264 DnvemiklhkQLVEKSNALSAMEGKFIQLQ-EKQRTLRISHDALMANGDELNMQLKEQRlkcCSLEKQLHSMKFSERRIE 342
Cdd:PRK02224 627 E---------RLAEKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEEKLDELREER---DDLQAEIGAVENELEELE 694
|
250 260
....*....|....*....|.
gi 816197642 343 ELQDRINDLEKERELLKENYD 363
Cdd:PRK02224 695 ELRERREALENRVEALEALYD 715
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
207-410 |
9.48e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 9.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 207 EIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIElsllqlreqqatdqrsnirdnvemiKLHKQLVEKSNALSAME 286
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE-------------------------DLEKEIKRLELEIEEVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 287 GKFIQLQEKQRTLRishdalmaNGDELNmqlkeqrlkccSLEKQLHSMKfseRRIEELQDRINDLEKERELLKENYDKLy 366
Cdd:COG1579 73 ARIKKYEEQLGNVR--------NNKEYE-----------ALQKEIESLK---RRISDLEDEILELMERIEELEEELAEL- 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 816197642 367 dSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRL 410
Cdd:COG1579 130 -EAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
312-601 |
1.13e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.50 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 312 ELNMQLKEQRLKCCSLEKQLHSMKFSERRIE-----------ELQDRINDLEKERELLKENYD-KLYDSAFSAAHEEQWK 379
Cdd:TIGR01612 562 EIKKELEEENEDSIHLEKEIKDLFDKYLEIDdeiiyinklklELKEKIKNISDKNEYIKKAIDlKKIIENNNAYIDELAK 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 380 LKEQQLKVQIAQLET---ALKSDLTDKTE-ILDRLKTERdqnEKLVQENrelQLQYLEQKQQLDELKKRI-KLYNQENDI 454
Cdd:TIGR01612 642 ISPYQVPEHLKNKDKiysTIKSELSKIYEdDIDALYNEL---SSIVKEN---AIDNTEDKAKLDDLKSKIdKEYDKIQNM 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 455 NADELSEALLLIkaqKEQKNGDLSFLVKVD----SEINKDLERSMRELQATHAE---TVQELEKTRNML-IMQHKINK-- 524
Cdd:TIGR01612 716 ETATVELHLSNI---ENKKNELLDIIVEIKkhihGEINKDLNKILEDFKNKEKElsnKINDYAKEKDELnKYKSKISEik 792
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 816197642 525 -DYQMEVEAVTRKMENLQQDYElKVEQYVHLLDIRAARIHKLEAQLKDiaygtkqykfkpeiMPDDSVDEFDETIHLE 601
Cdd:TIGR01612 793 nHYNDQINIDNIKDEDAKQNYD-KSKEYIKTISIKEDEIFKIINEMKF--------------MKDDFLNKVDKFINFE 855
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
193-539 |
1.36e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 193 FTKYGNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQR--SNIRDNVEMIK 270
Cdd:TIGR00606 696 FISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRlkNDIEEQETLLG 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 271 LHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQlHSMKFSERRIEELQDRIND 350
Cdd:TIGR00606 776 TIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQ-HELDTVVSKIELNRKLIQD 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 351 LEKERELLKENYDKLYDSAFS--------AAHEEQW--KLKE--------QQLKVQIAQLETALKSDLTDKTEILDRLKT 412
Cdd:TIGR00606 855 QQEQIQHLKSKTNELKSEKLQigtnlqrrQQFEEQLveLSTEvqslireiKDAKEQDSPLETFLEKDQQEKEELISSKET 934
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 413 ERDQNEKLVQE-NRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSfLVKVDSEINKDL 491
Cdd:TIGR00606 935 SNKKAQDKVNDiKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMR-LMRQDIDTQKIQ 1013
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 816197642 492 ERSMRE--LQATHAETVQELEKTRNMLIMQhkINKDYQMEVEAVTRKMEN 539
Cdd:TIGR00606 1014 ERWLQDnlTLRKRENELKEVEEELKQHLKE--MGQMQVLQMKQEHQKLEE 1061
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
64-511 |
1.44e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 64 LKQHARKQEDKIKRMATKLIRLvnDKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQ 143
Cdd:TIGR00606 700 LQSKLRLAPDKLKSTESELKKK--EKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTI 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 144 GYRQTPYNNVQSRINTGRRKANEnagLQECPRKgIKFQDADVAETPHPMFTKYGNSLLEEARGEIRNLENVIQSQRGQIE 223
Cdd:TIGR00606 778 MPEEESAKVCLTDVTIMERFQME---LKDVERK-IAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQ 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 224 ELEHLAEILKTQLRR-KENEIELSLLQLREQQATDQRSNIRDNV-EMIKLHKQLVEKSNALSAMEGKFiqLQEKQRTLRI 301
Cdd:TIGR00606 854 DQQEQIQHLKSKTNElKSEKLQIGTNLQRRQQFEEQLVELSTEVqSLIREIKDAKEQDSPLETFLEKD--QQEKEELISS 931
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 302 SHDALMANGDELNMQLKEqrlkccsLEKQLHSMKFSERRIEELQDRiNDLEKERELLKENYDKLYDSAFSAAHEEQWKLK 381
Cdd:TIGR00606 932 KETSNKKAQDKVNDIKEK-------VKNIHGYMKDIENKIQDGKDD-YLKQKETELNTVNAQLEECEKHQEKINEDMRLM 1003
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 382 EQQLKVQIAQlETALKSDLT--DKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQ--LDELKK-------RIKLYNQ 450
Cdd:TIGR00606 1004 RQDIDTQKIQ-ERWLQDNLTlrKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEenIDLIKRnhvlalgRQKGYEK 1082
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 816197642 451 ENDINADELSEALLlikAQKEQKNGDLSFLVKVDSEINKDLERSMRELQAT----HAETVQELEK 511
Cdd:TIGR00606 1083 EIKHFKKELREPQF---RDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAimkfHSMKMEEINK 1144
|
|
| HpsJ_fam |
NF038305 |
HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the ... |
403-499 |
1.66e-03 |
|
HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the biosynthesis or secretion of an extracellular polysaccharide shared by many Cyanobacteria.
Pssm-ID: 468465 [Multi-domain] Cd Length: 230 Bit Score: 41.42 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 403 KTEILDRLKTERDQNEKLVQeNRELQLQYLEQKQQLDELKKRIKLYNQEndINADELSEALL-LIKAQKEQKNGDLSFLV 481
Cdd:NF038305 106 STQALQQINQQAGQQETQLQ-QQLNQLQAQTSPQQLNQLLKSEQKQGQA--LASGQLPEEQKeQLQQFKSNPQALDKFLA 182
|
90
....*....|....*...
gi 816197642 482 KVDSEINKDLERSMRELQ 499
Cdd:NF038305 183 QQLTQIRTQAEEAEKQAR 200
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
112-462 |
1.68e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 112 IEQLQEKVHELEKQNETLKNRLISAKQQLQTQgyrqtpynnvqsrintgRRKANENAGLQEcprkgIKFQDADVAetphp 191
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDAL-----------------QERREALQRLAE-----YSWDEIDVA----- 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 192 mftkygnslleEARGEIRNLENVIQSQR---GQIEELEHLAEILKTQLRRKENEI-----ELSLLQLREQQATDQRSNIR 263
Cdd:COG4913 665 -----------SAEREIAELEAELERLDassDDLAALEEQLEELEAELEELEEELdelkgEIGRLEKELEQAEEELDELQ 733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 264 DNVEMIKLHKQLVEKSNAlsamEGKFIQLQEKQRTLRIShDALMANGDELNMQLKEQRLKccsLEKQLHsmKFSERRIEE 343
Cdd:COG4913 734 DRLEAAEDLARLELRALL----EERFAAALGDAVERELR-ENLEERIDALRARLNRAEEE---LERAMR--AFNREWPAE 803
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 344 LQDRINDLEKERELLKEnYDKLYDSAFsAAHEEQWK-LKEQQLKVQIAQLETALKSDLTDKTEILDRLkterdqNEKLVQ 422
Cdd:COG4913 804 TADLDADLESLPEYLAL-LDRLEEDGL-PEYEERFKeLLNENSIEFVADLLSKLRRAIREIKERIDPL------NDSLKR 875
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 816197642 423 ----ENRELQLQYLE-QKQQLDELKKRIKLYNQENDINADELSEA 462
Cdd:COG4913 876 ipfgPGRYLRLEARPrPDPEVREFRQELRAVTSGASLFDEELSEA 920
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
209-564 |
2.60e-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: 42.08 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 209 RNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQAtdQRSNIRDNVEmiKLHKQLVEKSNALSAMEGK 288
Cdd:pfam01576 211 RKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETA--QKNNALKKIR--ELEAQISELQEDLESERAA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 289 FIQLQEKQRTLrishdalmanGDELNMQLKEqrlkccsLEKQLHSMKFSerriEELQDRindLEKERELLKEnydklyds 368
Cdd:pfam01576 287 RNKAEKQRRDL----------GEELEALKTE-------LEDTLDTTAAQ----QELRSK---REQEVTELKK-------- 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 369 afsaAHEEQWKLKEQQLKvQIAQLETALKSDLTDKTEILDRLKTERDQNEK-LVQENRELQ--LQYLEQKQQLDELKKRi 445
Cdd:pfam01576 335 ----ALEEETRSHEAQLQ-EMRQKHTQALEELTEQLEQAKRNKANLEKAKQaLESENAELQaeLRTLQQAKQDSEHKRK- 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 446 KLYNQENDINA---------DELSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQAThaetvQEL--EKTRN 514
Cdd:pfam01576 409 KLEGQLQELQArlseserqrAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT-----QELlqEETRQ 483
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 816197642 515 MLIMQHKINkdyQMEVEAvTRKMENLQQDYELK--VEQYVHLLDIRAARIHK 564
Cdd:pfam01576 484 KLNLSTRLR---QLEDER-NSLQEQLEEEEEAKrnVERQLSTLQAQLSDMKK 531
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
27-513 |
2.89e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 27 LQETSTTRTMKSRQAVSRVSREELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERvgggpkrlgRDV 106
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE---------EEE 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 107 EMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQgyrQTPYNNVQSRINTGRRKANENAGLQECPRKGIKFQDADVA 186
Cdd:COG1196 460 ALLELLAELLEEAALLEAALAELLEELAEAAARLLLL---LEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 187 ETphpmftkygnsLLEEARGEIRNLENVIQSQRGQieeleHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDnv 266
Cdd:COG1196 537 EA-----------ALEAALAAALQNIVVEDDEVAA-----AAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIG-- 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 267 EMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMA--NGDELNMQLKEQRLkccSLEKQLHSMKFSERRIEEL 344
Cdd:COG1196 599 AAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVtlAGRLREVTLEGEGG---SAGGSLTGGSRRELLAALL 675
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 345 QDRINDLEKERELLKENYDKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQEN 424
Cdd:COG1196 676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 425 RELQLQYLEQKQQLDELKKRIK-LynqeNDIN------ADELSEALLLIKAQKEqkngdlsflvkvdseinkDLERSMRE 497
Cdd:COG1196 756 LPEPPDLEELERELERLEREIEaL----GPVNllaieeYEELEERYDFLSEQRE------------------DLEEARET 813
|
490
....*....|....*.
gi 816197642 498 LQathaETVQELEKTR 513
Cdd:COG1196 814 LE----EAIEEIDRET 825
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
206-437 |
3.04e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.99 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 206 GEIRNLENVIQSQRG----QIEELEHLAEILKTQLRRKEN-------------------EIELSLLQLREQQATDQRSNI 262
Cdd:COG5022 817 ACIIKLQKTIKREKKlretEEVEFSLKAEVLIQKFGRSLKakkrfsllkketiylqsaqRVELAERQLQELKIDVKSISS 896
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 263 RDNVEmIKLHKQLVEKSNALSamegKFIQLQEKQRTLRISHDALMANgdelNMQLKEQRLKCCSLEKQLHSMKFSERRIE 342
Cdd:COG5022 897 LKLVN-LELESEIIELKKSLS----SDLIENLEFKTELIARLKKLLN----NIDLEEGPSIEYVKLPELNKLHEVESKLK 967
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 343 ELQDRINDL-----EKERELLK--ENYDKLYDSAFS------AAHEEQWKLKEqqLKVQIAQLETALKSDLTDKTEiLDR 409
Cdd:COG5022 968 ETSEEYEDLlkkstILVREGNKanSELKNFKKELAElskqygALQESTKQLKE--LPVEVAELQSASKIISSESTE-LSI 1044
|
250 260
....*....|....*....|....*...
gi 816197642 410 LKTERDQNEKLVQENRELQLQYLEQKQQ 437
Cdd:COG5022 1045 LKPLQKLKGLLLLENNQLQARYKALKLR 1072
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
202-534 |
4.09e-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: 41.65 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 202 EEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRK-ENEIELSLLQLREQQATDQRsnIRDN---VEMIKLHkqlve 277
Cdd:pfam17380 306 EEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAmERERELERIRQEERKRELER--IRQEeiaMEISRMR----- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 278 ksnalsamEGKFIQLQEKQRTLRISHDALMANgdELNMQLKEQRLKCCSLEKQLHSMKFSERRIEELQDRINDLEKEREL 357
Cdd:pfam17380 379 --------ELERLQMERQQKNERVRQELEAAR--KVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREM 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 358 lkenydklydsafsaaheEQWKLKEQQLKVQIAQLEtalKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQ 437
Cdd:pfam17380 449 ------------------ERVRLEEQERQQQVERLR---QQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQA 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 438 LDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNgdlsflvKVDSEINKDLERSMRELQATHAEtVQELEKTRNMLi 517
Cdd:pfam17380 508 MIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRK-------QQEMEERRRIQEQMRKATEERSR-LEAMEREREMM- 578
|
330
....*....|....*..
gi 816197642 518 MQHKINKDYQMEVEAVT 534
Cdd:pfam17380 579 RQIVESEKARAEYEATT 595
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
198-569 |
4.46e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.26 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 198 NSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRdNVEMIKLHKQLVE 277
Cdd:pfam05557 89 NKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQL-RQNLEKQQSSLAE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 278 KSNALSAMEGKfIQLQE---------KQRTLRISH-DALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSERRIEELQDR 347
Cdd:pfam05557 168 AEQRIKELEFE-IQSQEqdseivknsKSELARIPElEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREE 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 348 INDLEKERELLKEnydKLydsafsaaheEQWKLKEQQLKVQI-------AQLETALKSDLT---DKTEILDRLKTERDQN 417
Cdd:pfam05557 247 AATLELEKEKLEQ---EL----------QSWVKLAQDTGLNLrspedlsRRIEQLQQREIVlkeENSSLTSSARQLEKAR 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 418 EKLVQENRELQLQYLE-------QKQQLDELKKRIKLYNQE------------NDINADELSEALLLIKAQKEQ------ 472
Cdd:pfam05557 314 RELEQELAQYLKKIEDlnkklkrHKALVRRLQRRVLLLTKErdgyrailesydKELTMSNYSPQLLERIEEAEDmtqkmq 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 473 -KNGDLSFLVKVDSE-------INKDLERSMREL--QATHA------ETVQELEKTRNMLIMQHKINKDYQMEVEAVTRK 536
Cdd:pfam05557 394 aHNEEMEAQLSVAEEelggykqQAQTLERELQALrqQESLAdpsyskEEVDSLRRKLETLELERQRLREQKNELEMELER 473
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 816197642 537 mENLQQDYELKVEQYVHLLD--------IRAARIHKLEAQL 569
Cdd:pfam05557 474 -RCLQGDYDPKKTKVLHLSMnpaaeayqQRKNQLEKLQAEI 513
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
39-517 |
4.54e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 41.28 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 39 RQAVSRVSREELEDrFLRLHDENIL-LKQHARKQEDKIKRMATKLIRLVNDKKryERVGGGPKRLGRDVEMEEMIE-QLQ 116
Cdd:pfam07111 131 RKNLEEGSQRELEE-IQRLHQEQLSsLTQAHEEALSSLTSKAEGLEKSLNSLE--TKRAGEAKQLAEAQKEAELLRkQLS 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 117 EKVHELEKQNETLKNRLISAKQQLQTQGYRQTPYNNVQSRINTGRRKANENAGLQ----------------------ECP 174
Cdd:pfam07111 208 KTQEELEAQVTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQatvellqvrvqslthmlalqeeELT 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 175 RKgikFQDADVAEtphPMFTKYGNSLLEEARGEIRNLENVIQSQrgqieELEHLAEIlkTQLRRKENEIELSLLQLREQQ 254
Cdd:pfam07111 288 RK---IQPSDSLE---PEFPKKCRSLLNRWREKVFALMVQLKAQ-----DLEHRDSV--KQLRGQVAELQEQVTSQSQEQ 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 255 ATDQRSnIRDN-----VEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELN---MQLKEQRLKCCS 326
Cdd:pfam07111 355 AILQRA-LQDKaaeveVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLEttmTRVEQAVARIPS 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 327 LEKQL-------HSMK-FSERRIEELQDRIN-------------DLEKERELLKENYDKLYDSAFSAAH---------EE 376
Cdd:pfam07111 434 LSNRLsyavrkvHTIKgLMARKVALAQLRQEscpppppappvdaDLSLELEQLREERNRLDAELQLSAHliqqevgraRE 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 377 QWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQlQYLEQKQQLDELKKRIKLYNQENDINA 456
Cdd:pfam07111 514 QGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLR-QELTQQQEIYGQALQEKVAEVETRLRE 592
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 816197642 457 DELSEALLLIKAQKEQKNGDLSfLVKVDSEINKDLERS--MRELQATH--------AETVQELEKTRNMLI 517
Cdd:pfam07111 593 QLSDTKRRLNEARREQAKAVVS-LRQIQHRATQEKERNqeLRRLQDEArkeegqrlARRVQELERDKNLML 662
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
199-354 |
5.31e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 199 SLLEEARGEIRNLENVIQ---------SQRGQIEELEhLAEILKTQLRRKENEIELSLLQLREQQAtdqrsnirdnvEMI 269
Cdd:PRK04863 949 QTQRDAKQQAFALTEVVQrrahfsyedAAEMLAKNSD-LNEKLRQRLEQAEQERTRAREQLRQAQA-----------QLA 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 270 KLHKQLvekSNALSAMEGKFIQLQEKQR-----TLRISHDA---LMANGDELNMQLKEQRLKCCSLEKQLhsmKFSERRI 341
Cdd:PRK04863 1017 QYNQVL---ASLKSSYDAKRQMLQELKQelqdlGVPADSGAeerARARRDELHARLSANRSRRNQLEKQL---TFCEAEM 1090
|
170
....*....|...
gi 816197642 342 EELQDRINDLEKE 354
Cdd:PRK04863 1091 DNLTKKLRKLERD 1103
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
327-455 |
5.97e-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: 40.61 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 327 LEKQLHSMKFSERRIEELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQwklKEQQLKVQIAQLETALKSD---LTDK 403
Cdd:pfam06160 279 LEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYTLNENELE---RVRGLEKQLEELEKRYDEIverLEEK 355
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 816197642 404 ----TEILDRLKTERDQNEKLvqenRELQLQYLEQKQQL--DELKKRIKLYNQENDIN 455
Cdd:pfam06160 356 evaySELQEELEEILEQLEEI----EEEQEEFKESLQSLrkDELEAREKLDEFKLELR 409
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
221-416 |
6.77e-03 |
|
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: 39.52 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 221 QIEELEHLAEILK--TQLRRKENEIELSLLQLREQ--QATDQRSNIRDNVEmiKLHKQLVEKSNALSAMEGKFIQLQEKQ 296
Cdd:COG1579 5 DLRALLDLQELDSelDRLEHRLKELPAELAELEDElaALEARLEAAKTELE--DLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 297 RTLRishdalmaNGDELNmqlkeqrlkccSLEKQLHSMKfseRRIEELQDRINDLEKEREllkenydklydsafsaAHEE 376
Cdd:COG1579 83 GNVR--------NNKEYE-----------ALQKEIESLK---RRISDLEDEILELMERIE----------------ELEE 124
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 816197642 377 QWKLKEQQL---KVQIAQLETALKSDLTDKTEILDRLKTERDQ 416
Cdd:COG1579 125 ELAELEAELaelEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
208-452 |
7.07e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 40.43 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 208 IRNLENVIQSQRGQIEELEHLAEILkTQLRRKENEIELSLLQLreQQATDQRSNIRDNVEMIKLHKQLVEKSNALSAMEG 287
Cdd:pfam15742 92 IRELELEVLKQAQSIKSQNSLQEKL-AQEKSRVADAEEKILEL--QQKLEHAHKVCLTDTCILEKKQLEERIKEASENEA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 288 KF-IQLQEKQRTLRIshdaLMANGDELNMQLKEQRLKCCSLE----KQLHSMKFSERRIEELQDRIND------------ 350
Cdd:pfam15742 169 KLkQQYQEEQQKRKL----LDQNVNELQQQVRSLQDKEAQLEmtnsQQQLRIQQQEAQLKQLENEKRKsdehlksnqels 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 351 -----LEKERELLKENYDKLYDSAfsAAHEEQWKLKEQQLKVQIAQL------ETALKS----DLTDKTEILDRL----- 410
Cdd:pfam15742 245 eklssLQQEKEALQEELQQVLKQL--DVHVRKYNEKHHHHKAKLRRAkdrlvhEVEQRDerikQLENEIGILQQQsekek 322
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 816197642 411 ---KTERDQNEKLVQENRELQLQYLEQ-------KQQLDELKKRIKLYNQEN 452
Cdd:pfam15742 323 afqKQVTAQNEILLLEKRKLLEQLTEQeeliknnKRTISSVQNRVNFLDEEN 374
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
244-510 |
8.20e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.30 E-value: 8.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 244 ELSLLQLREQQATDQRSNIRDNVE-MIKLhKQLVEKSNALSAMEGKFIQLQEKQRTLRIshdalmangDELnmqLKEQRL 322
Cdd:PRK05771 27 ELGVVHIEDLKEELSNERLRKLRSlLTKL-SEALDKLRSYLPKLNPLREEKKKVSVKSL---------EEL---IKDVEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 323 KCCSLEKQLHSMkfsERRIEELQDRINDLEKERELLK--ENYD----KLYDSAFSAA-----HEEQWKLKEQQLKVQIAQ 391
Cdd:PRK05771 94 ELEKIEKEIKEL---EEEISELENEIKELEQEIERLEpwGNFDldlsLLLGFKYVSVfvgtvPEDKLEELKLESDVENVE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 392 LET-----------ALKSDLTDKTEILDRLKTERDQ--NEKLVQEN-RELQLQYLEQKQQLDELKKRIKLYNQENDINAD 457
Cdd:PRK05771 171 YIStdkgyvyvvvvVLKELSDEVEEELKKLGFERLEleEEGTPSELiREIKEELEEIEKERESLLEELKELAKKYLEELL 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 816197642 458 ELSEALLLIKAQKEQKNGDLS----FLVK--VDSEINKDLERSMRELQATHAEtVQELE 510
Cdd:PRK05771 251 ALYEYLEIELERAEALSKFLKtdktFAIEgwVPEDRVKKLKELIDKATGGSAY-VEFVE 308
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
198-399 |
8.70e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 198 NSLLEEARGEIRNLENVIQSQRGQIEELEhlAEILKTQLRRKENEIELSLLQLREQQATDQRSN-IRDN---------VE 267
Cdd:COG3883 29 QAELEAAQAELDALQAELEELNEEYNELQ--AELEALQAEIDKLQAEIAEAEAEIEERREELGErARALyrsggsvsyLD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 268 MIKLHK---QLVEKSNALSAMEGKFIQLQEKQRTLRishDALMANGDELNMQLKEQRLKCCSLEKQLHSMkfsERRIEEL 344
Cdd:COG3883 107 VLLGSEsfsDFLDRLSALSKIADADADLLEELKADK---AELEAKKAELEAKLAELEALKAELEAAKAEL---EAQQAEQ 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 816197642 345 QDRINDLEKERELLKENYDKLydSAFSAAHEEQWKLKEQQLKVQIAQLETALKSD 399
Cdd:COG3883 181 EALLAQLSAEEAAAEAQLAEL--EAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
180-573 |
8.93e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 40.33 E-value: 8.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 180 FQDADVAETPHPMFTKYGNSLLEEARGEIRNLENVI-----------QSQRGQIEELEHLAEILKTQLRRKENEIELSLL 248
Cdd:COG5185 113 EWSADILISLLYLYKSEIVALKDELIKVEKLDEIADieasygevetgIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 249 QLREQQATDQRSNIRDNVEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQlKEQRLKCCSLE 328
Cdd:COG5185 193 SELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVE-QNTDLRLEKLG 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 329 KQLHSMKfserRIEELqdrINDLEKERELLKENYDKLYDSAFSAAHEEQWK--LKEQQLKVQIAQLETALKSDLTDKTEI 406
Cdd:COG5185 272 ENAESSK----RLNEN---ANNLIKQFENTKEKIAEYTKSIDIKKATESLEeqLAAAEAEQELEESKRETETGIQNLTAE 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 407 LDRLKTERDQNEKLVQENRElqlqYLEQKQQLDELKKRIKLYNQENDINADELSEALlliKAQKEQKNgdlsflvkvdsE 486
Cdd:COG5185 345 IEQGQESLTENLEAIKEEIE----NIVGEVELSKSSEELDSFKDTIESTKESLDEIP---QNQRGYAQ-----------E 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816197642 487 INKDLERSMRELQATHAETVQELEK-TRNMLIMQHKINKDYQMEVEAVTRKMENLQQDYElkvEQYVHLLDIRAARIHKL 565
Cdd:COG5185 407 ILATLEDTLKAADRQIEELQRQIEQaTSSNEEVSKLLNELISELNKVMREADEESQSRLE---EAYDEINRSVRSKKEDL 483
|
....*...
gi 816197642 566 EAQLKDIA 573
Cdd:COG5185 484 NEELTQIE 491
|
|
| |
