|
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 |
1.52e-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: 1.52e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 597 TIHLERGENLFEIHINKVTFSSEVLQASGDKEPVTFCTYAFYDFELQTTPVVRGLHPEYNFTSQYLVHVNDLFLQYIQKN 676
Cdd:pfam11618 1 TVELERGENLFELHIGGVTFSPEALRALGDKEPSTFCTYDFYDFETQTTPVVRGLNPFYDFTSQYKVTVDDLFLQYLQTN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118442834 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 ... |
1145-1308 |
2.26e-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: 235.39 E-value: 2.26e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 1145 PSEKIRIEIIALSL-NDSQVTMDDTIQRLFVECRFYSLPAE--ETPVSLPKPKSGQWVYYNYSNVIYVDKENNKAKRDIL 1221
Cdd:pfam18111 1 DSDTIRIEIISLQLlNESEVMQDDNIQQLFVEYRFLGRPEEetETPVSLPKPKTGQELYYNFSKVIDVDKEKNSARREIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 1222 KAILQKQEMPNRSLRFTVVSDPPeDEQDLECEDIGVAHVDLADMFQEGRDLIEQNIDVFDARADGEGIGKLRVTVEALHA 1301
Cdd:pfam18111 81 RSMLLPEDPNQGNLKFTVVSEPL-DTEDGECEEIGYAYVDLKQILQSGRDIIEQDLDVKDARDENEQIGKLKVSVEALAA 159
|
....*..
gi 118442834 1302 LQSVYKQ 1308
Cdd:pfam18111 160 LRAIYSE 166
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
201-543 |
2.38e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.99 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEI------LKTQLRRKEneIELSLLQLREQQATDQRsnirdnvemikLHKQ 274
Cdd:COG1196 181 LEATEENLERLEDILGELERQLEPLERQAEKaeryreLKEELKELE--AELLLLKLRELEAELEE-----------LEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 275 LVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHS----MKFSERRIEELQDRIND 350
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARleerRRELEERLEELEEELAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 351 LEKERELLKENYDKLydsafsAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQ 430
Cdd:COG1196 328 LEEELEELEEELEEL------EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 431 YLEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEIN------KDLERSMRELQATHAE 504
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEallellAELLEEAALLEAALAE 481
|
330 340 350
....*....|....*....|....*....|....*....
gi 118442834 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 |
3.94e-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: 84.34 E-value: 3.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIElsllQLREQQATDQRSNIRDNVEMIKLHKQLVEKSN 280
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE----QLEERIAQLSKELTELEAEIEELEERLEEAEE 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 281 ALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKE-------QRLKCCSLEKQLHSmkfSERRIEELQDRINDLEK 353
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanLRERLESLERRIAA---TERRLEDLEEQIEELSE 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 354 ERELLKENYDKLydSAFSAAHEEQWKLKEQQLKVQIAQLEtALKSDLTDKTEILDRLKTERDQNEKLVQENRE----LQL 429
Cdd:TIGR02168 853 DIESLAAEIEEL--EELIEELESELEALLNERASLEEALA-LLRSELEELSEELRELESKRSELRRELEELREklaqLEL 929
|
250
....*....|....*.
gi 118442834 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 |
8.59e-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: 8.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 198 NSLLEEARgEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIElsllqlreqqatdqrsnirdnvemiKLHKQLVE 277
Cdd:TIGR02168 670 SSILERRR-EIEELEEKIEELEEKIAELEKALAELRKELEELEEELE-------------------------QLRKELEE 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 278 KSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSmkfSERRIEELQDRINDLEKEREL 357
Cdd:TIGR02168 724 LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE---AEAEIEELEAQIEQLKEELKA 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 358 LKENYDKLydsafSAAHEEQwKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQ 437
Cdd:TIGR02168 801 LREALDEL-----RAELTLL-NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 438 LDELKKRIklynqendinaDELSEALLLIKAQKEQKNGDLsflvKVDSEINKDLERSMRELQATHAETVQELEKTRNMLI 517
Cdd:TIGR02168 875 LEALLNER-----------ASLEEALALLRSELEELSEEL----RELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 118442834 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 |
3.94e-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: 66.71 E-value: 3.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 792 LHITIRCCNHLQSRASHLQPHPYVVYKFFDFADHDTAIIPSSNDPQFDDHMYFPVPMNMdldrylkSESLSFYVFDDSDT 871
Cdd:cd00030 1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQKFKTKVVKNTLNPVWNETFEFPVLDPE-------SDTLTVEVWDKDRF 73
|
90 100
....*....|....*....|
gi 118442834 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 |
4.94e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 74.32 E-value: 4.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 106 VEMEEMIEQLQEKVHELEKQNETLKnrlisaKQQLQTQGYR--QTPYNNVQSRINTGRRKANenaglqecpRKGIKFQDA 183
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQLKSLE------RQAEKAERYKelKAELRELELALLVLRLEEL---------REELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 184 DVAETphpmftkygNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKT---QLRRKENEIELSLLQLREQQATDQRS 260
Cdd:TIGR02168 247 ELKEA---------EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKelyALANEISRLEQQKQILRERLANLERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 261 NIRDNVEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSER- 339
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAs 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 340 ---RIEELQDRINDLEKERELLKENydklydsafsaAHEEQWKLKEQQLKVQIAQLETaLKSDLTDKTEILDRLkteRDQ 416
Cdd:TIGR02168 398 lnnEIERLEARLERLEDRRERLQQE-----------IEELLKKLEEAELKELQAELEE-LEEELEELQEELERL---EEA 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 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 |
6.06e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.94 E-value: 6.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 101 RLGRDVEmeemIEQLQEKVHELEKQNETLKNRLISAKQQLQT---------QGYRQTPYNNVQSRINTGRRKANENAGLQ 171
Cdd:TIGR02168 672 ILERRRE----IEELEEKIEELEEKIAELEKALAELRKELEEleeeleqlrKELEELSRQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 172 ECPRKGIKFQDADVAETPHpmftkygNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENeiELSLLQLR 251
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEEL-------EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA--ELTLLNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 252 EQQATDQRSNIRDNVEMIK-----LHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRlkccs 326
Cdd:TIGR02168 819 AANLRERLESLERRIAATErrledLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR----- 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 327 lekqlhsmkfseRRIEELQDRINDLEKERELLKENYDKLydsafsAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEI 406
Cdd:TIGR02168 894 ------------SELEELSEELRELESKRSELRRELEEL------REKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE 955
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 407 LDRLkterdqneklvQENRELQLQYLEQKqqLDELKKRIKlynQENDINADELSEAlllikaqkEQKNGDLSFLVKVDSE 486
Cdd:TIGR02168 956 AEAL-----------ENKIEDDEEEARRR--LKRLENKIK---ELGPVNLAAIEEY--------EELKERYDFLTAQKED 1011
|
410
....*....|....*
gi 118442834 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 ... |
48-600 |
1.40e-12 |
|
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: 72.36 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 48 EELEDrflrlhDENILLKQHARKQE--DKIKRMATKLIRLVNDKKRYErvgggpkrlgrdvemeEMIEQLQEKVHELEKQ 125
Cdd:TIGR04523 169 EELEN------ELNLLEKEKLNIQKniDKIKNKLLKLELLLSNLKKKI----------------QKNKSLESQISELKKQ 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 126 NETLKNRLISAKQQLQTQgyrQTPYNNVQSRINTGRRKANEnaglqecprkgIKFQDADvaetphpmftkyGNSLLEEAR 205
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEK---TTEISNTQTQLNQLKDEQNK-----------IKKQLSE------------KQKELEQNN 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 206 GEIRNLENVIQSQRGQIEEL-----EHLAEILKTQLRRKENEIELSLLQLRE-----QQATDQRSNIRD-----NVEMIK 270
Cdd:TIGR04523 281 KKIKELEKQLNQLKSEISDLnnqkeQDWNKELKSELKNQEKKLEEIQNQISQnnkiiSQLNEQISQLKKeltnsESENSE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 271 LHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDAL---MANGDELNmQLKEQRLKCCSLEKQLhsmkfSERRIEELQDR 347
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLeskIQNQEKLN-QQKDEQIKKLQQEKEL-----LEKEIERLKET 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 348 INDLEKE-RELLKENYDK--LYDSAFSAAHEEQWKLKEqqLKVQIAQLETAL---KSDLTDKTEILDRLKTERDQNEKLV 421
Cdd:TIGR04523 435 IIKNNSEiKDLTNQDSVKelIIKNLDNTRESLETQLKV--LSRSINKIKQNLeqkQKELKSKEKELKKLNEEKKELEEKV 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 422 QENRELQLQYLEQKQQLDELKKRI--KLYNQENDINADELSEALLLIKAQKEQKNGDLSFLvkvdSEINKDLERSMRELQ 499
Cdd:TIGR04523 513 KDLTKKISSLKEKIEKLESEKKEKesKISDLEDELNKDDFELKKENLEKEIDEKNKEIEEL----KQTQKSLKKKQEEKQ 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 500 athaETVQELEKTRNMLIMQHKInkdYQMEVEAVTRKMENLQQDYElKVEQYVHLLDIRAARIHKLEAQLKDIAYGTKQY 579
Cdd:TIGR04523 589 ----ELIDQKEKEKKDLIKEIEE---KEKKISSLEKELEKAKKENE-KLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNK 660
|
570 580
....*....|....*....|...
gi 118442834 580 kfKPEIMPD--DSVDEFDETIHL 600
Cdd:TIGR04523 661 --WPEIIKKikESKTKIDDIIEL 681
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
107-570 |
1.79e-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: 68.99 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 107 EMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQGyrqtpyNNVQSRINTGRRKANENAGLQECprkgikfQDADVA 186
Cdd:pfam15921 257 KIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQA------NSIQSQLEIIQEQARNQNSMYMR-------QLSDLE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 187 ETphpmftkygnslLEEARGEIRNLENVIQSQrgqIEELEHLAEILKTQLRRKENEielsllqlrEQQATDQRSNIRDNV 266
Cdd:pfam15921 324 ST------------VSQLRSELREAKRMYEDK---IEELEKQLVLANSELTEARTE---------RDQFSQESGNLDDQL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 267 E--MIKLHKQlvEKSNALSAMEGKfiQLQEKQRTLRISHDALMANGDELNMQ-------LKEQRLKC-CSLEKQLHSMKF 336
Cdd:pfam15921 380 QklLADLHKR--EKELSLEKEQNK--RLWDRDTGNSITIDHLRRELDDRNMEvqrlealLKAMKSECqGQMERQMAAIQG 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 337 SERRIEELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQW------KLKEQQLKVQIAQLE-TALKSDLTDKTEILDR 409
Cdd:pfam15921 456 KNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTvsdltaSLQEKERAIEATNAEiTKLRSRVDLKLQELQH 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 410 LKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQENDINAdELSEALLLIKAQKEQKNGDLSFLVKvDSEINK 489
Cdd:pfam15921 536 LKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHG-RTAGAMQVEKAQLEKEINDRRLELQ-EFKILK 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 490 DLERS-MRELQATHAETvqELEKT--------RNMLIMQHKINKDYQM-EVEAVTRKMENLQQDYELKVEQYVHLLDIRA 559
Cdd:pfam15921 614 DKKDAkIRELEARVSDL--ELEKVklvnagseRLRAVKDIKQERDQLLnEVKTSRNELNSLSEDYEVLKRNFRNKSEEME 691
|
490
....*....|.
gi 118442834 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 |
9.52e-11 |
|
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: 65.17 E-value: 9.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 368 SAFSAAHEEQWKLKEQ--QLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRI 445
Cdd:COG4942 13 LAAAAQADAAAEAEAEleQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 446 KLYNQENDINADELSEalLLIKAQKEQKNGDLSFLVKVDS--------EINKDLERSMRELQATHAETVQELEKTRNMLI 517
Cdd:COG4942 93 AELRAELEAQKEELAE--LLRALYRLGRQPPLALLLSPEDfldavrrlQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 118442834 518 MQHKINKDYQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDI 572
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
64-598 |
3.52e-10 |
|
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: 64.66 E-value: 3.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 64 LKQHARKQEDKIKRMATKLIRLVND-KKRYERVGGGPKRLGRDvemEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQT 142
Cdd:TIGR04523 24 YKNIANKQDTEEKQLEKKLKTIKNElKNKEKELKNLDKNLNKD---EEKINNSNNKIKILEQQIKDLNDKLKKNKDKINK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 143 QGYRQTPYNN-VQSRINTGRRKANENAGLQECPRKGIKFQDADVAE-TPHPMFTKYGNSLLEEARGEIRNLENVIQSQRG 220
Cdd:TIGR04523 101 LNSDLSKINSeIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEiKKKEKELEKLNNKYNDLKKQKEELENELNLLEK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 221 QIEELEHLAEILKTQLRRKE-------------NEIELSLLQLREQQATDQRSNIRDNVEM------------------- 268
Cdd:TIGR04523 181 EKLNIQKNIDKIKNKLLKLElllsnlkkkiqknKSLESQISELKKQNNQLKDNIEKKQQEInektteisntqtqlnqlkd 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 269 --IKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGD-----ELNMQLKEQRLKCCSLEKQLHSmkfSERRI 341
Cdd:TIGR04523 261 eqNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQ---NNKII 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 342 EELQDRINDLEKERELLKENYDKLydsafsaahEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDrLKTERDQNEKlv 421
Cdd:TIGR04523 338 SQLNEQISQLKKELTNSESENSEK---------QRELEEKQNEIEKLKKENQSYKQEIKNLESQIND-LESKIQNQEK-- 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 422 qENRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEaLLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQAT 501
Cdd:TIGR04523 406 -LNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD-LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 502 HAETVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQdyelKVEQYVHLLDIRAARIHKLEAQLKDIAYGTKQYKF 581
Cdd:TIGR04523 484 LEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKE----KIEKLESEKKEKESKISDLEDELNKDDFELKKENL 559
|
570
....*....|....*..
gi 118442834 582 KPEImpddsvDEFDETI 598
Cdd:TIGR04523 560 EKEI------DEKNKEI 570
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
39-572 |
4.45e-10 |
|
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: 64.37 E-value: 4.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 39 RQAVSRVSRE---ELEDRFLRLHDENILLKQHARKQEDKIKRMATKLirlvnDKKRYERVGGGPKRLGRDVEMEEMIEQL 115
Cdd:pfam15921 73 KEHIERVLEEyshQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKL-----QEMQMERDAMADIRRRESQSQEDLRNQL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 116 QEKVHELEKQNETLKNRLISAKQQLQTQGYRQTPYNNVQSRINTGRRKANENAGlqecprKGIKFQDAdvaetphpMFTK 195
Cdd:pfam15921 148 QNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASG------KKIYEHDS--------MSTM 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 196 YGNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRK-----------------ENEIELSLLQLREQQATDQ 258
Cdd:pfam15921 214 HFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKielllqqhqdrieqlisEHEVEITGLTEKASSARSQ 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 259 RSNIRDNVEMIKlhkQLVEKSNA-----LSAMEGKFIQLQEKQRTL-RISHDALmangDELNMQL--KEQRLKCCSLEKQ 330
Cdd:pfam15921 294 ANSIQSQLEIIQ---EQARNQNSmymrqLSDLESTVSQLRSELREAkRMYEDKI----EELEKQLvlANSELTEARTERD 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 331 LHSMKfSERRIEELQDRINDL---EKERELLKENYDKLYD----SAFSAAHEEQwKLKEQQLKVQ-IAQLETALKSDLTD 402
Cdd:pfam15921 367 QFSQE-SGNLDDQLQKLLADLhkrEKELSLEKEQNKRLWDrdtgNSITIDHLRR-ELDDRNMEVQrLEALLKAMKSECQG 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 403 KTEilDRLKTERDQNEKLvQENRELQLQYLEQKQQL----DELK-KRIKLYNQENDINadELSEALLLIKAQKEQKNGDL 477
Cdd:pfam15921 445 QME--RQMAAIQGKNESL-EKVSSLTAQLESTKEMLrkvvEELTaKKMTLESSERTVS--DLTASLQEKERAIEATNAEI 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 478 SFL-VKVDSEIN-----KDLERSMRELQAT-HAETVQELEKTRNMLIMQHKINKDYQ-----------MEVEAVtrKMEN 539
Cdd:pfam15921 520 TKLrSRVDLKLQelqhlKNEGDHLRNVQTEcEALKLQMAEKDKVIEILRQQIENMTQlvgqhgrtagaMQVEKA--QLEK 597
|
570 580 590
....*....|....*....|....*....|...
gi 118442834 540 LQQDYELKVEQYVHLLDIRAARIHKLEAQLKDI 572
Cdd:pfam15921 598 EINDRRLELQEFKILKDKKDAKIRELEARVSDL 630
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
201-512 |
5.23e-10 |
|
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: 64.32 E-value: 5.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLR--EQQATDQRSNIRDNVEMI-----KLHK 273
Cdd:TIGR02169 697 LRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSslEQEIENVKSELKELEARIeeleeDLHK 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 274 qLVEKSNALSAMEG--KFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKqlhSMKFSERRIEELQDRINDL 351
Cdd:TIGR02169 777 -LEEALNDLEARLShsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEK---EIQELQEQRIDLKEQIKSI 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 352 EKERELLKenydklydsafsaAHEEQWKLKEQQLKVQIAQLETALKSdltdkteildrLKTERDQNEKlvqENRELQLQY 431
Cdd:TIGR02169 853 EKEIENLN-------------GKKEELEEELEELEAALRDLESRLGD-----------LKKERDELEA---QLRELERKI 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 432 LEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSfLVKVDSEINKdLERSMRELQATHAETVQELEK 511
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQR-VEEEIRALEPVNMLAIQEYEE 983
|
.
gi 118442834 512 T 512
Cdd:TIGR02169 984 V 984
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
109-572 |
5.68e-10 |
|
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: 63.89 E-value: 5.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 109 EEMIEQLQEKVHELEKQNETLKNRLISAKQQLQtqgyrqtpynNVQSRINTGRRKANENAGLQECPRKGIKFQDADVAET 188
Cdd:TIGR04523 151 EKELEKLNNKYNDLKKQKEELENELNLLEKEKL----------NIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQI 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 189 PHpmFTKYGNSL---LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELS-----------------LL 248
Cdd:TIGR04523 221 SE--LKKQNNQLkdnIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNnkkikelekqlnqlkseIS 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 249 QLREQQATDQRSNIRDNVEMIKlhKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLE 328
Cdd:TIGR04523 299 DLNNQKEQDWNKELKSELKNQE--KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLK 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 329 KQLHSMKFSerrIEELQDRINDLE------KERELLKENYDKLYDSAFSAAHEEQWKLKEQ---------QLKVQIAQLE 393
Cdd:TIGR04523 377 KENQSYKQE---IKNLESQINDLEskiqnqEKLNQQKDEQIKKLQQEKELLEKEIERLKETiiknnseikDLTNQDSVKE 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 394 TALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEALLLI------K 467
Cdd:TIGR04523 454 LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIekleseK 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 468 AQKEQKNGDL-SFLVKVDSEINKD-LERSMRELQathaETVQELEKTRNMLIMQHK----INKDYQMEVEAVTRKMENlq 541
Cdd:TIGR04523 534 KEKESKISDLeDELNKDDFELKKEnLEKEIDEKN----KEIEELKQTQKSLKKKQEekqeLIDQKEKEKKDLIKEIEE-- 607
|
490 500 510
....*....|....*....|....*....|.
gi 118442834 542 qdYELKVEQYVHLLDIRAARIHKLEAQLKDI 572
Cdd:TIGR04523 608 --KEKKISSLEKELEKAKKENEKLSSIIKNI 636
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
211-569 |
5.97e-10 |
|
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: 64.04 E-value: 5.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 211 LENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQrsnirdnvemiKLHKQLVEKSNALSAMEGKFI 290
Cdd:pfam01576 73 LEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQ-----------KLQLEKVTTEAKIKKLEEDIL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 291 QLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSmkfSERRIEELQDRINDLEKERELLKENYDKLyDSAF 370
Cdd:pfam01576 142 LLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNK---HEAMISDLEERLKKEEKGRQELEKAKRKL-EGES 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 371 SAAHEEQWKLKEQ--QLKVQIAQLETALKSdltdkteILDRLKTERDQNEKLVQENRELQLQYLEQKQQLD-ELKKRIKL 447
Cdd:pfam01576 218 TDLQEQIAELQAQiaELRAQLAKKEEELQA-------ALARLEEETAQKNNALKKIRELEAQISELQEDLEsERAARNKA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 448 YNQENDINAD------ELSEALLLIKAQKE---QKNGDLSFLVKVDSEINKDLERSMRELQATHAETVQE---------- 508
Cdd:pfam01576 291 EKQRRDLGEElealktELEDTLDTTAAQQElrsKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEElteqleqakr 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118442834 509 -----------LEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQL 569
Cdd:pfam01576 371 nkanlekakqaLESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSEL 442
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
216-572 |
1.27e-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: 63.16 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 216 QSQRGQIEELEHLAEILKTQLRRKENEIElsllqlreqQATDQRSNirdnvemikLHKQLVEKSNALSAMEGKFIQLQEK 295
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLD---------ELSQELSD---------ASRKIGEIEKEIEQLEQEEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 296 ----QRTLRISHDALMANGDE---LNMQLKEQRLKCCSLEKQLHSMK--FSERRIEELQDRINDLEKER--------ELL 358
Cdd:TIGR02169 739 leelEEDLSSLEQEIENVKSElkeLEARIEELEEDLHKLEEALNDLEarLSHSRIPEIQAELSKLEEEVsriearlrEIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 359 KENYDKLYDSAFsaAHEEQWKLKEQQ--LKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQ 436
Cdd:TIGR02169 819 QKLNRLTLEKEY--LEKEIQELQEQRidLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 437 QLDELKKRIklynQENDINADELSEALLLIKAQKEQKNGDLSflvkvdseinkDLERSMRELQATHAETVQElektrnml 516
Cdd:TIGR02169 897 QLRELERKI----EELEAQIEKKRKRLSELKAKLEALEEELS-----------EIEDPKGEDEEIPEEELSL-------- 953
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118442834 517 imqhkinKDYQMEVEAVTRKMENLQ-------QDYELKVEQYVHLLDIRAarihKLEAQLKDI 572
Cdd:TIGR02169 954 -------EDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRA----KLEEERKAI 1005
|
|
| C2 |
smart00239 |
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ... |
792-887 |
1.57e-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: 56.34 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 792 LHITIRCCNHLQSRASHLQPHPYVVYKFFDFADHD--TAIIPSSNDPQFDDHMYFPVPmnmdldrYLKSESLSFYVFDDS 869
Cdd:smart00239 2 LTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKkkTKVVKNTLNPVWNETFEFEVP-------PPELAELEIEVYDKD 74
|
90
....*....|....*...
gi 118442834 870 DTQENIYIGKVNVPLISL 887
Cdd:smart00239 75 RFGRDDFIGQVTIPLSDL 92
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
107-566 |
2.31e-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: 61.91 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 107 EMEEMIEQLQEKVHELEKQNETL--KNRLISAKQQLQTQGYRQTP----YNNVQSRINTGRRKAN---ENAGLQECpRKG 177
Cdd:TIGR00618 230 HLREALQQTQQSHAYLTQKREAQeeQLKKQQLLKQLRARIEELRAqeavLEETQERINRARKAAPlaaHIKAVTQI-EQQ 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 178 IKFQDADVAETphpmftkygnsllEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQ--LRRKENEIELSLLQLREQQA 255
Cdd:TIGR00618 309 AQRIHTELQSK-------------MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQeiHIRDAHEVATSIREISCQQH 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 256 TDqRSNIRDNVEMIKLhkqLVEKSNALSAMEGKFIQLQEKQRTLRISHDAL----MANGDELNMQLKEQRLKCCSLEKQL 331
Cdd:TIGR00618 376 TL-TQHIHTLQQQKTT---LTQKLQSLCKELDILQREQATIDTRTSAFRDLqgqlAHAKKQQELQQRYAELCAAAITCTA 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 332 HSMKFSERRIEELQDRInDLEKERELLKENYDKLYdsafsaahEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLK 411
Cdd:TIGR00618 452 QCEKLEKIHLQESAQSL-KEREQQLQTKEQIHLQE--------TRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDN 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 412 TERDQNEKLVQENRELQLQYLEQK--QQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEINK 489
Cdd:TIGR00618 523 PGPLTRRMQRGEQTYAQLETSEEDvyHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEK 602
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 118442834 490 DLERSMRELQATHAETVQELEKTRNMLIMQH--KINKDYQMEVEAVTRKMENLQQDyelkvEQYVHLLDIRAARIHKLE 566
Cdd:TIGR00618 603 LSEAEDMLACEQHALLRKLQPEQDLQDVRLHlqQCSQELALKLTALHALQLTLTQE-----RVREHALSIRVLPKELLA 676
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
201-446 |
3.08e-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: 60.55 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIelsllQLREQQATDQRSNIRDN-VEMIKLHKQLVEKS 279
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI-----RALEQELAALEAELAELeKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 280 NALSAMegkfiqLQEKQRTLRISHDALMANGDELNMQLKEQRlkccsLEKQLhsMKFSERRIEELQDRINDLEKERELLK 359
Cdd:COG4942 104 EELAEL------LRALYRLGRQPPLALLLSPEDFLDAVRRLQ-----YLKYL--APARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 360 ENYDKLydsafsaaheeqwklkeQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEklvQENRELQLQYLEQKQQLD 439
Cdd:COG4942 171 AERAEL-----------------EALLAELEEERAALEALKAERQKLLARLEKELAELA---AELAELQQEAEELEALIA 230
|
....*..
gi 118442834 440 ELKKRIK 446
Cdd:COG4942 231 RLEAEAA 237
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
341-573 |
4.15e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 4.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 341 IEELQDRINDLEKEREL------LKENYdKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTER 414
Cdd:COG1196 195 LGELERQLEPLERQAEKaeryreLKEEL-KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 415 DQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEInKDLERS 494
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL-EEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 495 MRELQATHAETVQEL-EKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDIA 573
Cdd:COG1196 353 LEEAEAELAEAEEALlEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
|
| C2 |
pfam00168 |
C2 domain; |
792-899 |
6.02e-09 |
|
C2 domain;
Pssm-ID: 425499 [Multi-domain] Cd Length: 104 Bit Score: 54.63 E-value: 6.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 792 LHITIRCCNHLQSRASHLQPHPYV-VYKFFDFADHDTAIIPSSNDPQFDDHMYFPVPMNMDldrylksESLSFYVFDDSD 870
Cdd:pfam00168 3 LTVTVIEAKNLPPKDGNGTSDPYVkVYLLDGKQKKKTKVVKNTLNPVWNETFTFSVPDPEN-------AVLEIEVYDYDR 75
|
90 100
....*....|....*....|....*....
gi 118442834 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 |
6.57e-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: 59.39 E-value: 6.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 273 KQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLhsmKFSERRIEELQDRINDLE 352
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL---AALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 353 KERELLKENYDKLYDSAFSAAHEEQWKLK---------------EQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQN 417
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPLALLlspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118442834 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 |
3.14e-08 |
|
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: 58.26 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 229 AEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNV-----------EM-IKLHKQLVEKSNALSAMEGKFIQLQEKQ 296
Cdd:pfam01576 12 EELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLqaetelcaeaeEMrARLAARKQELEEILHELESRLEEEEERS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 297 RTLRISHDALMANGDELNMQLKE-----QRLKccsLEKQL--HSMKFSERRIEELQDRINDLEKERELLKEnydKLYDSA 369
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLEEQLDEeeaarQKLQ---LEKVTteAKIKKLEEDILLLEDQNSKLSKERKLLEE---RISEFT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 370 FSAAHEEQWKLKEQQLKVQiaqlETALKSDLTDkteildRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYN 449
Cdd:pfam01576 166 SNLAEEEEKAKSLSKLKNK----HEAMISDLEE------RLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 450 QENDINADELSEALLLIKAQKEQKNgdlsflvkvdseinkDLERSMRELQATHAETVQELEKTRNMLIMQHKINKDYQME 529
Cdd:pfam01576 236 AQLAKKEEELQAALARLEEETAQKN---------------NALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEE 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 118442834 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 |
3.17e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 58.21 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 49 ELEDRFLRLHDEnilLKQHARKQEDKIKRMATKLIrLVNDK---KRYERVGGGPKRLGRDVEMEEMIEQLQEKVHEL--- 122
Cdd:pfam15921 321 DLESTVSQLRSE---LREAKRMYEDKIEELEKQLV-LANSElteARTERDQFSQESGNLDDQLQKLLADLHKREKELsle 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 123 EKQNETLKNR----------------------------LISAKQQLQTQGYRQTPynNVQSRINTGRRKANENAGLQ--- 171
Cdd:pfam15921 397 KEQNKRLWDRdtgnsitidhlrrelddrnmevqrlealLKAMKSECQGQMERQMA--AIQGKNESLEKVSSLTAQLEstk 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 172 ECPRKGIKFQDAD--VAETPHPMFTKYGNSLLEEARG-EIRNLEnvIQSQRGQI----EELEHLAEiLKTQLRRKENEIE 244
Cdd:pfam15921 475 EMLRKVVEELTAKkmTLESSERTVSDLTASLQEKERAiEATNAE--ITKLRSRVdlklQELQHLKN-EGDHLRNVQTECE 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 245 LSLLQLREQQATDQ--RSNIRDNVEMIKLHKQ-----LVEKSNALSAMEGKFIQLQEkqrtLRISHDALMANGDELNMQL 317
Cdd:pfam15921 552 ALKLQMAEKDKVIEilRQQIENMTQLVGQHGRtagamQVEKAQLEKEINDRRLELQE----FKILKDKKDAKIRELEARV 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 318 KEQRLKCCSL----EKQLHSMKFSERRIEELQDRINDLEKERELLKENYDKLydsafsaahEEQWKLKEQQLKVQIAQLE 393
Cdd:pfam15921 628 SDLELEKVKLvnagSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVL---------KRNFRNKSEEMETTTNKLK 698
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 394 TALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKlYNQENDINADELSEALllikaqKEQK 473
Cdd:pfam15921 699 MQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQ-FLEEAMTNANKEKHFL------KEEK 771
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 474 NGDLSFLVKVDSEINKdlerSMRELQATHAETVQELEKTRNMLIMQHKINKDYQmEVEAVTRKMEnlQQDYELKVEqyvH 553
Cdd:pfam15921 772 NKLSQELSTVATEKNK----MAGELEVLRSQERRLKEKVANMEVALDKASLQFA-ECQDIIQRQE--QESVRLKLQ---H 841
|
....*
gi 118442834 554 LLDIR 558
Cdd:pfam15921 842 TLDVK 846
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
48-569 |
6.65e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 6.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 48 EELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRL-GRDVEMEEMIEQLQEKVHELEKQN 126
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLeEKIRELEERIEELKKEIEELEEKV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 127 ETLKN---------RLISAKQQLQTQGYR--------QTPYNNVQSRINTGRRKANENAGLQEcPRKGIKfQDADVAETP 189
Cdd:PRK03918 283 KELKElkekaeeyiKLSEFYEEYLDELREiekrlsrlEEEINGIEERIKELEEKEERLEELKK-KLKELE-KRLEELEER 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 190 HpmftkygnSLLEEARGEIRNLENViqSQRGQIEELEHLAEILKTQLRRKEnEIELSLLQLREQQAT--DQRSNIRDNVE 267
Cdd:PRK03918 361 H--------ELYEEAKAKKEELERL--KKRLTGLTPEKLEKELEELEKAKE-EIEEEISKITARIGElkKEIKELKKAIE 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 268 MIKLHK----------------QLVEKSNA-LSAMEGKFIQLQEKQRTLRishdalmANGDELNMQLKEQR--LKCCSLE 328
Cdd:PRK03918 430 ELKKAKgkcpvcgrelteehrkELLEEYTAeLKRIEKELKEIEEKERKLR-------KELRELEKVLKKESelIKLKELA 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 329 KQLHSM--KFSERRIEELQDRindlEKERELLKENYDKLyDSAFSAAHEEQWKLKEqqLKVQIAQLETALKSDLTDKTEI 406
Cdd:PRK03918 503 EQLKELeeKLKKYNLEELEKK----AEEYEKLKEKLIKL-KGEIKSLKKELEKLEE--LKKKLAELEKKLDELEEELAEL 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 407 LDRLKTE----RDQNEKLVQENRELQLQYLEQK---QQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNgdlSF 479
Cdd:PRK03918 576 LKELEELgfesVEELEERLKELEPFYNEYLELKdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE---EL 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 480 LVKVDSEINKDLERSMRELQATHA----------ETVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQDYElKVE 549
Cdd:PRK03918 653 EKKYSEEEYEELREEYLELSRELAglraeleeleKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELRE-KVK 731
|
570 580
....*....|....*....|.
gi 118442834 550 QYVHLLDIRA-ARIHKLEAQL 569
Cdd:PRK03918 732 KYKALLKERAlSKVGEIASEI 752
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
201-573 |
8.37e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 8.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNVEMIKLH-KQLVEKS 279
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERlEELRELE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 280 NALSAMEGKFIQLQEKQRTLRISHDAlmangdelnmqLKEQRLKccSLEKQLHSMkfsERRIEELQDRINDLEKERELLK 359
Cdd:COG4717 163 EELEELEAELAELQEELEELLEQLSL-----------ATEEELQ--DLAEELEEL---QQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 360 ENYDKLYDSAFSAAHEEQWKLKEQQLKV--QIAQLETALKSDLTDKTEILDRLKT---------ERDQNEKLVQENRELQ 428
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARLLLLIaaALLALLGLGGSLLSLILTIAGVLFLvlgllallfLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 429 LQYLEQKQQLD--ELKKRIKLYNQENDINADELSEALLLIKAQKEQkngdLSFLVKVDSEInkDLERSMRELQATHAETV 506
Cdd:COG4717 307 LQALPALEELEeeELEELLAALGLPPDLSPEELLELLDRIEELQEL----LREAEELEEEL--QLEELEQEIAALLAEAG 380
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 118442834 507 QELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLqqDYELKVEQYVHLLDIRAARIHKLEAQLKDIA 573
Cdd:COG4717 381 VEDEEELRAALEQAEEYQELKEELEELEEQLEEL--LGELEELLEALDEEELEEELEELEEELEELE 445
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
66-594 |
1.10e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 66 QHARKQEDKIKRMATKLiRLVNDKKRYERVGggpKRLgrdVEMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQGY 145
Cdd:COG4913 265 AAARERLAELEYLRAAL-RLWFAQRRLELLE---AEL---EELRAELARLEAELERLEARLDALREELDELEAQIRGNGG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 146 RQTpyNNVQSRINTGRRKANENAGLQECPRKGIKFQDADVAETPhpmftkygnSLLEEARGEIRNLENVIQSQRGQIEEL 225
Cdd:COG4913 338 DRL--EQLEREIERLERELEERERRRARLEALLAALGLPLPASA---------EEFAALRAEAAALLEALEEELEALEEA 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 226 EHLAEILKTQLRRKENEIELSLLQLREqqatdQRSNIRDnvEMIKLHKQLVEksnALSAME------GKFIQLQEKQ--- 296
Cdd:COG4913 407 LAEAEAALRDLRRELRELEAEIASLER-----RKSNIPA--RLLALRDALAE---ALGLDEaelpfvGELIEVRPEEerw 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 297 --------RTLRIS---------------------------------HDALMANGDE-----------------LNMQLK 318
Cdd:COG4913 477 rgaiervlGGFALTllvppehyaaalrwvnrlhlrgrlvyervrtglPDPERPRLDPdslagkldfkphpfrawLEAELG 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 319 EQR-LKCCSLEKQLHSMKFS---------------------------------------ERRIEELQDRINDLEKERELL 358
Cdd:COG4913 557 RRFdYVCVDSPEELRRHPRAitragqvkgngtrhekddrrrirsryvlgfdnraklaalEAELAELEEELAEAEERLEAL 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 359 KENYDKL--YDSAFSAAHEEQWKLKE-QQLKVQIAQLETALKsDLTDKTEILDRLKTERDQNEK----LVQENRELQLQY 431
Cdd:COG4913 637 EAELDALqeRREALQRLAEYSWDEIDvASAEREIAELEAELE-RLDASSDDLAALEEQLEELEAeleeLEEELDELKGEI 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 432 LEQKQQLDELKKRIK-LYNQENDINADELSEALLLIKAQKEQKNGDlsflvKVDSEINKDLERSMRELQATHAETVQELE 510
Cdd:COG4913 716 GRLEKELEQAEEELDeLQDRLEAAEDLARLELRALLEERFAAALGD-----AVERELRENLEERIDALRARLNRAEEELE 790
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 511 KTRnmlimqHKINKDYQMEVEAVT----------RKMENLQQD----YELK------------VEQYVHLLD--IRAA-- 560
Cdd:COG4913 791 RAM------RAFNREWPAETADLDadleslpeylALLDRLEEDglpeYEERfkellnensiefVADLLSKLRraIREIke 864
|
650 660 670
....*....|....*....|....*....|....*
gi 118442834 561 RIHKLEAQLKDIAYGT-KQYKFKPEIMPDDSVDEF 594
Cdd:COG4913 865 RIDPLNDSLKRIPFGPgRYLRLEARPRPDPEVREF 899
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
219-580 |
1.55e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 219 RGQIEELehlAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNVEmiKLHKQlveKSNALsamegKFIQLQEKQRT 298
Cdd:COG1196 158 RAIIEEA---AGISKYKERKEEAERKLEATEENLERLEDILGELERQLE--PLERQ---AEKAE-----RYRELKEELKE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 299 LRISHDALmangdelnmQLKEQRLKccsLEKQLHSMKFSERRIEELQDRINDLEKERELLKENYDKLyDSAFSAAHEEqw 378
Cdd:COG1196 225 LEAELLLL---------KLRELEAE---LEELEAELEELEAELEELEAELAELEAELEELRLELEEL-ELELEEAQAE-- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 379 klkEQQLKVQIAQLETALKSDLTDKTEILDRLkterdqnEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQEndinADE 458
Cdd:COG1196 290 ---EYELLAELARLEQDIARLEERRRELEERL-------EELEEELAELEEELEELEEELEELEEELEEAEEE----LEE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 459 LSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQATHAEtVQELEKTRNMLIMQHKINKDYQMEVEAVTRKME 538
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ-LEELEEAEEALLERLERLEEELEELEEALAELE 434
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 118442834 539 NLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDIAYGTKQYK 580
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
65-549 |
2.70e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 65 KQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELEKQNEtLKNRLISAKqqlqtqg 144
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADE-AKKKAEEAK------- 1444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 145 yrqtpynnvqsRINTGRRKANENAGLQECPRKGIKFQDADVAETPHPMFTKygnslLEEARGEIRNLENVIQSQRGQIEE 224
Cdd:PTZ00121 1445 -----------KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK-----ADEAKKKAEEAKKKADEAKKAAEA 1508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 225 LEHLAEILKTQLRRKENEIElsllQLREQQATDQRSNIRDNVEMIKLHK-QLVEKSNALSAMEGKFIQLQEKQRTLRISh 303
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAK----KAEEAKKADEAKKAEEKKKADELKKaEELKKAEEKKKAEEAKKAEEDKNMALRKA- 1583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 304 dalmangdELNMQLKEQRL-KCCSLEKQLHSMKFSE-RRIEELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQWKLK 381
Cdd:PTZ00121 1584 --------EEAKKAEEARIeEVMKLYEEEKKMKAEEaKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 382 EQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKK--RIKLYNQENDINADEL 459
Cdd:PTZ00121 1656 EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKaeELKKAEEENKIKAEEA 1735
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 460 SEallliKAQKEQKNGDlsfLVKVDSEINKDLERSMRELQATHAETVQELEKtrnmlIMQHKINKDYQMEVEAVTRKMEN 539
Cdd:PTZ00121 1736 KK-----EAEEDKKKAE---EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA-----VIEEELDEEDEKRRMEVDKKIKD 1802
|
490
....*....|
gi 118442834 540 LQQDYELKVE 549
Cdd:PTZ00121 1803 IFDNFANIIE 1812
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
206-446 |
2.74e-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: 55.46 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 206 GEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIElSLLQLREQQA---------------------TDQRSNIRD 264
Cdd:TIGR02169 230 KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLE-EIEQLLEELNkkikdlgeeeqlrvkekigelEAEIASLER 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 265 NV-----EMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKqlhsmKFSER 339
Cdd:TIGR02169 309 SIaekerELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDK-----EFAET 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 340 RIE--ELQDRINDLEKERELLKENYDKLYDSAfsaaheEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQN 417
Cdd:TIGR02169 384 RDElkDYREKLEKLKREINELKRELDRLQEEL------QRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
250 260
....*....|....*....|....*....
gi 118442834 418 EKLVQENRELQLQYLEQKQQLDELKKRIK 446
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKELS 486
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
47-571 |
2.89e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 47 REELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDV-EMEEMIEQLQEKVHELEKQ 125
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIsRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 126 NETLKNRLISAKQQLQTQGYR----QTPYNNVQSRINTGRRKANENAGLQECPRKGIKFQDAdvaetphpmftkygnsLL 201
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEElaelEEKLEELKEELESLEAELEELEAELEELESRLEELEE----------------QL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 202 EEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNVEMI------------ 269
Cdd:TIGR02168 382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELeelqeelerlee 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 270 ---KLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFS---ERRIEE 343
Cdd:TIGR02168 462 aleELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDegyEAAIEA 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 344 -LQDRINDLEKER--------ELLKEN---------YDKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALK-----SDL 400
Cdd:TIGR02168 542 aLGGRLQAVVVENlnaakkaiAFLKQNelgrvtflpLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKlrkalSYL 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 401 TDKTEILDRLKTERDQNEKLVQENR--------------------ELQLQYLEQKQQLDELKKRIKLynQENDINA---- 456
Cdd:TIGR02168 622 LGGVLVVDDLDNALELAKKLRPGYRivtldgdlvrpggvitggsaKTNSSILERRREIEELEEKIEE--LEEKIAEleka 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 457 -DELSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQaTHAETVQELEKTRNMLIMQHKINKDY----QMEVE 531
Cdd:TIGR02168 700 lAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE-QLEERIAQLSKELTELEAEIEELEERleeaEEELA 778
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 118442834 532 AVTRKMENLQQDyelkVEQYVHLLDIRAARIHKLEAQLKD 571
Cdd:TIGR02168 779 EAEAEIEELEAQ----IEQLKEELKALREALDELRAELTL 814
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
148-511 |
3.19e-07 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 54.91 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 148 TPYNNVQSRINTGRRKANENAGLQECPRKGIKFQDADVAetphpmftkygnslLEEARGEIRNLE-NVIQSQRGQIEELE 226
Cdd:PLN02939 91 TSSDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQ--------------LEDLVGMIQNAEkNILLLNQARLQALE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 227 HLAEIL--KTQLRRKENEIELSLLQLREQQATDQRSNIrdNVEMikLHKQLVEKSNALSAmegkfiqlqekqrTLRISHD 304
Cdd:PLN02939 157 DLEKILteKEALQGKINILEMRLSETDARIKLAAQEKI--HVEI--LEEQLEKLRNELLI-------------RGATEGL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 305 ALMANGDELNMqLKEQRLkccSLEKQLHSMKFSERRIEELQDRINDLEKERELLKENYDKLyDSAFSAAHEEQWKLKEQQ 384
Cdd:PLN02939 220 CVHSLSKELDV-LKEENM---LLKDDIQFLKAELIEVAETEERVFKLEKERSLLDASLREL-ESKFIVAQEDVSKLSPLQ 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 385 LKVQIAQLETalksdLTDkteILDRLKTERDQNEKLVQENRELqlqyleqKQQLDELKKRIKLYN--QENDINADELSEA 462
Cdd:PLN02939 295 YDCWWEKVEN-----LQD---LLDRATNQVEKAALVLDQNQDL-------RDKVDKLEASLKEANvsKFSSYKVELLQQK 359
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 118442834 463 LLLIKAQKEQKNGDLSFLVKVdseinkdLERSMRELQATHAETVQELEK 511
Cdd:PLN02939 360 LKLLEERLQASDHEIHSYIQL-------YQESIKEFQDTLSKLKEESKK 401
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
341-578 |
5.00e-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: 5.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 341 IEELQDRINDLEKERELlKENYDKLydsafsaaheeQWKLKEQQLKVQIAQLETALKSdltdKTEILDRLKTERDQNEKL 420
Cdd:TIGR02169 193 IDEKRQQLERLRREREK-AERYQAL-----------LKEKREYEGYELLKEKEALERQ----KEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 421 VQENRELQLQYLEQKQQLDELKKRIKlynQENDINADELSEALLLIKAQKEQKNGDLSF-----------LVKVDSEINK 489
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEELNKKIK---DLGEEEQLRVKEKIGELEAEIASLERSIAEkereledaeerLAKLEAEIDK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 490 ------DLERSMRELQATHA---ETVQELEKTRNMLIMQ-------HKI----NKDYQMEVEAVTRKMENLQQDY----E 545
Cdd:TIGR02169 334 llaeieELEREIEEERKRRDkltEEYAELKEELEDLRAEleevdkeFAEtrdeLKDYREKLEKLKREINELKRELdrlqE 413
|
250 260 270
....*....|....*....|....*....|....*....
gi 118442834 546 LKVEQYVHLLDIRA------ARIHKLEAQLKDIAYGTKQ 578
Cdd:TIGR02169 414 ELQRLSEELADLNAaiagieAKINELEEEKEDKALEIKK 452
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
200-569 |
5.25e-07 |
|
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: 54.34 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 200 LLEEARGEIRNLENVIQSQ----RGQIEELEHLA---EILKTQLRR-----KENEIELSLLQLREQQATDQRSnirdnVE 267
Cdd:pfam05483 262 LLEESRDKANQLEEKTKLQdenlKELIEKKDHLTkelEDIKMSLQRsmstqKALEEDLQIATKTICQLTEEKE-----AQ 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 268 MIKLHKQLVEKSNALSAMEGKFIQLQEkqrTLRISHDALMANGDELNMQLKEQRLKCCSLEKQlhsMKFSERRIEELQDR 347
Cdd:pfam05483 337 MEELNKAKAAHSFVVTEFEATTCSLEE---LLRTEQQRLEKNEDQLKIITMELQKKSSELEEM---TKFKNNKEVELEEL 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 348 INDLEKERELLKEN--YDKLYDSAFSAAHEEQWKLKEQQ-----LKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKL 420
Cdd:pfam05483 411 KKILAEDEKLLDEKkqFEKIAEELKGKEQELIFLLQAREkeihdLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIEL 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 421 VQENRELQLQYLEQKQQLDELKkrIKLYNQENDINADELSEALLL-----IKAQKEQKNGDLSF----LVKVDSEINKDL 491
Cdd:pfam05483 491 TAHCDKLLLENKELTQEASDMT--LELKKHQEDIINCKKQEERMLkqienLEEKEMNLRDELESvreeFIQKGDEVKCKL 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 492 ERSMRELQATHAETvqeLEKTRNMLIMQHKINkDYQMEVEAVTRKMENLQQD---YELKVEQYVHLLDIRAARIHKLEAQ 568
Cdd:pfam05483 569 DKSEENARSIEYEV---LKKEKQMKILENKCN-NLKKQIENKNKNIEELHQEnkaLKKKGSAENKQLNAYEIKVNKLELE 644
|
.
gi 118442834 569 L 569
Cdd:pfam05483 645 L 645
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
201-463 |
7.68e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 7.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 201 LEEARGEIRNLEnviqsqrgqiEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRdnvemIKLHKQLVEKSN 280
Cdd:COG4913 237 LERAHEALEDAR----------EQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRR-----LELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 281 ALSAmegkfiQLQEKQRTLRISHDALMANGDELNMQLKEQRLkccslekqlhsmkfseRRIEELQDRINDLEKERELLKE 360
Cdd:COG4913 302 AELA------RLEAELERLEARLDALREELDELEAQIRGNGG----------------DRLEQLEREIERLERELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 361 NYDKlYDSAFSAAHEEqWKLKEQQLKVQIAQLETALksdlTDKTEILDRLKTERDQnekLVQENRELQLQYLEQKQQLDE 440
Cdd:COG4913 360 RRAR-LEALLAALGLP-LPASAEEFAALRAEAAALL----EALEEELEALEEALAE---AEAALRDLRRELRELEAEIAS 430
|
250 260
....*....|....*....|...
gi 118442834 441 LKKRIKLYNQENDINADELSEAL 463
Cdd:COG4913 431 LERRKSNIPARLLALRDALAEAL 453
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
47-365 |
9.54e-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: 9.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 47 REELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVN-DKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELEKQ 125
Cdd:TIGR02168 718 RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTElEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 126 NETLKNRLISAKQQLQTQgyrqtpynnvqsrintgrrkaNENAGLQECPRKGIKFQDADVAETphpmftkygnslLEEAR 205
Cdd:TIGR02168 798 LKALREALDELRAELTLL---------------------NEEAANLRERLESLERRIAATERR------------LEDLE 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 206 GEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIE-----LSLLQLREQQATDQRSNIRDNV-----EMIKLHKQL 275
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERAsleeaLALLRSELEELSEELRELESKRselrrELEELREKL 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 276 VEKSNALSAMEGKFIQLQEKQRTL-RISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMK----FSERRIEELQDRIND 350
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGpvnlAAIEEYEELKERYDF 1004
|
330
....*....|....*
gi 118442834 351 LEKERELLKENYDKL 365
Cdd:TIGR02168 1005 LTAQKEDLTEAKETL 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
225-586 |
1.43e-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: 53.14 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 225 LEHLAEILKTQLRRKEneielSLLQLREQQA-----TDQRSNIRDNVEmiKLHKQlVEKSNalsamegKFIQLQEKQRTL 299
Cdd:TIGR02168 161 FEEAAGISKYKERRKE-----TERKLERTREnldrlEDILNELERQLK--SLERQ-AEKAE-------RYKELKAELREL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 300 RIS-----HDALMANGDELNMQLKEQRLKCCSLEKQLHSmkfSERRIEELQDRINDLEKERELLKENYDKLydsafsaah 374
Cdd:TIGR02168 226 ELAllvlrLEELREELEELQEELKEAEEELEELTAELQE---LEEKLEELRLEVSELEEEIEELQKELYAL--------- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 375 eeqwklkeqqlkvqiaqleTALKSDLTDKTEILDrlktERDQNekLVQENRELQLQYLEQKQQLDELKKRI-----KLYN 449
Cdd:TIGR02168 294 -------------------ANEISRLEQQKQILR----ERLAN--LERQLEELEAQLEELESKLDELAEELaeleeKLEE 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 450 QENDINA--DELSEALLLIKAQK----------EQKNGDLSFLVKVDSEINKDLER---SMRELQATHAETVQELEKTRN 514
Cdd:TIGR02168 349 LKEELESleAELEELEAELEELEsrleeleeqlETLRSKVAQLELQIASLNNEIERleaRLERLEDRRERLQQEIEELLK 428
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118442834 515 MLIMQHKinKDYQMEVEAVTRKMENLQQDYELKVEQyvhlLDIRAARIHKLEAQLKDIAYGTKQYKFKPEIM 586
Cdd:TIGR02168 429 KLEEAEL--KELQAELEELEEELEELQEELERLEEA----LEELREELEEAEQALDAAERELAQLQARLDSL 494
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
63-474 |
1.59e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 63 LLKQHARKQEDKI--KRMATKLIRLVNDKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELEKQNETLKNRLISAKQQL 140
Cdd:COG4717 46 MLLERLEKEADELfkPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 141 QTQGYRQTP------YNNVQSRINTGRRKANENAGLQEcprkGIKFQDADVAETpHPMFTKYGNSLLEEARGEIRNLENV 214
Cdd:COG4717 126 QLLPLYQELealeaeLAELPERLEELEERLEELRELEE----ELEELEAELAEL-QEELEELLEQLSLATEEELQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 215 IQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQrsnIRDNVEMIKLHKQLVEKSNALSAMEGKFIQLQE 294
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER---LKEARLLLLIAAALLALLGLGGSLLSLILTIAG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 295 KQRT-----------LRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSE--------------RRIEELQDRIN 349
Cdd:COG4717 278 VLFLvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPdlspeellelldriEELQELLREAE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 350 DLEKEREL--LKENYDKLYDSAFSAAHEE-----QWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTE--RDQNEKL 420
Cdd:COG4717 358 ELEEELQLeeLEQEIAALLAEAGVEDEEElraalEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEEL 437
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 118442834 421 VQENRELQLQYLEQKQQLDELKKRIKlyNQENDinaDELSEALLLIKAQKEQKN 474
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELE--QLEED---GELAELLQELEELKAELR 486
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
339-514 |
1.81e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 339 RRIEELQDRINDLEKERELLkenydklyDSAFSAAHEEQWKLKEQQLKVQIAQLETA---LKSDLTDKTEILDRLKTERD 415
Cdd:COG4913 262 ERYAAARERLAELEYLRAAL--------RLWFAQRRLELLEAELEELRAELARLEAElerLEARLDALREELDELEAQIR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 416 QN-----EKLVQENRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEINKD 490
Cdd:COG4913 334 GNggdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAA 413
|
170 180
....*....|....*....|....
gi 118442834 491 LERSMRELQATHAEtVQELEKTRN 514
Cdd:COG4913 414 LRDLRRELRELEAE-IASLERRKS 436
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
107-572 |
1.93e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 107 EMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTqgyrqtpynnvqsrINTGRRKANENAGLQECPRKGIKFQDADVA 186
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEE--------------LEEERDDLLAEAGLDDADAEAVEARREELE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 187 ETphpmftkygnslLEEARGEIRNLENVIQSQRGQIE-------ELEHLAEILKTQLRRKENEIELSLLQLREQQA--TD 257
Cdd:PRK02224 321 DR------------DEELRDRLEECRVAAQAHNEEAEslredadDLEERAEELREEAAELESELEEAREAVEDRREeiEE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 258 QRSNIRDN--------VEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRIS---HDALMANG---------------- 310
Cdd:PRK02224 389 LEEEIEELrerfgdapVDLGNAEDFLEELREERDELREREAELEATLRTARERveeAEALLEAGkcpecgqpvegsphve 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 311 ---------DELNMQLKEQRLKCCSLEK---QLHSMKFSERRIEELQDRINDLEK----ERELLKENYDKL--------- 365
Cdd:PRK02224 469 tieedrervEELEAELEDLEEEVEEVEErleRAEDLVEAEDRIERLEERREDLEEliaeRRETIEEKRERAeelreraae 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 366 YDSAFSAAHEEQWKLKEQQLKVQ--IAQLETALkSDLTDKTEILDRLKT---ERDQNEKLVQENRE----LQLQYLEQKQ 436
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEAReeVAELNSKL-AELKERIESLERIRTllaAIADAEDEIERLREkreaLAELNDERRE 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 437 QLDELKKRIKlyNQENDINADELSEAllliKAQKEQKNgdlSFLVKVDSEInKDLERSMRELQATHAETVQELEKTRNmL 516
Cdd:PRK02224 628 RLAEKRERKR--ELEAEFDEARIEEA----REDKERAE---EYLEQVEEKL-DELREERDDLQAEIGAVENELEELEE-L 696
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 118442834 517 IMQHKINKDYQMEVEAVTRKMENLQQDY-ELKVEqyvhlldIRAARIHKLEAQLKDI 572
Cdd:PRK02224 697 RERREALENRVEALEALYDEAEELESMYgDLRAE-------LRQRNVETLERMLNET 746
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
223-588 |
2.90e-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: 51.65 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 223 EELEHLAEILKTQLRRKENEIELSLLQLREQQAT---------DQRSNIRDNVEMIKLH----KQLVEKSNAL-SAMEGK 288
Cdd:pfam05483 222 EKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKmkdltflleESRDKANQLEEKTKLQdenlKELIEKKDHLtKELEDI 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 289 FIQLQEKQRTLR-ISHDALMANGDELNM-QLKEQRLKCCSLEKQLHSMKfserrIEELQDRINDLEkerELLKENYDKLY 366
Cdd:pfam05483 302 KMSLQRSMSTQKaLEEDLQIATKTICQLtEEKEAQMEELNKAKAAHSFV-----VTEFEATTCSLE---ELLRTEQQRLE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 367 DsafsaaHEEQWKLKEQQLKVQIAQLETALKsdLTDKTEI-LDRLKTERDQNEKLVQENREL-----QLQYLEQKQQLDE 440
Cdd:pfam05483 374 K------NEDQLKIITMELQKKSSELEEMTK--FKNNKEVeLEELKKILAEDEKLLDEKKQFekiaeELKGKEQELIFLL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 441 LKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEINKD-LERSMRELQATHAETVQELEKTRNMLIMQ 519
Cdd:pfam05483 446 QAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDkLLLENKELTQEASDMTLELKKHQEDIINC 525
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 118442834 520 HKINKDYQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDIAYGTKQYKFKPEIMPD 588
Cdd:pfam05483 526 KKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILEN 594
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
221-499 |
4.40e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 221 QIEELEHLAEILKTQLRRKENEIElsllqlREQQATDQRSNIRDNVEMIKlhKQLVEKSNALSAMEGKFIQLQEKQRTLR 300
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIE------RLEKFIKRTENIEELIKEKE--KELEEVLREINEISSELPELREELEKLE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 301 ISHDALmangDELNMQLKEQRLKCCSLEKqlhSMKFSERRIEELQDRINDLEKERELLKENYDKL-----YDSAFSAAHE 375
Cdd:PRK03918 228 KEVKEL----EELKEEIEELEKELESLEG---SKRKLEEKIRELEERIEELKKEIEELEEKVKELkelkeKAEEYIKLSE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 376 --EQWKLKEQQLKVQIAQLETALK------SDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQ---QLDELKKR 444
Cdd:PRK03918 301 fyEEYLDELREIEKRLSRLEEEINgieeriKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAkkeELERLKKR 380
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 118442834 445 IKLYNQEndinadELSEALLLIKAQKEQKNGDLSFLVKVDSEIN---KDLERSMRELQ 499
Cdd:PRK03918 381 LTGLTPE------KLEKELEELEKAKEEIEEEISKITARIGELKkeiKELKKAIEELK 432
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
37-572 |
6.23e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 6.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 37 KSRQAVSRVSREELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERvgggpkrlgRDVEMEEMIEQLQ 116
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE---------RRRELEERLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 117 EKVHELEKQNETLKNRLISAKQQLQTQGYRQTpyNNVQSRINTGRRKANENAGLQECPRKGIKFQDADVAETphpmftky 196
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELE--EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL-------- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 197 gnSLLEEARGEIRNLENVIQSQRGQIEELEHLAEilktQLRRKENEIELSLLQLREQQATDQRSNIRDNVEMIKLHKQLV 276
Cdd:COG1196 393 --RAAAELAAQLEELEEAEEALLERLERLEEELE----ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 277 EKSNALSAMEGKFIQLQEKQRTLRISHDALMA--------NGDELNMQLKEQRLKCCSLEKQLHSMKFSERRIEE----- 343
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLLLEaeadyegfLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEaalaa 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 344 -LQDRIN----DLEKERELLKEN---------YDKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDR 409
Cdd:COG1196 547 aLQNIVVeddeVAAAAIEYLKAAkagratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 410 LKTERDQNEKLVQenRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQkngdlsflvkVDSEINK 489
Cdd:COG1196 627 LVAARLEAALRRA--VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAER----------LAEEELE 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 490 DLERSMRELQATHAETVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRA--ARIHKLEA 567
Cdd:COG1196 695 LEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEleRELERLER 774
|
....*
gi 118442834 568 QLKDI 572
Cdd:COG1196 775 EIEAL 779
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
201-443 |
6.95e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 6.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILK------TQLRRKENEIELSLLQLREqqatdQRSNIRDNVEMIKLH-K 273
Cdd:PRK03918 202 LEEVLREINEISSELPELREELEKLEKEVKELEelkeeiEELEKELESLEGSKRKLEE-----KIRELEERIEELKKEiE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 274 QLVEKSNALSAMEGKfiqlQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSERRIEELQDRINDLEK 353
Cdd:PRK03918 277 ELEEKVKELKELKEK----AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 354 ERELLKEnYDKLYDSAfSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKterdqneKLVQENRELQLQYLE 433
Cdd:PRK03918 353 RLEELEE-RHELYEEA-KAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEIS-------KITARIGELKKEIKE 423
|
250
....*....|
gi 118442834 434 QKQQLDELKK 443
Cdd:PRK03918 424 LKKAIEELKK 433
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
39-375 |
9.18e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 9.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 39 RQAVSRVSRE--ELEDRFLRLHDE----NILLKQHARKQ---EDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDVEME 109
Cdd:TIGR02169 708 SQELSDASRKigEIEKEIEQLEQEeeklKERLEELEEDLsslEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 110 EMIEQLQEKVHELEKQNETLKN---RLISAKQQLQTQGYR----QTPYNNVQSRINTGRRKANENaglqecpRKGIKFQD 182
Cdd:TIGR02169 788 LSHSRIPEIQAELSKLEEEVSRieaRLREIEQKLNRLTLEkeylEKEIQELQEQRIDLKEQIKSI-------EKEIENLN 860
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 183 ADVAETphpmftkygNSLLEEARGEIRNLENVIQSQRGQIEELEhlAEIlkTQLRRKENEIELSLLQLREQQA--TDQRS 260
Cdd:TIGR02169 861 GKKEEL---------EEELEELEAALRDLESRLGDLKKERDELE--AQL--RELERKIEELEAQIEKKRKRLSelKAKLE 927
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 261 NIRDNVEMI-KLHKQLVEKSNALSAMEGKFIQLQEKQRtlrishdALMANGDeLNMQLKEQrlkccslekqlhsMKFSER 339
Cdd:TIGR02169 928 ALEEELSEIeDPKGEDEEIPEEELSLEDVQAELQRVEE-------EIRALEP-VNMLAIQE-------------YEEVLK 986
|
330 340 350
....*....|....*....|....*....|....*....
gi 118442834 340 RIEELQDRINDLEKERELLK---ENYDKLYDSAFSAAHE 375
Cdd:TIGR02169 987 RLDELKEKRAKLEEERKAILeriEEYEKKKREVFMEAFE 1025
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
201-365 |
1.61e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 201 LEEARGEIR---------NLENVIQSQRGQIEELEhlAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNVEMIKL 271
Cdd:COG3206 191 LEEAEAALEefrqknglvDLSEEAKLLLQQLSELE--SQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQL 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 272 HKQLVEKSNALSAMEGKF-------IQLQEKQRTLRISHDALMANG-DELNMQLKEQRLKCCSLEKQLHSMKFSERRIEE 343
Cdd:COG3206 269 RAQLAELEAELAELSARYtpnhpdvIALRAQIAALRAQLQQEAQRIlASLEAELEALQAREASLQAQLAQLEARLAELPE 348
|
170 180
....*....|....*....|..
gi 118442834 344 LQDRINDLEKERELLKENYDKL 365
Cdd:COG3206 349 LEAELRRLEREVEVARELYESL 370
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
208-460 |
1.88e-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: 49.05 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 208 IRNLENVIQSQRGQIEELEHLAEILKTQ--------------LRRKENEIElsllQLREQQATDQRSNIRDNVEMIKLHK 273
Cdd:pfam10174 403 IENLQEQLRDKDKQLAGLKERVKSLQTDssntdtalttleeaLSEKERIIE----RLKEQREREDRERLEELESLKKENK 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 274 QLVEKSNAL----SAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQL---HSMKFSERRIEELQD 346
Cdd:pfam10174 479 DLKEKVSALqpelTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLkkaHNAEEAVRTNPEIND 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 347 RINDLEKERELLKE-------NYDKLYDSAFSAAHEEQWKLKeqqlkvQIAQLETALKSDLTDKTEILDRLKT----ERD 415
Cdd:pfam10174 559 RIRLLEQEVARYKEesgkaqaEVERLLGILREVENEKNDKDK------KIAELESLTLRQMKEQNKKVANIKHgqqeMKK 632
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 118442834 416 QNEKLVQENRELQLQYLE--QKQQLDELKKRIKLYNQENDINADELS 460
Cdd:pfam10174 633 KGAQLLEEARRREDNLADnsQQLQLEELMGALEKTRQELDATKARLS 679
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
201-477 |
1.96e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQAtdqrsnirdnvEMIKLHKQLVEKSN 280
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQA-----------ELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 281 ALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSERRIEELQDRINDLEKERELlke 360
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL--- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 361 nyDKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDE 440
Cdd:COG4372 186 --DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
|
250 260 270
....*....|....*....|....*....|....*..
gi 118442834 441 LKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDL 477
Cdd:COG4372 264 ELAILVEKDTEEEELEIAALELEALEEAALELKLLAL 300
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
191-533 |
2.01e-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: 49.20 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 191 PMFTKYGNSLLEEARGEIRNLENVIQSQR-----GQIEELEHLAEILKTQLRRK--ENEIELSLLQLREQQATDQRSNIR 263
Cdd:TIGR00618 601 EKLSEAEDMLACEQHALLRKLQPEQDLQDvrlhlQQCSQELALKLTALHALQLTltQERVREHALSIRVLPKELLASRQL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 264 DNVEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLR--------ISHDA---LMANGDELNMQLKE----QRLKCCSLE 328
Cdd:TIGR00618 681 ALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDrefneienASSSLgsdLAAREDALNQSLKElmhqARTVLKART 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 329 KQlHSMKFSERRIE-----ELQDRINDLEKERELLKENYdklydsafsaaheeqwklkeQQLKVQIAQLETALKSDLTDK 403
Cdd:TIGR00618 761 EA-HFNNNEEVTAAlqtgaELSHLAAEIQFFNRLREEDT--------------------HLLKTLEAEIGQEIPSDEDIL 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 404 TEILDRLKTERDQNEKLVQEN-------RELQLQYLEQKQQLDELKKRIKLYNQendinadeLSEALLLIKAQKEQKNGD 476
Cdd:TIGR00618 820 NLQCETLVQEEEQFLSRLEEKsatlgeiTHQLLKYEECSKQLAQLTQEQAKIIQ--------LSDKLNGINQIKIQFDGD 891
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 118442834 477 LsfLVKVDSEINKDLERSMRELQATHAETVQELektrnmlimQHKINKDYQMEVEAV 533
Cdd:TIGR00618 892 A--LIKFLHEITLYANVRLANQSEGRFHGRYAD---------SHVNARKYQGLALLV 937
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
109-464 |
2.44e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 109 EEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQGYRQTPYNNVQSRINTGRRKANENAGLQECPRKGIKFQDADVAet 188
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEE-- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 189 phpmftkygnslLEEARGEIRNLENVIQSQRGQ--IEELEHLAEILKT----QLRRKENEIELSLLQLREQQATDQRSNI 262
Cdd:COG4717 165 ------------LEELEAELAELQEELEELLEQlsLATEEELQDLAEEleelQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 263 RDNVEMIKLHKQLVEKSN------ALSAMEGKFIQLQEKQRT------------------LRISHDALMANGDELNMQLK 318
Cdd:COG4717 233 ENELEAAALEERLKEARLllliaaALLALLGLGGSLLSLILTiagvlflvlgllallfllLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 319 EQRLKCCSLEKQLHSMKFSE--------------RRIEELQDRINDLEKEREL--LKENYDKLYDSAFSAAHEE-----Q 377
Cdd:COG4717 313 LEELEEEELEELLAALGLPPdlspeellelldriEELQELLREAEELEEELQLeeLEQEIAALLAEAGVEDEEElraalE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 378 WKLKEQQLKVQIAQLETALKS---------DLTDKTEI---LDRLKTERDQNEKLVQENRE------LQLQYLEQKQQLD 439
Cdd:COG4717 393 QAEEYQELKEELEELEEQLEEllgeleellEALDEEELeeeLEELEEELEELEEELEELREelaeleAELEQLEEDGELA 472
|
410 420 430
....*....|....*....|....*....|
gi 118442834 440 ELKKRI-----KLYNQENDINADELSEALL 464
Cdd:COG4717 473 ELLQELeelkaELRELAEEWAALKLALELL 502
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
316-517 |
2.77e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 316 QLKEQRLKCCSLEKQLHSMKFSERRIEELQDRINDLEKERELLKENYDKLydsafsaaheeqwkLKEQQLKVQIAQLEtA 395
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL--------------EKLLQLLPLYQELE-A 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 396 LKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQEndiNADELSEALLLIKAQKEQKNG 475
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE---ELQDLAEELEELQQRLAELEE 213
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 118442834 476 DLSFLVKVDSEINKDLERsmRELQATHAETVQELEKTRNMLI 517
Cdd:COG4717 214 ELEEAQEELEELEEELEQ--LENELEAAALEERLKEARLLLL 253
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
244-562 |
2.84e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 244 ELSLLQLREQQATDQ------RSNIRDNVEMIKLHKQLVEKSNALSAMEGKF---IQLQEKQRT--LRISH--------- 303
Cdd:COG3206 72 GLSSLSASDSPLETQieilksRPVLERVVDKLNLDEDPLGEEASREAAIERLrknLTVEPVKGSnvIEISYtspdpelaa 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 304 ---DALMANGDELNMQLKEQRLKccslekqlHSMKFSERRIEELQDRINDLEKERELLKENYDkLYDSafsaahEEQWKL 380
Cdd:COG3206 152 avaNALAEAYLEQNLELRREEAR--------KALEFLEEQLPELRKELEEAEAALEEFRQKNG-LVDL------SEEAKL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 381 KEQQLkVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQEN------RELQLQYLEQKQQLDELKKRiklYNQENDI 454
Cdd:COG3206 217 LLQQL-SELESQLAEARAELAEAEARLAALRAQLGSGPDALPELlqspviQQLRAQLAELEAELAELSAR---YTPNHPD 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 455 nadelsealllIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQATHAETVQELEKTRNMLimqhkinkdyqMEVEAVT 534
Cdd:COG3206 293 -----------VIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARL-----------AELPELE 350
|
330 340
....*....|....*....|....*....
gi 118442834 535 RKMENLQQDYELKVEQYVHLLD-IRAARI 562
Cdd:COG3206 351 AELRRLEREVEVARELYESLLQrLEEARL 379
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
221-504 |
2.92e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.60 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 221 QIEELEHLAEILKT---QLRRKENEIELSLLQLREQqatdqrsniRDnvemiKLHKQLVEKSNALSAMEGKFIQLQEKQR 297
Cdd:COG1340 9 SLEELEEKIEELREeieELKEKRDELNEELKELAEK---------RD-----ELNAQVKELREEAQELREKRDELNEKVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 298 TLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSERRIEELQDRIN----DLEKERELLKE--NYDKLYDSAfs 371
Cdd:COG1340 75 ELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQtevlSPEEEKELVEKikELEKELEKA-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 372 aaheeqwkLKEQQLKVQIAQLETALKsdltdktEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQE 451
Cdd:COG1340 153 --------KKALEKNEKLKELRAELK-------ELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKE 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 118442834 452 ND---INADELSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQATHAE 504
Cdd:COG1340 218 IVeaqEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIF 273
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
69-552 |
3.24e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 69 RKQEDKIKRMATKL---IRLVNDKKRYERvgggpkrlGRDVEMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQGY 145
Cdd:PTZ00121 1194 RKAEDARKAEAARKaeeERKAEEARKAED--------AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHF 1265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 146 --RQTPYNNVQSRINTGRRKANENAGLQECpRKGIKFQDADVAETPHPMFTKygnslLEEARGEIRNLENVIQSQRGQIE 223
Cdd:PTZ00121 1266 arRQAAIKAEEARKADELKKAEEKKKADEA-KKAEEKKKADEAKKKAEEAKK-----ADEAKKKAEEAKKKADAAKKKAE 1339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 224 ELEHLAEILKTQLRRKENEIELSllQLREQQATDQRSNIRDNVEMIKLHKQLVEKSNALsamEGKFIQLQEKQRTLRISH 303
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEAA--EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEA---KKKAEEDKKKADELKKAA 1414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 304 DAlMANGDELNMQLKEQRlKCCSLEKQLHSmkfsERRIEELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQWKLKEQ 383
Cdd:PTZ00121 1415 AA-KKKADEAKKKAEEKK-KADEAKKKAEE----AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEA 1488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 384 QLKVQiaqlETALKSDLTDKTEildRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKriklynQENDINADELSEAL 463
Cdd:PTZ00121 1489 KKKAE----EAKKKADEAKKAA---EAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK------AEEKKKADELKKAE 1555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 464 LLIKAQKEQKNgdlsflvkvdSEINKDLERsmRELQATHAETVQELEKTRNMLIMQhKINKDYQMEVEAVTRKMENLQQD 543
Cdd:PTZ00121 1556 ELKKAEEKKKA----------EEAKKAEED--KNMALRKAEEAKKAEEARIEEVMK-LYEEEKKMKAEEAKKAEEAKIKA 1622
|
....*....
gi 118442834 544 YELKVEQYV 552
Cdd:PTZ00121 1623 EELKKAEEE 1631
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
47-492 |
3.29e-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: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 47 REELEDRFLRLhDENILLKQHARKQEDKIKRMATKLIR---LVNDKKRYErvggGPKRLGRDVEMEEMIEQLQEKVHELE 123
Cdd:TIGR02169 176 LEELEEVEENI-ERLDLIIDEKRQQLERLRREREKAERyqaLLKEKREYE----GYELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 124 KQNETLKnrlisakQQLQTQGYRQTPYNNVQSRINTGRRKANENAGLQecprkgIKFQdadvaetphpmftkygnslLEE 203
Cdd:TIGR02169 251 EELEKLT-------EEISELEKRLEEIEQLLEELNKKIKDLGEEEQLR------VKEK-------------------IGE 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 204 ARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIElsllQLREQQATDQRSNIRDNVEMIKLHKQlveksnals 283
Cdd:TIGR02169 299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE----ELEREIEEERKRRDKLTEEYAELKEE--------- 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 284 aMEGKFIQLQEKQRTLRISHDALMAngdelnmqlkeqrlkccslekqlhsmkfSERRIEELQDRINDLEKERELLKENYD 363
Cdd:TIGR02169 366 -LEDLRAELEEVDKEFAETRDELKD----------------------------YREKLEKLKREINELKRELDRLQEELQ 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 364 KLydSAFSAAHEEQWKLKEQQLKVQIAQLETA---LKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDE 440
Cdd:TIGR02169 417 RL--SEELADLNAAIAGIEAKINELEEEKEDKaleIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 118442834 441 LKKRIKLYNQENDINADelseALLLIKAQKEQKNGDLSFLVKVDSEINKDLE 492
Cdd:TIGR02169 495 AEAQARASEERVRGGRA----VEEVLKASIQGVHGTVAQLGSVGERYATAIE 542
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
311-512 |
3.56e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 311 DELNMQLKEQRLKCCSLEKQLHSMkfsERRIEELQDRINDLEKERELLKENYDKLYDSAfsAAHEEQWKLKEQQLKVQIA 390
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDAL---QAELEELNEEYNELQAELEALQAEIDKLQAEI--AEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 391 Q----------LETALKS-DLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLynqendiNADEL 459
Cdd:COG3883 94 AlyrsggsvsyLDVLLGSeSFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEA-------LKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 118442834 460 SEALLLIKAQKEQKNGDLSFLvkvdSEINKDLERSMRELQATHAETVQELEKT 512
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQL----SAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
209-446 |
3.58e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 209 RNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIE-------LSLLQLREQQATDQRSNIRDnvemiklhkQLVEKSNA 281
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEefrqkngLVDLSEEAKLLLQQLSELES---------QLAEARAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 282 LSAMEGKFIQLQEKQRTLRISHDALMAngDELNMQLKEQRLKccsLEKQLHSM--KFSER--RIEELQDRINDLekeREL 357
Cdd:COG3206 235 LAEAEARLAALRAQLGSGPDALPELLQ--SPVIQQLRAQLAE---LEAELAELsaRYTPNhpDVIALRAQIAAL---RAQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 358 LKENYDKLYDSAFSAAheeqwklkeQQLKVQIAQLETALksdltdkteilDRLKTERDQNEKLVQENRELQLQYLEQKQQ 437
Cdd:COG3206 307 LQQEAQRILASLEAEL---------EALQAREASLQAQL-----------AQLEARLAELPELEAELRRLEREVEVAREL 366
|
....*....
gi 118442834 438 LDELKKRIK 446
Cdd:COG3206 367 YESLLQRLE 375
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
372-513 |
4.03e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 372 AAHEEQWKLKE-QQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQ 450
Cdd:COG1579 1 AMPEDLRALLDlQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 451 -------ENDINA------------DELSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQATHAETVQELEK 511
Cdd:COG1579 81 qlgnvrnNKEYEAlqkeieslkrriSDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
..
gi 118442834 512 TR 513
Cdd:COG1579 161 LE 162
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
208-561 |
5.39e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 5.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 208 IRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIElsllQLREQQATDQRSNIRDNVEMIKLHKQLVEKSNALSAMEG 287
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELE----QLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 288 KFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLhsmKFSERRIEELQDRINDLEKERELLKENYDKLYD 367
Cdd:COG4372 102 ELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI---AEREEELKELEEQLESLQEELAALEQELQALSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 368 safSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKL 447
Cdd:COG4372 179 ---AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 448 YNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQATHAETVQELEKTRNMLIMQHKINKDYQ 527
Cdd:COG4372 256 ILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
|
330 340 350
....*....|....*....|....*....|....
gi 118442834 528 MEVEAVTRKMENLQQDYELKVEQYVHLLDIRAAR 561
Cdd:COG4372 336 LAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
388-569 |
5.69e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 388 QIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEAlllik 467
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 468 AQKEQKNGD----LSFLVKVDSeINKDLERS--MRELQATHAETVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQ 541
Cdd:COG3883 92 ARALYRSGGsvsyLDVLLGSES-FSDFLDRLsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180
....*....|....*....|....*...
gi 118442834 542 QDYELKVEQYVHLLDIRAARIHKLEAQL 569
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQL 198
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
202-462 |
6.17e-05 |
|
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: 47.20 E-value: 6.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 202 EEARGEIRNLENVIQSQRGQIEELEhlaeilkTQLRRKENEIELSLLQLREQQATDQRSNIR---DNVEMIKLHKQLVEK 278
Cdd:pfam07888 125 AAHEARIRELEEDIKTLTQRVLERE-------TELERMKERAKKAGAQRKEEEAERKQLQAKlqqTEEELRSLSKEFQEL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 279 SNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRlkccSLEKQLHSmkfSERRIEELQDRINDLEKERell 358
Cdd:pfam07888 198 RNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELR----SLQERLNA---SERKVEGLGEELSSMAAQR--- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 359 kenydklyDSAFSAAHeeQWKLKEQQLKVQIAQLETALKSDLT----DKTEILDRLKTERDQNEKLvqeNRELQ-LQYLE 433
Cdd:pfam07888 268 --------DRTQAELH--QARLQAAQLTLQLADASLALREGRArwaqERETLQQSAEADKDRIEKL---SAELQrLEERL 334
|
250 260
....*....|....*....|....*....
gi 118442834 434 QKQQLDELKKRIKLyNQENDINADELSEA 462
Cdd:pfam07888 335 QEERMEREKLEVEL-GREKDCNRVQLSES 362
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
43-442 |
7.03e-05 |
|
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: 47.53 E-value: 7.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 43 SRVSREELEdRFLRLHD-----ENIllKQHARKQEDKIKRMATKLIRLVNDKKRYervgggpkrlgrdVEMEEMIEQLQE 117
Cdd:pfam12128 216 SRLNRQQVE-HWIRDIQaiagiMKI--RPEFTKLQQEFNTLESAELRLSHLHFGY-------------KSDETLIASRQE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 118 KVHELEKQnetLKNRLISAKQQLQtqgyrqtpynnvQSRINTGRRKANENAGLQECPrkgikfQDADVAETPHPMFTKYG 197
Cdd:pfam12128 280 ERQETSAE---LNQLLRTLDDQWK------------EKRDELNGELSAADAAVAKDR------SELEALEDQHGAFLDAD 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 198 nslLEEARGEIRNLENViqsqRGQIEELEHLAEILKTQLRRKENEIElSLLQLREQQATDQRSNIRDNVEMIK--LHKQL 275
Cdd:pfam12128 339 ---IETAAADQEQLPSW----QSELENLEERLKALTGKHQDVTAKYN-RRRSKIKEQNNRDIAGIKDKLAKIReaRDRQL 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 276 VEKSNALSAMEGKfiqlqekqrtLRISHDALMANGDELNMQLKEqrlkccslekqlhsmkfserRIEELQDRINDLEKER 355
Cdd:pfam12128 411 AVAEDDLQALESE----------LREQLEAGKLEFNEEEYRLKS--------------------RLGELKLRLNQATATP 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 356 ELLKENydKLYDSAFSAAHEEQWKLKEQQLkvqiaqletALKSDLTdkteildRLKTERDQ-NEKLVQENRELQlqylEQ 434
Cdd:pfam12128 461 ELLLQL--ENFDERIERAREEQEAANAEVE---------RLQSELR-------QARKRRDQaSEALRQASRRLE----ER 518
|
....*...
gi 118442834 435 KQQLDELK 442
Cdd:pfam12128 519 QSALDELE 526
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
109-321 |
8.60e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 8.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 109 EEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQ----GYRQTPYNNVQSRINTGRRKANENAGLQECPRKGIKFQDAD 184
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALerriAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 185 VAE----------TPHPMFTKYGNSLLEEARGeIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIElSLLQLREQQ 254
Cdd:COG4942 106 LAEllralyrlgrQPPLALLLSPEDFLDAVRR-LQYLKYLAPARREQAEELRADLAELAALRAELEAERA-ELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 118442834 255 ATDQRsnirdnvemiKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQR 321
Cdd:COG4942 184 EEERA----------ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
232-598 |
9.26e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.55 E-value: 9.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 232 LKTQLRRK--ENEIELSLL---------QLRE--QQATDQRSNIRDNVEMIKLHKQLVEKSNALSAMEgkfiqLQEKQRT 298
Cdd:PHA02562 147 LSAPARRKlvEDLLDISVLsemdklnkdKIRElnQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGEN-----IARKQNK 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 299 LrishdalmangDELnmqLKEqrlkccslEKQLHSmkfserRIEELQDRINDLEKERELLKENYDKLYDSAFsaaheeqw 378
Cdd:PHA02562 222 Y-----------DEL---VEE--------AKTIKA------EIEELTDELLNLVMDIEDPSAALNKLNTAAA-------- 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 379 klkeqQLKVQIAQLETALKSdLTDKTEI---LDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNqendin 455
Cdd:PHA02562 266 -----KIKSKIEQFQKVIKM-YEKGGVCptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFN------ 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 456 adELSEALLLIKAQKEQKNGDLSFLVKVdseiNKDLERSMRELQATHAETVQELEKTRNMLImqhKINKDYQmevEAVTR 535
Cdd:PHA02562 334 --EQSKKLLELKNKISTNKQSLITLVDK----AKKVKAAIEELQAEFVDNAEELAKLQDELD---KIVKTKS---ELVKE 401
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118442834 536 KME-----NLQQDYELKveqyvhlldiraARIHKleaqlKDIAYGTKQYKFKPEIMPDDSV----DEFDETI 598
Cdd:PHA02562 402 KYHrgivtDLLKDSGIK------------ASIIK-----KYIPYFNKQINHYLQIMEADYNftldEEFNETI 456
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
264-552 |
1.83e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 264 DNVEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKE---QRLKccSLEKQLHSMKFSERR 340
Cdd:PRK04863 835 PEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADEtlaDRVE--EIREQLDEAEEAKRF 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 341 IEELQDRINDLEKERELLK---ENYDKLYDSAFSAahEEQWKLKEQQLK--VQIAQLETALK-----SDLTDKTEILDRL 410
Cdd:PRK04863 913 VQQHGNALAQLEPIVSVLQsdpEQFEQLKQDYQQA--QQTQRDAKQQAFalTEVVQRRAHFSyedaaEMLAKNSDLNEKL 990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 411 KTERDQNEklvQENRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEAlllikaqkEQKNGDLSflVKVDSEINKD 490
Cdd:PRK04863 991 RQRLEQAE---QERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQEL--------KQELQDLG--VPADSGAEER 1057
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 118442834 491 LERSMRELQA---THAETVQELEKTRNMLimqhkinkdyQMEVEAVTRKMENLQQDYELKVEQYV 552
Cdd:PRK04863 1058 ARARRDELHArlsANRSRRNQLEKQLTFC----------EAEMDNLTKKLRKLERDYHEMREQVV 1112
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
207-323 |
1.83e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 207 EIRNLENVIQSQRGQIEELEHLAEILK--TQLRRKENEIELSLLQLRE--QQATDQRSNIRDNVEMIK-----LHKQLVE 277
Cdd:COG1340 141 KIKELEKELEKAKKALEKNEKLKELRAelKELRKEAEEIHKKIKELAEeaQELHEEMIELYKEADELRkeadeLHKEIVE 220
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 118442834 278 KSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLK 323
Cdd:COG1340 221 AQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
198-367 |
2.56e-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: 44.15 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 198 NSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIElsllQLREQQATDQR--SNIRDNVEMIKLHKQL 275
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE----EVEARIKKYEEqlGNVRNNKEYEALQKEI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 276 VEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEqrlkccsLEKQLhsmkfsERRIEELQDRINDLEKER 355
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEE-------KKAEL------DEELAELEAELEELEAER 165
|
170
....*....|....*.
gi 118442834 356 ELLKENYD----KLYD 367
Cdd:COG1579 166 EELAAKIPpellALYE 181
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
341-454 |
2.82e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.46 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 341 IEELQDRINDLEKERELLKENYDKLydsafSAAHEEQWKLKEQQLKVQIAQLETALKSDltdkTEILDRLKTERDQNEKL 420
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEA-----SFERLAELRDELAELEEELEALKARWEAE----KELIEEIQELKEELEQR 483
|
90 100 110
....*....|....*....|....*....|....
gi 118442834 421 VQENRELQLQYLEQKQQLDELKKRIKLYNQENDI 454
Cdd:COG0542 484 YGKIPELEKELAELEEELAELAPLLREEVTEEDI 517
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
207-410 |
3.85e-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: 43.37 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 207 EIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIElsllqlreqqatDQRSNIRDNVEMIKLHKQLVEKSnalsame 286
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE------------DLEKEIKRLELEIEEVEARIKKY------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 287 gkfiqlQEKQRTLRishdalmaNGDELNmqlkeqrlkccSLEKQLHSMKfseRRIEELQDRINDLEKERELLKENYDKLy 366
Cdd:COG1579 79 ------EEQLGNVR--------NNKEYE-----------ALQKEIESLK---RRISDLEDEILELMERIEELEEELAEL- 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 118442834 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 |
4.02e-04 |
|
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: 45.04 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 312 ELNMQLKEQRLKCCSLEKQLHSMKFSERRIE-----------ELQDRINDLEKERELLKENYD--KLYDSAfSAAHEEQW 378
Cdd:TIGR01612 562 EIKKELEEENEDSIHLEKEIKDLFDKYLEIDdeiiyinklklELKEKIKNISDKNEYIKKAIDlkKIIENN-NAYIDELA 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 379 KLKEQQLKVQIAQLET---ALKSDLTDKTE-ILDRLKTERdqnEKLVQENrelQLQYLEQKQQLDELKKRI-KLYNQEND 453
Cdd:TIGR01612 641 KISPYQVPEHLKNKDKiysTIKSELSKIYEdDIDALYNEL---SSIVKEN---AIDNTEDKAKLDDLKSKIdKEYDKIQN 714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 454 INADELSEALLLIkaqKEQKNGDLSFLVKVD----SEINKDLERSMRELQATHAE---TVQELEKTRNML-IMQHKINK- 524
Cdd:TIGR01612 715 METATVELHLSNI---ENKKNELLDIIVEIKkhihGEINKDLNKILEDFKNKEKElsnKINDYAKEKDELnKYKSKISEi 791
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 118442834 525 --DYQMEVEAVTRKMENLQQDYElKVEQYVHLLDIRAARIHKLEAQLKDiaygtkqykfkpeiMPDDSVDEFDETIHLE 601
Cdd:TIGR01612 792 knHYNDQINIDNIKDEDAKQNYD-KSKEYIKTISIKEDEIFKIINEMKF--------------MKDDFLNKVDKFINFE 855
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
64-511 |
5.20e-04 |
|
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: 44.65 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 64 LKQHARKQEDKIKRMATKLIRLvnDKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQ 143
Cdd:TIGR00606 700 LQSKLRLAPDKLKSTESELKKK--EKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTI 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 144 GYRQTPYNNVQSRINTGRRKANEnagLQECPRKgIKFQDADVAETPHPMFTKYGNSLLEEARGEIRNLENVIQSQRGQIE 223
Cdd:TIGR00606 778 MPEEESAKVCLTDVTIMERFQME---LKDVERK-IAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQ 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 224 ELEHLAEILKTQLRR-KENEIELSLLQLREQQATDQRSNIRDNV-EMIKLHKQLVEKSNALSAMEGKFiqLQEKQRTLRI 301
Cdd:TIGR00606 854 DQQEQIQHLKSKTNElKSEKLQIGTNLQRRQQFEEQLVELSTEVqSLIREIKDAKEQDSPLETFLEKD--QQEKEELISS 931
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 302 SHDALMANGDELNMQLKEqrlkccsLEKQLHSMKFSERRIEELQDRiNDLEKERELLKENYDKLYDSAFSAAHEEQWKLK 381
Cdd:TIGR00606 932 KETSNKKAQDKVNDIKEK-------VKNIHGYMKDIENKIQDGKDD-YLKQKETELNTVNAQLEECEKHQEKINEDMRLM 1003
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 382 EQQLKVQIAQlETALKSDLT--DKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQ--LDELKK-------RIKLYNQ 450
Cdd:TIGR00606 1004 RQDIDTQKIQ-ERWLQDNLTlrKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEenIDLIKRnhvlalgRQKGYEK 1082
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 118442834 451 ENDINADELSEALLlikAQKEQKNGDLSFLVKVDSEINKDLERSMRELQAT----HAETVQELEK 511
Cdd:TIGR00606 1083 EIKHFKKELREPQF---RDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAimkfHSMKMEEINK 1144
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
193-539 |
5.95e-04 |
|
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: 44.27 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 193 FTKYGNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQR--SNIRDNVEMIK 270
Cdd:TIGR00606 696 FISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRlkNDIEEQETLLG 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 271 LHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQlHSMKFSERRIEELQDRIND 350
Cdd:TIGR00606 776 TIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQ-HELDTVVSKIELNRKLIQD 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 351 LEKERELLKENYDKLYDSAFS--------AAHEEQW--KLKE--------QQLKVQIAQLETALKSDLTDKTEILDRLKT 412
Cdd:TIGR00606 855 QQEQIQHLKSKTNELKSEKLQigtnlqrrQQFEEQLveLSTEvqslireiKDAKEQDSPLETFLEKDQQEKEELISSKET 934
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 413 ERDQNEKLVQE-NRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSfLVKVDSEINKDL 491
Cdd:TIGR00606 935 SNKKAQDKVNDiKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMR-LMRQDIDTQKIQ 1013
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 118442834 492 ERSMRE--LQATHAETVQELEKTRNMLIMQhkINKDYQMEVEAVTRKMEN 539
Cdd:TIGR00606 1014 ERWLQDnlTLRKRENELKEVEEELKQHLKE--MGQMQVLQMKQEHQKLEE 1061
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
209-564 |
5.97e-04 |
|
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: 44.40 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 209 RNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQAtdQRSNIRDNVEmiKLHKQLVEKSNALSAMEGK 288
Cdd:pfam01576 211 RKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETA--QKNNALKKIR--ELEAQISELQEDLESERAA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 289 FIQLQEKQRTLrishdalmanGDELNMQLKEqrlkccsLEKQLHSMKFSerriEELQDRindLEKERELLKEnydklyds 368
Cdd:pfam01576 287 RNKAEKQRRDL----------GEELEALKTE-------LEDTLDTTAAQ----QELRSK---REQEVTELKK-------- 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 369 afsaAHEEQWKLKEQQLKvQIAQLETALKSDLTDKTEILDRLKTERDQNEK-LVQENRELQ--LQYLEQKQQLDELKKRi 445
Cdd:pfam01576 335 ----ALEEETRSHEAQLQ-EMRQKHTQALEELTEQLEQAKRNKANLEKAKQaLESENAELQaeLRTLQQAKQDSEHKRK- 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 446 KLYNQENDINA---------DELSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQAThaetvQEL--EKTRN 514
Cdd:pfam01576 409 KLEGQLQELQArlseserqrAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT-----QELlqEETRQ 483
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 118442834 515 MLIMQHKINkdyQMEVEAvTRKMENLQQDYELK--VEQYVHLLDIRAARIHK 564
Cdd:pfam01576 484 KLNLSTRLR---QLEDER-NSLQEQLEEEEEAKrnVERQLSTLQAQLSDMKK 531
|
|
| C2A_Tricalbin-like |
cd04044 |
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ... |
792-916 |
6.45e-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: 41.00 E-value: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 792 LHITIRCCNHLQSRASHLQ-PHPYVVYKFFDFADHD-TAIIPSSNDPQFDDHMYFPVpmNMDldrylkSESLSFYVFDDS 869
Cdd:cd04044 4 LAVTIKSARGLKGSDIIGGtVDPYVTFSISNRRELArTKVKKDTSNPVWNETKYILV--NSL------TEPLNLTVYDFN 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 118442834 870 DTQENIYIGKVNVPLISLAHDRCISGI-FELTDHQKhPAGTIHVILKW 916
Cdd:cd04044 76 DKRKDKLIGTAEFDLSSLLQNPEQENLtKNLLRNGK-PVGELNYDLRF 122
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
112-462 |
9.38e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 9.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 112 IEQLQEKVHELEKQNETLKNRLISAKQQLQTQgyrqtpynnvqsrintgRRKANENAGLQEcprkgIKFQDADVAetphp 191
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDAL-----------------QERREALQRLAE-----YSWDEIDVA----- 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 192 mftkygnslleEARGEIRNLENVIQSQR---GQIEELEHLAEILKTQLRRKENEI-----ELSLLQLREQQATDQRSNIR 263
Cdd:COG4913 665 -----------SAEREIAELEAELERLDassDDLAALEEQLEELEAELEELEEELdelkgEIGRLEKELEQAEEELDELQ 733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 264 DNVEMIKLHKQLVEKSNAlsamEGKFIQLQEKQRTLRIShDALMANGDELNMQLKEQRLKccsLEKQLHsmKFSERRIEE 343
Cdd:COG4913 734 DRLEAAEDLARLELRALL----EERFAAALGDAVERELR-ENLEERIDALRARLNRAEEE---LERAMR--AFNREWPAE 803
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 344 LQDRINDLEKERELLKEnYDKLYDSAFsAAHEEQWK-LKEQQLKVQIAQLETALKSDLTDKTEILDRLkterdqNEKLVQ 422
Cdd:COG4913 804 TADLDADLESLPEYLAL-LDRLEEDGL-PEYEERFKeLLNENSIEFVADLLSKLRRAIREIKERIDPL------NDSLKR 875
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 118442834 423 ----ENRELQLQYLE-QKQQLDELKKRIKLYNQENDINADELSEA 462
Cdd:COG4913 876 ipfgPGRYLRLEARPrPDPEVREFRQELRAVTSGASLFDEELSEA 920
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
198-569 |
1.16e-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: 43.19 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 198 NSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRdNVEMIKLHKQLVE 277
Cdd:pfam05557 89 NKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQL-RQNLEKQQSSLAE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 278 KSNALSAMEGKfIQLQE---------KQRTLRISH-DALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSERRIEELQDR 347
Cdd:pfam05557 168 AEQRIKELEFE-IQSQEqdseivknsKSELARIPElEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREE 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 348 INDLEKERELLKEnydKLydsafsaaheEQWKLKEQQLKVQI-------AQLETALKSDLT---DKTEILDRLKTERDQN 417
Cdd:pfam05557 247 AATLELEKEKLEQ---EL----------QSWVKLAQDTGLNLrspedlsRRIEQLQQREIVlkeENSSLTSSARQLEKAR 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 418 EKLVQENRELQLQYLE-------QKQQLDELKKRIKLYNQE------------NDINADELSEALLLIKAQKEQ------ 472
Cdd:pfam05557 314 RELEQELAQYLKKIEDlnkklkrHKALVRRLQRRVLLLTKErdgyrailesydKELTMSNYSPQLLERIEEAEDmtqkmq 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 473 -KNGDLSFLVKVDSE-------INKDLERSMREL--QATHA------ETVQELEKTRNMLIMQHKINKDYQMEVEAVTRK 536
Cdd:pfam05557 394 aHNEEMEAQLSVAEEelggykqQAQTLERELQALrqQESLAdpsyskEEVDSLRRKLETLELERQRLREQKNELEMELER 473
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 118442834 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 |
1.27e-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: 43.20 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 39 RQAVSRVSREELEDrFLRLHDENIL-LKQHARKQEDKIKRMATKLIRLVNDKKRyeRVGGGPKRLGRDVEMEEMIE-QLQ 116
Cdd:pfam07111 131 RKNLEEGSQRELEE-IQRLHQEQLSsLTQAHEEALSSLTSKAEGLEKSLNSLET--KRAGEAKQLAEAQKEAELLRkQLS 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 117 EKVHELEKQNETLKNRLISAKQQLQTQGYRQTPYNNVQSRINTGRRKANENAGLQ----------------------ECP 174
Cdd:pfam07111 208 KTQEELEAQVTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQatvellqvrvqslthmlalqeeELT 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 175 RKgikFQDADVAEtphPMFTKYGNSLLEEARGEIRNLENVIQSQrgqieELEHLAEIlkTQLRRKENEIELSLLQLREQQ 254
Cdd:pfam07111 288 RK---IQPSDSLE---PEFPKKCRSLLNRWREKVFALMVQLKAQ-----DLEHRDSV--KQLRGQVAELQEQVTSQSQEQ 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 255 ATDQRSnIRDN-----VEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELN---MQLKEQRLKCCS 326
Cdd:pfam07111 355 AILQRA-LQDKaaeveVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLEttmTRVEQAVARIPS 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 327 LEKQL-------HSMK-FSERRIEELQDRIN-------------DLEKERELLKENYDKLYDSAFSAAH---------EE 376
Cdd:pfam07111 434 LSNRLsyavrkvHTIKgLMARKVALAQLRQEscpppppappvdaDLSLELEQLREERNRLDAELQLSAHliqqevgraRE 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 377 QWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQlQYLEQKQQLDELKKRIKLYNQENDINA 456
Cdd:pfam07111 514 QGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLR-QELTQQQEIYGQALQEKVAEVETRLRE 592
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 118442834 457 DELSEALLLIKAQKEQKNGDLSfLVKVDSEINKDLERS--MRELQATH--------AETVQELEKTRNMLI 517
Cdd:pfam07111 593 QLSDTKRRLNEARREQAKAVVS-LRQIQHRATQEKERNqeLRRLQDEArkeegqrlARRVQELERDKNLML 662
|
|
| HpsJ_fam |
NF038305 |
HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the ... |
403-499 |
1.48e-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: 41.80 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 403 KTEILDRLKTERDQNEKLVQeNRELQLQYLEQKQQLDELKKRIKLYNQEndINADELSEALL-LIKAQKEQKNGDLSFLV 481
Cdd:NF038305 106 STQALQQINQQAGQQETQLQ-QQLNQLQAQTSPQQLNQLLKSEQKQGQA--LASGQLPEEQKeQLQQFKSNPQALDKFLA 182
|
90
....*....|....*...
gi 118442834 482 KVDSEINKDLERSMRELQ 499
Cdd:NF038305 183 QQLTQIRTQAEEAEKQAR 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
27-513 |
1.52e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 27 LQETSTTRTMKSRQAVSRVSREELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERvgggpkrlgRDV 106
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE---------EEE 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 107 EMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQgyrQTPYNNVQSRINTGRRKANENAGLQECPRKGIKFQDADVA 186
Cdd:COG1196 460 ALLELLAELLEEAALLEAALAELLEELAEAAARLLLL---LEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 187 ETphpmftkygnsLLEEARGEIRNLENVIQSQRGQieeleHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDnv 266
Cdd:COG1196 537 EA-----------ALEAALAAALQNIVVEDDEVAA-----AAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIG-- 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 267 EMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMA--NGDELNMQLKEQRLkccSLEKQLHSMKFSERRIEEL 344
Cdd:COG1196 599 AAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVtlAGRLREVTLEGEGG---SAGGSLTGGSRRELLAALL 675
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 345 QDRINDLEKERELLKENYDKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQEN 424
Cdd:COG1196 676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 425 RELQLQYLEQKQQLDELKKRIK-LynqeNDIN------ADELSEALLLIKAQKEqkngdlsflvkvdseinkDLERSMRE 497
Cdd:COG1196 756 LPEPPDLEELERELERLEREIEaL----GPVNllaieeYEELEERYDFLSEQRE------------------DLEEARET 813
|
490
....*....|....*.
gi 118442834 498 LQathaETVQELEKTR 513
Cdd:COG1196 814 LE----EAIEEIDRET 825
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
202-534 |
1.81e-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: 42.80 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 202 EEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRK-ENEIELSLLQLREQQATDQRsnIRDN---VEMIKLHkqlve 277
Cdd:pfam17380 306 EEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAmERERELERIRQEERKRELER--IRQEeiaMEISRMR----- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 278 ksnalsamEGKFIQLQEKQRTLRISHDALMANgdELNMQLKEQRLKCCSLEKQLHSMKFSERRIEELQDRINDLEKEREL 357
Cdd:pfam17380 379 --------ELERLQMERQQKNERVRQELEAAR--KVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREM 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 358 lkenydklydsafsaaheEQWKLKEQQLKVQIAQLEtalKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQ 437
Cdd:pfam17380 449 ------------------ERVRLEEQERQQQVERLR---QQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQA 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 438 LDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNgdlsflvKVDSEINKDLERSMRELQATHAEtVQELEKTRNMLi 517
Cdd:pfam17380 508 MIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRK-------QQEMEERRRIQEQMRKATEERSR-LEAMEREREMM- 578
|
330
....*....|....*..
gi 118442834 518 MQHKINKDYQMEVEAVT 534
Cdd:pfam17380 579 RQIVESEKARAEYEATT 595
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
206-437 |
1.86e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 206 GEIRNLENVIQSQRG----QIEELEHLAEILKTQLRRKEN-------------------EIELSLLQLREQQATDQRSNI 262
Cdd:COG5022 817 ACIIKLQKTIKREKKlretEEVEFSLKAEVLIQKFGRSLKakkrfsllkketiylqsaqRVELAERQLQELKIDVKSISS 896
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 263 RDNVEmIKLHKQLVEKSNALSamegKFIQLQEKQRTLRISHDALMANgdelNMQLKEQRLKCCSLEKQLHSMKFSERRIE 342
Cdd:COG5022 897 LKLVN-LELESEIIELKKSLS----SDLIENLEFKTELIARLKKLLN----NIDLEEGPSIEYVKLPELNKLHEVESKLK 967
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 343 ELQDRINDL-----EKERELLK--ENYDKLYDSAFS------AAHEEQWKLKEqqLKVQIAQLETALKSDLTDKTEiLDR 409
Cdd:COG5022 968 ETSEEYEDLlkkstILVREGNKanSELKNFKKELAElskqygALQESTKQLKE--LPVEVAELQSASKIISSESTE-LSI 1044
|
250 260
....*....|....*....|....*...
gi 118442834 410 LKTERDQNEKLVQENRELQLQYLEQKQQ 437
Cdd:COG5022 1045 LKPLQKLKGLLLLENNQLQARYKALKLR 1072
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
208-452 |
2.27e-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: 41.97 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 208 IRNLENVIQSQRGQIEELEHLAEILkTQLRRKENEIELSLLQLreQQATDQRSNIRDNVEMIKLHKQLVEKSNALSAMEG 287
Cdd:pfam15742 92 IRELELEVLKQAQSIKSQNSLQEKL-AQEKSRVADAEEKILEL--QQKLEHAHKVCLTDTCILEKKQLEERIKEASENEA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 288 KF-IQLQEKQRTLRIshdaLMANGDELNMQLKEQRLKCCSLE----KQLHSMKFSERRIEELQDRIND------------ 350
Cdd:pfam15742 169 KLkQQYQEEQQKRKL----LDQNVNELQQQVRSLQDKEAQLEmtnsQQQLRIQQQEAQLKQLENEKRKsdehlksnqels 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 351 -----LEKERELLKENYDKLYDSAfsAAHEEQWKLKEQQLKVQIAQL------ETALKS----DLTDKTEILDRL----- 410
Cdd:pfam15742 245 eklssLQQEKEALQEELQQVLKQL--DVHVRKYNEKHHHHKAKLRRAkdrlvhEVEQRDerikQLENEIGILQQQsekek 322
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 118442834 411 ---KTERDQNEKLVQENRELQLQYLEQ-------KQQLDELKKRIKLYNQEN 452
Cdd:pfam15742 323 afqKQVTAQNEILLLEKRKLLEQLTEQeeliknnKRTISSVQNRVNFLDEEN 374
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
180-573 |
2.36e-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: 42.25 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 180 FQDADVAETPHPMFTKYGNSLLEEARGEIRNLENVI-----------QSQRGQIEELEHLAEILKTQLRRKENEIELSLL 248
Cdd:COG5185 113 EWSADILISLLYLYKSEIVALKDELIKVEKLDEIADieasygevetgIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 249 QLREQQATDQRSNIRDNVEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQlKEQRLKCCSLE 328
Cdd:COG5185 193 SELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVE-QNTDLRLEKLG 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 329 KQLHSMKfserRIEELqdrINDLEKERELLKENYDKLYDSAFSAAHEEQWK--LKEQQLKVQIAQLETALKSDLTDKTEI 406
Cdd:COG5185 272 ENAESSK----RLNEN---ANNLIKQFENTKEKIAEYTKSIDIKKATESLEeqLAAAEAEQELEESKRETETGIQNLTAE 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 407 LDRLKTERDQNEKLVQENRElqlqYLEQKQQLDELKKRIKLYNQENDINADELSEALlliKAQKEQKNgdlsflvkvdsE 486
Cdd:COG5185 345 IEQGQESLTENLEAIKEEIE----NIVGEVELSKSSEELDSFKDTIESTKESLDEIP---QNQRGYAQ-----------E 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 487 INKDLERSMRELQATHAETVQELEK-TRNMLIMQHKINKDYQMEVEAVTRKMENLQQDYElkvEQYVHLLDIRAARIHKL 565
Cdd:COG5185 407 ILATLEDTLKAADRQIEELQRQIEQaTSSNEEVSKLLNELISELNKVMREADEESQSRLE---EAYDEINRSVRSKKEDL 483
|
....*...
gi 118442834 566 EAQLKDIA 573
Cdd:COG5185 484 NEELTQIE 491
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
221-416 |
2.43e-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: 41.06 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 221 QIEELEHLAEILK--TQLRRKENEIELSLLQLREQ--QATDQRSNIRDNVEmiKLHKQLVEKSNALSAMEGKFIQLQEKQ 296
Cdd:COG1579 5 DLRALLDLQELDSelDRLEHRLKELPAELAELEDElaALEARLEAAKTELE--DLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 297 RTLRishdalmaNGDELNmqlkeqrlkccSLEKQLHSMKfseRRIEELQDRINDLEKEREllkenydklydsafsaAHEE 376
Cdd:COG1579 83 GNVR--------NNKEYE-----------ALQKEIESLK---RRISDLEDEILELMERIE----------------ELEE 124
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 118442834 377 QWKLKEQQL---KVQIAQLETALKSDLTDKTEILDRLKTERDQ 416
Cdd:COG1579 125 ELAELEAELaelEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
333-574 |
2.98e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 333 SMKFSERRIEELQDRINDLEKERELLKENYDKLYDSAfsaaheEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKT 412
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEEL------KELAEKRDELNAQVKELREEAQELREKRDELNEKVKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 413 ERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQ---------------------ENDI--NADELSEALLLIKAQ 469
Cdd:COG1340 76 LKEERDELNEKLNELREELDELRKELAELNKAGGSIDKlrkeierlewrqqtevlspeeEKELveKIKELEKELEKAKKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 470 KEQKN------GDLSFLVKVDSEINKDLERSMRELQATHA---ETVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENL 540
Cdd:COG1340 156 LEKNEklkelrAELKELRKEAEEIHKKIKELAEEAQELHEemiELYKEADELRKEADELHKEIVEAQEKADELHEEIIEL 235
|
250 260 270
....*....|....*....|....*....|....*
gi 118442834 541 QQDYELKVEQYVHLLDI-RAARIHKLEAQLKDIAY 574
Cdd:COG1340 236 QKELRELRKELKKLRKKqRALKREKEKEELEEKAE 270
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
49-516 |
3.00e-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: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 49 ELEDRFLRLHDENILLKQHARKQEDKIKRMATKL--------------------IRLVNDK-KRYERVGGGPKRLGRDVE 107
Cdd:pfam01576 135 KLEEDILLLEDQNSKLSKERKLLEERISEFTSNLaeeeekakslsklknkheamISDLEERlKKEEKGRQELEKAKRKLE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 108 MEemIEQLQEKVHELEKQNETLKNRLISAKQQLQTQGYR----QTPYNNVQSRIntgRRKANENAGLQEcprkgikfqDA 183
Cdd:pfam01576 215 GE--STDLQEQIAELQAQIAELRAQLAKKEEELQAALARleeeTAQKNNALKKI---RELEAQISELQE---------DL 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 184 DVAETPHPMFTKYGNSLLEEARGEIRNLENVIQSQRGQIE-------ELEHLAEILKTQLRRKENEIElsllQLReQQAT 256
Cdd:pfam01576 281 ESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQElrskreqEVTELKKALEEETRSHEAQLQ----EMR-QKHT 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 257 DQRSNIRDNVEMIKLHKQLVEKSNAlsAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSlekqlhsmkf 336
Cdd:pfam01576 356 QALEELTEQLEQAKRNKANLEKAKQ--ALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE---------- 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 337 SERRIEELQDRINDLEKERELLKENYDKLyDSAFSAAHEEQWKLKEQQLKVQ-IAQLETALKSDLTDKTEILDRLKTE-R 414
Cdd:pfam01576 424 SERQRAELAEKLSKLQSELESVSSLLNEA-EGKNIKLSKDVSSLESQLQDTQeLLQEETRQKLNLSTRLRQLEDERNSlQ 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 415 DQNEKLVQENRELQLQYLEQKQQLDELKKRIklynqendinadelsealllikaqkEQKNGDLSFLVKVDSEINKDLERS 494
Cdd:pfam01576 503 EQLEEEEEAKRNVERQLSTLQAQLSDMKKKL-------------------------EEDAGTLEALEEGKKRLQRELEAL 557
|
490 500
....*....|....*....|..
gi 118442834 495 MRELQaTHAETVQELEKTRNML 516
Cdd:pfam01576 558 TQQLE-EKAAAYDKLEKTKNRL 578
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
327-455 |
3.00e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 41.76 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 327 LEKQLHSMKFSERRIEELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQwklKEQQLKVQIAQLETALKSD---LTDK 403
Cdd:pfam06160 279 LEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYTLNENELE---RVRGLEKQLEELEKRYDEIverLEEK 355
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 118442834 404 ----TEILDRLKTERDQNEKLvqenRELQLQYLEQKQQL--DELKKRIKLYNQENDIN 455
Cdd:pfam06160 356 evaySELQEELEEILEQLEEI----EEEQEEFKESLQSLrkDELEAREKLDEFKLELR 409
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
107-550 |
3.54e-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: 41.96 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 107 EMEEMIEQLQEKVHELEKQNETLKNR-LISAKQQLQTQGYRQTPYNNVQSRIN--------TGRRKANEnagLQECPRKG 177
Cdd:TIGR00606 252 NRLKEIEHNLSKIMKLDNEIKALKSRkKQMEKDNSELELKMEKVFQGTDEQLNdlyhnhqrTVREKERE---LVDCQREL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 178 IKFQDAdvaetphpmftkygNSLLEEARGEIRNLENVIQSQRGQIEElehlaEILKTQLRRKENEIELSLLQLREQQATD 257
Cdd:TIGR00606 329 EKLNKE--------------RRLLNQEKTELLVEQGRLQLQADRHQE-----HIRARDSLIQSLATRLELDGFERGPFSE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 258 qrsnirdnVEMIKLHKQLVEKSNALSAMEGKFiqLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFS 337
Cdd:TIGR00606 390 --------RQIKNFHTLVIERQEDEAKTAAQL--CADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFV 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 338 ERRIEELQDRIND-LEKERELLKenydklydsafsaaheeqwKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQ 416
Cdd:TIGR00606 460 IKELQQLEGSSDRiLELDQELRK-------------------AERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKL 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 417 NEKLVQENRELQlqylEQKQQLDELKKRIKLYNQENDIN---ADELSEALLLIKAQKEQKNgdlsFLVKVDSEINKDLER 493
Cdd:TIGR00606 521 DQEMEQLNHHTT----TRTQMEMLTKDKMDKDEQIRKIKsrhSDELTSLLGYFPNKKQLED----WLHSKSKEINQTRDR 592
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118442834 494 sMRELQathaETVQELEKtrnmliMQHKINKDYQMEVEAVTRKMENL-----QQDYELKVEQ 550
Cdd:TIGR00606 593 -LAKLN----KELASLEQ------NKNHINNELESKEEQLSSYEDKLfdvcgSQDEESDLER 643
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
59-426 |
3.85e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.63 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 59 DENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKrlGRDVEMEEMIEQLQEKVHELEKQ------------- 125
Cdd:pfam05483 394 EEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELK--GKEQELIFLLQAREKEIHDLEIQltaiktseehylk 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 126 ----------NETLKNRLISA---------KQQLQTQGYRQTPYNNVQSRINTGRrKANENAGLQECPRKGIKFQDADVA 186
Cdd:pfam05483 472 evedlkteleKEKLKNIELTAhcdklllenKELTQEASDMTLELKKHQEDIINCK-KQEERMLKQIENLEEKEMNLRDEL 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 187 ETPHPMFTKYGNSL---LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIElSLLQlrEQQATDQRSNIR 263
Cdd:pfam05483 551 ESVREEFIQKGDEVkckLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIE-ELHQ--ENKALKKKGSAE 627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 264 D---NVEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEqrlkccslekqlhSMKFSERR 340
Cdd:pfam05483 628 NkqlNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADE-------------AVKLQKEI 694
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 341 IEELQDRINDLEKERELLKENYDKLYDSAFSAAHeeQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKL 420
Cdd:pfam05483 695 DKRCQHKIAEMVALMEKHKHQYDKIIEERDSELG--LYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKL 772
|
....*.
gi 118442834 421 VQENRE 426
Cdd:pfam05483 773 KMEAKE 778
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
342-633 |
3.88e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.63 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 342 EELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQWKLKEQQLKVQiaQLETALKSDLTDKTEILDRL---KTERDQNE 418
Cdd:pfam05483 179 EETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQ--HLEEEYKKEINDKEKQVSLLliqITEKENKM 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 419 K----LVQENRElQLQYLEQKQQLDElkKRIKLYNQENDINADELSE-ALLLIKAQKEQK--NGDLSFLVKVDSEINKDL 491
Cdd:pfam05483 257 KdltfLLEESRD-KANQLEEKTKLQD--ENLKELIEKKDHLTKELEDiKMSLQRSMSTQKalEEDLQIATKTICQLTEEK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 492 ERSMREL---QATHAETVQELEKTR---------------------NMLIMQ-----------HKINKDYQMEVEAV--- 533
Cdd:pfam05483 334 EAQMEELnkaKAAHSFVVTEFEATTcsleellrteqqrleknedqlKIITMElqkksseleemTKFKNNKEVELEELkki 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 534 ----------TRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDIAYGTKQYKFKPEIMPDDSVDEFDETIHLERG 603
Cdd:pfam05483 414 laedeklldeKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAH 493
|
330 340 350
....*....|....*....|....*....|..
gi 118442834 604 ENLFEIHINKVT--FSSEVLQASGDKEPVTFC 633
Cdd:pfam05483 494 CDKLLLENKELTqeASDMTLELKKHQEDIINC 525
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
27-571 |
4.04e-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: 41.70 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 27 LQETSTTRTMKSRQAVSRVSR-EELEDrflrlhDENILLKQHARKQEDKI---KRMATKLIRLVNDKKRYERVGG----- 97
Cdd:pfam01576 470 LQDTQELLQEETRQKLNLSTRlRQLED------ERNSLQEQLEEEEEAKRnveRQLSTLQAQLSDMKKKLEEDAGtleal 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 98 --GPKRLGRDVEmeEMIEQLQEKVHELEKQNETlKNRLisaKQQLQTQGYRQTPYNNVQSRINTGRRKANEnaGLQECPR 175
Cdd:pfam01576 544 eeGKKRLQRELE--ALTQQLEEKAAAYDKLEKT-KNRL---QQELDDLLVDLDHQRQLVSNLEKKQKKFDQ--MLAEEKA 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 176 KGIKFQDA-DVAETPHPMFTKYGNSL---LEEARGEIRNLENVIQSQRGQIEEL---------------------EHLAE 230
Cdd:pfam01576 616 ISARYAEErDRAEAEAREKETRALSLaraLEEALEAKEELERTNKQLRAEMEDLvsskddvgknvhelerskralEQQVE 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 231 ILKTQLRRKENEIE------LSL--------------LQLREQQATDQRsnirdnvemiklhKQLVEKSNALSAMegkfI 290
Cdd:pfam01576 696 EMKTQLEELEDELQatedakLRLevnmqalkaqferdLQARDEQGEEKR-------------RQLVKQVRELEAE----L 758
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 291 QLQEKQRTLrishdaLMANGDELNMQLKEqrlkccsLEKQLHSMKFSE----RRIEELQDRINDLEKERELLKENYDKLy 366
Cdd:pfam01576 759 EDERKQRAQ------AVAAKKKLELDLKE-------LEAQIDAANKGReeavKQLKKLQAQMKDLQRELEEARASRDEI- 824
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 367 dsaFSAAHEEQWKLKEQ-----QLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDEL 441
Cdd:pfam01576 825 ---LAQSKESEKKLKNLeaellQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEE 901
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 442 KKRIKLYNqendinaDELSEALLLIKAQKEQKNGDLSFLVKVDSEiNKDLERSMRELQATHAETVQELEKTRNMLI--MQ 519
Cdd:pfam01576 902 QSNTELLN-------DRLRKSTLQVEQLTTELAAERSTSQKSESA-RQQLERQNKELKAKLQEMEGTVKSKFKSSIaaLE 973
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118442834 520 HKINK-DYQMEVEAVTRKMEN--------------LQQDYELKV-EQYVHLLDIRAARIHKLEAQLKD 571
Cdd:pfam01576 974 AKIAQlEEQLEQESRERQAANklvrrtekklkevlLQVEDERRHaDQYKDQAEKGNSRMKQLKRQLEE 1041
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
199-354 |
4.08e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 199 SLLEEARGEIRNLENVIQ---------SQRGQIEELEhLAEILKTQLRRKENEIELSLLQLREQQAtdqrsnirdnvEMI 269
Cdd:PRK04863 949 QTQRDAKQQAFALTEVVQrrahfsyedAAEMLAKNSD-LNEKLRQRLEQAEQERTRAREQLRQAQA-----------QLA 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 270 KLHKQLvekSNALSAMEGKFIQLQEKQR-----TLRISHDA---LMANGDELNMQLKEQRLKCCSLEKQLhsmKFSERRI 341
Cdd:PRK04863 1017 QYNQVL---ASLKSSYDAKRQMLQELKQelqdlGVPADSGAeerARARRDELHARLSANRSRRNQLEKQL---TFCEAEM 1090
|
170
....*....|...
gi 118442834 342 EELQDRINDLEKE 354
Cdd:PRK04863 1091 DNLTKKLRKLERD 1103
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
59-598 |
4.32e-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: 41.58 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 59 DENILLKQHARKQEDKIKRMATKLIRLVND----KKRYERVGGgpkrlgrdvEMEEMIEQLqEKVHELEKQNETLKNrlI 134
Cdd:TIGR01612 1104 EENIKYADEINKIKDDIKNLDQKIDHHIKAleeiKKKSENYID---------EIKAQINDL-EDVADKAISNDDPEE--I 1171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 135 SAKQQ--LQTQGYRQTPYNNVQSRINTGRRKANENAGLQECprKGIKFQdadvaetphpmftkYGNSL----LEEARGEI 208
Cdd:TIGR01612 1172 EKKIEniVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEV--KGINLS--------------YGKNLgklfLEKIDEEK 1235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 209 RNLENVIQSQRGQIEELEHLAEilKTQLRRKENEI------ELSLLQLREQQATDQRSNIRDNVEMIklhKQLVEKSNAL 282
Cdd:TIGR01612 1236 KKSEHMIKAMEAYIEDLDEIKE--KSPEIENEMGIemdikaEMETFNISHDDDKDHHIISKKHDENI---SDIREKSLKI 1310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 283 SAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKE-----QRLKCCSLEKQLHSMKFSERRIEELQDRIND-LEKERE 356
Cdd:TIGR01612 1311 IEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEianiyNILKLNKIKKIIDEVKEYTKEIEENNKNIKDeLDKSEK 1390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 357 LLKENYDKLYDSAFSAAHEEQWKLKEQQLKVQ-IAQLETALKSDLTDKTEILDRLKtERDQNEKLVQENREL---QLQYL 432
Cdd:TIGR01612 1391 LIKKIKDDINLEECKSKIESTLDDKDIDECIKkIKELKNHILSEESNIDTYFKNAD-ENNENVLLLFKNIEMadnKSQHI 1469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 433 EQKQQ----------LDELKKRI---KLYNQENDINADELSEALLLIKAQKEQ------KNGDLSFLVKVDsEINKDLER 493
Cdd:TIGR01612 1470 LKIKKdnatndhdfnINELKEHIdksKGCKDEADKNAKAIEKNKELFEQYKKDvtellnKYSALAIKNKFA-KTKKDSEI 1548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 494 SMRELQATHAETVQELEKTRNMliMQHKINKDYQMEVEAVTRKMEN-----LQQDYELKVEQYVHLLDIRA------ARI 562
Cdd:TIGR01612 1549 IIKEIKDAHKKFILEAEKSEQK--IKEIKKEKFRIEDDAAKNDKSNkaaidIQLSLENFENKFLKISDIKKkindclKET 1626
|
570 580 590
....*....|....*....|....*....|....*.
gi 118442834 563 HKLEAQLKDIAYGTKQYKFKPEIMPDDSVDEFDETI 598
Cdd:TIGR01612 1627 ESIEKKISSFSIDSQDTELKENGDNLNSLQEFLESL 1662
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
244-510 |
5.48e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 244 ELSLLQLREQQATDQRSNIRDNVE-MIKLhKQLVEKSNALSAMEGKFIQLQEKQRTLRIshdalmangDELnmqLKEQRL 322
Cdd:PRK05771 27 ELGVVHIEDLKEELSNERLRKLRSlLTKL-SEALDKLRSYLPKLNPLREEKKKVSVKSL---------EEL---IKDVEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 323 KCCSLEKQLHSMkfsERRIEELQDRINDLEKERELLK--ENYD----KLYDSAFSAA-----HEEQWKLKEQQLKVQIAQ 391
Cdd:PRK05771 94 ELEKIEKEIKEL---EEEISELENEIKELEQEIERLEpwGNFDldlsLLLGFKYVSVfvgtvPEDKLEELKLESDVENVE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 392 LET-----------ALKSDLTDKTEILDRLKTERDQ--NEKLVQEN-RELQLQYLEQKQQLDELKKRIKLYNQENDINAD 457
Cdd:PRK05771 171 YIStdkgyvyvvvvVLKELSDEVEEELKKLGFERLEleEEGTPSELiREIKEELEEIEKERESLLEELKELAKKYLEELL 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 118442834 458 ELSEALLLIKAQKEQKNGDLS----FLVK--VDSEINKDLERSMRELQATHAEtVQELE 510
Cdd:PRK05771 251 ALYEYLEIELERAEALSKFLKtdktFAIEgwVPEDRVKKLKELIDKATGGSAY-VEFVE 308
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
369-612 |
5.55e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 369 AFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLY 448
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 449 NQENDINADELSEA---LLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQATHAEtVQELEKTRNMLIMQHKINKD 525
Cdd:COG4372 107 QEEAEELQEELEELqkeRQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE-LAALEQELQALSEAEAEQAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 526 YQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDIAYGTKQYKFKPEIMPDDSVDEFDETIHLERGEN 605
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
....*..
gi 118442834 606 LFEIHIN 612
Cdd:COG4372 266 AILVEKD 272
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
239-460 |
5.99e-03 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 41.08 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 239 KENEIE-----LSLLQLREQQATDQRSNIRDNVEMIKL-----HKQLVEKSNALSAMEGKFIQLQEkqrtlriSHDALMA 308
Cdd:pfam15818 90 KEKEIEglketLKALQVSKYSLQKKVSEMEQKLQLHLLakedhHKQLNEIEKYYATITGQFGLVKE-------NHGKLEQ 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 309 NGDE---LNMQL----KEQRLKCCSLEKQL---------------HSMK-------FSERRIEELQDRIN-DLEKERELL 358
Cdd:pfam15818 163 NVQEaiqLNKRLsalnKKQESEICSLKKELkkvtsdlikskvtcqYKMGeeninltIKEQKFQELQERLNmELELNKKIN 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 359 KEN---YDKLYDSAFSAAHEeqwklkeQQLKVQIAQLETALKSDLTDKTEilDRLKTERD---QNEKlVQENRE--LQLQ 430
Cdd:pfam15818 243 EEIthiQEEKQDIIISFQHM-------QQLLQQQTQANTEMEAELKALKE--NNQTLERDnelQREK-VKENEEkfLNLQ 312
|
250 260 270
....*....|....*....|....*....|
gi 118442834 431 YlEQKQQLDELKKRIKLYNQENDINADELS 460
Cdd:pfam15818 313 N-EHEKALGTWKKHVEELNGEINEIKNELS 341
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
198-399 |
7.23e-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: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 198 NSLLEEARGEIRNLENVIQSQRGQIEELEhlAEILKTQLRRKENEIELSLLQLREQQATDQRSN-IRDN---------VE 267
Cdd:COG3883 29 QAELEAAQAELDALQAELEELNEEYNELQ--AELEALQAEIDKLQAEIAEAEAEIEERREELGErARALyrsggsvsyLD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 268 MIKLHK---QLVEKSNALSAMEGKFIQLQEKQRTLRishDALMANGDELNMQLKEQRLKCCSLEKQLHSMkfsERRIEEL 344
Cdd:COG3883 107 VLLGSEsfsDFLDRLSALSKIADADADLLEELKADK---AELEAKKAELEAKLAELEALKAELEAAKAEL---EAQQAEQ 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 118442834 345 QDRINDLEKERELLKENYDKLydSAFSAAHEEQWKLKEQQLKVQIAQLETALKSD 399
Cdd:COG3883 181 EALLAQLSAEEAAAEAQLAEL--EAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
209-447 |
8.30e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 39.90 E-value: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 209 RNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNVEMIKLHKQLVEKSNALSAMEGK 288
Cdd:pfam13868 55 RALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 289 FIQLQEKQRTLRIshdalmangdeLNMQLKEQRLKCCSLEKQLHSMKFSERRI------EELQDRINDLEKERELLKENY 362
Cdd:pfam13868 135 FNEEQAEWKELEK-----------EEEREEDERILEYLKEKAEREEEREAEREeieeekEREIARLRAQQEKAQDEKAER 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 363 DKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKT-ERDQNEKLVQENRELQLQYLEQKQQLDEL 441
Cdd:pfam13868 204 DELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAeEAEREEEEFERMLRKQAEDEEIEQEEAEK 283
|
....*.
gi 118442834 442 KKRIKL 447
Cdd:pfam13868 284 RRMKRL 289
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
60-621 |
8.31e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.73 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 60 ENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELEKQNETLKNRLISAKQQ 139
Cdd:pfam02463 187 ELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 140 LQTQGYRQTPYNNVQSRINTGRRKANENAGLQEcprkgIKFQDADVAEtphpmftKYGNSLLEEARGEIRNLENVIQSQR 219
Cdd:pfam02463 267 LAQVLKENKEEEKEKKLQEEELKLLAKEEEELK-----SELLKLERRK-------VDDEEKLKESEKEKKKAEKELKKEK 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 220 GQIEELEHLAEILKTQLRRKENEIElSLLQLREQQATDQRSNIRdnvemiklhKQLVEKSNALSAMEGKFIQLQEKQRTL 299
Cdd:pfam02463 335 EEIEELEKELKELEIKREAEEEEEE-ELEKLQEKLEQLEEELLA---------KKKLESERLSSAAKLKEEELELKSEEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 300 RISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSERRIEELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQWK 379
Cdd:pfam02463 405 KEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 380 LKEQQLKVQIAQLETALKSDLTDKTEILDRL--------------KTERDQNEKLVQENRELQLQYLEQKQQLDELKKRI 445
Cdd:pfam02463 485 QLELLLSRQKLEERSQKESKARSGLKVLLALikdgvggriisahgRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQ 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 446 KLYNQENDINADELSEALLLIKAQKEQKNGD----------LSFLVKVDSEINKDLERSMRELQATHAETVQELEKTRNM 515
Cdd:pfam02463 565 KLVRALTELPLGARKLRLLIPKLKLPLKSIAvleidpilnlAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAK 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834 516 LIMQHKINKDYQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDIAYGTKQYKFKPEIMPDDSVDEFD 595
Cdd:pfam02463 645 ESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLA 724
|
570 580
....*....|....*....|....*.
gi 118442834 596 ETIHLERGENLFEIHINKVTFSSEVL 621
Cdd:pfam02463 725 DRVQEAQDKINEELKLLKQKIDEEEE 750
|
|
| |
