|
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 ... |
601-742 |
1.33e-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: 1.33e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 601 TIHLERGENLFEIHINKVTFSSEVLQASGDKEPVTFCTYAFYDFELQTTPVVRGLHPEYNFTSQYLVHVNDLFLQYIQKN 680
Cdd:pfam11618 1 TVELERGENLFELHIGGVTFSPEALRALGDKEPSTFCTYDFYDFETQTTPVVRGLNPFYDFTSQYKVTVDDLFLQYLQTN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530423734 681 TITLEVHQAYSTEYETIAACQLKFHEILEK-SGRIFCTASLIGTKGDIPNFGTVEYWFRLRVP 742
Cdd:pfam11618 81 SLTLELHQALGVDFKTLAAAQLRLHGLLEDrGGRIHGTVTLTGVEGEIQIIGTLEYWIRLRVP 143
|
|
| RPGR1_C |
pfam18111 |
Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain ... |
1103-1266 |
6.26e-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: 234.23 E-value: 6.26e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 1103 PSEKIRIEIIALSL-NDSQVTMDDTIQRLFVECRFYSLPAE--ETPVSLPKPKSGQWVYYNYSNVIYVDKENNKAKRDIL 1179
Cdd:pfam18111 1 DSDTIRIEIISLQLlNESEVMQDDNIQQLFVEYRFLGRPEEetETPVSLPKPKTGQELYYNFSKVIDVDKEKNSARREIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 1180 KAILQKQEMPNRSLRFTVVSDPPeDEQDLECEDIGVAHVDLADMFQEGRDLIEQNIDVFDARADGEGIGKLRVTVEALHA 1259
Cdd:pfam18111 81 RSMLLPEDPNQGNLKFTVVSEPL-DTEDGECEEIGYAYVDLKQILQSGRDIIEQDLDVKDARDENEQIGKLKVSVEALAA 159
|
....*..
gi 530423734 1260 LQSVYKQ 1266
Cdd:pfam18111 160 LRAIYSE 166
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
201-449 |
8.47e-17 |
|
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: 86.26 E-value: 8.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIElsllQLREQQATDQRSNIRDNVEMIKLHKQLVEKSN 280
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE----QLEERIAQLSKELTELEAEIEELEERLEEAEE 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 281 ALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKE-------QRLKCCSLEKQLHSmkfSERRIEELQDRINDLEK 353
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanLRERLESLERRIAA---TERRLEDLEEQIEELSE 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 354 ERELLKENYDKLydSAFSAAHEEQWKLKEQQLKVQIAQLEtALKSDLTDKTEILDRLKTERGALINQNEKLVQENRELQL 433
Cdd:TIGR02168 853 DIESLAAEIEEL--EELIEELESELEALLNERASLEEALA-LLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929
|
250
....*....|....*.
gi 530423734 434 QYLEQKQQLDELKKRI 449
Cdd:TIGR02168 930 RLEGLEVRIDNLQERL 945
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
201-484 |
5.52e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.90 E-value: 5.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQAtdqrsnirdnvEMIKLHKQLVEKSN 280
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA-----------ELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 281 ALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHsmKFSERRIEELQDRINDLEKERELLKE 360
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA--EAEEALLEAEAELAEAEEELEELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 361 NYDKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERGALINQNEKLVQENRELQlqylEQKQ 440
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE----ALLE 463
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 530423734 441 QLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFL 484
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
198-576 |
1.80e-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: 75.48 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 198 NSLLEEARgEIRNLENviqsqrgQIEELEHLAEILKTQLrrkeneielsllqlreQQATDQRSNIRDNVEmiKLHKQLVE 277
Cdd:TIGR02168 670 SSILERRR-EIEELEE-------KIEELEEKIAELEKAL----------------AELRKELEELEEELE--QLRKELEE 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 278 KSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSmkfSERRIEELQDRINDLEKEREL 357
Cdd:TIGR02168 724 LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE---AEAEIEELEAQIEQLKEELKA 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 358 LKENYDKLydsafSAAHEEQwKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERGALinqnEKLVQENRELQLQYLE 437
Cdd:TIGR02168 801 LREALDEL-----RAELTLL-NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI----ESLAAEIEELEELIEE 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 438 QKQQLDELKKRIklynqendinaDELSEALLLIKAQKEQKNGDLsflvKVDSEINKDLERSMRELQATHAETVQELEKTR 517
Cdd:TIGR02168 871 LESELEALLNER-----------ASLEEALALLRSELEELSEEL----RELESKRSELRRELEELREKLAQLELRLEGLE 935
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 518 NMLI-MQHKINKDYQMEVEAVTRKMENLqQDYELKVEQyvhlldiraaRIHKLEAQLKDI 576
Cdd:TIGR02168 936 VRIDnLQERLSEEYSLTLEEAEALENKI-EDDEEEARR----------RLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
106-496 |
2.15e-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: 75.09 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 106 VEMEEMIEQLQEKVHELEKQNETLKnrlisaKQQLQTQGYR--QTPYNNVQSRINTGRRKANenaglqecpRKGIKFQDA 183
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQLKSLE------RQAEKAERYKelKAELRELELALLVLRLEEL---------REELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 184 DVAETphpmftkygNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKT---QLRRKENEIELSLLQLREQQATDQRS 260
Cdd:TIGR02168 247 ELKEA---------EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKelyALANEISRLEQQKQILRERLANLERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 261 NIRDNVEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSER- 339
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAs 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 340 ---RIEELQDRINDLEKERELLKENydklydsafsaAHEEQWKLKEQQLKVQIAQLETalksdltdKTEILDRLKTERGA 416
Cdd:TIGR02168 398 lnnEIERLEARLERLEDRRERLQQE-----------IEELLKKLEEAELKELQAELEE--------LEEELEELQEELER 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 417 LINQNEKLVQENRELQLQYLEQKQQLDELKKRIK-LYNQENdiNADELSEALLLIKAQKEQKNGD---LSFLVKVDSEIN 492
Cdd:TIGR02168 459 LEEALEELREELEEAEQALDAAERELAQLQARLDsLERLQE--NLEGFSEGVKALLKNQSGLSGIlgvLSELISVDEGYE 536
|
....
gi 530423734 493 KDLE 496
Cdd:TIGR02168 537 AAIE 540
|
|
| C2 |
cd00030 |
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ... |
796-895 |
4.81e-13 |
|
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.
Pssm-ID: 175973 [Multi-domain] Cd Length: 102 Bit Score: 66.32 E-value: 4.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 796 LHITIRCCNHLQSRASHLQPHPYVVYKFFDFADHDTAIIPSSNDPQFDDHMYFPVPMNMdldrylkSESLSFYVFDDSDT 875
Cdd:cd00030 1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQKFKTKVVKNTLNPVWNETFEFPVLDPE-------SDTLTVEVWDKDRF 73
|
90 100
....*....|....*....|
gi 530423734 876 QENIYIGKVNVPLISLAHDR 895
Cdd:cd00030 74 SKDDFLGEVEIPLSELLDSG 93
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
39-576 |
6.29e-11 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 67.07 E-value: 6.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 39 RQAVSRVSRE---ELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLvndkkRYERVGGGPKRLGRDVEMEEMIEQL 115
Cdd:pfam15921 73 KEHIERVLEEyshQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEM-----QMERDAMADIRRRESQSQEDLRNQL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 116 QEKVHELEKQNETLKNRLISAKQQLQTQGYRQTPYNNVQSRINTGRRKANENAGlqecprKGIKFQDAdvaetphpMFTK 195
Cdd:pfam15921 148 QNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASG------KKIYEHDS--------MSTM 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 196 YGNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRK-----------------ENEIELSLLQLREQQATDQ 258
Cdd:pfam15921 214 HFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKielllqqhqdrieqlisEHEVEITGLTEKASSARSQ 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 259 RSNIRDNVEMIKlhkQLVEKSNA-----LSAMEGKFIQLQEKQRTL-RISHDALmangDELNMQL--KEQRLKCCSLEKQ 330
Cdd:pfam15921 294 ANSIQSQLEIIQ---EQARNQNSmymrqLSDLESTVSQLRSELREAkRMYEDKI----EELEKQLvlANSELTEARTERD 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 331 LHSMKfSERRIEELQDRINDL---EKERELLKENYDKLYD----SAFSAAHEEQwKLKEQQLKVQiaQLETALKsdlTDK 403
Cdd:pfam15921 367 QFSQE-SGNLDDQLQKLLADLhkrEKELSLEKEQNKRLWDrdtgNSITIDHLRR-ELDDRNMEVQ--RLEALLK---AMK 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 404 TEILDRLKTERGALINQNEKLvQENRELQLQYLEQKQQL----DELK-KRIKLYNQENDINadELSEALLLIKAQKEQKN 478
Cdd:pfam15921 440 SECQGQMERQMAAIQGKNESL-EKVSSLTAQLESTKEMLrkvvEELTaKKMTLESSERTVS--DLTASLQEKERAIEATN 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 479 GDLSFL-VKVDSEIN-----KDLERSMRELQAT-HAETVQELEKTRNMLIMQHKINKDYQ-----------MEVEAVtrK 540
Cdd:pfam15921 517 AEITKLrSRVDLKLQelqhlKNEGDHLRNVQTEcEALKLQMAEKDKVIEILRQQIENMTQlvgqhgrtagaMQVEKA--Q 594
|
570 580 590
....*....|....*....|....*....|....*.
gi 530423734 541 MENLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDI 576
Cdd:pfam15921 595 LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL 630
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
219-574 |
5.62e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 5.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 219 RGQIEELehlAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNVEmiKLHKQlveKSNALsamegKFIQLQEKQRT 298
Cdd:COG1196 158 RAIIEEA---AGISKYKERKEEAERKLEATEENLERLEDILGELERQLE--PLERQ---AEKAE-----RYRELKEELKE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 299 LRISH-----DALMANGDELNMQLKEQRLKCCSLEKQLHSMkfsERRIEELQDRINDLEKERELLKEnydKLYDSAFSAA 373
Cdd:COG1196 225 LEAELlllklRELEAELEELEAELEELEAELEELEAELAEL---EAELEELRLELEELELELEEAQA---EEYELLAELA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 374 HEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERGALINQNEKLVQENRELQLQYLEQKQQLDELKKRIklyn 453
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL---- 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 454 QENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERsMRELQATHAETVQELEKTRNMLIMQHKINKDYQME 533
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER-LEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 530423734 534 VEAVTRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQLK 574
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
64-546 |
8.79e-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: 63.12 E-value: 8.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 64 LKQHARKQEDKIKRMATKLIRLVND-KKRYERVGGGPKRLGRDvemEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQT 142
Cdd:TIGR04523 24 YKNIANKQDTEEKQLEKKLKTIKNElKNKEKELKNLDKNLNKD---EEKINNSNNKIKILEQQIKDLNDKLKKNKDKINK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 143 QGYRQTPYNN-VQSRINTGRRKANENAGLQECPRKGIKFQDADVAE-TPHPMFTKYGNSLLEEARGEIRNLENVIQSQRG 220
Cdd:TIGR04523 101 LNSDLSKINSeIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEiKKKEKELEKLNNKYNDLKKQKEELENELNLLEK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 221 QIEELEHLAEILKTQLRRKEneIELSLLQLREQQAT----------DQRSNIRDNVEmiKLHKQLVEKSNALSAMEGKFI 290
Cdd:TIGR04523 181 EKLNIQKNIDKIKNKLLKLE--LLLSNLKKKIQKNKslesqiselkKQNNQLKDNIE--KKQQEINEKTTEISNTQTQLN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 291 QLQEKQrtlrishdalmangDELNMQLKEQRLKccsLEKQLHSMKFSERRIEELQDRINDLEKEREllkENYDKLYDSAF 370
Cdd:TIGR04523 257 QLKDEQ--------------NKIKKQLSEKQKE---LEQNNKKIKELEKQLNQLKSEISDLNNQKE---QDWNKELKSEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 371 SAAHEEQWKLKEQ---------QLKVQIAQLET----------ALKSDLTDKTEILDRLKTERGALINQNEKLVQENREL 431
Cdd:TIGR04523 317 KNQEKKLEEIQNQisqnnkiisQLNEQISQLKKeltnsesensEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 432 QLQYLEQKQQLDELKKRIKLYNQENdinaDELSEALLLIKAQKEQKNGDLSFLVKVDSEIN-----------------KD 494
Cdd:TIGR04523 397 ESKIQNQEKLNQQKDEQIKKLQQEK----ELLEKEIERLKETIIKNNSEIKDLTNQDSVKEliiknldntresletqlKV 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 530423734 495 LERSMRELQATHAETVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQ 546
Cdd:TIGR04523 473 LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKE 524
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
368-576 |
9.31e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.09 E-value: 9.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 368 SAFSAAHEEQWKLKEQ--QLKVQIAQLETALKSDLTDKTEILDRLKTERGALINQNEKLvqenRELQLQYLEQKQQLDEL 445
Cdd:COG4942 13 LAAAAQADAAAEAEAEleQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI----RALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 446 KKRIKLYNQENDINADELSEalLLIKAQKEQKNGDLSFLVKVDS--------EINKDLERSMRELQATHAETVQELEKTR 517
Cdd:COG4942 89 EKEIAELRAELEAQKEELAE--LLRALYRLGRQPPLALLLSPEDfldavrrlQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 530423734 518 NMLIMQHKINKDYQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDI 576
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
216-516 |
1.22e-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: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 216 QSQRGQIEELEHLAEILKTQLRRKENEIElsllqlreqQATDQRSNirdnvemikLHKQLVEKSNALSAMEGKFIQLQEK 295
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLD---------ELSQELSD---------ASRKIGEIEKEIEQLEQEEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 296 ----QRTLRISHDALMANGDE---LNMQLKEQRLKCCSLEKQLHSMK--FSERRIEELQDRINDLEKER----------- 355
Cdd:TIGR02169 739 leelEEDLSSLEQEIENVKSElkeLEARIEELEEDLHKLEEALNDLEarLSHSRIPEIQAELSKLEEEVsriearlreie 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 356 -ELLKENYDKLYDSAFSAAHEEQ---WKLKEQQLKVQIAQLET---ALKSDLTDKTEILDRLKTERGALINQNEKLVQEN 428
Cdd:TIGR02169 819 qKLNRLTLEKEYLEKEIQELQEQridLKEQIKSIEKEIENLNGkkeELEEELEELEAALRDLESRLGDLKKERDELEAQL 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 429 RELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSfLVKVDSEINKdLERSMRELQATHAE 508
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQR-VEEEIRALEPVNML 976
|
....*...
gi 530423734 509 TVQELEKT 516
Cdd:TIGR02169 977 AIQEYEEV 984
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
201-448 |
1.34e-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: 61.70 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIelsllQLREQQATDQRSNIRDN-VEMIKLHKQLVEKS 279
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI-----RALEQELAALEAELAELeKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 280 NALSAMegkfiqLQEKQRTLRISHDALMANGDELNMQLKEQRlkccsLEKQLhsMKFSERRIEELQDRINDLEKERELLK 359
Cdd:COG4942 104 EELAEL------LRALYRLGRQPPLALLLSPEDFLDAVRRLQ-----YLKYL--APARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 360 ENYDKLydsafsaaheeqwklkeQQLKVQIAQLETALKSDLTDKTEILDRLKTERGALINQNEKLVQENRELQLQYLEQK 439
Cdd:COG4942 171 AERAEL-----------------EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
....*....
gi 530423734 440 QQLDELKKR 448
Cdd:COG4942 234 AEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
273-477 |
1.79e-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: 61.32 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 273 KQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLhsmKFSERRIEELQDRINDLE 352
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL---AALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 353 KERELLKENYDKLYDSAFSAAHEEQWKLK---------------EQQLKVQIAQLETALKSDLTDKTEILDRLKTERGAL 417
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPLALLlspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530423734 418 INQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQENDI---NADELSEALLLIKAQKEQK 477
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAElqqEAEELEALIARLEAEAAAA 239
|
|
| C2 |
smart00239 |
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ... |
796-891 |
2.11e-09 |
|
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.
Pssm-ID: 214577 [Multi-domain] Cd Length: 101 Bit Score: 55.96 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 796 LHITIRCCNHLQSRASHLQPHPYVVYKFFDFADHD--TAIIPSSNDPQFDDHMYFPVPmnmdldrYLKSESLSFYVFDDS 873
Cdd:smart00239 2 LTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKkkTKVVKNTLNPVWNETFEFEVP-------PPELAELEIEVYDKD 74
|
90
....*....|....*...
gi 530423734 874 DTQENIYIGKVNVPLISL 891
Cdd:smart00239 75 RFGRDDFIGQVTIPLSDL 92
|
|
| C2 |
pfam00168 |
C2 domain; |
796-903 |
7.79e-09 |
|
C2 domain;
Pssm-ID: 425499 [Multi-domain] Cd Length: 104 Bit Score: 54.25 E-value: 7.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 796 LHITIRCCNHLQSRASHLQPHPYV-VYKFFDFADHDTAIIPSSNDPQFDDHMYFPVPMNMDldrylksESLSFYVFDDSD 874
Cdd:pfam00168 3 LTVTVIEAKNLPPKDGNGTSDPYVkVYLLDGKQKKKTKVVKNTLNPVWNETFTFSVPDPEN-------AVLEIEVYDYDR 75
|
90 100
....*....|....*....|....*....
gi 530423734 875 TQENIYIGKVNVPLISLAHDRCISGIFEL 903
Cdd:pfam00168 76 FGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
201-577 |
1.64e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNVEMIKLH-KQLVEKS 279
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERlEELRELE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 280 NALSAMEGKFIQLQEKQRTLRISHDALMANgdelnmqlkeqrlkccSLEKQLHSMKFSERRIEELQDRINDLEKERELLK 359
Cdd:COG4717 163 EELEELEAELAELQEELEELLEQLSLATEE----------------ELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 360 ENYDKLYDSAFSAAHEEQWKLKEQQLKV--QIAQLETALKSDLTDKTEILDRLKTERGALI-----NQNEKLVQENRELQ 432
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARLLLLIaaALLALLGLGGSLLSLILTIAGVLFLVLGLLAllfllLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 433 LQYLEQKQQLD--ELKKRIKLYNQENDINADELSEALLLIKAQKEQkngdLSFLVKVDSEInkDLERSMRELQATHAETV 510
Cdd:COG4717 307 LQALPALEELEeeELEELLAALGLPPDLSPEELLELLDRIEELQEL----LREAEELEEEL--QLEELEQEIAALLAEAG 380
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530423734 511 QELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLqqDYELKVEQYVHLLDIRAARIHKLEAQLKDIA 577
Cdd:COG4717 381 VEDEEELRAALEQAEEYQELKEELEELEEQLEEL--LGELEELLEALDEEELEEELEELEEELEELE 445
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
211-573 |
3.67e-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: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 211 LENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQrsnirdnvemiKLHKQLVEKSNALSAMEGKFI 290
Cdd:pfam01576 73 LEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQ-----------KLQLEKVTTEAKIKKLEEDIL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 291 QLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSmkfSERRIEELQDRINDLEKERELLKENYDKLyDSAF 370
Cdd:pfam01576 142 LLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNK---HEAMISDLEERLKKEEKGRQELEKAKRKL-EGES 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 371 SAAHEEQWKLKEQ--QLKVQIAQLETALKSdltdkteILDRLKTERGalinQNEKLVQENRELQLQYLEQKQQLD-ELKK 447
Cdd:pfam01576 218 TDLQEQIAELQAQiaELRAQLAKKEEELQA-------ALARLEEETA----QKNNALKKIRELEAQISELQEDLEsERAA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 448 RIKLYNQENDINAD------ELSEALLLIKAQKE---QKNGDLSFLVKVDSEINKDLERSMRELQATHAETVQE------ 512
Cdd:pfam01576 287 RNKAEKQRRDLGEElealktELEDTLDTTAAQQElrsKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEElteqle 366
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530423734 513 ---------------LEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQL 573
Cdd:pfam01576 367 qakrnkanlekakqaLESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSEL 442
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
107-570 |
4.10e-08 |
|
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: 58.06 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 107 EMEEMIEQLQEKVHELEKQNETL--KNRLISAKQQLQTQGYRQTP----YNNVQSRINTGRRKAN---ENAGLQECpRKG 177
Cdd:TIGR00618 230 HLREALQQTQQSHAYLTQKREAQeeQLKKQQLLKQLRARIEELRAqeavLEETQERINRARKAAPlaaHIKAVTQI-EQQ 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 178 IKFQDADVAETphpmftkygnsllEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQ--LRRKENEIELSLLQLREQQA 255
Cdd:TIGR00618 309 AQRIHTELQSK-------------MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQeiHIRDAHEVATSIREISCQQH 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 256 TDqRSNIRDNVEMIKLhkqLVEKSNALSAMEGKFIQLQEKQRTLRISHDAL----MANGDELNMQLKEQRLKCCSLEKQL 331
Cdd:TIGR00618 376 TL-TQHIHTLQQQKTT---LTQKLQSLCKELDILQREQATIDTRTSAFRDLqgqlAHAKKQQELQQRYAELCAAAITCTA 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 332 HSMKFSERRIEELQDRInDLEKERELLKENYDKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLk 411
Cdd:TIGR00618 452 QCEKLEKIHLQESAQSL-KEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRR- 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 412 TERGalinqneklvqENRELQLQYLEQK--QQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDS 489
Cdd:TIGR00618 530 MQRG-----------EQTYAQLETSEEDvyHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQD 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 490 EINKDLERSMRELQATHAETVQELEKTRNMLIMQH--KINKDYQMEVEAVTRKMENLQQDyelkvEQYVHLLDIRAARIH 567
Cdd:TIGR00618 599 LTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHlqQCSQELALKLTALHALQLTLTQE-----RVREHALSIRVLPKE 673
|
...
gi 530423734 568 KLE 570
Cdd:TIGR00618 674 LLA 676
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
47-575 |
4.75e-08 |
|
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: 57.76 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 47 REELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDV-EMEEMIEQLQEKVHELEKQ 125
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIsRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 126 NETLKNRLISAKQQLQTQGYR----QTPYNNVQSRINTGRRKANENAGLQECPRKGIKFQDAdvaetphpmftkygnsLL 201
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEElaelEEKLEELKEELESLEAELEELEAELEELESRLEELEE----------------QL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 202 EEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNVEMI------------ 269
Cdd:TIGR02168 382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELeelqeelerlee 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 270 ---KLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFS---ERRIEE 343
Cdd:TIGR02168 462 aleELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDegyEAAIEA 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 344 -LQDRINDLEKER--------ELLKEN---------YDKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALK-------- 397
Cdd:TIGR02168 542 aLGGRLQAVVVENlnaakkaiAFLKQNelgrvtflpLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKlrkalsyl 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 398 -------SDLTDKTEILDRLK------TERGALINQNEKLVQENRELQLQYLEQKQQLDELKKRIKLynQENDINA---- 460
Cdd:TIGR02168 622 lggvlvvDDLDNALELAKKLRpgyrivTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEE--LEEKIAEleka 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 461 -DELSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQaTHAETVQELEKTRNMLIMQHKINKDY----QMEVE 535
Cdd:TIGR02168 700 lAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE-QLEERIAQLSKELTELEAEIEELEERleeaEEELA 778
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 530423734 536 AVTRKMENLQQDyelkVEQYVHLLDIRAARIHKLEAQLKD 575
Cdd:TIGR02168 779 EAEAEIEELEAQ----IEQLKEELKALREALDELRAELTL 814
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
328-577 |
5.07e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 328 EKQLHSMkfsERRIEELQDRINDLEKERELLK------ENYDKLydsafsaaheeQWKLKEQQLKVQIAQLETAlksdlt 401
Cdd:COG1196 178 ERKLEAT---EENLERLEDILGELERQLEPLErqaekaERYREL-----------KEELKELEAELLLLKLREL------ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 402 dkTEILDRLKTERGALINQNEKLVQENRELQLQYLEQKQQLDELKKRIklynqendinaDELSEALLLIKAQKEQKNGDL 481
Cdd:COG1196 238 --EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL-----------EEAQAEEYELLAELARLEQDI 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 482 SFLVKVDSEINKDLER---SMRELQATHAETVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQDYELKVEQYVHL 558
Cdd:COG1196 305 ARLEERRRELEERLEEleeELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
250
....*....|....*....
gi 530423734 559 LDIRAARIHKLEAQLKDIA 577
Cdd:COG1196 385 AEELLEALRAAAELAAQLE 403
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
229-576 |
7.11e-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: 57.11 E-value: 7.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 229 AEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNV-----------EM-IKLHKQLVEKSNALSAMEGKFIQLQEKQ 296
Cdd:pfam01576 12 EELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLqaetelcaeaeEMrARLAARKQELEEILHELESRLEEEEERS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 297 RTLRISHDALMANGDELNMQLKE-----QRLKccsLEKQL--HSMKFSERRIEELQDRINDLEKERELLKEnydKLYDSA 369
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLEEQLDEeeaarQKLQ---LEKVTteAKIKKLEEDILLLEDQNSKLSKERKLLEE---RISEFT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 370 FSAAHEEQWKLKEQQLKVQiaqlETALKSDLTdkteilDRLKTE---RGALINQNEKLVQENRELQLQYLEQKQQLDELk 446
Cdd:pfam01576 166 SNLAEEEEKAKSLSKLKNK----HEAMISDLE------ERLKKEekgRQELEKAKRKLEGESTDLQEQIAELQAQIAEL- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 447 kRIKLYNQEndinaDELSEALLLIKAQKEQKNgdlsflvkvdseinkDLERSMRELQATHAETVQELEKTRNMLIMQHKI 526
Cdd:pfam01576 235 -RAQLAKKE-----EELQAALARLEEETAQKN---------------NALKKIRELEAQISELQEDLESERAARNKAEKQ 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 527 NKDYQMEVEAVTRKME------NLQQDYELKVEQYVHLLDiRA----ARIHklEAQLKDI 576
Cdd:pfam01576 294 RRDLGEELEALKTELEdtldttAAQQELRSKREQEVTELK-KAleeeTRSH--EAQLQEM 350
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
201-576 |
8.18e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 8.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 201 LEEARGEIRNLENVIQSQRGQIEELEhlAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNVEMIKLHKQLVEKSN 280
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLE--EKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 281 ALSAMEGKfiqLQEKQRTLRishdALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSER---RIEELQDRINDLEKEREL 357
Cdd:PRK03918 311 EIEKRLSR---LEEEINGIE----ERIKELEEKEERLEELKKKLKELEKRLEELEERHElyeEAKAKKEELERLKKRLTG 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 358 L-KENYDKLYDSAFSAAHEEQWKLKE-----QQLKVQIAQLETAL-------------KSDLTDK---------TEILDR 409
Cdd:PRK03918 384 LtPEKLEKELEELEKAKEEIEEEISKitariGELKKEIKELKKAIeelkkakgkcpvcGRELTEEhrkelleeyTAELKR 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 410 LKTERGALINQNEKLVQENRELQ---------LQYLEQKQQLDELKKRIKLYNQENDINADELSEAL--LLIKAQKEQKN 478
Cdd:PRK03918 464 IEKELKEIEEKERKLRKELRELEkvlkkeselIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLkeKLIKLKGEIKS 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 479 gdlsflVKVDSEINKDLERSMRELQathaETVQELEKTRNMLImqHKINKDYQMEVEAVTRKMENLQQDYE--LKVEQYV 556
Cdd:PRK03918 544 ------LKKELEKLEELKKKLAELE----KKLDELEEELAELL--KELEELGFESVEELEERLKELEPFYNeyLELKDAE 611
|
410 420
....*....|....*....|
gi 530423734 557 HLLDIRAARIHKLEAQLKDI 576
Cdd:PRK03918 612 KELEREEKELKKLEEELDKA 631
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
48-573 |
1.02e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 48 EELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRL-GRDVEMEEMIEQLQEKVHELEKQN 126
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLeEKIRELEERIEELKKEIEELEEKV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 127 ETLKN---------RLISAKQQLQTQGYR--------QTPYNNVQSRINTGRRKANENAGLQEcPRKGIKfQDADVAETP 189
Cdd:PRK03918 283 KELKElkekaeeyiKLSEFYEEYLDELREiekrlsrlEEEINGIEERIKELEEKEERLEELKK-KLKELE-KRLEELEER 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 190 HpmftkygnSLLEEARGEIRNLENViqSQRGQIEELEHLAEILKTQLRRKEnEIELSLLQLREQQAT--DQRSNIRDNVE 267
Cdd:PRK03918 361 H--------ELYEEAKAKKEELERL--KKRLTGLTPEKLEKELEELEKAKE-EIEEEISKITARIGElkKEIKELKKAIE 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 268 MIKLHK----------------QLVEKSNA-LSAMEGKFIQLQEKQRTLRishdalmANGDELNMQLKEQR--LKCCSLE 328
Cdd:PRK03918 430 ELKKAKgkcpvcgrelteehrkELLEEYTAeLKRIEKELKEIEEKERKLR-------KELRELEKVLKKESelIKLKELA 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 329 KQLHSM--KFSERRIEELQDRindlEKERELLKENYDKLyDSAFSAAHEEQWKLKEqqLKVQIAQLETALKSDLTDKTEI 406
Cdd:PRK03918 503 EQLKELeeKLKKYNLEELEKK----AEEYEKLKEKLIKL-KGEIKSLKKELEKLEE--LKKKLAELEKKLDELEEELAEL 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 407 LDRLKTERGALINQNEKLVQENRELQLQYLEQK---QQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNgdlSF 483
Cdd:PRK03918 576 LKELEELGFESVEELEERLKELEPFYNEYLELKdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE---EL 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 484 LVKVDSEINKDLERSMRELQATHA----------ETVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQDYElKVE 553
Cdd:PRK03918 653 EKKYSEEEYEELREEYLELSRELAglraeleeleKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELRE-KVK 731
|
570 580
....*....|....*....|.
gi 530423734 554 QYVHLLDIRA-ARIHKLEAQL 573
Cdd:PRK03918 732 KYKALLKERAlSKVGEIASEI 752
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
338-598 |
1.61e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 338 ERRIEELQDRINDLEKERELLKENYDKL---------YDSAFSAAHEEQWKLKE-QQLKVQIAQLETALKsDLTDKTEIL 407
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALeaeldalqeRREALQRLAEYSWDEIDvASAEREIAELEAELE-RLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 408 DRLKTERGALINQNEKLVQENRELQLQYLEQKQQLDELKKRIK-LYNQENDINADELSEALLLIKAQKEQKNGDlsflvK 486
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDeLQDRLEAAEDLARLELRALLEERFAAALGD-----A 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 487 VDSEINKDLERSMRELQATHAETVQELEKTRnmlimqHKINKDYQMEVEAVT----------RKMENLQQD----YELK- 551
Cdd:COG4913 763 VERELRENLEERIDALRARLNRAEEELERAM------RAFNREWPAETADLDadleslpeylALLDRLEEDglpeYEERf 836
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530423734 552 -----------VEQYVHLLD--IRAA--RIHKLEAQLKDIAYGT-KQYKFKPEIMPDDSVDEF 598
Cdd:COG4913 837 kellnensiefVADLLSKLRraIREIkeRIDPLNDSLKRIPFGPgRYLRLEARPRPDPEVREF 899
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
114-481 |
2.73e-07 |
|
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: 55.03 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 114 QLQEKVHELEKQNETLKNRLISAKQQLQTQgyrQTPYNNVQSRINTGRRKANEnaglqecprkgIKFQDADvaetphpmf 193
Cdd:TIGR04523 215 SLESQISELKKQNNQLKDNIEKKQQEINEK---TTEISNTQTQLNQLKDEQNK-----------IKKQLSE--------- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 194 tkyGNSLLEEARGEIRNLENVIQSQRGQIEEL-----EHLAEILKTQLRRKENEIELSLLQLRE-----QQATDQRSNIR 263
Cdd:TIGR04523 272 ---KQKELEQNNKKIKELEKQLNQLKSEISDLnnqkeQDWNKELKSELKNQEKKLEEIQNQISQnnkiiSQLNEQISQLK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 264 D-----NVEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDAL---MANGDELNmQLKEQRLKCCSLEKQLHS-- 333
Cdd:TIGR04523 349 KeltnsESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLeskIQNQEKLN-QQKDEQIKKLQQEKELLEke 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 334 --------------MKFSERRIEELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQWKLKE--------QQLKVQIAQ 391
Cdd:TIGR04523 428 ierlketiiknnseIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKElkskekelKKLNEEKKE 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 392 LETALK------SDLTDKTEILDRLKTERGALINQNEKLVqENRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSE 465
Cdd:TIGR04523 508 LEEKVKdltkkiSSLKEKIEKLESEKKEKESKISDLEDEL-NKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEE 586
|
410
....*....|....*.
gi 530423734 466 ALLLIKaQKEQKNGDL 481
Cdd:TIGR04523 587 KQELID-QKEKEKKDL 601
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
206-508 |
3.18e-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: 55.07 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 206 GEIRNLENVIQSQRGQIEELEhlAEILKTQLRRKENEIELsllqlreqqatdqrsnirdnVEMIKLHKQLVEKSNALSam 285
Cdd:TIGR02169 230 KEKEALERQKEAIERQLASLE--EELEKLTEEISELEKRL--------------------EEIEQLLEELNKKIKDLG-- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 286 EGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKfseRRIEELQDRINDLEKERELLKENYDKL 365
Cdd:TIGR02169 286 EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL---AEIEELEREIEEERKRRDKLTEEYAEL 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 366 ydsafsaaheeqwKLKEQQLKVQIAQLET---ALKSDLTDKTEILDRLKTERGALINQNEKLVQENRELQLQYLEQKQQL 442
Cdd:TIGR02169 363 -------------KEELEDLRAELEEVDKefaETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAI 429
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530423734 443 DELKKRIKLYNQENDINADELSEA---LLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQATHAE 508
Cdd:TIGR02169 430 AGIEAKINELEEEKEDKALEIKKQewkLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
201-467 |
1.13e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 201 LEEARGEIRNLEnviqsqrgqiEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRdnvemIKLHKQLVEKSN 280
Cdd:COG4913 237 LERAHEALEDAR----------EQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRR-----LELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 281 ALSAmegkfiQLQEKQRTLRISHDALMANGDELNMQLKEQRLkccslekqlhsmkfseRRIEELQDRINDLEKERELLKE 360
Cdd:COG4913 302 AELA------RLEAELERLEARLDALREELDELEAQIRGNGG----------------DRLEQLEREIERLERELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 361 NYDKlYDSAFSAAHEEqWKLKEQQLKVQIAQLETALksdlTDKTEILDRLKTERGALINQNEKLVQENRELQlqyleqkQ 440
Cdd:COG4913 360 RRAR-LEALLAALGLP-LPASAEEFAALRAEAAALL----EALEEELEALEEALAEAEAALRDLRRELRELE-------A 426
|
250 260
....*....|....*....|....*..
gi 530423734 441 QLDELKKRIKLYNQENDINADELSEAL 467
Cdd:COG4913 427 EIASLERRKSNIPARLLALRDALAEAL 453
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
107-435 |
2.82e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.04 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 107 EMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQGYRQTPYNNVQSRINTGRRKANENAGLQECPRKGIKFQDADVA 186
Cdd:pfam15921 549 ECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVS 628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 187 --ETPHPMFTKYGNSLLEEARG---EIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQrsn 261
Cdd:pfam15921 629 dlELEKVKLVNAGSERLRAVKDikqERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQ--- 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 262 irdnvemiklhKQLVEKSNALSAMEGkfiqlqekqrtlrishdalmANGDELNMQLKEQRlKCCSLEKQLHSMkfsERRI 341
Cdd:pfam15921 706 -----------SELEQTRNTLKSMEG--------------------SDGHAMKVAMGMQK-QITAKRGQIDAL---QSKI 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 342 EELQDRINDLEKERELLKENYDKLYDSAFSAAHE--------EQWKLKEQQLKVQIAQLETALKSDLTDKTEILDrlkte 413
Cdd:pfam15921 751 QFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEknkmagelEVLRSQERRLKEKVANMEVALDKASLQFAECQD----- 825
|
330 340
....*....|....*....|..
gi 530423734 414 rgaLINQNEklvQENRELQLQY 435
Cdd:pfam15921 826 ---IIQRQE---QESVRLKLQH 841
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
63-548 |
5.23e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 5.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 63 LLKQHARKQEDKI--KRMATKLIRLVNDKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELEKQNETLKNRLISAKQQL 140
Cdd:COG4717 46 MLLERLEKEADELfkPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 141 QTQGYRQTP------YNNVQSRINTGRRKANENAGLQEcprkGIKFQDADVAETpHPMFTKYGNSLLEEARGEIRNLENV 214
Cdd:COG4717 126 QLLPLYQELealeaeLAELPERLEELEERLEELRELEE----ELEELEAELAEL-QEELEELLEQLSLATEEELQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 215 IQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQrsnIRDNVEMIKLHKQLVeksnALSAMEGKFIQLQE 294
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER---LKEARLLLLIAAALL----ALLGLGGSLLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 295 KQRTLRISHDALMANGDELNMQLKEQRLKccSLEKQLHSMKFSERRIEELQDRINDLEKERELLKENYDKLYDSAfSAAH 374
Cdd:COG4717 274 TIAGVLFLVLGLLALLFLLLAREKASLGK--EAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRI-EELQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 375 EEQWKLKEQQLKVQIAQLETALKsdltdktEILDRLKTERGALINQNEKLVQENRELQLQYLEQKQQLDELKKRIKlyNQ 454
Cdd:COG4717 351 ELLREAEELEEELQLEELEQEIA-------ALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELE--EL 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 455 ENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEIN---KDLERSmRELQATHAEtVQELEKTRNMLIMQHKInkdYQ 531
Cdd:COG4717 422 LEALDEEELEEELEELEEELEELEEELEELREELAELEaelEQLEED-GELAELLQE-LEELKAELRELAEEWAA---LK 496
|
490
....*....|....*..
gi 530423734 532 MEVEAVTRKMENLQQDY 548
Cdd:COG4717 497 LALELLEEAREEYREER 513
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
107-576 |
5.94e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 5.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 107 EMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTqgyrqtpynnvqsrINTGRRKANENAGLQECPRKGIKFQDADVA 186
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEE--------------LEEERDDLLAEAGLDDADAEAVEARREELE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 187 ETphpmftkygnslLEEARGEIRNLENVIQSQRGQIE-------ELEHLAEILKTQLRRKENEIELSLLQLREQQA--TD 257
Cdd:PRK02224 321 DR------------DEELRDRLEECRVAAQAHNEEAEslredadDLEERAEELREEAAELESELEEAREAVEDRREeiEE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 258 QRSNIRDN--------VEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRIS---HDALMANG---------------- 310
Cdd:PRK02224 389 LEEEIEELrerfgdapVDLGNAEDFLEELREERDELREREAELEATLRTARERveeAEALLEAGkcpecgqpvegsphve 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 311 ---------DELNMQLKEQRLKCCSLEK---QLHSMKFSERRIEELQDRINDLEK----ERELLKENYDKL--------- 365
Cdd:PRK02224 469 tieedrervEELEAELEDLEEEVEEVEErleRAEDLVEAEDRIERLEERREDLEEliaeRRETIEEKRERAeelreraae 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 366 YDSAFSAAHEEQWKLKEQQLKVQ--IAQLETALkSDLTDKTEILDRLKTeRGALINQNEKLVQENRE----LQLQYLEQK 439
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEAReeVAELNSKL-AELKERIESLERIRT-LLAAIADAEDEIERLREkreaLAELNDERR 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 440 QQLDELKKRIKlyNQENDINADELSEAllliKAQKEQKNgdlSFLVKVDSEInKDLERSMRELQATHAETVQELEKTRNm 519
Cdd:PRK02224 627 ERLAEKRERKR--ELEAEFDEARIEEA----REDKERAE---EYLEQVEEKL-DELREERDDLQAEIGAVENELEELEE- 695
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 530423734 520 LIMQHKINKDYQMEVEAVTRKMENLQQDY-ELKVEqyvhlldIRAARIHKLEAQLKDI 576
Cdd:PRK02224 696 LRERREALENRVEALEALYDEAEELESMYgDLRAE-------LRQRNVETLERMLNET 746
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
201-455 |
9.05e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 9.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIR-DNVEMIKLHKQLVEKS 279
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDaSSDDLAALEEQLEELE 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 280 NALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLkEQRLKCCSLEKQLHsmkFSERRIEELQDRI-----NDLEKE 354
Cdd:COG4913 699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL-EAAEDLARLELRAL---LEERFAAALGDAVerelrENLEER 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 355 RELLKENYDKLYDSAFSAAHE--EQWKLKEQQLKVQIAqletalksDLTDKTEILDRLKTERgaLINQNEKLVQENRELQ 432
Cdd:COG4913 775 IDALRARLNRAEEELERAMRAfnREWPAETADLDADLE--------SLPEYLALLDRLEEDG--LPEYEERFKELLNENS 844
|
250 260
....*....|....*....|....*...
gi 530423734 433 LQYLEQ-----KQQLDELKKRIKLYNQE 455
Cdd:COG4913 845 IEFVADllsklRRAIREIKERIDPLNDS 872
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
341-582 |
1.44e-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: 49.68 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 341 IEELQDRINDLEKERElLKENYDKLydsafsaaheeQWKLKEQQLKVQIAQLETALKS------DLTDKTEILDRLKTER 414
Cdd:TIGR02169 193 IDEKRQQLERLRRERE-KAERYQAL-----------LKEKREYEGYELLKEKEALERQkeaierQLASLEEELEKLTEEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 415 GALINQNEKLVQENRELQLQ--------YLEQKQQLDELKKRIKLYNQENDINADELSEalllikAQKEQKNGDlSFLVK 486
Cdd:TIGR02169 261 SELEKRLEEIEQLLEELNKKikdlgeeeQLRVKEKIGELEAEIASLERSIAEKERELED------AEERLAKLE-AEIDK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 487 VDSEInKDLERSMRELQATHA---ETVQELEKTRNMLIMQ-------HKI----NKDYQMEVEAVTRKMENLQQDY---- 548
Cdd:TIGR02169 334 LLAEI-EELEREIEEERKRRDkltEEYAELKEELEDLRAEleevdkeFAEtrdeLKDYREKLEKLKREINELKRELdrlq 412
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 530423734 549 ELKVEQYVHLLDIRA------ARIHKLEAQLKDIAYGTKQ 582
Cdd:TIGR02169 413 EELQRLSEELADLNAaiagieAKINELEEEKEDKALEIKK 452
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
148-515 |
1.64e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 49.52 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 148 TPYNNVQSRINTGRRKANENAGLQECPRKGIKFQDADVAetphpmftkygnslLEEARGEIRNLE-NVIQSQRGQIEELE 226
Cdd:PLN02939 91 TSSDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQ--------------LEDLVGMIQNAEkNILLLNQARLQALE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 227 HLAEIL--KTQLRRKENEIELSLLQLREQQATDQRSNIrdNVEMikLHKQLVEKSNALSAmegkfiqlqekqrTLRISHD 304
Cdd:PLN02939 157 DLEKILteKEALQGKINILEMRLSETDARIKLAAQEKI--HVEI--LEEQLEKLRNELLI-------------RGATEGL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 305 ALMANGDELNMqLKEQRLkccSLEKQLHSMKFSERRIEELQDRINDLEKERELLKENYDKLyDSAFSAAHEEQWKLKEQQ 384
Cdd:PLN02939 220 CVHSLSKELDV-LKEENM---LLKDDIQFLKAELIEVAETEERVFKLEKERSLLDASLREL-ESKFIVAQEDVSKLSPLQ 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 385 LKVQIAQLETalksdLTDkteILDRLKtergaliNQNEK---LVQENRELqlqyleqKQQLDELKKRIKlynqenDINAD 461
Cdd:PLN02939 295 YDCWWEKVEN-----LQD---LLDRAT-------NQVEKaalVLDQNQDL-------RDKVDKLEASLK------EANVS 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530423734 462 ELSEALLLIKAQK----EQKngdlsfLVKVDSEINKDL---ERSMRELQATHAETVQELEK 515
Cdd:PLN02939 347 KFSSYKVELLQQKlkllEER------LQASDHEIHSYIqlyQESIKEFQDTLSKLKEESKK 401
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
221-503 |
1.64e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 221 QIEELEHLAEILKTQLRRKENEIElsllqlREQQATDQRSNIRDNVEMIKlhKQLVEKSNALSAMEGKFIQLQEKQRTLR 300
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIE------RLEKFIKRTENIEELIKEKE--KELEEVLREINEISSELPELREELEKLE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 301 ISHDALmangDELNMQLKEQRLKCCSLEKqlhSMKFSERRIEELQDRINDLEKERELLKENYDKL-----YDSAFSAAHE 375
Cdd:PRK03918 228 KEVKEL----EELKEEIEELEKELESLEG---SKRKLEEKIRELEERIEELKKEIEELEEKVKELkelkeKAEEYIKLSE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 376 --EQWKLKEQQLKVQIAQLETALK------SDLTDKTEILDRLKTERGALINQNEKLvqENRELQLQYLEQKQ-QLDELK 446
Cdd:PRK03918 301 fyEEYLDELREIEKRLSRLEEEINgieeriKELEEKEERLEELKKKLKELEKRLEEL--EERHELYEEAKAKKeELERLK 378
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 447 KRIKLYNQEndinadELSEALLLIKAQKEQKNGDLSFLVKVDSEIN---KDLERSMRELQ 503
Cdd:PRK03918 379 KRLTGLTPE------KLEKELEELEKAKEEIEEEISKITARIGELKkeiKELKKAIEELK 432
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
37-600 |
1.90e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 37 KSRQAVSRVSREELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERvgggpkrlgRDVEMEEMIEQLQ 116
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE---------RRRELEERLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 117 EKVHELEKQNETLKNRLISAKQQLQTQGYRQTpyNNVQSRINTGRRKANENAGLQECPRKGIKFQDADVAETphpmftky 196
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELE--EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL-------- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 197 gnSLLEEARGEIRNLENVIQSQRGQIEELEHLAEilktQLRRKENEIELSLLQLREQQATDQRSNIRDNVEMIKLHKQLV 276
Cdd:COG1196 393 --RAAAELAAQLEELEEAEEALLERLERLEEELE----ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 277 EKSNALSAMEGKFIQLQEKQRTLRISHDALMAngDELNMQLKEQRLKccslekqlhsmkfsERRIEELQDRINDLEKERE 356
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLLLE--AEADYEGFLEGVK--------------AALLLAGLRGLAGAVAVLI 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 357 LLKENYDKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTdkteiLDRLKTERGALINQNEKLVQENRELQLQYL 436
Cdd:COG1196 531 GVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAT-----FLPLDKIRARAALAAALARGAIGAAVDLVA 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 437 EQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQkngdlsfLVKVDSEINKDLERSMRELQATHAETVQELEKT 516
Cdd:COG1196 606 SDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGR-------LREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 517 RNMLIMQHKINKDYQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDIAYGTKQYKFKPEIMPDDSVD 596
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
|
....
gi 530423734 597 EFDE 600
Cdd:COG1196 759 PPDL 762
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
209-443 |
1.98e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 209 RNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIE-------LSLLQLREQQATDQRSNIRDnvemiklhkQLVEKSNA 281
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEefrqkngLVDLSEEAKLLLQQLSELES---------QLAEARAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 282 LSAMEGKFIQLQEKQRTLRISHDALMAngDELNMQLKEQRLKccsLEKQLHSM--KFSER--RIEELQDRINDLekeREL 357
Cdd:COG3206 235 LAEAEARLAALRAQLGSGPDALPELLQ--SPVIQQLRAQLAE---LEAELAELsaRYTPNhpDVIALRAQIAAL---RAQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 358 LKENYDKLYDSAFSAAheEQWKLKEQQLKVQIAQLETALKSdLTDKTEILDRLKTErgalinqneklVQENRELQLQYLE 437
Cdd:COG3206 307 LQQEAQRILASLEAEL--EALQAREASLQAQLAQLEARLAE-LPELEAELRRLERE-----------VEVARELYESLLQ 372
|
....*.
gi 530423734 438 QKQQLD 443
Cdd:COG3206 373 RLEEAR 378
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
335-566 |
2.05e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 335 KFSERRIEELQDRINDLEKERELLKENYDkLYDSafsaahEEQWKLKEQQLkVQIAQLETALKSDLTDKTEILDRLKTER 414
Cdd:COG3206 178 EFLEEQLPELRKELEEAEAALEEFRQKNG-LVDL------SEEAKLLLQQL-SELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 415 GALINQNEKLVQ--ENRELQLQYLEQKQQLDELKKRiklYNQENDInadelsealllIKAQKEQKNGDLSFLVKVDSEIN 492
Cdd:COG3206 250 GSGPDALPELLQspVIQQLRAQLAELEAELAELSAR---YTPNHPD-----------VIALRAQIAALRAQLQQEAQRIL 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530423734 493 KDLERSMRELQATHAETVQELEKTRNMLimqhkinkdyqMEVEAVTRKMENLQQDYELKVEQYVHLLD-IRAARI 566
Cdd:COG3206 316 ASLEAELEALQAREASLQAQLAQLEARL-----------AELPELEAELRRLEREVEVARELYESLLQrLEEARL 379
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
191-537 |
2.41e-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: 48.81 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 191 PMFTKYGNSLLEEARGEIRNLENVIQSQR-----GQIEELEHLAEILKTQLRRK--ENEIELSLLQLREQQATDQRSNIR 263
Cdd:TIGR00618 601 EKLSEAEDMLACEQHALLRKLQPEQDLQDvrlhlQQCSQELALKLTALHALQLTltQERVREHALSIRVLPKELLASRQL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 264 DNVEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLR--------ISHDA---LMANGDELNMQLKE----QRLKCCSLE 328
Cdd:TIGR00618 681 ALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDrefneienASSSLgsdLAAREDALNQSLKElmhqARTVLKART 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 329 KQlHSMKFSERRIE-----ELQDRINDLEKERELLKENYdklydsafsaaheeqwklkeQQLKVQIAQLETALKSDLTDK 403
Cdd:TIGR00618 761 EA-HFNNNEEVTAAlqtgaELSHLAAEIQFFNRLREEDT--------------------HLLKTLEAEIGQEIPSDEDIL 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 404 TEILDRLKTERGALINQNEKLVQ---ENRELQLQYLEQKQQLDELKKRIKLYNQendinadeLSEALLLIKAQKEQKNGD 480
Cdd:TIGR00618 820 NLQCETLVQEEEQFLSRLEEKSAtlgEITHQLLKYEECSKQLAQLTQEQAKIIQ--------LSDKLNGINQIKIQFDGD 891
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 530423734 481 LsfLVKVDSEINKDLERSMRELQATHAETVQELektrnmlimQHKINKDYQMEVEAV 537
Cdd:TIGR00618 892 A--LIKFLHEITLYANVRLANQSEGRFHGRYAD---------SHVNARKYQGLALLV 937
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
201-365 |
2.45e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 201 LEEARGEIR---------NLENVIQSQRGQIEELEhlAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNVEMIKL 271
Cdd:COG3206 191 LEEAEAALEefrqknglvDLSEEAKLLLQQLSELE--SQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQL 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 272 HKQLVEKSNALSAMEGKF-------IQLQEKQRTLRISHDALMANG-DELNMQLKEQRLKCCSLEKQLHSMKFSERRIEE 343
Cdd:COG3206 269 RAQLAELEAELAELSARYtpnhpdvIALRAQIAALRAQLQQEAQRIlASLEAELEALQAREASLQAQLAQLEARLAELPE 348
|
170 180
....*....|....*....|..
gi 530423734 344 LQDRINDLEKERELLKENYDKL 365
Cdd:COG3206 349 LEAELRRLEREVEVARELYESL 370
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
225-590 |
2.55e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 225 LEHLAEILKTQLRRKEneielSLLQLREQQA-----TDQRSNIRDNVEMIKLHKQLVEKSNALSAmegkfiQLQEKQRTL 299
Cdd:TIGR02168 161 FEEAAGISKYKERRKE-----TERKLERTREnldrlEDILNELERQLKSLERQAEKAERYKELKA------ELRELELAL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 300 RISH-DALMANGDELNMQLKEQRLKCCSLEKQLHSmkfSERRIEELQDRINDLEKERELLKENYdklydsafsaaheeqw 378
Cdd:TIGR02168 230 LVLRlEELREELEELQEELKEAEEELEELTAELQE---LEEKLEELRLEVSELEEEIEELQKEL---------------- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 379 klkeQQLKVQIAQLETalksdltDKTEILDRLktergalinqnEKLVQENRELQLQYLEQKQQLDELKKRI-----KLYN 453
Cdd:TIGR02168 291 ----YALANEISRLEQ-------QKQILRERL-----------ANLERQLEELEAQLEELESKLDELAEELaeleeKLEE 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 454 QENDINA--DELSEALLLIKAQK----------EQKNGDLSFLVKVDSEINKDLER---SMRELQATHAETVQELEKTRN 518
Cdd:TIGR02168 349 LKEELESleAELEELEAELEELEsrleeleeqlETLRSKVAQLELQIASLNNEIERleaRLERLEDRRERLQQEIEELLK 428
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530423734 519 MLIMQHKinKDYQMEVEAVTRKMENLQQDYELKVEQyvhlLDIRAARIHKLEAQLKDIAYGTKQYKFKPEIM 590
Cdd:TIGR02168 429 KLEEAEL--KELQAELEELEEELEELQEELERLEEA----LEELREELEEAEQALDAAERELAQLQARLDSL 494
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
221-508 |
2.84e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.60 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 221 QIEELEHLAEILKT---QLRRKENEIELSLLQLREQqatdqrsniRDnvemiKLHKQLVEKSNALSAMEGKFIQLQEKQR 297
Cdd:COG1340 9 SLEELEEKIEELREeieELKEKRDELNEELKELAEK---------RD-----ELNAQVKELREEAQELREKRDELNEKVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 298 TLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSERRIEELQDRIN----DLEKERELLkenydklydsafsaa 373
Cdd:COG1340 75 ELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQtevlSPEEEKELV--------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 374 heEQWKLKEQQLKVQIAQLEtaLKSDLTDKTEILDRLKTERGALINQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYN 453
Cdd:COG1340 140 --EKIKELEKELEKAKKALE--KNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELH 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 530423734 454 QEND---INADELSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQATHAE 508
Cdd:COG1340 216 KEIVeaqEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIF 273
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
39-375 |
2.86e-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: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 39 RQAVSRVSRE--ELEDRFLRLHDE----NILLKQHARKQ---EDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDVEME 109
Cdd:TIGR02169 708 SQELSDASRKigEIEKEIEQLEQEeeklKERLEELEEDLsslEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 110 EMIEQLQEKVHELEKQNETLKN---RLISAKQQLQTQGYR----QTPYNNVQSRINTGRRKANENaglqecpRKGIKFQD 182
Cdd:TIGR02169 788 LSHSRIPEIQAELSKLEEEVSRieaRLREIEQKLNRLTLEkeylEKEIQELQEQRIDLKEQIKSI-------EKEIENLN 860
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 183 ADVAETphpmftkygNSLLEEARGEIRNLENVIQSQRGQIEELEhlAEIlkTQLRRKENEIELSLLQLREQQA--TDQRS 260
Cdd:TIGR02169 861 GKKEEL---------EEELEELEAALRDLESRLGDLKKERDELE--AQL--RELERKIEELEAQIEKKRKRLSelKAKLE 927
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 261 NIRDNVEMI-KLHKQLVEKSNALSAMEGKFIQLQEKQRtlrishdALMANGDeLNMQLKEQrlkccslekqlhsMKFSER 339
Cdd:TIGR02169 928 ALEEELSEIeDPKGEDEEIPEEELSLEDVQAELQRVEE-------EIRALEP-VNMLAIQE-------------YEEVLK 986
|
330 340 350
....*....|....*....|....*....|....*....
gi 530423734 340 RIEELQDRINDLEKERELLK---ENYDKLYDSAFSAAHE 375
Cdd:TIGR02169 987 RLDELKEKRAKLEEERKAILeriEEYEKKKREVFMEAFE 1025
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
208-464 |
3.57e-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: 48.28 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 208 IRNLENVIQSQRGQIEELEHLAEILKTQ--------------LRRKENEIElsllQLREQQATDQRSNIRDNVEMIKLHK 273
Cdd:pfam10174 403 IENLQEQLRDKDKQLAGLKERVKSLQTDssntdtalttleeaLSEKERIIE----RLKEQREREDRERLEELESLKKENK 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 274 QLVEKSNAL----SAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQL---HSMKFSERRIEELQD 346
Cdd:pfam10174 479 DLKEKVSALqpelTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLkkaHNAEEAVRTNPEIND 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 347 RINDLEKERELLKE-------NYDKLYDSAFSAAHEEQWKLKeqqlkvQIAQLETALKSDLTDKTEILDRLKTERGALIN 419
Cdd:pfam10174 559 RIRLLEQEVARYKEesgkaqaEVERLLGILREVENEKNDKDK------KIAELESLTLRQMKEQNKKVANIKHGQQEMKK 632
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 530423734 420 QNEKLVQENRELQLQYLE--QKQQLDELKKRIKLYNQENDINADELS 464
Cdd:pfam10174 633 KGAQLLEEARRREDNLADnsQQLQLEELMGALEKTRQELDATKARLS 679
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
200-573 |
3.63e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.18 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 200 LLEEARGEIRNLENVIQSQ----RGQIEELEHLA---EILKTQLRR-----KENEIELSLLQLREQQATDQRSnirdnVE 267
Cdd:pfam05483 262 LLEESRDKANQLEEKTKLQdenlKELIEKKDHLTkelEDIKMSLQRsmstqKALEEDLQIATKTICQLTEEKE-----AQ 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 268 MIKLHKQLVEKSNALSAMEGKFIQLQEkqrTLRISHDALMANGDELNMQLKEQRLKCCSLEKQlhsMKFSERRIEELQDR 347
Cdd:pfam05483 337 MEELNKAKAAHSFVVTEFEATTCSLEE---LLRTEQQRLEKNEDQLKIITMELQKKSSELEEM---TKFKNNKEVELEEL 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 348 INDLEKERELLKEN--YDKLYDSAFSAAHEEQWKLKEQQLKVQIAQLE-TALKSDLTDKTEILDRLKTERGALINQNEKL 424
Cdd:pfam05483 411 KKILAEDEKLLDEKkqFEKIAEELKGKEQELIFLLQAREKEIHDLEIQlTAIKTSEEHYLKEVEDLKTELEKEKLKNIEL 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 425 VQENRELQLQYLEQKQQLDELKkrIKLYNQENDINADELSEALLL-----IKAQKEQKNGDLSF----LVKVDSEINKDL 495
Cdd:pfam05483 491 TAHCDKLLLENKELTQEASDMT--LELKKHQEDIINCKKQEERMLkqienLEEKEMNLRDELESvreeFIQKGDEVKCKL 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 496 ERSMRELQATHAETvqeLEKTRNMLIMQHKINkDYQMEVEAVTRKMENLQQD---YELKVEQYVHLLDIRAARIHKLEAQ 572
Cdd:pfam05483 569 DKSEENARSIEYEV---LKKEKQMKILENKCN-NLKKQIENKNKNIEELHQEnkaLKKKGSAENKQLNAYEIKVNKLELE 644
|
.
gi 530423734 573 L 573
Cdd:pfam05483 645 L 645
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
204-554 |
3.74e-05 |
|
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: 48.03 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 204 ARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLRE---QQATDQRSNIR-----DNVEMIKLHKQl 275
Cdd:COG5185 204 VNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSdklEKLVEQNTDLRleklgENAESSKRLNE- 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 276 vEKSNALSAMEGKFIQLQEKQRTLRISHDAlmangDELNMQLKEQRLKCCSLEKQLHSMKFSERRIEELQDRINDLEKER 355
Cdd:COG5185 283 -NANNLIKQFENTKEKIAEYTKSIDIKKAT-----ESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 356 ELLKENYDKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERGALINQNEKLVQENRELQLQY 435
Cdd:COG5185 357 EAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSN 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 436 LEQKQQLDELKKRIKLYNQENDINADElsealLLIKAQKEQKNGDLSFLVKVDSEINKdLERSMRELQAT----HAETVQ 511
Cdd:COG5185 437 EEVSKLLNELISELNKVMREADEESQS-----RLEEAYDEINRSVRSKKEDLNEELTQ-IESRVSTLKATleklRAKLER 510
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 530423734 512 ELEKTRNMLIMQHKINKDYQMEVE-AVTRKMENLQQDYELKVEQ 554
Cdd:COG5185 511 QLEGVRSKLDQVAESLKDFMRARGyAHILALENLIPASELIQAS 554
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
201-450 |
6.40e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 6.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIElsllQLREQQATDQRSNIRDNVEMIKLHKQLVEKSN 280
Cdd:TIGR02169 296 IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE----ELEREIEEERKRRDKLTEEYAELKEELEDLRA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 281 ALSAMEGKFIQLQEKQRTLRISHDALmanGDELNMQLKEQRLKCCSLEKQLHSMKFSERRIEELQDRINDLEKEREllke 360
Cdd:TIGR02169 372 ELEEVDKEFAETRDELKDYREKLEKL---KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKE---- 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 361 nydklydsafsAAHEEQWKlKEQQLKVQIAQLETAlKSDLTDKTEILDRLKTERGALINQNEKLVQENRELQLQYLEQKQ 440
Cdd:TIGR02169 445 -----------DKALEIKK-QEWKLEQLAADLSKY-EQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRA 511
|
250
....*....|
gi 530423734 441 QLDELKKRIK 450
Cdd:TIGR02169 512 VEEVLKASIQ 521
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
223-592 |
6.46e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.41 E-value: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 223 EELEHLAEILKTQLRRKENEIELSLLQLREQQAT---------DQRSNIRDNVEMIKLH----KQLVEKSNAL-SAMEGK 288
Cdd:pfam05483 222 EKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKmkdltflleESRDKANQLEEKTKLQdenlKELIEKKDHLtKELEDI 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 289 FIQLQEKQRTLR-ISHDALMANGDELNM-QLKEQRLKCCSLEKQLHSMKfserrIEELQDRINDLEkerELLKENYDKLY 366
Cdd:pfam05483 302 KMSLQRSMSTQKaLEEDLQIATKTICQLtEEKEAQMEELNKAKAAHSFV-----VTEFEATTCSLE---ELLRTEQQRLE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 367 DSafsaahEEQWKLKEQQLKVQIAQLETALKsdLTDKTEI-LDRLKTergaLINQNEKLVQENRELQLQYLEQKQQLDEL 445
Cdd:pfam05483 374 KN------EDQLKIITMELQKKSSELEEMTK--FKNNKEVeLEELKK----ILAEDEKLLDEKKQFEKIAEELKGKEQEL 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 446 -----KKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEINKD-LERSMRELQATHAETVQELEKTRNM 519
Cdd:pfam05483 442 ifllqAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDkLLLENKELTQEASDMTLELKKHQED 521
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530423734 520 LIMQHKINKDYQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDIAYGTKQYKFKPEIMPD 592
Cdd:pfam05483 522 IINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILEN 594
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
398-573 |
6.59e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 398 SDLTDKTEILDRLKTERGALINQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEALLLIK--AQKE 475
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGerARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 476 QKNGD----LSFLVKVDSeINKDLERS--MRELQATHAETVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQDYE 549
Cdd:COG3883 96 YRSGGsvsyLDVLLGSES-FSDFLDRLsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180
....*....|....*....|....
gi 530423734 550 LKVEQYVHLLDIRAARIHKLEAQL 573
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQL 198
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
244-444 |
6.62e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.64 E-value: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 244 ELSLLQLREQQATDQRSNIRDNVEMIKLHK-------QLVEKSNALSAMEGKFIQLQEKQRTLRiSHDALMANGDELNMQ 316
Cdd:COG3096 442 YLAAFRAKEQQATEEVLELEQKLSVADAARrqfekayELVCKIAGEVERSQAWQTARELLRRYR-SQQALAQRLQQLRAQ 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 317 LKEqrlkccsLEKQLHSMKFSERRIEELQDRIN-------DLEKERELLKENYDKLYDSAfSAAHEEQWKLKEQ--QLKV 387
Cdd:COG3096 521 LAE-------LEQRLRQQQNAERLLEEFCQRIGqqldaaeELEELLAELEAQLEELEEQA-AEAVEQRSELRQQleQLRA 592
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530423734 388 QIAQLET------ALKSDLTDKTEILDRLKTERGALINQNEKLVQENRELQL---QYLEQKQQLDE 444
Cdd:COG3096 593 RIKELAArapawlAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVerdELAARKQALES 658
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
339-518 |
8.10e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 8.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 339 RRIEELQDRINDLEKERELLkenydklyDSAFSAAHEEQWKLKEQQLKVQIAQLETA---LKSDLTDKTEILDRLKTERG 415
Cdd:COG4913 262 ERYAAARERLAELEYLRAAL--------RLWFAQRRLELLEAELEELRAELARLEAElerLEARLDALREELDELEAQIR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 416 ALINQN-EKLVQENRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEINKD 494
Cdd:COG4913 334 GNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAA 413
|
170 180
....*....|....*....|....
gi 530423734 495 LERSMRELQATHAEtVQELEKTRN 518
Cdd:COG4913 414 LRDLRRELRELEAE-IASLERRKS 436
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
107-520 |
8.33e-05 |
|
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: 47.04 E-value: 8.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 107 EMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQGyrqtpyNNVQSRINTGRRKANENAGLQECprkgikfQDADVA 186
Cdd:pfam15921 257 KIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQA------NSIQSQLEIIQEQARNQNSMYMR-------QLSDLE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 187 ETphpmftkygnslLEEARGEIRNLENVIQSQrgqIEELEHLAEILKTQLRRKENEielsllqlrEQQATDQRSNIRDNV 266
Cdd:pfam15921 324 ST------------VSQLRSELREAKRMYEDK---IEELEKQLVLANSELTEARTE---------RDQFSQESGNLDDQL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 267 E--MIKLHKQlvEKSNALSAMEGKfiQLQEKQRTLRISHDALMANGDELNMQ-------LKEQRLKC-CSLEKQLHSMKF 336
Cdd:pfam15921 380 QklLADLHKR--EKELSLEKEQNK--RLWDRDTGNSITIDHLRRELDDRNMEvqrlealLKAMKSECqGQMERQMAAIQG 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 337 SERRIEELQDRINDLEKERELLKENYDKLY-----------------------DSAFSAAHEEQWKLKE---------QQ 384
Cdd:pfam15921 456 KNESLEKVSSLTAQLESTKEMLRKVVEELTakkmtlessertvsdltaslqekERAIEATNAEITKLRSrvdlklqelQH 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 385 LK-----VQIAQLET-ALKSDLTDKTEILDRLKTE--------------RGALINQNEKLVQE--NRELQLQYLE----- 437
Cdd:pfam15921 536 LKnegdhLRNVQTECeALKLQMAEKDKVIEILRQQienmtqlvgqhgrtAGAMQVEKAQLEKEinDRRLELQEFKilkdk 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 438 QKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEIN-----------------KDLERSMR 500
Cdd:pfam15921 616 KDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNslsedyevlkrnfrnksEEMETTTN 695
|
490 500
....*....|....*....|
gi 530423734 501 ELQATHAETVQELEKTRNML 520
Cdd:pfam15921 696 KLKMQLKSAQSELEQTRNTL 715
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
109-321 |
1.32e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 109 EEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQ----GYRQTPYNNVQSRINTGRRKANENAGLQECPRKGIKFQDAD 184
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALerriAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 185 VAE----------TPHPMFTKYGNSLLEEARGeIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIElSLLQLREQQ 254
Cdd:COG4942 106 LAEllralyrlgrQPPLALLLSPEDFLDAVRR-LQYLKYLAPARREQAEELRADLAELAALRAELEAERA-ELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530423734 255 ATDQRsnirdnvemiKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQR 321
Cdd:COG4942 184 EEERA----------ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
311-516 |
1.54e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 311 DELNMQLKEQRLKCCSLEKQLHSMkfsERRIEELQDRINDLEKERELLKENYDKLYDSAfsAAHEEQWKLKEQQLKVQIA 390
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDAL---QAELEELNEEYNELQAELEALQAEIDKLQAEI--AEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 391 Q----------LETALKSdlTDKTEILDRLKTeRGALINQNEKLVQENRELQLQYLEQKQQLDELKKRIKLynqendiNA 460
Cdd:COG3883 94 AlyrsggsvsyLDVLLGS--ESFSDFLDRLSA-LSKIADADADLLEELKADKAELEAKKAELEAKLAELEA-------LK 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 530423734 461 DELSEALLLIKAQKEQKNGDLSFLvkvdSEINKDLERSMRELQATHAETVQELEKT 516
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQL----SAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
312-605 |
1.55e-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: 46.58 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 312 ELNMQLKEQRLKCCSLEKQLHSMKFSERRIE-----------ELQDRINDLEKERELLKENYD-KLYDSAFSAAHEEQWK 379
Cdd:TIGR01612 562 EIKKELEEENEDSIHLEKEIKDLFDKYLEIDdeiiyinklklELKEKIKNISDKNEYIKKAIDlKKIIENNNAYIDELAK 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 380 LKEQQLKVQIAQLETALKsdlTDKTEILDRLKTERGALINQNEKLVQENrelQLQYLEQKQQLDELKKRI-KLYNQENDI 458
Cdd:TIGR01612 642 ISPYQVPEHLKNKDKIYS---TIKSELSKIYEDDIDALYNELSSIVKEN---AIDNTEDKAKLDDLKSKIdKEYDKIQNM 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 459 NADELSEALLLIkaqKEQKNGDLSFLVKVD----SEINKDLERSMRELQATHAE---TVQELEKTRNML-IMQHKINK-- 528
Cdd:TIGR01612 716 ETATVELHLSNI---ENKKNELLDIIVEIKkhihGEINKDLNKILEDFKNKEKElsnKINDYAKEKDELnKYKSKISEik 792
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530423734 529 -DYQMEVEAVTRKMENLQQDYElKVEQYVHLLDIRAARIHKLEAQLKDiaygtkqykfkpeiMPDDSVDEFDETIHLE 605
Cdd:TIGR01612 793 nHYNDQINIDNIKDEDAKQNYD-KSKEYIKTISIKEDEIFKIINEMKF--------------MKDDFLNKVDKFINFE 855
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
372-517 |
2.51e-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: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 372 AAHEEQWKLKE-QQLKVQIAQLETALKSDLTDKTEILDRLKTERGALINQNEKLvqenRELQLQYLEQKQQLDELKKRIK 450
Cdd:COG1579 1 AMPEDLRALLDlQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTEL----EDLEKEIKRLELEIEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 451 LYNQ-------ENDINA------------DELSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQATHAETVQ 511
Cdd:COG1579 77 KYEEqlgnvrnNKEYEAlqkeieslkrriSDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
....*.
gi 530423734 512 ELEKTR 517
Cdd:COG1579 157 ELEELE 162
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
48-453 |
3.62e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 48 EELEDRFLRLHDenilLKQHARKQEDKIKRMATKLIRLVNDKkryervggGPKRLGRDVEMEEMIEQLQEKVHELEKQNE 127
Cdd:COG4717 149 EELEERLEELRE----LEEELEELEAELAELQEELEELLEQL--------SLATEEELQDLAEELEELQQRLAELEEELE 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 128 TLKNRLISAKQQLQtQGYRQTPYNNVQSRINTGRRKANENAGLqeCPRKGIKFQDADVAETPHPMFTKYGnSLLEEARGE 207
Cdd:COG4717 217 EAQEELEELEEELE-QLENELEAAALEERLKEARLLLLIAAAL--LALLGLGGSLLSLILTIAGVLFLVL-GLLALLFLL 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 208 IRNLENVIQSQRGQIEELEHLAEILKTQLRRkeneielsLLQLREQQATDQRSNIRDNVEMIKLHKQLVEKSNALsameg 287
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEE--------LLAALGLPPDLSPEELLELLDRIEELQELLREAEEL----- 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 288 kfiqlqEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKfseRRIEELQDRINDLEKERELLKENYDklyd 367
Cdd:COG4717 360 ------EEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELK---EELEELEEQLEELLGELEELLEALD---- 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 368 safsaahEEQWKLKEQQLKVQIAQLETAlksdltdkteiLDRLKTERGALINQNEKLVQENR--ELQLQYLEQKQQLDEL 445
Cdd:COG4717 427 -------EEELEEELEELEEELEELEEE-----------LEELREELAELEAELEQLEEDGElaELLQELEELKAELREL 488
|
....*...
gi 530423734 446 KKRIKLYN 453
Cdd:COG4717 489 AEEWAALK 496
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
49-520 |
5.11e-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: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 49 ELEDRFLRLHDENILLKQHARKQEDKIKRMATKL--------------------IRLVNDK-KRYERVGGGPKRLGRDVE 107
Cdd:pfam01576 135 KLEEDILLLEDQNSKLSKERKLLEERISEFTSNLaeeeekakslsklknkheamISDLEERlKKEEKGRQELEKAKRKLE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 108 MEemIEQLQEKVHELEKQNETLKNRLISAKQQLQTQGYR----QTPYNNVQSRIntgRRKANENAGLQEcprkgikfqDA 183
Cdd:pfam01576 215 GE--STDLQEQIAELQAQIAELRAQLAKKEEELQAALARleeeTAQKNNALKKI---RELEAQISELQE---------DL 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 184 DVAETPHPMFTKYGNSLLEEARGEIRNLENVIQSQRGQIE-------ELEHLAEILKTQLRRKENEIElsllQLReQQAT 256
Cdd:pfam01576 281 ESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQElrskreqEVTELKKALEEETRSHEAQLQ----EMR-QKHT 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 257 DQRSNIRDNVEMIKLHKQLVEKSNAlsAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSlekqlhsmkf 336
Cdd:pfam01576 356 QALEELTEQLEQAKRNKANLEKAKQ--ALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE---------- 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 337 SERRIEELQDRINDLEKERELLKENYDKLyDSAFSAAHEEQWKLKEQQLKVQ-IAQLETALKSDLTDKteiLDRLKTERG 415
Cdd:pfam01576 424 SERQRAELAEKLSKLQSELESVSSLLNEA-EGKNIKLSKDVSSLESQLQDTQeLLQEETRQKLNLSTR---LRQLEDERN 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 416 ALINQNEKLVQENRELQLQYLEQKQQLDELKKRIklynqendinadelsealllikaqkEQKNGDLSFLVKVDSEINKDL 495
Cdd:pfam01576 500 SLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKL-------------------------EEDAGTLEALEEGKKRLQREL 554
|
490 500
....*....|....*....|....*
gi 530423734 496 ERSMRELQaTHAETVQELEKTRNML 520
Cdd:pfam01576 555 EALTQQLE-EKAAAYDKLEKTKNRL 578
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
198-360 |
5.24e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 198 NSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIElsllQLREQQATDQR--SNIRDNVEMIKLHKQL 275
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE----EVEARIKKYEEqlGNVRNNKEYEALQKEI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 276 VEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEqrlkccsLEKQLhsmkfsERRIEELQDRINDLEKER 355
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEE-------KKAEL------DEELAELEAELEELEAER 165
|
....*
gi 530423734 356 ELLKE 360
Cdd:COG1579 166 EELAA 170
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
201-555 |
7.16e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 7.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQAtdqrsnirdnvEMIKLHKQLVEKSN 280
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQA-----------ELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 281 ALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQrlkccslekqlhsmkfsERRIEELQDRINDLEKERELLKE 360
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER-----------------EEELKELEEQLESLQEELAALEQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 361 NYDKL----YDSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERGALINQNEKLVQENRELQLQYL 436
Cdd:COG4372 172 ELQALseaeAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEEL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 437 EQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQATHAETVQELEKT 516
Cdd:COG4372 252 LEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELA 331
|
330 340 350
....*....|....*....|....*....|....*....
gi 530423734 517 RNMLIMQHKINKDYQMEVEAVTRKMENLQQDYELKVEQY 555
Cdd:COG4372 332 LAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
339-577 |
7.44e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 43.52 E-value: 7.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 339 RRIEELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQWKLKEQ-QLKVQIAQLETALKS----------DLTDKTEIL 407
Cdd:pfam19220 41 RELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELeELVARLAKLEAALREaeaakeelriELRDKTAQA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 408 DRLKTERGALINQNEKLVQENREL--QLQYLEQK-----QQLDELKKRIKLYNQEN---DINADELSEALllikAQKEQK 477
Cdd:pfam19220 121 EALERQLAAETEQNRALEEENKALreEAQAAEKAlqraeGELATARERLALLEQENrrlQALSEEQAAEL----AELTRR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 478 NGDLSFLVKVDSEINKDLERSMRELQATH--AETVQELEKTRnmliMQHKINKdYQMEVEAVTRKMENLQQdyeLKVEQY 555
Cdd:pfam19220 197 LAELETQLDATRARLRALEGQLAAEQAERerAEAQLEEAVEA----HRAERAS-LRMKLEALTARAAATEQ---LLAEAR 268
|
250 260
....*....|....*....|..
gi 530423734 556 VHLLDiRAARIHKLEAQLKDIA 577
Cdd:pfam19220 269 NQLRD-RDEAIRAAERRLKEAS 289
|
|
| C2A_Tricalbin-like |
cd04044 |
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ... |
796-920 |
7.49e-04 |
|
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are present in Tricalbin, a yeast homolog of Synaptotagmin, which is involved in membrane trafficking and sorting. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-II topology.
Pssm-ID: 176009 [Multi-domain] Cd Length: 124 Bit Score: 40.62 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 796 LHITIRCCNHLQSRASHLQ-PHPYVVYKFFDFADHD-TAIIPSSNDPQFDDHMYFPVpmNMDldrylkSESLSFYVFDDS 873
Cdd:cd04044 4 LAVTIKSARGLKGSDIIGGtVDPYVTFSISNRRELArTKVKKDTSNPVWNETKYILV--NSL------TEPLNLTVYDFN 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 530423734 874 DTQENIYIGKVNVPLISLAHDRCISGI-FELTDHQKhPAGTIHVILKW 920
Cdd:cd04044 76 DKRKDKLIGTAEFDLSSLLQNPEQENLtKNLLRNGK-PVGELNYDLRF 122
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
271-456 |
7.89e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 43.26 E-value: 7.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 271 LHKQLVEKSNALSAMEGKFIQlQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHS----MKFSERRIEELQD 346
Cdd:pfam15905 127 LEKQLLELTRVNELLKAKFSE-DGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVtqknLEHSKGKVAQLEE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 347 RINDLEKERELLKENYDKL--YDSAFSAAHE--EQWKLKEQQLKVQIAQLET---ALKSDLTDKTEILDRLKTERGA--- 416
Cdd:pfam15905 206 KLVSTEKEKIEEKSETEKLleYITELSCVSEqvEKYKLDIAQLEELLKEKNDeieSLKQSLEEKEQELSKQIKDLNEkck 285
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 530423734 417 -LINQNEKLVQENRELQLQYleqKQQLDELKKRIKLYNQEN 456
Cdd:pfam15905 286 lLESEKEELLREYEEKEQTL---NAELEELKEKLTLEEQEH 323
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
207-410 |
9.34e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 9.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 207 EIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIElsllqlreqqatdqrsnirdnvemiKLHKQLVEKSNALSAME 286
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE-------------------------DLEKEIKRLELEIEEVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 287 GKFIQLQEKQRTLRishdalmaNGDELNmqlkeqrlkccSLEKQLHSMKfseRRIEELQDRINDLEKERELLKENYDKLy 366
Cdd:COG1579 73 ARIKKYEEQLGNVR--------NNKEYE-----------ALQKEIESLK---RRISDLEDEILELMERIEELEEELAEL- 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 530423734 367 dSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRL 410
Cdd:COG1579 130 -EAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
202-466 |
1.08e-03 |
|
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: 42.96 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 202 EEARGEIRNLENVIQSQRGQIEELEhlaeilkTQLRRKENEIELSLLQLREQQATDQRSNIR---DNVEMIKLHKQLVEK 278
Cdd:pfam07888 125 AAHEARIRELEEDIKTLTQRVLERE-------TELERMKERAKKAGAQRKEEEAERKQLQAKlqqTEEELRSLSKEFQEL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 279 SNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRlkccSLEKQLHSmkfSERRIEELQDRINDLEKERell 358
Cdd:pfam07888 198 RNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELR----SLQERLNA---SERKVEGLGEELSSMAAQR--- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 359 kenydklyDSAFSAAHeeQWKLKEQQLKVQIAQLETALKSDLTdkteildRLKTERGALIN----QNEKLVQENRELQ-L 433
Cdd:pfam07888 268 --------DRTQAELH--QARLQAAQLTLQLADASLALREGRA-------RWAQERETLQQsaeaDKDRIEKLSAELQrL 330
|
250 260 270
....*....|....*....|....*....|...
gi 530423734 434 QYLEQKQQLDELKKRIKLyNQENDINADELSEA 466
Cdd:pfam07888 331 EERLQEERMEREKLEVEL-GREKDCNRVQLSES 362
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
65-624 |
1.19e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 65 KQHARKQEDKIKRMATKLirlVNDKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELEKQNETLKNRLISAKqqlqtqg 144
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEKA---EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK------- 1418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 145 yrqtpynnvqsRINTGRRKANENAGLQECPRKGIKFQDADVAETPhpmftkygnslLEEARgEIRNLENVIQSQRgQIEE 224
Cdd:PTZ00121 1419 -----------KADEAKKKAEEKKKADEAKKKAEEAKKADEAKKK-----------AEEAK-KAEEAKKKAEEAK-KADE 1474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 225 LEHLAEilktqLRRKENEielslLQLREQQATDQRSNIRDNVEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHD 304
Cdd:PTZ00121 1475 AKKKAE-----EAKKADE-----AKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEE 1544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 305 ALMAngDELNmqlKEQRLKCCSLEKQLHSMKFSERRIEELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQWKLKEQQ 384
Cdd:PTZ00121 1545 KKKA--DELK---KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK 1619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 385 LKVQIAQLETALKSDLTDKTEILDRLKTERGALINQNEKLVQENRELQLQYLEQKQQLDELKKRiklynqendiNADELS 464
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA----------EEDEKK 1689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 465 EALLLIKAQKEQKNGDlsflvkvdsEINKDLERSMRElqathAETVQELEKTRNMLIMQHKinkdyqMEVEAVTRKMENL 544
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAE---------ELKKKEAEEKKK-----AEELKKAEEENKIKAEEAK------KEAEEDKKKAEEA 1749
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 545 QQDYEL--KVEQYVHLLDIRAARIHKLEAQLkdIAYGTKQYKFKPEIMPDDSV-DEFDETIHLERGENLFEIHIN--KVT 619
Cdd:PTZ00121 1750 KKDEEEkkKIAHLKKEEEKKAEEIRKEKEAV--IEEELDEEDEKRRMEVDKKIkDIFDNFANIIEGGKEGNLVINdsKEM 1827
|
....*
gi 530423734 620 FSSEV 624
Cdd:PTZ00121 1828 EDSAI 1832
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
29-576 |
1.35e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.29 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 29 ETSTTRTMKSRQAVSRVSREEL---EDRFLRLHDEnilLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGggPKRLGRD 105
Cdd:pfam12128 271 ETLIASRQEERQETSAELNQLLrtlDDQWKEKRDE---LNGELSAADAAVAKDRSELEALEDQHGAFLDAD--IETAAAD 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 106 VEMEEMIEQlqekvhELEKQNETLKnrLISAKQQLQTQGYRqtpynnvqsrintgRRKANENaglQECPRK--GIKFQDA 183
Cdd:pfam12128 346 QEQLPSWQS------ELENLEERLK--ALTGKHQDVTAKYN--------------RRRSKIK---EQNNRDiaGIKDKLA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 184 DVAETphpmftkyGNSLLEEARGEIRNLENVIQSQRGQieeleHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIR 263
Cdd:pfam12128 401 KIREA--------RDRQLAVAEDDLQALESELREQLEA-----GKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 264 DNVEMIKLHKQLVEKSNAlsamegKFIQLQEKQRTLRISHD-ALMANGDElNMQLKEQRLKCCSLEKQL----HSMkfse 338
Cdd:pfam12128 468 NFDERIERAREEQEAANA------EVERLQSELRQARKRRDqASEALRQA-SRRLEERQSALDELELQLfpqaGTL---- 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 339 rrieelqdrINDLEKERELLKENYDKLYDSAF-------------SAAHEE---------------QWKLKEQQLKVQIA 390
Cdd:pfam12128 537 ---------LHFLRKEAPDWEQSIGKVISPELlhrtdldpevwdgSVGGELnlygvkldlkridvpEWAASEEELRERLD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 391 QLETALKSDLTDKTEILDRLKTERGALINQNEKL------VQENRELQLQYLEQKQQL-----DELKKRIKLYNQENDIN 459
Cdd:pfam12128 608 KAEEALQSAREKQAAAEEQLVQANGELEKASREEtfartaLKNARLDLRRLFDEKQSEkdkknKALAERKDSANERLNSL 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 460 ADELSEALLLIKAQKEQKNGDLsflvkvdseinkdlersmRELQATHAETVQELEKTRNMLIMQHKINKDyqMEVEAVTR 539
Cdd:pfam12128 688 EAQLKQLDKKHQAWLEEQKEQK------------------REARTEKQAYWQVVEGALDAQLALLKAAIA--ARRSGAKA 747
|
570 580 590
....*....|....*....|....*....|....*..
gi 530423734 540 KMENLQQDYELKVEQyvhlLDIRAARIHKLEAQLKDI 576
Cdd:pfam12128 748 ELKALETWYKRDLAS----LGVDPDVIAKLKREIRTL 780
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
209-568 |
1.37e-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: 43.24 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 209 RNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQAtdqrsnirdnvemiklhkqlvEKSNALSamegk 288
Cdd:pfam01576 211 RKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETA---------------------QKNNALK----- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 289 fiqlqekqrtlriSHDALMANGDELNMQLKEQRLKCCSLEKQlhsmkfseRRieelqdrinDLEKERELLKENYDKLYDS 368
Cdd:pfam01576 265 -------------KIRELEAQISELQEDLESERAARNKAEKQ--------RR---------DLGEELEALKTELEDTLDT 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 369 afSAAHEEQWKLKEQQL--------------KVQIAQLETALKSDLTDKTEILDRLKTERGALINQNEKLVQENRELQ-- 432
Cdd:pfam01576 315 --TAAQQELRSKREQEVtelkkaleeetrshEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQae 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 433 LQYLEQKQQLDELKKRiKLYNQENDINA---------DELSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQ 503
Cdd:pfam01576 393 LRTLQQAKQDSEHKRK-KLEGQLQELQArlseserqrAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQ 471
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530423734 504 AThaetvQEL--EKTRNMLIMQHKINkdyQMEVEAvTRKMENLQQDYELK--VEQYVHLLDIRAARIHK 568
Cdd:pfam01576 472 DT-----QELlqEETRQKLNLSTRLR---QLEDER-NSLQEQLEEEEEAKrnVERQLSTLQAQLSDMKK 531
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
208-456 |
1.41e-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: 42.74 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 208 IRNLENVIQSQRGQIEELEHLAEILkTQLRRKENEIELSLLQLreQQATDQRSNIRDNVEMIKLHKQLVEKSNALSAMEG 287
Cdd:pfam15742 92 IRELELEVLKQAQSIKSQNSLQEKL-AQEKSRVADAEEKILEL--QQKLEHAHKVCLTDTCILEKKQLEERIKEASENEA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 288 KF-IQLQEKQRTLRIshdaLMANGDELNMQLKEQRLKCCSLE----KQLHSMKFSERRIEELQDRIND------------ 350
Cdd:pfam15742 169 KLkQQYQEEQQKRKL----LDQNVNELQQQVRSLQDKEAQLEmtnsQQQLRIQQQEAQLKQLENEKRKsdehlksnqels 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 351 -----LEKERELLKENYDKLYDSAfsAAHEEQWKLKEQQLKVQIAQL------ETALKS----DLTDKTEILDRL----K 411
Cdd:pfam15742 245 eklssLQQEKEALQEELQQVLKQL--DVHVRKYNEKHHHHKAKLRRAkdrlvhEVEQRDerikQLENEIGILQQQsekeK 322
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 530423734 412 TERGALINQNEKLVQENRELQLQYLEQ-------KQQLDELKKRIKLYNQEN 456
Cdd:pfam15742 323 AFQKQVTAQNEILLLEKRKLLEQLTEQeeliknnKRTISSVQNRVNFLDEEN 374
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
69-556 |
1.88e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 69 RKQEDKIKRMATKL---IRLVNDKKRYERvgggpkrlGRDVEMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQGY 145
Cdd:PTZ00121 1194 RKAEDARKAEAARKaeeERKAEEARKAED--------AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHF 1265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 146 --RQTPYNNVQSRINTGRRKANENAGLQECpRKGIKFQDADVAETPHPMFTKygnslLEEARGEIRNLENVIQSQRGQIE 223
Cdd:PTZ00121 1266 arRQAAIKAEEARKADELKKAEEKKKADEA-KKAEEKKKADEAKKKAEEAKK-----ADEAKKKAEEAKKKADAAKKKAE 1339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 224 ELEHLAEILKTQLRRKENEIELSllQLREQQATDQRSNIRDNVEMIKLHKQLVEKSNALsamEGKFIQLQEKQRTLRISH 303
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEAA--EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEA---KKKAEEDKKKADELKKAA 1414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 304 DAlMANGDELNMQLKEQRlKCCSLEKQLHSmkfsERRIEELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQWKLKEQ 383
Cdd:PTZ00121 1415 AA-KKKADEAKKKAEEKK-KADEAKKKAEE----AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEA 1488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 384 QLKVQiaqlETALKSDLTDKTEildrlktERGALINQNEKLVQENRELQLQYLEQKQQLDELKKriklynQENDINADEL 463
Cdd:PTZ00121 1489 KKKAE----EAKKKADEAKKAA-------EAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK------AEEKKKADEL 1551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 464 SEALLLIKAQKEQKNgdlsflvkvdSEINKDLERsmRELQATHAETVQELEKTRNMLIMQhKINKDYQMEVEAVTRKMEN 543
Cdd:PTZ00121 1552 KKAEELKKAEEKKKA----------EEAKKAEED--KNMALRKAEEAKKAEEARIEEVMK-LYEEEKKMKAEEAKKAEEA 1618
|
490
....*....|...
gi 530423734 544 LQQDYELKVEQYV 556
Cdd:PTZ00121 1619 KIKAEELKKAEEE 1631
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
341-458 |
1.94e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 341 IEELQDRINDLEKERELLKENYDKLydsafSAAHEEQWKLKEQQLKVQIAQLETALKSDltdkTEILDRLKTERGALINQ 420
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEA-----SFERLAELRDELAELEEELEALKARWEAE----KELIEEIQELKEELEQR 483
|
90 100 110
....*....|....*....|....*....|....*...
gi 530423734 421 NEKLVQENRELQlqylEQKQQLDELKKRIKLYNQENDI 458
Cdd:COG0542 484 YGKIPELEKELA----ELEEELAELAPLLREEVTEEDI 517
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
264-556 |
2.14e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 264 DNVEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKE---QRLKccSLEKQLHSMKFSERR 340
Cdd:PRK04863 835 PEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADEtlaDRVE--EIREQLDEAEEAKRF 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 341 IEELQDRINDLEKERELLK---ENYDKLYDSAFSAahEEQWKLKEQQLK--VQIAQLETALK-----SDLTDKTEILDRL 410
Cdd:PRK04863 913 VQQHGNALAQLEPIVSVLQsdpEQFEQLKQDYQQA--QQTQRDAKQQAFalTEVVQRRAHFSyedaaEMLAKNSDLNEKL 990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 411 KTERGALINQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEalllikaqkeqkngdlsFLVKVDSE 490
Cdd:PRK04863 991 RQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQD-----------------LGVPADSG 1053
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530423734 491 INKDLERSMRELQA---THAETVQELEKTRNMLimqhkinkdyQMEVEAVTRKMENLQQDYELKVEQYV 556
Cdd:PRK04863 1054 AEERARARRDELHArlsANRSRRNQLEKQLTFC----------EAEMDNLTKKLRKLERDYHEMREQVV 1112
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
232-515 |
2.39e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 232 LKTQLRRK--ENEIELSLL---------QLRE--QQATDQRSNIRDNVEMIKLHKQLVEKSNALSAMEgkfiqLQEKQRT 298
Cdd:PHA02562 147 LSAPARRKlvEDLLDISVLsemdklnkdKIRElnQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGEN-----IARKQNK 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 299 LrishdalmangDELnmqLKEqrlkccslEKQLHSmkfserRIEELQDRINDLEKERELLKENYDKLYDSAFSAaheeqw 378
Cdd:PHA02562 222 Y-----------DEL---VEE--------AKTIKA------EIEELTDELLNLVMDIEDPSAALNKLNTAAAKI------ 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 379 KLKEQQLKVQIAQLET-----ALKSDLTDKTEILdrlktergalinqnEKLVQENRELQLQYLEQKQQLDELKKRIKLYN 453
Cdd:PHA02562 268 KSKIEQFQKVIKMYEKggvcpTCTQQISEGPDRI--------------TKIKDKLKELQHSLEKLDTAIDELEEIMDEFN 333
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530423734 454 qendinadELSEALLLIKAQKEQKNGDLSFLVKVdseiNKDLERSMRELQATHAETVQELEK 515
Cdd:PHA02562 334 --------EQSKKLLELKNKISTNKQSLITLVDK----AKKVKAAIEELQAEFVDNAEELAK 383
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
83-360 |
2.62e-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: 42.03 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 83 IRLVNDKKRYERVgggpKRLGRDVEMEEM--IEQLQekvHELEKQNETLKNRLISAKQQLQTQGYRQTPYNNvQSRINTG 160
Cdd:pfam17380 353 IRQEERKRELERI----RQEEIAMEISRMreLERLQ---MERQQKNERVRQELEAARKVKILEEERQRKIQQ-QKVEMEQ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 161 RRKANENAGLQECPRkgikfqdadvaetphpmftkygnslLEEARGeiRNLENVIQSQrgqiEELEHLAEILKTQ-LRRK 239
Cdd:pfam17380 425 IRAEQEEARQREVRR-------------------------LEEERA--REMERVRLEE----QERQQQVERLRQQeEERK 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 240 ENEIELSLLQLREQQATDQRSNIRDNvEMIKLHKQLVEKSNALSAMEGkfiQLQEKQRTLRISHDALMANGDELNMQLKE 319
Cdd:pfam17380 474 RKKLELEKEKRDRKRAEEQRRKILEK-ELEERKQAMIEEERKRKLLEK---EMEERQKAIYEEERRREAEEERRKQQEME 549
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 530423734 320 QRLKccsLEKQLhsMKFSERRieelqDRINDLEKERELLKE 360
Cdd:pfam17380 550 ERRR---IQEQM--RKATEER-----SRLEAMEREREMMRQ 580
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
248-450 |
3.20e-03 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 40.96 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 248 LQLREQQATDQRSNI-RDNVEMIKLHKQLVEKSNALSAM----EGKFIQLQEKQRTLRISHDALMANgdelnmQLKEQRL 322
Cdd:pfam17045 37 LDIREEELLSARNTLeRKHKEIGLLRQQLEELEKGKQELvakyEQQLQKLQEELSKLKRSYEKLQRK------QLKEARE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 323 KCCSLEKQLHSMKFSERRIEEL--------------QDRINDLEKERELLKENYDKLYDSAFSA--AHEEQwKLKEQQLK 386
Cdd:pfam17045 111 EAKSREEDRSELSRLNGKLEEFrqksleweqqrlqyQQQVASLEAQRKALAEQSSLIQSAAYQVqlEGRKQ-CLEASQSE 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530423734 387 VQ--IAQLETALKSDLTDKTEIlDRLKTERGALINQNEKLVQENRELQLQ---YLEQKQQLDELKKRIK 450
Cdd:pfam17045 190 IQrlRSKLERAQDSLCAQELEL-ERLRMRVSELGDSNRKLLEEQQRLLEElrmSQRQLQVLQNELMELK 257
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
112-470 |
3.32e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 112 IEQLQEKVHELEKQNETLKNRLISAKQQLQTQgyrQTPYNNVQSRINTG--------RRKANENAGLQECPRKGIKFQDA 183
Cdd:PRK11281 123 LRQLESRLAQTLDQLQNAQNDLAEYNSQLVSL---QTQPERAQAALYANsqrlqqirNLLKGGKVGGKALRPSQRVLLQA 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 184 DVAetphpmftkYGNSLLEEARGEIRN---LENVIQSQR----GQIEELEHLAEILKTQLRRKEneielslLQLREQQAt 256
Cdd:PRK11281 200 EQA---------LLNAQNDLQRKSLEGntqLQDLLQKQRdyltARIQRLEHQLQLLQEAINSKR-------LTLSEKTV- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 257 dqrsnirdnvemiklhKQLVEKSNALSAMEGKFIQlQEKQRTLRIShDALMANGDELNmQLKEQRLKccsLEKQLHSMKF 336
Cdd:PRK11281 263 ----------------QEAQSQDEAARIQANPLVA-QELEINLQLS-QRLLKATEKLN-TLTQQNLR---VKNWLDRLTQ 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 337 SERRIEE------------------------------LQDRINDLEKERELLKENYDKLYDSAFSAAheeqwKLKEQQLK 386
Cdd:PRK11281 321 SERNIKEqisvlkgslllsrilyqqqqalpsadliegLADRIADLRLEQFEINQQRDALFQPDAYID-----KLEAGHKS 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 387 VQIAQLETALKSDLTDKTEILDRLKTERGALINQ------------------NEKLVQE------NRELQLQYLEQ---- 438
Cdd:PRK11281 396 EVTDEVRDALLQLLDERRELLDQLNKQLNNQLNLainlqlnqqqllsvsdslQSTLTQQifwvnsNKPMDLDWLKAfpqa 475
|
410 420 430
....*....|....*....|....*....|...
gi 530423734 439 -KQQLDELKKRIKLYNqendiNADELSEALLLI 470
Cdd:PRK11281 476 lKDQFKSLKITVSFSN-----LWDGLFIALLLF 503
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
201-517 |
3.45e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.75 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKEneielsllqlREQQATDQRSNiRDNVEMIKLHKQLVEKSN 280
Cdd:pfam12128 236 IMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIA----------SRQEERQETSA-ELNQLLRTLDDQWKEKRD 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 281 A----LSAMEGKfiqLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMkfsERRIEELQDRINDLEKERE 356
Cdd:pfam12128 305 ElngeLSAADAA---VAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENL---EERLKALTGKHQDVTAKYN 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 357 LLKENYDklydsafsaaheeqwklkeQQLKVQIAQLEtalkSDLTDKTEILDRLKT-ERGALINQ----NEKLVQENREL 431
Cdd:pfam12128 379 RRRSKIK-------------------EQNNRDIAGIK----DKLAKIREARDRQLAvAEDDLQALeselREQLEAGKLEF 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 432 QLQYLEQKQQLDELKKRiklynqendINADELSEALLLikaQKEQKNGDLSFLVKVDSEINKDLERSMRELQATHAETVQ 511
Cdd:pfam12128 436 NEEEYRLKSRLGELKLR---------LNQATATPELLL---QLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQ 503
|
....*.
gi 530423734 512 ELEKTR 517
Cdd:pfam12128 504 ASEALR 509
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
198-573 |
3.84e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.65 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 198 NSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRdNVEMIKLHKQLVE 277
Cdd:pfam05557 89 NKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQL-RQNLEKQQSSLAE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 278 KSNALSAMEGKfIQLQE---------KQRTLRISH-DALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSERRIEELQDR 347
Cdd:pfam05557 168 AEQRIKELEFE-IQSQEqdseivknsKSELARIPElEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREE 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 348 INDLEKERELLKENYDKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERGALINQNEKLVQE 427
Cdd:pfam05557 247 AATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKK 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 428 NRELQLQYLEQKQQLDELKKRIKLYNQE------------NDINADELSEALLLIKAQKEQ-------KNGDLSFLVKVD 488
Cdd:pfam05557 327 IEDLNKKLKRHKALVRRLQRRVLLLTKErdgyrailesydKELTMSNYSPQLLERIEEAEDmtqkmqaHNEEMEAQLSVA 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 489 SE-------INKDLERSMREL--QATHA------ETVQELEKTRNMLIMQHKINKDYQMEVEAVTRKmENLQQDYELKVE 553
Cdd:pfam05557 407 EEelggykqQAQTLERELQALrqQESLAdpsyskEEVDSLRRKLETLELERQRLREQKNELEMELER-RCLQGDYDPKKT 485
|
410 420
....*....|....*....|....*...
gi 530423734 554 QYVHLLD--------IRAARIHKLEAQL 573
Cdd:pfam05557 486 KVLHLSMnpaaeayqQRKNQLEKLQAEI 513
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
112-466 |
4.66e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 112 IEQLQEKVHELEKQNETLKNRLISAKQQLQTQgyrqtpynnvqsrintgRRKANENAGLQEcprkgIKFQDADVAetphp 191
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDAL-----------------QERREALQRLAE-----YSWDEIDVA----- 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 192 mftkygnslleEARGEIRNLENVIQSQR---GQIEELEHLAEILKTQLRRKENEI-----ELSLLQLREQQATDQRSNIR 263
Cdd:COG4913 665 -----------SAEREIAELEAELERLDassDDLAALEEQLEELEAELEELEEELdelkgEIGRLEKELEQAEEELDELQ 733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 264 DNVEMIKLHKQLVEKSNAlsamEGKFIQLQEKQRTLRIShDALMANGDELNMQLKEQRLKccsLEKQLHsmKFSERRIEE 343
Cdd:COG4913 734 DRLEAAEDLARLELRALL----EERFAAALGDAVERELR-ENLEERIDALRARLNRAEEE---LERAMR--AFNREWPAE 803
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 344 LQDRINDLEKERELLKEnYDKLYDSAFsAAHEEQWK-LKEQQLKVQIAQLETALKSDLTDKTEILDRLktergalinqNE 422
Cdd:COG4913 804 TADLDADLESLPEYLAL-LDRLEEDGL-PEYEERFKeLLNENSIEFVADLLSKLRRAIREIKERIDPL----------ND 871
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 530423734 423 KLVQ----ENRELQLQYLE-QKQQLDELKKRIKLYNQENDINADELSEA 466
Cdd:COG4913 872 SLKRipfgPGRYLRLEARPrPDPEVREFRQELRAVTSGASLFDEELSEA 920
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
199-354 |
4.98e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 199 SLLEEARGEIRNLENVIQ---------SQRGQIEELEhLAEILKTQLRRKENEIELSLLQLREQQAtdqrsnirdnvEMI 269
Cdd:PRK04863 949 QTQRDAKQQAFALTEVVQrrahfsyedAAEMLAKNSD-LNEKLRQRLEQAEQERTRAREQLRQAQA-----------QLA 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 270 KLHKQLvekSNALSAMEGKFIQLQEKQR-----TLRISHDA---LMANGDELNMQLKEQRLKCCSLEKQLhsmKFSERRI 341
Cdd:PRK04863 1017 QYNQVL---ASLKSSYDAKRQMLQELKQelqdlGVPADSGAeerARARRDELHARLSANRSRRNQLEKQL---TFCEAEM 1090
|
170
....*....|...
gi 530423734 342 EELQDRINDLEKE 354
Cdd:PRK04863 1091 DNLTKKLRKLERD 1103
|
|
| YtrI |
COG5926 |
Uncharacterized sporulation protein YtrI [Cell cycle control, cell division, chromosome ... |
339-439 |
5.47e-03 |
|
Uncharacterized sporulation protein YtrI [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444627 [Multi-domain] Cd Length: 167 Bit Score: 39.16 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 339 RRIEELQDRINDLEKERELLKENYDKLYDsafsaahEEQWKLKEQQLKVQIAQLETaLKSDLTDKTEILDRLKTERGALI 418
Cdd:COG5926 43 EENRELQEEIAELENKIEILLEDQEELNE-------ENKEKLTVQSIEIKITNAES-YKLDNLTLHELEELIKEELSHLI 114
|
90 100
....*....|....*....|.
gi 530423734 419 NQNEKLVQENRELQLQYLEQK 439
Cdd:COG5926 115 GKDIETVAKSRDLLISTIENK 135
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
47-370 |
6.37e-03 |
|
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: 40.81 E-value: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 47 REELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDV-EMEEMIEQLQEKVHELEKQ 125
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAaNLRERLESLERRIAATERR 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 126 NETLKNRLISAKQQLQtqgyrqtpynNVQSRINTGRRKANEnagLQEcprkgiKFQDADVAETPHPMFTKYGNSLLEEAR 205
Cdd:TIGR02168 840 LEDLEEQIEELSEDIE----------SLAAEIEELEELIEE---LES------ELEALLNERASLEEALALLRSELEELS 900
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 206 GEIRNLENVIQSQRGQIEELEHLAEilktQLRRKENEIELSLLQLREQQATDQrsniRDNVEMIKLHKQLVEKSnaLSAM 285
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLA----QLELRLEGLEVRIDNLQERLSEEY----SLTLEEAEALENKIEDD--EEEA 970
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 286 EGKFIQLQEKQRTL-RISHDALmangDELnmQLKEQRLKccSLEKQLHSMKFSERRIEELQDRINDLEKER-----ELLK 359
Cdd:TIGR02168 971 RRRLKRLENKIKELgPVNLAAI----EEY--EELKERYD--FLTAQKEDLTEAKETLEEAIEEIDREARERfkdtfDQVN 1042
|
330
....*....|.
gi 530423734 360 ENYDKLYDSAF 370
Cdd:TIGR02168 1043 ENFQRVFPKLF 1053
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
221-428 |
7.95e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 221 QIEELEHLAEILKTQLRRKENEIElsllQLREQQATDQRSNIRDnvemiKLHKQLVEKSNALSAMEGKFIQlqekqrtlr 300
Cdd:PRK12704 32 KIKEAEEEAKRILEEAKKEAEAIK----KEALLEAKEEIHKLRN-----EFEKELRERRNELQKLEKRLLQ--------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 301 ishdalmangdelnmqlKEQRLkccslEKQLHSMKFSERRIEELQDRINDLEKERELLKENYDKLydsafsaaHEEQwkl 380
Cdd:PRK12704 94 -----------------KEENL-----DRKLELLEKREEELEKKEKELEQKQQELEKKEEELEEL--------IEEQ--- 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 530423734 381 kEQQLKvQIAQL--ETAlKSDLTDKTEilDRLKTERGALINQNEKLVQEN 428
Cdd:PRK12704 141 -LQELE-RISGLtaEEA-KEILLEKVE--EEARHEAAVLIKEIEEEAKEE 185
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
341-546 |
8.71e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 39.90 E-value: 8.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 341 IEELQDRI-NDLEKERELLKENydklydsafsAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERGALIN 419
Cdd:pfam00038 6 LQELNDRLaSYIDKVRFLEQQN----------KLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 420 QNEKLVQENRELQLQYleqkqqLDELKKRIklyNQENDINA-----DELSEALLLIKAQKEQKNGDLSFLVKVDSEinkd 494
Cdd:pfam00038 76 ELDNLRLAAEDFRQKY------EDELNLRT---SAENDLVGlrkdlDEATLARVDLEAKIESLKEELAFLKKNHEE---- 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530423734 495 lerSMRELQATHAETV----------QELEKTRNMLIMQH-KINKDYQMEVEA-VTRKMENLQQ 546
Cdd:pfam00038 143 ---EVRELQAQVSDTQvnvemdaarkLDLTSALAEIRAQYeEIAAKNREEAEEwYQSKLEELQQ 203
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
198-399 |
9.04e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 9.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 198 NSLLEEARGEIRNLENVIQSQRGQIEELEhlAEILKTQLRRKENEIELSLLQLREQQATDQRSN-IRDN---------VE 267
Cdd:COG3883 29 QAELEAAQAELDALQAELEELNEEYNELQ--AELEALQAEIDKLQAEIAEAEAEIEERREELGErARALyrsggsvsyLD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530423734 268 MIKLHK---QLVEKSNALSAMEGKFIQLQEKQRTLRishDALMANGDELNMQLKEQRLKCCSLEKQLHSMkfsERRIEEL 344
Cdd:COG3883 107 VLLGSEsfsDFLDRLSALSKIADADADLLEELKADK---AELEAKKAELEAKLAELEALKAELEAAKAEL---EAQQAEQ 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 530423734 345 QDRINDLEKERELLKENYDKLydSAFSAAHEEQWKLKEQQLKVQIAQLETALKSD 399
Cdd:COG3883 181 EALLAQLSAEEAAAEAQLAEL--EAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| |
