|
Name |
Accession |
Description |
Interval |
E-value |
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
2-680 |
0e+00 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 915.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 2 KRRNTEaGKPPRRPVKRAGKFaEGVCGSSFVYIKFVTIWLFILLADFILEFRFEYMWPFWLLLQSVYDTFKYQGLAYSVF 81
Cdd:pfam09726 1 KRRNAD-CSKLRRPLKRNRIT-EGIYGSTFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLLIRSVYDSFKYQGLAFSVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 82 FVCIAITSDTICLLFIPIQWLFFMASTYVWIHYVWHTDKGICLPTVSLWLLFMYIEATMRLRDLKSspFHIDLCRPFAAH 161
Cdd:pfam09726 79 FVCIAFTSDIICLLFIPVQWLFFAASTYVWVQYVWHTEKGICLPTVSLWILFVYIEAAIRFKDLKN--FHVDLCRPFAAH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 162 CIGHPSCDYGIGFKSYVSYRFKLRMQREVQKENTFYYELLRQALPKEQlnhtlSVTDKDKSEVSTPSNTSNGVLPHV--K 239
Cdd:pfam09726 157 CIGYPVVTLGFGFKSYVSYKMRLRKQREVQKENEFYMQLLQQALPKEQ-----QMLDRQERETSETAKGLSEVDPLAlnQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 240 KSHDRSKSspishDNTLQIAEVTPSPTKTT--------------VSSSGSSSTPSLSRKS--ANKSVPEHIPIWTPPVQE 303
Cdd:pfam09726 232 NGHSLNKK-----DSTLQLPELEYREKKNSgtssgsdskkshnhNIHNLNHVDSKLQEKEymENHSNSKRLNISTSPGSE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 304 IEVIFRKSNKSKKSSNESASSPTQQQQKSKSSNSGNNSPKSLKQNSSSRSSSVHSNDSEKQKAPILPNGHLgVKEVIPLP 383
Cdd:pfam09726 307 EDLLVRESVSSKSSSSSSSSNKNYKNASGGSANSSNSSPRSHSHNSGSVTSSSSSKNSKKQKGPGGKSGAR-HKDPAENC 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 384 LTNGHVipektenkieliSTPSAIERLEATIAKLQSELNQARKNDQEMKNQISLLTNLERSAKNDVNQLKKENDMLQTKV 463
Cdd:pfam09726 386 IPNNQL------------SKPDALVRLEQDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKL 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 464 NSMVSGKQKDKQSMQSMEKKLKSEADSRVNVEKQLHEEKRRRKEEEETAKHAAAQAQNNReKEKAEALKQAKHDLENEIL 543
Cdd:pfam09726 454 HNAVSAKQKDKQTVQQLEKRLKAEQEARASAEKQLAEEKKRKKEEEATAARAVALAAASR-GECTESLKQRKRELESEIK 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 544 KLEGQLKAKQEECDVMKKEISEFQLQEKSAKESETLMSALQAMQDKNLMLENSLSAETRLKLDLFSALGDVKRQLELAHG 623
Cdd:pfam09726 533 KLTHDIKLKEEQIRELEIKVQELRKYKESEKDTEVLMSALSAMQDKNQHLENSLSAETRIKLDLFSALGDAKRQLEIAQG 612
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 118344134 624 AIYKRDAEIVDLKSRLADILSILPE-SRIRSSTPHYSANFLEKPPLVRLSPTQEYPNN 680
Cdd:pfam09726 613 QIYQKDQEIKDLKQKIAEVMAVMPStSRITPVTPHYSSKFMDTSPSMRDPNASVYPPL 670
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
392-646 |
7.77e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 7.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 392 EKTENKIELISTpsAIERLEATIAKLQSELNQARKNDQEMKNQISLLTNLERSAKNDVNQLKKENDMLQTKVNSMVSGKQ 471
Cdd:COG1196 242 EELEAELEELEA--ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 472 KDKQSMQSMEKKLKSEADSRVNVEKQL------------HEEKRRRKEEEETAKHAAAQAQNNREKEKAEALKQAKHDLE 539
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELeeaeeeleeaeaELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 540 NEILKLEGQLKAKQEECDVMKKEISEfqLQEKSAKESETLMSALQAMQDKNLMLENSLSAETRLKLdlfsALGDVKRQLE 619
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEE--LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE----LLAELLEEAA 473
|
250 260
....*....|....*....|....*..
gi 118344134 620 LAHGAIYKRDAEIVDLKSRLADILSIL 646
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAE 500
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
407-639 |
6.92e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 6.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 407 IERLEATIAKLQSELNQARKNDQEMKNQISLLTNLERSAKNDVNQLKKENDMLQTKVnsmvsgkQKDKQSMQSMEKKLKS 486
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV-------EQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 487 EADSRVNVEKQLHEEKRRRKEEEetAKHAAAQAQNNREKEKAEALKQAKHDLENEILKLEGQLKAKQEECDVMKKEISEF 566
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAE--AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118344134 567 Q-----LQEKSAKESETLMSALQAMQDKNLMLENsLSAETRLKLDLFSALgdvKRQLELAHGAIYKRDAEIVDLKSRL 639
Cdd:TIGR02168 837 ErrledLEEQIEELSEDIESLAAEIEELEELIEE-LESELEALLNERASL---EEALALLRSELEELSEELRELESKR 910
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
392-652 |
3.09e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.45 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 392 EKTENKIELISTPSAIERLEATIAKLQSELNQARKNDQEMKNQISLLTNLERSAKNDVNQLKKENDMLQTKVNSMVSGKQ 471
Cdd:COG4372 60 ELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 472 KDKQSMQSMEKKLKSEADSRVNVEKQLHEEKRRRKEEEETAKHAAAQAQNNREKEKAEALKQAKHDLENEILKLEGQLKA 551
Cdd:COG4372 140 ELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 552 KQEEcdVMKKEISEFQLQEKSAKESETLMSALQAmqdknlmLENSLSAETRLKLDLFSALGDVKRQLELAHGAIYKRDAE 631
Cdd:COG4372 220 LLEA--KDSLEAKLGLALSALLDALELEEDKEEL-------LEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
|
250 260
....*....|....*....|.
gi 118344134 632 IVDLKSRLADILSILPESRIR 652
Cdd:COG4372 291 AALELKLLALLLNLAALSLIG 311
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
406-619 |
6.28e-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: 56.34 E-value: 6.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 406 AIERLEATIAKLQSEL-------NQARKNDQEMKNQI-SLLTNLE------------RSAK-NDVNQLKK----ENDMLQ 460
Cdd:pfam01576 265 KIRELEAQISELQEDLeseraarNKAEKQRRDLGEELeALKTELEdtldttaaqqelRSKReQEVTELKKaleeETRSHE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 461 TKVNSMvsgKQKDKQSMQSMEKKLKSEADSRVNVEKqlheekrrrkeeeetAKHAAaQAQNNREKEKAEALKQAKHDLEN 540
Cdd:pfam01576 345 AQLQEM---RQKHTQALEELTEQLEQAKRNKANLEK---------------AKQAL-ESENAELQAELRTLQQAKQDSEH 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 541 EILKLEGQLKAKQEECDVMKKEISEfqLQEKSAK---ESETLMSALQAMQDKNLMLENSLSA--------------ETRL 603
Cdd:pfam01576 406 KRKKLEGQLQELQARLSESERQRAE--LAEKLSKlqsELESVSSLLNEAEGKNIKLSKDVSSlesqlqdtqellqeETRQ 483
|
250
....*....|....*.
gi 118344134 604 KLDLFSALgdvkRQLE 619
Cdd:pfam01576 484 KLNLSTRL----RQLE 495
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
410-639 |
1.27e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.51 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 410 LEATIAKLQSELNQARK----NDQEMKNQISLLTNLERSAKNDVNQLKKENDMLQTKVNSMVSGKQKDKQSMqSMEKklk 485
Cdd:pfam15921 322 LESTVSQLRSELREAKRmyedKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKEL-SLEK--- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 486 sEADSRVnvekqlheeKRRRKEEEETAKHaaaqaqnnrekekaeaLKQAKHDLENEILKLEGQLKAKQEECD-VMKKEIS 564
Cdd:pfam15921 398 -EQNKRL---------WDRDTGNSITIDH----------------LRRELDDRNMEVQRLEALLKAMKSECQgQMERQMA 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118344134 565 EFQLQEKSAKESETLMSALQAMQDknlMLENSLSAETRLKLDLFSA---LGDVKRQLELAHGAIYKRDAEIVDLKSRL 639
Cdd:pfam15921 452 AIQGKNESLEKVSSLTAQLESTKE---MLRKVVEELTAKKMTLESSertVSDLTASLQEKERAIEATNAEITKLRSRV 526
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
392-643 |
1.07e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 392 EKTENKIEliSTPSAIERLEATIAKLQSELN----QARKND--QEMKNQislLTNLERS-AKNDVNQLKKENDMLQTKVN 464
Cdd:TIGR02168 175 KETERKLE--RTRENLDRLEDILNELERQLKslerQAEKAEryKELKAE---LRELELAlLVLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 465 SMvsgkqkdkqsmQSMEKKLKSEADsrvnvEKQlheekrrrkeeeetAKHAAAQAQNNREKEKAEALKQAKHDLENEILK 544
Cdd:TIGR02168 250 EA-----------EEELEELTAELQ-----ELE--------------EKLEELRLEVSELEEEIEELQKELYALANEISR 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 545 LEGQLKAKQEECDVMKKEISEFQLQ-EKSAKESETLMSALQAMQDKNLMLENslsaetrlKLDLFSALGDVKR-QLELAH 622
Cdd:TIGR02168 300 LEQQKQILRERLANLERQLEELEAQlEELESKLDELAEELAELEEKLEELKE--------ELESLEAELEELEaELEELE 371
|
250 260
....*....|....*....|.
gi 118344134 623 GAIYKRDAEIVDLKSRLADIL 643
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLE 392
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
391-602 |
1.39e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 391 PEKTENKIELISTPSAIERLEATIAKLQSELNQARKNDQEMKNQISLLTNLERSAKNDVNQLKKENDMLQTKVNSMVSGK 470
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 471 QKDKQSMQSMEKKLKSE--AD--SRVNVEKQLHEEKRRRKEEEETAKHAAAQAQnnrekekaEALKQAKHDLENEILKLE 546
Cdd:COG3883 96 YRSGGSVSYLDVLLGSEsfSDflDRLSALSKIADADADLLEELKADKAELEAKK--------AELEAKLAELEALKAELE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 118344134 547 GQLKAKQEECDVMKKEISEFQLQEKSAKESETLMSALQAMQDKNLMLENSLSAETR 602
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
390-643 |
1.67e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 390 IPEKTEN-----KIELISTPSAIERLEATIAKLQSELNQA----RKNDQEMKNQISLLTNLERsaknDVNQLKKENDMLQ 460
Cdd:TIGR02169 281 IKDLGEEeqlrvKEKIGELEAEIASLERSIAEKERELEDAeerlAKLEAEIDKLLAEIEELER----EIEEERKRRDKLT 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 461 TKVNSMVSGKQKDKQSMQSMEKKLKSEADSRVNVEKQLheekrrrkeEEETAKHAAAQAQNNREKEKAEALKQAKHDLEN 540
Cdd:TIGR02169 357 EEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL---------EKLKREINELKRELDRLQEELQRLSEELADLNA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 541 EILKLEGQLKAKQEECDVMKKEISEF-----QLQEKSAKESETLmSALQAMQDKnlmLENSLSaETRLKLDLFSALGDVK 615
Cdd:TIGR02169 428 AIAGIEAKINELEEEKEDKALEIKKQewkleQLAADLSKYEQEL-YDLKEEYDR---VEKELS-KLQRELAEAEAQARAS 502
|
250 260
....*....|....*....|....*...
gi 118344134 616 RQlelahGAIYKRDAEIVdLKSRLADIL 643
Cdd:TIGR02169 503 EE-----RVRGGRAVEEV-LKASIQGVH 524
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
397-676 |
1.69e-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: 51.66 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 397 KIELISTPSaiERLEAtIAKLQSELNQARKNDQEMKNQISLLTN----LERSAKNDVNQLKKENDMLQTKVNSMVSGKQK 472
Cdd:pfam15921 634 KVKLVNAGS--ERLRA-VKDIKQERDQLLNEVKTSRNELNSLSEdyevLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQ 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 473 DKQSMQSMEKKLKSEADSRVNVEKQLheekrrrkeeeeTAKHAAAQAQNNREKEKAEALKQA---KHDLENEILKLEGQL 549
Cdd:pfam15921 711 TRNTLKSMEGSDGHAMKVAMGMQKQI------------TAKRGQIDALQSKIQFLEEAMTNAnkeKHFLKEEKNKLSQEL 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 550 KAKQEECDVMKKEISEFQLQEKSAKESETLM------SALQAMQDKNLmLENSLSAETRLKLdlfSALGDVKrqlELaHG 623
Cdd:pfam15921 779 STVATEKNKMAGELEVLRSQERRLKEKVANMevaldkASLQFAECQDI-IQRQEQESVRLKL---QHTLDVK---EL-QG 850
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 118344134 624 AIYKRDAEivdLKSRLADILSIL-PESRIRSStpHYSANFLE----KPPLVRLSPTQE 676
Cdd:pfam15921 851 PGYTSNSS---MKPRLLQPASFTrTHSNVPSS--QSTASFLShhsrKTNALKEDPTRD 903
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
392-639 |
1.77e-06 |
|
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: 51.56 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 392 EKTENKIELISTPSAIERLEATIAKLQSELNQARKNDQEMKNQISLLTNLERSAKNDVNQLKKENDMLQTKVNSMVSGKQ 471
Cdd:TIGR04523 322 KLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 472 KDKQSMQSMEKKLKSEADSRVNVEKQlheekrrrkeeeetakHAAAQAQNNREKEKAEALKQAKHDLENEILKLEGQLKA 551
Cdd:TIGR04523 402 NQEKLNQQKDEQIKKLQQEKELLEKE----------------IERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 552 KQEECDVMKKEI-SEFQLQEKSAKESETLMSALQAMQDKNLMLENSLSaetrlklDLFSALGDVKRQLELAHGAIYKRDA 630
Cdd:TIGR04523 466 LETQLKVLSRSInKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK-------DLTKKISSLKEKIEKLESEKKEKES 538
|
....*....
gi 118344134 631 EIVDLKSRL 639
Cdd:TIGR04523 539 KISDLEDEL 547
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
407-658 |
6.14e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 6.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 407 IERLEATIAKLQSELNQARKNDQEMKNQIslltnleRSAKNDVNQLKKENDMLQTKVNSMVSGKQKDKQSMQSMEKKLKS 486
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLEEEL-------EQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 487 EADSRVNVEKQLheekrrrkeEEETAKHAAAQAQNNREKEKAEALKQAKHDLENEILKLEGQLKAKQEECDVMKKEISEF 566
Cdd:COG4372 113 LQEELEELQKER---------QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 567 QLQE-KSAKESETLMSALQAMQDKNLMLENSLSAETRLKLDLFSALGDVKRQLELAHGAIYKRDAEIVDLKSRLADILSI 645
Cdd:COG4372 184 ALDElLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
|
250
....*....|...
gi 118344134 646 LPESRIRSSTPHY 658
Cdd:COG4372 264 ELAILVEKDTEEE 276
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
404-565 |
8.70e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.61 E-value: 8.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 404 PSAIERLEATIAKLQSELNQARKNDQEMKNQIslltnleRSAKNDVNQLKKENDMLQTKVNSMVSGKQkdkqsMQSMEKK 483
Cdd:COG1579 30 PAELAELEDELAALEARLEAAKTELEDLEKEI-------KRLELEIEEVEARIKKYEEQLGNVRNNKE-----YEALQKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 484 LKSEADSRVNVEKQLheekRRRKEEEETAKHAAAQAQNNREKEKAEaLKQAKHDLENEILKLEGQLKAKQEECDVMKKEI 563
Cdd:COG1579 98 IESLKRRISDLEDEI----LELMERIEELEEELAELEAELAELEAE-LEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
..
gi 118344134 564 SE 565
Cdd:COG1579 173 PP 174
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
392-620 |
2.66e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.66 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 392 EKTENKIELISTPSAIERLEATIAKLQSELNQARKNDQEMKNQISLLTNLERSAK-NDVNQLKKENDMLQTKVNSMVSGK 470
Cdd:pfam02463 237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLaKEEEELKSELLKLERRKVDDEEKL 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 471 QKDKQSMQSMEKKLKSEADSRVNVEKQLHEekrrrkeeeetakHAAAQAQNNREKEKAEALKQAKHDLENEILKLEGQLK 550
Cdd:pfam02463 317 KESEKEKKKAEKELKKEKEEIEELEKELKE-------------LEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES 383
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 551 AKQEECDVMKKEISEFQLQEKSAKESETLMSALQAMQDKNLMLENSLSAETRLKLDLFSALGDVKRQLEL 620
Cdd:pfam02463 384 ERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEEL 453
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
515-646 |
3.04e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 515 AAAQAQNNREKEKAEALKQAKHDLENEILKLEGQLKAKQEEcdvmKKEISEFQLQEKSAKESETLMSALQAMQDKNLMLE 594
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR----IKKYEEQLGNVRNNKEYEALQKEIESLKRRISDLE 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 118344134 595 NSLsaetrlkLDLFSALGDVKRQLELAHGAIYKRDAEIVDLKSRLADILSIL 646
Cdd:COG1579 110 DEI-------LELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
392-619 |
3.28e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 392 EKTENKIELISTPSAIERLEATIAKLQSELN--QARKNDQEMKNqislLTNLERSAKNDVNQLKKENDMLQTKVNSMVSG 469
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLHKLEEALNdlEARLSHSRIPE----IQAELSKLEEEVSRIEARLREIEQKLNRLTLE 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 470 KQKDKQSMQSMEKKLKSEADSRVNVEKQLHeekrrrkeeeetakhaaaqaqnNREKEKAEALKQAKhDLENEILKLEGQL 549
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIE----------------------NLNGKKEELEEELE-ELEAALRDLESRL 884
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118344134 550 KAKQEECDVMKKEISEFQLQEKSAKES--------ETLMSALQAMQDKNLMLENSLSAETRLKLDLFSaLGDVKRQLE 619
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQiekkrkrlSELKAKLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQ 961
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
392-588 |
3.73e-05 |
|
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: 47.32 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 392 EKTENKIELISTpsAIERLEATIAKLQSELNQARKNDQEMKNQISLLTNLERSAKNDVNQLKKENDMLQTKVNSMVSGKQ 471
Cdd:TIGR04523 457 KNLDNTRESLET--QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKK 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 472 KDKQSMQSMEKKLKSEAD--SRVNVEKQLHEEKRRRKEEEETAKhaAAQAQNNREKEKAEALKQAKHDLENEILKLEGQL 549
Cdd:TIGR04523 535 EKESKISDLEDELNKDDFelKKENLEKEIDEKNKEIEELKQTQK--SLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI 612
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 118344134 550 KAKQEECDVMKKEISEFQLQEKSAKES-ETLMSALQAMQD 588
Cdd:TIGR04523 613 SSLEKELEKAKKENEKLSSIIKNIKSKkNKLKQEVKQIKE 652
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
399-636 |
3.77e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 399 ELISTPSAIERLEATIAKLQSELNQARKNDQEMKNqisLLTNLERSAKNDVNQLKKENDMLQTKVNSMVSGKqKDKQSMQ 478
Cdd:PRK03918 540 EIKSLKKELEKLEELKKKLAELEKKLDELEEELAE---LLKELEELGFESVEELEERLKELEPFYNEYLELK-DAEKELE 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 479 SMEKKLKSEADSRVNVEKQLheekRRRKEEEETAKHAAAQAQNNREKEKAEALKQAKHDLENEILKLEGQLKAKQEECDV 558
Cdd:PRK03918 616 REEKELKKLEEELDKAFEEL----AETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREE 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 559 MKKEISEFQLQ----EKSAKESETLMSALQAMQD--------KNLMLENSLSAETRLKLDLFSALGDVKRQlelahGAIY 626
Cdd:PRK03918 692 IKKTLEKLKEEleerEKAKKELEKLEKALERVEElrekvkkyKALLKERALSKVGEIASEIFEELTEGKYS-----GVRV 766
|
250
....*....|
gi 118344134 627 KRDAEIVDLK 636
Cdd:PRK03918 767 KAEENKVKLF 776
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
395-619 |
6.13e-05 |
|
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: 46.55 E-value: 6.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 395 ENKIELIStpSAIERLEATIAKLQSELNQARKNDQEMKNQISlltNLERSAKNDVNQLKKENDMLqTKVNS----MVSGK 470
Cdd:TIGR04523 39 EKKLKTIK--NELKNKEKELKNLDKNLNKDEEKINNSNNKIK---ILEQQIKDLNDKLKKNKDKI-NKLNSdlskINSEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 471 QKDKQSMQSMEKKLKSEADSRVNVEKQLheekrRRKEEEETAKHAAAQAQNNrekeKAEALKQAKHDLENEILKLEGQLK 550
Cdd:TIGR04523 113 KNDKEQKNKLEVELNKLEKQKKENKKNI-----DKFLTEIKKKEKELEKLNN----KYNDLKKQKEELENELNLLEKEKL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118344134 551 AKQEECDVMKKEISEFQLQ----EKSAKESETLMSALQAMQDKNLMLENSLSAETRLKLDLFSALGDVKRQLE 619
Cdd:TIGR04523 184 NIQKNIDKIKNKLLKLELLlsnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLN 256
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
408-677 |
9.82e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 9.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 408 ERLEATIAKLQSELNQARKNDQEMknqISLLTNLERSAKNDVNQLKKENDMLQTKVnsmvsgkQKDKQSMQSMEKKLKSE 487
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGIL---IAALSEQLRKALFELDKLQEELEQLREEL-------EQAREELEQLEEELEQA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 488 ADSRVNVEKQLheEKRRRKEEEETAKHAAAQAQNNREKEKAEALKQAKHDLENEILKLEGQLKAKQEECDVMKKEISEfq 567
Cdd:COG4372 72 RSELEQLEEEL--EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAE-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 568 lQEKSAKESETLMSALQAmQDKNLMLENSLSAETRLKLDLFSALGDVKRQLELAHGAIYKRDAEIVDLKSRLADILSILP 647
Cdd:COG4372 148 -REEELKELEEQLESLQE-ELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKD 225
|
250 260 270
....*....|....*....|....*....|
gi 118344134 648 ESRIRSSTPHYSANFLEKPPLVRLSPTQEY 677
Cdd:COG4372 226 SLEAKLGLALSALLDALELEEDKEELLEEV 255
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
422-571 |
1.14e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 422 NQARKNDQEMKNQ----ISLLTNLERSAKND---VNQLKKENDMLQTKVnsmvsgkQKDKQSMQSMEKKLKSEADSRVNv 494
Cdd:PRK00409 505 EEAKKLIGEDKEKlnelIASLEELERELEQKaeeAEALLKEAEKLKEEL-------EEKKEKLQEEEDKLLEEAEKEAQ- 576
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118344134 495 ekqlheekrrrkEEEETAKHAAAQA-QNNREKEKAEALKQAKHDLENEILKLEGQLKAKQEECDVMKKEISEFQLQEK 571
Cdd:PRK00409 577 ------------QAIKEAKKEADEIiKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVGDE 642
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
407-646 |
1.16e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 407 IERLE--ATIAK----LQSELNQARKndQEMKNQISLLTNLERSAKNDVNQLKKENDMLQTKVNSMVSGKQKDKQSMQSM 480
Cdd:COG1196 202 LEPLErqAEKAEryreLKEELKELEA--ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 481 EKKLKS------EADSRV-NVEKQLHEEKRRRKEEEETAKHAAAQAQnnREKEKAEALKQAKHDLENEILKLEGQLKAKQ 553
Cdd:COG1196 280 ELELEEaqaeeyELLAELaRLEQDIARLEERRRELEERLEELEEELA--ELEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 554 EECDVMKKEISEF-----QLQEKSAKESETLMSALQAMQDKNLMLENSLSAETRLKLDLFSALGDVKRQLELAHGAIYKR 628
Cdd:COG1196 358 AELAEAEEALLEAeaelaEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250
....*....|....*...
gi 118344134 629 DAEIVDLKSRLADILSIL 646
Cdd:COG1196 438 EEEEEALEEAAEEEAELE 455
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
515-634 |
1.75e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 515 AAAQAQNNREKEKAEALKQAKHDLENEILKLEGQLKAKQEECDVMKKEISEfqLQEKSAKESETLMSALQAMQdKNLMLE 594
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE--AEAEIEERREELGERARALY-RSGGSV 102
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 118344134 595 NSLSAetrlkldLFSA--LGDVKRQLELAhGAIYKRDAEIVD 634
Cdd:COG3883 103 SYLDV-------LLGSesFSDFLDRLSAL-SKIADADADLLE 136
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
405-577 |
1.90e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 405 SAIERLEATIAKLQSELNQARKNDQEMKNQISlltnlerSAKNDVNQLKKEndmlqtkvnsmVSGKQKDKQSMQSMEKKL 484
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLE-------AAKTELEDLEKE-----------IKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 485 kseadsrvnvEKQLheekrrrkeeeetakhaaAQAQNNRE-----KEKaEALKQAKHDLENEILKLEGQLKAKQEECDVM 559
Cdd:COG1579 79 ----------EEQL------------------GNVRNNKEyealqKEI-ESLKRRISDLEDEILELMERIEELEEELAEL 129
|
170
....*....|....*...
gi 118344134 560 KKEISEFQlQEKSAKESE 577
Cdd:COG1579 130 EAELAELE-AELEEKKAE 146
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
394-603 |
2.04e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 394 TENKIELISTPSAIERLEATIAKLQSELNQARKNDQEMKNQISLLTNLERSAK---------NDVNQLKKENDMLQTKVN 464
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEeyiklsefyEEYLDELREIEKRLSRLE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 465 SMVSGKQKDKQSMQSMEKKLKSEADSRVNVEKQLhEEKRRRKEEEETAKHAAAQAQN------NREKEKAEA----LKQA 534
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEELKKKLKELEKRL-EELEERHELYEEAKAKKEELERlkkrltGLTPEKLEKeleeLEKA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 535 KHDLENEILKLE---GQLKAKQEE--------------CDVMKKEISEFQLQE----------KSAKESETLMSALQAMQ 587
Cdd:PRK03918 400 KEEIEEEISKITariGELKKEIKElkkaieelkkakgkCPVCGRELTEEHRKElleeytaelkRIEKELKEIEEKERKLR 479
|
250
....*....|....*.
gi 118344134 588 DKNLMLENSLSAETRL 603
Cdd:PRK03918 480 KELRELEKVLKKESEL 495
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
407-649 |
2.23e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 407 IERLEATIAKLQSELNQARKNDQEMKNQISlltnlerSAKNDVNQLKKENDMLQTKVNSMVSGKQKDKQSMQS------- 479
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLE-------ELKEELESLEAELEELEAELEELESRLEELEEQLETlrskvaq 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 480 MEKKLKSEADSRVNVEKQLHEekrrrkeeeetakhaaaqAQNNREKEKAEALKQAKHDLENEILKLEGQLKAKQEECDVM 559
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLER------------------LEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEEL 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 560 KKEISEFQLQEKSAKES-ETLMSALQAMQDKnlmlENSLSAEtrlkldlFSALGDVKRQLELAHGAIykrdAEIVDLKSR 638
Cdd:TIGR02168 453 QEELERLEEALEELREElEEAEQALDAAERE----LAQLQAR-------LDSLERLQENLEGFSEGV----KALLKNQSG 517
|
250
....*....|.
gi 118344134 639 LADILSILPES 649
Cdd:TIGR02168 518 LSGILGVLSEL 528
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
407-642 |
2.37e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.63 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 407 IERLEATIAKLQSELNQARKNDQEMKNQISLLTNLERSAKNDVNQLKKENDMLQTKVNSMvsgkQKDKQSMQSMEKKLKS 486
Cdd:TIGR04523 119 KNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLL----EKEKLNIQKNIDKIKN 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 487 EadsRVNVEKQLHEEKRRRKEEEE-TAKHAAAQAQNNREKEKAEALKQAKHDLENEILKLEGQLKAKQEECDVMKKEISE 565
Cdd:TIGR04523 195 K---LLKLELLLSNLKKKIQKNKSlESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSE 271
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118344134 566 FQLQ-EKSAKESETLMSALQAMQDKNLMLENSLSAEtrLKLDLFSALGDVKRQLELAHGAIYKRDAEIVDLKSRLADI 642
Cdd:TIGR04523 272 KQKElEQNNKKIKELEKQLNQLKSEISDLNNQKEQD--WNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQL 347
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
411-585 |
2.72e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 411 EATIAKLQSELNQARKNDQEMKNQI-SLLTNLErSAKNDVNQLKKENDMLQTKVNSMVSGKQKDKQSMQSMEKKLKS--- 486
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELdALQAELE-ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 487 ----------------EADS------RVNVEKQLHEEKRRRKEEEETAKHAAAQAQNNREKEKAEA------LKQAKHDL 538
Cdd:COG3883 94 alyrsggsvsyldvllGSESfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELealkaeLEAAKAEL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 118344134 539 ENEILKLEGQLKAKQEECDVMKKEISEFQLQEKSAKESETLMSALQA 585
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
449-642 |
4.97e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 449 VNQLKKENDMLQTKvnsmvSGKQK--DKQSMQSMEKKLKSEAdsrvnvEKQLHEEKRRRKEEEETAKHAAAQAQNNREKE 526
Cdd:COG4717 48 LERLEKEADELFKP-----QGRKPelNLKELKELEEELKEAE------EKEEEYAELQEELEELEEELEELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 527 KAEALKQAK--HDLENEILKLEGQLKAKQEECDVMKKEISEF-QLQEKSAKESETLMSALQAMQDknLMLENSLSAETRL 603
Cdd:COG4717 117 ELEKLEKLLqlLPLYQELEALEAELAELPERLEELEERLEELrELEEELEELEAELAELQEELEE--LLEQLSLATEEEL 194
|
170 180 190
....*....|....*....|....*....|....*....
gi 118344134 604 KlDLFSALGDVKRQLELAHGAIYKRDAEIVDLKSRLADI 642
Cdd:COG4717 195 Q-DLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
392-555 |
5.73e-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: 42.83 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 392 EKTENKI-----ELISTPSAIERLEATIAKLQSELNQARKNDQEMKNQIS-LLTNLERSAKND-VNQLKKENDMLQTKVN 464
Cdd:COG4942 58 AALERRIaalarRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAeLLRALYRLGRQPpLALLLSPEDFLDAVRR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 465 SMVSGK--QKDKQSMQSMEKKLKSEADSRVNVEKQLHEEKRRRKEEEE------------TAKHAAAQAQNNREKEKAEA 530
Cdd:COG4942 138 LQYLKYlaPARREQAEELRADLAELAALRAELEAERAELEALLAELEEeraalealkaerQKLLARLEKELAELAAELAE 217
|
170 180
....*....|....*....|....*
gi 118344134 531 LKQAKHDLENEILKLEGQLKAKQEE 555
Cdd:COG4942 218 LQQEAEELEALIARLEAEAAAAAER 242
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
412-619 |
8.47e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 41.05 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 412 ATIAKLQSELNQARKNDQEMKNQISLLTNLERSAKNDVNQLKKENDMLQTKVNsmvsGKQKDKQSMQSMEKKLKSeadsr 491
Cdd:pfam13851 26 ELIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLE----NYEKDKQSLKNLKARLKV----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 492 vnVEKQLHeekrrrkeeeetakhaaaqaqnnREKEKAEALKQAKHDLENEIlkleGQLKAKQEECdvmkkeISEfqLQEK 571
Cdd:pfam13851 97 --LEKELK-----------------------DLKWEHEVLEQRFEKVERER----DELYDKFEAA------IQD--VQQK 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 118344134 572 SAKESETLMSALQAMQD----KNLMLENSLSAetrLKLDLfSALGDVKRQLE 619
Cdd:pfam13851 140 TGLKNLLLEKKLQALGEtlekKEAQLNEVLAA---ANLDP-DALQAVTEKLE 187
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
415-642 |
9.25e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 9.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 415 AKLQSElnQARKnDQEMKNQISLLTNLERSAKNDVNQLKKENDMLQTKVNSMVSGKQKDKQSMQSM-----EKKLKSEAD 489
Cdd:PTZ00121 1618 AKIKAE--ELKK-AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAkkaeeDEKKAAEAL 1694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 490 SRVNVEKQlheekrrrkeeeetaKHAAAQAQNNREKEKAEALKQAKhdlENEILKLEgQLKAKQEEcdvMKKEISEFQLQ 569
Cdd:PTZ00121 1695 KKEAEEAK---------------KAEELKKKEAEEKKKAEELKKAE---EENKIKAE-EAKKEAEE---DKKKAEEAKKD 1752
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118344134 570 EKSAKE-----SETLMSALQAMQDKNLMLENSLSAEtrlkldlfsalgDVKRQLELahgaiykrDAEIVDLKSRLADI 642
Cdd:PTZ00121 1753 EEEKKKiahlkKEEEKKAEEIRKEKEAVIEEELDEE------------DEKRRMEV--------DKKIKDIFDNFANI 1810
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
424-665 |
9.33e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 9.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 424 ARKNDQEMKNQISLLTNLERSAKNDVNQLKKENDMLQTKVNSMvsgKQKDKQSMQSMEKKLKSEADSRVNVEKQLHEEKR 503
Cdd:PTZ00121 1348 AKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK---KKADEAKKKAEEDKKKADELKKAAAAKKKADEAK 1424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 504 RRKEEEETAKHAAAQAQNNR----------EKEKAE-ALKQAKHDLENEILKLEGQLKAKQEE----CDVMKKEISEFQL 568
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAKkadeakkkaeEAKKAEeAKKKAEEAKKADEAKKKAEEAKKADEakkkAEEAKKKADEAKK 1504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 569 QEKSAKESETLMSALQAMQDKNL-------MLENSLSAETRLKLDLFSALGDVKRQLELAHGAIYKRDAEIVDLKSRLAD 641
Cdd:PTZ00121 1505 AAEAKKKADEAKKAEEAKKADEAkkaeeakKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE 1584
|
250 260
....*....|....*....|....
gi 118344134 642 ILSILPESRIRSSTPHYSANFLEK 665
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMK 1608
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
386-636 |
1.16e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.36 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 386 NGHVIPEKTE--NKIE--LISTPSAIERLEATIAKLQSELNQARKNDQEMKNQIslltnleRSAKNDVNQLKKENDMLQT 461
Cdd:TIGR02169 789 SHSRIPEIQAelSKLEeeVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQR-------IDLKEQIKSIEKEIENLNG 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 462 KVNSMVSGKQKDKQSMQSMEKKLKSEADSRVNVEKQLHEekrrrkeeeetakhaaaqAQNNREKEKAEALKQAKH--DLE 539
Cdd:TIGR02169 862 KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE------------------LERKIEELEAQIEKKRKRlsELK 923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 540 NEILKLEGQLKAKQEECDVMKKEISEFQLQEKSAKESETLMSALQAMQDKNlMLENSLSAETRLKLDlfsALGDVKRQLE 619
Cdd:TIGR02169 924 AKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVN-MLAIQEYEEVLKRLD---ELKEKRAKLE 999
|
250
....*....|....*..
gi 118344134 620 LAHGAIYKRDAEIVDLK 636
Cdd:TIGR02169 1000 EERKAILERIEEYEKKK 1016
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
397-641 |
1.86e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 397 KIELISTPSAIERLEATIAKLQSELNQARKNDQEMKNQISLLTNlersakndvnQLKKENDmlqtKVNSMVSGKQKDKQS 476
Cdd:pfam01576 123 QLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTS----------NLAEEEE----KAKSLSKLKNKHEAM 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 477 MQSMEKKLKSEADSRVNVEKqlheekrrrkeeeetakhaaaqaqnNREKEKAEA--LKQAKHDLENEILKLEGQLKAKQE 554
Cdd:pfam01576 189 ISDLEERLKKEEKGRQELEK-------------------------AKRKLEGEStdLQEQIAELQAQIAELRAQLAKKEE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 555 ECDVMKKEISEFQLQE----KSAKESETLMSALQ-------AMQDKNLMLENSLSAETR-LKLDLFSALGDVKRQLELAH 622
Cdd:pfam01576 244 ELQAALARLEEETAQKnnalKKIRELEAQISELQedleserAARNKAEKQRRDLGEELEaLKTELEDTLDTTAAQQELRS 323
|
250
....*....|....*....
gi 118344134 623 gaiyKRDAEIVDLKSRLAD 641
Cdd:pfam01576 324 ----KREQEVTELKKALEE 338
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
396-555 |
1.89e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 396 NKIELISTPSAIERLEATIAKLQSELNQARKNDQEMKNQISLLTNLERSAKNDVNQLkkENDMLQtkvnsmVSGKQKD-- 473
Cdd:COG4913 272 AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDEL--EAQIRG------NGGDRLEql 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 474 KQSMQSMEKKLKSEADSRVNVEKQLHEEKRRRKEEEE--TAKHAAAQAQNNREKEKAEALKQAKHDLENEILKLEGQLKA 551
Cdd:COG4913 344 EREIERLERELEERERRRARLEALLAALGLPLPASAEefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
|
....
gi 118344134 552 KQEE 555
Cdd:COG4913 424 LEAE 427
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
438-602 |
2.05e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 438 LTNLERSAKNDVNQLKKEndmlqtkvnsMVSGKQKDKQSMQSMEKKLKSEADSRVNvEKQLHEekrrrkeeeetakhaaa 517
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKE----------AEAIKKEALLEAKEEIHKLRNEFEKELR-ERRNEL----------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 518 QAQNNREKEKAEALKQAKHDL---ENEILKLEGQLKAKQEECDVMKKEISEfqLQEKSAKESETLmSALQAMQDKNLMLE 594
Cdd:PRK12704 85 QKLEKRLLQKEENLDRKLELLekrEEELEKKEKELEQKQQELEKKEEELEE--LIEEQLQELERI-SGLTAEEAKEILLE 161
|
....*...
gi 118344134 595 NsLSAETR 602
Cdd:PRK12704 162 K-VEEEAR 168
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
362-602 |
2.53e-03 |
|
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: 41.49 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 362 EKQKAPILPNGHLGVKEVipLPLTNGHVIPEKTENKIELISTPSAIERLEATiAKLQSELNQARKNDQEMKNQISLLTNL 441
Cdd:TIGR00618 206 LTLCTPCMPDTYHERKQV--LEKELKHLREALQQTQQSHAYLTQKREAQEEQ-LKKQQLLKQLRARIEELRAQEAVLEET 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 442 ERSakndVNQLKKENDML--QTKVNSMVSGKQKDKQSMQSMEKKLKSEADSRVNVEKQ-LHEEKRRRKEEEETAKHAAAQ 518
Cdd:TIGR00618 283 QER----INRARKAAPLAahIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQqSSIEEQRRLLQTLHSQEIHIR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 519 AQNNREKEKAEALKQAkHDLENEILKLEGQLKAKQEECDVMKKEISefQLQEKSAKeSETLMSALQAMQDKNLMLENSLS 598
Cdd:TIGR00618 359 DAHEVATSIREISCQQ-HTLTQHIHTLQQQKTTLTQKLQSLCKELD--ILQREQAT-IDTRTSAFRDLQGQLAHAKKQQE 434
|
....
gi 118344134 599 AETR 602
Cdd:TIGR00618 435 LQQR 438
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
395-652 |
2.57e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 395 ENKIELISTPSAIERLEATIAKLQSELNQARKNDQEMKNQISLLTNLERsaknDVNQLKKENDMLQTKVNSMVSGKQKDK 474
Cdd:PRK03918 197 EKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEK----ELESLEGSKRKLEEKIRELEERIEELK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 475 QSMQSMEKK------LKSEADSRVNVEKQLHEEKRRRKEEEETAKHAAAQAQNNRE--------KEKAEALKQAKHDLEN 540
Cdd:PRK03918 273 KEIEELEEKvkelkeLKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEErikeleekEERLEELKKKLKELEK 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 541 EILKLEG------QLKAKQEECDVMKKEISEFQLqEKSAKESETLMSALQAMQDKNLMLENSLSAETRLKLDLFSALGDV 614
Cdd:PRK03918 353 RLEELEErhelyeEAKAKKEELERLKKRLTGLTP-EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEEL 431
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 118344134 615 K----------RQLELAH--GAIYKRDAEIVDLKSRLADILSILPESRIR 652
Cdd:PRK03918 432 KkakgkcpvcgRELTEEHrkELLEEYTAELKRIEKELKEIEEKERKLRKE 481
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
407-577 |
2.90e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 407 IERLEAT----IAKLQSELNQARKNDQEMKNQISLLT----NLERSAKNDVNQLKKENdMLQTKVNSMVSGKQKD----- 473
Cdd:PHA02562 204 IEEQRKKngenIARKQNKYDELVEEAKTIKAEIEELTdellNLVMDIEDPSAALNKLN-TAAAKIKSKIEQFQKVikmye 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 474 --------KQSMQSMEKKLKSEADSRVNVEKQLHEEKRRRKEEEETAKHAAAQAQNNRE-KEKAEALKQAKHDLENEILK 544
Cdd:PHA02562 283 kggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLElKNKISTNKQSLITLVDKAKK 362
|
170 180 190
....*....|....*....|....*....|....*
gi 118344134 545 LEGQLKAKQEECDVMKKEISEFQ--LQEKSAKESE 577
Cdd:PHA02562 363 VKAAIEELQAEFVDNAEELAKLQdeLDKIVKTKSE 397
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
392-572 |
3.19e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 392 EKTENKIE-------LISTPSAIERLEATIAKLQSELNQARKNDQEMKNQISLLTNLERSAKND---------VNQLKKE 455
Cdd:COG3206 192 EEAEAALEefrqkngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDAlpellqspvIQQLRAQ 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 456 NDMLQTKVNSMVSGKQKDKQSMQSMEKKLKsEADSRVNVEKQLHEEKRRRKEEEETAKHAAAQAQNNREKEKAEALKQak 535
Cdd:COG3206 272 LAELEAELAELSARYTPNHPDVIALRAQIA-ALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPE-- 348
|
170 180 190
....*....|....*....|....*....|....*..
gi 118344134 536 hdLENEILKLEGQLKAKQEECDVMKKEISEFQLQEKS 572
Cdd:COG3206 349 --LEAELRRLEREVEVARELYESLLQRLEEARLAEAL 383
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
407-577 |
3.38e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 407 IERLEATIAKLQSELNQARKNdQEMKNQISLLTNLERSAKNDVNQLKKEndmLQTKVNSMVSGKQKdkqsmqsmEKKLKS 486
Cdd:COG1340 142 IKELEKELEKAKKALEKNEKL-KELRAELKELRKEAEEIHKKIKELAEE---AQELHEEMIELYKE--------ADELRK 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 487 EADsrvnvekqlheekrrrkeeeetakhaAAQAQNNREKEKAEALKQAKHDLENEILKLEGQLKAKQEECDVMKKEISEF 566
Cdd:COG1340 210 EAD--------------------------ELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKE 263
|
170
....*....|.
gi 118344134 567 QLQEKsAKESE 577
Cdd:COG1340 264 ELEEK-AEEIF 273
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
515-642 |
3.82e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 515 AAAQAQNNREKEKAEALKQAKHDLENEILKLEGQLKAKQEECDVMKKEISEFQ-----LQEKSAKESETLMSALQAMQdk 589
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEkeiaeLRAELEAQKEELAELLRALY-- 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 118344134 590 nlmlenSLSAETRLKLdLFSA--LGDVKRQLELAHGAIYKRDAEIVDLKSRLADI 642
Cdd:COG4942 115 ------RLGRQPPLAL-LLSPedFLDAVRRLQYLKYLAPARREQAEELRADLAEL 162
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
392-654 |
4.23e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 40.51 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 392 EKTENKIElisTPSAIERLEATIAKLQSEL--NQARKNDQEMKNQISLLTNLERSAKNDV--NQLKKENDMLQTKVNSMV 467
Cdd:pfam07111 175 EKSLNSLE---TKRAGEAKQLAEAQKEAELlrKQLSKTQEELEAQVTLVESLRKYVGEQVppEVHSQTWELERQELLDTM 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 468 SGKQKDKQSMQSMEKKLKseadsrVNVEKQLHEEKRRRKEEeeTAKhaaAQAQNNREKEKAEALKQAKHDLENEILKLEG 547
Cdd:pfam07111 252 QHLQEDRADLQATVELLQ------VRVQSLTHMLALQEEEL--TRK---IQPSDSLEPEFPKKCRSLLNRWREKVFALMV 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 548 QLKAKQ-EECDVMKK-EISEFQLQEKSAKESETLMSALQAMQDKNLMLENSLSAETRLKLDLFSA----------LGDVK 615
Cdd:pfam07111 321 QLKAQDlEHRDSVKQlRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAqearrrqqqqTASAE 400
|
250 260 270
....*....|....*....|....*....|....*....
gi 118344134 616 RQLELAHGAIYKRDAEIVDLKSRLADILSILPESRIRSS 654
Cdd:pfam07111 401 EQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLS 439
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
389-595 |
4.25e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.39 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 389 VIPEKTENKIELISTPSAIERLEATIAKLQSELNQARKNDQEMKNQISllTNLERSAKNDVNQLKKENDMLQTKVNSMVS 468
Cdd:TIGR04523 258 LKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNNK 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 469 GKQKDKQSMQSMEKKLKSEADSRVNVEKQLheekrrrkeeeeTAKHAAAQA---QNNREKEKAEALKQAKHDLENEILK- 544
Cdd:TIGR04523 336 IISQLNEQISQLKKELTNSESENSEKQREL------------EEKQNEIEKlkkENQSYKQEIKNLESQINDLESKIQNq 403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 118344134 545 ------LEGQLKAKQEECDVMKKEISEfqLQEKSAKESETLMSALQAMQDKNLMLEN 595
Cdd:TIGR04523 404 eklnqqKDEQIKKLQQEKELLEKEIER--LKETIIKNNSEIKDLTNQDSVKELIIKN 458
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
406-631 |
4.76e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 39.32 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 406 AIERLEATIAKLQSELNQARKNDQEMKNQISLLtnlersaKNDVNQLKKENDMLQTKVNSMVSGKQKDKQSMQSMEKKLK 485
Cdd:pfam06008 13 APYKINYNLENLTKQLQEYLSPENAHKIQIEIL-------EKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 486 SEADSRVNVEKQLHeekrrrkeeeetakhaaaqaqnnrekekaEALKQAKHDLENEILKLEGQLKAKQEECDVMKKEISE 565
Cdd:pfam06008 86 ELAEAIKNLIDNIK-----------------------------EINEKVATLGENDFALPSSDLSRMLAEAQRMLGEIRS 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118344134 566 FQLQ------EKSAKESETLMSALQAMQDKNLMLENSLSAETRLKLDLFSA-LGDVKRQLELAhgAIYKRDAE 631
Cdd:pfam06008 137 RDFGtqlqnaEAELKAAQDLLSRIQTWFQSPQEENKALANALRDSLAEYEAkLSDLRELLREA--AAKTRDAN 207
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
432-551 |
5.58e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 39.71 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 432 KNQISLLTNLErSAKNDVNQLKKENDMLQTKVNSMVSGKQKDKQSMQSMEKKLkseADSRVNVEKqlheekrrrkeeeeT 511
Cdd:TIGR04320 254 NSLAALQAKLA-TAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKEL---ANAQAQALQ--------------T 315
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 118344134 512 AKHAAAQAQNNREKEKAEaLKQAKHDLENEILKLEGQLKA 551
Cdd:TIGR04320 316 AQNNLATAQAALANAEAR-LAKAKEALANLNADLAKKQAA 354
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
457-642 |
5.82e-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: 40.21 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 457 DMLQTKVNSMVSGKQKDKQSMQSMEKKLKSEADSRVNVEKQLHEEKRRRKEEEETAKHAAAQAQNNREK----------- 525
Cdd:pfam12128 586 DLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDlrrlfdekqse 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 526 --EKAEALKQAKHDLENEILKLEGQLKAKQEECDVMKKEISEfQLQEKSAKESETLMSALQAMQDK-NLMLENSLSAETR 602
Cdd:pfam12128 666 kdKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKE-QKREARTEKQAYWQVVEGALDAQlALLKAAIAARRSG 744
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 118344134 603 LKLDLFSALGDVKRQLElAHGA----IYKRDAEIVDLKSRLADI 642
Cdd:pfam12128 745 AKAELKALETWYKRDLA-SLGVdpdvIAKLKREIRTLERKIERI 787
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
408-599 |
6.16e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 408 ERLEAT---IAKLQSELNQARKNDQEMKNQ-------ISLLTNLERSAKNDVNQLKKENDMLQTKVNSMVSGKQKDKQSM 477
Cdd:COG4942 27 AELEQLqqeIAELEKELAALKKEEKALLKQlaalerrIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 478 QSMEKKL-KSEADSRVNVekQLHEEKRRRKEEEETAKHAAAQAQNNRE---KEKAEALKQAKHDLENEILKLEGQLKAKQ 553
Cdd:COG4942 107 AELLRALyRLGRQPPLAL--LLSPEDFLDAVRRLQYLKYLAPARREQAeelRADLAELAALRAELEAERAELEALLAELE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 118344134 554 EECDVMKKEISEFQ-LQEKSAKESETLMSALQAMQDKNLMLENSLSA 599
Cdd:COG4942 185 EERAALEALKAERQkLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
449-631 |
6.42e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 39.52 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 449 VNQLKKENDMLQTKVNSM----VSGKQKDKQSMQS----MEKKLKSEADSRVNVEKQLHeekrrrkeeeeTAKHAAAQAQ 520
Cdd:pfam00038 20 VRFLEQQNKLLETKISELrqkkGAEPSRLYSLYEKeiedLRRQLDTLTVERARLQLELD-----------NLRLAAEDFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 521 NNREKE-----KAEA-LKQAKHDLENEIL---KLEGQLKAKQEECDVMKK----EISEFQLQEKSakesetlmsalqamQ 587
Cdd:pfam00038 89 QKYEDElnlrtSAENdLVGLRKDLDEATLarvDLEAKIESLKEELAFLKKnheeEVRELQAQVSD--------------T 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 118344134 588 DKNLMLENSLsaetrlKLDLFSALGDVKRQLElAHGAIYKRDAE 631
Cdd:pfam00038 155 QVNVEMDAAR------KLDLTSALAEIRAQYE-EIAAKNREEAE 191
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
409-564 |
6.80e-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: 39.77 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 409 RLEATIAKLQSELNQARKNdQEMKN--------QISLLTN---LERSA----KNDVNQLKKENDMLQTKVNSMVSG-KQK 472
Cdd:pfam01576 886 RLEARIAQLEEELEEEQSN-TELLNdrlrkstlQVEQLTTelaAERSTsqksESARQQLERQNKELKAKLQEMEGTvKSK 964
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 473 DKQSMQSMEKK-------LKSEADSRVNVEKQLHEEKRRRKEEEETAKHAAAQAQNNREK-EKAEA-LKQAKHDL---EN 540
Cdd:pfam01576 965 FKSSIAALEAKiaqleeqLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQaEKGNSrMKQLKRQLeeaEE 1044
|
170 180 190
....*....|....*....|....*....|.
gi 118344134 541 EIL-------KLEGQLKAKQEECDVMKKEIS 564
Cdd:pfam01576 1045 EASranaarrKLQRELDDATESNESMNREVS 1075
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
406-548 |
7.87e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 406 AIERLEATIAKLQSELNQARKNDQEMKNQISLLTNLERSAKND-VNQLKKENDMLQTKVNSMVSGKQKDKQSMQSMEKKL 484
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPL 375
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118344134 485 KSEADSRVNVEKQLHEEKRRRkeeeeTAKHAAAQAQNNREKEKAEALKQAKHDLENEILKLEGQ 548
Cdd:COG4913 376 PASAEEFAALRAEAAALLEAL-----EEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
374-619 |
8.91e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 374 LGVKEVIPLPLTNGHVIPEKTENKIELISTPSAIERLE--ATIAKLQSELNQARKNDQEMKNQISLLTNLERSAKNDVNQ 451
Cdd:COG4717 283 LGLLALLFLLLAREKASLGKEAEELQALPALEELEEEEleELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 452 LKKENdmLQTKVNSMVsgKQKDKQSMQSMEKKLKsEADSRVNVEKQLheekrrrkeeeetaKHAAAQAQNNREKEKAEAL 531
Cdd:COG4717 363 LQLEE--LEQEIAALL--AEAGVEDEEELRAALE-QAEEYQELKEEL--------------EELEEQLEELLGELEELLE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 532 KQAKHDLENEILKLEGQLKAKQEECDVMKKEISEFQLQEKSAKESETLMSALQAMQDKNLMLENSLSAETRLKLdLFSAL 611
Cdd:COG4717 424 ALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKL-ALELL 502
|
....*...
gi 118344134 612 GDVKRQLE 619
Cdd:COG4717 503 EEAREEYR 510
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
409-570 |
9.15e-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: 39.39 E-value: 9.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 409 RLEATIAKLQSELNQARKNDQEMKNQISLLTNLERSAKNDVNQLKKENDMLQTKVNSMVSGKQKDKQSMQ-------SME 481
Cdd:pfam01576 409 KLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQeetrqklNLS 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 482 KKLKSEADSRVNVEKQLHEEKRRRKEEEETAKHAAAQAQNNREK-----EKAEALKQAKHDLENEILKLEGQLKAKQEEC 556
Cdd:pfam01576 489 TRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKleedaGTLEALEEGKKRLQRELEALTQQLEEKAAAY 568
|
170
....*....|....
gi 118344134 557 DVMKKEISEFQlQE 570
Cdd:pfam01576 569 DKLEKTKNRLQ-QE 581
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
395-574 |
9.58e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 38.74 E-value: 9.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 395 ENKIELISTpsAIERLEATIAKLQSELNQAR-----KNDQ--EMKNQISLLTNLERSAKNDVNQLKKENDMLQTKVN--- 464
Cdd:COG1340 14 EEKIEELRE--EIEELKEKRDELNEELKELAekrdeLNAQvkELREEAQELREKRDELNEKVKELKEERDELNEKLNelr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 465 -------SMVSGKQKDKQSMQSMEKKLKSE------ADSRVNVEKQLHEEKRRRKEEEETAKHAAAQAQNNRE------- 524
Cdd:COG1340 92 eeldelrKELAELNKAGGSIDKLRKEIERLewrqqtEVLSPEEEKELVEKIKELEKELEKAKKALEKNEKLKElraelke 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 118344134 525 -KEKAEALKQAKHDLENEILKLEGQLKAKQEECDVMKKEISEF--QLQEKSAK 574
Cdd:COG1340 172 lRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELhkEIVEAQEK 224
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
470-639 |
9.86e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 38.59 E-value: 9.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 470 KQKDKQSMQSMEKKLKSEADSRVNVEKQLHEEKrrrkeeeeTAKHAAAQAQNNREKEKAEALKQAKHDLENEILKLEGQL 549
Cdd:pfam09787 13 KQKAARILQSKEKLIASLKEGSGVEGLDSSTAL--------TLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344134 550 kakQEECDVMKKEISEFQLQ---EKSAKESetlmsalqamqdknlmLENSLSaetRLKLDLFSALGDVKRQLELAHGAIY 626
Cdd:pfam09787 85 ---QEEAESSREQLQELEEQlatERSARRE----------------AEAELE---RLQEELRYLEEELRRSKATLQSRIK 142
|
170
....*....|...
gi 118344134 627 KRDAEIVDLKSRL 639
Cdd:pfam09787 143 DREAEIEKLRNQL 155
|
|
| |
