|
Name |
Accession |
Description |
Interval |
E-value |
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
2-836 |
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: 630.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 2 KRRNADCGKLRRPIKRNKITEGMYGSTtVLYMKFLILWAIVMVADFMFMFRFEFLWPFWLLLRSVHDSFKYKGLAFSVLF 81
Cdd:pfam09726 1 KRRNADCSKLRRPLKRNRITEGIYGST-FLYLKFLVVWALVLLADFVLEFRFEYLWPFWLLIRSVYDSFKYQGLAFSVFF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 82 VCIAITSDLVCLFFIPVHWLLFAASTYVWVQYVWHTDKGICLPTIILWMLFVYLEVGIRWKDSRHMpHLDLCRPFAAHCI 161
Cdd:pfam09726 80 VCIAFTSDIICLLFIPVQWLFFAASTYVWVQYVWHTEKGICLPTVSLWILFVYIEAAIRFKDLKNF-HVDLCRPFAAHCI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 162 GYPVVTLGFGFKSYVGYRMRQRKQREVAKDNEFYMQLLQQALPAEEAAEEAAAgqaatsstvvvangsattpalvaSSGA 241
Cdd:pfam09726 159 GYPVVTLGFGFKSYVSYKMRLRKQREVQKENEFYMQLLQQALPKEQQMLDRQE-----------------------RETS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 242 TAANGVLATATQAQNHhehhhsggagassssssnsnhhhhhhhnnssgnsgsnhnsnsssggakdnstsesasgaaassi 321
Cdd:pfam09726 216 ETAKGLSEVDPLALNQ---------------------------------------------------------------- 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 322 tassatgaalaaaasassasttsgsssssastgkqssssaasaattatsNGHAGGSRNHRRSMDKDKHRNKGDAADNEHN 401
Cdd:pfam09726 232 -------------------------------------------------NGHSLNKKDSTLQLPELEYREKKNSGTSSGS 262
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 402 NGTRHGGKNSGNNQVDSAATATATVTATSSNSKDKDKEKSDWDSSTsypqqqqQGGKEKHEKKAGNAVPNGNANHledet 481
Cdd:pfam09726 263 DSKKSHNHNIHNLNHVDSKLQEKEYMENHSNSKRLNISTSPGSEED-------LLVRESVSSKSSSSSSSSNKNY----- 330
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 482 asveptppvEKATKGRRNRGkkdNAAKDNHSHQQQLAQQQKEKDKENTANNNNNDASSVSSSASSTssnaiaNLASKVVS 561
Cdd:pfam09726 331 ---------KNASGGSANSS---NSSPRSHSHNSGSVTSSSSSKNSKKQKGPGGKSGARHKDPAEN------CIPNNQLS 392
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 562 KICETClKLEADVKKYRAEISHMKQIENELRQKLDANLTS----KSTLQAKQKECDDLEKRIQELNNARHADMLNLQTVE 637
Cdd:pfam09726 393 KPDALV-RLEQDIKKLKAELQASRQTEQELRSQISSLTSLerslKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLE 471
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 638 RRLNEERRQKQSLDSQLSNEKKARKLAEEKAARP---------ECSSQCKQRRQQMDEEQKRLRSDLKQAEEakqlaveh 708
Cdd:pfam09726 472 KRLKAEQEARASAEKQLAEEKKRKKEEEATAARAvalaaasrgECTESLKQRKRELESEIKKLTHDIKLKEE-------- 543
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 709 grkveqEYRMLEAK---LRNRESSQPDPEILLNALAAMQDKNATLEKNLSAETRVKLDLFSALGAAKRQIEISDNHRRSK 785
Cdd:pfam09726 544 ------QIRELEIKvqeLRKYKESEKDTEVLMSALSAMQDKNQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQIYQK 617
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 442624373 786 EDEVIDLKAKIAQLLAVMPD-NLCMNTGPHGPSSSIlrmnDTPPLQSGPGPS 836
Cdd:pfam09726 618 DQEIKDLKQKIAEVMAVMPStSRITPVTPHYSSKFM----DTSPSMRDPNAS 665
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
568-801 |
2.20e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 568 LKLEADV-KKYRAeishmkqIENELRQkLDANLTSKStLQAKQKECDDLEKRIQELNNARHADMLNLQTVERRLNEERRQ 646
Cdd:COG1196 205 LERQAEKaERYRE-------LKEELKE-LEAELLLLK-LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 647 KQSLDSQLS------NEKKARKLAEEKAARPEC--SSQCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEYRM 718
Cdd:COG1196 276 LEELELELEeaqaeeYELLAELARLEQDIARLEerRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 719 LEAKLRNRESSQPDpeiLLNALAAMQDKNATLEKNLSAETRVKLDLFSALGAAKRQIEISDNHRRSKEDEVIDLKAKIAQ 798
Cdd:COG1196 356 AEAELAEAEEALLE---AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
...
gi 442624373 799 LLA 801
Cdd:COG1196 433 LEE 435
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
569-801 |
2.88e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 60.30 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 569 KLEADVKKYRAEISHMKQIENELRQKLDANL-TSKSTLQAKQKECDDLEKRIQELNNarhadmlNLQTVERRLNEERRQK 647
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLrKALFELDKLQEELEQLREELEQARE-------ELEQLEEELEQARSEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 648 QSLDSQLsnEKKARKLAEEKAARpecsSQCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEYRMLEAKLRNRE 727
Cdd:COG4372 76 EQLEEEL--EELNEQLQAAQAEL----AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAERE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442624373 728 SSQpdpEILLNALAAMQDKNATLEKNLSAETRVKLD--LFSALGAAKRQIEISDNHRRSKEDEVIDLKAKIAQLLA 801
Cdd:COG4372 150 EEL---KELEEQLESLQEELAALEQELQALSEAEAEqaLDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLE 222
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
570-807 |
1.71e-08 |
|
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: 58.93 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 570 LEADVKKYRAEIshmKQIENELRQKLDAnltskstLQAKQKECDDLEKRIQELNNARHADMLNLQTVERRLNEERRQK-- 647
Cdd:TIGR02169 728 LEQEEEKLKERL---EELEEDLSSLEQE-------IENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEiq 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 648 -----------------QSLDSQLSNEKKARKLAEEKAA-----RPECSSQCKQRRQQMDEEQKRLRsDLKQAEEAKQLA 705
Cdd:TIGR02169 798 aelskleeevsriearlREIEQKLNRLTLEKEYLEKEIQelqeqRIDLKEQIKSIEKEIENLNGKKE-ELEEELEELEAA 876
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 706 VehgRKVEQEYRMLEAKLRNRESSQPDPEILLNALAAMQDKNATLEKNLSAETRVKLDLFSALGAAKRQIEISDNHRRSK 785
Cdd:TIGR02169 877 L---RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL 953
|
250 260
....*....|....*....|..
gi 442624373 786 EDEVIDLKAKIAQLLAVMPDNL 807
Cdd:TIGR02169 954 EDVQAELQRVEEEIRALEPVNM 975
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
569-797 |
2.78e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 57.22 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 569 KLEADVKKYRAEIshmKQIENELRQkldanltSKSTLQAKQKECDDLEKRIQELNNARHADMLNLQTVERRLNEERRQKQ 648
Cdd:COG4372 42 KLQEELEQLREEL---EQAREELEQ-------LEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 649 SLDSQLSN--------EKKARKLAEEKAARPECSSQCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEhgRKVEQEYRMLE 720
Cdd:COG4372 112 ELQEELEElqkerqdlEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE--AEAEQALDELL 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442624373 721 AKLRNRESSQPDPEILLNALAAMQDKNATLEKNLSAETRVKLDLFSALGAAKRQIEISDNHRRSKEDEVIDLKAKIA 797
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
576-801 |
4.65e-08 |
|
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: 57.39 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 576 KYRAEISHMKQIE-NELRQKLDANLTSKSTLQakqKECDDLEKRIQELNNARHADMLNLQTVERRLNEERRQKQSLDSQL 654
Cdd:TIGR02169 212 RYQALLKEKREYEgYELLKEKEALERQKEAIE---RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEE 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 655 SNEKKaRKLAEEKAARPECSSQ---CKQRRQQMDEEQKRLRSDL-KQAEEAKQLAvehgRKVEqEYRMLEAKLRNR-ESS 729
Cdd:TIGR02169 289 QLRVK-EKIGELEAEIASLERSiaeKERELEDAEERLAKLEAEIdKLLAEIEELE----REIE-EERKRRDKLTEEyAEL 362
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442624373 730 QPDPEILLNALAAMQDKNATLEKNLSAETRVKLDLFSALGAAKRQIEISDNHRRSKEDEVIDLKAKIAQLLA 801
Cdd:TIGR02169 363 KEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA 434
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
572-799 |
6.50e-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: 56.99 E-value: 6.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 572 ADVKKYRAEISHMKQIENELRQKLDAnltSKSTLQAKQKECDDLEKRIQELN---NARHADMLNLQ----TVERRLNEER 644
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEE---LTAELQELEEKLEELRLEVSELEeeiEELQKELYALAneisRLEQQKQILR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 645 RQKQSLDSQLS--------NEKKARKLAEEKAARPECSSQCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEY 716
Cdd:TIGR02168 309 ERLANLERQLEeleaqleeLESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 717 RMLE---AKLRNRESSQpdpEILLNALAAMQDKN----------------ATLEKNLSAETRVKLDLFSALGAAKRQIEI 777
Cdd:TIGR02168 389 AQLElqiASLNNEIERL---EARLERLEDRRERLqqeieellkkleeaelKELQAELEELEEELEELQEELERLEEALEE 465
|
250 260
....*....|....*....|..
gi 442624373 778 SDNHRRSKEDEVIDLKAKIAQL 799
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAQL 487
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
570-757 |
8.90e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 8.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 570 LEADVKKYRAEISHMKQIENELRQKLDANLTSKSTLQAKQKEcddLEKRIQELNNARHADMLNLQTVERRLNEERRQKQS 649
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE---AEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 650 LDSQLSNEKKARKLAEEKAARpecssqCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEYRMLEAKLRNRESS 729
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEA------LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
170 180
....*....|....*....|....*....
gi 442624373 730 QPDP-EILLNALAAMQDKNATLEKNLSAE 757
Cdd:COG1196 465 LAELlEEAALLEAALAELLEELAEAAARL 493
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
569-770 |
2.60e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 569 KLEADVKKY-----RAEISHMKQIEnELRQKLDANLTSKSTLQAKQKECDDLEKRIQELNNA---------RHADMLNLQ 634
Cdd:COG4717 50 RLEKEADELfkpqgRKPELNLKELK-ELEEELKEAEEKEEEYAELQEELEELEEELEELEAEleelreeleKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 635 TVERRLNEERRQKQSLDSQLSN-EKKARKLAEEKAARPECSSQCKQRRQQMDEEQKRLrsDLKQAEEAKQLAVEHgRKVE 713
Cdd:COG4717 129 PLYQELEALEAELAELPERLEElEERLEELRELEEELEELEAELAELQEELEELLEQL--SLATEEELQDLAEEL-EELQ 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 442624373 714 QEYRMLEAKLrnrESSQPDPEILLNALAAMQDKNATLEKNLS-AETRVKLDLFSALGA 770
Cdd:COG4717 206 QRLAELEEEL---EEAQEELEELEEELEQLENELEAAALEERlKEARLLLLIAAALLA 260
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
562-774 |
4.50e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 4.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 562 KICETCLKLEADVKKYRAEISHMKQIENELR---QKLDANLTSKSTLQAKQKE-----CDDLEKRIQELNNArHADMLNL 633
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAeleKKLDELEEELAELLKELEElgfesVEELEERLKELEPF-YNEYLEL 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 634 QTVERRLNEERRQKQSLDSQLsnEKKARKLAEEKAARPECSSQCKQRRQQMDEEQKR--------LRSDLKQAEEAKQLA 705
Cdd:PRK03918 608 KDAEKELEREEKELKKLEEEL--DKAFEELAETEKRLEELRKELEELEKKYSEEEYEelreeyleLSRELAGLRAELEEL 685
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442624373 706 VEHGRKVEQEYRMLEAKLRNRESSQPDPEILLNALAAMQD--------KNATLEKNLSAETRVKLDLFSALGAAKRQ 774
Cdd:PRK03918 686 EKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEElrekvkkyKALLKERALSKVGEIASEIFEELTEGKYS 762
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
616-803 |
6.81e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 6.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 616 EKRIQELNNARHADMlNLQTVERRLNEERRQKQSLDSQLSNEKKARKL-AEEKAARPECSsqcKQRRQQMDEEQKRLRSD 694
Cdd:TIGR02168 172 ERRKETERKLERTRE-NLDRLEDILNELERQLKSLERQAEKAERYKELkAELRELELALL---VLRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 695 LKQAEEAKQLAVEHGRKVEQEYRMLEAKLRNRESSQPDPEILLNALAAMQdknATLEKNLsAETRVKLD-LFSALGAAKR 773
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI---SRLEQQK-QILRERLAnLERQLEELEA 323
|
170 180 190
....*....|....*....|....*....|
gi 442624373 774 QIEISDNHRRSKEDEVIDLKAKIAQLLAVM 803
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEEL 353
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
580-786 |
7.65e-07 |
|
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: 53.20 E-value: 7.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 580 EISHMKQIEnelrqkldanltsKSTLQAKQKEcddlEKRIQELNNARHADMLNlQTVERRLNEERRQKQSLDSQLSN--E 657
Cdd:pfam17380 373 EISRMRELE-------------RLQMERQQKN----ERVRQELEAARKVKILE-EERQRKIQQQKVEMEQIRAEQEEarQ 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 658 KKARKLAEEKAARPECSSQCKQRRQ-------QMDEEQKRLRSDLKQAEEAKQLAVEHGRKV-EQEYR-----MLEAKlR 724
Cdd:pfam17380 435 REVRRLEEERAREMERVRLEEQERQqqverlrQQEEERKRKKLELEKEKRDRKRAEEQRRKIlEKELEerkqaMIEEE-R 513
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442624373 725 NRESSQPDPEILLNALAAMQDKNATLEKN-----------------LSAETRVKLDLFSALGAAKRQIEISDNHRRSKE 786
Cdd:pfam17380 514 KRKLLEKEMEERQKAIYEEERRREAEEERrkqqemeerrriqeqmrKATEERSRLEAMEREREMMRQIVESEKARAEYE 592
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
571-799 |
8.78e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 8.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 571 EADVKKYRAEiSHMKQIENELRQKLDANLTSKSTLQAKQKECDDLEKRIQELNNARHADMLNLQTVERRLNEERRQKQSL 650
Cdd:TIGR02168 772 EAEEELAEAE-AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 651 DSQLsnEKKARKLAEEKAARPECSSQckqrRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEYRMLEAKLRNRESSQ 730
Cdd:TIGR02168 851 SEDI--ESLAAEIEELEELIEELESE----LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442624373 731 PDpeiLLNALAAMQDKNATLEKNLSAETRVKLDLFSALGAAKrqieisDNHRRSKEDEVIDLKAKIAQL 799
Cdd:TIGR02168 925 AQ---LELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKI------EDDEEEARRRLKRLENKIKEL 984
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
569-687 |
2.78e-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: 49.54 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 569 KLEADVKKYRAEISHMKQIENELRQKLDANLTSKStLQAKQKECDDLEKRIQELNNARHADMLNLQTVERRLNEERRQKQ 648
Cdd:COG1579 56 DLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE-YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELA 134
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 442624373 649 SLDSQLSNEKKAR--KLAEEKAARPECSSQCKQRRQQMDEE 687
Cdd:COG1579 135 ELEAELEEKKAELdeELAELEAELEELEAEREELAAKIPPE 175
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
568-727 |
6.47e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 6.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 568 LKLEADVKKYRAEISHMKQIENELRQKLDANltskstlqaKQKECDDLEKRIQELNNARHADML----NLQTVERRLNEE 643
Cdd:COG4717 330 LPPDLSPEELLELLDRIEELQELLREAEELE---------EELQLEELEQEIAALLAEAGVEDEeelrAALEQAEEYQEL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 644 RRQKQSLDSQLSNEKKARKLAEEKAARPECSSQ----------CKQRRQQMDEEQKRLRSDLKQAEEAKQLAvehgrKVE 713
Cdd:COG4717 401 KEELEELEEQLEELLGELEELLEALDEEELEEEleeleeeleeLEEELEELREELAELEAELEQLEEDGELA-----ELL 475
|
170
....*....|....
gi 442624373 714 QEYRMLEAKLRNRE 727
Cdd:COG4717 476 QELEELKAELRELA 489
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
605-799 |
6.99e-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: 6.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 605 LQAKQKECDDLEKRIQELNNARHAdmlnLQTVERRLNEERRQKQSLDSQLSNEKKARKLAEEKAARpecssqcKQRRQQM 684
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEA----LEAELDALQERREALQRLAEYSWDEIDVASAEREIAEL-------EAELERL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 685 DEEQ---KRLRSDLKQAEEAKQLAVEHGRKVEQEYRMLEAKLRNRESSQPDPEILLNALAAMqdknATLEKNLSAETRvk 761
Cdd:COG4913 681 DASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL----ARLELRALLEER-- 754
|
170 180 190
....*....|....*....|....*....|....*...
gi 442624373 762 ldlFSALGAAKRQIEIsdnhRRSKEDEVIDLKAKIAQL 799
Cdd:COG4913 755 ---FAAALGDAVEREL----RENLEERIDALRARLNRA 785
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
569-800 |
1.15e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 569 KLEADVKKYRAEISHMKQIENELRQKLDANLTSKST------LQAKQKECDDLEKRIQELNnarhADMLNLQTVERRLNE 642
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERREALQRLAEYswdeidVASAEREIAELEAELERLD----ASSDDLAALEEQLEE 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 643 ERRQKQSLDSQLsnekkarklaeekaarpecsSQCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEYrmLEAK 722
Cdd:COG4913 697 LEAELEELEEEL--------------------DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL--LEER 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 723 LRNressQPDPEILLNALAAMQDKNATLEKNLSAETRvklDLFSALGAAKRQ---------IEISDN------HRRSKED 787
Cdd:COG4913 755 FAA----ALGDAVERELRENLEERIDALRARLNRAEE---ELERAMRAFNREwpaetadldADLESLpeylalLDRLEED 827
|
250
....*....|...
gi 442624373 788 EVIDLKAKIAQLL 800
Cdd:COG4913 828 GLPEYEERFKELL 840
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
613-724 |
1.19e-05 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 46.20 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 613 DDLEKRIQELNNARHADMLNLQT------VERRLNEERRQ-KQSLDSQLSNEKKARklAEEKAARPEcssQCKQRRQQMD 685
Cdd:pfam15346 10 EETARRVEEAVAKRVEEELEKRKdeieaeVERRVEEARKImEKQVLEELEREREAE--LEEERRKEE---EERKKREELE 84
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 442624373 686 EEqkrLRSDLKQAEEA-KQLAVEHGRKVEQEYRMLEAKLR 724
Cdd:pfam15346 85 RI---LEENNRKIEEAqRKEAEERLAMLEEQRRMKEERQR 121
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
602-805 |
1.26e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 602 KSTLQAK---------QKECDDLEK---RIQELNNAR----HADMLNLQTVERRLNEERRQKQSLDSQLSNEKKARKLAE 665
Cdd:COG4717 36 KSTLLAFiramllerlEKEADELFKpqgRKPELNLKElkelEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 666 EKAARPECSSQC-------KQRRQQMDEEQKRLRSDLKQAEEAKQLavehgrkvEQEYRMLEAKlrnressqpdpeilln 738
Cdd:COG4717 116 EELEKLEKLLQLlplyqelEALEAELAELPERLEELEERLEELREL--------EEELEELEAE---------------- 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442624373 739 aLAAMQDKNATLEKNLSAETRVKL-DLFSALGAAKRQIEISDNHRRSKEDEVIDLKAKIAQLLAVMPD 805
Cdd:COG4717 172 -LAELQEELEELLEQLSLATEEELqDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
568-803 |
1.27e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 568 LKLEADVKKYRAEISHMKQIENELRQKLDANLTSKSTLQAKQKECDDLEKriQELNNARHADMLN----LQTVERRLNEE 643
Cdd:PRK03918 401 EEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHR--KELLEEYTAELKRiekeLKEIEEKERKL 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 644 RRQKQSLDSQLSNEKKARKLaeekaarpecssqckqrrQQMDEEQKRLRSDLKQ--AEEAKQLAVEHgRKVEQEYRMLEA 721
Cdd:PRK03918 479 RKELRELEKVLKKESELIKL------------------KELAEQLKELEEKLKKynLEELEKKAEEY-EKLKEKLIKLKG 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 722 KLRNRESSQPDPEILLNALAAMQDKNATLEKNLSA----------------ETRVK-----LDLFSALGAAKRQIEISDN 780
Cdd:PRK03918 540 EIKSLKKELEKLEELKKKLAELEKKLDELEEELAEllkeleelgfesveelEERLKelepfYNEYLELKDAEKELEREEK 619
|
250 260
....*....|....*....|...
gi 442624373 781 HRRSKEDEVIDLKAKIAQLLAVM 803
Cdd:PRK03918 620 ELKKLEEELDKAFEELAETEKRL 642
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
572-732 |
1.34e-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: 49.30 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 572 ADVKKYRAEISHMKQIENELRQKLDANLTSKSTLQAKQKecdDLEKRIQELNNARHadmlNLQTVERRLNEERRQKQSLD 651
Cdd:TIGR02169 350 KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK---DYREKLEKLKREIN----ELKRELDRLQEELQRLSEEL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 652 SQLSNE---KKARKLA-----EEKAARPECSSQ-CKQRRQQMDEEQKRLRSDlkqaeEAKQLAVEHG-RKVEQEYRMLEA 721
Cdd:TIGR02169 423 ADLNAAiagIEAKINEleeekEDKALEIKKQEWkLEQLAADLSKYEQELYDL-----KEEYDRVEKElSKLQRELAEAEA 497
|
170
....*....|.
gi 442624373 722 KLRNRESSQPD 732
Cdd:TIGR02169 498 QARASEERVRG 508
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
578-783 |
1.67e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.07 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 578 RAEISHMKQIENELRQKLDAnltSKSTLQAKQKECDDLEKRI----QELNNARHADMLNLQTVERrlNEERRQkqsldsQ 653
Cdd:pfam12128 589 RIDVPEWAASEEELRERLDK---AEEALQSAREKQAAAEEQLvqanGELEKASREETFARTALKN--ARLDLR------R 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 654 LSNEKKARKLAEEKAaRPECSSQCKQRRQQMDEEQKRLRSDLKQA-EEAKQLAVEHGRKVEQEYRMLEAKLRNRESSqpd 732
Cdd:pfam12128 658 LFDEKQSEKDKKNKA-LAERKDSANERLNSLEAQLKQLDKKHQAWlEEQKEQKREARTEKQAYWQVVEGALDAQLAL--- 733
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 442624373 733 peiLLNALAAMQDKNATLEKNLsaETRVKLDLfSALGA-----AKRQIEISDNHRR 783
Cdd:pfam12128 734 ---LKAAIAARRSGAKAELKAL--ETWYKRDL-ASLGVdpdviAKLKREIRTLERK 783
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
569-721 |
2.94e-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: 48.13 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 569 KLEADVKKYRAEISHMKQIENELRQKLDANLTSKSTLQA-----------KQKECDDLEKRIQELNNARHADMLNLQTVE 637
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEalallrseleeLSEELRELESKRSELRRELEELREKLAQLE 928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 638 RRLNEERRQKQSLDSQLSNEkkARKLAEEKAARPEcssQCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEYR 717
Cdd:TIGR02168 929 LRLEGLEVRIDNLQERLSEE--YSLTLEEAEALEN---KIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYD 1003
|
....
gi 442624373 718 MLEA 721
Cdd:TIGR02168 1004 FLTA 1007
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
569-780 |
3.77e-05 |
|
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: 47.86 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 569 KLEADVKKYRAEISHMKQIENELR---QKLDANLTSKST-LQAKQKECDDLEKRIQELNNarhadmlNLQTVERRLNEER 644
Cdd:pfam01576 409 KLEGQLQELQARLSESERQRAELAeklSKLQSELESVSSlLNEAEGKNIKLSKDVSSLES-------QLQDTQELLQEET 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 645 RQKQSLDSQLsnekkaRKLAEEKAARpecssqckqrRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEYRMLEAKLR 724
Cdd:pfam01576 482 RQKLNLSTRL------RQLEDERNSL----------QEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEE 545
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 442624373 725 NRESSQPDPEillNALAAMQDKNATLEKNLSAETRVKLDLFSALGAAKRQIEISDN 780
Cdd:pfam01576 546 GKKRLQRELE---ALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSN 598
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
581-730 |
4.55e-05 |
|
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: 47.43 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 581 ISHMKQIENELRQKLDANLTSKSTLQAKQKECDDLEKR--IQELNNARHADMLNLQTV---ERRLNEERRQKQSLDSQLS 655
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRrkLEEAEKARQAEMDRQAAIyaeQERMAMERERELERIRQEE 357
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442624373 656 NEKKARKLAEEKAARpECSSQCKQRRQQMDEEQK--RLRSDLKQAEEAKQLAVEHGRKVEQEYRMLEAKLRNRESSQ 730
Cdd:pfam17380 358 RKRELERIRQEEIAM-EISRMRELERLQMERQQKneRVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEAR 433
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
637-724 |
4.83e-05 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 44.65 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 637 ERRLNEERRQKQSLDSQLSNEKKARKLAEEKAARPECSSQCKQRRQQMDEEQKRLRSdlKQAEEAKQLAVEHGRKVEQEY 716
Cdd:pfam05672 26 QREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAE--EEAEEREQREQEEQERLQKQK 103
|
....*...
gi 442624373 717 RMLEAKLR 724
Cdd:pfam05672 104 EEAEAKAR 111
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
580-799 |
4.96e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 580 EISHMKQIENELRQKLDANLTSKSTLQAKQKECDDLEKRIQELNNARHADMLNLQTVERRLNEERRQKQSLDSQLSNEKK 659
Cdd:PRK03918 208 EINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 660 ARKLAEEKAARPECSSQCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEYRMLEAKLRNRESSQPDPEILLNA 739
Cdd:PRK03918 288 LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEA 367
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 740 LAAMQDKNaTLEKNLSAETRVKLdlfsalgaaKRQIEISDNHRRSKEDEVIDLKAKIAQL 799
Cdd:PRK03918 368 KAKKEELE-RLKKRLTGLTPEKL---------EKELEELEKAKEEIEEEISKITARIGEL 417
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
575-727 |
6.54e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.96 E-value: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 575 KKYRAEISHMKQIENELRQKLDANLTSK----STLQAKQKECDDLEKRIQElnnarhadmlNLQTVERRLNEERRQKQSL 650
Cdd:TIGR00606 948 EKVKNIHGYMKDIENKIQDGKDDYLKQKetelNTVNAQLEECEKHQEKINE----------DMRLMRQDIDTQKIQERWL 1017
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442624373 651 DSQLSNEKKARKLAEEKAARPECSSQCKQRR-QQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEYRMLEAKLRNRE 727
Cdd:TIGR00606 1018 QDNLTLRKRENELKEVEEELKQHLKEMGQMQvLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
552-744 |
7.10e-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: 7.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 552 IANLASKVVSKICE-TCLKLEAD-VKKYRAEISHMK-------QIENELRQKLDaNLTS-----KSTLQAKQKECDDLEK 617
Cdd:pfam15921 519 ITKLRSRVDLKLQElQHLKNEGDhLRNVQTECEALKlqmaekdKVIEILRQQIE-NMTQlvgqhGRTAGAMQVEKAQLEK 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 618 RIqelnNARHADMLNLQTVERRLNEERRQKQSLDSQLSNEKKarKLAEEKAARPECSSQCKQRRQQMDEEQKRLRSDLKQ 697
Cdd:pfam15921 598 EI----NDRRLELQEFKILKDKKDAKIRELEARVSDLELEKV--KLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNS 671
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 442624373 698 AEEAKQLAVEHGRKVEQEYRMLEAKLRNR-ESSQPDPEILLNALAAMQ 744
Cdd:pfam15921 672 LSEDYEVLKRNFRNKSEEMETTTNKLKMQlKSAQSELEQTRNTLKSME 719
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
561-726 |
8.15e-05 |
|
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: 46.71 E-value: 8.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 561 SKICETCLK-LEADVKKYRAEIS----HMKQIE---NELRQKLDANLTSKSTLQAKQKEcddLEKRIQELNNARHADMLN 632
Cdd:pfam01576 828 SKESEKKLKnLEAELLQLQEDLAaserARRQAQqerDELADEIASGASGKSALQDEKRR---LEARIAQLEEELEEEQSN 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 633 LQTVERRLNEERRQKQSLDSQLSNEKKARKLAEekAARPECSSQCKQRRQQMDEEQKRLRSDLKQ---AEEAKQLAVEHG 709
Cdd:pfam01576 905 TELLNDRLRKSTLQVEQLTTELAAERSTSQKSE--SARQQLERQNKELKAKLQEMEGTVKSKFKSsiaALEAKIAQLEEQ 982
|
170
....*....|....*..
gi 442624373 710 RKVEQEYRMLEAKLRNR 726
Cdd:pfam01576 983 LEQESRERQAANKLVRR 999
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
609-715 |
9.05e-05 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 43.88 E-value: 9.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 609 QKECDDLEKRIQElnnarHADMLNLQTVERRLNEERRQKQSLDSQLSNEKKARKLAEEKAARPECssqcKQRRQQMDEEQ 688
Cdd:pfam05672 26 QREREEQERLEKE-----EEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEA----EEREQREQEEQ 96
|
90 100
....*....|....*....|....*..
gi 442624373 689 KRLRsdlKQAEEAKQLAVEHGRKVEQE 715
Cdd:pfam05672 97 ERLQ---KQKEEAEAKAREEAERQRQE 120
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
631-801 |
9.46e-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: 44.92 E-value: 9.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 631 LNLQTVERRLNEERRQKQSLDSQLSNEKKARKLAEEKAARpecssqCKQRRQQMDEEQKRLRSDLKQAEEakqlavehgR 710
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEA------AKTELEDLEKEIKRLELEIEEVEA---------R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 711 KVEQEYRMLEAKlRNRESsqpdpEILLNALAAMQDKNATLEKNLsaetrvkLDLFSALGAAKRQIEISDNHRRSKEDEVI 790
Cdd:COG1579 75 IKKYEEQLGNVR-NNKEY-----EALQKEIESLKRRISDLEDEI-------LELMERIEELEEELAELEAELAELEAELE 141
|
170
....*....|.
gi 442624373 791 DLKAKIAQLLA 801
Cdd:COG1579 142 EKKAELDEELA 152
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
574-782 |
1.27e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.20 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 574 VKKYRAEISHMKQIENELRQKLDANLTSKSTLQAKQKeCDDLEKRI---------------QELNNARH-ADMLNL---- 633
Cdd:PRK10929 67 AKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMS-TDALEQEIlqvssqlleksrqaqQEQDRAREiSDSLSQlpqq 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 634 QTVERR-LNEERRQKQSLDSQLSNEKKARKLA--EEKAARP------ECSSQCKQRRQqmdeEQKRLRSDLKQaeeakql 704
Cdd:PRK10929 146 QTEARRqLNEIERRLQTLGTPNTPLAQAQLTAlqAESAALKalvdelELAQLSANNRQ----ELARLRSELAK------- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 705 avehgRKVEQEYRMLEAkLRNRESS--QPDPEILLNALAAMQDKNATLEKNLSAETRVKLDLFSALG-AAKRQIEISDNH 781
Cdd:PRK10929 215 -----KRSQQLDAYLQA-LRNQLNSqrQREAERALESTELLAEQSGDLPKSIVAQFKINRELSQALNqQAQRMDLIASQQ 288
|
.
gi 442624373 782 R 782
Cdd:PRK10929 289 R 289
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
571-715 |
1.33e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 45.71 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 571 EADVKKYRAEISHMKQIENELRQKLDANLTSKstlQAKQKEcDDLEKRIQELNNARHADMLnlqtvERRLNEERRQKQsL 650
Cdd:pfam15709 388 EIRLRKQRLEEERQRQEEEERKQRLQLQAAQE---RARQQQ-EEFRRKLQELQRKKQQEEA-----ERAEAEKQRQKE-L 457
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442624373 651 DSQLSNE-KKARKLAEEKaaRPEcssqcKQRRQQMDEEQKRLRSDLK--QAEEAKQLAVEHGRKVEQE 715
Cdd:pfam15709 458 EMQLAEEqKRLMEMAEEE--RLE-----YQRQKQEAEEKARLEAEERrqKEEEAARLALEEAMKQAQE 518
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
637-783 |
1.63e-04 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 45.80 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 637 ERRLNeeRRQKQsldsQLSNEKKARKLAEEKAARpecSSQCKQRRQQMDEEQKRlRSDLK--QAEEAKQLAVEHGRKVEQ 714
Cdd:PRK10811 638 ENRRN--RRQAQ----QQTAETRESQQAEVTEKA---RTQDEQQQAPRRERQRR-RNDEKrqAQQEAKALNVEEQSVQET 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 715 EY-------------RMLEAKLRnRESSQPDPEILLNALAAMQDKNATLEKNLSAETRVKLDLFSALGAAKRQIEISDNH 781
Cdd:PRK10811 708 EQeervqqvqprrkqRQLNQKVR-IEQSVAEEAVAPVVEETVAAEPVVQEVPAPRTELVKVPLPVVAQTAPEQDEENNAE 786
|
..
gi 442624373 782 RR 783
Cdd:PRK10811 787 NR 788
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
569-729 |
1.76e-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: 45.14 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 569 KLEADVKKYRAEISHMKQIENELRQKLDANL--------TSKSTLQAKQKECDDLEKRIQELNNARHADMLNLQTVERRL 640
Cdd:COG4942 80 ALEAELAELEKEIAELRAELEAQKEELAELLralyrlgrQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 641 NEERRQKQSLDSQLsnEKKARKLAEEKAARPECSSQCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEYRMLE 720
Cdd:COG4942 160 AELAALRAELEAER--AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
....*....
gi 442624373 721 AKLRNRESS 729
Cdd:COG4942 238 AAAERTPAA 246
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
570-807 |
1.85e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 570 LEADVKKYRAEISHMKQIEnELRQKLDANLTSKSTLQA---------KQKECDDLEKRIQELnnarhadmlnlqtverrl 640
Cdd:COG4913 240 AHEALEDAREQIELLEPIR-ELAERYAAARERLAELEYlraalrlwfAQRRLELLEAELEEL------------------ 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 641 neeRRQKQSLDSQLSNEKKARKLAEEKAARPEcssqcKQRRQQMDEEQKRLRSDLKQAEEAKqlavehgRKVEQEYRMLE 720
Cdd:COG4913 301 ---RAELARLEAELERLEARLDALREELDELE-----AQIRGNGGDRLEQLEREIERLEREL-------EERERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 721 AKLRNRESSQP-DPEILLNALAAMQDKNATLEKNLSAETRVKLDLFSALGAAKRQI-----EISD-NHRRSK-EDEVIDL 792
Cdd:COG4913 366 ALLAALGLPLPaSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELreleaEIASlERRKSNiPARLLAL 445
|
250
....*....|....*
gi 442624373 793 KAKIAQLLAVMPDNL 807
Cdd:COG4913 446 RDALAEALGLDEAEL 460
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
588-790 |
1.91e-04 |
|
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: 45.48 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 588 ENELRQKLDANLTSKST-----LQAKQKECDDLE--------------KRIQELNN------------ARHADMLNLQTv 636
Cdd:pfam05483 423 EKKQFEKIAEELKGKEQeliflLQAREKEIHDLEiqltaiktseehylKEVEDLKTelekeklknielTAHCDKLLLEN- 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 637 eRRLNEE--------RRQKQSLDSQLSNEKKARKLAE-----EKAARPECSSQCKQRRQQMDEeqkrLRSDLKQAEEAKQ 703
Cdd:pfam05483 502 -KELTQEasdmtlelKKHQEDIINCKKQEERMLKQIEnleekEMNLRDELESVREEFIQKGDE----VKCKLDKSEENAR 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 704 LAVEHGRKVEQEYRMLEAKLRNR----ESSQPDPEILLNALAAMQDKNATLEKNLSA-ETRV-KLDLfsALGAAKRQI-E 776
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNLkkqiENKNKNIEELHQENKALKKKGSAENKQLNAyEIKVnKLEL--ELASAKQKFeE 654
|
250
....*....|....
gi 442624373 777 ISDNHRRSKEDEVI 790
Cdd:pfam05483 655 IIDNYQKEIEDKKI 668
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
585-799 |
1.98e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 585 KQIENELRQKLDANLTSKSTLQAKQKEcddlEKRIQELNNARHADMLNLQTVERRLNEERRQKQSLDSQLSNEKKA---- 660
Cdd:PTZ00121 1564 KKAEEAKKAEEDKNMALRKAEEAKKAE----EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVeqlk 1639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 661 RKLAEEKAARPECSSQCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEYRMLEAKLRNRESSQPDPEillNAL 740
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE---EKK 1716
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 741 AAMQDKNATLEKNLSAETrvkldlfsalgaAKRQIEisDNHRRSKEDEVID-LKAKIAQL 799
Cdd:PTZ00121 1717 KAEELKKAEEENKIKAEE------------AKKEAE--EDKKKAEEAKKDEeEKKKIAHL 1762
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
578-730 |
2.28e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.94 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 578 RAEISHMKQIENELRQKLDAnltSKSTLQAKQKECDDLEKRIQELNNARHADMLNL----QTVERRLNEERRQKQSLDSQ 653
Cdd:pfam15709 339 RAERAEMRRLEVERKRREQE---EQRRLQQEQLERAEKMREELELEQQRRFEEIRLrkqrLEEERQRQEEEERKQRLQLQ 415
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442624373 654 LSNEKkARKLAEEkaARPECssQCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQ-EYRMLEAKLRNRESSQ 730
Cdd:pfam15709 416 AAQER-ARQQQEE--FRRKL--QELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMaEEERLEYQRQKQEAEE 488
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
568-810 |
2.85e-04 |
|
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: 44.96 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 568 LKLEADVKKYRAEISHMKQIENELR----QKLDANLTSKSTLQAKQKECDDLEKR----IQELNNARHADMLNLQTVERR 639
Cdd:pfam02463 771 LKEKELAEEREKTEKLKVEEEKEEKlkaqEEELRALEEELKEEAELLEEEQLLIEqeekIKEEELEELALELKEEQKLEK 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 640 LNEErRQKQSLDSQLSNEKKARKLAEEKAARPECSsqcKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEYRML 719
Cdd:pfam02463 851 LAEE-ELERLEEEITKEELLQELLLKEEELEEQKL---KDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEE 926
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 720 EAKLRNRESSQPDPEILLNALAAMQDKNATLEKNLSAETRVKLDLFSALGAAKRQIEISDNHRRSKED-EVIDLKAKIAQ 798
Cdd:pfam02463 927 AEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDElEKERLEEEKKK 1006
|
250
....*....|..
gi 442624373 799 LLAVMPDNLCMN 810
Cdd:pfam02463 1007 LIRAIIEETCQR 1018
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
570-776 |
3.24e-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: 44.29 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 570 LEADVKKYRAEISHMKQIENELRQKLDANltskstlQAKQKECDDLEKRIQELNNARHADMLNLQTVERRLNEERRQKQS 649
Cdd:pfam19220 36 IEAILRELPQAKSRLLELEALLAQERAAY-------GKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 650 LDSQLSnEKKARKLAEEKAARPEcssqcKQRRQQMDEEQKRLRSDLKQAEEAKQlAVEHGRKVEQEYRMLEA----KLRN 725
Cdd:pfam19220 109 LRIELR-DKTAQAEALERQLAAE-----TEQNRALEEENKALREEAQAAEKALQ-RAEGELATARERLALLEqenrRLQA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 726 RESSQPDpEI---------LLNALAAMQDKNATLEKNLSAETrvkldlfSALGAAKRQIE 776
Cdd:pfam19220 182 LSEEQAA-ELaeltrrlaeLETQLDATRARLRALEGQLAAEQ-------AERERAEAQLE 233
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
588-801 |
4.56e-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: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 588 ENELRQKLDANLTSKSTLQAKQKECDDLEKRIQELNNARHADMLNLQT----------------------------VERR 639
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAetelcaeaeemrarlaarkqeleeilheLESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 640 LNEERRQKQsldsQLSNEKK---------ARKLAEEKAArpecssqckqrRQQMDEEQKRLRSDLKQAEEAKQLAVEHGR 710
Cdd:pfam01576 84 LEEEEERSQ----QLQNEKKkmqqhiqdlEEQLDEEEAA-----------RQKLQLEKVTTEAKIKKLEEDILLLEDQNS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 711 KVEQEYRMLEAKLRNRESSQPDPEILLNALAAMQDKN----ATLEKNLSAETRVKLDlfsaLGAAKRQI--EISDNHrrs 784
Cdd:pfam01576 149 KLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHeamiSDLEERLKKEEKGRQE----LEKAKRKLegESTDLQ--- 221
|
250
....*....|....*..
gi 442624373 785 keDEVIDLKAKIAQLLA 801
Cdd:pfam01576 222 --EQIAELQAQIAELRA 236
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
568-742 |
4.94e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 568 LKLEADVKKYRAEISHMKQIENELRQKLDANLTSKSTLQAKQKECDDLEKRIQELNNARHADMLN-LQTVERRLNEERRQ 646
Cdd:COG4913 281 LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEReIERLERELEERERR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 647 KQSLDSQ-----LSNEKKARKLAEEKAarpecssQCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEyrmLEA 721
Cdd:COG4913 361 RARLEALlaalgLPLPASAEEFAALRA-------EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE---IAS 430
|
170 180
....*....|....*....|..
gi 442624373 722 kLRNRESSQPDPEI-LLNALAA 742
Cdd:COG4913 431 -LERRKSNIPARLLaLRDALAE 451
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
569-727 |
5.94e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.53 E-value: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 569 KLEADVKKYRAEISHM----KQIENELRQKLDANLT--SKSTLQ-------AKQKEcddlekRIQE----LNNARHADML 631
Cdd:PRK11637 100 QLNKQIDELNASIAKLeqqqAAQERLLAAQLDAAFRqgEHTGLQlilsgeeSQRGE------RILAyfgyLNQARQETIA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 632 NLQTVERRLNEERR---QKQSLDSQLSNEKKAR--KLAEEKAAR----PECSSQCKQRRQQMDEEQK---RLRSDLKQAE 699
Cdd:PRK11637 174 ELKQTREELAAQKAeleEKQSQQKTLLYEQQAQqqKLEQARNERkktlTGLESSLQKDQQQLSELRAnesRLRDSIARAE 253
|
170 180 190
....*....|....*....|....*....|
gi 442624373 700 -EAKQLAvehgrkvEQEYRmlEA-KLRNRE 727
Cdd:PRK11637 254 rEAKARA-------EREAR--EAaRVRDKQ 274
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
569-728 |
6.46e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 6.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 569 KLEADVKKYRAEISHMKQIENeLRQKLdanltskstlqaKQKECDDLEKRIQELNNARhadmlnlQTVERRLNEERRQKQ 648
Cdd:PRK03918 356 ELEERHELYEEAKAKKEELER-LKKRL------------TGLTPEKLEKELEELEKAK-------EEIEEEISKITARIG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 649 SLDSQLSNEKKArkLAEEKAARPECSSqCkqRRQQMDEEQKRL----RSDLKQAEEAKQLAVEHGRKVEQEYRMLEaKLR 724
Cdd:PRK03918 416 ELKKEIKELKKA--IEELKKAKGKCPV-C--GRELTEEHRKELleeyTAELKRIEKELKEIEEKERKLRKELRELE-KVL 489
|
....
gi 442624373 725 NRES 728
Cdd:PRK03918 490 KKES 493
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
605-807 |
7.69e-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: 7.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 605 LQAKQKECDDLEKRIQELNNArhadmlnLQTVERRLNEERRQKQSLDSQLSNEKKARKLAEEKAArpecssQCKQRRQQM 684
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAE-------LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE------EVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 685 DEEQKRLRS--DLKQAEeaKQLAVEHGRKVEQEYRMLEAkLRNRESSQpdpeillNALAAMQDKNATLEKNLSAETrvkl 762
Cdd:COG1579 79 EEQLGNVRNnkEYEALQ--KEIESLKRRISDLEDEILEL-MERIEELE-------EELAELEAELAELEAELEEKK---- 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 442624373 763 dlfsalgaAKRQIEISDnhrrsKEDEVIDLKAKIAQLLAVMPDNL 807
Cdd:COG1579 145 --------AELDEELAE-----LEAELEELEAEREELAAKIPPEL 176
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
569-724 |
8.27e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.60 E-value: 8.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 569 KLEADVKKYRAEISHMKQIENELRQKLDANLtsKSTLQAKQKECDDLEKRIQELNNARHADMLNLQTVERRLNEERRQKQ 648
Cdd:pfam13868 127 QLREEIDEFNEEQAEWKELEKEEEREEDERI--LEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERD 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 649 SLDSQL---SNEKKARKLAEEKAARP--ECSSQCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEYRMLEAKL 723
Cdd:pfam13868 205 ELRAKLyqeEQERKERQKEREEAEKKarQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKR 284
|
.
gi 442624373 724 R 724
Cdd:pfam13868 285 R 285
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
585-734 |
9.06e-04 |
|
Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.
Pssm-ID: 282585 [Multi-domain] Cd Length: 511 Bit Score: 43.13 E-value: 9.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 585 KQIENELRQKLDANLTSKSTLQAKQKECDDLE--KRIQELNNARHADMlnlQTVERRLNEERRQKQSLDSQLSNEKKARK 662
Cdd:pfam04747 28 KSQRNQFRQWLLTAVLPNSINDQRKEAFASLEltEQPQQVEKVKKSEK---KKAQKQIAKDHEAEQKVNAKKAAEKEARR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 663 L---AEEKAARPECSSQCKQRRQQMDEEQKRLRSDLK--QAEEAKQLAV--EHGRKVEQ----------EYRMLEAKLRN 725
Cdd:pfam04747 105 AeaeAKKRAAQEEEHKQWKAEQERIQKEQEKKEADLKklQAEKKKEKAVkaEKAEKAEKtkkastpapvEEEIVVKKVAN 184
|
....*....
gi 442624373 726 RESSQPDPE 734
Cdd:pfam04747 185 DRSAAPAPE 193
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
602-779 |
1.02e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.49 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 602 KSTLQAKQKECDDLEKRIQELNNARHADMLNLQTVER-RLNEERRQKQSLDsQLSNEKKARKLAEEKAARpecssQCKQR 680
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKeRLAAQEQKKQAEE-AAKQAALKQKQAEEAAAK-----AAAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 681 RQQMDEEQKRLRSDLKQAEE--AKQLAVEHGRKVEQEYRM---LEAKLRNRESSQPDPEILLNALAAMQDK--------- 746
Cdd:PRK09510 146 KAKAEAEAKRAAAAAKKAAAeaKKKAEAEAAKKAAAEAKKkaeAEAAAKAAAEAKKKAEAEAKKKAAAEAKkkaaaeaka 225
|
170 180 190
....*....|....*....|....*....|....*.
gi 442624373 747 ---NATLEKNLSAETRVKLDLFSALGAAKRQIEISD 779
Cdd:PRK09510 226 aaaKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDD 261
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
637-798 |
1.13e-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: 42.57 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 637 ERRLNEERRQKQSLdsqlsnekkARKLAEEKAARPECSSQCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEY 716
Cdd:pfam07888 33 QNRLEECLQERAEL---------LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 717 RMLEaklRNRESSQPDPEILLNALAAMQDKNATLEKNLSAETRVKLDLFSALGAAKRQIEISDNHRRSKEDEVIDLKAKI 796
Cdd:pfam07888 104 KELS---ASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKL 180
|
..
gi 442624373 797 AQ 798
Cdd:pfam07888 181 QQ 182
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
569-801 |
1.19e-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: 42.44 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 569 KLEADVKKYRAEIshmkqieNELRQKLDANLTSKSTLQakqKECDDLEKRIQELNNARHADMLNLQTVERRLNEERRQKQ 648
Cdd:COG4942 24 EAEAELEQLQQEI-------AELEKELAALKKEEKALL---KQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 649 SLDSQLSNEKKArkLAEEKAARpecssqckQRRQQMDEEQKRLRS-DLKQAEEAKQLAVEHGRKVEQEYRMLEAKLRNRE 727
Cdd:COG4942 94 ELRAELEAQKEE--LAELLRAL--------YRLGRQPPLALLLSPeDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442624373 728 SSQPDPEILLNALAAMQDKNATLEKNLSAETRVKLDLFSALgaaKRQIEISDNHRRSKEDEVIDLKAKIAQLLA 801
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARL---EKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
604-771 |
1.63e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 604 TLQAKQKECDDLEKRIQELnnarhADMLNLqtverrlneERRQKQSLDSQLSNEKkarklAEEKAARPEcssqcKQRRQQ 683
Cdd:PRK09039 47 EISGKDSALDRLNSQIAEL-----ADLLSL---------ERQGNQDLQDSVANLR-----ASLSAAEAE-----RSRLQA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 684 MDEEQKRLRSDL--------KQAEEAKQLAVEHGRKVEQEYRMLEAkLRNRessqpdpeilLNALAAMQDknatLEKNLS 755
Cdd:PRK09039 103 LLAELAGAGAAAegragelaQELDSEKQVSARALAQVELLNQQIAA-LRRQ----------LAALEAALD----ASEKRD 167
|
170
....*....|....*..
gi 442624373 756 AETRVKL-DLFSALGAA 771
Cdd:PRK09039 168 RESQAKIaDLGRRLNVA 184
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
570-778 |
1.79e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 570 LEADVKKYRAEIShmkQIENELRQKLDANLTSKSTLQAKQkecddLEKRIQELNNArhadmlnLQTVERRLNEERRQKQS 649
Cdd:COG3206 180 LEEQLPELRKELE---EAEAALEEFRQKNGLVDLSEEAKL-----LLQQLSELESQ-------LAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 650 LDSQLSNEKKARKLAEEKAARPECSSQCKQRRQQMDEEQKRLRSD-------LKQAEEAKQLAVEHGRKVEQEYRMLEAK 722
Cdd:COG3206 245 LRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNhpdvialRAQIAALRAQLQQEAQRILASLEAELEA 324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442624373 723 LRNRESSqpdpeiLLNALAAMQDKNATLEK------NLSAETRVKLDLFSALGAAKRQIEIS 778
Cdd:COG3206 325 LQAREAS------LQAQLAQLEARLAELPEleaelrRLEREVEVARELYESLLQRLEEARLA 380
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
575-703 |
1.82e-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: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 575 KKYRAEISHMKQIENELRQKLDANLTSKSTLQAKQKECDDLEKRIQELNNARHADmlnlqtverrlnEERRQKQSLDSQL 654
Cdd:pfam17380 485 DRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAE------------EERRKQQEMEERR 552
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 442624373 655 SNEKKARKLAEEKAarpecssqckqRRQQMDEEQKRLRSdLKQAEEAKQ 703
Cdd:pfam17380 553 RIQEQMRKATEERS-----------RLEAMEREREMMRQ-IVESEKARA 589
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
620-788 |
2.40e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 620 QELNNARHADMLNLQTV---ERRLNE----ERRQKQS-----LDSQLSNEKKArKLAEEKAarpecssqckqrRQQMDEE 687
Cdd:pfam01576 319 QELRSKREQEVTELKKAleeETRSHEaqlqEMRQKHTqaleeLTEQLEQAKRN-KANLEKA------------KQALESE 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 688 QKRLRSDLKQAEEAKQlAVEHGR-KVEQEYRMLEAKLRNRESS-----------QPDPEILLNALAAMQDKNATLEKNLS 755
Cdd:pfam01576 386 NAELQAELRTLQQAKQ-DSEHKRkKLEGQLQELQARLSESERQraelaeklsklQSELESVSSLLNEAEGKNIKLSKDVS 464
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 442624373 756 A--------------ETRVKLDLFSALgaakRQIEISDNHRRSKEDE 788
Cdd:pfam01576 465 SlesqlqdtqellqeETRQKLNLSTRL----RQLEDERNSLQEQLEE 507
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
571-727 |
2.53e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.06 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 571 EADVKKYRAEISHMKQIE-NELRQKLDANltskstlQAKQKECDDL-EKRIQElNNARHADMLNLQTVERRLNEERRQKQ 648
Cdd:pfam13868 168 EEEREAEREEIEEEKEREiARLRAQQEKA-------QDEKAERDELrAKLYQE-EQERKERQKEREEAEKKARQRQELQQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 649 SLDSQLsnEKKARKLAEEKA------ARPECSSQCKQRRQQMDEEQKRLRSD------LKQAEEAKQLAVEHGRKVEQEY 716
Cdd:pfam13868 240 AREEQI--ELKERRLAEEAEreeeefERMLRKQAEDEEIEQEEAEKRRMKRLehrrelEKQIEEREEQRAAEREEELEEG 317
|
170
....*....|.
gi 442624373 717 RMLEAKLRNRE 727
Cdd:pfam13868 318 ERLREEEAERR 328
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
568-789 |
2.90e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 568 LKLEADVKKYRAEISHMKQIE----NELRQKLDANLTSKSTLQAKQKEcddLEKRIQELNNARHADMLNLQTVERRLNEE 643
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEkkkaEELKKAEEENKIKAAEEAKKAEE---DKKKAEEAKKAEEDEKKAAEALKKEAEEA 1701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 644 RRQKQSLDSQLSNEKKARKLAEEKAARPECSSQCKQRrqqmDEEQKRLRSDLKQAEEAK----QLAVEHGRKVEQEYRML 719
Cdd:PTZ00121 1702 KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE----AEEDKKKAEEAKKDEEEKkkiaHLKKEEEKKAEEIRKEK 1777
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 720 EAKLRnRESSQPDPEILLNALAAMQD------------KNATLEKNLSAETRVkldlfsalgAAKRQIEISDNHRRSKED 787
Cdd:PTZ00121 1778 EAVIE-EELDEEDEKRRMEVDKKIKDifdnfaniieggKEGNLVINDSKEMED---------SAIKEVADSKNMQLEEAD 1847
|
..
gi 442624373 788 EV 789
Cdd:PTZ00121 1848 AF 1849
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
570-796 |
2.90e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 570 LEADVKKYRAEISHMKQIENELRQKLDAnltSKSTLQA---KQKECDDLEKRIQELNNARHADMLNLQTVERRLNEERRQ 646
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDE---ADEVLEEheeRREELETLEAEIEDLRETIAETEREREELAEEVRDLRER 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 647 KQSLDSQLSN---------------EKKARKLAEEKAARPECSSQCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRK 711
Cdd:PRK02224 288 LEELEEERDDllaeaglddadaeavEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 712 VEQEYRMLEAKLRNRESsqpdpeillnALAAMQDKNATLEKNLsAETRVKLDlfsalGAAKRQIEISDNHRRSKEDEViD 791
Cdd:PRK02224 368 LESELEEAREAVEDRRE----------EIEELEEEIEELRERF-GDAPVDLG-----NAEDFLEELREERDELREREA-E 430
|
....*
gi 442624373 792 LKAKI 796
Cdd:PRK02224 431 LEATL 435
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
561-776 |
3.24e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 561 SKICETCLKLEADVKKYRAEISHMKQIENELRQKLDanltskstlqaKQKECDDLEKRIQELNNARHADMLNLQTVERRL 640
Cdd:PRK02224 464 SPHVETIEEDRERVEELEAELEDLEEEVEEVEERLE-----------RAEDLVEAEDRIERLEERREDLEELIAERRETI 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 641 NEERRQKQSLDSQLSN--------EKKARKLAEEKAARPECSSQCKQRRQQMDEEQKRL---RSDLKQAEEAKQLAVEHG 709
Cdd:PRK02224 533 EEKRERAEELRERAAEleaeaeekREAAAEAEEEAEEAREEVAELNSKLAELKERIESLeriRTLLAAIADAEDEIERLR 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 710 RKVEQ------EYRMLEAKLRNREsSQPDPEILLNALAAMQDKNATLEK-------NLSAETRVKLDLFSALGAAKRQIE 776
Cdd:PRK02224 613 EKREAlaelndERRERLAEKRERK-RELEAEFDEARIEEAREDKERAEEyleqveeKLDELREERDDLQAEIGAVENELE 691
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
569-744 |
3.39e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 569 KLEADVKKYRAEISHMKQIENELRQKLDAnltSKSTLQAKQKECDDLEKRIQELNN-----ARH---------------- 627
Cdd:COG3883 34 AAQAELDALQAELEELNEEYNELQAELEA---LQAEIDKLQAEIAEAEAEIEERREelgerARAlyrsggsvsyldvllg 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 628 ----ADMLNLQTVERRLNEerRQKQSLDSQlsnEKKARKLAEEKAARPECSSQCKQRRQQMDEEQKRLRSDLKQAEEAKQ 703
Cdd:COG3883 111 sesfSDFLDRLSALSKIAD--ADADLLEEL---KADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLA 185
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 442624373 704 LAVEHGRKVEQEYRMLEAKLRNRESSQPDPEILLNALAAMQ 744
Cdd:COG3883 186 QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
645-715 |
3.61e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.95 E-value: 3.61e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442624373 645 RQKQSLDSQLSNEKKARKLAEEKAARPECSSQCKQRRQQMDEEQK-RLRSDLKQAEEAKQLAVEHGRKVEQE 715
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERlAAQEQKKQAEEAAKQAALKQKQAEEA 137
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
569-714 |
3.69e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 569 KLEADVKKYRAEISHMKQIENELRQKLDANLTSKSTLQAKQKECDDLEKRIQELNNARHADMLNLQTVERRLNEERRQKQ 648
Cdd:COG1340 47 ELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQ 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 649 SLDSQLSNEK----KARKLAEEkaarpecssqcKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQ 714
Cdd:COG1340 127 TEVLSPEEEKelveKIKELEKE-----------LEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKE 185
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
552-725 |
3.79e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 41.20 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 552 IANLASKVVSKICETCLKLEA-------------DVKKYRAEISHMKQIENELRQKLDAnltsKSTLQAKQKECDDLEKR 618
Cdd:pfam13166 288 LQKLIEKVESAISSLLAQLPAvsdlasllsafelDVEDIESEAEVLNSQLDGLRRALEA----KRKDPFKSIELDSVDAK 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 619 IQELNNArhadmlnLQTVERRLNEERRQKQSLDSqlsNEKKARKlaeekAARPECSSQCKQRRQQMDEEQKRLRSDLKQA 698
Cdd:pfam13166 364 IESINDL-------VASINELIAKHNEITDNFEE---EKNKAKK-----KLRLHLVEEFKSEIDEYKDKYAGLEKAINSL 428
|
170 180
....*....|....*....|....*..
gi 442624373 699 EEAKQLAVEHGRKVEQEYRMLEAKLRN 725
Cdd:pfam13166 429 EKEIKNLEAEIKKLREEIKELEAQLRD 455
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
569-800 |
4.25e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 40.29 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 569 KLEADVKKYRAEISHMKQ-IENELRQKLDAnltsKSTLQAKQKECD-------DLEKRIQELNnarhaDMLNLQtveRRL 640
Cdd:pfam00038 72 RLQLELDNLRLAAEDFRQkYEDELNLRTSA----ENDLVGLRKDLDeatlarvDLEAKIESLK-----EELAFL---KKN 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 641 NEER---RQKQSLDSQLSNEKKArklaeekAARPECSSQCKQRRQQMDEEQKRLRSDLK-----QAEEAKQLAVEHGRKV 712
Cdd:pfam00038 140 HEEEvreLQAQVSDTQVNVEMDA-------ARKLDLTSALAEIRAQYEEIAAKNREEAEewyqsKLEELQQAAARNGDAL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 713 EQ------EYRMleaKLRNRESSqpdpeillnaLAAMQDKNATLEKNLsAETRVKLDLfsALGAAKRQIEisdnhrrSKE 786
Cdd:pfam00038 213 RSakeeitELRR---TIQSLEIE----------LQSLKKQKASLERQL-AETEERYEL--QLADYQELIS-------ELE 269
|
250
....*....|....
gi 442624373 787 DEVIDLKAKIAQLL 800
Cdd:pfam00038 270 AELQETRQEMARQL 283
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
565-706 |
4.26e-03 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 38.88 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 565 ETCLKLEADVKKYRAEISHMK--QIENELRQKLDAnltskstlqAKQKecddLEKRI-QELNNARHADmlnLQTVERRLN 641
Cdd:pfam15346 11 ETARRVEEAVAKRVEEELEKRkdEIEAEVERRVEE---------ARKI----MEKQVlEELEREREAE---LEEERRKEE 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 642 EERRQKQSLDSQL-SNEKKA----RKLAEEKAARPEcssqckqRRQQMDEEQKRLRSDLKQAEEAKQLAV 706
Cdd:pfam15346 75 EERKKREELERILeENNRKIeeaqRKEAEERLAMLE-------EQRRMKEERQRREKEEEEREKREQQKI 137
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
585-717 |
4.47e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 585 KQIENELRQKL-DANLTSKST-----LQAKQKECD---DLEKRIQELNNarhadmlNLQTVERRLneeRRQKQSLDSQLS 655
Cdd:PRK12704 34 KEAEEEAKRILeEAKKEAEAIkkealLEAKEEIHKlrnEFEKELRERRN-------ELQKLEKRL---LQKEENLDRKLE 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442624373 656 N-EKKARKLAEEKaarpecsSQCKQRRQQMDEEQKRLRSDLKQ------------AEEAKQLAVEhgrKVEQEYR 717
Cdd:PRK12704 104 LlEKREEELEKKE-------KELEQKQQELEKKEEELEELIEEqlqelerisgltAEEAKEILLE---KVEEEAR 168
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
569-646 |
4.94e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 39.05 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 569 KLEADVKKYRAEIshmKQIENELRQKL-----DANLTSKSTLQAKQKECDDLEKRIQELNNARHADMlnlqtvERRLNEE 643
Cdd:COG2825 47 KLEKEFKKRQAEL---QKLEKELQALQeklqkEAATLSEEERQKKERELQKKQQELQRKQQEAQQDL------QKRQQEL 117
|
...
gi 442624373 644 RRQ 646
Cdd:COG2825 118 LQP 120
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
569-646 |
5.04e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 38.33 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 569 KLEADVKKYRAEIshmKQIENELRQKL-----DANLTSKSTLQAKQKECDDLEKRIQELNNARHADMlnlqtvERRLNEE 643
Cdd:smart00935 22 QLEKEFKKRQAEL---EKLEKELQKLKeklqkDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDL------QKRQQEE 92
|
...
gi 442624373 644 RRQ 646
Cdd:smart00935 93 LQK 95
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
632-729 |
5.73e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 632 NLQTVERRLNEERRQKQSLDSQLSN-EKKARKLAEEKAARPECSSQCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGR 710
Cdd:PRK03918 166 NLGEVIKEIKRRIERLEKFIKRTENiEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEK 245
|
90 100
....*....|....*....|..
gi 442624373 711 ---KVEQEYRMLEAKLRNRESS 729
Cdd:PRK03918 246 eleSLEGSKRKLEEKIRELEER 267
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
637-724 |
6.83e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 40.24 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 637 ERRLNEERRQKQSLDSQLSnEKKARKLAEEKAARPECSSQCKQRRQQMDEEQKRlrsdLKQAEEAKQLAVEHGR---KVE 713
Cdd:pfam02029 247 EQKLEELRRRRQEKESEEF-EKLRQKQQEAELELEELKKKREERRKLLEEEEQR----RKQEEAERKLREEEEKrrmKEE 321
|
90
....*....|.
gi 442624373 714 QEYRMLEAKLR 724
Cdd:pfam02029 322 IERRRAEAAEK 332
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
584-704 |
7.19e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 39.52 E-value: 7.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 584 MKQIENELRQKLDAnLTSKSTLQAKQKecddLEKRIQELNNA--RHADMLnlQTVERRLNEERRQKQSLDSQLSNEKKA- 660
Cdd:pfam00038 168 LTSALAEIRAQYEE-IAAKNREEAEEW----YQSKLEELQQAaaRNGDAL--RSAKEEITELRRTIQSLEIELQSLKKQk 240
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 442624373 661 ----RKLAEEKAARPECSSQCKQRRQQMDEEQKRLRSDL-KQAEEAKQL 704
Cdd:pfam00038 241 asleRQLAETEERYELQLADYQELISELEAELQETRQEMaRQLREYQEL 289
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
613-799 |
8.45e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 8.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 613 DDLEKRIQELNNArHADMLNLQTVERRLNEERRQKQSLDSQLSNEKKARKLAEekAARPECSSQckqRRQQMDEEQKRLR 692
Cdd:COG4913 228 DALVEHFDDLERA-HEALEDAREQIELLEPIRELAERYAAARERLAELEYLRA--ALRLWFAQR---RLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 693 SDLKQAEEAKQLAVEHGRKVEQEYRMLEAKLRNRESSQPDPeiLLNALAAMQDKNATLEKNLSA-ETRVK-LDL------ 764
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ--LEREIERLERELEERERRRARlEALLAaLGLplpasa 379
|
170 180 190
....*....|....*....|....*....|....*...
gi 442624373 765 --FSAL-GAAKRQIEISDNHRRSKEDEVIDLKAKIAQL 799
Cdd:COG4913 380 eeFAALrAEAAALLEALEEELEALEEALAEAEAALRDL 417
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
570-799 |
8.71e-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: 40.00 E-value: 8.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 570 LEADVKKYRAEISHMKQIENELRQKLDANLTSKSTLQAKQKECDDLEKRIQELNNARHADMLNLQTVERRLNEERRQKQS 649
Cdd:TIGR04523 171 LENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 650 LDSQLSNEK----KARKLAEEKaarpecSSQCKQRRQQMDEEQKRLR------SDLKQAEEA---KQLAvEHGRKVEQEY 716
Cdd:TIGR04523 251 TQTQLNQLKdeqnKIKKQLSEK------QKELEQNNKKIKELEKQLNqlkseiSDLNNQKEQdwnKELK-SELKNQEKKL 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 717 RMLEAKLRNREssqpdpeillNALAAMQDKNATLEKNLSAETRVKLDLFSALGAAKRQIEISDNHRRSKEDEVIDLKAKI 796
Cdd:TIGR04523 324 EEIQNQISQNN----------KIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI 393
|
...
gi 442624373 797 AQL 799
Cdd:TIGR04523 394 NDL 396
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
569-736 |
8.95e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.75 E-value: 8.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 569 KLEADVKKYRAEISHMKQIENELRQKLDANLTSKSTLQAKQKEcddLEKRIQELNNarhadmlNLQTVERRLNEERRQK- 647
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKR---LELEIEEVEA-------RIKKYEEQLGNVRNNKe 90
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 648 -QSLDSQLSNEKKARKLAEEK-----AARPECSSQCKQRRQQMDEEQKRLRSDLKQAEEAKQlavehgrKVEQEYRMLEA 721
Cdd:COG1579 91 yEALQKEIESLKRRISDLEDEilelmERIEELEEELAELEAELAELEAELEEKKAELDEELA-------ELEAELEELEA 163
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170
....*....|....*
gi 442624373 722 KlRNRESSQPDPEIL 736
Cdd:COG1579 164 E-REELAAKIPPELL 177
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| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
606-747 |
9.59e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 39.52 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 606 QAKQKECDDLEKRIQELNNARHADMLNLQTV-ERRLNEERRQ-KQSLDSQLSNEKKARKLAEEKAARPECSSQCKQRRQQ 683
Cdd:pfam13868 32 KRIKAEEKEEERRLDEMMEEERERALEEEEEkEEERKEERKRyRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 684 MDEE---------QKRLRSDLKQAEEAKQL---------------AVEHGRKVEQEYRMLEAKLRNRESSQpdpEILLNA 739
Cdd:pfam13868 112 EEDQaeaeeklekQRQLREEIDEFNEEQAEwkelekeeereederILEYLKEKAEREEEREAEREEIEEEK---EREIAR 188
|
....*...
gi 442624373 740 LAAMQDKN 747
Cdd:pfam13868 189 LRAQQEKA 196
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| mukB |
PRK04863 |
chromosome partition protein MukB; |
633-763 |
9.88e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 9.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624373 633 LQTVERRLNEERRQ-------KQSLDSQLSNEKKARKLAEEKAARPECSSQCKqrrqqmdEEQKRLRSDLKQAEEAKQLA 705
Cdd:PRK04863 522 LSELEQRLRQQQRAerllaefCKRLGKNLDDEDELEQLQEELEARLESLSESV-------SEARERRMALRQQLEQLQAR 594
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442624373 706 VEHGRKVEQEYRMLEAKL-RNRESS---QPDPEILLNALAAMQD--KNATLEKNLSAETRVKLD 763
Cdd:PRK04863 595 IQRLAARAPAWLAAQDALaRLREQSgeeFEDSQDVTEYMQQLLEreRELTVERDELAARKQALD 658
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