|
Name |
Accession |
Description |
Interval |
E-value |
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
2-893 |
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: 611.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 2 KRRNADCGKLRRPIKRNKITEGMYGSTtVLYMKFLILWAIVMVADFMFMFRFEFLWPFWLLLRSVHDSFKYKGLAFSVLF 81
Cdd:pfam09726 1 KRRNADCSKLRRPLKRNRITEGIYGST-FLYLKFLVVWALVLLADFVLEFRFEYLWPFWLLIRSVYDSFKYQGLAFSVFF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 82 VCIAITSDLVCLFFIPVHWLLFAASTYVWVQYVWHTDKGICLPTIILWMLFVYLEVGIRWKDSRHMpHLDLCRPFAAHCI 161
Cdd:pfam09726 80 VCIAFTSDIICLLFIPVQWLFFAASTYVWVQYVWHTEKGICLPTVSLWILFVYIEAAIRFKDLKNF-HVDLCRPFAAHCI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 162 GYPVVTLGFGFKSYVGYRMRQRKQREVAKDNEFYMQLLQQALPAEEAAEEAAAgqaatsstvvvangsattpalvaSSGA 241
Cdd:pfam09726 159 GYPVVTLGFGFKSYVSYKMRLRKQREVQKENEFYMQLLQQALPKEQQMLDRQE-----------------------RETS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 242 TAANGVLATATQAQNHhehhhsggagassssssnsnhhhhhhhnnssgnsgsnhnsnsssggakdnstsesasgaaassi 321
Cdd:pfam09726 216 ETAKGLSEVDPLALNQ---------------------------------------------------------------- 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 322 tassatgaalaaaasassasttsgsssssastgkqssssaasaattgaattsstpvsdfsalaaslatqqqqhqsvatay 401
Cdd:pfam09726 --------------------------------------------------------------------------------
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 402 patssarsssstsegvdadgccgatsNGHAGGSRNHRRSMDKDKHRNKGDAADNEHNNGTRHGGKNSGNNQVDSAATATA 481
Cdd:pfam09726 232 --------------------------NGHSLNKKDSTLQLPELEYREKKNSGTSSGSDSKKSHNHNIHNLNHVDSKLQEK 285
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 482 TVTATSSNSKDKDKEKSDWDSSTsypqqqqQGGKEKHEKKAGNAVPNGNANHledetasveptppvEKATKGRRNRGkkd 561
Cdd:pfam09726 286 EYMENHSNSKRLNISTSPGSEED-------LLVRESVSSKSSSSSSSSNKNY--------------KNASGGSANSS--- 341
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 562 NAAKDNHSHQQQLAQQQKEKDKENTANNNNNDASSVSSSASSTssnaiaNLASKVVSKICETClKLEADVKKYRAEISHM 641
Cdd:pfam09726 342 NSSPRSHSHNSGSVTSSSSSKNSKKQKGPGGKSGARHKDPAEN------CIPNNQLSKPDALV-RLEQDIKKLKAELQAS 414
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 642 KQIENELRQKLDANLTS----KSTLQAKQKECDDLEKRIQELNNARHADMLNLQTVERRLNEERRQKQSLDSQLSNEKKA 717
Cdd:pfam09726 415 RQTEQELRSQISSLTSLerslKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKRLKAEQEARASAEKQLAEEKKR 494
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 718 RKLAEEKAARP---------ECSSQCKQRRQQMDEEQKRLRSDLKQAEEakqlavehgrkveqEYRMLEAK---LRNRES 785
Cdd:pfam09726 495 KKEEEATAARAvalaaasrgECTESLKQRKRELESEIKKLTHDIKLKEE--------------QIRELEIKvqeLRKYKE 560
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 786 SQPDPEILLNALAAMQDKNATLEKNLSAETRVKLDLFSALGAAKRQIEISDNHRRSKEDEVIDLKAKIAQLLAVMPD-NL 864
Cdd:pfam09726 561 SEKDTEVLMSALSAMQDKNQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQIYQKDQEIKDLKQKIAEVMAVMPStSR 640
|
890 900
....*....|....*....|....*....
gi 442624369 865 CMNTGPHGPSSSIlrmnDTPPLQSGPGPS 893
Cdd:pfam09726 641 ITPVTPHYSSKFM----DTSPSMRDPNAS 665
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
625-858 |
1.88e-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: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 625 LKLEADV-KKYRAeishmkqIENELRQkLDANLTSKStLQAKQKECDDLEKRIQELNNARHADMLNLQTVERRLNEERRQ 703
Cdd:COG1196 205 LERQAEKaERYRE-------LKEELKE-LEAELLLLK-LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 704 KQSLDSQLS------NEKKARKLAEEKAARPEC--SSQCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEYRM 775
Cdd:COG1196 276 LEELELELEeaqaeeYELLAELARLEQDIARLEerRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 776 LEAKLRNRESSQPDpeiLLNALAAMQDKNATLEKNLSAETRVKLDLFSALGAAKRQIEISDNHRRSKEDEVIDLKAKIAQ 855
Cdd:COG1196 356 AEAELAEAEEALLE---AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
...
gi 442624369 856 LLA 858
Cdd:COG1196 433 LEE 435
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
626-858 |
1.62e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 61.07 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 626 KLEADVKKYRAEISHMKQIENELRQKLDANL-TSKSTLQAKQKECDDLEKRIQELNNarhadmlNLQTVERRLNEERRQK 704
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLrKALFELDKLQEELEQLREELEQARE-------ELEQLEEELEQARSEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 705 QSLDSQLsnEKKARKLAEEKAARpecsSQCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEYRMLEAKLRNRE 784
Cdd:COG4372 76 EQLEEEL--EELNEQLQAAQAEL----AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAERE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442624369 785 SSQpdpEILLNALAAMQDKNATLEKNLSAETRVKLD--LFSALGAAKRQIEISDNHRRSKEDEVIDLKAKIAQLLA 858
Cdd:COG4372 150 EEL---KELEEQLESLQEELAALEQELQALSEAEAEqaLDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLE 222
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
627-864 |
1.16e-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: 59.31 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 627 LEADVKKYRAEIshmKQIENELRQKLDAnltskstLQAKQKECDDLEKRIQELNNARHADMLNLQTVERRLNEERRQK-- 704
Cdd:TIGR02169 728 LEQEEEKLKERL---EELEEDLSSLEQE-------IENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEiq 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 705 -----------------QSLDSQLSNEKKARKLAEEKAA-----RPECSSQCKQRRQQMDEEQKRLRsDLKQAEEAKQLA 762
Cdd:TIGR02169 798 aelskleeevsriearlREIEQKLNRLTLEKEYLEKEIQelqeqRIDLKEQIKSIEKEIENLNGKKE-ELEEELEELEAA 876
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 763 VehgRKVEQEYRMLEAKLRNRESSQPDPEILLNALAAMQDKNATLEKNLSAETRVKLDLFSALGAAKRQIEISDNHRRSK 842
Cdd:TIGR02169 877 L---RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL 953
|
250 260
....*....|....*....|..
gi 442624369 843 EDEVIDLKAKIAQLLAVMPDNL 864
Cdd:TIGR02169 954 EDVQAELQRVEEEIRALEPVNM 975
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
626-854 |
1.95e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 57.60 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 626 KLEADVKKYRAEIshmKQIENELRQkldanltSKSTLQAKQKECDDLEKRIQELNNARHADMLNLQTVERRLNEERRQKQ 705
Cdd:COG4372 42 KLQEELEQLREEL---EQAREELEQ-------LEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 706 SLDSQLSN--------EKKARKLAEEKAARPECSSQCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEhgRKVEQEYRMLE 777
Cdd:COG4372 112 ELQEELEElqkerqdlEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE--AEAEQALDELL 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442624369 778 AKLRNRESSQPDPEILLNALAAMQDKNATLEKNLSAETRVKLDLFSALGAAKRQIEISDNHRRSKEDEVIDLKAKIA 854
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
633-858 |
3.20e-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: 58.16 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 633 KYRAEISHMKQIE-NELRQKLDANLTSKSTLQakqKECDDLEKRIQELNNARHADMLNLQTVERRLNEERRQKQSLDSQL 711
Cdd:TIGR02169 212 RYQALLKEKREYEgYELLKEKEALERQKEAIE---RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEE 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 712 SNEKKaRKLAEEKAARPECSSQ---CKQRRQQMDEEQKRLRSDL-KQAEEAKQLAvehgRKVEqEYRMLEAKLRNR-ESS 786
Cdd:TIGR02169 289 QLRVK-EKIGELEAEIASLERSiaeKERELEDAEERLAKLEAEIdKLLAEIEELE----REIE-EERKRRDKLTEEyAEL 362
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442624369 787 QPDPEILLNALAAMQDKNATLEKNLSAETRVKLDLFSALGAAKRQIEISDNHRRSKEDEVIDLKAKIAQLLA 858
Cdd:TIGR02169 363 KEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA 434
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
629-856 |
4.38e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 4.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 629 ADVKKYRAEISHMKQIENELRQKLDAnltSKSTLQAKQKECDDLEKRIQELN---NARHADMLNLQ----TVERRLNEER 701
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEE---LTAELQELEEKLEELRLEVSELEeeiEELQKELYALAneisRLEQQKQILR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 702 RQKQSLDSQLS--------NEKKARKLAEEKAARPECSSQCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEY 773
Cdd:TIGR02168 309 ERLANLERQLEeleaqleeLESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 774 RMLE---AKLRNRESSQpdpEILLNALAAMQDKN----------------ATLEKNLSAETRVKLDLFSALGAAKRQIEI 834
Cdd:TIGR02168 389 AQLElqiASLNNEIERL---EARLERLEDRRERLqqeieellkkleeaelKELQAELEELEEELEELQEELERLEEALEE 465
|
250 260
....*....|....*....|..
gi 442624369 835 SDNHRRSKEDEVIDLKAKIAQL 856
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAQL 487
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
627-814 |
8.21e-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: 8.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 627 LEADVKKYRAEISHMKQIENELRQKLDANLTSKSTLQAKQKEcddLEKRIQELNNARHADMLNLQTVERRLNEERRQKQS 706
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE---AEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 707 LDSQLSNEKKARKLAEEKAARpecssqCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEYRMLEAKLRNRESS 786
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEA------LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
170 180
....*....|....*....|....*....
gi 442624369 787 QPDP-EILLNALAAMQDKNATLEKNLSAE 814
Cdd:COG1196 465 LAELlEEAALLEAALAELLEELAEAAARL 493
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
619-831 |
1.46e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 619 KICETCLKLEADVKKYRAEISHMKQIENELR---QKLDANLTSKSTLQAKQKE-----CDDLEKRIQELNNArHADMLNL 690
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAeleKKLDELEEELAELLKELEElgfesVEELEERLKELEPF-YNEYLEL 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 691 QTVERRLNEERRQKQSLDSQLsnEKKARKLAEEKAARPECSSQCKQRRQQMDEEQKR--------LRSDLKQAEEAKQLA 762
Cdd:PRK03918 608 KDAEKELEREEKELKKLEEEL--DKAFEELAETEKRLEELRKELEELEKKYSEEEYEelreeyleLSRELAGLRAELEEL 685
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442624369 763 VEHGRKVEQEYRMLEAKLRNRESSQPDPEILLNALAAMQD--------KNATLEKNLSAETRVKLDLFSALGAAKRQ 831
Cdd:PRK03918 686 EKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEElrekvkkyKALLKERALSKVGEIASEIFEELTEGKYS 762
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
626-827 |
1.84e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 626 KLEADVKKY-----RAEISHMKQIEnELRQKLDANLTSKSTLQAKQKECDDLEKRIQELNNA---------RHADMLNLQ 691
Cdd:COG4717 50 RLEKEADELfkpqgRKPELNLKELK-ELEEELKEAEEKEEEYAELQEELEELEEELEELEAEleelreeleKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 692 TVERRLNEERRQKQSLDSQLSN-EKKARKLAEEKAARPECSSQCKQRRQQMDEEQKRLrsDLKQAEEAKQLAVEHgRKVE 770
Cdd:COG4717 129 PLYQELEALEAELAELPERLEElEERLEELRELEEELEELEAELAELQEELEELLEQL--SLATEEELQDLAEEL-EELQ 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 442624369 771 QEYRMLEAKLrnrESSQPDPEILLNALAAMQDKNATLEKNLS-AETRVKLDLFSALGA 827
Cdd:COG4717 206 QRLAELEEEL---EEAQEELEELEEELEQLENELEAAALEERlKEARLLLLIAAALLA 260
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
637-843 |
4.52e-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: 53.97 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 637 EISHMKQIEnelrqkldanltsKSTLQAKQKEcddlEKRIQELNNARHADMLNlQTVERRLNEERRQKQSLDSQLSN--E 714
Cdd:pfam17380 373 EISRMRELE-------------RLQMERQQKN----ERVRQELEAARKVKILE-EERQRKIQQQKVEMEQIRAEQEEarQ 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 715 KKARKLAEEKAARPECSSQCKQRRQ-------QMDEEQKRLRSDLKQAEEAKQLAVEHGRKV-EQEYR-----MLEAKlR 781
Cdd:pfam17380 435 REVRRLEEERAREMERVRLEEQERQqqverlrQQEEERKRKKLELEKEKRDRKRAEEQRRKIlEKELEerkqaMIEEE-R 513
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442624369 782 NRESSQPDPEILLNALAAMQDKNATLEKN-----------------LSAETRVKLDLFSALGAAKRQIEISDNHRRSKE 843
Cdd:pfam17380 514 KRKLLEKEMEERQKAIYEEERRREAEEERrkqqemeerrriqeqmrKATEERSRLEAMEREREMMRQIVESEKARAEYE 592
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
673-860 |
5.35e-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: 53.91 E-value: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 673 EKRIQELNNARHADMlNLQTVERRLNEERRQKQSLDSQLSNEKKARKL-AEEKAARPECSsqcKQRRQQMDEEQKRLRSD 751
Cdd:TIGR02168 172 ERRKETERKLERTRE-NLDRLEDILNELERQLKSLERQAEKAERYKELkAELRELELALL---VLRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 752 LKQAEEAKQLAVEHGRKVEQEYRMLEAKLRNRESSQPDPEILLNALAAMQdknATLEKNLsAETRVKLD-LFSALGAAKR 830
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI---SRLEQQK-QILRERLAnLERQLEELEA 323
|
170 180 190
....*....|....*....|....*....|
gi 442624369 831 QIEISDNHRRSKEDEVIDLKAKIAQLLAVM 860
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEEL 353
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
628-856 |
6.95e-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: 6.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 628 EADVKKYRAEiSHMKQIENELRQKLDANLTSKSTLQAKQKECDDLEKRIQELNNARHADMLNLQTVERRLNEERRQKQSL 707
Cdd:TIGR02168 772 EAEEELAEAE-AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 708 DSQLsnEKKARKLAEEKAARPECSSQckqrRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEYRMLEAKLRNRESSQ 787
Cdd:TIGR02168 851 SEDI--ESLAAEIEELEELIEELESE----LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442624369 788 PDpeiLLNALAAMQDKNATLEKNLSAETRVKLDLFSALGAAKrqieisDNHRRSKEDEVIDLKAKIAQL 856
Cdd:TIGR02168 925 AQ---LELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKI------EDDEEEARRRLKRLENKIKEL 984
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
626-744 |
2.07e-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: 49.92 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 626 KLEADVKKYRAEISHMKQIENELRQKLDANLTSKStLQAKQKECDDLEKRIQELNNARHADMLNLQTVERRLNEERRQKQ 705
Cdd:COG1579 56 DLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE-YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELA 134
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 442624369 706 SLDSQLSNEKKAR--KLAEEKAARPECSSQCKQRRQQMDEE 744
Cdd:COG1579 135 ELEAELEEKKAELdeELAELEAELEELEAEREELAAKIPPE 175
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
670-795 |
3.57e-06 |
|
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: 47.74 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 670 DDLEKRIQELNNARHADMLNLQT------VERRLNEERRQ-KQSLDSQLSNEKKARklAEEKAARPEcssQCKQRRQQMD 742
Cdd:pfam15346 10 EETARRVEEAVAKRVEEELEKRKdeieaeVERRVEEARKImEKQVLEELEREREAE--LEEERRKEE---EERKKREELE 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 442624369 743 EEqkrLRSDLKQAEEA-KQLAVEHGRKVEQEYRMLEAKLR----NRESSQPDPEILLN 795
Cdd:pfam15346 85 RI---LEENNRKIEEAqRKEAEERLAMLEEQRRMKEERQRrekeEEEREKREQQKILN 139
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
625-860 |
3.65e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 625 LKLEADVKKYRAEISHMKQIENELRQKLDANLTSKSTLQAKQKECDDLEKriQELNNARHADMLN----LQTVERRLNEE 700
Cdd:PRK03918 401 EEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHR--KELLEEYTAELKRiekeLKEIEEKERKL 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 701 RRQKQSLDSQLSNEKKARKLaeekaarpecssqckqrrQQMDEEQKRLRSDLKQ--AEEAKQLAVEHgRKVEQEYRMLEA 778
Cdd:PRK03918 479 RKELRELEKVLKKESELIKL------------------KELAEQLKELEEKLKKynLEELEKKAEEY-EKLKEKLIKLKG 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 779 KLRNRESSQPDPEILLNALAAMQDKNATLEKNLSA----------------ETRVK-----LDLFSALGAAKRQIEISDN 837
Cdd:PRK03918 540 EIKSLKKELEKLEELKKKLAELEKKLDELEEELAEllkeleelgfesveelEERLKelepfYNEYLELKDAEKELEREEK 619
|
250 260
....*....|....*....|...
gi 442624369 838 HRRSKEDEVIDLKAKIAQLLAVM 860
Cdd:PRK03918 620 ELKKLEEELDKAFEELAETEKRL 642
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
625-784 |
5.28e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 625 LKLEADVKKYRAEISHMKQIENELRQKLDANltskstlqaKQKECDDLEKRIQELNNARHADML----NLQTVERRLNEE 700
Cdd:COG4717 330 LPPDLSPEELLELLDRIEELQELLREAEELE---------EELQLEELEQEIAALLAEAGVEDEeelrAALEQAEEYQEL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 701 RRQKQSLDSQLSNEKKARKLAEEKAARPECSSQ----------CKQRRQQMDEEQKRLRSDLKQAEEAKQLAvehgrKVE 770
Cdd:COG4717 401 KEELEELEEQLEELLGELEELLEALDEEELEEEleeleeeleeLEEELEELREELAELEAELEQLEEDGELA-----ELL 475
|
170
....*....|....
gi 442624369 771 QEYRMLEAKLRNRE 784
Cdd:COG4717 476 QELEELKAELRELA 489
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
662-856 |
7.06e-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: 7.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 662 LQAKQKECDDLEKRIQELNNARHAdmlnLQTVERRLNEERRQKQSLDSQLSNEKKARKLAEEKAARpecssqcKQRRQQM 741
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEA----LEAELDALQERREALQRLAEYSWDEIDVASAEREIAEL-------EAELERL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 742 DEEQ---KRLRSDLKQAEEAKQLAVEHGRKVEQEYRMLEAKLRNRESSQPDPEILLNALAAMqdknATLEKNLSAETRvk 818
Cdd:COG4913 681 DASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL----ARLELRALLEER-- 754
|
170 180 190
....*....|....*....|....*....|....*...
gi 442624369 819 ldlFSALGAAKRQIEIsdnhRRSKEDEVIDLKAKIAQL 856
Cdd:COG4913 755 ---FAAALGDAVEREL----RENLEERIDALRARLNRA 785
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
629-789 |
9.52e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 9.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 629 ADVKKYRAEISHMKQIENELRQKLDANLTSKSTLQAKQKecdDLEKRIQELNNARHadmlNLQTVERRLNEERRQKQSLD 708
Cdd:TIGR02169 350 KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK---DYREKLEKLKREIN----ELKRELDRLQEELQRLSEEL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 709 SQLSNE---KKARKLA-----EEKAARPECSSQ-CKQRRQQMDEEQKRLRSDlkqaeEAKQLAVEHG-RKVEQEYRMLEA 778
Cdd:TIGR02169 423 ADLNAAiagIEAKINEleeekEDKALEIKKQEWkLEQLAADLSKYEQELYDL-----KEEYDRVEKElSKLQRELAEAEA 497
|
170
....*....|.
gi 442624369 779 KLRNRESSQPD 789
Cdd:TIGR02169 498 QARASEERVRG 508
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
659-862 |
9.77e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 9.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 659 KSTLQAK---------QKECDDLEK---RIQELNNAR----HADMLNLQTVERRLNEERRQKQSLDSQLSNEKKARKLAE 722
Cdd:COG4717 36 KSTLLAFiramllerlEKEADELFKpqgRKPELNLKElkelEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 723 EKAARPECSSQC-------KQRRQQMDEEQKRLRSDLKQAEEAKQLavehgrkvEQEYRMLEAKlrnressqpdpeilln 795
Cdd:COG4717 116 EELEKLEKLLQLlplyqelEALEAELAELPERLEELEERLEELREL--------EEELEELEAE---------------- 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442624369 796 aLAAMQDKNATLEKNLSAETRVKL-DLFSALGAAKRQIEISDNHRRSKEDEVIDLKAKIAQLLAVMPD 862
Cdd:COG4717 172 -LAELQEELEELLEQLSLATEEELqDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
626-857 |
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 442624369 626 KLEADVKKYRAEISHMKQIENELRQKLDANLTSKST------LQAKQKECDDLEKRIQELNnarhADMLNLQTVERRLNE 699
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERREALQRLAEYswdeidVASAEREIAELEAELERLD----ASSDDLAALEEQLEE 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 700 ERRQKQSLDSQLsnekkarklaeekaarpecsSQCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEYrmLEAK 779
Cdd:COG4913 697 LEAELEELEEEL--------------------DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL--LEER 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 780 LRNressQPDPEILLNALAAMQDKNATLEKNLSAETRvklDLFSALGAAKRQ---------IEISDN------HRRSKED 844
Cdd:COG4913 755 FAA----ALGDAVERELRENLEERIDALRARLNRAEE---ELERAMRAFNREwpaetadldADLESLpeylalLDRLEED 827
|
250
....*....|...
gi 442624369 845 EVIDLKAKIAQLL 857
Cdd:COG4913 828 GLPEYEERFKELL 840
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
635-840 |
1.41e-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: 49.45 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 635 RAEISHMKQIENELRQKLDAnltSKSTLQAKQKECDDLEKRI----QELNNARHADMLNLQTVERrlNEERRQkqsldsQ 710
Cdd:pfam12128 589 RIDVPEWAASEEELRERLDK---AEEALQSAREKQAAAEEQLvqanGELEKASREETFARTALKN--ARLDLR------R 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 711 LSNEKKARKLAEEKAaRPECSSQCKQRRQQMDEEQKRLRSDLKQA-EEAKQLAVEHGRKVEQEYRMLEAKLRNRESSqpd 789
Cdd:pfam12128 658 LFDEKQSEKDKKNKA-LAERKDSANERLNSLEAQLKQLDKKHQAWlEEQKEQKREARTEKQAYWQVVEGALDAQLAL--- 733
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 442624369 790 peiLLNALAAMQDKNATLEKNLsaETRVKLDLfSALGA-----AKRQIEISDNHRR 840
Cdd:pfam12128 734 ---LKAAIAARRSGAKAELKAL--ETWYKRDL-ASLGVdpdviAKLKREIRTLERK 783
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
637-856 |
2.41e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 637 EISHMKQIENELRQKLDANLTSKSTLQAKQKECDDLEKRIQELNNARHADMLNLQTVERRLNEERRQKQSLDSQLSNEKK 716
Cdd:PRK03918 208 EINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 717 ARKLAEEKAARPECSSQCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEYRMLEAKLRNRESSQPDPEILLNA 796
Cdd:PRK03918 288 LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEA 367
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 797 LAAMQDKNaTLEKNLSAETRVKLdlfsalgaaKRQIEISDNHRRSKEDEVIDLKAKIAQL 856
Cdd:PRK03918 368 KAKKEELE-RLKKRLTGLTPEKL---------EKELEELEKAKEEIEEEISKITARIGEL 417
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
626-778 |
2.66e-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: 48.51 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 626 KLEADVKKYRAEISHMKQIENELRQKLDANLTSKSTLQA-----------KQKECDDLEKRIQELNNARHADMLNLQTVE 694
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEalallrseleeLSEELRELESKRSELRRELEELREKLAQLE 928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 695 RRLNEERRQKQSLDSQLSNEkkARKLAEEKAARPEcssQCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEYR 774
Cdd:TIGR02168 929 LRLEGLEVRIDNLQERLSEE--YSLTLEEAEALEN---KIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYD 1003
|
....
gi 442624369 775 MLEA 778
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 ... |
626-837 |
2.90e-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: 48.25 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 626 KLEADVKKYRAEISHMKQIENELR---QKLDANLTSKST-LQAKQKECDDLEKRIQELNNarhadmlNLQTVERRLNEER 701
Cdd:pfam01576 409 KLEGQLQELQARLSESERQRAELAeklSKLQSELESVSSlLNEAEGKNIKLSKDVSSLES-------QLQDTQELLQEET 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 702 RQKQSLDSQLsnekkaRKLAEEKAARpecssqckqrRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEYRMLEAKLR 781
Cdd:pfam01576 482 RQKLNLSTRL------RQLEDERNSL----------QEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEE 545
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 442624369 782 NRESSQPDPEillNALAAMQDKNATLEKNLSAETRVKLDLFSALGAAKRQIEISDN 837
Cdd:pfam01576 546 GKKRLQRELE---ALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSN 598
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
694-781 |
3.44e-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: 45.03 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 694 ERRLNEERRQKQSLDSQLSNEKKARKLAEEKAARPECSSQCKQRRQQMDEEQKRLRSdlKQAEEAKQLAVEHGRKVEQEY 773
Cdd:pfam05672 26 QREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAE--EEAEEREQREQEEQERLQKQK 103
|
....*...
gi 442624369 774 RMLEAKLR 781
Cdd:pfam05672 104 EEAEAKAR 111
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
638-787 |
3.71e-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: 47.81 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 638 ISHMKQIENELRQKLDANLTSKSTLQAKQKECDDLEKR--IQELNNARHADMLNLQTV---ERRLNEERRQKQSLDSQLS 712
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRrkLEEAEKARQAEMDRQAAIyaeQERMAMERERELERIRQEE 357
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442624369 713 NEKKARKLAEEKAARpECSSQCKQRRQQMDEEQK--RLRSDLKQAEEAKQLAVEHGRKVEQEYRMLEAKLRNRESSQ 787
Cdd:pfam17380 358 RKRELERIRQEEIAM-EISRMRELERLQMERQQKneRVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEAR 433
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
666-789 |
4.90e-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: 4.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 666 QKECDDLEKRIQElnnarHADMLNLQTVERRLNEERRQKQSLDSQLSNEKKARKLAEEKAARPECssqcKQRRQQMDEEQ 745
Cdd:pfam05672 26 QREREEQERLEKE-----EEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEA----EEREQREQEEQ 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 746 KRLRsdlKQAEEAKQLAVE-----------HGRKVEQEY-----RMLEAKLRNRESSQPD 789
Cdd:pfam05672 97 ERLQ---KQKEEAEAKAREeaerqrqerekIMQQEEQERlerkkRIEEIMKRTRKSDQAE 153
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
632-784 |
4.91e-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: 47.73 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 632 KKYRAEISHMKQIENELRQKLDANLTSK----STLQAKQKECDDLEKRIQElnnarhadmlNLQTVERRLNEERRQKQSL 707
Cdd:TIGR00606 948 EKVKNIHGYMKDIENKIQDGKDDYLKQKetelNTVNAQLEECEKHQEKINE----------DMRLMRQDIDTQKIQERWL 1017
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442624369 708 DSQLSNEKKARKLAEEKAARPECSSQCKQRR-QQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEYRMLEAKLRNRE 784
Cdd:TIGR00606 1018 QDNLTLRKRENELKEVEEELKQHLKEMGQMQvLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
609-860 |
5.61e-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: 47.42 E-value: 5.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 609 IANLASKVVSKICE-TCLKLEAD-VKKYRAEISHMK-------QIENELRQKLDaNLTS-----KSTLQAKQKECDDLEK 674
Cdd:pfam15921 519 ITKLRSRVDLKLQElQHLKNEGDhLRNVQTECEALKlqmaekdKVIEILRQQIE-NMTQlvgqhGRTAGAMQVEKAQLEK 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 675 RIqelnNARHADMLNLQTVERRLNEERRQKQSLDSQLSNEKKarKLAEEKAARPECSSQCKQRRQQMDEEQKRLRSDLKQ 754
Cdd:pfam15921 598 EI----NDRRLELQEFKILKDKKDAKIRELEARVSDLELEKV--KLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNS 671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 755 AEEAKQLAVEHGRKVEQEYRMLEAKLRNR-ESSQPDPEILLNALAAMQ--DKNAT-----LEKNLSAEtRVKLDlfsALG 826
Cdd:pfam15921 672 LSEDYEVLKRNFRNKSEEMETTTNKLKMQlKSAQSELEQTRNTLKSMEgsDGHAMkvamgMQKQITAK-RGQID---ALQ 747
|
250 260 270
....*....|....*....|....*....|....
gi 442624369 827 AAKRQIEISDNHRRSKEDEVIDLKAKIAQLLAVM 860
Cdd:pfam15921 748 SKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTV 781
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
618-783 |
6.32e-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: 47.09 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 618 SKICETCLK-LEADVKKYRAEIS----HMKQIE---NELRQKLDANLTSKSTLQAKQKEcddLEKRIQELNNARHADMLN 689
Cdd:pfam01576 828 SKESEKKLKnLEAELLQLQEDLAaserARRQAQqerDELADEIASGASGKSALQDEKRR---LEARIAQLEEELEEEQSN 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 690 LQTVERRLNEERRQKQSLDSQLSNEKKARKLAEekAARPECSSQCKQRRQQMDEEQKRLRSDLKQ---AEEAKQLAVEHG 766
Cdd:pfam01576 905 TELLNDRLRKSTLQVEQLTTELAAERSTSQKSE--SARQQLERQNKELKAKLQEMEGTVKSKFKSsiaALEAKIAQLEEQ 982
|
170
....*....|....*..
gi 442624369 767 RKVEQEYRMLEAKLRNR 783
Cdd:pfam01576 983 LEQESRERQAANKLVRR 999
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
688-858 |
7.01e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 688 LNLQTVERRLNEERRQKQSLDSQLSNEKKARKLAEEKAARpecssqCKQRRQQMDEEQKRLRSDLKQAEEakqlavehgR 767
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEA------AKTELEDLEKEIKRLELEIEEVEA---------R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 768 KVEQEYRMLEAKlRNRESsqpdpEILLNALAAMQDKNATLEKNLsaetrvkLDLFSALGAAKRQIEISDNHRRSKEDEVI 847
Cdd:COG1579 75 IKKYEEQLGNVR-NNKEY-----EALQKEIESLKRRISDLEDEI-------LELMERIEELEEELAELEAELAELEAELE 141
|
170
....*....|.
gi 442624369 848 DLKAKIAQLLA 858
Cdd:COG1579 142 EKKAELDEELA 152
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
622-847 |
7.95e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.64 E-value: 7.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 622 ETCLKLEADVKKYRAEISHMKQIENELRQKlDANLTSksTLQAKQKECDDLE--------------KRIQELNN------ 681
Cdd:pfam05483 408 EELKKILAEDEKLLDEKKQFEKIAEELKGK-EQELIF--LLQAREKEIHDLEiqltaiktseehylKEVEDLKTelekek 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 682 ------ARHADMLNLQTveRRLNEE--------RRQKQSLDSQLSNEKKARKLAE-----EKAARPECSSQCKQRRQQMD 742
Cdd:pfam05483 485 lknielTAHCDKLLLEN--KELTQEasdmtlelKKHQEDIINCKKQEERMLKQIEnleekEMNLRDELESVREEFIQKGD 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 743 EeqkrLRSDLKQAEEAKQLAVEHGRKVEQEYRMLEAKLRNR----ESSQPDPEILLNALAAMQDKNATLEKNLSA-ETRV 817
Cdd:pfam05483 563 E----VKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLkkqiENKNKNIEELHQENKALKKKGSAENKQLNAyEIKV 638
|
250 260 270
....*....|....*....|....*....|..
gi 442624369 818 -KLDLfsALGAAKRQI-EISDNHRRSKEDEVI 847
Cdd:pfam05483 639 nKLEL--ELASAKQKFeEIIDNYQKEIEDKKI 668
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
626-855 |
9.91e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 9.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 626 KLEADVKKYRAEISHMKQIENELRQKLDANLTSKSTLQAKQ-KECDDLEKRIQElnNARHADMLNLQTVERRLNEERRQK 704
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkKKADEAKKKAEE--DKKKADELKKAAAAKKKADEAKKK 1426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 705 QSldsQLSNEKKARKLAEEKAARPECSSQCKQRRQ----QMDEEQKRLRSDLK-------QAEEAKQLAVEHGRKVEQEY 773
Cdd:PTZ00121 1427 AE---EKKKADEAKKKAEEAKKADEAKKKAEEAKKaeeaKKKAEEAKKADEAKkkaeeakKADEAKKKAEEAKKKADEAK 1503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 774 RMLEAKLRNRESSQPDPEILLNALAAMQDKNATLEKNLSAETRVKLDLFSALGAAK-RQIEISDNHRRSKEDEVIDL-KA 851
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKaEEKKKAEEAKKAEEDKNMALrKA 1583
|
....
gi 442624369 852 KIAQ 855
Cdd:PTZ00121 1584 EEAK 1587
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
628-772 |
1.08e-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: 46.10 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 628 EADVKKYRAEISHMKQIENELRQKLDANLTSKstlQAKQKEcDDLEKRIQELNNARHADMLnlqtvERRLNEERRQKQsL 707
Cdd:pfam15709 388 EIRLRKQRLEEERQRQEEEERKQRLQLQAAQE---RARQQQ-EEFRRKLQELQRKKQQEEA-----ERAEAEKQRQKE-L 457
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442624369 708 DSQLSNE-KKARKLAEEKaaRPEcssqcKQRRQQMDEEQKRLRSDLK--QAEEAKQLAVEHGRKVEQE 772
Cdd:pfam15709 458 EMQLAEEqKRLMEMAEEE--RLE-----YQRQKQEAEEKARLEAEERrqKEEEAARLALEEAMKQAQE 518
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
642-856 |
1.15e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 642 KQIENELRQKLDANLTSKSTLQAKQKEcddlEKRIQELNNARHADMLNLQTVERRLNEERRQKQSLDSQLSNEKKA---- 717
Cdd:PTZ00121 1564 KKAEEAKKAEEDKNMALRKAEEAKKAE----EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVeqlk 1639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 718 RKLAEEKAARPECSSQCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEYRMLEAKLRNRESSQPDPEillNAL 797
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE---EKK 1716
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 798 AAMQDKNATLEKNLSAETrvkldlfsalgaAKRQIEisDNHRRSKEDEVID-LKAKIAQL 856
Cdd:PTZ00121 1717 KAEELKKAEEENKIKAEE------------AKKEAE--EDKKKAEEAKKDEeEKKKIAHL 1762
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
625-867 |
1.23e-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: 46.12 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 625 LKLEADVKKYRAEISHMKQIENELR----QKLDANLTSKSTLQAKQKECDDLEKR----IQELNNARHADMLNLQTVERR 696
Cdd:pfam02463 771 LKEKELAEEREKTEKLKVEEEKEEKlkaqEEELRALEEELKEEAELLEEEQLLIEqeekIKEEELEELALELKEEQKLEK 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 697 LNEErRQKQSLDSQLSNEKKARKLAEEKAARPECSsqcKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEYRML 776
Cdd:pfam02463 851 LAEE-ELERLEEEITKEELLQELLLKEEELEEQKL---KDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEE 926
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 777 EAKLRNRESSQPDPEILLNALAAMQDKNATLEKNLSAETRVKLDLFSALGAAKRQIEISDNHRRSKED-EVIDLKAKIAQ 855
Cdd:pfam02463 927 AEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDElEKERLEEEKKK 1006
|
250
....*....|..
gi 442624369 856 LLAVMPDNLCMN 867
Cdd:pfam02463 1007 LIRAIIEETCQR 1018
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
631-839 |
1.36e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.20 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 631 VKKYRAEISHMKQIENELRQKLDANLTSKSTLQAKQKeCDDLEKRI---------------QELNNARH-ADMLNL---- 690
Cdd:PRK10929 67 AKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMS-TDALEQEIlqvssqlleksrqaqQEQDRAREiSDSLSQlpqq 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 691 QTVERR-LNEERRQKQSLDSQLSNEKKARKLA--EEKAARP------ECSSQCKQRRQqmdeEQKRLRSDLKQaeeakql 761
Cdd:PRK10929 146 QTEARRqLNEIERRLQTLGTPNTPLAQAQLTAlqAESAALKalvdelELAQLSANNRQ----ELARLRSELAK------- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 762 avehgRKVEQEYRMLEAkLRNRESS--QPDPEILLNALAAMQDKNATLEKNLSAETRVKLDLFSALG-AAKRQIEISDNH 838
Cdd:PRK10929 215 -----KRSQQLDAYLQA-LRNQLNSqrQREAERALESTELLAEQSGDLPKSIVAQFKINRELSQALNqQAQRMDLIASQQ 288
|
.
gi 442624369 839 R 839
Cdd:PRK10929 289 R 289
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
627-864 |
1.61e-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: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 627 LEADVKKYRAEISHMKQIEnELRQKLDANLTSKSTLQA---------KQKECDDLEKRIQELnnarhadmlnlqtverrl 697
Cdd:COG4913 240 AHEALEDAREQIELLEPIR-ELAERYAAARERLAELEYlraalrlwfAQRRLELLEAELEEL------------------ 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 698 neeRRQKQSLDSQLSNEKKARKLAEEKAARPEcssqcKQRRQQMDEEQKRLRSDLKQAEEAKqlavehgRKVEQEYRMLE 777
Cdd:COG4913 301 ---RAELARLEAELERLEARLDALREELDELE-----AQIRGNGGDRLEQLEREIERLEREL-------EERERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 778 AKLRNRESSQP-DPEILLNALAAMQDKNATLEKNLSAETRVKLDLFSALGAAKRQI-----EISD-NHRRSK-EDEVIDL 849
Cdd:COG4913 366 ALLAALGLPLPaSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELreleaEIASlERRKSNiPARLLAL 445
|
250
....*....|....*
gi 442624369 850 KAKIAQLLAVMPDNL 864
Cdd:COG4913 446 RDALAEALGLDEAEL 460
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
626-786 |
1.81e-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: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 626 KLEADVKKYRAEISHMKQIENELRQKLDANL--------TSKSTLQAKQKECDDLEKRIQELNNARHADMLNLQTVERRL 697
Cdd:COG4942 80 ALEAELAELEKEIAELRAELEAQKEELAELLralyrlgrQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 698 NEERRQKQSLDSQLsnEKKARKLAEEKAARPECSSQCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEYRMLE 777
Cdd:COG4942 160 AELAALRAELEAER--AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
....*....
gi 442624369 778 AKLRNRESS 786
Cdd:COG4942 238 AAAERTPAA 246
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
694-840 |
1.95e-04 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 45.42 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 694 ERRLNeeRRQKQsldsQLSNEKKARKLAEEKAARpecSSQCKQRRQQMDEEQKRlRSDLK--QAEEAKQLAVEHGRKVEQ 771
Cdd:PRK10811 638 ENRRN--RRQAQ----QQTAETRESQQAEVTEKA---RTQDEQQQAPRRERQRR-RNDEKrqAQQEAKALNVEEQSVQET 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 772 EY-------------RMLEAKLRnRESSQPDPEILLNALAAMQDKNATLEKNLSAETRVKLDLFSALGAAKRQIEISDNH 838
Cdd:PRK10811 708 EQeervqqvqprrkqRQLNQKVR-IEQSVAEEAVAPVVEETVAAEPVVQEVPAPRTELVKVPLPVVAQTAPEQDEENNAE 786
|
..
gi 442624369 839 RR 840
Cdd:PRK10811 787 NR 788
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
626-785 |
2.02e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 626 KLEADVKKYRAEISHMKQIENeLRQKLdanltskstlqaKQKECDDLEKRIQELNNARhadmlnlQTVERRLNEERRQKQ 705
Cdd:PRK03918 356 ELEERHELYEEAKAKKEELER-LKKRL------------TGLTPEKLEKELEELEKAK-------EEIEEEISKITARIG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 706 SLDSQLSNEKKArkLAEEKAARPECSSqCkqRRQQMDEEQKRL----RSDLKQAEEAKQLAVEHGRKVEQEYRMLEaKLR 781
Cdd:PRK03918 416 ELKKEIKELKKA--IEELKKAKGKCPV-C--GRELTEEHRKELleeyTAELKRIEKELKEIEEKERKLRKELRELE-KVL 489
|
....
gi 442624369 782 NRES 785
Cdd:PRK03918 490 KKES 493
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
635-787 |
2.08e-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: 45.33 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 635 RAEISHMKQIENELRQKLDAnltSKSTLQAKQKECDDLEKRIQELNNARHADMLNL----QTVERRLNEERRQKQSLDSQ 710
Cdd:pfam15709 339 RAERAEMRRLEVERKRREQE---EQRRLQQEQLERAEKMREELELEQQRRFEEIRLrkqrLEEERQRQEEEERKQRLQLQ 415
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442624369 711 LSNEKkARKLAEEkaARPECssQCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQ-EYRMLEAKLRNRESSQ 787
Cdd:pfam15709 416 AAQER-ARQQQEE--FRRKL--QELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMaEEERLEYQRQKQEAEE 488
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
645-858 |
3.17e-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: 44.78 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 645 ENELRQKLDANLTSKSTLQAKQKECDDLEKRIQELNNARHADMLNLQT----------------------------VERR 696
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAetelcaeaeemrarlaarkqeleeilheLESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 697 LNEERRQKQsldsQLSNEKK---------ARKLAEEKAArpecssqckqrRQQMDEEQKRLRSDLKQAEEAKQLAVEHGR 767
Cdd:pfam01576 84 LEEEEERSQ----QLQNEKKkmqqhiqdlEEQLDEEEAA-----------RQKLQLEKVTTEAKIKKLEEDILLLEDQNS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 768 KVEQEYRMLEAKLRNRESSQPDPEILLNALAAMQDKN----ATLEKNLSAETRVKLDlfsaLGAAKRQI--EISDNHrrs 841
Cdd:pfam01576 149 KLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHeamiSDLEERLKKEEKGRQE----LEKAKRKLegESTDLQ--- 221
|
250
....*....|....*..
gi 442624369 842 keDEVIDLKAKIAQLLA 858
Cdd:pfam01576 222 --EQIAELQAQIAELRA 236
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
627-833 |
3.49e-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: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 627 LEADVKKYRAEISHMKQIENELRQKLDANltskstlQAKQKECDDLEKRIQELNNARHADMLNLQTVERRLNEERRQKQS 706
Cdd:pfam19220 36 IEAILRELPQAKSRLLELEALLAQERAAY-------GKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 707 LDSQLSnEKKARKLAEEKAARPEcssqcKQRRQQMDEEQKRLRSDLKQAEEAKQlAVEHGRKVEQEYRMLEA----KLRN 782
Cdd:pfam19220 109 LRIELR-DKTAQAEALERQLAAE-----TEQNRALEEENKALREEAQAAEKALQ-RAEGELATARERLALLEqenrRLQA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 783 RESSQPDpEI---------LLNALAAMQDKNATLEKNLSAETrvkldlfSALGAAKRQIE 833
Cdd:pfam19220 182 LSEEQAA-ELaeltrrlaeLETQLDATRARLRALEGQLAAEQ-------AERERAEAQLE 233
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
626-781 |
3.92e-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: 43.75 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 626 KLEADVKKYRAEISHMKQIENELRQKLDANLtsKSTLQAKQKECDDLEKRIQELNNARHADMLNLQTVERRLNEERRQKQ 705
Cdd:pfam13868 127 QLREEIDEFNEEQAEWKELEKEEEREEDERI--LEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERD 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 706 SLDSQL---SNEKKARKLAEEKAARP--ECSSQCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEYRMLEAKL 780
Cdd:pfam13868 205 ELRAKLyqeEQERKERQKEREEAEKKarQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKR 284
|
.
gi 442624369 781 R 781
Cdd:pfam13868 285 R 285
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
626-789 |
4.13e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 626 KLEADVKKYRAEISHMKQIENELRQKLDANLTSKSTLQAKQKeCDDLEKRIQElnnARHADmlnlqtvERRLNEERRQKQ 705
Cdd:PTZ00121 1289 KKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKK-ADAAKKKAEE---AKKAA-------EAAKAEAEAAAD 1357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 706 SLDSQLSNEKKARKLAEEKAARPECSSQCKQRRQQMDEEQKRLRSDLKQAEE------AKQLAVEHGRKVEQEYRMLEAK 779
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADElkkaaaAKKKADEAKKKAEEKKKADEAK 1437
|
170
....*....|
gi 442624369 780 LRNRESSQPD 789
Cdd:PTZ00121 1438 KKAEEAKKAD 1447
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
662-864 |
4.85e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 662 LQAKQKECDDLEKRIQELNNArhadmlnLQTVERRLNEERRQKQSLDSQLSNEKKARKLAEEKAArpecssQCKQRRQQM 741
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAE-------LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE------EVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 742 DEEQKRLRS--DLKQAEeaKQLAVEHGRKVEQEYRMLEAkLRNRESSQpdpeillNALAAMQDKNATLEKNLSAETrvkl 819
Cdd:COG1579 79 EEQLGNVRNnkEYEALQ--KEIESLKRRISDLEDEILEL-MERIEELE-------EELAELEAELAELEAELEEKK---- 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 442624369 820 dlfsalgaAKRQIEISDnhrrsKEDEVIDLKAKIAQLLAVMPDNL 864
Cdd:COG1579 145 --------AELDEELAE-----LEAELEELEAEREELAAKIPPEL 176
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
625-799 |
5.02e-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: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 625 LKLEADVKKYRAEISHMKQIENELRQKLDANLTSKSTLQAKQKECDDLEKRIQELNNARHADMLN-LQTVERRLNEERRQ 703
Cdd:COG4913 281 LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEReIERLERELEERERR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 704 KQSLDSQ-----LSNEKKARKLAEEKAarpecssQCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEyrmLEA 778
Cdd:COG4913 361 RARLEALlaalgLPLPASAEEFAALRA-------EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE---IAS 430
|
170 180
....*....|....*....|..
gi 442624369 779 kLRNRESSQPDPEI-LLNALAA 799
Cdd:COG4913 431 -LERRKSNIPARLLaLRDALAE 451
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
642-791 |
7.55e-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: 43.51 E-value: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 642 KQIENELRQKLDANLTSKSTLQAKQKECDDLE--KRIQELNNARHADMlnlQTVERRLNEERRQKQSLDSQLSNEKKARK 719
Cdd:pfam04747 28 KSQRNQFRQWLLTAVLPNSINDQRKEAFASLEltEQPQQVEKVKKSEK---KKAQKQIAKDHEAEQKVNAKKAAEKEARR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 720 L---AEEKAARPECSSQCKQRRQQMDEEQKRLRSDLK--QAEEAKQLAV--EHGRKVEQ----------EYRMLEAKLRN 782
Cdd:pfam04747 105 AeaeAKKRAAQEEEHKQWKAEQERIQKEQEKKEADLKklQAEKKKEKAVkaEKAEKAEKtkkastpapvEEEIVVKKVAN 184
|
....*....
gi 442624369 783 RESSQPDPE 791
Cdd:pfam04747 185 DRSAAPAPE 193
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
626-784 |
8.52e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.14 E-value: 8.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 626 KLEADVKKYRAEISHM----KQIENELRQKLDANLtskstlqaKQKECDDLE-----------KRIQE----LNNARHAD 686
Cdd:PRK11637 100 QLNKQIDELNASIAKLeqqqAAQERLLAAQLDAAF--------RQGEHTGLQlilsgeesqrgERILAyfgyLNQARQET 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 687 MLNLQTVERRLNEERR---QKQSLDSQLSNEKKAR--KLAEEKAAR----PECSSQCKQRRQQMDEEQK---RLRSDLKQ 754
Cdd:PRK11637 172 IAELKQTREELAAQKAeleEKQSQQKTLLYEQQAQqqKLEQARNERkktlTGLESSLQKDQQQLSELRAnesRLRDSIAR 251
|
170 180 190
....*....|....*....|....*....|..
gi 442624369 755 AE-EAKQLAvehgrkvEQEYRmlEA-KLRNRE 784
Cdd:PRK11637 252 AErEAKARA-------EREAR--EAaRVRDKQ 274
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
628-784 |
9.31e-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: 9.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 628 EADVKKYRAEISHMKQIE-NELRQKLDANltskstlQAKQKECDDL-EKRIQElNNARHADMLNLQTVERRLNEERRQKQ 705
Cdd:pfam13868 168 EEEREAEREEIEEEKEREiARLRAQQEKA-------QDEKAERDELrAKLYQE-EQERKERQKEREEAEKKARQRQELQQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 706 SLDSQLsnEKKARKLAEEKA------ARPECSSQCKQRRQQMDEEQKRLRSD------LKQAEEAKQLAVEHGRKVEQEY 773
Cdd:pfam13868 240 AREEQI--ELKERRLAEEAEreeeefERMLRKQAEDEEIEQEEAEKRRMKRLehrrelEKQIEEREEQRAAEREEELEEG 317
|
170
....*....|.
gi 442624369 774 RMLEAKLRNRE 784
Cdd:pfam13868 318 ERLREEEAERR 328
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
642-792 |
1.03e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 642 KQIENELRQKLDANLTSKSTLQAKQKECDDLEKRIQElnnARHADMLNLQTVERRLNEERRQKQSLDSQLSNE------K 715
Cdd:PTZ00121 1277 ARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE---AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEaakaeaE 1353
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442624369 716 KARKLAEEKAARPECSSQCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEYRMLEAKLRNRESSQPDPEI 792
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEK 1430
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
694-855 |
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 442624369 694 ERRLNEERRQKQSLdsqlsnekkARKLAEEKAARPECSSQCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQEY 773
Cdd:pfam07888 33 QNRLEECLQERAEL---------LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 774 RMLEaklRNRESSQPDPEILLNALAAMQDKNATLEKNLSAETRVKLDLFSALGAAKRQIEISDNHRRSKEDEVIDLKAKI 853
Cdd:pfam07888 104 KELS---ASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKL 180
|
..
gi 442624369 854 AQ 855
Cdd:pfam07888 181 QQ 182
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
626-858 |
1.24e-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: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 626 KLEADVKKYRAEIshmkqieNELRQKLDANLTSKSTLQakqKECDDLEKRIQELNNARHADMLNLQTVERRLNEERRQKQ 705
Cdd:COG4942 24 EAEAELEQLQQEI-------AELEKELAALKKEEKALL---KQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 706 SLDSQLSNEKKArkLAEEKAARpecssqckQRRQQMDEEQKRLRS-DLKQAEEAKQLAVEHGRKVEQEYRMLEAKLRNRE 784
Cdd:COG4942 94 ELRAELEAQKEE--LAELLRAL--------YRLGRQPPLALLLSPeDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442624369 785 SSQPDPEILLNALAAMQDKNATLEKNLSAETRVKLDLFSALgaaKRQIEISDNHRRSKEDEVIDLKAKIAQLLA 858
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARL---EKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
622-763 |
1.25e-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: 40.42 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 622 ETCLKLEADVKKYRAEISHMK--QIENELRQKLDAnltskstlqAKQKecddLEKRI-QELNNARHADmlnLQTVERRLN 698
Cdd:pfam15346 11 ETARRVEEAVAKRVEEELEKRkdEIEAEVERRVEE---------ARKI----MEKQVlEELEREREAE---LEEERRKEE 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 699 EERRQKQSLDSQL-SNEKKA----RKLAEEKAARPEcssqckqRRQQMDEEQKRLRSDLKQAEEAKQLAV 763
Cdd:pfam15346 75 EERKKREELERILeENNRKIeeaqRKEAEERLAMLE-------EQRRMKEERQRREKEEEEREKREQQKI 137
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
632-760 |
1.34e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.80 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 632 KKYRAEISHMKQIENELRQKLDANLTSKSTLQAKQKECDDLEKRIQELNNARHADmlnlqtverrlnEERRQKQSLDSQL 711
Cdd:pfam17380 485 DRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAE------------EERRKQQEMEERR 552
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 442624369 712 SNEKKARKLAEEKAarpecssqckqRRQQMDEEQKRLRSdLKQAEEAKQ 760
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 ... |
677-845 |
1.63e-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: 42.47 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 677 QELNNARHADMLNLQTV---ERRLNE----ERRQKQS-----LDSQLSNEKKArKLAEEKAarpecssqckqrRQQMDEE 744
Cdd:pfam01576 319 QELRSKREQEVTELKKAleeETRSHEaqlqEMRQKHTqaleeLTEQLEQAKRN-KANLEKA------------KQALESE 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 745 QKRLRSDLKQAEEAKQlAVEHGR-KVEQEYRMLEAKLRNRESS-----------QPDPEILLNALAAMQDKNATLEKNLS 812
Cdd:pfam01576 386 NAELQAELRTLQQAKQ-DSEHKRkKLEGQLQELQARLSESERQraelaeklsklQSELESVSSLLNEAEGKNIKLSKDVS 464
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 442624369 813 A--------------ETRVKLDLFSALgaakRQIEISDNHRRSKEDE 845
Cdd:pfam01576 465 SlesqlqdtqellqeETRQKLNLSTRL----RQLEDERNSLQEQLEE 507
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
625-846 |
1.63e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 625 LKLEADVKKYRAEISHMKQIE----NELRQKLDANLTSKSTLQAKQKEcddLEKRIQELNNARHADMLNLQTVERRLNEE 700
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEkkkaEELKKAEEENKIKAAEEAKKAEE---DKKKAEEAKKAEEDEKKAAEALKKEAEEA 1701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 701 RRQKQSLDSQLSNEKKARKLAEEKAARPECSSQCKQRrqqmDEEQKRLRSDLKQAEEAK----QLAVEHGRKVEQEYRML 776
Cdd:PTZ00121 1702 KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE----AEEDKKKAEEAKKDEEEKkkiaHLKKEEEKKAEEIRKEK 1777
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 777 EAKLRnRESSQPDPEILLNALAAMQD------------KNATLEKNLSAETRVkldlfsalgAAKRQIEISDNHRRSKED 844
Cdd:PTZ00121 1778 EAVIE-EELDEEDEKRRMEVDKKIKDifdnfaniieggKEGNLVINDSKEMED---------SAIKEVADSKNMQLEEAD 1847
|
..
gi 442624369 845 EV 846
Cdd:PTZ00121 1848 AF 1849
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
626-771 |
1.83e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 626 KLEADVKKYRAEISHMKQIENELRQKLDANLTSKSTLQAKQKECDDLEKRIQELNNARHADMLNLQTVERRLNEERRQKQ 705
Cdd:COG1340 47 ELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQ 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 706 SLDSQLSNEK----KARKLAEEkaarpecssqcKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRKVEQ 771
Cdd:COG1340 127 TEVLSPEEEKelveKIKELEKE-----------LEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKE 185
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
659-836 |
1.85e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.72 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 659 KSTLQAKQKECDDLEKRIQELNNARHADMLNLQTVER-RLNEERRQKQSLDsQLSNEKKARKLAEEKAARpecssQCKQR 737
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKeRLAAQEQKKQAEE-AAKQAALKQKQAEEAAAK-----AAAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 738 RQQMDEEQKRLRSDLKQAEE--AKQLAVEHGRKVEQEYRM---LEAKLRNRESSQPDPEILLNALAAMQDK--------- 803
Cdd:PRK09510 146 KAKAEAEAKRAAAAAKKAAAeaKKKAEAEAAKKAAAEAKKkaeAEAAAKAAAEAKKKAEAEAKKKAAAEAKkkaaaeaka 225
|
170 180 190
....*....|....*....|....*....|....*.
gi 442624369 804 ---NATLEKNLSAETRVKLDLFSALGAAKRQIEISD 836
Cdd:PRK09510 226 aaaKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDD 261
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
627-835 |
1.91e-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: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 627 LEADVKKYRAEIShmkQIENELRQKLDANLTSKSTLQAKQkecddLEKRIQELNNArhadmlnLQTVERRLNEERRQKQS 706
Cdd:COG3206 180 LEEQLPELRKELE---EAEAALEEFRQKNGLVDLSEEAKL-----LLQQLSELESQ-------LAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 707 LDSQLSNEKKARKLAEEKAARPECSSQCKQRRQQMDEEQKRLRSD-------LKQAEEAKQLAVEHGRKVEQEYRMLEAK 779
Cdd:COG3206 245 LRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNhpdvialRAQIAALRAQLQQEAQRILASLEAELEA 324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442624369 780 LRNRESSqpdpeiLLNALAAMQDKNATLEK------NLSAETRVKLDLFSALGAAKRQIEIS 835
Cdd:COG3206 325 LQAREAS------LQAQLAQLEARLAELPEleaelrRLEREVEVARELYESLLQRLEEARLA 380
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
661-828 |
2.19e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.49 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 661 TLQAKQKECDDLEKRIQELnnarhADMLNLqtverrlneERRQKQSLDSQLSNEKkarklAEEKAARPEcssqcKQRRQQ 740
Cdd:PRK09039 47 EISGKDSALDRLNSQIAEL-----ADLLSL---------ERQGNQDLQDSVANLR-----ASLSAAEAE-----RSRLQA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 741 MDEEQKRLRSDL--------KQAEEAKQLAVEHGRKVEQEYRMLEAkLRNRessqpdpeilLNALAAMQDknatLEKNLS 812
Cdd:PRK09039 103 LLAELAGAGAAAegragelaQELDSEKQVSARALAQVELLNQQIAA-LRRQ----------LAALEAALD----ASEKRD 167
|
170
....*....|....*..
gi 442624369 813 AETRVKL-DLFSALGAA 828
Cdd:PRK09039 168 RESQAKIaDLGRRLNVA 184
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
627-853 |
2.49e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 627 LEADVKKYRAEISHMKQIENELRQKLDAnltSKSTLQA---KQKECDDLEKRIQELNNARHADMLNLQTVERRLNEERRQ 703
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDE---ADEVLEEheeRREELETLEAEIEDLRETIAETEREREELAEEVRDLRER 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 704 KQSLDSQLSN---------------EKKARKLAEEKAARPECSSQCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGRK 768
Cdd:PRK02224 288 LEELEEERDDllaeaglddadaeavEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 769 VEQEYRMLEAKLRNRESsqpdpeillnALAAMQDKNATLEKNLsAETRVKLDlfsalGAAKRQIEISDNHRRSKEDEViD 848
Cdd:PRK02224 368 LESELEEAREAVEDRRE----------EIEELEEEIEELRERF-GDAPVDLG-----NAEDFLEELREERDELREREA-E 430
|
....*
gi 442624369 849 LKAKI 853
Cdd:PRK02224 431 LEATL 435
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
609-782 |
2.62e-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: 41.58 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 609 IANLASKVVSKICETCLKLEA-------------DVKKYRAEISHMKQIENELRQKLDAnltsKSTLQAKQKECDDLEKR 675
Cdd:pfam13166 288 LQKLIEKVESAISSLLAQLPAvsdlasllsafelDVEDIESEAEVLNSQLDGLRRALEA----KRKDPFKSIELDSVDAK 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 676 IQELNNArhadmlnLQTVERRLNEERRQKQSLDSqlsNEKKARKlaeekAARPECSSQCKQRRQQMDEEQKRLRSDLKQA 755
Cdd:pfam13166 364 IESINDL-------VASINELIAKHNEITDNFEE---EKNKAKK-----KLRLHLVEEFKSEIDEYKDKYAGLEKAINSL 428
|
170 180
....*....|....*....|....*..
gi 442624369 756 EEAKQLAVEHGRKVEQEYRMLEAKLRN 782
Cdd:pfam13166 429 EKEIKNLEAEIKKLREEIKELEAQLRD 455
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
626-857 |
2.63e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.06 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 626 KLEADVKKYRAEISHMKQ-IENELRQKLDAnltsKSTLQAKQKECD-------DLEKRIQELNnarhaDMLNLQtveRRL 697
Cdd:pfam00038 72 RLQLELDNLRLAAEDFRQkYEDELNLRTSA----ENDLVGLRKDLDeatlarvDLEAKIESLK-----EELAFL---KKN 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 698 NEER---RQKQSLDSQLSNEKKArklaeekAARPECSSQCKQRRQQMDEEQKRLRSDLK-----QAEEAKQLAVEHGRKV 769
Cdd:pfam00038 140 HEEEvreLQAQVSDTQVNVEMDA-------ARKLDLTSALAEIRAQYEEIAAKNREEAEewyqsKLEELQQAAARNGDAL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 770 EQ------EYRMleaKLRNRESSqpdpeillnaLAAMQDKNATLEKNLsAETRVKLDLfsALGAAKRQIEisdnhrrSKE 843
Cdd:pfam00038 213 RSakeeitELRR---TIQSLEIE----------LQSLKKQKASLERQL-AETEERYEL--QLADYQELIS-------ELE 269
|
250
....*....|....
gi 442624369 844 DEVIDLKAKIAQLL 857
Cdd:pfam00038 270 AELQETRQEMARQL 283
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
627-856 |
2.87e-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: 41.54 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 627 LEADVKKYRAEISHMKQIENELRQKLDANLTSKSTLQAKQKECDDLEKRIQELNNARHADMLNLQTVERRLNEERRQKQS 706
Cdd:TIGR04523 171 LENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 707 LDSQLSNEK----KARKLAEEKaarpecSSQCKQRRQQMDEEQKRLR------SDLKQAEEA---KQLAvEHGRKVEQEY 773
Cdd:TIGR04523 251 TQTQLNQLKdeqnKIKKQLSEK------QKELEQNNKKIKELEKQLNqlkseiSDLNNQKEQdwnKELK-SELKNQEKKL 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 774 RMLEAKLRNRESSqpdpeilLNALaamQDKNATLEKNLSAETRVKLDLFSALGAAKRQIEISDNHRRSKEDEVIDLKAKI 853
Cdd:TIGR04523 324 EEIQNQISQNNKI-------ISQL---NEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI 393
|
...
gi 442624369 854 AQL 856
Cdd:TIGR04523 394 NDL 396
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
618-833 |
2.88e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 618 SKICETCLKLEADVKKYRAEISHMKQIENELRQKLDanltskstlqaKQKECDDLEKRIQELNNARHADMLNLQTVERRL 697
Cdd:PRK02224 464 SPHVETIEEDRERVEELEAELEDLEEEVEEVEERLE-----------RAEDLVEAEDRIERLEERREDLEELIAERRETI 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 698 NEERRQKQSLDSQLSN--------EKKARKLAEEKAARPECSSQCKQRRQQMDEEQKRL---RSDLKQAEEAKQLAVEHG 766
Cdd:PRK02224 533 EEKRERAEELRERAAEleaeaeekREAAAEAEEEAEEAREEVAELNSKLAELKERIESLeriRTLLAAIADAEDEIERLR 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 767 RKVEQ------EYRMLEAKLRNREsSQPDPEILLNALAAMQDKNATLEK-------NLSAETRVKLDLFSALGAAKRQIE 833
Cdd:PRK02224 613 EKREAlaelndERRERLAEKRERK-RELEAEFDEARIEEAREDKERAEEyleqveeKLDELREERDDLQAEIGAVENELE 691
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
689-786 |
3.19e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 689 NLQTVERRLNEERRQKQSLDSQLSN-EKKARKLAEEKAARPECSSQCKQRRQQMDEEQKRLRSDLKQAEEAKQLAVEHGR 767
Cdd:PRK03918 166 NLGEVIKEIKRRIERLEKFIKRTENiEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEK 245
|
90 100
....*....|....*....|..
gi 442624369 768 ---KVEQEYRMLEAKLRNRESS 786
Cdd:PRK03918 246 eleSLEGSKRKLEEKIRELEER 267
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
642-774 |
3.22e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 642 KQIENELRQKLDA------NLTSKSTLQAKQKECD---DLEKRIQELNNarhadmlNLQTVERRLneeRRQKQSLDSQLS 712
Cdd:PRK12704 34 KEAEEEAKRILEEakkeaeAIKKEALLEAKEEIHKlrnEFEKELRERRN-------ELQKLEKRL---LQKEENLDRKLE 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442624369 713 N-EKKARKLAEEKaarpecsSQCKQRRQQMDEEQKRLRSDLKQ------------AEEAKQLAVEhgrKVEQEYR 774
Cdd:PRK12704 104 LlEKREEELEKKE-------KELEQKQQELEKKEEELEELIEEqlqelerisgltAEEAKEILLE---KVEEEAR 168
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
663-804 |
3.86e-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: 40.67 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 663 QAKQKECDDLEKRIQELNNARHADMLNLQTV-ERRLNEERRQ-KQSLDSQLSNEKKARKLAEEKAARPECSSQCKQRRQQ 740
Cdd:pfam13868 32 KRIKAEEKEEERRLDEMMEEERERALEEEEEkEEERKEERKRyRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 741 MDEE---------QKRLRSDLKQAEEAKQL---------------AVEHGRKVEQEYRMLEAKLRNRESSQpdpEILLNA 796
Cdd:pfam13868 112 EEDQaeaeeklekQRQLREEIDEFNEEQAEwkelekeeereederILEYLKEKAEREEEREAEREEIEEEK---EREIAR 188
|
....*...
gi 442624369 797 LAAMQDKN 804
Cdd:pfam13868 189 LRAQQEKA 196
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
626-703 |
4.56e-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: 38.72 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 626 KLEADVKKYRAEIshmKQIENELRQKL-----DANLTSKSTLQAKQKECDDLEKRIQELNNARHADMlnlqtvERRLNEE 700
Cdd:smart00935 22 QLEKEFKKRQAEL---EKLEKELQKLKeklqkDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDL------QKRQQEE 92
|
...
gi 442624369 701 RRQ 703
Cdd:smart00935 93 LQK 95
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
626-703 |
4.65e-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: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 626 KLEADVKKYRAEIshmKQIENELRQKL-----DANLTSKSTLQAKQKECDDLEKRIQELNNARHADMlnlqtvERRLNEE 700
Cdd:COG2825 47 KLEKEFKKRQAEL---QKLEKELQALQeklqkEAATLSEEERQKKERELQKKQQELQRKQQEAQQDL------QKRQQEL 117
|
...
gi 442624369 701 RRQ 703
Cdd:COG2825 118 LQP 120
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
702-772 |
5.04e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.56 E-value: 5.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442624369 702 RQKQSLDSQLSNEKKARKLAEEKAARPECSSQCKQRRQQMDEEQK-RLRSDLKQAEEAKQLAVEHGRKVEQE 772
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERlAAQEQKKQAEEAAKQAALKQKQAEEA 137
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
694-781 |
5.08e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 40.62 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 694 ERRLNEERRQKQSLDSQLSnEKKARKLAEEKAARPECSSQCKQRRQQMDEEQKRlrsdLKQAEEAKQLAVEHGR---KVE 770
Cdd:pfam02029 247 EQKLEELRRRRQEKESEEF-EKLRQKQQEAELELEELKKKREERRKLLEEEEQR----RKQEEAERKLREEEEKrrmKEE 321
|
90
....*....|.
gi 442624369 771 QEYRMLEAKLR 781
Cdd:pfam02029 322 IERRRAEAAEK 332
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
641-761 |
6.11e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 39.90 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 641 MKQIENELRQKLDAnLTSKSTLQAKQKecddLEKRIQELNNA--RHADMLnlQTVERRLNEERRQKQSLDSQLSNEKKA- 717
Cdd:pfam00038 168 LTSALAEIRAQYEE-IAAKNREEAEEW----YQSKLEELQQAaaRNGDAL--RSAKEEITELRRTIQSLEIELQSLKKQk 240
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 442624369 718 ----RKLAEEKAARPECSSQCKQRRQQMDEEQKRLRSDL-KQAEEAKQL 761
Cdd:pfam00038 241 asleRQLAETEERYELQLADYQELISELEAELQETRQEMaRQLREYQEL 289
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
626-793 |
6.14e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 6.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 626 KLEADVKKYRAEISHMKQIENELRQKLDANLTSKSTLQAKQKEcddLEKRIQELNNarhadmlNLQTVERRLNEERRQK- 704
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKR---LELEIEEVEA-------RIKKYEEQLGNVRNNKe 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 705 -QSLDSQLSNEKKARKLAEEK-----AARPECSSQCKQRRQQMDEEQKRLRSdlKQAEEAKQLAvehgrKVEQEYRMLEA 778
Cdd:COG1579 91 yEALQKEIESLKRRISDLEDEilelmERIEELEEELAELEAELAELEAELEE--KKAELDEELA-----ELEAELEELEA 163
|
170
....*....|....*
gi 442624369 779 KlRNRESSQPDPEIL 793
Cdd:COG1579 164 E-REELAAKIPPELL 177
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
670-856 |
8.02e-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: 8.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 670 DDLEKRIQELNNArHADMLNLQTVERRLNEERRQKQSLDSQLSNEKKARKLAEekAARPECSSQckqRRQQMDEEQKRLR 749
Cdd:COG4913 228 DALVEHFDDLERA-HEALEDAREQIELLEPIRELAERYAAARERLAELEYLRA--ALRLWFAQR---RLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 750 SDLKQAEEAKQLAVEHGRKVEQEYRMLEAKLRNRESSQPDPeiLLNALAAMQDKNATLEKNLSA-ETRVK-LDL------ 821
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ--LEREIERLERELEERERRRARlEALLAaLGLplpasa 379
|
170 180 190
....*....|....*....|....*....|....*...
gi 442624369 822 --FSAL-GAAKRQIEISDNHRRSKEDEVIDLKAKIAQL 856
Cdd:COG4913 380 eeFAALrAEAAALLEALEEELEALEEALAEAEAALRDL 417
|
|
| ALIX_LYPXL_bnd |
pfam13949 |
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ... |
670-811 |
8.07e-03 |
|
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV p9Gag to this domain is necessary for viral budding.This domain is generally central between an N-terminal Bro1 domain, pfam03097 and a C-terminal proline-rich domain. The retroviruses thus used this domain to hijack the ESCRT system of the cell.
Pssm-ID: 464053 [Multi-domain] Cd Length: 294 Bit Score: 39.53 E-value: 8.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 670 DDLEKRIQELNNARHADMLNLQTVERRLNEERRQkqsldsqlsnEKKARKLAEEKAARPECSSQCKQRRQQMDeeqkRLR 749
Cdd:pfam13949 20 ERLEKSLDDLPKLKQRNREILDEAEKLLDEEESE----------DEQLRAKYGTRWTRPPSSELTATLRAEIR----KYR 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442624369 750 SDLKQAEEA----KQLAVEHGRKVE---QEYRMLEAKLRNRESSQPDPEI---------LLNALAAMQDKNATLEKNL 811
Cdd:pfam13949 86 EILEQASESdsqvRSKFREHEEDLEllsGPDEDLEAFLPSSRRAKNSPSVeeqvaklreLLNKLNELKREREQLLKDL 163
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
626-801 |
9.79e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 9.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 626 KLEADVKKYRAEISHMKQIENELRQKLDAnltSKSTLQAKQKECDDLEKRIQELNN-----ARH---------------- 684
Cdd:COG3883 34 AAQAELDALQAELEELNEEYNELQAELEA---LQAEIDKLQAEIAEAEAEIEERREelgerARAlyrsggsvsyldvllg 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624369 685 ----ADMLNLQTVERRLNEerRQKQSLDSQlsnEKKARKLAEEKAARPECSSQCKQRRQQMDEEQKRLRSDLKQAEEAKQ 760
Cdd:COG3883 111 sesfSDFLDRLSALSKIAD--ADADLLEEL---KADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLA 185
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 442624369 761 LAVEHGRKVEQEYRMLEAKLRNRESSQPDPEILLNALAAMQ 801
Cdd:COG3883 186 QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| |
