|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2-1167 |
0e+00 |
|
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: 605.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 2 YIKSIVLEGFKSYAQRTEIrDFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASSLQDLVYKNGQAGVNKATVSI 81
Cdd:pfam02463 1 YLKRIEIEGFKSYAKTVIL-PFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIHSKSGAFVNSAEVEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 82 TFDNSDKKnsplGFENNDEITITRQVIVGGRNKYLINGMNASNNRVQDLFGSVGLNVNNPHFLIMQGQITKVLNMKPTEI 161
Cdd:pfam02463 80 TFDNEDHE----LPIDKEEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 162 LAMIEEAAGTRMYECKKITAHKTIEKKESKLDEIRRIITEEISPTLEKLKEARASYLEYQKMTREVENLRRIYVAFQYVR 241
Cdd:pfam02463 156 LEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 242 AEEIKDRSTNALKEAQANKKKIFESMAENEKKVKELAQQIEETEKKNNEEFGAKLHSLEAAFSELQRVDAKVRSDLDHRK 321
Cdd:pfam02463 236 EERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 322 QNLNSEENRLKELIKIMQEEFKAFTSKEKEIKKIKEGLNGLQEESKKDAEALASAQQHFNAVSAGLSSNDSGQGTSLADQ 401
Cdd:pfam02463 316 LKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 402 MMTCKNEISKAATEAKQAQMKLKYAQQELKTKQAEVKKMDGSYKEDQEAFEAIRKTKEKLQDEMKKLKYEEAEQEAHLAK 481
Cdd:pfam02463 396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 482 KKQLSSEISSLRELCESIEAKHPYLRFEYKNPEKNWNPNCVKGLVVTLITVKDISTSKALEAVAGGKLYNIVVDTEATGK 561
Cdd:pfam02463 476 ETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 562 KILEKGQLKHRYTIIPLSKISANSIGHEIISLAKNLIGHREVHIAIsLIDYNSELQKAMEYVFGTTLVCSSMDNAKKVTF 641
Cdd:pfam02463 556 TADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDP-ILNLAQLDKATLEADEDDKRAKVVEGILKDTEL 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 642 DKRIMRKTVTLQGDIFDPQGTLSGGASSHVTPILSKLKTMRDAEDELKIKTSQLEATEKELANLKNMAEKYQHLKQQWEM 721
Cdd:pfam02463 635 TKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKK 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 722 KSEEAELLQTKIQQSAYHKQQEDLLALKKTIAECEETLKKTEESQRKAEEEYKALENKMKNAEAERGKEIKNAQQKLNSA 801
Cdd:pfam02463 715 LKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEE 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 802 KKKADDSSRKMKEKQQEVEALVLELEQLKQEQASYKQQSEAAQQAIASLKEQVSALEAEAVKTRESLKNAENELSSEKGL 881
Cdd:pfam02463 795 KLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLL 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 882 MEERTKDIKAKSAKIEKYREQNNELQLSINALEHDINKYQQETADASSTLDKLLKEYKWIASEKELFGQADTTYDFEANN 961
Cdd:pfam02463 875 KEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENN 954
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 962 PKETGQKLQKLLTKKEKLEKSLNMRAMNLLSEAEERYNDLMKKKRMVENDKIKILATIEELDRKKNKALHIAWEKVNKDF 1041
Cdd:pfam02463 955 KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWN 1034
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 1042 GSIFSMLLPGAKAMLVPSKKQNILDGLEFRVGLGDIWKENLTELSGGQRSLAALSLILAILLFKPAPIYILDEVDAALDL 1121
Cdd:pfam02463 1035 KVFFYLELGGSAELRLEDPDDPFSGGIEISARPPGKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDD 1114
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|....*..
gi 2500794 1122 SHTQNIGQMLHAHFKQSQFLVVSLKDGMFNNANVLYRTKFV-DGIST 1167
Cdd:pfam02463 1115 QNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGVTMVeNGVST 1161
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-1168 |
3.14e-106 |
|
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: 361.69 E-value: 3.14e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 2 YIKSIVLEGFKSYAQRTEIrDFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASSLQDLVYK-NGQAGVNKATVS 80
Cdd:TIGR02169 1 YIERIELENFKSFGKKKVI-PFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKAMRAERLSDLISNgKNGQSGNEAYVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 81 ITFDNSDKKNSplgfennDEITITRQVIVGGRNK---YLINGMNASNNRVQDLFGSVGLNVNNPHFlIMQGQITKVLNMK 157
Cdd:TIGR02169 80 VTFKNDDGKFP-------DELEVVRRLKVTDDGKysyYYLNGQRVRLSEIHDFLAAAGIYPEGYNV-VLQGDVTDFISMS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 158 PTEILAMIEEAAGTRMYECKKITAHKTIEKKESKLDEIRRIItEEISPTLEKLKEARASYLEYQKMTREVENLRRIYVAF 237
Cdd:TIGR02169 152 PVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLII-DEKRQQLERLRREREKAERYQALLKEKREYEGYELLK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 238 QYVRAEEIKDRSTNALKEAQANKKKIFESMAENEKKV-------KELAQQIEETEKKNNEEFGAKLHSLEAAFSELQR-V 309
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLeeieqllEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERsI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 310 DAKVRS--DLDHRKQNLNSEENRLK----ELIKIMQEEFKAFTSKEKEIKKIKEGLNGLQEESKKDAEALASAQQHFNAV 383
Cdd:TIGR02169 311 AEKEREleDAEERLAKLEAEIDKLLaeieELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 384 SAGLSsndsgqgtSLADQMMTCKNEISKAATEAKQAQMKLKYAQQELKTKQAEVKKMDgsyKEDQEAFEAIRKTKEKLQD 463
Cdd:TIGR02169 391 REKLE--------KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE---EEKEDKALEIKKQEWKLEQ 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 464 EMKKLKYEEAEQEAHLAKKKQLSSEISSLRELCESIEAKHPYLR---FEYKNPEKNWNPNC--VKGLVVTLITVKDiSTS 538
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEervRGGRAVEEVLKASIqgVHGTVAQLGSVGE-RYA 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 539 KALEAVAGGKLYNIVVDTEATGKKILE--KGQLKHRYTIIPLSKISANSIGHEIISLAKnlighrEVHIAISLIDYNSEL 616
Cdd:TIGR02169 539 TAIEVAAGNRLNNVVVEDDAVAKEAIEllKRRKAGRATFLPLNKMRDERRDLSILSEDG------VIGFAVDLVEFDPKY 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 617 QKAMEYVFGTTLVCSSMDNAKKVTFDKRImrktVTLQGDIFDPQGTLSGGASSHVTPIL------SKLKTMRDAEDELKI 690
Cdd:TIGR02169 613 EPAFKYVFGDTLVVEDIEAARRLMGKYRM----VTLEGELFEKSGAMTGGSRAPRGGILfsrsepAELQRLRERLEGLKR 688
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 691 ktsQLEATEKELANLKNMAEKYQHLKQQWEMKSEEAELLQTKIQQSAyHKQQEDLLALKKTIAECEETLKKTEESQRKAE 770
Cdd:TIGR02169 689 ---ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEE-EKLKERLEELEEDLSSLEQEIENVKSELKELE 764
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 771 EEYKALENKMKNAEAE--------RGKEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEALVLELEQLKQEQASYKQQSEA 842
Cdd:TIGR02169 765 ARIEELEEDLHKLEEAlndlearlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID 844
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 843 AQQAIASLKEQVSALEAEAVKTRESLKNAENELSSEKGLMEERTKDIKAKSAKIEKYREQNNELQLSINALEHDINKYQQ 922
Cdd:TIGR02169 845 LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKA 924
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 923 ETADASSTLDKLLKEYKWIASEKELFGQADTTYdfeannpketgQKLQKLLTKKEKLEkSLNMRAMNLLSEAEERYNDLM 1002
Cdd:TIGR02169 925 KLEALEEELSEIEDPKGEDEEIPEEELSLEDVQ-----------AELQRVEEEIRALE-PVNMLAIQEYEEVLKRLDELK 992
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 1003 KKKRMVENDKIKILATIEELDRKKNKALHIAWEKVNKDFGSIFSMLLPGAKAMLVPSKKQNILDGLEFRVGLGDIWKENL 1082
Cdd:TIGR02169 993 EKRAKLEEERKAILERIEEYEKKKREVFMEAFEAINENFNEIFAELSGGTGELILENPDDPFAGGLELSAKPKGKPVQRL 1072
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 1083 TELSGGQRSLAALSLILAILLFKPAPIYILDEVDAALDLSHTQNIGQMLHAHFKQSQFLVVSLKDGMFNNA-NVLYRTKF 1161
Cdd:TIGR02169 1073 EAMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEAQFIVVSLRSPMIEYAdRAIGVTMR 1152
|
....*..
gi 2500794 1162 VDGISTV 1168
Cdd:TIGR02169 1153 RNGESQV 1159
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-1144 |
2.88e-104 |
|
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: 356.29 E-value: 2.88e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 2 YIKSIVLEGFKSYAQRTEIrDFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASSLQDLVYkNG---QAGVNKAT 78
Cdd:TIGR02168 1 RLKKLELAGFKSFADPTTI-NFDKGITGIVGPNGCGKSNIVDAIRWVLGEQSAKALRGGKMEDVIF-NGsetRKPLSLAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 79 VSITFDNSDKknsPLGFENNDEITITRQVIVGGRNKYLINGMNASNNRVQDLFGSVGLNVNNpHFLIMQGQITKVLNMKP 158
Cdd:TIGR02168 79 VELVFDNSDG---LLPGADYSEISITRRLYRDGESEYFINGQPCRLKDIQDLFLDTGLGKRS-YSIIEQGKISEIIEAKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 159 TEILAMIEEAAGTRMYECKKITAHKTIEKKESKLDEIRRIItEEISPTLEKLKEARASYLEYQKMTREVENLRRIYVAFQ 238
Cdd:TIGR02168 155 EERRAIFEEAAGISKYKERRKETERKLERTRENLDRLEDIL-NELERQLKSLERQAEKAERYKELKAELRELELALLVLR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 239 YVRAEEIKDRSTNALKEAQ-------ANKKKIFESMAENEKKVKELAQQIEETEK-------------KNNEEFGAKLHS 298
Cdd:TIGR02168 234 LEELREELEELQEELKEAEeeleeltAELQELEEKLEELRLEVSELEEEIEELQKelyalaneisrleQQKQILRERLAN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 299 LEAAFSELQRVDAKVRSDLDHRKQNLNSEENRLKELIKIMQEEFKAFTSKEKEIKKIKEGLNGLQEESKKDAEALASAQQ 378
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 379 HFNAVSAGLSSNDSgQGTSLADQMMTCKNEISKAATEAKQAQMKLkyAQQELKTKQAEVKKMDGSYKEDQEAFEAIRKTK 458
Cdd:TIGR02168 394 QIASLNNEIERLEA-RLERLEDRRERLQQEIEELLKKLEEAELKE--LQAELEELEEELEELQEELERLEEALEELREEL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 459 EKLQDEMKKLKYEEAeqeahlakkkQLSSEISSLRELCESIEAKHPYLRFEYKNpekNWNPNCVKGLVVTLITVkDISTS 538
Cdd:TIGR02168 471 EEAEQALDAAERELA----------QLQARLDSLERLQENLEGFSEGVKALLKN---QSGLSGILGVLSELISV-DEGYE 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 539 KALEAVAGGKLYNIVVDTEATGKKILE--KGQLKHRYTIIPLSKISANSIGHEIISLAKNLIGHreVHIAISLIDYNSEL 616
Cdd:TIGR02168 537 AAIEAALGGRLQAVVVENLNAAKKAIAflKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGF--LGVAKDLVKFDPKL 614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 617 QKAMEYVFGTTLVCSSMDNA----KKVTFDKRImrktVTLQGDIFDPQGTLSGGASSHVTPILSKLKTMRDAEDELKIKT 692
Cdd:TIGR02168 615 RKALSYLLGGVLVVDDLDNAlelaKKLRPGYRI----VTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELE 690
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 693 SQLEATEKELANLKnmaekyqhlKQQWEMKSEEAELLQTKIQQS-AYHKQQEDLLALKKTIAECEET---LKKTEESQRK 768
Cdd:TIGR02168 691 EKIAELEKALAELR---------KELEELEEELEQLRKELEELSrQISALRKDLARLEAEVEQLEERiaqLSKELTELEA 761
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 769 AEEEYKALENKMKNAEAERGKEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEAL-------VLELEQLKQEQASYKQQSE 841
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeaanlRERLESLERRIAATERRLE 841
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 842 AAQQAIASLKEQVSALEAEAVKTRES-------LKNAENELSSEKGLMEERTKDIKAKSAKIEKYREQNNELQLSINALE 914
Cdd:TIGR02168 842 DLEEQIEELSEDIESLAAEIEELEELieeleseLEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 915 HDINKYQQETADASSTLDKLLKEykwiasekeLFGQADTTYDFEANNPKETGQKLQKLLTKKEKLEKSL------NMRAM 988
Cdd:TIGR02168 922 EKLAQLELRLEGLEVRIDNLQER---------LSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIkelgpvNLAAI 992
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 989 NLLSEAEERYNDLMKKKRMVENDKIKILATIEELDRKKNKALHIAWEKVNKDFGSIFSMLLPGAKAMLVPSKKQNILD-G 1067
Cdd:TIGR02168 993 EEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNENFQRVFPKLFGGGEAELRLTDPEDLLEaG 1072
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2500794 1068 LEFRVGLGDIWKENLTELSGGQRSLAALSLILAILLFKPAPIYILDEVDAALDLSHTQNIGQMLHAHFKQSQFLVVS 1144
Cdd:TIGR02168 1073 IEIFAQPPGKKNQNLSLLSGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDDANVERFANLLKEFSKNTQFIVIT 1149
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1-172 |
2.90e-98 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 312.70 E-value: 2.90e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 1 MYIKSIVLEGFKSYAQRTEIRDFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASSLQDLVYKNGQAGVNKATVS 80
Cdd:cd03273 1 MHIKEIILDGFKSYATRTVISGFDPQFNAITGLNGSGKSNILDAICFVLGITNLSTVRASNLQDLIYKRGQAGITKASVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 81 ITFDNSDKKNSPLGFENNDEITITRQVIVGGRNKYLINGMNASNNRVQDLFGSVGLNVNNPHFLIMQGQITKVLNMKPTE 160
Cdd:cd03273 81 IVFDNSDKSQSPIGFENYPEITVTRQIVLGGTNKYLINGHRAQQQRVQDLFQSVQLNVNNPHFLIMQGRITKVLNMGGVW 160
|
170
....*....|..
gi 2500794 161 ILAMIEEAAGTR 172
Cdd:cd03273 161 KESLTELSGGQR 172
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-1157 |
2.06e-72 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 261.41 E-value: 2.06e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 1 MYIKSIVLEGFKSYAQRTEIrDFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASSLQDLVYkNGQAG---VNKA 77
Cdd:COG1196 1 MRLKRLELAGFKSFADPTTI-PFEPGITAIVGPNGSGKSNIVDAIRWVLGEQSAKSLRGGKMEDVIF-AGSSSrkpLGRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 78 TVSITFDNSDKKnSPLGFennDEITITRQVIVGGRNKYLINGMNASNNRVQDLFGSVGLNVNNpHFLIMQGQITKVLNMK 157
Cdd:COG1196 79 EVSLTFDNSDGT-LPIDY---DEVTITRRLYRSGESEYYINGKPCRLKDIQDLFLDTGLGPES-YSIIGQGMIDRIIEAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 158 PTEILAMIEEAAGtrmyeckkITAHKT-IEKKESKLDEIR------RIITEEISPTLEKLKEARASYLEYQKMTREVENL 230
Cdd:COG1196 154 PEERRAIIEEAAG--------ISKYKErKEEAERKLEATEenlerlEDILGELERQLEPLERQAEKAERYRELKEELKEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 231 RRIYVAFQYVRAEEIKDRSTNALKEAQANKKKIFESMAENEKKVKELAQQIEETEkknneefgAKLHSLEAAFSELQRVD 310
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE--------LELEEAQAEEYELLAEL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 311 AKVRSDLDHRKQNLNSEENRLKELIKIMQEEFKAFTSKEKEIKKIKEGLNGLQEESKKDAEALASAQQHFNAVSAGLSSN 390
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 391 DSGQgTSLADQMMTCKNEISKAATEAKQAQMKLKYAQQELKTKQAEVKKMDGSYKEDQEAFEAIRKTKEK---------- 460
Cdd:COG1196 378 EEEL-EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEaaeeeaelee 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 461 ----LQDEMKKLKYEEAEQEAHLAKKKQLSSEISSLRELCESIEAKHPYLRFEYKNPEKNWNPNCVKGLVVTLITVKDIS 536
Cdd:COG1196 457 eeeaLLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 537 TsKALEAVAGGKLYNIVVDTEATGKKILE--KGQLKHRYTIIPLSKISANsigheiiSLAKNLIGHREVHIAISLIDYNS 614
Cdd:COG1196 537 E-AALEAALAAALQNIVVEDDEVAAAAIEylKAAKAGRATFLPLDKIRAR-------AALAAALARGAIGAAVDLVASDL 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 615 ELQKAMEYVFGTTLVcssmdnakkvtfdkrimrktvtlqgdifdpqgtlsgGASSHVTPILSKLKTMRDAEDELKIKTsq 694
Cdd:COG1196 609 READARYYVLGDTLL------------------------------------GRTLVAARLEAALRRAVTLAGRLREVT-- 650
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 695 leatekelanlknmaekyqhlkqqwemkSEEAELLQTKIQQSAYHKQQEDLLALKKTIAEceetlkktEESQRKAEEEYK 774
Cdd:COG1196 651 ----------------------------LEGEGGSAGGSLTGGSRRELLAALLEAEAELE--------ELAERLAEEELE 694
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 775 ALENKMKNAEAErgkeiknaqqklnsakkkaddssRKMKEKQQEVEALVLELEQLKQEQASYKQQSEAAQQAIASLKEQV 854
Cdd:COG1196 695 LEEALLAEEEEE-----------------------RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 855 SALEAEAVKTRESLknaenelssekglmEERTKDIKAKsakiekyreqnnelqlsINALEhdinkyqqetadasstldkl 934
Cdd:COG1196 752 ALEELPEPPDLEEL--------------ERELERLERE-----------------IEALG-------------------- 780
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 935 lkeykwiasekelfgqadttydfeannpketgqklqklltkkeklekSLNMRAMNLLSEAEERYNDLMKKKRMVENDKIK 1014
Cdd:COG1196 781 -----------------------------------------------PVNLLAIEEYEELEERYDFLSEQREDLEEARET 813
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 1015 ILATIEELDRKKNKALHIAWEKVNKDFGSIFSMLLPGAKAMLVPSKKQNILD-GLEFRV---GlgdiwKEN--LTELSGG 1088
Cdd:COG1196 814 LEEAIEEIDRETRERFLETFDAVNENFQELFPRLFGGGEAELLLTDPDDPLEtGIEIMAqppG-----KKLqrLSLLSGG 888
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 1089 -------------QRslaalslilaillFKPAPIYILDEVDAALDLSHTQNIGQMLHAHFKQSQFLVVSLKDGMFNNANV 1155
Cdd:COG1196 889 ekaltalallfaiFR-------------LNPSPFCVLDEVDAPLDDANVERFAELLKEMSEDTQFIVITHNKRTMEAADR 955
|
..
gi 2500794 1156 LY 1157
Cdd:COG1196 956 LY 957
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1073-1169 |
7.53e-49 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 174.41 E-value: 7.53e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 1073 GLGDIWKENLTELSGGQRSLAALSLILAILLFKPAPIYILDEVDAALDLSHTQNIGQMLHAHFKQSQFLVVSLKDGMFNN 1152
Cdd:cd03273 155 NMGGVWKESLTELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGSQFIVVSLKEGMFNN 234
|
90
....*....|....*..
gi 2500794 1153 ANVLYRTKFVDGISTVS 1169
Cdd:cd03273 235 ANVLFRTRFVDGTSTVT 251
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
3-164 |
6.46e-30 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 119.29 E-value: 6.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 3 IKSIVLEGFKSYAQRTEIRDFDPLFNAITGLNGSGKSNILDSICFLLGISNlSQVRASSLQDLVYKNGQAGVNKATVSIT 82
Cdd:cd03272 1 IKQVIIQGFKSYKDQTVIEPFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEY-THLREEQRQALLHEGSGPSVMSAYVEII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 83 FDNSDKKNSplgfENNDEITItRQVIVGGRNKYLINGMNASNNRVQDLFGSVGLNVNNPHFLIMQGQITKVLNMKPTEIL 162
Cdd:cd03272 80 FDNSDNRFP----IDKEEVRL-RRTIGLKKDEYFLDKKNVTKNDVMNLLESAGFSRSNPYYIVPQGKINSLTNMKQDEQQ 154
|
..
gi 2500794 163 AM 164
Cdd:cd03272 155 EM 156
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
522-639 |
1.23e-28 |
|
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 214944 [Multi-domain] Cd Length: 120 Bit Score: 111.55 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 522 VKGLVVTLITVKDiSTSKALEAVAGGKLYNIVVDTEATGKKILEKGQLKH--RYTIIPLSKISANSIGHEIISLAkNLIG 599
Cdd:smart00968 3 VLGRVADLISVDP-KYETALEAALGGRLQAVVVDTEETAKKAIEFLKKNRlgRATFLPLDKIKPRSPAGSKLREA-LLPE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2500794 600 HREVHIAISLIDYNSELQKAMEYVFGTTLVCSSMDNAKKV 639
Cdd:smart00968 81 PGFVGPAIDLVEYDPELRPALEYLLGNTLVVDDLETARRL 120
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
3-89 |
1.47e-26 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 108.32 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 3 IKSIVLEGFKSYAQRTEIrDFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASSLQDLVYK--NGQAGVNKATVS 80
Cdd:cd03278 1 LKKLELKGFKSFADKTTI-PFPPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAKSLRGEKMSDVIFAgsETRKPANFAEVT 79
|
....*....
gi 2500794 81 ITFDNSDKK 89
Cdd:cd03278 80 LTFDNSDGR 88
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
3-86 |
2.99e-24 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 100.85 E-value: 2.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 3 IKSIVLEGFKSYAQRTEIRDFDPlFNAITGLNGSGKSNILDSICFLLGISNLSQVRASSLQdLVYKNGQAGVNKATVSIT 82
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSNS-FNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLF-LAGGGVKAGINSASVEIT 78
|
....
gi 2500794 83 FDNS 86
Cdd:cd03239 79 FDKS 82
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
522-639 |
1.38e-22 |
|
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 461926 [Multi-domain] Cd Length: 116 Bit Score: 93.87 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 522 VKGLVVTLITVKDIsTSKALEAVAGGKLYNIVVDTEATGKKILE--KGQLKHRYTIIPLSKISANsighEIISLAKNLIG 599
Cdd:pfam06470 4 VLGRLADLIEVDEG-YEKAVEAALGGRLQAVVVDDEDDAKRAIEflKKNKLGRATFLPLDRLKPR----PRRPGADLKGG 78
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2500794 600 hreVHIAISLIDYNSELQKAMEYVFGTTLVCSSMDNAKKV 639
Cdd:pfam06470 79 ---AGPLLDLVEYDDEYRKALRYLLGNTLVVDDLDEALEL 115
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
3-158 |
4.86e-20 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 90.71 E-value: 4.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 3 IKSIVLEGFKSYAQRTEIRDFDPlFNAITGLNGSGKSNILDSICFLLGISNlSQVRASSLQDLVY--KNGQAGVNKATVS 80
Cdd:cd03275 1 LKRLELENFKSYKGRHVIGPFDR-FTCIIGPNGSGKSNLMDAISFVLGEKS-SHLRSKNLKDLIYraRVGKPDSNSAYVT 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2500794 81 ITFDNsdkknsplgfENNDEITITRqVIVGGRNKYLINGMNASNNRVQDLFGSVGLNVNNPHFLIMQGQITKVLNMKP 158
Cdd:cd03275 79 AVYED----------DDGEEKTFRR-IITGGSSSYRINGKVVSLKEYNEELEKINILVKARNFLVFQGDVESIASKNP 145
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1085-1167 |
8.41e-20 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 88.13 E-value: 8.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 1085 LSGGQRSLAALSLILAILLFKPAPIYILDEVDAALDLSHTQNIGQMLHAHFK-QSQFLVVSLKDGMFNNANVLYRTKFVD 1163
Cdd:cd03239 95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKhTSQFIVITLKKEMFENADKLIGVLFVH 174
|
....
gi 2500794 1164 GIST 1167
Cdd:cd03239 175 GVST 178
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
159-939 |
1.71e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 88.66 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 159 TEILAMIEEAagtRMYECKKITAHKTIEKKESKLDEIRRIITEEISPTLEKLKEAR-ASYLEYQKMTREVENLRRIYVAF 237
Cdd:PTZ00121 1094 EEAFGKAEEA---KKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARkAEDAKRVEIARKAEDARKAEEAR 1170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 238 QYVRAEEIKD-------RSTNALKEAQANKKKIFESMAENEKKVKEL--------AQQIEETEKKNNEEFGAKLHSLEAA 302
Cdd:PTZ00121 1171 KAEDAKKAEAarkaeevRKAEELRKAEDARKAEAARKAEEERKAEEArkaedakkAEAVKKAEEAKKDAEEAKKAEEERN 1250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 303 FSELQRVDAKVRSDLDHRKQNLNSEENRLKELIKIMQEEFKAFTSKEKEIKKIKEGLNGLQEESKKDAEALASAQQHFNA 382
Cdd:PTZ00121 1251 NEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKK 1330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 383 VSAGLSSNDSGQGTSLADqmmtcKNEISKAATEAKQAQMKLKYAqqELKTKQAEvKKMDGSYKEDQE---AFEAIRKTKE 459
Cdd:PTZ00121 1331 ADAAKKKAEEAKKAAEAA-----KAEAEAAADEAEAAEEKAEAA--EKKKEEAK-KKADAAKKKAEEkkkADEAKKKAEE 1402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 460 --KLQDEMKKlkYEEAEQEAHLAKKKqlSSEISSLRELCESIEAKHPYLRFEYKNPEKNWNPNCVKGlvVTLITVKDIST 537
Cdd:PTZ00121 1403 dkKKADELKK--AAAAKKKADEAKKK--AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK--AEEAKKADEAK 1476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 538 SKALEAVAGGKLYNIVVDTEATGKKILEKGQLKHRYTIIPLS---KISANSIGHEIISLAKNLIGHREVHIAISLiDYNS 614
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAeeaKKADEAKKAEEAKKADEAKKAEEKKKADEL-KKAE 1555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 615 ELQKAMEYvfgttlvcSSMDNAKKVTFDKRIMRKTVTLQGDIFDPQGTlsggasshvtpilsklKTMRDAEDELKIKTSQ 694
Cdd:PTZ00121 1556 ELKKAEEK--------KKAEEAKKAEEDKNMALRKAEEAKKAEEARIE----------------EVMKLYEEEKKMKAEE 1611
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 695 LEATEKELANLKNMAEKYQHLKQQWEMKSEEAEllqtKIQQSAYHKQQEDLLALKKtiaecEETLKKTEESQRKAEEEYK 774
Cdd:PTZ00121 1612 AKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE----EKKKAEELKKAEEENKIKA-----AEEAKKAEEDKKKAEEAKK 1682
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 775 ALENKMKNAEAERGKEikNAQQKLNSAKKKADDSSRKMKEKQQEVEALVLELEQLKQEQASYKQQSEAA------QQAIA 848
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEA--EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAkkdeeeKKKIA 1760
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 849 SLKEQVSALEAEAVKTRESLKNAENELSSEKGLM--EERTKDIKAKSAKIEkyrEQNNELQLSINALEHDINKYQQETAD 926
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMevDKKIKDIFDNFANII---EGGKEGNLVINDSKEMEDSAIKEVAD 1837
|
810
....*....|...
gi 2500794 927 ASSTLDKLLKEYK 939
Cdd:PTZ00121 1838 SKNMQLEEADAFE 1850
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1-83 |
4.87e-16 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213241 [Multi-domain] Cd Length: 212 Bit Score: 78.11 E-value: 4.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 1 MYIKSIVLEGFKSYAQRTEIRDFDPLFNAITGLNGSGKSNILDSICFLLGIsNLSQVRASSLQDLVYK-NGQAGVNKATV 79
Cdd:cd03274 1 LIITKLVLENFKSYAGEQVIGPFHKSFSAIVGPNGSGKSNVIDSMLFVFGF-RASKMRQKKLSDLIHNsAGHPNLDSCSV 79
|
....
gi 2500794 80 SITF 83
Cdd:cd03274 80 EVHF 83
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
3-202 |
6.02e-14 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 71.96 E-value: 6.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 3 IKSIVLEGFKSYAQRTEIrDFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASSlqDLVYKngqaGVNKATVSIT 82
Cdd:COG0419 2 LLRLRLENFRSYRDTETI-DFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRS--DLINV----GSEEASVELE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 83 FDNSDKknsplgfenndEITITRQvivggrnkylingmnasnnrvqdlfgsvglnvnnphflimQGQITKVLNMKPTEIL 162
Cdd:COG0419 75 FEHGGK-----------RYRIERR----------------------------------------QGEFAEFLEAKPSERK 103
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2500794 163 AMIEEAAGTRMYECKKITAHKTIEKKESKLDEIRRIITEE 202
Cdd:COG0419 104 EALKRLLGLEIYEELKERLKELEEALESALEELAELQKLK 143
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
5-83 |
3.81e-13 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 68.54 E-value: 3.81e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2500794 5 SIVLEGFKSYAQRTEIRDFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRasslqdlvYKNGQAGVNKATVSITF 83
Cdd:cd03227 1 KIVLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRR--------RSGVKAGCIVAAVSAEL 71
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1104-1157 |
7.97e-13 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 68.65 E-value: 7.97e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2500794 1104 FKPAPIYILDEVDAALDLSHTQNIGQMLHAHFKQSQFLVVSLKDGMFNNANVLY 1157
Cdd:cd03278 133 VRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAADRLY 186
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
675-1039 |
1.65e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.48 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 675 LSKLKTMRDAEDELKIKTSQLEATEkELANLKNMAEKYQHLKQqwemKSEEAELLQTKIQQSAYHKQQEDLLALKKTIAE 754
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKAEEKKKAD-EAKKKAEEAKKADEAKK----KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK 1484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 755 CEETLKKTEESQRKAEEEYKALENKMKNAEAERGKEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEALVLELEQLKQEQA 834
Cdd:PTZ00121 1485 ADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKK 1564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 835 SYKQQSEAAQQAIASLKEQVSALEAEAVKTRESLKNAENElSSEKGLMEERTKDIKAKSAKIEKYREQNNELQLSINALE 914
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE-KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA 1643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 915 HDINKYQQetadasstLDKLLKEYKWIASEKELFGQADTTYDFEANNPKETGQKLQKLLTKKEklEKSLNMRAMNLLSEA 994
Cdd:PTZ00121 1644 EEKKKAEE--------LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA--EEAKKAEELKKKEAE 1713
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2500794 995 EERYNDLMKKKRMVENDKIKILATIEELDRKKNKALHIAWEKVNK 1039
Cdd:PTZ00121 1714 EKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKK 1758
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1-924 |
2.87e-12 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 71.54 E-value: 2.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 1 MYIKSIVLEGFKSYaQRTEIRDFDPL--FNAITGLNGSGKSNILDSICFLLgISNLSQVRASSLQDLVYKNGQAGVNKAT 78
Cdd:TIGR00618 1 MKPLRLTLKNFGSY-KGTHTIDFTALgpIFLICGKTGAGKTTLLDAITYAL-YGKLPRRSEVIRSLNSLYAAPSEAAFAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 79 VSITFDNSDKK-----NSPLGFENNDEITITRQVIVGGRNKYLINGMNASNNRVQDLFGsvglnVNNPHF----LIMQGQ 149
Cdd:TIGR00618 79 LEFSLGTKIYRvhrtlRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLK-----LDYKTFtrvvLLPQGE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 150 ITKVLNMKPTEILAMIEEAAGTRMYECKKITA---HKTIEKKESKLD---EIRRIITEEISPTLEKLKEARASYL----E 219
Cdd:TIGR00618 154 FAQFLKAKSKEKKELLMNLFPLDQYTQLALMEfakKKSLHGKAELLTlrsQLLTLCTPCMPDTYHERKQVLEKELkhlrE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 220 YQKMTREVENLRRiyvafQYVRAEEIKDRSTNALKEAQANKKKIFESMAENEKKVKELAQQIEETEKKNNEEFGAKLH-S 298
Cdd:TIGR00618 234 ALQQTQQSHAYLT-----QKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEqQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 299 LEAAFSELQRVDAKVRSDLDHR----KQNLNSEENRLKELIKIMQEE-FKAFTSKEKEIKKIKEGLNGLQEESKKDAEAL 373
Cdd:TIGR00618 309 AQRIHTELQSKMRSRAKLLMKRaahvKQQSSIEEQRRLLQTLHSQEIhIRDAHEVATSIREISCQQHTLTQHIHTLQQQK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 374 ASAQQHFNAVSAGLSSNDSGQGTSLADQMMTCKNEISKAATEAK-QAQMKLKYAQQELKTKQAEVKKMdgsykEDQEAFE 452
Cdd:TIGR00618 389 TTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQqELQQRYAELCAAAITCTAQCEKL-----EKIHLQE 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 453 AIRKTKEKLQDEMKKLKYEEAEQEAHLAKKKQLSSEISSLRELCESIEAKHPYLRFEYkNPEKNWNPNCvkglvvtlitv 532
Cdd:TIGR00618 464 SAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDID-NPGPLTRRMQ----------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 533 KDISTSKALEAvAGGKLYNIVVDTEATGKKILEKGQLKHRYTIIPLSKISANSIGHEIISLAKNLIGHrevhiaisLIDY 612
Cdd:TIGR00618 532 RGEQTYAQLET-SEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQD--------LTEK 602
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 613 NSELQKameyvfgtTLVCSSMDNAKKVTFDKRIMRKTVTLQGDIFDPQGTLsggasSHVTPILSKLKTMRDAEDELKIKT 692
Cdd:TIGR00618 603 LSEAED--------MLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKL-----TALHALQLTLTQERVREHALSIRV 669
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 693 SQLEATEKELANLKNMAEKYQHLKQQWEMKSEEAELLQ---TKIQQSA--YHKQQEDLLALKKTIAECEETLkktEESQR 767
Cdd:TIGR00618 670 LPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLReleTHIEEYDreFNEIENASSSLGSDLAAREDAL---NQSLK 746
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 768 KAEEEYKALENKMKNAEAERGKEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEALVLELEQLKQEQASYKQQSEAAQQAI 847
Cdd:TIGR00618 747 ELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETL 826
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2500794 848 ASLKEQVSALEAEAVKTRESLKNAENELSSEKGLMEERTKDIKAKSAKIEKYREQNnelQLSINALEHDINKYQQET 924
Cdd:TIGR00618 827 VQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGIN---QIKIQFDGDALIKFLHEI 900
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
696-1028 |
5.20e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.94 E-value: 5.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 696 EATEKELANLKNMAEKYQHLKQQWEMKSEEAELLQTKIQQSAYHKQQEDLLA--LKKTIAE---CEETLKKTEESQRKAE 770
Cdd:PTZ00121 1253 EIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKAdeAKKKAEEakkADEAKKKAEEAKKKAD 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 771 EEYKALENKMKNAEAERGKEiKNAQQKLNSAKKKADDSSRKMKEKQQEVEALVLELEQLKQEQASYKQQSEAAQQAiasl 850
Cdd:PTZ00121 1333 AAKKKAEEAKKAAEAAKAEA-EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA---- 1407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 851 kEQVSALEAEAVKTRESLKNAENELSSE--KGLMEERTKDIKAKSaKIEKYREQNNELQLSINALEHDINKYQQETADAS 928
Cdd:PTZ00121 1408 -DELKKAAAAKKKADEAKKKAEEKKKADeaKKKAEEAKKADEAKK-KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA 1485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 929 STLDKLLKEYKWIASE----KELFGQADTTYDFEANNPKETGQKLQKL-----LTKKEKLEKSLNMRAMNLLSEAEERYN 999
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEakkaAEAKKKADEAKKAEEAKKADEAKKAEEAkkadeAKKAEEKKKADELKKAEELKKAEEKKK 1565
|
330 340
....*....|....*....|....*....
gi 2500794 1000 dlMKKKRMVENDKIKILATIEELDRKKNK 1028
Cdd:PTZ00121 1566 --AEEAKKAEEDKNMALRKAEEAKKAEEA 1592
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
2-132 |
5.40e-12 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 68.64 E-value: 5.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 2 YIKSIVLEGFKSYAQrTEIrDFDPLFNAITGLNGSGKSNILDSICFLlgiSNLSQVRASSLQDLVyKNGQAGvnkATVSI 81
Cdd:COG1195 1 RLKRLSLTNFRNYES-LEL-EFSPGINVLVGPNGQGKTNLLEAIYLL---ATGRSFRTARDAELI-RFGADG---FRVRA 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2500794 82 TFDNSDkKNSPLGfenndeITITRqvivGGRNKYLINGMNASnnRVQDLFG 132
Cdd:COG1195 72 EVERDG-REVRLG------LGLSR----GGKKRVRINGKPVR--RLSDLAG 109
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1082-1164 |
5.68e-12 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 65.07 E-value: 5.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 1082 LTELSGGQRSLAALSLILAILLFKPAPIYILDEVDAALDLSHTQNIGQMLHAHF-KQSQFLVVSLKDGMFNNANVLYRTK 1160
Cdd:cd03227 75 RLQLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLIHIK 154
|
....
gi 2500794 1161 FVDG 1164
Cdd:cd03227 155 KVIT 158
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
679-889 |
8.71e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.94 E-value: 8.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 679 KTMRDAEDELKIKTSQLEAtekeLANLKNMAEKYQHLKqqwemksEEAELLQTKIQQSAYHKQQEDLLALKKTIAECEET 758
Cdd:COG4913 235 DDLERAHEALEDAREQIEL----LEPIRELAERYAAAR-------ERLAELEYLRAALRLWFAQRRLELLEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 759 LKKTEESQRKAEEEYKALENKMKNAEAER----GKEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEALVLELEQLKQEQA 834
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIrgngGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFA 383
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2500794 835 SYKQQSEAAQQAIASLKEQVSALEAEAVKTRESLKNAENELSSEKGLMEERTKDI 889
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNI 438
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
677-1039 |
2.15e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 68.63 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 677 KLKTMRDAEDELKIKTSQLEATEKELANLKNMAEKYQHLKQQWEMKSEEAELLQTKiqqSAYHKQQEDLLALKKTIAECE 756
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKA---AAAKKKADEAKKKAEEKKKAD 1434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 757 ETLKKTEES------QRKAEEEYKALENKMKNAEAERGKEIKNA---QQKLNSAKKKADDSSRKMKEKQQEVEALVLELE 827
Cdd:PTZ00121 1435 EAKKKAEEAkkadeaKKKAEEAKKAEEAKKKAEEAKKADEAKKKaeeAKKADEAKKKAEEAKKKADEAKKAAEAKKKADE 1514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 828 QLKQEQASYKQQSEAAQQAIAS--LKEQVSALEAEAVKTRESLKNAENELSSEKGLMEERTKDIKAKSAKIEKYREQNNE 905
Cdd:PTZ00121 1515 AKKAEEAKKADEAKKAEEAKKAdeAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 906 LQLSINALEHDINKYQQ-----ETADASSTLDKLLKEYKWIASEKElfGQADTTYDFEANNPKETGQKLQKL-LTKKEKL 979
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEakkaeEAKIKAEELKKAEEEKKKVEQLKK--KEAEEKKKAEELKKAEEENKIKAAeEAKKAEE 1672
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 980 EKSLNMRAMNllSEAEERYNDLMKKKRMVENDKIKILATIEELDRKKNKALHIAwEKVNK 1039
Cdd:PTZ00121 1673 DKKKAEEAKK--AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA-EEENK 1729
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
22-130 |
2.38e-11 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213208 [Multi-domain] Cd Length: 276 Bit Score: 65.69 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 22 DFDPLFNAITGLNGSGKSNILDSICFLLGIsnlsqvRASSlqDLVykngQAGVNKATVSITFDNSDKKN-----SPLGFE 96
Cdd:cd03241 18 DFEEGLTVLTGETGAGKSILLDALSLLLGG------RASA--DLI----RSGAEKAVVEGVFDISDEEEakallLELGIE 85
|
90 100 110
....*....|....*....|....*....|....
gi 2500794 97 NNDEITITRQVIVGGRNKYLINGMNASNNRVQDL 130
Cdd:cd03241 86 DDDDLIIRREISRKGRSRYFINGQSVTLKLLREL 119
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
734-929 |
2.63e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 66.71 E-value: 2.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 734 QQSAYHKQQEDLLALKKTIAECEETLKKTEESQRKAEEEYKALENKMKNAEAERGK---EIKNAQQKLNSAKKKADDSSR 810
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAleqELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 811 KMKEKQQEVEALVLELEQ----------LKQEQAS--------YKQQSEAAQQAIASLK---EQVSALEAEAVKTRESLK 869
Cdd:COG4942 98 ELEAQKEELAELLRALYRlgrqpplallLSPEDFLdavrrlqyLKYLAPARREQAEELRadlAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2500794 870 NAENELSSEKG----LMEERTKDIKAKSAKIEKYREQNNELQLSINALEHDINKYQQETADASS 929
Cdd:COG4942 178 ALLAELEEERAaleaLKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1081-1169 |
1.39e-10 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 63.05 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 1081 NLTELSGGQRSLAALSLILAILLFKPAPIYILDEVDAALDLSHTQNIGQMLHAHFKQSQFLVVSLKDGMFNNANVLYRTK 1160
Cdd:cd03272 155 EMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEVADKFYGVK 234
|
....*....
gi 2500794 1161 FVDGISTVS 1169
Cdd:cd03272 235 FRNKVSTID 243
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
3-99 |
1.94e-10 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 61.46 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 3 IKSIVLEGFKSYAqRTEIrDFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASSLQDLVyKNGQagvNKATVSIT 82
Cdd:cd03276 1 IESITLKNFMCHR-HLQI-EFGPRVNFIVGNNGSGKSAILTALTIGLGGKASDTNRGSSLKDLI-KDGE---SSAKITVT 74
|
90
....*....|....*..
gi 2500794 83 FDNSDKKNSPLGFENND 99
Cdd:cd03276 75 LKNQGLDANPLCVLSQD 91
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
677-1028 |
2.24e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.55 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 677 KLKTMRDAEDELKIKTSQLEATEKELANLKNMAEKYQHLKQQWEMKSEEAELLQTKIQQSAYHKQQEDLLALKKTIAECE 756
Cdd:PTZ00121 1201 KAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKA 1280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 757 ETLKKTEESQ-----RKAEEEYKALENKMKNAEAERGKEIKnaqQKLNSAKKKADDSSRKMKEKQQEVEALVLELEQLKQ 831
Cdd:PTZ00121 1281 DELKKAEEKKkadeaKKAEEKKKADEAKKKAEEAKKADEAK---KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD 1357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 832 EQASYKQQSEAAQQAIASLKEQVSAL--EAEAVKTRESLKNAENELSSE----KGLMEERTKDIKAKSA-----KIEKYR 900
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAkkKAEEKKKADEAKKKAEEDKKKadelKKAAAAKKKADEAKKKaeekkKADEAK 1437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 901 EQNNELQLSINALEHDINKYQQETADASSTLDKLLKEYKWIASEKELFGQADTTYDfEANNPKETGQKLQKLLTKKEKLE 980
Cdd:PTZ00121 1438 KKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE-EAKKKADEAKKAAEAKKKADEAK 1516
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2500794 981 KSLNMRAMNLLSEAEE-RYNDLMKKKRmvENDKIKILATIEELDRKKNK 1028
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEaKKADEAKKAE--EKKKADELKKAEELKKAEEK 1563
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1078-1160 |
4.61e-10 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213241 [Multi-domain] Cd Length: 212 Bit Score: 60.77 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 1078 WKeNLTELSGGQRSLAALSLILAILLFKPAPIYILDEVDAALDLSHTQNIGQMLHAHFKQSQFLVVSLKDGMFNNANVL- 1156
Cdd:cd03274 122 WK-NISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELADRLv 200
|
....*.
gi 2500794 1157 --YRTK 1160
Cdd:cd03274 201 giYKTN 206
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
739-898 |
5.03e-10 |
|
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: 61.09 E-value: 5.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 739 HKQQEDLLALKKT---IAECEETLKKTEESQRKAEEEYKALENKMKNAEAERG---KEIKNAQQKLNSAKKKADDSSRKM 812
Cdd:COG1579 3 PEDLRALLDLQELdseLDRLEHRLKELPAELAELEDELAALEARLEAAKTELEdleKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 813 KE--KQQEVEALVLELEQLKQEQASYKQQSEAAQQAIASLKEQVSALEAEAVKTRESLKNAENELSSEKGLMEERTKDIK 890
Cdd:COG1579 83 GNvrNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
....*...
gi 2500794 891 AKSAKIEK 898
Cdd:COG1579 163 AEREELAA 170
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
676-1041 |
1.42e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 676 SKLKTMRDAEDELKIKTSQLEATEKELANLKNMAEKYQHLKQQWEMKSEEAELLQTKIQQSayhkqQEDLLALKKTIAEC 755
Cdd:PRK03918 204 EVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIREL-----EERIEELKKEIEEL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 756 EETLKKTEESQRKAEE--EYKALENKMKNAEAERGKEIKNAQQKLNSAKKKADDSSrkmkEKQQEVEALVLELEQLKQEQ 833
Cdd:PRK03918 279 EEKVKELKELKEKAEEyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE----EKEERLEELKKKLKELEKRL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 834 ASYKQQSEAAQQAIAsLKEQVSALEAEavKTRESLKNAENELSSEKGLMEERTKDIKAKSAKIEKYREQNNELQLSINAL 913
Cdd:PRK03918 355 EELEERHELYEEAKA-KKEELERLKKR--LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEEL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 914 EH--------------------------DINKYQQETADASSTLDKLLKEY----KWIASEKELFGQADTTYDFEANNPK 963
Cdd:PRK03918 432 KKakgkcpvcgrelteehrkelleeytaELKRIEKELKEIEEKERKLRKELreleKVLKKESELIKLKELAEQLKELEEK 511
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2500794 964 ETGQKLQKLLTKKEKLEKsLNMRAMNLLSEAeERYNDLMKKKRMVENDKIKILATIEELDRKKNKALHIAWEKVNKDF 1041
Cdd:PRK03918 512 LKKYNLEELEKKAEEYEK-LKEKLIKLKGEI-KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESV 587
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-132 |
1.43e-09 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 61.33 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 1 MYIKSIVLEGFKSYAqRTEIrDFDPLFNAITGLNGSGKSNILDSICFLlgiSNLSQVRASSLQDLVyKNGQAGvnkATVS 80
Cdd:PRK00064 1 MYLTRLSLTDFRNYE-ELDL-ELSPGVNVLVGENGQGKTNLLEAIYLL---APGRSHRTARDKELI-RFGAEA---AVIH 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2500794 81 ITFDNSdkknsplGFENNDEITITRQvivgGRNKYLINGMNASnnRVQDLFG 132
Cdd:PRK00064 72 GRVEKG-------GRELPLGLEIDKK----GGRKVRINGEPQR--KLAELAG 110
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
3-87 |
2.16e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 60.71 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 3 IKSIVLEGFKSyaqrteIRDFD-PL--FNAITGLNGSGKSNILDSICFL--LGISNLSQVRASS--LQDLVYKNGQAGVN 75
Cdd:COG4637 2 ITRIRIKNFKS------LRDLElPLgpLTVLIGANGSGKSNLLDALRFLsdAARGGLQDALARRggLEELLWRGPRTITE 75
|
90
....*....|..
gi 2500794 76 KATVSITFDNSD 87
Cdd:COG4637 76 PIRLELEFAEED 87
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
192-871 |
2.47e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 192 LDEIRRIItEEISPTLEKLKEARASYLEYQKMTREVENLRRIYVAFQYVRAEEIKDRSTNALKEAQANKKKIFESMAENE 271
Cdd:COG4913 237 LERAHEAL-EDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 272 KKVKELAQQIEETEKKNNEEFGAKLHSLEAAFSELQRvdakvrsDLDHRKQNLNSEENRLKELikimqeefkaftskeke 351
Cdd:COG4913 316 ARLDALREELDELEAQIRGNGGDRLEQLEREIERLER-------ELEERERRRARLEALLAAL----------------- 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 352 ikkikeglnGLQEESkkDAEALASAQQHFNAVSAGLSSNdsgqgtsladqmmtcKNEISKAATEAKQAQMKLKYAQQELK 431
Cdd:COG4913 372 ---------GLPLPA--SAEEFAALRAEAAALLEALEEE---------------LEALEEALAEAEAALRDLRRELRELE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 432 TKQAEVKKMDGSYKEDQEAF-EAIRKtkeklqdemkKLKYEEAEqeahlakkkqlsseissLRELCESIEakhpyLRFEy 510
Cdd:COG4913 426 AEIASLERRKSNIPARLLALrDALAE----------ALGLDEAE-----------------LPFVGELIE-----VRPE- 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 511 knpEKNWNPncvkglvvtlitvkdistskALEAVAGGKLYNIVVDTEATGK--KILEKGQLKHRytiIPLSKISANSIGH 588
Cdd:COG4913 473 ---EERWRG--------------------AIERVLGGFALTLLVPPEHYAAalRWVNRLHLRGR---LVYERVRTGLPDP 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 589 EIISLAKNLIGHReVHIAIS-LIDY-NSELQKAMEYVfgttlVCSSMDNAKKVtfdkrimRKTVTLQGDIFDPQGTLSGG 666
Cdd:COG4913 527 ERPRLDPDSLAGK-LDFKPHpFRAWlEAELGRRFDYV-----CVDSPEELRRH-------PRAITRAGQVKGNGTRHEKD 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 667 ASSHVT--PIL-----SKLKTMRD----AEDELKIKTSQLEATEKELANLKNMAEKYQHLKQQWE----MKSEEAELLQT 731
Cdd:COG4913 594 DRRRIRsrYVLgfdnrAKLAALEAelaeLEEELAEAEERLEALEAELDALQERREALQRLAEYSWdeidVASAEREIAEL 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 732 KIQQSAYHKQQEDLLALKKTIAECEETLKKTEESQRKAEEEYKALENKMKNAEAergkEIKNAQQKLNSAKKKADdssrk 811
Cdd:COG4913 674 EAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE----ELDELQDRLEAAEDLAR----- 744
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2500794 812 mkekqqevEALVLELEQLKQE---QASYKQQSEAAQQAIASLKEQVSALEAEAVKTRESLKNA 871
Cdd:COG4913 745 --------LELRALLEERFAAalgDAVERELRENLEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1104-1156 |
3.12e-09 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 59.12 E-value: 3.12e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2500794 1104 FKPAPIYILDEVDAALDlshTQNIGQMlhAHF------KQSQFLVVSLKDGMFNNANVL 1156
Cdd:cd03275 175 YQPAPFFVLDEVDAALD---NTNVGKV--ASYireqagPNFQFIVISLKEEFFSKADAL 228
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
684-877 |
4.45e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.84 E-value: 4.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 684 AEDELKIKTSQLEATEKEL----ANLKNMAEKYQHLKQQWEMKSEEAELLQTKIQQSayhkqQEDLLALKKTIAECEETL 759
Cdd:COG3883 14 ADPQIQAKQKELSELQAELeaaqAELDALQAELEELNEEYNELQAELEALQAEIDKL-----QAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 760 KKTEESQRKAEEEYKALE------------------NKMKNAEAERGKEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEA 821
Cdd:COG3883 89 GERARALYRSGGSVSYLDvllgsesfsdfldrlsalSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 822 LVLELEQLKQEQ----ASYKQQSEAAQQAIASLKEQVSALEAEAVKTRESLKNAENELSS 877
Cdd:COG3883 169 AKAELEAQQAEQeallAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-197 |
8.91e-09 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 56.35 E-value: 8.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 6 IVLEGFKSYaQRTEIrDFDPLFNAITGLNGSGKSNILDSICFLLG--ISNLSQVRASSLQDLVYKNGQAGVNKATVSITF 83
Cdd:pfam13476 1 LTIENFRSF-RDQTI-DFSKGLTLITGPNGSGKTTILDAIKLALYgkTSRLKRKSGGGFVKGDIRIGLEGKGKAYVEITF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 84 DNSDKKNSPLgFENNDEITITRQVIVGGRNKYLINgMNASNNRVQDLFGSvgLNVNNPHFLIM-QGQITKVLNMKPTEIL 162
Cdd:pfam13476 79 ENNDGRYTYA-IERSRELSKKKGKTKKKEILEILE-IDELQQFISELLKS--DKIILPLLVFLgQEREEEFERKEKKERL 154
|
170 180 190
....*....|....*....|....*....|....*
gi 2500794 163 AMIEEAAGTRMYECKKITAHKTIEKKESKLDEIRR 197
Cdd:pfam13476 155 EELEKALEEKEDEKKLLEKLLQLKEKKKELEELKE 189
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
193-949 |
1.30e-08 |
|
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: 59.47 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 193 DEIRRIitEEISPTLEKLKEARAsyleyqkmTREVENLRRIYVAFQYVRAEEIKDRSTNALKEAQANKKKIFESMaenEK 272
Cdd:pfam12128 231 QAIAGI--MKIRPEFTKLQQEFN--------TLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTL---DD 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 273 KVKELAQQIEETEKKNNEEFGAKLHSLEAAFSELQRVDakvRSDLDHRKQNLNSEENRLKELiKIMQEEFKAFTSK---- 348
Cdd:pfam12128 298 QWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFL---DADIETAAADQEQLPSWQSEL-ENLEERLKALTGKhqdv 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 349 --------EKEIKKIKEGLNGLQEESKKDAEA----LASAQQHFNAVSAGLSSNDSGQGTSLADQmmtcKNEISKAATEA 416
Cdd:pfam12128 374 takynrrrSKIKEQNNRDIAGIKDKLAKIREArdrqLAVAEDDLQALESELREQLEAGKLEFNEE----EYRLKSRLGEL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 417 KQAQMKLKYAQQELKTKQAEVKKMDGSykedQEAFEAIRKTKEKLQDEMKKLKYEEAEQEAHLAKKKQLSSEI-SSLREL 495
Cdd:pfam12128 450 KLRLNQATATPELLLQLENFDERIERA----REEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERqSALDEL 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 496 CESIEAK----HPYLRfeykNPEKNWNPNCVKGLVVTLITVKDISTSKALEAVAGG-KLYNIVVDTEATGkkilekgqlk 570
Cdd:pfam12128 526 ELQLFPQagtlLHFLR----KEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGElNLYGVKLDLKRID---------- 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 571 hrytiIPLSKISANSIGHEIISLAKNLIGHREVHIAIS--LIDYNSELQKAmeyvfgttlvcssmdnAKKVTFDKRIMRK 648
Cdd:pfam12128 592 -----VPEWAASEEELRERLDKAEEALQSAREKQAAAEeqLVQANGELEKA----------------SREETFARTALKN 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 649 TVTLQGDIFDPQGTLsggasshvtpilsKLKTMRDAEDELKIKTSQLEATEKELANLKNmaEKYQHLKQQWEMKSEeael 728
Cdd:pfam12128 651 ARLDLRRLFDEKQSE-------------KDKKNKALAERKDSANERLNSLEAQLKQLDK--KHQAWLEEQKEQKRE---- 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 729 LQTKIQQsayhKQQEDLLALKKTIAECEETLKKtEESQRKAEEeyKALENKMKNAEAERG----------KEIKNAQQKL 798
Cdd:pfam12128 712 ARTEKQA----YWQVVEGALDAQLALLKAAIAA-RRSGAKAEL--KALETWYKRDLASLGvdpdviaklkREIRTLERKI 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 799 NSAKKKADDSSRKMKEKQ----QEVEALVLELEQLKQEQASYKQQ----SEAAQQAIASLKEQVSALEAEAVKTRESLKN 870
Cdd:pfam12128 785 ERIAVRRQEVLRYFDWYQetwlQRRPRLATQLSNIERAISELQQQlarlIADTKLRRAKLEMERKASEKQQVRLSENLRG 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 871 AENELSSEKGLMEERTKD-----IKAKSAKIEKYREQNNELQLSINA-LEHDIN---------------KYQQETADASS 929
Cdd:pfam12128 865 LRCEMSKLATLKEDANSEqaqgsIGERLAQLEDLKLKRDYLSESVKKyVEHFKNviadhsgsglaetweSLREEDHYQND 944
|
810 820
....*....|....*....|
gi 2500794 930 TLDKLLKEYKWIASEKELFG 949
Cdd:pfam12128 945 KGIRLLDYRKLVPYLEQWFD 964
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-105 |
3.08e-08 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 55.31 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 3 IKSIVLEGFKSYAQRTEIrDFDPLFNAITGLNGSGKSNILDSICF-LLGISNLSQVRASSLQDLVYKngqaGVNKATVSI 81
Cdd:cd03240 1 IDKLSIRNIRSFHERSEI-EFFSPLTLIVGQNGAGKTTIIEALKYaLTGELPPNSKGGAHDPKLIRE----GEVRAQVKL 75
|
90 100
....*....|....*....|....
gi 2500794 82 TFDNSDKKnsplgfenndEITITR 105
Cdd:cd03240 76 AFENANGK----------KYTITR 89
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
735-1027 |
3.36e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 735 QSAYHKQQEDLLALKKTIAECEETLKKTEESQRKAEEEYKALENKMKnaeaergkEIKNAQQKLnsakkkaddssRKMKE 814
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLR--------EINEISSEL-----------PELRE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 815 KQQEVEALVLELEQLKQEQASYKQQSEAAQQAIASLKEQVSALE---AEAVKTRESLKNAENELSSEKGLMEERTKDIKA 891
Cdd:PRK03918 222 ELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEeriEELKKEIEELEEKVKELKELKEKAEEYIKLSEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 892 KsakiEKYREQNNELQLSINALEHDINKYQQETADASST---LDKLLKEYKWIASEKELFgqadttydfeannpKETGQK 968
Cdd:PRK03918 302 Y----EEYLDELREIEKRLSRLEEEINGIEERIKELEEKeerLEELKKKLKELEKRLEEL--------------EERHEL 363
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2500794 969 LQKLLTKKEKLEKSLNMRAMNLLSEAEERYNDLMKKKRMVENDKIKILATIEELDRKKN 1027
Cdd:PRK03918 364 YEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIK 422
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-84 |
4.85e-08 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 56.55 E-value: 4.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 1 MYIKSIVLEGFKSYaQRTEIrDFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASslqDLvYKNGQAGVNKATVS 80
Cdd:COG3593 1 MKLEKIKIKNFRSI-KDLSI-ELSDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFDEE---DF-YLGDDPDLPEIEIE 74
|
....
gi 2500794 81 ITFD 84
Cdd:COG3593 75 LTFG 78
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
676-945 |
5.24e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 57.44 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 676 SKLKTMRDAEDELKIKTSQLEATEKELANLKNMA----EKYQHLKQQWE-MKSEEAELLQTKIQQSAYHK-------QQE 743
Cdd:pfam15921 493 SSERTVSDLTASLQEKERAIEATNAEITKLRSRVdlklQELQHLKNEGDhLRNVQTECEALKLQMAEKDKvieilrqQIE 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 744 DLLAL------------------KKTIAECEETLKKTEESQRKAEEEYKALENKMKNAEAERGKEIKNAQQKLNSA---K 802
Cdd:pfam15921 573 NMTQLvgqhgrtagamqvekaqlEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVkdiK 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 803 KKADDSSRKMKEKQQEVEALVLELEQLKQeqaSYKQQSEAAQQAIASLKEQVSALEAEAVKTRESLKNAENELSSEKGLM 882
Cdd:pfam15921 653 QERDQLLNEVKTSRNELNSLSEDYEVLKR---NFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVA 729
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2500794 883 EERTKDIKAKsakiekyREQNNELQLSINALEHDINKYQQETADASSTLDKLLKEYKWIASEK 945
Cdd:pfam15921 730 MGMQKQITAK-------RGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEK 785
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
3-135 |
6.19e-08 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213209 [Multi-domain] Cd Length: 270 Bit Score: 55.38 E-value: 6.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 3 IKSIVLEGFKSYAqrtEIR-DFDPLFNAITGLNGSGKSNILDSICFLlgiSNLSQVRASSLQDLVykngQAGVNKATVSI 81
Cdd:cd03242 1 LKSLELRNFRNYA---ELElEFEPGVTVLVGENAQGKTNLLEAISLL---ATGKSHRTSRDKELI----RWGAEEAKISA 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2500794 82 TFDNSdkknsplGFENNDEITITRqvivGGRNKYLINGMNAsnNRVQDLFGSVG 135
Cdd:cd03242 71 VLERQ-------GGELALELTIRS----GGGRKARLNGIKV--RRLSDLLGVLN 111
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
676-896 |
7.28e-08 |
|
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: 56.78 E-value: 7.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 676 SKLKTMRDAEDELKIKTSQLEATEKELANlknmaeKYQHLKQqwemkseEAELLQTKIQQSAYHKQQEdllalKKTIAEC 755
Cdd:pfam09726 409 AELQASRQTEQELRSQISSLTSLERSLKS------ELGQLRQ-------ENDLLQTKLHNAVSAKQKD-----KQTVQQL 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 756 EETLKK------------TEESQRKAEEEYKALENKMKNAEA--ERGKEIKNAQQKLNSAKKKAddsSRKMKEKQQEVEA 821
Cdd:pfam09726 471 EKRLKAeqearasaekqlAEEKKRKKEEEATAARAVALAAASrgECTESLKQRKRELESEIKKL---THDIKLKEEQIRE 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 822 LVLELEQLKQEQASYKqQSEAAQQAIASLKEQVSALEAE-AVKTR------ESLKNAENELSSEKGLMEERTKDIKAKSA 894
Cdd:pfam09726 548 LEIKVQELRKYKESEK-DTEVLMSALSAMQDKNQHLENSlSAETRikldlfSALGDAKRQLEIAQGQIYQKDQEIKDLKQ 626
|
..
gi 2500794 895 KI 896
Cdd:pfam09726 627 KI 628
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
694-921 |
7.47e-08 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 56.67 E-value: 7.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 694 QLEATEKELANLKNMAEKYQH-LKQQWEMKSEEAELLQTKIQQ---------SAYHKQQEDLLALKKTIAECEETLKKTE 763
Cdd:pfam05557 17 EKKQMELEHKRARIELEKKASaLKRQLDRESDRNQELQKRIRLlekreaeaeEALREQAELNRLKKKYLEALNKKLNEKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 764 ESQRKAEEEYKALENKMknaeAERGKEIKNAQQKLNSAKKKADDSSRKMKEKQQ--------------------EVEALV 823
Cdd:pfam05557 97 SQLADAREVISCLKNEL----SELRRQIQRAELELQSTNSELEELQERLDLLKAkaseaeqlrqnlekqqsslaEAEQRI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 824 LELEQLKQEQASYKQQSEAAQQAIASLKEqvsaLEAEAVKTRESLKNAeNELSSEKGLMEERTKDIKAKSAKIEKYREQN 903
Cdd:pfam05557 173 KELEFEIQSQEQDSEIVKNSKSELARIPE----LEKELERLREHNKHL-NENIENKLLLKEEVEDLKRKLEREEKYREEA 247
|
250
....*....|....*...
gi 2500794 904 NELQLSINALEHDINKYQ 921
Cdd:pfam05557 248 ATLELEKEKLEQELQSWV 265
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
742-878 |
8.16e-08 |
|
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: 54.55 E-value: 8.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 742 QEDLLALKKTIAECEETLKKTEESQRKAEEEYKALENKMKNAEAERG-----KEIKNAQQKLNSAKKKADDSSRKMKEKQ 816
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvrnnKEYEALQKEIESLKRRISDLEDEILELM 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2500794 817 QEVEALVLELEQLKQEQASYKQQSEAAQqaiASLKEQVSALEAEAVKTRESLKNAENELSSE 878
Cdd:COG1579 117 ERIEELEEELAELEAELAELEAELEEKK---AELDEELAELEAELEELEAEREELAAKIPPE 175
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
678-876 |
8.57e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 8.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 678 LKTMRDAEDELKIKTSQLEATEKELANLKNMAEKYQHLKQQWEMKSEEAELLQTKIQQSAYHKQQEDLLALKKTIAECEE 757
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 758 TLKKTEESQRKAEEEYKALENkmknaeaergkEIKNAQQKLNSAKKKADDssrkmkEKQQEVEALVLELEQLKQEQASYK 837
Cdd:COG4717 150 ELEERLEELRELEEELEELEA-----------ELAELQEELEELLEQLSL------ATEEELQDLAEELEELQQRLAELE 212
|
170 180 190
....*....|....*....|....*....|....*....
gi 2500794 838 QQSEAAQQAIASLKEQVSALEAEAVKTRESLKNAENELS 876
Cdd:COG4717 213 EELEEAQEELEELEEELEQLENELEAAALEERLKEARLL 251
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
747-932 |
9.77e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 9.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 747 ALKKTIAECEETLKKTEESQRKAEEEYKALENK---MKNAEAERGKEIKNAQ-----QKLNSAKKKADDSSRKMKEKQQE 818
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERreaLQRLAEYSWDEIDVASaereiAELEAELERLDASSDDLAALEEQ 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 819 VEALVLELEQLKQEQASYKQQSEAAQQAIASLKEQVSALE-----AEAVKTRESLKNAENELSSEkgLMEERTKDIKAK- 892
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQdrleaAEDLARLELRALLEERFAAA--LGDAVERELRENl 771
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2500794 893 SAKIEKYREQNNELQlsiNALEHDINKYQQETADASSTLD 932
Cdd:COG4913 772 EERIDALRARLNRAE---EELERAMRAFNREWPAETADLD 808
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
709-905 |
1.24e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.20 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 709 AEKYQHLKQQWEMKSEEAELLQTKIQQSAYHKQQEDLLALKKtIAECEETLKKTEESQRKAEEEYKALENKMKNAEAERG 788
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQER-LKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 789 KEIKNAQQKLNSAKKKADDSSRKMKEkqqEVEALVLELEQLKQEQASYKQQSEAAQQAIASLKEQVSALEAEAVKTRESL 868
Cdd:PRK09510 140 KAAAAAKAKAEAEAKRAAAAAKKAAA---EAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAK 216
|
170 180 190
....*....|....*....|....*....|....*....
gi 2500794 869 KNAENE--LSSEKGLMEERTKDIKAKSAKIEKYREQNNE 905
Cdd:PRK09510 217 KKAAAEakAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
800-1029 |
1.30e-07 |
|
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: 55.16 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 800 SAKKKADDSSRKMKEKQQEVEALVLELEQLKQEQASYKQQSEAAQQAIASLKEQVSALEAEAVKTRESLKNAENELSSEK 879
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 880 GLMEERTKDIKAKSAKIEKYREQNNELQL----SINALEHDINKYQQETADASSTLDKLLKEYKWIASEKELFGQADTTY 955
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPLALLlspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2500794 956 DFEANNPKETGQKLQKLLTKKEKLEKSLNMRamnlLSEAEERYNDLMKKKRMVENDKIKILATIEELDRKKNKA 1029
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKE----LAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-63 |
1.63e-07 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 54.23 E-value: 1.63e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2500794 1 MYIKSIVLEGFKSYAQRtEIrDFD--PLFNAITGLNGSGKSNILDSICFLLG--ISNLSQVRASSLQ 63
Cdd:COG3950 1 MRIKSLTIENFRGFEDL-EI-DFDnpPRLTVLVGENGSGKTTLLEAIALALSglLSRLDDVKFRKLL 65
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
750-947 |
1.91e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 750 KTIAECEETLKKTEESqrkaEEEYKALENKMKNAEAErgkeIKNAQQKLNSAKKKaddssRKMKEKQQEVEALVLELEQL 829
Cdd:COG4717 71 KELKELEEELKEAEEK----EEEYAELQEELEELEEE----LEELEAELEELREE-----LEKLEKLLQLLPLYQELEAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 830 KQEQASYKQQSEAAQQAIASLKE---QVSALEAEAVKTRESLKNAENELSsekglmeertkdiKAKSAKIEKYREQNNEL 906
Cdd:COG4717 138 EAELAELPERLEELEERLEELREleeELEELEAELAELQEELEELLEQLS-------------LATEEELQDLAEELEEL 204
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2500794 907 QLSINALEHDINKYQQETADASSTLDKLLKEYKWIASEKEL 947
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERL 245
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
681-913 |
2.10e-07 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 55.03 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 681 MRDAEDELKIKTSQLEATEKE-LANLKNMAEKYQHLKQQWE---MKSEEAEL--LQTKIQQSayhkqQEDLLALKKTIAE 754
Cdd:pfam05667 286 GSSTTDTGLTKGSRFTHTEKLqFTNEAPAATSSPPTKVETEeelQQQREEELeeLQEQLEDL-----ESSIQELEKEIKK 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 755 CEETLKKTEESQRKAEEEYKALENKMKNAEaERGKEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEA----LVLELEQLK 830
Cdd:pfam05667 361 LESSIKQVEEELEELKEQNEELEKQYKVKK-KTLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKhrvpLIEEYRALK 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 831 QEQAsyKQQSEAAQQA--IASLKEQVSALEAEAVKTRESLKNAENELSSEKGLME---------ERTKDIKAKSAKIEKY 899
Cdd:pfam05667 440 EAKS--NKEDESQRKLeeIKELREKIKEVAEEAKQKEELYKQLVAEYERLPKDVSrsaytrrilEIVKNIKKQKEEITKI 517
|
250
....*....|....
gi 2500794 900 REQNNELQLSINAL 913
Cdd:pfam05667 518 LSDTKSLQKEINSL 531
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
681-993 |
2.18e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.50 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 681 MRDAEDELKIKTSQLEATEKELanlknmaEKYQHLKQQWEMKSEEAELLQTKIQQSAYHKQQEDLLAlkKTIAECEETLK 760
Cdd:pfam05483 372 LEKNEDQLKIITMELQKKSSEL-------EEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIA--EELKGKEQELI 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 761 KTEESQRKAEEEYKALENKMKNAEAERGKEIKNAQQKLNSAKKK-------ADDSSRKMKEKQQEVEALVLELEQLKQEQ 833
Cdd:pfam05483 443 FLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKnieltahCDKLLLENKELTQEASDMTLELKKHQEDI 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 834 ASYKQQSEAAQQAIASLKEQVSALEAEAVKTRESLKNAENELSSEKGLMEERTKDIKAKSAKIEK----YREQNNELQLS 909
Cdd:pfam05483 523 INCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKqmkiLENKCNNLKKQ 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 910 INALEHDINKYQQET---ADASSTLDKLLKEYKW--------IASEKELFGQADTTYDFEANNPKETGQKLQKLLTKKE- 977
Cdd:pfam05483 603 IENKNKNIEELHQENkalKKKGSAENKQLNAYEIkvnkleleLASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKa 682
|
330 340
....*....|....*....|..
gi 2500794 978 ------KLEKSLNMRAMNLLSE 993
Cdd:pfam05483 683 iadeavKLQKEIDKRCQHKIAE 704
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
757-953 |
2.22e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 757 ETLKKTEESQRKAEEEYKALEnkmknaeaergkEIKNAQQKLNSAKKKADdssrkmkekQQEVEALVLELEQLKQEQASY 836
Cdd:COG4913 235 DDLERAHEALEDAREQIELLE------------PIRELAERYAAARERLA---------ELEYLRAALRLWFAQRRLELL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 837 KQQSEAAQQAIASLKEQVSALEAEAVKTRESLKNAENELSSEKG--------LMEERTKDIKAKSAKIEKYREQNNELQL 908
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGdrleqlerEIERLERELEERERRRARLEALLAALGL 373
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2500794 909 SINALEHDINKYQQETADASSTLDKLLKE-----YKWIASEKELFGQADT 953
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEEELEAleealAEAEAALRDLRRELRE 423
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
679-983 |
5.46e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.87 E-value: 5.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 679 KTMRDAEDELKIKTSQLEATEKELANLKNMAEKYQHLKQQWEMKSEEaelLQTKIQQSayhkqqedllalKKTIAECEET 758
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIND---LESKIQNQ------------EKLNQQKDEQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 759 LKKTEESQRKAEEEYKALenkmKNAEAERGKEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEALVLELEQLKQEQASYKQ 838
Cdd:TIGR04523 414 IKKLQQEKELLEKEIERL----KETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQK 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 839 QSEAAQQAIASLKEQVSALE---AEAVKTRESLKNAENELSSEKGLMEERTKDIKAKSAKI------EKYREQNNELQLS 909
Cdd:TIGR04523 490 ELKSKEKELKKLNEEKKELEekvKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDdfelkkENLEKEIDEKNKE 569
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2500794 910 INALEHDINKYQQETADASSTLDKLLKEYKWIASEKELFGQADTTYDFEANNPKETGQKL----QKLLTKKEKLEKSL 983
Cdd:TIGR04523 570 IEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLssiiKNIKSKKNKLKQEV 647
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
677-1022 |
6.20e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.87 E-value: 6.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 677 KLKTMRDAEDELKIKTSQLEATEKELANLKNMAEK--YQHLKQQWEMKSEEAELLQTKIQQSayhkqQEDLLALKKTIAE 754
Cdd:TIGR04523 272 KQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwNKELKSELKNQEKKLEEIQNQISQN-----NKIISQLNEQISQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 755 CEETLKKTEESQRKAEEEYKALENKMKNAEAERG---KEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEALVLELEQLKQ 831
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEKLKKENQsykQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 832 EQASYKQQSEAAQQAIASLKEQVSALEAEAVK---TRESLKNA----ENELSSEKGLMEERTKDIKAKSAKIEKYREQNN 904
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNQDSVKELIIKNldnTRESLETQlkvlSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 905 ELQ--------------LSINALEHDINKYQQETADASSTLDKLLKEYKWIASEKELFGQADT------TYDFEANNPKE 964
Cdd:TIGR04523 507 ELEekvkdltkkisslkEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEieelkqTQKSLKKKQEE 586
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2500794 965 TGQKLQKLLTKKEKLEKSLNMRAMnLLSEAEERYNDLMKKKRMVENDKIKILATIEEL 1022
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEIEEKEK-KISSLEKELEKAKKENEKLSSIIKNIKSKKNKL 643
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
682-1030 |
7.57e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 7.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 682 RDAEDELKIKTSQLEATEKElANLKNMAEKYQHLKQQWEMKSEEAELLQTKIQ--QSAYHKQQEDLLALKKTIAECEETL 759
Cdd:PRK02224 322 RDEELRDRLEECRVAAQAHN-EEAESLREDADDLEERAEELREEAAELESELEeaREAVEDRREEIEELEEEIEELRERF 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 760 KKTEESQRKAEEEYKALE---NKMKNAEAERGKEIKNAQQKLNSAKKKAD------------DSSR--KMKEKQQEVEAL 822
Cdd:PRK02224 401 GDAPVDLGNAEDFLEELReerDELREREAELEATLRTARERVEEAEALLEagkcpecgqpveGSPHveTIEEDRERVEEL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 823 VLELEQLKQEQASYKQQSEAAQQA----------------------------------IASLKEQVSALEAEAVKTRESL 868
Cdd:PRK02224 481 EAELEDLEEEVEEVEERLERAEDLveaedrierleerredleeliaerretieekrerAEELRERAAELEAEAEEKREAA 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 869 KNAENELSSEKglmeERTKDIKAKSAKIEKYREQNNELQLSINALEhDINKYQQETADASSTLDKLLKEYKWIASEK--- 945
Cdd:PRK02224 561 AEAEEEAEEAR----EEVAELNSKLAELKERIESLERIRTLLAAIA-DAEDEIERLREKREALAELNDERRERLAEKrer 635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 946 --ELFGqadttyDFEANNPKETGQKLQKLLTKKEKLEKSLNmramnllsEAEERYNDLMKKKRMVENDkikiLATIEELd 1023
Cdd:PRK02224 636 krELEA------EFDEARIEEAREDKERAEEYLEQVEEKLD--------ELREERDDLQAEIGAVENE----LEELEEL- 696
|
....*..
gi 2500794 1024 RKKNKAL 1030
Cdd:PRK02224 697 RERREAL 703
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
1-89 |
7.85e-07 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 51.12 E-value: 7.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 1 MYIKSIVLEGFKSYAQRTEIrDF-----DPLFnAITGLNGSGKSNILDSICFLLgisnLSQVRASSLQDLVYKNGQAGVN 75
Cdd:cd03279 1 MKPLKLELKNFGPFREEQVI-DFtgldnNGLF-LICGPTGAGKSTILDAITYAL----YGKTPRYGRQENLRSVFAPGED 74
|
90
....*....|....
gi 2500794 76 KATVSITFDNSDKK 89
Cdd:cd03279 75 TAEVSFTFQLGGKK 88
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
3-89 |
8.89e-07 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 51.06 E-value: 8.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 3 IKSIVLEGFKSYAQrTEIRdFDPLFNAITGLNGSGKSNILDSICFLLG--ISNLSqvRASSLQDLVyKNGQagvNKATVS 80
Cdd:cd03277 3 IVRIKLENFVTYDE-TEFR-PGPSLNMIIGPNGSGKSSIVCAICLGLGgkPKLLG--RAKKVGEFV-KRGC---DEGTIE 74
|
....*....
gi 2500794 81 ITFDNSDKK 89
Cdd:cd03277 75 IELYGNPGN 83
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
763-968 |
1.04e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 763 EESQRKAEEEYKALENKMKNAEAErgkeIKNAQQKLNSAKKKADDSSRKMKEKQQEVEALVLELEQLKQEQAsyKQQSEA 842
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAE----LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE--ERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 843 AQQAIASLKEQVSALEAEAVKTRESLKNA-------ENELSSEKGLMEERTKDIKAKSAKIEKYREQNNELQLSINALEH 915
Cdd:COG3883 89 GERARALYRSGGSVSYLDVLLGSESFSDFldrlsalSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2500794 916 DINKYQQETADASSTLDKLLKEYKWIASEKELFGQADTTYDFEANNPKETGQK 968
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
674-1090 |
1.18e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 674 ILSKLKTMRDAEDELKIKTSQLEATEKELANLKNMAEKYQHLKQqwemKSEEAELLQTKIQQSAYHKQQEDLLALKKTIA 753
Cdd:PRK03918 326 IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKA----KKEELERLKKRLTGLTPEKLEKELEELEKAKE 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 754 ECEETLKKTEESQRKAEEEYKALE---NKMKNA------------EAERGKEIKNAQQKLN---SAKKKADDSSRKMKEK 815
Cdd:PRK03918 402 EIEEEISKITARIGELKKEIKELKkaiEELKKAkgkcpvcgreltEEHRKELLEEYTAELKrieKELKEIEEKERKLRKE 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 816 QQEVEALVL-------------ELEQLKQEQASY-KQQSEAAQQAIASLKEQVSALEAEAVKTRESLKNaENELSSEKGL 881
Cdd:PRK03918 482 LRELEKVLKkeseliklkelaeQLKELEEKLKKYnLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK-LEELKKKLAE 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 882 MEERTKDIKAKSAKIEKYREQN-----NELQLSINALEHDINKY--------------------QQETADASSTLDKLLK 936
Cdd:PRK03918 561 LEKKLDELEEELAELLKELEELgfesvEELEERLKELEPFYNEYlelkdaekelereekelkklEEELDKAFEELAETEK 640
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 937 EYKWIASEKELFGQADTTYDFE--ANNPKETGQKLQKLLTKKEKLEKSLNmRAMNLLSEAEERYNDLMKKKRMVENDKiK 1014
Cdd:PRK03918 641 RLEELRKELEELEKKYSEEEYEelREEYLELSRELAGLRAELEELEKRRE-EIKKTLEKLKEELEEREKAKKELEKLE-K 718
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 1015 ILATIEELDRK----KNKALHIAWEKVNKDFGSIFSMLLPGAKAMLVPSKKQNildglefRVGLGDIW---KENLTELSG 1087
Cdd:PRK03918 719 ALERVEELREKvkkyKALLKERALSKVGEIASEIFEELTEGKYSGVRVKAEEN-------KVKLFVVYqgkERPLTFLSG 791
|
...
gi 2500794 1088 GQR 1090
Cdd:PRK03918 792 GER 794
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
695-931 |
1.90e-06 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 51.30 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 695 LEATEKELANLKNMAekyqhlkqqwemkseeAELLQTK---IQQSAYHKQQEDLLALKKTIAECEETLKKTEESQ---RK 768
Cdd:pfam09787 2 LESAKQELADYKQKA----------------ARILQSKeklIASLKEGSGVEGLDSSTALTLELEELRQERDLLReeiQK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 769 AEEEYKALENKMKNAEAERGKEIKNAQQKLNSAKKKAddssRKMKEKQQEVEAlvlELEQLKQEQASYKqqsEAAQQAIA 848
Cdd:pfam09787 66 LRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQL----ATERSARREAEA---ELERLQEELRYLE---EELRRSKA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 849 SLKEQVSALEAEAVKTRESLKNAENELSSEKGLmEER----TKDIKAKSAKIEKYREQNNELQLSINALEHDINKYQQET 924
Cdd:pfam09787 136 TLQSRIKDREAEIEKLRNQLTSKSQSSSSQSEL-ENRlhqlTETLIQKQTMLEALSTEKNSLVLQLERMEQQIKELQGEG 214
|
....*..
gi 2500794 925 ADASSTL 931
Cdd:pfam09787 215 SNGTSIN 221
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
676-1030 |
2.22e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.03 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 676 SKLKTMRDAEDELKIKTSQLE-ATEKELANLKNMAEKYQHLkqqwemkSEEAELLQTKIQQSAYHKQ--QEDLLALKKTI 752
Cdd:pfam05483 254 NKMKDLTFLLEESRDKANQLEeKTKLQDENLKELIEKKDHL-------TKELEDIKMSLQRSMSTQKalEEDLQIATKTI 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 753 AECEETLKKTEESQRKAEEEYKALENKMKNAEAERGKEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEALV-------LE 825
Cdd:pfam05483 327 CQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTkfknnkeVE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 826 LEQLKQEQASyKQQSEAAQQAIASLKEQVSALEAEAV---KTRE-SLKNAENELSSEKGLMEERTKDIKAKSAKIEKYRE 901
Cdd:pfam05483 407 LEELKKILAE-DEKLLDEKKQFEKIAEELKGKEQELIfllQAREkEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKL 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 902 QNNELQLSINALEHDINKYQQETADASSTLDKLLKEYKWIASEKE-LFGQADTTYDFEAN----------NPKETGQKLQ 970
Cdd:pfam05483 486 KNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEErMLKQIENLEEKEMNlrdelesvreEFIQKGDEVK 565
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 971 KLLTKKEKLEKSLNMRAMNLLSEAEERYNDLMKKKRMVENDKikilATIEELdRKKNKAL 1030
Cdd:pfam05483 566 CKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKN----KNIEEL-HQENKAL 620
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
682-877 |
2.61e-06 |
|
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: 51.30 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 682 RDAEDELKIKTSQLEATEKELANLKNMAEKYQHLKQQWEMKSEEAELLQTKIQQsAYHKQQEDLLALKKTIAECEETLKK 761
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ-ELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 762 TEE----------------------SQRKAEEEYKALE--NKMKNAEAERGKEIKNAQQKLNSAKKKADDSSRKMKEKQQ 817
Cdd:COG4942 102 QKEelaellralyrlgrqpplalllSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2500794 818 EVEALVLELEQLKQEQ----ASYKQQSEAAQQAIASLKEQVSALEAEAVKTRESLKNAENELSS 877
Cdd:COG4942 182 ELEEERAALEALKAERqkllARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
668-1031 |
2.71e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.04 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 668 SSHVTPILSKLKTMRDAEDELKIKTSQLEATEKELANLKNMaekyqHLKQQWEMKSEEAELLQTKIQQSAYHKQQEDLLA 747
Cdd:pfam15921 274 SEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSM-----YMRQLSDLESTVSQLRSELREAKRMYEDKIEELE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 748 LKKTIAECEETLKKTEESQrkAEEEYKALENKMKNAEAERGKEIKNAQQKLNSAKKKADDSS----------RKMKEKQQ 817
Cdd:pfam15921 349 KQLVLANSELTEARTERDQ--FSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTgnsitidhlrRELDDRNM 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 818 EVEALVLELEQLKQE-QASYKQQSEAAQQAIASLkEQVSALEAEAVKTRESLKNAENELSSEKGLME------------- 883
Cdd:pfam15921 427 EVQRLEALLKAMKSEcQGQMERQMAAIQGKNESL-EKVSSLTAQLESTKEMLRKVVEELTAKKMTLEssertvsdltasl 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 884 -ERTKDIKAKSAKIEKYREQNN----ELQLSINALEH------DINKYQQETADASSTLDKLLKEykwIASEKELFGQAd 952
Cdd:pfam15921 506 qEKERAIEATNAEITKLRSRVDlklqELQHLKNEGDHlrnvqtECEALKLQMAEKDKVIEILRQQ---IENMTQLVGQH- 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 953 ttydfeannpketGQKLQKLLTKKEKLEKSLNMRAMNL-------------LSEAEERYNDLMKKKRMVENDKIKILATI 1019
Cdd:pfam15921 582 -------------GRTAGAMQVEKAQLEKEINDRRLELqefkilkdkkdakIRELEARVSDLELEKVKLVNAGSERLRAV 648
|
410
....*....|..
gi 2500794 1020 EELDRKKNKALH 1031
Cdd:pfam15921 649 KDIKQERDQLLN 660
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
22-123 |
2.96e-06 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 51.23 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 22 DFDPLFNAITGLNGSGKSNILDSICFLLGisnlsqVRASSlqDLVYkngqAGVNKATVSITFDNSDkkNSPL-------G 94
Cdd:COG0497 19 EFGPGLTVLTGETGAGKSILLDALGLLLG------GRADA--SLVR----HGADKAEVEAVFDLSD--DPPLaawleenG 84
|
90 100 110
....*....|....*....|....*....|
gi 2500794 95 FENND-EITITRQVIVGGRNKYLINGMNAS 123
Cdd:COG0497 85 LDLDDgELILRREISADGRSRAFINGRPVT 114
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
683-916 |
7.63e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 7.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 683 DAEDELKIKTSQLEATEKELANLknmAEKYQHLKQQWEMKSEEAELLQTKIQQSayhkqqeDLLA---LKKTIAECEETL 759
Cdd:PRK04863 834 DPEAELRQLNRRRVELERALADH---ESQEQQQRSQLEQAKEGLSALNRLLPRL-------NLLAdetLADRVEEIREQL 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 760 KKTEESQR----------KAEEEYKALENKMKNAEAERGkEIKNAQQKLNSAKKKAD---------------DSSRKMKE 814
Cdd:PRK04863 904 DEAEEAKRfvqqhgnalaQLEPIVSVLQSDPEQFEQLKQ-DYQQAQQTQRDAKQQAFaltevvqrrahfsyeDAAEMLAK 982
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 815 KQQEVEALVLELEQLKQEQASYKQQSEAAQQAIASLKEQVSALEAEAVKTRESLKNAENELsSEKGLMEERTKDIKAKSA 894
Cdd:PRK04863 983 NSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQEL-QDLGVPADSGAEERARAR 1061
|
250 260 270
....*....|....*....|....*....|
gi 2500794 895 KIEKY------REQNNEL--QLSINALEHD 916
Cdd:PRK04863 1062 RDELHarlsanRSRRNQLekQLTFCEAEMD 1091
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
752-1086 |
1.27e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 752 IAECEETLKKTEESQRKAEEEYKALENKMKNAEaergKEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEALVLELEQLKQ 831
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAR----EELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 832 EQASYKQQSEAAQQAIASLKEQVSALEAEAVKTRESLKNAENELSSEKGLMEERTKDIKAKSAKIEKYREQNNelQLSIN 911
Cdd:COG4372 102 ELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ--ALSEA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 912 ALEHDINKYQQEtadASSTLDKLLKEYKWIASEKELFGQADTTYDFEANNPKETGQKLQKLLTKKEKLEKSLNMRAMNLL 991
Cdd:COG4372 180 EAEQALDELLKE---ANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 992 SEAEERYNDLMKKKRMVENDKIKILATIEELDRKKNKALHIAWEKVNKDFGSIFSMLLPGAKAMLVPSKKQNILDGLEFR 1071
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
330
....*....|....*
gi 2500794 1072 VGLGDIWKENLTELS 1086
Cdd:COG4372 337 AELADLLQLLLVGLL 351
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
684-1029 |
1.39e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 49.30 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 684 AEDELKIKTSQLEATEKELA----NLKNMAEKYQHLKQQWEMKSEEAE-LLQTKIQQSAYHKQQEDLLALKKTIAECEEt 758
Cdd:pfam05622 81 ARDDYRIKCEELEKEVLELQhrneELTSLAEEAQALKDEMDILRESSDkVKKLEATVETYKKKLEDLGDLRRQVKLLEE- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 759 lKKTEESQRKAEeeykaLENKMKNAEAERG------KEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEALVLELEQLKQE 832
Cdd:pfam05622 160 -RNAEYMQRTLQ-----LEEELKKANALRGqletykRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 833 QASYKQ----------QSEAAQQAIASLKEQVS-----ALEAEAVKTRESLKNAENE----LSSEKGLMEERTKDIKA-- 891
Cdd:pfam05622 234 RDTLREtneelrcaqlQQAELSQADALLSPSSDpgdnlAAEIMPAEIREKLIRLQHEnkmlRLGQEGSYRERLTELQQll 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 892 --KSAKIEKYREQNNELQLSINALEH---DINKYQQET---ADASSTLDKLLKEYKWIASEKELFGQADTTYdFEANNPK 963
Cdd:pfam05622 314 edANRRKNELETQNRLANQRILELQQqveELQKALQEQgskAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQ-IEELEPK 392
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2500794 964 ETGQKLQKLLTKKEKL-EKSLNMRAMnllseaEERYNDLMKKKRMVendkikilatIEELDRKKNKA 1029
Cdd:pfam05622 393 QDSNLAQKIDELQEALrKKDEDMKAM------EERYKKYVEKAKSV----------IKTLDPKQNPA 443
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
716-902 |
1.40e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 716 KQQWEMKSEEAELlqtkiqQSAYHKQQEDLLALKKTIAECEETLKKTEESQRKAEEEYKALENKMKNAEAERGKEIKNAQ 795
Cdd:COG3883 23 KELSELQAELEAA------QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 796 QK-------------------------LNSAKKKADDSSRKMKEKQQEVEALVLELEQLKQEQASYKQQSEAAQQAIASL 850
Cdd:COG3883 97 RSggsvsyldvllgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2500794 851 KEQVSALEAEAVKTRESLKNAENELSSEKGLMEERTKDIKAKSAKIEKYREQ 902
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
789-939 |
1.43e-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: 47.61 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 789 KEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEALVLELEQLKQEQASYKQQSEAAQQAIASLKEQVSAleaeaVKTRESL 868
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-----VRNNKEY 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2500794 869 KNAENELSSEKGLMEERTKDIKAKSAKIEKYREQNNELQLSINALEHDINKYQQETADASSTLDKLLKEYK 939
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
679-898 |
1.60e-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: 49.27 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 679 KTMRDAEDELKIKTSQLEATEKELANLKNMAEKYQHLKQQWEMKSEEAELLQTKIQQsAYHKQQEDLLALKKTIAECEET 758
Cdd:TIGR00606 850 KLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKD-AKEQDSPLETFLEKDQQEKEEL 928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 759 LKKTEESQRKAEEEYKALENKMKNAEAERgKEIKNAQQklnsakkkaDDSSRKMKEKQQEVEALVLELEQLKQEQASYKQ 838
Cdd:TIGR00606 929 ISSKETSNKKAQDKVNDIKEKVKNIHGYM-KDIENKIQ---------DGKDDYLKQKETELNTVNAQLEECEKHQEKINE 998
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2500794 839 QSEAAQQAIASLKEQVSALEAEAV--KTRESLKNAENELSSEKGLM-EERTKDIKAKSAKIEK 898
Cdd:TIGR00606 999 DMRLMRQDIDTQKIQERWLQDNLTlrKRENELKEVEEELKQHLKEMgQMQVLQMKQEHQKLEE 1061
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
674-902 |
1.73e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.98 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 674 ILSKLKTMRDAEDELKIKTSQLEATEKELANLKN-MAEKYQHLKQQWEMKSEEAELLQTKI-----QQSAYHKQQEDLLA 747
Cdd:COG1340 34 LNEELKELAEKRDELNAQVKELREEAQELREKRDeLNEKVKELKEERDELNEKLNELREELdelrkELAELNKAGGSIDK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 748 LKKTIAECE---ETLKKTEESQRKAEEEYKALENKMKNAEAERG--KEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEAL 822
Cdd:COG1340 114 LRKEIERLEwrqQTEVLSPEEEKELVEKIKELEKELEKAKKALEknEKLKELRAELKELRKEAEEIHKKIKELAEEAQEL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 823 VLELEQLKQEQASYKQQSEAAQQAIASLKEQVSALEAEAVKTRESLKNAENELSS--EKGLMEERTKDIKAKSAKIEKYR 900
Cdd:COG1340 194 HEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKlrKKQRALKREKEKEELEEKAEEIF 273
|
..
gi 2500794 901 EQ 902
Cdd:COG1340 274 EK 275
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
670-937 |
2.43e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.80 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 670 HVTPILSKLKTMRDAEDELKIKTSQLEATEKELANLKNmAEKyqHLKQQWEMKSEEAELLQTKI-QQSAYHKQQEDLLAL 748
Cdd:COG3096 283 LSERALELRRELFGARRQLAEEQYRLVEMARELEELSA-RES--DLEQDYQAASDHLNLVQTALrQQEKIERYQEDLEEL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 749 KKTIAECEETLKKTEESQRK-------AEEEYKALENKMK------NAEAERGKEIKNAQQKLNSAK----------KKA 805
Cdd:COG3096 360 TERLEEQEEVVEEAAEQLAEaearleaAEEEVDSLKSQLAdyqqalDVQQTRAIQYQQAVQALEKARalcglpdltpENA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 806 DDSSRKMKEKQQEVEALVLELEQLKQEQASYKQQSEAAQQAIASLKEQVSALEAeAVKTRESLKNAenelsSEKGLMEER 885
Cdd:COG3096 440 EDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVERSQA-WQTARELLRRY-----RSQQALAQR 513
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2500794 886 TKDIKAKSAKIEKYREQNNELQlsinALEHDINKYQQETADASSTLDKLLKE 937
Cdd:COG3096 514 LQQLRAQLAELEQRLRQQQNAE----RLLEEFCQRIGQQLDAAEELEELLAE 561
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
749-895 |
2.51e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 749 KKTIAECEETLKKT-EESQRKAE-----------EEYKALENKMKNAEAERGKEIKNAQQKLNSAKKKADDSSRKMKEKQ 816
Cdd:PRK12704 30 EAKIKEAEEEAKRIlEEAKKEAEaikkealleakEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKRE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 817 QEVEALVLELEQLKQEqasYKQQSEAAQQAIASLK---EQVSALEAEAVKtRESLKNAENELSSEKGLM----EERTKDI 889
Cdd:PRK12704 110 EELEKKEKELEQKQQE---LEKKEEELEELIEEQLqelERISGLTAEEAK-EILLEKVEEEARHEAAVLikeiEEEAKEE 185
|
....*.
gi 2500794 890 KAKSAK 895
Cdd:PRK12704 186 ADKKAK 191
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
756-939 |
2.66e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 756 EETLKKTEESQRKA----EEEYKALENKMKNAEAERgKEIKnAQQKLNSAKKKADDSSRKMKEKQQEVEALVLELEQLKQ 831
Cdd:COG3206 163 EQNLELRREEARKAleflEEQLPELRKELEEAEAAL-EEFR-QKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 832 EQASYKQQSEAAQQA---------IASLKEQVSALEAE--------------AVKTRESLKNAENELSSE-KGLMEERTK 887
Cdd:COG3206 241 RLAALRAQLGSGPDAlpellqspvIQQLRAQLAELEAElaelsarytpnhpdVIALRAQIAALRAQLQQEaQRILASLEA 320
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2500794 888 DIKAKSAKIEKYREQNNELQ---LSINALEHDINKYQQETADASSTLDKLLKEYK 939
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEarlAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
679-871 |
2.69e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.35 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 679 KTMRDA-EDELKIKTSQLEATEKELANLK----NMAEKYQHLKQQWEMKSEEAELLqtkIQQSAYHKQ-----QEDLLAL 748
Cdd:pfam07888 65 KRDREQwERQRRELESRVAELKEELRQSRekheELEEKYKELSASSEELSEEKDAL---LAQRAAHEArirelEEDIKTL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 749 KKTIAECEETLKKTEESQRKA-------EEEYKALENKMKNAEAE------RGKEIKNAQQKLNSAKKKADDSSRKMKEK 815
Cdd:pfam07888 142 TQRVLERETELERMKERAKKAgaqrkeeEAERKQLQAKLQQTEEElrslskEFQELRNSLAQRDTQVLQLQDTITTLTQK 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2500794 816 QQEVEALVLELEQLKQEQASYKQQSEAAQQAIASLKEQVSALEAEAVKTRESLKNA 871
Cdd:pfam07888 222 LTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQA 277
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
671-899 |
2.77e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 47.92 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 671 VTPILSKLKTMRDAEDELKIKTSQL--EATEKELANLKNMAEKYQHLKQQWEMKSEEAELLQTKIQQSAYHKQQEDLLAL 748
Cdd:TIGR02794 52 ANRIQQQKKPAAKKEQERQKKLEQQaeEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 749 KKTIAECEETLKKTEESQRKAEEEykalenKMKNAEAERGKEIKNAQQKLNSAKKKADDSsrkmKEKQQEVEAlvleleQ 828
Cdd:TIGR02794 132 AKAKAEAEAERKAKEEAAKQAEEE------AKAKAAAEAKKKAEEAKKKAEAEAKAKAEA----EAKAKAEEA------K 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2500794 829 LKQEQASYKQQSEAAQQAiASLKEQVSALEAEAvKTRESLKNAENELSSEKGLMEERTKDIKAKSAKIEKY 899
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKA-EAEAAAAAAAEAER-KADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKY 264
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
675-931 |
2.87e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 48.37 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 675 LSKLKTMRDAEDELKIKTSQLEATEKELANLKNMAEKYQHLKQQW-----EMKSEEAELlqTKIQQSAYHKQQEDLLALk 749
Cdd:PRK11281 45 LDALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLaqapaKLRQAQAEL--EALKDDNDEETRETLSTL- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 750 kTIAECEETLKKTEESQRKAEEEYKALENKMKNAEA--ERG-KEIKNAQ---QKLNSAKKKADDSSRKMKEKQQ-----E 818
Cdd:PRK11281 122 -SLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTqpERAqAALYANSqrlQQIRNLLKGGKVGGKALRPSQRvllqaE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 819 VEALVLELEQLKQE-------QASYKQQSEAAQQAIASLKEQVSALEaEAVktreslkNAENELSSEKGLMEERTKDIKA 891
Cdd:PRK11281 201 QALLNAQNDLQRKSlegntqlQDLLQKQRDYLTARIQRLEHQLQLLQ-EAI-------NSKRLTLSEKTVQEAQSQDEAA 272
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2500794 892 KSakiekyreQNNEL---QLSINaleHDINKYQQETADASSTL 931
Cdd:PRK11281 273 RI--------QANPLvaqELEIN---LQLSQRLLKATEKLNTL 304
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
673-907 |
2.91e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 673 PILSKLKTMRDAEDELKIKTSQLEATEKELANLKNMAEKYQHLKQQWEMKSEEAELLQTKI--QQSAYHKQQEDLLALKK 750
Cdd:PRK02224 465 PHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIaeRRETIEEKRERAEELRE 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 751 TIAECEETLKKTEESQRKAE-------EEYKALENKMKNAEAER----------------GKEIKNAQQKLNSAKKKADD 807
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEeeaeearEEVAELNSKLAELKERIeslerirtllaaiadaEDEIERLREKREALAELNDE 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 808 SSRKMKEKQQEVEALVLELEQLKQEQAsyKQQSEAAQQAIASLKEQVSALEAEAVKTRESLKNAENELSSEKGLMEERtK 887
Cdd:PRK02224 625 RRERLAEKRERKRELEAEFDEARIEEA--REDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERR-E 701
|
250 260
....*....|....*....|
gi 2500794 888 DIKAKSAKIEKYREQNNELQ 907
Cdd:PRK02224 702 ALENRVEALEALYDEAEELE 721
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
745-996 |
3.02e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.43 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 745 LLALKKTIAECEETLKKTEESQRKAEEEYKalenKMKNAEAERGKEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEALVL 824
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTQLALMEFA----KKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLRE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 825 ELEQLKQEQASYKQQSEAAQQAIA---SLKEQVSALE-AEAVKTRESLKNAENELSSEKglmeERTKDIKAKSAKIEKYR 900
Cdd:TIGR00618 234 ALQQTQQSHAYLTQKREAQEEQLKkqqLLKQLRARIEeLRAQEAVLEETQERINRARKA----APLAAHIKAVTQIEQQA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 901 EQ-NNELQLSINALEHDINKYQQETADASSTLDKLLKEYKWIASEKELFGQADTTYDFEANNPKETG--QKLQKLLTKKE 977
Cdd:TIGR00618 310 QRiHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTltQHIHTLQQQKT 389
|
250
....*....|....*....
gi 2500794 978 KLEKSLNMRAMNLLSEAEE 996
Cdd:TIGR00618 390 TLTQKLQSLCKELDILQRE 408
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
674-1028 |
3.30e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.09 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 674 ILSKLKTMRDAEDELKIKTSQLEATEKELANLKNMAEKYQHLKQQWEMKSEEAELLQTKIQQ--SAYHKQQEDLLALKKT 751
Cdd:TIGR04523 182 KLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEktTEISNTQTQLNQLKDE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 752 IAECEETLKKTEESQRKAEEEYKALENKMKNAEAERGKEIKNAQQKLN--------SAKKKADDSSRKMKEKQQEVEALV 823
Cdd:TIGR04523 262 QNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNkelkselkNQEKKLEEIQNQISQNNKIISQLN 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 824 LELEQLKQEQASYKQQSEAAQQAIASLKEQVSALEAEAVKTRESLKNAENELSSEKGLMEERTKDIKAKSAKIEKYREQN 903
Cdd:TIGR04523 342 EQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEK 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 904 NELQLSINALEHDINKYQQETADASSTLDKLLKEYKWIASEKELFGQADTTYDFEANNPKETGQKLQKLLTKKEKLEKSL 983
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL 501
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2500794 984 NMRAMNL---LSEAEERYNDLMKKKRMVENDKIKILATIEELDRKKNK 1028
Cdd:TIGR04523 502 NEEKKELeekVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK 549
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
693-902 |
3.34e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 693 SQLEATEKELANLKNMAEKYQHLKQQWEMKSEEAELLQTkiqqsAYHKQQEDLLALKKTIAECEETLKKTEESQRKAEEE 772
Cdd:PRK02224 206 ERLNGLESELAELDEEIERYEEQREQARETRDEADEVLE-----EHEERREELETLEAEIEDLRETIAETEREREELAEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 773 YKALENKMKNAEAERgkeiknaqqklNSAKKKADDSSRKMKEKQQEVEALVLELEQLKQEQASYKQQSEAAQQAIASLKE 852
Cdd:PRK02224 281 VRDLRERLEELEEER-----------DDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRE 349
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2500794 853 QVSALEAEAVKTRESLKNAENELSSEKGLMEERTKDIKAKSAKIEKYREQ 902
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRER 399
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
672-945 |
3.41e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 48.28 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 672 TPILSKLKTMRDAEDELK-IKTSQLEATEKELANLKN----------MAEKYQHLKQQWEMKSEEAELLQTKIQ----QS 736
Cdd:pfam10174 240 TKISSLERNIRDLEDEVQmLKTNGLLHTEDREEEIKQmevykshskfMKNKIDQLKQELSKKESELLALQTKLEtltnQN 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 737 AYHKQQEDLL-------------------ALKKTIAECEETL-KKTEESQRKAEE------EYKALENKMKNAEAERG-- 788
Cdd:pfam10174 320 SDCKQHIEVLkesltakeqraailqtevdALRLRLEEKESFLnKKTKQLQDLTEEkstlagEIRDLKDMLDVKERKINvl 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 789 -KEIKNAQQKLNSAKKKADDSSRKMK---------------------EKQQEVEAL-----------VLELEQLKQEQAS 835
Cdd:pfam10174 400 qKKIENLQEQLRDKDKQLAGLKERVKslqtdssntdtalttleealsEKERIIERLkeqreredrerLEELESLKKENKD 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 836 YKQQSEAAQ-------QAIASLKEQVSALEAEAVKTRESLKNAENELSSEKglmEE--RTKDIKAKSAKIEKYREQNNEL 906
Cdd:pfam10174 480 LKEKVSALQpeltekeSSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKK---EEcsKLENQLKKAHNAEEAVRTNPEI 556
|
330 340 350
....*....|....*....|....*....|....*....
gi 2500794 907 QLSINALEHDINKYQQETADASSTLDKLLKEYKWIASEK 945
Cdd:pfam10174 557 NDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEK 595
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
691-877 |
3.45e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.49 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 691 KTSQLEATEKELANLKNMAEKYQH--LKQQWEMKSEEAELLQTKIQQsayhKQQED---LLALKKTIAEcEETLKKTEES 765
Cdd:PRK09510 71 QKSAKRAEEQRKKKEQQQAEELQQkqAAEQERLKQLEKERLAAQEQK----KQAEEaakQAALKQKQAE-EAAAKAAAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 766 QRKAEEEYKALENKMKNAEAE-RGKEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEALVLELEQLKQEQASYKQQSEAAQ 844
Cdd:PRK09510 146 KAKAEAEAKRAAAAAKKAAAEaKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKA 225
|
170 180 190
....*....|....*....|....*....|...
gi 2500794 845 QAIASLKEQVSALEAEAVKTRESLKNAENELSS 877
Cdd:PRK09510 226 AAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
825-1029 |
5.73e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 825 ELEQLKQEQASYKQQSEAAQQAIASLKEQVSALEAEAVKTRESLKNAENElssekglMEERTKDIKAKSAKIEKYREQNN 904
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE-------IDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 905 ELQLSINALEHDINKYQQ--ETADASSTLDKLLKEYKWIASEKELFGQADTTYDFEANNPKETGQKLQKLLTKKEKLEKS 982
Cdd:COG3883 90 ERARALYRSGGSVSYLDVllGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2500794 983 LNmRAMNLLSEAEERYNDLMKKKRMVENDKIKILATIEELDRKKNKA 1029
Cdd:COG3883 170 KA-ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
3-100 |
6.08e-05 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 46.58 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 3 IKSIVLEGFKSYAQRTEI----RDFDPL-FNAITGLNGSGKSNILDSICFLLGISNLSQVRASSLQDLVYKNGQAGVNKA 77
Cdd:COG1106 2 LISFSIENFRSFKDELTLsmvaSGLRLLrVNLIYGANASGKSNLLEALYFLRNLVLNSSQPGDKLVEPFLLDSESKNEPS 81
|
90 100
....*....|....*....|...
gi 2500794 78 TVSITFdNSDKKNSPLGFENNDE 100
Cdd:COG1106 82 EFEILF-LLDGVRYEYGFELDKE 103
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
677-996 |
7.41e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 7.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 677 KLKTMRDAEDELKIKTSQLEATEKELANLKnmaEKYQHLKQQWEMKSEE-----AELLQTKIQQSAYHKQQEDLlalKKT 751
Cdd:PRK02224 249 RREELETLEAEIEDLRETIAETEREREELA---EEVRDLRERLEELEEErddllAEAGLDDADAEAVEARREEL---EDR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 752 IAECEETLKKTEESQRKAEEEYKALENKMKNAEaERGKEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEAlvlELEQLKQ 831
Cdd:PRK02224 323 DEELRDRLEECRVAAQAHNEEAESLREDADDLE-ERAEELREEAAELESELEEAREAVEDRREEIEELEE---EIEELRE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 832 EQASYKQQSEAAQQAIASLKEQVSALEAEAVKTRESLKNAENELSSEKGLMEERT-----KDIKAKS--AKIEKYREQNN 904
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgQPVEGSPhvETIEEDRERVE 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 905 ELQLsinalehdinkyqqETADASSTLDKLLKEYKWIASEKELFGQADTTYDFEANNPKETGQKLQKLLTKKEKLEkSLN 984
Cdd:PRK02224 479 ELEA--------------ELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAE-ELR 543
|
330
....*....|..
gi 2500794 985 MRAMNLLSEAEE 996
Cdd:PRK02224 544 ERAAELEAEAEE 555
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
686-1016 |
7.86e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 7.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 686 DELKIKTSQLEATEKELANLKNMAE--KYQHLKQQWEMKSEEAELLQTKIQQSAYHKQQEDL----LALKKTIAECEETL 759
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKenKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELenelNLLEKEKLNIQKNI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 760 KKTEESQRKAEEEYKALENKMKNAEaERGKEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEALVLELEQLKQEQASYKQQ 839
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKIQKNK-SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 840 SEAAQQAIASLKEQVSALEAEAVKTRESLKNAENElsSEKGLMEERTKDIKAKSAKIEKYREQNNELQLSINALEHDINK 919
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ--KEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 920 YQQETADASSTLDKLLKEYKWIASEKELFGQADTTYDFEANNPKETGQKLQKLLTKKEKLEKSLNMRAMNLLSEAE--ER 997
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEllEK 426
|
330
....*....|....*....
gi 2500794 998 YNDLMKKKRMVENDKIKIL 1016
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDL 445
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
694-980 |
8.18e-05 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 46.82 E-value: 8.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 694 QLEATEKELANLKNMAEKyqHLKQQWEMKSEEAELLQTKIQqsayhKQQEDL----LALKKTIAECEETLKKTEESQRKA 769
Cdd:pfam15964 357 QCEQLKSELERQKERLEK--ELASQQEKRAQEKEALRKEMK-----KEREELgatmLALSQNVAQLEAQVEKVTREKNSL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 770 EEEYKALENKMKNAEAERGKEIKNAQQKLNSAKKKADDSSRKMKE-----------KQQEVEALVLELEQlkqeqasYKQ 838
Cdd:pfam15964 430 VSQLEEAQKQLASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEHREyrtktgrqleiKDQEIEKLGLELSE-------SKQ 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 839 QSEAAQQAIASLKEqvsaleaEAVKTRESLKNAENEL---SSEKGLMEER-TKDIKAKSAKIEKyREQnnELQLSINALE 914
Cdd:pfam15964 503 RLEQAQQDAARARE-------ECLKLTELLGESEHQLhltRLEKESIQQSfSNEAKAQALQAQQ-REQ--ELTQKMQQME 572
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2500794 915 HDINKYQQET----ADASSTLDKLLKEYKWIASEKELFGQADTTYDFEANNPKE-TGQKLQKLLTKKEKLE 980
Cdd:pfam15964 573 AQHDKTVNEQysllTSQNTFIAKLKEECCTLAKKLEEITQKSRSEVEQLSQEKEyLQDRLEKLQKRNEELE 643
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
749-946 |
9.17e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.86 E-value: 9.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 749 KKTIAECEETLKKTEES-----QRKA--EEEYKALENKMKNAEAERGKEIKNAQQKLNS---AKKKADDSSRKMKEKQQE 818
Cdd:PRK05035 435 KAEIRAIEQEKKKAEEAkarfeARQArlEREKAAREARHKKAAEARAAKDKDAVAAALArvkAKKAAATQPIVIKAGARP 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 819 VEALVLELEQLKQEQASYKQQSEAAQQAIASLKEQVSALEAeavktRESLKNAENELSSEKGlmEERTKDIKAK------ 892
Cdd:PRK05035 515 DNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIA-----RAKAKKAAQQAANAEA--EEEVDPKKAAvaaaia 587
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2500794 893 SAKIEKYREQNNELQLSINALEHDINKYQQETADASSTLDKLLKEYKWIASEKE 946
Cdd:PRK05035 588 RAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPV 641
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
242-477 |
1.01e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 242 AEEIKDRSTNALKEAQANKKKIFESMAENEKKVKELAQQIEETEKKNNEEfGAKLHSLEAAFSELQRVDAKVRSDLDHRK 321
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL-ARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 322 QNLNSEENRLKELIKIMQ-------EEFKAFTSKEKEIKKIKEGLNGLQEESKKDAEALASAQQHFNAVSAGLSSNdsgq 394
Cdd:COG4942 97 AELEAQKEELAELLRALYrlgrqppLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE---- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 395 gtsladqmmtcKNEISKAATEAKQAQMKLkyaQQELKTKQAEVKKMDGSYKEDQEAFEAIRKTKEKLQDEMKKLKYEEAE 474
Cdd:COG4942 173 -----------RAELEALLAELEEERAAL---EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
...
gi 2500794 475 QEA 477
Cdd:COG4942 239 AAE 241
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-501 |
1.04e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 1 MYIKSIVLEGFKSYaqRTEIRDFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASSLQDLVykngQAGVNKATVS 80
Cdd:PRK03918 1 MKIEELKIKNFRSH--KSSVVEFDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKGLKKDDFT----RIGGSGTEIE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 81 ITFDNSDKKNSPLGFENNDEITITRQVIvggrNKYLINGMNASNNRVQDLfgsVGLNVNNPHFLIMQGQITKVLNMKPT- 159
Cdd:PRK03918 75 LKFEKNGRKYRIVRSFNRGESYLKYLDG----SEVLEEGDSSVREWVERL---IPYHVFLNAIYIRQGEIDAILESDESr 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 160 -----EILAMIE-EAAGTRMYECKK-----ITAHKTIEKKESKLDEIRRIITEEISPTLEKLKEARAsylEYQKMTREVE 228
Cdd:PRK03918 148 ekvvrQILGLDDyENAYKNLGEVIKeikrrIERLEKFIKRTENIEELIKEKEKELEEVLREINEISS---ELPELREELE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 229 NLRRiyvafQYVRAEEIKDRSTNA---LKEAQANKKKIFESMAENEKKVKELAQQIEETEKKNNEEfgAKLHSLEAAFSE 305
Cdd:PRK03918 225 KLEK-----EVKELEELKEEIEELekeLESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL--KELKEKAEEYIK 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 306 LQrvdaKVRSDLDHRKQNLNSEENRLKELIKIMQEEFKAFTSKEKEIKKIKEGLNGLQ---EESKKDAEALASAQQ---H 379
Cdd:PRK03918 298 LS----EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEkrlEELEERHELYEEAKAkkeE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 380 FNAVSAGLSSNDSGQGTSLADQMMTCKNEISKAATEAKQAQMKLKYAQQELKTKQAEVKKMDGS---------------- 443
Cdd:PRK03918 374 LERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelteehrkel 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2500794 444 YKEDQEAFEAIRKTKEKLQDEMKKLKYEEAEQEAHLAKKkqlsSEISSLRELCESIEA 501
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKE----SELIKLKELAEQLKE 507
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
724-925 |
1.14e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.99 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 724 EEAELLQTKIQQSAYHKQQEDLLALKKTIAECEETLKKTEESQRKAEEEYKAlenkMKNAEAERGKEIKNAQQKLNSAKK 803
Cdd:TIGR02794 75 QQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKA----KQAAEAKAKAEAEAERKAKEEAAK 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 804 KAddssrkmkekqqEVEALVLELEQLKQEQASYKQQSEAAQQAIAslkeqvsalEAEAVKTRESLKnAENELSSEKGLME 883
Cdd:TIGR02794 151 QA------------EEEAKAKAAAEAKKKAEEAKKKAEAEAKAKA---------EAEAKAKAEEAK-AKAEAAKAKAAAE 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2500794 884 ERTKDIKAKSAKIEKYREQNNELQL--SINALEHDINKYQQETA 925
Cdd:TIGR02794 209 AAAKAEAEAAAAAAAEAERKADEAElgDIFGLASGSNAEKQGGA 252
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
782-945 |
1.21e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 782 NAEAERGKEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEALVLELEQLKQEQASYKQQSEAAQQAIASLKEQVSALEAEA 861
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 862 VKTRESLKNAENELSSEKGLMEERTKDIKAKSAKIEKYREQNNELQLSINALEHDINKYQQETADASSTLDKLLKEYKWI 941
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
|
....
gi 2500794 942 ASEK 945
Cdd:COG4372 177 SEAE 180
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
743-859 |
1.43e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.97 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 743 EDLLALKKtiaECEETLKKTEESQRKAEEEYKALENKMKNAEAERGKEIKNAQQK----LNSAKKKADDSSRKMKEKQQE 818
Cdd:PRK00409 523 ASLEELER---ELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEaqqaIKEAKKEADEIIKELRQLQKG 599
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2500794 819 VEALVLElEQLKQEQASYKQQSEAAQQAIASLKEQVSALEA 859
Cdd:PRK00409 600 GYASVKA-HELIEARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
685-912 |
1.50e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 685 EDELKIKTSQLEATEKELANLKNmaekyqhlKQQWEMKSEEAELLQTKIQQSayhkqQEDLLALKKTIAECEETLKKTEE 764
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQ--------KNGLVDLSEEAKLLLQQLSEL-----ESQLAEARAELAEAEARLAALRA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 765 SQRKAEEEYKALENKmkNAEAERGKEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEALVLELEQ-LKQEQASYKQQSEAA 843
Cdd:COG3206 248 QLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQeAQRILASLEAELEAL 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2500794 844 QQAIASLKEQVSALEAEAvktrESLKNAENELSsekglmeERTKDIKAKSAKIEKYREQNNELQLSINA 912
Cdd:COG3206 326 QAREASLQAQLAQLEARL----AELPELEAELR-------RLEREVEVARELYESLLQRLEEARLAEAL 383
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
701-985 |
1.50e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.05 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 701 ELANLKNMAEKYQHLKQQweMKSEEAELLQTKIQQSAYHKQQEDLLALKKTIAECEETLKKTEESQRKAEEEYKALENKM 780
Cdd:PRK01156 157 EILEINSLERNYDKLKDV--IDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDY 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 781 KNAEAE--RGKEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEALVLELEQLKQEQAsYKQQSE-----AAQQAIASLKEQ 853
Cdd:PRK01156 235 NNLKSAlnELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPV-YKNRNYindyfKYKNDIENKKQI 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 854 VSALEAEAVKTRESLKNAENELS--SEKGLMEERTKDIKAKSAKIEKYREQNNELQLSINALEHDINKYQQETADASSTL 931
Cdd:PRK01156 314 LSNIDAEINKYHAIIKKLSVLQKdyNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFI 393
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2500794 932 DKLLKEYKWIASE-KELFGQADTTYDFEANNPKETGQKLQKLLTKKEKLEKSLNM 985
Cdd:PRK01156 394 SEILKIQEIDPDAiKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEM 448
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1-500 |
1.85e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 1 MYIKSIVLEGFKSYAQrTEIRdFDPLFNAITGLNGSGKSNILDSiCF--LLGISNLSQVrassLQDLVYKngqaGVNKAT 78
Cdd:PRK02224 1 MRFDRVRLENFKCYAD-ADLR-LEDGVTVIHGVNGSGKSSLLEA-CFfaLYGSKALDDT----LDDVITI----GAEEAE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 79 VSITFdnsdkknSPLGFE---------NNDEITITRQVIVGGRNkyLINGMNASNNRVQDLfgsvgLNVNNPHFL----I 145
Cdd:PRK02224 70 IELWF-------EHAGGEyhierrvrlSGDRATTAKCVLETPEG--TIDGARDVREEVTEL-----LRMDAEAFVncayV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 146 MQGQITKVLNMKPTEILAMI-------------EEAA----GTRMYECKKITA----HKTIEKKE------------SKL 192
Cdd:PRK02224 136 RQGEVNKLINATPSDRQDMIddllqlgkleeyrERASdarlGVERVLSDQRGSldqlKAQIEEKEekdlherlngleSEL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 193 DEIRRIIT--EEISPTLEKLKEARASYLEYQKMTR-EVENLrriyvafqyvrAEEIKDrSTNALKEAQANKKKIFESMAE 269
Cdd:PRK02224 216 AELDEEIEryEEQREQARETRDEADEVLEEHEERReELETL-----------EAEIED-LRETIAETEREREELAEEVRD 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 270 NEKKVKELAQQIEETEKKNNEEfGAKLHSLEAAFSELQRVDAKVRSDL-DHRK--QNLNSEENRLKELIKIMQEEFKaft 346
Cdd:PRK02224 284 LRERLEELEEERDDLLAEAGLD-DADAEAVEARREELEDRDEELRDRLeECRVaaQAHNEEAESLREDADDLEERAE--- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 347 skekeikkikeglnGLQEESKKDAEALASAQQHFNAVSAGLSSNDSgQGTSLADQMMTCKNEISKAATEAKQAQMKLKYA 426
Cdd:PRK02224 360 --------------ELREEAAELESELEEAREAVEDRREEIEELEE-EIEELRERFGDAPVDLGNAEDFLEELREERDEL 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 427 QQELKTKQAEVKKMDGSYKEDQEAFEA---------------------IRKTKEKLQDEMKKLKYEEAEQEAHLAKKKQL 485
Cdd:PRK02224 425 REREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphvetieeDRERVEELEAELEDLEEEVEEVEERLERAEDL 504
|
570
....*....|....*...
gi 2500794 486 S---SEISSLRELCESIE 500
Cdd:PRK02224 505 VeaeDRIERLEERREDLE 522
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
789-907 |
1.86e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 789 KEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEALVLELEQLKQEqasYKQQSEAAQQAIASLKEQvsaLEAEAVKTRESL 868
Cdd:PRK00409 509 KLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEE---LEEKKEKLQEEEDKLLEE---AEKEAQQAIKEA 582
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2500794 869 K-NAENELSSEKGLMEERTKDIKAKSAkIEKYREQNNELQ 907
Cdd:PRK00409 583 KkEADEIIKELRQLQKGGYASVKAHEL-IEARKRLNKANE 621
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
678-937 |
2.09e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 678 LKTMRDAEDELKIKTSQLEATEKELANLKNMAEKYQHLKQQWEMKSEEAELLQTKIQQSAYH---KQQEDLLALKKTIAE 754
Cdd:COG4717 131 YQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEelqDLAEELEELQQRLAE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 755 CEETLKKTEESQRKAEEEYKALENKMKNAEAER----------------------------------------------- 787
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQLENELEAAALEErlkearlllliaaallallglggsllsliltiagvlflvlgllallf 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 788 ---GKEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEALVLELEQLKQEQASYKQQSEAAQQAIASLKEQVSALEAEAVKT 864
Cdd:COG4717 291 lllAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 865 R-----------------------ESLKNAENELSSEKGLMEERTKDIKAKSAKI--EKYREQNNELQLSINALEHDINK 919
Cdd:COG4717 371 EiaallaeagvedeeelraaleqaEEYQELKEELEELEEQLEELLGELEELLEALdeEELEEELEELEEELEELEEELEE 450
|
330
....*....|....*...
gi 2500794 920 YQQETADASSTLDKLLKE 937
Cdd:COG4717 451 LREELAELEAELEQLEED 468
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
743-956 |
2.18e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 743 EDLLALKKTIAECEETLKKTEESQRKAEEEYKALENKMKNAEAER------GKEIKNAQQKLNSAKKKADDSSRKMKEKQ 816
Cdd:PRK02224 206 ERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERReeletlEAEIEDLRETIAETEREREELAEEVRDLR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 817 QEVEALVLELEQLKQEQAsykqQSEAAQQAIAslkEQVSALEAEAVKTRESLKNAENELSsekglmeERTKDIKAKSAKI 896
Cdd:PRK02224 286 ERLEELEEERDDLLAEAG----LDDADAEAVE---ARREELEDRDEELRDRLEECRVAAQ-------AHNEEAESLREDA 351
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 897 EKYREQNNELQLSINALEHDINKYQQETADASSTLDKLLKEykwIASEKELFGQADTTYD 956
Cdd:PRK02224 352 DDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEE---IEELRERFGDAPVDLG 408
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
683-859 |
2.67e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 683 DAEDELKIKTSQLEATEKELANLKNMAEKYQHLKQQWEmkseeaELLQTKIQQSAYHKQQEDLLALKKTIAECEETLkkT 762
Cdd:COG3206 209 DLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR------AQLGSGPDALPELLQSPVIQQLRAQLAELEAEL--A 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 763 EESQRKAEE--EYKALENKMKNAEAERGKEIKNA--------------QQKLNSAKKKADDSSRKMKEKQQEVEALVLEL 826
Cdd:COG3206 281 ELSARYTPNhpDVIALRAQIAALRAQLQQEAQRIlasleaelealqarEASLQAQLAQLEARLAELPELEAELRRLEREV 360
|
170 180 190
....*....|....*....|....*....|...
gi 2500794 827 EQLKQEQASYKQQSEAAQQAIASLKEQVSALEA 859
Cdd:COG3206 361 EVARELYESLLQRLEEARLAEALTVGNVRVIDP 393
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
696-950 |
2.96e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 696 EATEKELANLKNMAEKYQHLKQQWEMKSEEAELLQTKIQQSayhkqQEDLLALKKTIAECEETLKKTEESQRKAEEEYKA 775
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQA-----RSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 776 LENKMKNAEAE---RGKEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEALVLELEQLKQEQASYKQ--QSEAAQQAIASL 850
Cdd:COG4372 106 LQEEAEELQEEleeLQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQelQALSEAEAEQAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 851 KEQVSALEAEAVKTRESLKNAENELSSEKGLMEERTKDIKAKSAKIEKYREQNNELQLSINALEHDINKYQQETADASST 930
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
250 260
....*....|....*....|
gi 2500794 931 LDKLLKEYKWIASEKELFGQ 950
Cdd:COG4372 266 AILVEKDTEEEELEIAALEL 285
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
723-866 |
3.13e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 45.20 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 723 SEEAELLQTKIQQSAYHKQQEDLLALKKTIAECEETLKKT-EESQRKAEEEYKALENKMKNAEAERGKEIKNAQQKLNSA 801
Cdd:NF041483 665 AAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAqEEAARRRREAEETLGSARAEADQERERAREQSEELLASA 744
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2500794 802 KKKADdssrkmkEKQQEVEALVLELEQLKQEQASYKQQS------------EAAQQAIASLKeqvSALEAEAVKTRE 866
Cdd:NF041483 745 RKRVE-------EAQAEAQRLVEEADRRATELVSAAEQTaqqvrdsvaglqEQAEEEIAGLR---SAAEHAAERTRT 811
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
674-947 |
3.79e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 674 ILSKLKTMRDAEDELKIKTSQLEATEKELANLKN-MAEKYQHLKQQWEMKSEEAELLQTKIQQSAYHKQQ--EDLLALKK 750
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKELAEKRDeLNAQVKELREEAQELREKRDELNEKVKELKEERDElnEKLNELRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 751 TIAECEETLKKTEESQR---KAEEEYKALENKMKNA----EAERG--KEIKNAQQKLNsAKKKADDSSRKMKEKQQEVEA 821
Cdd:COG1340 93 ELDELRKELAELNKAGGsidKLRKEIERLEWRQQTEvlspEEEKElvEKIKELEKELE-KAKKALEKNEKLKELRAELKE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 822 LVLELEQLKQEQASYKQQSEAAQQAIASLKEQVSALEAEAvktreslknaenelssekglmEERTKDIKAKSAKIEKYRE 901
Cdd:COG1340 172 LRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEA---------------------DELHKEIVEAQEKADELHE 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2500794 902 QNNELQLSINALEHDINKYQQETADASSTLDKLLKEYKWIASEKEL 947
Cdd:COG1340 231 EIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKL 276
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
684-1036 |
3.96e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 684 AEDELKIKTSQLEATEKELANLKNMAE--KYQHLKQQWEMKSEEAELLQTKIQQSAYHKQQEDllALKKTIAECEETLKK 761
Cdd:PTZ00121 1100 AEEAKKTETGKAEEARKAEEAKKKAEDarKAEEARKAEDARKAEEARKAEDAKRVEIARKAED--ARKAEEARKAEDAKK 1177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 762 TEESQ-----RKAEEEYKAlENKMKNAEAERGKEIKNAQQKLNSAKKKADDSSRKMKE-KQQEVEALVLELEQLKQEQAS 835
Cdd:PTZ00121 1178 AEAARkaeevRKAEELRKA-EDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEaKKDAEEAKKAEEERNNEEIRK 1256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 836 YKQQSEAAQQAIASLKEQVSALEAEAVKTRESLKNAENELSSEKGLMEERTKDIKAKSAKIEKYREQNNELQLSINALEH 915
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKK 1336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 916 DINKYQQETADASSTLDKLLKEYKWIASEKELFGQADTTYDFEANNPKETGQKLQKLLTKKEKLEKSlNMRAMNLLSEAE 995
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEED-KKKADELKKAAA 1415
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2500794 996 ERYNDLMKKKRMVENDKIKILATIEELDRKKNKALHIAWEK 1036
Cdd:PTZ00121 1416 AKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA 1456
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
707-868 |
4.11e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.30 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 707 NMAEKYQHLKQQwemKSEEAELL-QTKIQQSA-------YHKQQEDLLALKKTIAECEETLKKTEESQRKAEE------- 771
Cdd:PRK11637 55 DIAAKEKSVRQQ---QQQRASLLaQLKKQEEAisqasrkLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERllaaqld 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 772 ------EYKALENKMKNAEAERGKEIKNAQQKLNSAKKKADDssrKMKEKQQEVEALVLELEQLKQEQASY----KQQSE 841
Cdd:PRK11637 132 aafrqgEHTGLQLILSGEESQRGERILAYFGYLNQARQETIA---ELKQTREELAAQKAELEEKQSQQKTLlyeqQAQQQ 208
|
170 180
....*....|....*....|....*..
gi 2500794 842 AAQQAIASLKEQVSALEAEAVKTRESL 868
Cdd:PRK11637 209 KLEQARNERKKTLTGLESSLQKDQQQL 235
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
847-1025 |
4.29e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 847 IASLKEQVSALEAEAVKTRESLKNAENELSSEKGLMEERTKDIKAKSAKIEKYREQNNELQLSINALEHDINKYQQ--ET 924
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 925 ADASSTLDKLLKEYKWIASEKELFGQADTTYDFEANNPKETGQKLQKLLTKKEKLEKSLNMRAMNLLSEAEERYNDLMKK 1004
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180
....*....|....*....|.
gi 2500794 1005 KRMVENDKIKILATIEELDRK 1025
Cdd:COG4717 208 LAELEEELEEAQEELEELEEE 228
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
709-846 |
4.60e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.22 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 709 AEKYQHLKQQWEMKSEEAELLQTKIQQSAYHKQQEdllalKKTIAECEETLKKTEESQR--KAEEEYKALENKMKNAEAE 786
Cdd:pfam05262 212 AKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQ-----RDEVRQKQQEAKNLPKPADtsSPKEDKQVAENQKREIEKA 286
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 787 RGKEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEALVLELEQLKQEQASYKQQSEAAQQA 846
Cdd:pfam05262 287 QIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEA 346
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
749-1026 |
4.69e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 749 KKTIAECEETLKKTEESQRKAEEEYKALENKMKNAEAERGKEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEALVLElEQ 828
Cdd:PTZ00121 1097 FGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAE-DA 1175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 829 LKQEQASYKQQSEAAQQ--AIASLKEQVSALEAEAVKTRESLKNAENELSSEKGLMEERTKDIKAKSAKIEKYREQNNEL 906
Cdd:PTZ00121 1176 KKAEAARKAEEVRKAEElrKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR 1255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 907 QLSINALEHDINKYQQETADASSTLDKlLKEYKWIASEKELFGQADTTYDFEANNPKETGQKLQKLLTKKEKLEKslnmR 986
Cdd:PTZ00121 1256 KFEEARMAHFARRQAAIKAEEARKADE-LKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK----K 1330
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2500794 987 AMNLLSEAEE--RYNDLMKKKRMVENDKIKILATIEELDRKK 1026
Cdd:PTZ00121 1331 ADAAKKKAEEakKAAEAAKAEAEAAADEAEAAEEKAEAAEKK 1372
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
814-922 |
4.91e-04 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 41.01 E-value: 4.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 814 EKQQEVEALVLELEQLKQEqasYKQQSEAAQQAIASLKEQVSALEAEAVKTRESLKNAENELSSEKGLMEERTKDIKAKS 893
Cdd:pfam13863 3 EKKREMFLVQLALDAKREE---IERLEELLKQREEELEKKEQELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEKE 79
|
90 100
....*....|....*....|....*....
gi 2500794 894 AKIEKYREQNNELQLSINALEHDINKYQQ 922
Cdd:pfam13863 80 KEIKKLTAQIEELKSEISKLEEKLEEYKP 108
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
740-839 |
5.78e-04 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 41.01 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 740 KQQEDLLALKKTIAECEETLKKTEESQRKAEEEYKALENKMKNAEAERGKEIKNAQQKLNSAKKKADDSSRKMKEKQQEV 819
Cdd:pfam13863 3 EKKREMFLVQLALDAKREEIERLEELLKQREEELEKKEQELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEKEKEI 82
|
90 100
....*....|....*....|
gi 2500794 820 EALVLELEQLKQEQASYKQQ 839
Cdd:pfam13863 83 KKLTAQIEELKSEISKLEEK 102
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
670-982 |
6.16e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.19 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 670 HVTPILSKLKTMRDAEDELKIKTSQLEATEKELANLKNMAEKYQHLKQQWEMKSEEAELLQTKIQQSAYHKQQEDLLALK 749
Cdd:TIGR00618 390 TLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLK 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 750 KtiaecEETLKKTEESQRKAEEEYKALENKMKNAEAERGKEIKNAQQKLNSAKKKADDSS----------RKMKEKQQEV 819
Cdd:TIGR00618 470 E-----REQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGpltrrmqrgeQTYAQLETSE 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 820 EALVLELEQLKQEQASYKQQSEAAQQAIASLKEQVSALEAEAVKTR----ESLKNAENELSSEKGLMEERTKDIKAKSAK 895
Cdd:TIGR00618 545 EDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQnitvRLQDLTEKLSEAEDMLACEQHALLRKLQPE 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 896 IEKYR----EQN--NELQLSINALEHDINKYQQETADASSTLDKLLKEYKWIASEKELfGQADTTYDFEANNPKETGQKL 969
Cdd:TIGR00618 625 QDLQDvrlhLQQcsQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLAL-QKMQSEKEQLTYWKEMLAQCQ 703
|
330
....*....|...
gi 2500794 970 QKLLTKKEKLEKS 982
Cdd:TIGR00618 704 TLLRELETHIEEY 716
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
694-902 |
6.59e-04 |
|
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: 43.96 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 694 QLEATEK-ELANLKNMAEKYQHLKQQWEMKSEEAELLQTKIQQSAYHKQQEDLLALKktIAECEETLKKTEESQRKAEEE 772
Cdd:pfam17380 317 KLEEAEKaRQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAME--ISRMRELERLQMERQQKNERV 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 773 YKALE--NKMKNAEAERGKEIKnaQQKLNSAKKKADDSSRKMKEKQQEVEALVLELEQLKQEQASYKQQSEAAQQAIASL 850
Cdd:pfam17380 395 RQELEaaRKVKILEEERQRKIQ--QQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2500794 851 KEQVSALEAEavKTRESLKNAENELSSEKGLMEERTKDIKAKSAK--IEKYREQ 902
Cdd:pfam17380 473 KRKKLELEKE--KRDRKRAEEQRRKILEKELEERKQAMIEEERKRklLEKEMEE 524
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
676-866 |
6.91e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.04 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 676 SKLKTMRDA-----EDELKIKTSQLEATEKELANLKN--MAEKYQHLKQQWEMKSEEAELLQTKIqqsayhkqqEDLL-A 747
Cdd:pfam10174 517 SKLKSLEIAveqkkEECSKLENQLKKAHNAEEAVRTNpeINDRIRLLEQEVARYKEESGKAQAEV---------ERLLgI 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 748 LKKTIAECEETLKKTEESQRKAEEEYKALENKMKNAEAERGKEIKNAQQKLNSAKKKADDSSRKMKEKQqeVEALVLELE 827
Cdd:pfam10174 588 LREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQ--LEELMGALE 665
|
170 180 190
....*....|....*....|....*....|....*....
gi 2500794 828 QLKQEQASYKQQSEAAQQAIASLKEQVSALEAEAVKTRE 866
Cdd:pfam10174 666 KTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLE 704
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
826-1025 |
9.03e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 9.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 826 LEQLKQEQASYKQQSEAAQQAIASLKEQ--VSALEAEAVKTRESLKNAENELSsekglmeERTKDIKAKSAKIEKYREQN 903
Cdd:COG3206 177 LEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLA-------EARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 904 NELQLSINALEHD--INKYQQETADASSTLDKLLKEYKwiasekelfgqadttydfeANNPketgqKLQKLLTKKEKLEK 981
Cdd:COG3206 250 GSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYT-------------------PNHP-----DVIALRAQIAALRA 305
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2500794 982 SLNMRAMNLLSEAEERYNDLMKKKRMVENDKIKILATIEELDRK 1025
Cdd:COG3206 306 QLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPEL 349
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
819-1004 |
9.89e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 9.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 819 VEALVLELEQLKQEQASYKQQSEAAQQAIASLKEQVSALE--AEAVKTRESLKNAENELSSekgLMEERtKDIKAKSAKI 896
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAE---LEAEL-ERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 897 EKYREQNNELQLSINALEHDINKYQQETADASSTLD---KLLKEYKWIASEKELFGQADTTYDFEANNPKETGQKLQKLL 973
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEqaeEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767
|
170 180 190
....*....|....*....|....*....|.
gi 2500794 974 tkKEKLEKSLnMRAMNLLSEAEERYNDLMKK 1004
Cdd:COG4913 768 --RENLEERI-DALRARLNRAEEELERAMRA 795
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
791-937 |
1.06e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 791 IKNAQQKLNSAKKKADDSSRKMKEKQQEVEAL-------------VLELEQLKQEQASYKQQSEAAQQAIASLKEQVSAL 857
Cdd:PRK11281 75 IDRQKEETEQLKQQLAQAPAKLRQAQAELEALkddndeetretlsTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 858 eaeavktRESLKNAENELSSekglMEERTKDIKA--KSAKIEKYR---EQNNELQLSINALEHDiNKYQQETADASSTLD 932
Cdd:PRK11281 155 -------QTQPERAQAALYA----NSQRLQQIRNllKGGKVGGKAlrpSQRVLLQAEQALLNAQ-NDLQRKSLEGNTQLQ 222
|
....*
gi 2500794 933 KLLKE 937
Cdd:PRK11281 223 DLLQK 227
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
682-823 |
1.46e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 682 RDAEDELKIKTSQLEATEKELANLKNMAEKYQHLKQQWEMKSEEAELLQTKIQ-QSAYHKQQEDLLALKKTIAECEETLK 760
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnNKEYEALQKEIESLKRRISDLEDEIL 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2500794 761 KTEESQRKAEEEYKALENKMKNAEAergkEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEALV 823
Cdd:COG1579 114 ELMERIEELEEELAELEAELAELEA----ELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
807-897 |
1.54e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.02 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 807 DSSRKMKEKQQEVEALVLELEQLKQEQASYKQQSEAAQQAIASLKEQVSALEAEAVKTRESLKN-AENELSSEKGLMEER 885
Cdd:PRK11448 139 DPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQlQEKAAETSQERKQKR 218
|
90
....*....|..
gi 2500794 886 TKDIKAKSAKIE 897
Cdd:PRK11448 219 KEITDQAAKRLE 230
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
756-857 |
1.66e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 39.73 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 756 EETLKKTEESQRKAEEEYKALENKMKNAEAErgkeiknAQQKLNSAKKKADDSSRKMKEK-QQEVEALVLE-LEQLKQEQ 833
Cdd:cd06503 36 AESLEEAEKAKEEAEELLAEYEEKLAEARAE-------AQEIIEEARKEAEKIKEEILAEaKEEAERILEQaKAEIEQEK 108
|
90 100
....*....|....*....|....
gi 2500794 834 asykqqseaaQQAIASLKEQVSAL 857
Cdd:cd06503 109 ----------EKALAELRKEVADL 122
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
686-938 |
1.66e-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: 42.70 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 686 DELKIKTSQLEATEKELANLKNMAEKYQHLKQQwEMKSEEAELLQTKIQQSAYHKQQEDLlalKKTIAECEETLKKTEES 765
Cdd:TIGR04523 457 KNLDNTRESLETQLKVLSRSINKIKQNLEQKQK-ELKSKEKELKKLNEEKKELEEKVKDL---TKKISSLKEKIEKLESE 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 766 QRKAEEEYKALENKMKNAEAERG-----KEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEALVLELEQLKQEQASYKQQS 840
Cdd:TIGR04523 533 KKEKESKISDLEDELNKDDFELKkenleKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 841 EAAQQAIASLKEQVSALEAEAVKtresLKNAENELSSEKGLMEERTKDIKAKSAKIEKyreqnnelqlSINALEHDINKY 920
Cdd:TIGR04523 613 SSLEKELEKAKKENEKLSSIIKN----IKSKKNKLKQEVKQIKETIKEIRNKWPEIIK----------KIKESKTKIDDI 678
|
250
....*....|....*...
gi 2500794 921 QQETADASSTLDKLLKEY 938
Cdd:TIGR04523 679 IELMKDWLKELSLHYKKY 696
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
692-877 |
1.70e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 692 TSQLEATEKELANLKNMAEKYQHLKQQWEMKSEEAELLQTKIQQSAYHKQQEDLLALKKtiAECEETLkkteESQRKAEE 771
Cdd:COG4717 322 EELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAG--VEDEEEL----RAALEQAE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 772 EYKALENKMKNAEAERGKEIKNAQQKLNSAKKkaddssrkmkekqqevEALVLELEQLKQEQASYKQQSEAAQQAIASLK 851
Cdd:COG4717 396 EYQELKEELEELEEQLEELLGELEELLEALDE----------------EELEEELEELEEELEELEEELEELREELAELE 459
|
170 180
....*....|....*....|....*...
gi 2500794 852 EQVSALEA--EAVKTRESLKNAENELSS 877
Cdd:COG4717 460 AELEQLEEdgELAELLQELEELKAELRE 487
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-49 |
1.85e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 42.20 E-value: 1.85e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2500794 1 MYIKSIVLEGFKSYaqRTEIRDFDPLFNAITGLNGSGKSNILDSICFLL 49
Cdd:pfam13175 1 MKIKSIIIKNFRCL--KDTEIDLDEDLTVLIGKNNSGKSSILEALDIFL 47
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
676-865 |
2.26e-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: 41.67 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 676 SKLKTMRDAEDELKIKTSQLEATEKELA----NLKNMAEKYQHLKQQWEMKSEE-AELLQTKIQQSAYHK-----QQEDL 745
Cdd:COG4942 52 ALLKQLAALERRIAALARRIRALEQELAaleaELAELEKEIAELRAELEAQKEElAELLRALYRLGRQPPlalllSPEDF 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 746 L--------------ALKKTIAECEETLKKTEESQRKAEEEYKALENKMKNAEAERgkeiKNAQQKLNSAKKKADDSSRK 811
Cdd:COG4942 132 LdavrrlqylkylapARREQAEELRADLAELAALRAELEAERAELEALLAELEEER----AALEALKAERQKLLARLEKE 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2500794 812 MKEKQQevealvlELEQLKQEQASYKQQSEAAQQAIASLKEQVSALEAEAVKTR 865
Cdd:COG4942 208 LAELAA-------ELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
753-895 |
2.29e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 41.78 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 753 AECEETLKKTEESQRKAEEEYKALEN--KMKNAEAERGKEIKNAQQKL--NSAKKKADDSSRKMKE-KQQEVEALVLELE 827
Cdd:COG2268 208 AERETEIAIAQANREAEEAELEQEREieTARIAEAEAELAKKKAEERReaETARAEAEAAYEIAEAnAEREVQRQLEIAE 287
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2500794 828 QLKQEQASYKQQSEAAQQAIASLKEQVSAlEAEAVKTREslkNAENELSSEKGLMEERTKDIKAKSAK 895
Cdd:COG2268 288 REREIELQEKEAEREEAELEADVRKPAEA-EKQAAEAEA---EAEAEAIRAKGLAEAEGKRALAEAWN 351
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
649-907 |
2.31e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 42.31 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 649 TVTLQGDifDPQGTLSGGASSHVTPILSKLKTMRDaedelKIKTSQLEATEKELANLKNmaeKYQHLKQQWEMKSEEAEL 728
Cdd:NF033838 47 TVTSSGN--ESQKEHAKEVESHLEKILSEIQKSLD-----KRKHTQNVALNKKLSDIKT---EYLYELNVLKEKSEAELT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 729 LQTKIQ-QSAYHKQQEDLLALKKTIAECEetlKKTEESQRKAEEEykalenkmknAEAERGKEIKNAQQKLnsakkkadd 807
Cdd:NF033838 117 SKTKKElDAAFEQFKKDTLEPGKKVAEAT---KKVEEAEKKAKDQ----------KEEDRRNYPTNTYKTL--------- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 808 ssrKMKEKQQEVEALVLELEQLKqEQASYKQQSEAAQQAIASLK-EQVSALEAEAVKTRESLKNAENELSSEKGLMEERT 886
Cdd:NF033838 175 ---ELEIAESDVEVKKAELELVK-EEAKEPRDEEKIKQAKAKVEsKKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVE 250
|
250 260
....*....|....*....|.
gi 2500794 887 KDIKAKSAKIEKYREQNNELQ 907
Cdd:NF033838 251 KNVATSEQDKPKRRAKRGVLG 271
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
723-968 |
2.31e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 723 SEEAELLQTKIQQSayhKQQEDLLALKKTIAECE-ETLKKTEESQRKAEEEYKALENKMKNAEAERGKEIKNAQQKLNSA 801
Cdd:PHA02562 166 SEMDKLNKDKIREL---NQQIQTLDMKIDHIQQQiKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 802 ----KKKADDSSRKMKEKQQEVEALVLELEQLKQEQASY---------KQQSEAAQQAIASLKEQVSALEaeavKTRESL 868
Cdd:PHA02562 243 llnlVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYekggvcptcTQQISEGPDRITKIKDKLKELQ----HSLEKL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 869 KNAENELSSEKGLMEERTKDIKAKSAKIEKYREQNNELQLSINALEHDINKYQQETADASSTLDKLLKEYKWIASEKELF 948
Cdd:PHA02562 319 DTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSEL 398
|
250 260
....*....|....*....|
gi 2500794 949 GQADTTYDFEANNPKETGQK 968
Cdd:PHA02562 399 VKEKYHRGIVTDLLKDSGIK 418
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
804-1025 |
2.47e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 804 KADDSSRKMKEKQQEVEALVLELEQLKQEQASYKQQSEAAQQAIASLKEQVSALEAEAVKTRESLKNAE----------N 873
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEkevkeleelkE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 874 ELSSEKGLMEERTKDIKAKSAKIEKYREQNNELQLSINALEHDINKYQ--QETADASSTLDKLLKEYKWIAS--EKELfg 949
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELReiEKRL-- 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2500794 950 qadTTYDFEANNPKETGQKLQKLLTKKEKLEKSLN--MRAMNLLSEAEERYNDLMKKKRMVENDKIKILA-TIEELDRK 1025
Cdd:PRK03918 317 ---SRLEEEINGIEERIKELEEKEERLEELKKKLKelEKRLEELEERHELYEEAKAKKEELERLKKRLTGlTPEKLEKE 392
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
687-932 |
2.56e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 687 ELKIK-TSQLEATEKELANLK----NMAEKYQHLKQQWEMKSEEAELLQTKIQQSAyHKQQEDLLALKKTIAECEETLKK 761
Cdd:pfam01576 349 EMRQKhTQALEELTEQLEQAKrnkaNLEKAKQALESENAELQAELRTLQQAKQDSE-HKRKKLEGQLQELQARLSESERQ 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 762 TEESQRKAEEEYKALENKMKNAEAERGKEIKnAQQKLNSAKKKADDSSRKMKEKQQEVEALVLELEQLKQEQASYKQQSE 841
Cdd:pfam01576 428 RAELAEKLSKLQSELESVSSLLNEAEGKNIK-LSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLE 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 842 AAQQAIASLKEQVSALEAEAVKTReslKNAENELSSEKGLMEERTKDIKaksaKIEKYREQNNELQLSINALEHDINKYQ 921
Cdd:pfam01576 507 EEEEAKRNVERQLSTLQAQLSDMK---KKLEEDAGTLEALEEGKKRLQR----ELEALTQQLEEKAAAYDKLEKTKNRLQ 579
|
250
....*....|.
gi 2500794 922 QETADASSTLD 932
Cdd:pfam01576 580 QELDDLLVDLD 590
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
741-874 |
3.04e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 741 QQEDLLALKKTIAECEETLKKTEESQRKAEEEYKALENKMKNAEAERgkeiknaqqklnSAKKKADDssrkmkEKQQEVE 820
Cdd:PRK09039 51 KDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAER------------SRLQALLA------ELAGAGA 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2500794 821 ALVLELEQLKQEQASYKQQSEAAQQAIASLKEQVSALEAEAVKTRESLKNAENE 874
Cdd:PRK09039 113 AAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKR 166
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
760-883 |
3.15e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 760 KKTEESQRKAEEEYKALENKMKNAEAERGKEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEALVLELEQLKQEQasykQQ 839
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEE----RR 459
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2500794 840 SEAAQQAIASLKEQVSALEAEAVKTRESLKNAENELSSEKGLME 883
Cdd:COG2433 460 EIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWK 503
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
693-1010 |
3.18e-03 |
|
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.
Pssm-ID: 311808 [Multi-domain] Cd Length: 393 Bit Score: 41.39 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 693 SQLEATEKELANLKNMAEKYQHLKQQWEMKSEEAELLQTKIQQSAYHKQQEDLLALKKTIAECEETLKKTEESQRKAEEE 772
Cdd:pfam08017 26 SQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 773 YKA--LENKMKNAEAERGKEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEALVLELEQLKQEQASYKQQSEAAQQAiASL 850
Cdd:pfam08017 106 SQGnvLERRQRDAENKSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRD-AEN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 851 KEQVSALEAEAvktreslKNAENElsSEKGLMEERTKDIKAKS-AKIEKYREQNNELQLSINALEH---------DINKY 920
Cdd:pfam08017 185 KSQGNVLERRQ-------RDAENR--SQGNVLERRQRDAENRSqGNVLERRQRDAENRSQGNVLERrqrdaenksQGNVL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 921 QQETADASSTLDKLLKEYKWIASEKELFGQADTTYDFEANNPKETGQklqkLLTKKEKLEKSLNMRAMNLLSEAEERYND 1000
Cdd:pfam08017 256 ERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENKSQVGQ----LIGKNPLLSKSIISRENNHSSQGDSNKQS 331
|
330
....*....|
gi 2500794 1001 LMKKKRMVEN 1010
Cdd:pfam08017 332 FSKKVSQVTN 341
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
792-923 |
3.26e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 792 KNAQQKLNSAKKKADdssRKMKEKQQEVEALVLELE-QLKQEQASYKQQseaaqqaiaslkeqvsaLEAEAVKTRESLKN 870
Cdd:PRK12704 27 KIAEAKIKEAEEEAK---RILEEAKKEAEAIKKEALlEAKEEIHKLRNE-----------------FEKELRERRNELQK 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2500794 871 AENELSSEKGLMEERTKDIKAKSAKIEKYREQNNELQLSINALEHDINKYQQE 923
Cdd:PRK12704 87 LEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE 139
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
782-859 |
3.40e-03 |
|
Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.
Pssm-ID: 432198 [Multi-domain] Cd Length: 238 Bit Score: 40.68 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 782 NAEAERGKEIKNAQQKLNSAKKKA----DDSSRKMKEKQQEVEALVLELEQLKQEQASYKQQSEAAQQAIASLKEQVSAL 857
Cdd:pfam11932 9 GALAATLDQALDLAEKAVAAAAQSqkkiDKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQIEEI 88
|
..
gi 2500794 858 EA 859
Cdd:pfam11932 89 ER 90
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
816-939 |
3.42e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.16 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 816 QQEVEALVLELEQLKQEQASYKQQSEAAQQAIASLKEQVSALE----AEAVKTRESLKNAENELSSEKGLMEERTKDIKA 891
Cdd:smart00787 157 KEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEdcdpTELDRAKEKLKKLLQEIMIKVKKLEELEEELQE 236
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2500794 892 KSAKIEKYREQNNELQLSINALEHDINKYQQETADASSTLDKLLKEYK 939
Cdd:smart00787 237 LESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQ 284
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
694-821 |
3.90e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 694 QLEATEKELANLKNMAEKyqhLKQQWEMKSEEAEllqtKIQQSAYHKQQEDL-LALKKTIAECEETLKKTEESQRKAEEE 772
Cdd:PRK00409 531 ELEQKAEEAEALLKEAEK---LKEELEEKKEKLQ----EEEDKLLEEAEKEAqQAIKEAKKEADEIIKELRQLQKGGYAS 603
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2500794 773 YKAlenkmknaeaergKEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEA 821
Cdd:PRK00409 604 VKA-------------HELIEARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
661-859 |
3.92e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 40.05 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 661 GTLSGGASSHVTPILSKLKTMRDAEDELKIKTSQLEATEKELANLKNMAEKYQHLKQQWEMKSEEA------ELLQTKIQ 734
Cdd:pfam04012 11 ANIHEGLDKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAAltkgneELAREALA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 735 QSAYHKQQedLLALKKTIAECEETLKKTEESQRKAEEEYKALENKmKNAEAERGKEIKnAQQKLNSAKKKADDSS----- 809
Cdd:pfam04012 91 EKKSLEKQ--AEALETQLAQQRSAVEQLRKQLAALETKIQQLKAK-KNLLKARLKAAK-AQEAVQTSLGSLSTSSatdsf 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2500794 810 RKMKEKQQEVEALVLELEQLKQEQaSYKQQSEAAQQAIASLKEQVSALEA 859
Cdd:pfam04012 167 ERIEEKIEEREARADAAAELASAV-DLDAKLEQAGIQMEVSEDVLARLKA 215
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
689-874 |
4.32e-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: 41.26 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 689 KIKTSQLEATEKELANLKNMAEKYQHLKQQWEMKSEeaellqtkiQQSAYHKQQEDLLALKKTIAECEETLKKTEESQRK 768
Cdd:pfam17380 424 QIRAEQEEARQREVRRLEEERAREMERVRLEEQERQ---------QQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRR 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 769 AEEEYKALENKMKNAEAERGKEIknaqqklnsAKKKADDSSRKMKEKQQEVEAlvlELEQLKQEQASYKQQseaAQQAIA 848
Cdd:pfam17380 495 KILEKELEERKQAMIEEERKRKL---------LEKEMEERQKAIYEEERRREA---EEERRKQQEMEERRR---IQEQMR 559
|
170 180
....*....|....*....|....*..
gi 2500794 849 SLKEQVSALEAEAvKTRESLKN-AENE 874
Cdd:pfam17380 560 KATEERSRLEAME-REREMMRQiVESE 585
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
793-1002 |
4.32e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 793 NAQQKLNSAKKKADDSSRKMKEKQQEVEALVLELEQLKQEQ--ASYKQQSEAAQQAIASLKEQVSALEAEAVKTRESLKN 870
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 871 AENELSSEKGLMEERTKDikaksAKIEKYREQNNELQLSINALEhdiNKYQqetaDASSTLDKLLKEykwIAS-EKELFG 949
Cdd:COG3206 245 LRAQLGSGPDALPELLQS-----PVIQQLRAQLAELEAELAELS---ARYT----PNHPDVIALRAQ---IAAlRAQLQQ 309
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2500794 950 QADTTYDFEANNPKETGQKLQKLLTKKEKLEKSLNMramnlLSEAEERYNDLM 1002
Cdd:COG3206 310 EAQRILASLEAELEALQAREASLQAQLAQLEARLAE-----LPELEAELRRLE 357
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
756-891 |
4.72e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 41.18 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 756 EETLKK----TEESQR----------KAEEEYKALENKMK----NAE--AERGKEIKNAQQKL-NSAKK-------KADD 807
Cdd:pfam10168 546 EEYLKKhdlaREEIQKrvkllklqkeQQLQELQSLEEERKslseRAEklAEKYEEIKDKQEKLmRRCKKvlqrlnsQLPV 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 808 SSRKMKEKQQEVEALVLELEQLKQ--EQASYKQQSEAAQQAIASLKEQVSALEAEAvKTRESLKNAENELSSEKGLMEER 885
Cdd:pfam10168 626 LSDAEREMKKELETINEQLKHLANaiKQAKKKMNYQRYQIAKSQSIRKKSSLSLSE-KQRKTIKEILKQLGSEIDELIKQ 704
|
....*.
gi 2500794 886 TKDIKA 891
Cdd:pfam10168 705 VKDINK 710
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
740-897 |
4.76e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 740 KQQEDLLALkktiaecEETLKKTEESQRKAEEEYKALENKMKNAEAERG--KEIKNAQQKLNSakkKADDSSRKMKEKQQ 817
Cdd:pfam01576 2 RQEEEMQAK-------EEELQKVKERQQKAESELKELEKKHQQLCEEKNalQEQLQAETELCA---EAEEMRARLAARKQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 818 EVEALVLELEQLKQEQASYKQQSEAA----QQAIASLKEQVSALEA-------EAVKTRESLKNAE----------NELS 876
Cdd:pfam01576 72 ELEEILHELESRLEEEEERSQQLQNEkkkmQQHIQDLEEQLDEEEAarqklqlEKVTTEAKIKKLEedillledqnSKLS 151
|
170 180
....*....|....*....|.
gi 2500794 877 SEKGLMEERTKDIKAKSAKIE 897
Cdd:pfam01576 152 KERKLLEERISEFTSNLAEEE 172
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
12-49 |
5.04e-03 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 39.15 E-value: 5.04e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2500794 12 KSYAQRTEIRDFDPLFN-----AITGLNGSGKSNILDSICFLL 49
Cdd:cd00267 7 FRYGGRTALDNVSLTLKageivALVGPNGSGKSTLLRAIAGLL 49
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
690-1026 |
5.41e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 5.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 690 IKTSQLEATEKELANLKNMAEKYQHlkqqwEMKSEEAELLQTKIQQSAYHKQQEDLLALKKTIAECEETLKKTEESQRKA 769
Cdd:TIGR00606 734 GRQSIIDLKEKEIPELRNKLQKVNR-----DIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKI 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 770 EEEYKALEN-KMKNAEAERGKEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEALVLELEQLKQEQAsykQQSEAAQQAiA 848
Cdd:TIGR00606 809 AQQAAKLQGsDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKL---QIGTNLQRR-Q 884
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 849 SLKEQVSALEAEAVKTRESLKNAENELSSEKGLMEertKDIKAKSAKIEKYREQNNELQLSINALEH----------DIN 918
Cdd:TIGR00606 885 QFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLE---KDQQEKEELISSKETSNKKAQDKVNDIKEkvknihgymkDIE 961
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 919 KYQQETAD-----ASSTLDKLLKEYKWIASEKELFGQADTTYDFEANNPKETGQKLQKLLTK----------KEKLEKSL 983
Cdd:TIGR00606 962 NKIQDGKDdylkqKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLrkrenelkevEEELKQHL 1041
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2500794 984 NMRAMNLLSEAEERYNDLMKKKRMVENDKIKILATIEELDRKK 1026
Cdd:TIGR00606 1042 KEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEI 1084
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
789-891 |
5.71e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 38.39 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 789 KEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEALVlelEQLKQEQASY-----------------KQQSEAAQQAIASLK 851
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQA---EIAREAQQNYerelvlhaedikalqalREELNELKAEIAELK 77
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2500794 852 EQVSALEAEAVKTRESLKNAENELSSEKGLMEERTKDIKA 891
Cdd:pfam07926 78 AEAESAKAELEESEESWEEQKKELEKELSELEKRIEDLNE 117
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
708-907 |
5.87e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 40.25 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 708 MAEKYQHLKQQWEMKSEE---AEL------LQTKIQQSAYHKQ---QEDLLALKKTIAECEETLKKteesQRKAEEeykA 775
Cdd:cd16269 99 LEEKKEEFCKQNEEASSKrcqALLqelsapLEEKISQGSYSVPggyQLYLEDREKLVEKYRQVPRK----GVKAEE---V 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 776 LENKMKNAEAErGKEIKNAQQKLNSAKKKaddssrkMKEKQQEVEALVLELEQLKQEQASYKQQSEAAQQaiaSLKEQVS 855
Cdd:cd16269 172 LQEFLQSKEAE-AEAILQADQALTEKEKE-------IEAERAKAEAAEQERKLLEEQQRELEQKLEDQER---SYEEHLR 240
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2500794 856 ALEAEAVKTRESLKNAENELSSEKgLMEERTKDIKAKSAKIEKYREQNNELQ 907
Cdd:cd16269 241 QLKEKMEEERENLLKEQERALESK-LKEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
838-923 |
5.93e-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: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 838 QQSEAAQQAIASLKEQVSALEAEAVKTRESLKNAENELSSEKGLMEErtkdiKAKSAKIEKYREQNNELQLSINALEHDI 917
Cdd:COG2825 36 QESPEGKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEAATLSE-----EERQKKERELQKKQQELQRKQQEAQQDL 110
|
....*.
gi 2500794 918 NKYQQE 923
Cdd:COG2825 111 QKRQQE 116
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1107-1144 |
6.26e-03 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 38.77 E-value: 6.26e-03
10 20 30
....*....|....*....|....*....|....*....
gi 2500794 1107 APIYILDEVDAALDLSHTQNIGQMLHAHFKQ-SQFLVVS 1144
Cdd:cd00267 99 PDLLLLDEPTSGLDPASRERLLELLRELAEEgRTVIIVT 137
|
|
| ATP-synt_B |
pfam00430 |
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ... |
747-864 |
6.48e-03 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 38.06 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 747 ALKKTIAECEETLKKTEESQRKAEEEYKALENKMKNAEAERGKEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEAlvlel 826
Cdd:pfam00430 27 VLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEKLKEEIVAAAEAEAERIIEQAA----- 101
|
90 100 110
....*....|....*....|....*....|....*...
gi 2500794 827 EQLKQEQasykqqseaaQQAIASLKEQVSALEAEAVKT 864
Cdd:pfam00430 102 AEIEQEK----------DRALAELRQQVVALAVQIAEK 129
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
683-997 |
6.80e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.71 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 683 DAEDELKIKTSQLEATEKELANLknmAEKYQHLKQQWEMKSEEAELLQtKIQQSAYHKQQEDLLALkktIAECEETLKKT 762
Cdd:COG3096 833 DPEAELAALRQRRSELERELAQH---RAQEQQLRQQLDQLKEQLQLLN-KLLPQANLLADETLADR---LEELREELDAA 905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 763 EESQRKAEEEYKALEnkmknaeaergkeiknaqqklnsakkKADDSSRKMKEKQQEVEALVLELEQLKQEQASYKQQ--- 839
Cdd:COG3096 906 QEAQAFIQQHGKALA--------------------------QLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQifa 959
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 840 -------------SEAAQQAIAS------LKEQVSALEAEAVKTRESLKNAENELSSEKGLM-----------------E 883
Cdd:COG3096 960 lsevvqrrphfsyEDAVGLLGENsdlnekLRARLEQAEEARREAREQLRQAQAQYSQYNQVLaslkssrdakqqtlqelE 1039
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 884 ERTKD--IKAKSAKIEKYREQNNEL--QLS-----INALEHDINKYQQETADASSTLDKLLKEYKwiaSEKElfgqadtt 954
Cdd:COG3096 1040 QELEElgVQADAEAEERARIRRDELheELSqnrsrRSQLEKQLTRCEAEMDSLQKRLRKAERDYK---QERE-------- 1108
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2500794 955 ydfEANNPKETGQKLQKlLTKKEKLEKSLNMRAMNLLSEAEER 997
Cdd:COG3096 1109 ---QVVQAKAGWCAVLR-LARDNDVERRLHRRELAYLSADELR 1147
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
27-56 |
7.15e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.07 E-value: 7.15e-03
10 20 30
....*....|....*....|....*....|
gi 2500794 27 FNAITGLNGSGKSNILDSICFLLGISNLSQ 56
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVI 30
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
675-946 |
7.95e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 40.41 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 675 LSKLKTMRDAEDELKIKTSQLEATEKELANLKNMAEKYQHL--KQQWEMKSEEAELLQTKIQQsayhKQQEdLLALKKTI 752
Cdd:PTZ00108 1051 IIKKKSEKITAEEEEGAEEDDEADDEDDEEELGAAVSYDYLlsMPIWSLTKEKVEKLNAELEK----KEKE-LEKLKNTT 1125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 753 AEC--EETLKKTE---ESQRKAEEEYKALENKMKNAEAERGKEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEALVLELE 827
Cdd:PTZ00108 1126 PKDmwLEDLDKFEealEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDE 1205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 828 QLKQEQASYKQQSEAAQQAIASLKEQVSALEAEAVKTRESLKNAENELSSEKGLMEERTKDIKAKSAKIEKYREQNNELQ 907
Cdd:PTZ00108 1206 KRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSP 1285
|
250 260 270
....*....|....*....|....*....|....*....
gi 2500794 908 LSINALEHDINKYQQETADASSTLDKLLKEYKWIASEKE 946
Cdd:PTZ00108 1286 PPPSKRPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKK 1324
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
757-1035 |
8.08e-03 |
|
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: 40.49 E-value: 8.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 757 ETLKKteESQRKAEEEYKALENKMKNAEAERGKEIKNAQQKLNSAKKKADDSSRKMKEKQQEVEAL-VLELEQLKQEQAS 835
Cdd:pfam15921 248 EALKS--ESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQnSMYMRQLSDLEST 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 836 YKQQSEAAQQAIASLKEQVSALEAEAVKTRESLKNAENE---LSSEKGLMEERTKDIKAKSAKIEK----YREQNNELQL 908
Cdd:pfam15921 326 VSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTErdqFSQESGNLDDQLQKLLADLHKREKelslEKEQNKRLWD 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 909 SINALEHDINKYQQETADASSTLDKLLKEYKWIASEKElfGQADTTYDfEANNPKETGQKLQKLLTK----KEKLEKSL- 983
Cdd:pfam15921 406 RDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQ--GQMERQMA-AIQGKNESLEKVSSLTAQlestKEMLRKVVe 482
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2500794 984 NMRAMNLLSEAEER-----YNDLMKKKRMVENDKIKILATIEELDRKKNKALHIAWE 1035
Cdd:pfam15921 483 ELTAKKMTLESSERtvsdlTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE 539
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
679-874 |
8.09e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 8.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 679 KTMRDAEDELKiktSQLEATEKELANLKNMA-----EKYQHLKQQWEMKSEEAEllqTKIQQsayhkqqedllaLKKTIA 753
Cdd:PRK12704 31 AKIKEAEEEAK---RILEEAKKEAEAIKKEAlleakEEIHKLRNEFEKELRERR---NELQK------------LEKRLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 754 ECEETLKKTEESQRKAEEEykaLENKMKNAEAERgkeiknaqqklnsakkkaddssRKMKEKQQEVEALVLELEQLKQEQ 833
Cdd:PRK12704 93 QKEENLDRKLELLEKREEE---LEKKEKELEQKQ----------------------QELEKKEEELEELIEEQLQELERI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2500794 834 ASYkQQSEAAQQAIASLKEQvsaLEAEAVKT-RESLKNAENE 874
Cdd:PRK12704 148 SGL-TAEEAKEILLEKVEEE---ARHEAAVLiKEIEEEAKEE 185
|
|
| BicD |
pfam09730 |
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled ... |
420-875 |
9.23e-03 |
|
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled domains and are involved in dynein-mediated minus end-directed transport from the Golgi apparatus to the endoplasmic reticulum (ER). For full functioning they bind with GSK-3beta pfam05350 to maintain the anchoring of microtubules to the centromere. It appears that amino-acid residues 437-617 of BicD and the kinase activity of GSK-3 are necessary for the formation of a complex between BicD and GSK-3beta in intact cells.
Pssm-ID: 462863 [Multi-domain] Cd Length: 717 Bit Score: 40.23 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 420 QMKLKYAQQELKTKQAEVKKMDGSYKEDQEAFEAIRKTKEKLQDEMKKLKYEEAEQEAHLAKKKQ----LSSEISSLREL 495
Cdd:pfam09730 40 QNELKQARAVLSNTQAENERLASLSQELKEECECVELQRGRMRDEIKEYKVREARLLQDYSELEEenisLQKQVSVLKQN 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 496 CESIEA-KHPYLRFEYKNpeknwnpNCVKGLVVTLITVKDISTSKALEAVAGGKlynivvdTEATGKKILEKgQLKHRYT 574
Cdd:pfam09730 120 QVEFEGlKHEITRKEEET-------ELLNSQLEEAIRLREIAERQLDEALETLK-------TEREQKNSLRK-ELSHYMT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 575 IIPLSKISANSIGHEIISLAKNLIGHREVhiaisliDYNSELQKAMEYVFGtTLVCSSMDNakkvtfdkrimRKTVTLQG 654
Cdd:pfam09730 185 LNDFDYVSHLSISLDGLKFSEDEGAGTEP-------NNDGEAMDGGENGGG-GLKNSGLDN-----------RTSTPRKS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 655 DIFDPqgtlsggASSHVTPILSKLKTmrdaEDELKIKtSQLEATEKELANL-KNMAEKYQHLKQQWEMKSEeaellqtki 733
Cdd:pfam09730 246 EVFPP-------APSLVSDLLSELNI----SEIQKLK-QQLIQVEREKVSLlSTLQESQKQLEQAKGALSE--------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 734 QQSAYHKQQEDLLALKKTIAECEETLKKTEESQRKAEEEY----------KALENKMKNAEAERGKeiknAQQKLNSAKK 803
Cdd:pfam09730 305 QQEKVNRLTENLEAMRGLQASKERQDALDSEKDRDSHEDGdyyevdingpEILECKYRVAVEEAGE----LREELKALKA 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2500794 804 KADDSSRKMKEKQQEVEALVLEL-EQLKQEQASYKQQseaaQQAIASLKEQVSALEAEAVKTRESLKNAENEL 875
Cdd:pfam09730 381 RYNTLEERYKEEKTRWEAEAQDLaEKIRQLEKASHQD----QERIAHLEKELGKTRKVAGESEGSLSVAQDEL 449
|
|
| FliJ |
pfam02050 |
Flagellar FliJ protein; |
806-904 |
9.56e-03 |
|
Flagellar FliJ protein;
Pssm-ID: 426581 [Multi-domain] Cd Length: 123 Bit Score: 37.65 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 806 DDSSRKMKEKQQEVEALVLELEQLKQEQASYKQQSEAAQQ-------------------AIASLKEQVSALEAEAVKTRE 866
Cdd:pfam02050 1 DEAARELAEAQRELQQAEEKLEELQQYRAEYQQQLSGAGQgisaaelrnyqafisqldeAIAQQQQELAQAEAQVEKARE 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 2500794 867 SLKNAENELSSEKGLMEERtkdiKAKSAKIEKYREQNN 904
Cdd:pfam02050 81 EWQEARQERKSLEKLRERE----KKEERKEQNRREQKQ 114
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
757-1169 |
9.67e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 757 ETLKKTEESQRKAEEEYKALENKMKnaeaergkEIKNAQQKLNSAK-KKADDSSRKMKEKQQEVEALVLELEQLKQEQAS 835
Cdd:PRK01156 476 EKKSRLEEKIREIEIEVKDIDEKIV--------DLKKRKEYLESEEiNKSINEYNKIESARADLEDIKIKINELKDKHDK 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 836 YkqqsEAAQQAIASLK------EQVSALEAEAVKTR---ESLKNAENELSSEKGLMEERTKDIKAKSAKIEKYREQN-NE 905
Cdd:PRK01156 548 Y----EEIKNRYKSLKledldsKRTSWLNALAVISLidiETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSiRE 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 906 LQLSINALEHDINKYQQETAdASSTLDKLLKEYKWIASEKELFGQADTTYDFEANNPKETGQKLQKLLTKKEKLEKSLNM 985
Cdd:PRK01156 624 IENEANNLNNKYNEIQENKI-LIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLES 702
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 986 RAMNLLSEAEERYNDLMKKKRMVENDKiKILATIEELDRKKNKAlhiawekvnkDFGSIFSMLLPGAKAMLVPSKKQNIL 1065
Cdd:PRK01156 703 TIEILRTRINELSDRINDINETLESMK-KIKKAIGDLKRLREAF----------DKSGVPAMIRKSASQAMTSLTRKYLF 771
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 1066 dglEFRVGLGDI--------------WKENLTELSGGQRSLAALSLILAILLF--KPAPIYILDEVDAALDLSHTQNIGQ 1129
Cdd:PRK01156 772 ---EFNLDFDDIdvdqdfnitvsrggMVEGIDSLSGGEKTAVAFALRVAVAQFlnNDKSLLIMDEPTAFLDEDRRTNLKD 848
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2500794 1130 MLHAHFKQS----QFLVVSLKDGMFNNANVLYRTKFVDGISTVS 1169
Cdd:PRK01156 849 IIEYSLKDSsdipQVIMISHHRELLSVADVAYEVKKSSGSSKVI 892
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
756-975 |
9.75e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.91 E-value: 9.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 756 EETLKKTEESQRKAEEEYKALENKMKNAEAErgkeIKNAQQKLNSAKKkaddssrkmkekqqeVEALVLELEQLKQE--- 832
Cdd:PRK05771 85 EELIKDVEEELEKIEKEIKELEEEISELENE----IKELEQEIERLEP---------------WGNFDLDLSLLLGFkyv 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500794 833 QASYKQQSEAAQQAIASLKEQVSALEAEAVKTRE-----SLKNAENELSSE---KGLMEERTKDIKAKSAKIEKYREQNN 904
Cdd:PRK05771 146 SVFVGTVPEDKLEELKLESDVENVEYISTDKGYVyvvvvVLKELSDEVEEElkkLGFERLELEEEGTPSELIREIKEELE 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2500794 905 ELQLSINALEHDINKYQQETADASSTLDKLLKEYKWIASEKELFGQADTTYDFEANNPKETGQKLQKLLTK 975
Cdd:PRK05771 226 EIEKERESLLEELKELAKKYLEELLALYEYLEIELERAEALSKFLKTDKTFAIEGWVPEDRVKKLKELIDK 296
|
|
| |
