|
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 |
1.77e-155 |
|
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: 495.65 E-value: 1.77e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 2 HVKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYKNGQAGITKASVSI 81
Cdd:pfam02463 1 YLKRIEIEGFKSYAKTVILP-FSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIHSKSGAFVNSAEVEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 82 TFDNSDKKqsplGFEVHDEITVTRQVVIGGRNKYLINGVNANNSRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPPEI 161
Cdd:pfam02463 80 TFDNEDHE----LPIDKEEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 162 LSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQKIMREIEHLSRLYIAYQFLL 241
Cdd:pfam02463 156 LEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 242 AEDTKERSAEELKEMQDKVVKLQEKLSENDKKIKALSHEIEELEKGKDKEIGGKLRSLEDALAEAQRVNTKSQSAFDLKK 321
Cdd:pfam02463 236 EERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 322 KNLASEENKRTELEKNMIEDSRTLAAKEKEVKKITDGLNALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLAGQ 401
Cdd:pfam02463 316 LKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 402 MMACKNDISKAQTEAKQAQMKLKHAQQELKTKQAEVKKMDSGYRKDQEALEAVKKLKEKLEAEMKKLNYEENKEEGLLEK 481
Cdd:pfam02463 396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 482 RRQLSRDISRLKETYEALLARFPNIQFAYRDPEKNWNRNCVKGLVASLISVKDTSTTTALELVAGERLYNVVVDTEVTGK 561
Cdd:pfam02463 476 ETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 562 KLLEKGELKRRYTIIPLNKISARCIAPETLRVAQNLVGPNNVHVALSLVEYKPeLQKAMEFVFGTTFVCNNMDNAKKVAF 641
Cdd:pfam02463 556 TADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQL-DKATLEADEDDKRAKVVEGILKDTEL 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 642 DKRIMTRTVTLGGEVFDPHGTLSGGARSQAASILTKFQELKNVQDELRIKENELQSLDEELAGLKNTAEKYRQLKQQWEM 721
Cdd:pfam02463 635 TKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKK 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 722 KTEEADLLQTKLQQSSYHKQQEELDALKKTIEESEETLKNTKEIQKKAEEKYEVLENKMKNAEAERDRELKDAQKKLDFA 801
Cdd:pfam02463 715 LKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEE 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 802 KTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYEVQIEAMAVEVAKNKESVNKAQEEVTKQKEV 881
Cdd:pfam02463 795 KLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLL 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 882 IIAQDNVIKAKYAEVAVHKEQNNDSQLKIKELDHNISKHKREAEDAASKVSKMLKDYDWINAEKHLFGQPNSAYDFKTNN 961
Cdd:pfam02463 875 KEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENN 954
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 962 PKEAGQRLQKLQEMKEKLGRNVNMRAMNVLTEAEERYNDLMKKKRIVENDKSKILATIEDLDQKKNQALNIAWQKVNKDF 1041
Cdd:pfam02463 955 KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWN 1034
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 1042 GSIFSTLLPGANAMLAPPEGQTVLDGLEFKVALGNTWKENLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDL 1121
Cdd:pfam02463 1035 KVFFYLELGGSAELRLEDPDDPFSGGIEISARPPGKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDD 1114
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|....*..
gi 1952970885 1122 SHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVLFKTKFV-DGVST 1167
Cdd:pfam02463 1115 QNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGVTMVeNGVST 1161
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
4-1144 |
8.26e-126 |
|
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: 415.99 E-value: 8.26e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 4 KSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYkNG---QAGITKASVS 80
Cdd:TIGR02168 3 KKLELAGFKSFADPTTIN-FDKGITGIVGPNGCGKSNIVDAIRWVLGEQSAKALRGGKMEDVIF-NGsetRKPLSLAEVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 81 ITFDNSDKkqsPLGFEVHDEITVTRQVVIGGRNKYLINGVNANNSRVQDLFCSVGLNVNNpHFLIMQGRITKVLNMKPPE 160
Cdd:TIGR02168 81 LVFDNSDG---LLPGADYSEISITRRLYRDGESEYFINGQPCRLKDIQDLFLDTGLGKRS-YSIIEQGKISEIIEAKPEE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 161 ILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEeITPTIQKLKEERSSYLEYQKIMREIEHLSRLYIAYQFL 240
Cdd:TIGR02168 157 RRAIFEEAAGISKYKERRKETERKLERTRENLDRLEDILNE-LERQLKSLERQAEKAERYKELKAELRELELALLVLRLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 241 LAEDTKERSAEELKEMQDKVVKLQEKLSENDKKIKALSHEIEELEKGKD--------------------KEIGGKLRSLE 300
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEelqkelyalaneisrleqqkQILRERLANLE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 301 DALAEAQRVNTKSQSAFDLKKKNLASEENKRTELEKNMIEDSRTLAAKEKEVKKITDGLNALQEASNKDAEALAAAQQHF 380
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 381 NAVSAGLSSNEDGAEAtLAGQMMACKNDISKAQTEAKQAQMKLkhAQQELKTKQAEVKKMDSGYRKDQEALEAVKKLKEK 460
Cdd:TIGR02168 396 ASLNNEIERLEARLER-LEDRRERLQQEIEELLKKLEEAELKE--LQAELEELEEELEELQEELERLEEALEELREELEE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 461 LEAEMKKLNYEENKEEGLLEKRRQLSRDISRLKETYEALLArfpniqfayrdpeKNWNRNCVKGLVASLISVkDTSTTTA 540
Cdd:TIGR02168 473 AEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLK-------------NQSGLSGILGVLSELISV-DEGYEAA 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 541 LELVAGERLYNVVVDTEVTGKK---LLEKGELKRRyTIIPLNKISARCIAPETLRVAQNLVGPnnVHVALSLVEYKPELQ 617
Cdd:TIGR02168 539 IEAALGGRLQAVVVENLNAAKKaiaFLKQNELGRV-TFLPLDSIKGTEIQGNDREILKNIEGF--LGVAKDLVKFDPKLR 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 618 KAMEFVFGTTFVCNNMDNAKKVAFDKRIMTRTVTLGGEVFDPHGTLSGGARSQAASILTKFQELKNVQDELRIKENELQS 697
Cdd:TIGR02168 616 KALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAE 695
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 698 LDEELAGLKntaekyrqlKQQWEMKTEEADLLQTKLQQS-SYHKQQEELDALKKTIEESEETLKNTKEIQKKAEEKYEVL 776
Cdd:TIGR02168 696 LEKALAELR---------KELEELEEELEQLRKELEELSrQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 777 E---NKMKNAEAERDRELKDAQKKLDFAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYEVQ 853
Cdd:TIGR02168 767 EerlEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 854 IEAMAVEVAKNKESVNKAQEEVTKQKEVIIAQDNVIKAKYAEVAVHKEQNNDSQLKIKELDHNISKHKREAEDAASKVSK 933
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 934 MLKDYDWINAE-KHLFGQPNSAY-----------DFKTNNPKEAGQRLQKLQEMKEKLGrNVNMRAMNVLTEAEERYNDL 1001
Cdd:TIGR02168 927 LELRLEGLEVRiDNLQERLSEEYsltleeaealeNKIEDDEEEARRRLKRLENKIKELG-PVNLAAIEEYEELKERYDFL 1005
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 1002 MKKKRIVENDKSKILATIEDLDQKKNQALNIAWQKVNKDFGSIFSTLLPGANAMLAPPEGQTVLD-GLEFKVALGNTWKE 1080
Cdd:TIGR02168 1006 TAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNENFQRVFPKLFGGGEAELRLTDPEDLLEaGIEIFAQPPGKKNQ 1085
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952970885 1081 NLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVS 1144
Cdd:TIGR02168 1086 NLSLLSGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDDANVERFANLLKEFSKNTQFIVIT 1149
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-1168 |
8.53e-122 |
|
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: 404.84 E-value: 8.53e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 2 HVKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYK-NGQAGITKASVS 80
Cdd:TIGR02169 1 YIERIELENFKSFGKKKVIP-FSKGFTVISGPNGSGKSNIGDAILFALGLSSSKAMRAERLSDLISNgKNGQSGNEAYVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 81 ITFDNSDKKqsplgfeVHDEITVTRQVVIGGRNK---YLINGVNANNSRVQDLFCSVGLNVNNPHFlIMQGRITKVLNMK 157
Cdd:TIGR02169 80 VTFKNDDGK-------FPDELEVVRRLKVTDDGKysyYYLNGQRVRLSEIHDFLAAAGIYPEGYNV-VLQGDVTDFISMS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 158 PPEILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITpTIQKLKEERSSYLEYQKIMREIEHLSRLYIAY 237
Cdd:TIGR02169 152 PVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQ-QLERLRREREKAERYQALLKEKREYEGYELLK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 238 QFLLAEDTKERSAEELKEMQDKVVKLQEKLSENDKKIKALSHEIEELEKGKDKEIGGKLRSLEDALAEAQRVNTKSQSAF 317
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 318 DLKKKNLASEENKRTELE------KNMIED-SRTLAAKEKEVKKITDGLNALQEASNKDAEALAAAQQHFNAVSAGLSSN 390
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEaeidklLAEIEElEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 391 EDGAEAtLAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKTKQAEVKKMDSgyRKDqEALEAVKKLKEKLEAEMKKLNY 470
Cdd:TIGR02169 391 REKLEK-LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEE--EKE-DKALEIKKQEWKLEQLAADLSK 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 471 EENKEEGLLEKRRQLSRDISRLKETYEALLARFPNIQFAYRDP-----EKNWNRNCVKGLVASLISVKDtSTTTALELVA 545
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGraveeVLKASIQGVHGTVAQLGSVGE-RYATAIEVAA 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 546 GERLYNVVVDTEVTGKKLLEKgeLKR----RYTIIPLNKISARCIAPETLRVaqnlvgPNNVHVALSLVEYKPELQKAME 621
Cdd:TIGR02169 546 GNRLNNVVVEDDAVAKEAIEL--LKRrkagRATFLPLNKMRDERRDLSILSE------DGVIGFAVDLVEFDPKYEPAFK 617
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 622 FVFGTTFVCNNMDNAKkvafdkRIM--TRTVTLGGEVFDPHGTLSGGARSQAASILTKFQ---ELKNVQDELRIKENELQ 696
Cdd:TIGR02169 618 YVFGDTLVVEDIEAAR------RLMgkYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSepaELQRLRERLEGLKRELS 691
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 697 SLDEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSyHKQQEELDALKKTIEESEETLKNTKEIQKKAEEKYEVL 776
Cdd:TIGR02169 692 SLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEE-EKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL 770
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 777 ENKMKNAEAE-RDRELKDAQKKLDfaktKADASSKKMKEKQQEVEAITLELE-ELKREHTSyKQQLEavnEAIKSYEVQI 854
Cdd:TIGR02169 771 EEDLHKLEEAlNDLEARLSHSRIP----EIQAELSKLEEEVSRIEARLREIEqKLNRLTLE-KEYLE---KEIQELQEQR 842
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 855 EamavEVAKNKESVNKAQEEVTKQKEVIIAQdnvIKAKYAEVAVHKEQNNDSQLKIKELDHNISKHKREAEDAASKVSKM 934
Cdd:TIGR02169 843 I----DLKEQIKSIEKEIENLNGKKEELEEE---LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKK 915
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 935 LKDYDWINAEKHLFGQPNSAYDFKTNNPKE---AGQRLQKLQEMKEKLGRN------VNMRAMNVLTEAEERYNDLMKKK 1005
Cdd:TIGR02169 916 RKRLSELKAKLEALEEELSEIEDPKGEDEEipeEELSLEDVQAELQRVEEEiralepVNMLAIQEYEEVLKRLDELKEKR 995
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 1006 RIVENDKSKILATIEDLDQKKNQALNIAWQKVNKDFGSIFSTLLPGanamlappEGQTVLD--------GLEFKVALGNT 1077
Cdd:TIGR02169 996 AKLEEERKAILERIEEYEKKKREVFMEAFEAINENFNEIFAELSGG--------TGELILEnpddpfagGLELSAKPKGK 1067
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 1078 WKENLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNA-NVL 1156
Cdd:TIGR02169 1068 PVQRLEAMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEAQFIVVSLRSPMIEYAdRAI 1147
|
1210
....*....|..
gi 1952970885 1157 FKTKFVDGVSTV 1168
Cdd:TIGR02169 1148 GVTMRRNGESQV 1159
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1-172 |
2.45e-102 |
|
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: 323.87 E-value: 2.45e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 1 MHVKSIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYKNGQAGITKASVS 80
Cdd:cd03273 1 MHIKEIILDGFKSYATRTVISGFDPQFNAITGLNGSGKSNILDAICFVLGITNLSTVRASNLQDLIYKRGQAGITKASVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 81 ITFDNSDKKQSPLGFEVHDEITVTRQVVIGGRNKYLINGVNANNSRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPPE 160
Cdd:cd03273 81 IVFDNSDKSQSPIGFENYPEITVTRQIVLGGTNKYLINGHRAQQQRVQDLFQSVQLNVNNPHFLIMQGRITKVLNMGGVW 160
|
170
....*....|..
gi 1952970885 161 ILSMIEEAAGTR 172
Cdd:cd03273 161 KESLTELSGGQR 172
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-1157 |
1.03e-88 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 308.79 E-value: 1.03e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 1 MHVKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYkNGQAG---ITKA 77
Cdd:COG1196 1 MRLKRLELAGFKSFADPTTIP-FEPGITAIVGPNGSGKSNIVDAIRWVLGEQSAKSLRGGKMEDVIF-AGSSSrkpLGRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 78 SVSITFDNSDKKqSPLGFevhDEITVTRQVVIGGRNKYLINGVNANNSRVQDLFCSVGLNVNNpHFLIMQGRITKVLNMK 157
Cdd:COG1196 79 EVSLTFDNSDGT-LPIDY---DEVTITRRLYRSGESEYYINGKPCRLKDIQDLFLDTGLGPES-YSIIGQGMIDRIIEAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 158 PPEILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILeEEITPTIQKLKEERSSYLEYQKIMREIEHLSRLYIAY 237
Cdd:COG1196 154 PEERRAIIEEAAGISKYKERKEEAERKLEATEENLERLEDIL-GELERQLEPLERQAEKAERYRELKEELKELEAELLLL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 238 QFLLAEDTKERSAEELKEMQDKVVKLQEKLSENDKKIKALSHEIEELEKgKDKEIGGKLRSLEDALAEAQRVNTKSQSAF 317
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL-ELEEAQAEEYELLAELARLEQDIARLEERR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 318 DLKKKNLASEENKRTELEKNMIEDSRTLAAKEKEVKKITDGLNALQEASNKDAEALAAAQQHFNAVSAGLSSNEDgAEAT 397
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE-ELLE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 398 LAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKTKQAEVKKMDSGYRKDQEALEAVKKLKEKLEAEMKKLN----YEEN 473
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLellaELLE 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 474 KEEGLLEKRRQLSRDISRLKETYEALLARFPNIQFAYRD---PEKNWNRNCVKGLVASLISVkDTSTTTALELVAGERLY 550
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvkaALLLAGLRGLAGAVAVLIGV-EAAYEAALEAALAAALQ 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 551 NVVVDTEVTGKKLLE--KGELKRRYTIIPLNKISARciAPETLRVAQNLVGPNNVHVALSLVEYKPELQKAMEFVFGTTF 628
Cdd:COG1196 550 NIVVEDDEVAAAAIEylKAAKAGRATFLPLDKIRAR--AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTL 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 629 VCNNMDNAKKVAFDKRIMTRTVTLGGEVFDPHGTLSGGARSQAASiltkfqelknvqdELRIKENELQSLDEELAglknt 708
Cdd:COG1196 628 VAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA-------------ALLEAEAELEELAERLA----- 689
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 709 aekyrqlkqqwemkteeadllqtklqqssyhkqqEELDALKKTIEESEETLKNTKEIQKKAEEKYEVLENKMKNAEAERD 788
Cdd:COG1196 690 ----------------------------------EEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 789 RELkdaqkkldfaktkadasskkmkEKQQEVEAITLELEELKREhtsykqqleavneaiksyevqieamavevaknkesv 868
Cdd:COG1196 736 ELL----------------------EELLEEEELLEEEALEELP------------------------------------ 757
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 869 nkaqeevtkqkeviiaqdnvikakyaevavhkeqnndsqlkikeldhniskhkrEAEDAAskvskmlkdydwinaekhlf 948
Cdd:COG1196 758 ------------------------------------------------------EPPDLE-------------------- 763
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 949 gqpnsaydfktnnpkEAGQRLQKLQEMKEKLGrNVNMRAMNVLTEAEERYNDLMKKKRIVENDKSKILATIEDLDQKKNQ 1028
Cdd:COG1196 764 ---------------ELERELERLEREIEALG-PVNLLAIEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRE 827
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 1029 ALNIAWQKVNKDFGSIFSTLLPGANAMLAPPEGQTVLD-GLEFKVALGNTWKENLTELSGGQRSLVALSLILSMLLFKPA 1107
Cdd:COG1196 828 RFLETFDAVNENFQELFPRLFGGGEAELLLTDPDDPLEtGIEIMAQPPGKKLQRLSLLSGGEKALTALALLFAIFRLNPS 907
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|
gi 1952970885 1108 PIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVLF 1157
Cdd:COG1196 908 PFCVLDEVDAPLDDANVERFAELLKEMSEDTQFIVITHNKRTMEAADRLY 957
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1074-1168 |
5.52e-63 |
|
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: 214.85 E-value: 5.52e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 1074 LGNTWKENLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNA 1153
Cdd:cd03273 156 MGGVWKESLTELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGSQFIVVSLKEGMFNNA 235
|
90
....*....|....*
gi 1952970885 1154 NVLFKTKFVDGVSTV 1168
Cdd:cd03273 236 NVLFRTRFVDGTSTV 250
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
522-639 |
5.67e-33 |
|
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: 123.88 E-value: 5.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 522 VKGLVASLISVKDtSTTTALELVAGERLYNVVVDTEVTGKKLLEKGELKR--RYTIIPLNKISARCIAPETLRvAQNLVG 599
Cdd:smart00968 3 VLGRVADLISVDP-KYETALEAALGGRLQAVVVDTEETAKKAIEFLKKNRlgRATFLPLDKIKPRSPAGSKLR-EALLPE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1952970885 600 PNNVHVALSLVEYKPELQKAMEFVFGTTFVCNNMDNAKKV 639
Cdd:smart00968 81 PGFVGPAIDLVEYDPELRPALEYLLGNTLVVDDLETARRL 120
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1085-1167 |
7.54e-31 |
|
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: 119.72 E-value: 7.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 1085 LSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTH-SQFIVVSLKEGMFNNANVLFKTKFVD 1163
Cdd:cd03239 95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHtSQFIVITLKKEMFENADKLIGVLFVH 174
|
....
gi 1952970885 1164 GVST 1167
Cdd:cd03239 175 GVST 178
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
3-164 |
6.24e-28 |
|
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: 113.51 E-value: 6.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 3 VKSIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLLGISNlSQVRASNLQDLVYKNGQAGITKASVSIT 82
Cdd:cd03272 1 IKQVIIQGFKSYKDQTVIEPFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEY-THLREEQRQALLHEGSGPSVMSAYVEII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 83 FDNSDKKqsplgFEVHDEITVTRQVVIGGRNKYLINGVNANNSRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPPEIL 162
Cdd:cd03272 80 FDNSDNR-----FPIDKEEVRLRRTIGLKKDEYFLDKKNVTKNDVMNLLESAGFSRSNPYYIVPQGKINSLTNMKQDEQQ 154
|
..
gi 1952970885 163 SM 164
Cdd:cd03272 155 EM 156
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
3-86 |
3.04e-25 |
|
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: 103.93 E-value: 3.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 3 VKSIILEGFKSYAQRTEVNGFDPlFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQdLVYKNGQAGITKASVSIT 82
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSNS-FNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLF-LAGGGVKAGINSASVEIT 78
|
....
gi 1952970885 83 FDNS 86
Cdd:cd03239 79 FDKS 82
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
4-89 |
2.33e-24 |
|
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: 101.77 E-value: 2.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 4 KSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYK--NGQAGITKASVSI 81
Cdd:cd03278 2 KKLELKGFKSFADKTTIP-FPPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAKSLRGEKMSDVIFAgsETRKPANFAEVTL 80
|
....*...
gi 1952970885 82 TFDNSDKK 89
Cdd:cd03278 81 TFDNSDGR 88
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1081-1157 |
2.13e-23 |
|
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: 99.08 E-value: 2.13e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952970885 1081 NLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVLF 1157
Cdd:cd03278 110 RLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAADRLY 186
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
522-640 |
6.48e-23 |
|
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: 95.02 E-value: 6.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 522 VKGLVASLISVKDTsTTTALELVAGERLYNVVVDTEVTGKKLLE--KGELKRRYTIIPLNKISARCIAPETLrvaqnlvG 599
Cdd:pfam06470 4 VLGRLADLIEVDEG-YEKAVEAALGGRLQAVVVDDEDDAKRAIEflKKNKLGRATFLPLDRLKPRPRRPGAD-------L 75
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1952970885 600 PNNVHVALSLVEYKPELQKAMEFVFGTTFVCNNMDNAKKVA 640
Cdd:pfam06470 76 KGGAGPLLDLVEYDDEYRKALRYLLGNTLVVDDLDEALELA 116
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
4-159 |
2.63e-21 |
|
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: 94.56 E-value: 2.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 4 KSIILEGFKSYAQRTEVNGFDPlFNAITGLNGSGKSNILDSICFLLGISNlSQVRASNLQDLVY--KNGQAGITKASVSI 81
Cdd:cd03275 2 KRLELENFKSYKGRHVIGPFDR-FTCIIGPNGSGKSNLMDAISFVLGEKS-SHLRSKNLKDLIYraRVGKPDSNSAYVTA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952970885 82 TFDNSDKkqsplgfevhdEITVTRQVVIGGRNKYLINGVNANNSRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPP 159
Cdd:cd03275 80 VYEDDDG-----------EEKTFRRIITGGSSSYRINGKVVSLKEYNEELEKINILVKARNFLVFQGDVESIASKNPP 146
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1082-1167 |
5.93e-19 |
|
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: 85.10 E-value: 5.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 1082 LTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTH-SQFIVVSLKEGMFNNANVLFKTK 1160
Cdd:cd03227 75 RLQLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKgAQVIVITHLPELAELADKLIHIK 154
|
....*...
gi 1952970885 1161 FV-DGVST 1167
Cdd:cd03227 155 KViTGVYK 162
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1081-1168 |
5.34e-18 |
|
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: 84.62 E-value: 5.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 1081 NLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVLFKTK 1160
Cdd:cd03272 155 EMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEVADKFYGVK 234
|
....*...
gi 1952970885 1161 FVDGVSTV 1168
Cdd:cd03272 235 FRNKVSTI 242
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1085-1156 |
4.08e-16 |
|
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: 79.15 E-value: 4.08e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952970885 1085 LSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFT-HSQFIVVSLKEGMFNNANVL 1156
Cdd:cd03275 156 LSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAGpNFQFIVISLKEEFFSKADAL 228
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1078-1156 |
3.18e-15 |
|
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: 75.80 E-value: 3.18e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952970885 1078 WKeNLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVL 1156
Cdd:cd03274 122 WK-NISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELADRL 199
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
3-156 |
3.67e-15 |
|
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: 75.80 E-value: 3.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 3 VKSIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLLGIsNLSQVRASNLQDLVYK-NGQAGITKASVSI 81
Cdd:cd03274 3 ITKLVLENFKSYAGEQVIGPFHKSFSAIVGPNGSGKSNVIDSMLFVFGF-RASKMRQKKLSDLIHNsAGHPNLDSCSVEV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952970885 82 TFDnsdkkqsplgfEVHDEitvtrqvviggrnkylingvnannsrvqDLFCSVGLNVNNPHFLIMQGRITKVLNM 156
Cdd:cd03274 82 HFQ-----------EIIDK----------------------------PLLKSKGIDLDHNRFLILQGEVEQIAQM 117
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
160-1016 |
1.35e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.41 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 160 EILSMIEEAagtRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSSY-LEYQKIMREIEHLSRLYIAYQ 238
Cdd:PTZ00121 1095 EAFGKAEEA---KKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEdAKRVEIARKAEDARKAEEARK 1171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 239 fllAEDTKE----------RSAEELKEMQDKVVKLQEKLSENDKKIKAL--------SHEIEELEKGKDKEIGGKLRSLE 300
Cdd:PTZ00121 1172 ---AEDAKKaeaarkaeevRKAEELRKAEDARKAEAARKAEEERKAEEArkaedakkAEAVKKAEEAKKDAEEAKKAEEE 1248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 301 DALAEAQRVNTKSQSAFDLKKKNLASEENKRTELEKNMIEDSRTLAAKEKEVKKITDGLNALQEASNKDAEALAAAQQHF 380
Cdd:PTZ00121 1249 RNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK 1328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 381 NAVSAGLSSNEDGAEATLAGQMMA--CKNDISKAQTEAKQAQMKLKHAQQ---ELKTKQAEVKKMDSGYRKDQE----AL 451
Cdd:PTZ00121 1329 KKADAAKKKAEEAKKAAEAAKAEAeaAADEAEAAEEKAEAAEKKKEEAKKkadAAKKKAEEKKKADEAKKKAEEdkkkAD 1408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 452 EAVKKLKEKLEAEMKKLNYEENKEEGLLEKRRQLSRDISRLKETYEallarfpniqfayrdpEKNWNRNCVKGlvASLIS 531
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE----------------EAKKAEEAKKK--AEEAK 1470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 532 VKDTSTTTALELVAGERLYNVVVDTEVTGKKLLEKGELKRRYTiiPLNKISARCIAPEtLRVAQNLVGPNNVHVALSlVE 611
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD--EAKKAEEAKKADE-AKKAEEAKKADEAKKAEE-KK 1546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 612 YKPELQKAMEFVFGTTfvCNNMDNAKKVAFDKRIMTRTVTLGGEVfdphgtlsggARSQAASILTKFQELKNVQDELRIK 691
Cdd:PTZ00121 1547 KADELKKAEELKKAEE--KKKAEEAKKAEEDKNMALRKAEEAKKA----------EEARIEEVMKLYEEEKKMKAEEAKK 1614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 692 ENELQSLDEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEEldalkktiEESEETLKNTKEIQKKAEE 771
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA--------KKAEEDKKKAEEAKKAEED 1686
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 772 KYEVLENKMKnaEAERDRELKDAQKKLDFAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEaIKSYE 851
Cdd:PTZ00121 1687 EKKAAEALKK--EAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKK-IAHLK 1763
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 852 VQIEAMAVEVAKNKESVNKaqEEVTKQKEVIIAQ-DNVIKAKYAEVAVHKEQNNDSQLKIKELDHNISKHKREAEDAASK 930
Cdd:PTZ00121 1764 KEEEKKAEEIRKEKEAVIE--EELDEEDEKRRMEvDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNM 1841
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 931 VSKMLKDYD----WINAEKHLFGQPNSAYDFKTNNPKEAGQRLQKLQEMK-------EKLGRNVNMRAMNvlteAEERYN 999
Cdd:PTZ00121 1842 QLEEADAFEkhkfNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEkidkddiEREIPNNNMAGKN----NDIIDD 1917
|
890 900
....*....|....*....|
gi 1952970885 1000 DLMK---KKRIVENDKSKIL 1016
Cdd:PTZ00121 1918 KLDKdeyIKRDAEETREEII 1937
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
5-83 |
2.95e-14 |
|
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: 71.62 E-value: 2.95e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952970885 5 SIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRasnlqdlvYKNGQAGITKASVSITF 83
Cdd:cd03227 1 KIVLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRR--------RSGVKAGCIVAAVSAEL 71
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
156-947 |
7.71e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.72 E-value: 7.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 156 MKPPEILSMIEEAagTRMYEYKKIAAQKTIEkkEAKLKEIKTILEEEITPTIQKlKEERSSYLEYQKIMREIEHLSRLYI 235
Cdd:PTZ00121 1121 KKKAEDARKAEEA--RKAEDARKAEEARKAE--DAKRVEIARKAEDARKAEEAR-KAEDAKKAEAARKAEEVRKAEELRK 1195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 236 AYQFLLAEDTK----ERSAEELKEMQDkvvklqEKLSENDKKIKALSHEIEELEKGKDKEIGGKLRSLEDAL-------- 303
Cdd:PTZ00121 1196 AEDARKAEAARkaeeERKAEEARKAED------AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARmahfarrq 1269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 304 ----AEAQRVNTKSQSAFDLKKKNLA--SEENKRTELEKNMIEDSRT---LAAKEKEVKKITDGLNALQEASNKDAEALA 374
Cdd:PTZ00121 1270 aaikAEEARKADELKKAEEKKKADEAkkAEEKKKADEAKKKAEEAKKadeAKKKAEEAKKKADAAKKKAEEAKKAAEAAK 1349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 375 AAQQhfnAVSAGLSSNEDGAEAT-LAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKTKQAEVKKMDSGYRKdqeALEA 453
Cdd:PTZ00121 1350 AEAE---AAADEAEAAEEKAEAAeKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKK---ADEA 1423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 454 VKKLKEKLEAEMKKLNYEENKEEGLLEKRRQLSRDISRLKETYEallaRFPNIQFAYRDPEKNWNRNCVKGLVASLISVK 533
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE----EAKKADEAKKKAEEAKKADEAKKKAEEAKKKA 1499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 534 DTSTTTALELVAGERLYNVvvdTEVTGKKLLEKGELKRRytiiplnkisarciaPETLRVAQNLVGPNNVHVAlslveyk 613
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKA---EEAKKADEAKKAEEAKK---------------ADEAKKAEEKKKADELKKA------- 1554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 614 PELQKAMEfvfgttfvCNNMDNAKKVAFDKRIMTRTVTLGGEVfdPHGTLSGGARSQAASILTKFQELKNVQDElRIKEN 693
Cdd:PTZ00121 1555 EELKKAEE--------KKKAEEAKKAEEDKNMALRKAEEAKKA--EEARIEEVMKLYEEEKKMKAEEAKKAEEA-KIKAE 1623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 694 ELQSLDEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSyHKQQEELDALKKTIEESEETLKNTKEIQKKAEEKY 773
Cdd:PTZ00121 1624 ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA-KKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 774 EVLEnkMKNAEAERDRELKDAQKKLDFAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYEVQ 853
Cdd:PTZ00121 1703 KAEE--LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 854 I-EAMAVEVAKNKESVNKAQEEVTKQKEVIIAQDN-----VIKAKYAEVAVHKEQNNDSQLKIKELDHnISKHKREAEDA 927
Cdd:PTZ00121 1781 IeEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKegnlvINDSKEMEDSAIKEVADSKNMQLEEADA-FEKHKFNKNNE 1859
|
810 820
....*....|....*....|
gi 1952970885 928 ASKVSKMLKDYdwiNAEKHL 947
Cdd:PTZ00121 1860 NGEDGNKEADF---NKEKDL 1876
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1-880 |
1.21e-13 |
|
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: 75.78 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 1 MHVKSIILEGFKSYaQRTEVNGFDPL--FNAITGLNGSGKSNILDSICFLLgisnLSQVRASNlQDLVYKNGQAGITKAS 78
Cdd:TIGR00618 1 MKPLRLTLKNFGSY-KGTHTIDFTALgpIFLICGKTGAGKTTLLDAITYAL----YGKLPRRS-EVIRSLNSLYAAPSEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 79 VSITFDNSDKKQSplgFEVHDEITVTR---------QVVI---GGRNKYLINGVNANNSRVQDLfcsvgLNVNNPHF--- 143
Cdd:TIGR00618 75 AFAELEFSLGTKI---YRVHRTLRCTRshrkteqpeQLYLeqkKGRGRILAAKKSETEEVIHDL-----LKLDYKTFtrv 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 144 -LIMQGRITKVLNMKPPEILSMIEEAAGTRMYE---------YKKIAAQKTIEKKEAKL------------KEIKTILEE 201
Cdd:TIGR00618 147 vLLPQGEFAQFLKAKSKEKKELLMNLFPLDQYTqlalmefakKKSLHGKAELLTLRSQLltlctpcmpdtyHERKQVLEK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 202 EITPTIQKLKEERSSYLEYQKIMREIEHLSRLYIAYQFLLAEDTKERSAEELKEMQDKVVKLQEKLSENDKKIKALSHeI 281
Cdd:TIGR00618 227 ELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQ-I 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 282 EELEKGKDKEIGGKLRSLEDALAEAQRVNTKSQSAFDLKKknlaSEENKRTELEKNMIEdsrtlAAKEKEVKKITDGLNA 361
Cdd:TIGR00618 306 EQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRR----LLQTLHSQEIHIRDA-----HEVATSIREISCQQHT 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 362 LQEASNKDAEALAAAQQHFNAVSAGLS--SNEDGAEATLAGQMMACKNDISKAQTEaKQAQMKLKHAQQELKTKQAEVKK 439
Cdd:TIGR00618 377 LTQHIHTLQQQKTTLTQKLQSLCKELDilQREQATIDTRTSAFRDLQGQLAHAKKQ-QELQQRYAELCAAAITCTAQCEK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 440 MdsgyrKDQEALEAVKKLKEKLEAEMKKLNYEENKEE--GLLEKRRQLSRDISRLKETYEallaRFPNIQfayrdpeknw 517
Cdd:TIGR00618 456 L-----EKIHLQESAQSLKEREQQLQTKEQIHLQETRkkAVVLARLLELQEEPCPLCGSC----IHPNPA---------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 518 nrncvkgLVASLISVKDTSTTTALE------LVAGERLYNVVVDTEVTGKKLLEKGELKRRYTIIPLNKISA-RCIAPET 590
Cdd:TIGR00618 517 -------RQDIDNPGPLTRRMQRGEqtyaqlETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRsKEDIPNL 589
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 591 LRVAQNL--VGPNNVHVALSLVEYKPELQKAMEfvfgttfvcNNMDNAKKVAFDKRIMTRTVTLGGEVFDPHGTLSGGAR 668
Cdd:TIGR00618 590 QNITVRLqdLTEKLSEAEDMLACEQHALLRKLQ---------PEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERV 660
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 669 SQAASILTKFQELKNVQDELriKENELQSLDEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSyHKQQEELDAL 748
Cdd:TIGR00618 661 REHALSIRVLPKELLASRQL--ALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENAS-SSLGSDLAAR 737
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 749 KKTIEESEETLKNTKEIQKKAEEKYEVLENKMKNAEAERDRELKDAQKKLDFAKTKADASSKKMKEKQQEVE-------- 820
Cdd:TIGR00618 738 EDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGqeipsded 817
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 821 AITLELEELKREHTSYKQQLEAVNEAIKSYEVQIEAMAvEVAKNKESVNKAQEEVTKQKE 880
Cdd:TIGR00618 818 ILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYE-ECSKQLAQLTQEQAKIIQLSD 876
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
4-257 |
1.38e-12 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 68.11 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 4 KSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSqvRASNLQDLVYKngqaGITKASVSITF 83
Cdd:COG0419 3 LRLRLENFRSYRDTETID-FDDGLNLIVGPNGAGKSTILEAIRYALYGKARS--RSKLRSDLINV----GSEEASVELEF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 84 DNSDKkqsplgfevhdEITVTRQvviggrnkylingvnannsrvqdlfcsvglnvnnphflimQGRITKVLNMKPPEILS 163
Cdd:COG0419 76 EHGGK-----------RYRIERR----------------------------------------QGEFAEFLEAKPSERKE 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 164 MIEEAAGTRMYeykkiaaqktiEKKEAKLKEIKTILEEEI--TPTIQKLKEER-SSYLEYQkimrEIEHLS---RLYIAY 237
Cdd:COG0419 105 ALKRLLGLEIY-----------EELKERLKELEEALESALeeLAELQKLKQEIlAQLSGLD----PIETLSggeRLRLAL 169
|
250 260
....*....|....*....|....*....
gi 1952970885 238 QFLLA---------EDTKERSAEELKEMQ 257
Cdd:COG0419 170 ADLLSlildfgsldEERLERLLDALEELA 198
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1046-1144 |
9.88e-12 |
|
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: 64.19 E-value: 9.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 1046 STLLPGANAMLAPPEGQTVLDGLEFKVALGNTWKEN---LTELSGGQRSLVALSLILsmlLFKPaPIYILDEVDAALDLS 1122
Cdd:cd00267 39 STLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRigyVPQLSGGQRQRVALARAL---LLNP-DLLLLDEPTSGLDPA 114
|
90 100
....*....|....*....|...
gi 1952970885 1123 HTQNIGQMLRTHF-THSQFIVVS 1144
Cdd:cd00267 115 SRERLLELLRELAeEGRTVIIVT 137
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
677-1024 |
9.90e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.78 E-value: 9.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 677 KFQELKNVQDELRIKENELQSLDEELAGLK-NTAEKYRQLKQQWEM-KTEEADLLQTKLQQSSYHKQQEELDALKKTIEE 754
Cdd:PTZ00121 1244 KAEEERNNEEIRKFEEARMAHFARRQAAIKaEEARKADELKKAEEKkKADEAKKAEEKKKADEAKKKAEEAKKADEAKKK 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 755 SEETLKNTKEIQKKAEEKYEVLENKMKNAEAERD------RELKDAQKKLDFAKTKADASSKKMKEKQQEVEAiTLELEE 828
Cdd:PTZ00121 1324 AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADeaeaaeEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEA-KKKAEE 1402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 829 LKREHTSYKQQLEAVNEAIKSYEVQIEAMAVEVAKNK-ESVNKAQEEVTKQKEVIIAQDNVIKAKYAEVAVHKEQNNDSQ 907
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKaEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEA 1482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 908 LKIKELDHNISKHKREAEDAASKVSKMLKDYDWINAEkhlfgQPNSAYDFKTNNPKEAGQRLQKLQEMKeklgRNVNMRA 987
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE-----EAKKADEAKKAEEAKKADEAKKAEEKK----KADELKK 1553
|
330 340 350
....*....|....*....|....*....|....*..
gi 1952970885 988 MNVLTEAEERYNdlMKKKRIVENDKSKILATIEDLDQ 1024
Cdd:PTZ00121 1554 AEELKKAEEKKK--AEEAKKAEEDKNMALRKAEEAKK 1588
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
2-259 |
7.30e-11 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 65.18 E-value: 7.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 2 HVKSIILEGFKSYAQrTEVNgFDPLFNAITGLNGSGKSNILDSICFLlgiSNLSQVRASNLQDLVyKNGQAGitkASVSI 81
Cdd:COG1195 1 RLKRLSLTNFRNYES-LELE-FSPGINVLVGPNGQGKTNLLEAIYLL---ATGRSFRTARDAELI-RFGADG---FRVRA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 82 TFDNSDKKqsplgFEVhdEITVTRqvviGGRNKYLINGVNAnnSRVQDLFCSvgLNVnnphflIMqgrITkvlnmkpPEI 161
Cdd:COG1195 72 EVERDGRE-----VRL--GLGLSR----GGKKRVRINGKPV--RRLSDLAGL--LPV------VL---FS-------PED 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 162 LSMIEEAAGTR-------------MY-----EYKKIAAQKTiekkeAKLKEIKT-------ILEEEITPTIQKLKEERSS 216
Cdd:COG1195 121 LRLVKGGPSERrrfldrllfqldpRYldalsRYERALKQRN-----ALLKQGREadlalldVWDEQLAELGAAIIAARLA 195
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1952970885 217 YLE---------YQKIMREIEHLSrlyIAYQFLLAEDT---KERSAEELKEMQDK 259
Cdd:COG1195 196 FLErlaplfaeiYAALSGGKEELE---LRYRSGWLYESaelEEALLEALAENRER 247
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
242-509 |
8.14e-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: 65.17 E-value: 8.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 242 AEDTKERSAEELKEMQDKVVKLQEKLSENDKKIKALSHEIEELEKgKDKEIGGKLRSLEDALAEAQRvntksqsafdlkk 321
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-RIAALARRIRALEQELAALEA------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 322 kNLASEENKRTELEKNmiedsrtLAAKEKEVKKItdgLNALQEASNKDAEALaaaqqhfnavsagLSSNEDGAEATLAGQ 401
Cdd:COG4942 84 -ELAELEKEIAELRAE-------LEAQKEELAEL---LRALYRLGRQPPLAL-------------LLSPEDFLDAVRRLQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 402 MMACKNDISKAQTEA-KQAQMKLKHAQQELKTKQAEVKKMDSGYRKDQEALEAVKKLKEKLEAEM-KKLNYEENKEEGLL 479
Cdd:COG4942 140 YLKYLAPARREQAEElRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLeKELAELAAELAELQ 219
|
250 260 270
....*....|....*....|....*....|
gi 1952970885 480 EKRRQLSRDISRLKETYEALLARFPNIQFA 509
Cdd:COG4942 220 QEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-196 |
1.57e-10 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 61.74 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 6 IILEGFKSYaQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLG--ISNLSQVRASNLQDLVYKNGQAGITKASVSITF 83
Cdd:pfam13476 1 LTIENFRSF-RDQTID-FSKGLTLITGPNGSGKTTILDAIKLALYgkTSRLKRKSGGGFVKGDIRIGLEGKGKAYVEITF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 84 DNSDKKQSplgFEVHDEITVTRQVVIGGRNKYL-INGVNANNSRVQDLFCSvgLNVNNPHFLIM-QGRITKVLNMKPPEI 161
Cdd:pfam13476 79 ENNDGRYT---YAIERSRELSKKKGKTKKKEILeILEIDELQQFISELLKS--DKIILPLLVFLgQEREEEFERKEKKER 153
|
170 180 190
....*....|....*....|....*....|....*
gi 1952970885 162 LSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIK 196
Cdd:pfam13476 154 LEELEKALEEKEDEKKLLEKLLQLKEKKKELEELK 188
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1-499 |
1.70e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.45 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 1 MHVKSIILEGFKSYAQrTEVnGFDPLFNAITGLNGSGKSNILDSiCF--LLGISNLSQVrasnLQDLVYKngqaGITKAS 78
Cdd:PRK02224 1 MRFDRVRLENFKCYAD-ADL-RLEDGVTVIHGVNGSGKSSLLEA-CFfaLYGSKALDDT----LDDVITI----GAEEAE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 79 VSITFdnsdkkqSPLGFEVH---------DEITVTRQVVIGGRNkyLINGVNANNSRVQDLfcsvgLNVNNPHFL----I 145
Cdd:PRK02224 70 IELWF-------EHAGGEYHierrvrlsgDRATTAKCVLETPEG--TIDGARDVREEVTEL-----LRMDAEAFVncayV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 146 MQGRITKVLNMKPPEILSMIEEAAGT-RMYEYKKIAA--------------------QKTIEKKEAK------------L 192
Cdd:PRK02224 136 RQGEVNKLINATPSDRQDMIDDLLQLgKLEEYRERASdarlgvervlsdqrgsldqlKAQIEEKEEKdlherlngleseL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 193 KEIKTILE--EEITPTIQKLKEERSSYLE-YQKIMREIEHLSRLYIAYQFLLAEDTKERS--AEELKEMQDKVVKLQEKL 267
Cdd:PRK02224 216 AELDEEIEryEEQREQARETRDEADEVLEeHEERREELETLEAEIEDLRETIAETEREREelAEEVRDLRERLEELEEER 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 268 SE-------NDKKIKALSHEIEELEKgKDKEIGgklRSLEDALAEAQRVNTKSQS----AFDLKKKNlASEENKRTELEK 336
Cdd:PRK02224 296 DDllaeaglDDADAEAVEARREELED-RDEELR---DRLEECRVAAQAHNEEAESlredADDLEERA-EELREEAAELES 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 337 NMIEDSRTLAAKEKEVKKITDGLNALQEASNKDAEALAAAQQHfnavSAGLSSNEDGA---EATLAGQMMACKNDISKAq 413
Cdd:PRK02224 371 ELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDF----LEELREERDELrerEAELEATLRTARERVEEA- 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 414 tEAKQAQMKLKHAQQELKtkqaevkkmDSGyrkDQEALEAVKKLKEKLEAEMKKLNYEENKEEGLLEKRRQLS---RDIS 490
Cdd:PRK02224 446 -EALLEAGKCPECGQPVE---------GSP---HVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVeaeDRIE 512
|
....*....
gi 1952970885 491 RLKETYEAL 499
Cdd:PRK02224 513 RLEERREDL 521
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
23-130 |
2.47e-10 |
|
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: 62.60 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 23 FDPLFNAITGLNGSGKSNILDSICFLLGIsnlsqvRASNlqDLVykngQAGITKASVSITFDNSDK-----KQSPLGFEV 97
Cdd:cd03241 19 FEEGLTVLTGETGAGKSILLDALSLLLGG------RASA--DLI----RSGAEKAVVEGVFDISDEeeakaLLLELGIED 86
|
90 100 110
....*....|....*....|....*....|...
gi 1952970885 98 HDEITVTRQVVIGGRNKYLINGVNANNSRVQDL 130
Cdd:cd03241 87 DDDLIIRREISRKGRSRYFINGQSVTLKLLREL 119
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
667-1030 |
7.46e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.62 E-value: 7.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 667 ARSQAASILTKFQELKNVQDELRIKENELQSLDEELAGLKNTAEKYRQLKQQWEMKtEEADLLQTKLQQssyhkqQEELD 746
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAK-KKADEAKKKAEE------KKKAD 1434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 747 ALKKTIEESeetlKNTKEIQKKAEEKYEVLENKMKNAEAERDRELKdaqKKLDFAKtKADASSKKMKEKQQEVEAITLEL 826
Cdd:PTZ00121 1435 EAKKKAEEA----KKADEAKKKAEEAKKAEEAKKKAEEAKKADEAK---KKAEEAK-KADEAKKKAEEAKKKADEAKKAA 1506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 827 EELKREHTSYKQQLEAVNEAIKSYEvqiEAMAVEVAKNKESVNKAqEEVTKQKEVIIAQDnvikAKYAEVAVHKEQNNDS 906
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKAE---EAKKADEAKKAEEKKKA-DELKKAEELKKAEE----KKKAEEAKKAEEDKNM 1578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 907 QLKIKELDHNISKHKREAEDAASKVSKMLKDYDWINAEKHlfgqpnsayDFKTNNPKEAGQRLQKLQEMKEKLGRNVNmR 986
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA---------KIKAEELKKAEEEKKKVEQLKKKEAEEKK-K 1648
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1952970885 987 AMNVLTEAEERYNDLMKKKRIVENDKSKI--LATIEDLDQKKNQAL 1030
Cdd:PTZ00121 1649 AEELKKAEEENKIKAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEAL 1694
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
668-895 |
1.72e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 668 RSQAASILTKFQELKNVQDELRIKENELQSLDEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSsyhkqQEELDA 747
Cdd:PRK03918 196 KEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIREL-----EERIEE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 748 LKKTIEESEETLKNTKEIQKKAEE---------KYEVLENKMKNAEAERDRELKDAQKKLDfaktKADASSKKMKEKQQE 818
Cdd:PRK03918 271 LKKEIEELEEKVKELKELKEKAEEyiklsefyeEYLDELREIEKRLSRLEEEINGIEERIK----ELEEKEERLEELKKK 346
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952970885 819 VEAITLELEELKREHTSYkQQLEAVNEAIKSYEVQIEAMAVEVAKNK-ESVNKAQEEVTKQKEVIIAQDNVIKAKYAE 895
Cdd:PRK03918 347 LKELEKRLEELEERHELY-EEAKAKKEELERLKKRLTGLTPEKLEKElEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
654-1142 |
1.93e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 654 GEVFDPHGTLSGGARSQAASILTKFQELKNVQDELRIKENELQSLDEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKL 733
Cdd:COG4717 56 DELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 734 Q-QSSYHKQQEELDALKKTIEESEETLKNTKEIQKKAEEKYEVLENKMKNAEAERDRELKDAQKKLDFAKTKADASSKKM 812
Cdd:COG4717 136 AlEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 813 KEKQQEVEAITLELEELKREHTSYKQQ------------------LEAVNEAIKSYEVQIEAMAVEVA-----------K 863
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEerlkearlllliaaallaLLGLGGSLLSLILTIAGVLFLVLgllallflllaR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 864 NKESVNKAQEEVTKQKEVIIAQDNVIKAKYAEVAVHKEQNNDSqlkIKELDHNIskhkREAEDAASKVSKMLKDYDWINA 943
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEE---LLELLDRI----EELQELLREAEELEEELQLEEL 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 944 EKHL-----FGQPNSAYDFktnnpKEAGQRLQKLQEMKEKL-----------GRNVNMRAMNVLTEAEERYNDLMKKKRI 1007
Cdd:COG4717 369 EQEIaallaEAGVEDEEEL-----RAALEQAEEYQELKEELeeleeqleellGELEELLEALDEEELEEELEELEEELEE 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 1008 VENDKSKILATIEDLDQKKNQ-----------------------------ALNIAWQ---------------KVNKDFGS 1043
Cdd:COG4717 444 LEEELEELREELAELEAELEQleedgelaellqeleelkaelrelaeewaALKLALElleeareeyreerlpPVLERASE 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 1044 IFSTLLPGANAMLAPPEgqtvldGLEFKVALGNTWKENLTELSGGQRSLVALSL---ILSMLLFKPAPIyILDEVDAALD 1120
Cdd:COG4717 524 YFSRLTDGRYRLIRIDE------DLSLKVDTEDGRTRPVEELSRGTREQLYLALrlaLAELLAGEPLPL-ILDDAFVNFD 596
|
570 580
....*....|....*....|..
gi 1952970885 1121 LSHTQNIGQMLRTHFTHSQFIV 1142
Cdd:COG4717 597 DERLRAALELLAELAKGRQVIY 618
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-808 |
2.54e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 1 MHVKSIILEGFKSYAQrTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYKNGqagiTKASVS 80
Cdd:PRK03918 1 MKIEELKIKNFRSHKS-SVVE-FDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKGLKKDDFTRIGG----SGTEIE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 81 ITFDNSDKKqsplgFEVHDEITVTRQVVIGGRNKYLINGVNANNSRVQDLFCSvgLNVNNPHFLIMQGRIT--------- 151
Cdd:PRK03918 75 LKFEKNGRK-----YRIVRSFNRGESYLKYLDGSEVLEEGDSSVREWVERLIP--YHVFLNAIYIRQGEIDailesdesr 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 152 -----KVLNMKPPEilSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSsylEYQKIMRE 226
Cdd:PRK03918 148 ekvvrQILGLDDYE--NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISS---ELPELREE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 227 IEHLSRLYIAYqfllaEDTKERSAE---ELKEMQDKVVKLQEKLSENDKKIKALSHEIEELEkgkdkEIGGKLRSLEDaL 303
Cdd:PRK03918 223 LEKLEKEVKEL-----EELKEEIEElekELESLEGSKRKLEEKIRELEERIEELKKEIEELE-----EKVKELKELKE-K 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 304 AEAQRVNTKSQSAFDLKKKNLASEENKRTELEKNMIEDSRTLAAKEKEVKKITDGLNALQeasnKDAEALAAAQQHFNAV 383
Cdd:PRK03918 292 AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELE----KRLEELEERHELYEEA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 384 SAgLSSNEDGAEATLAGQMmacKNDISKAQTEAKQAQMKLKHAQQELKTKQAEVKKMDSGYRKdqeALEAVKKLKEKLEA 463
Cdd:PRK03918 368 KA-KKEELERLKKRLTGLT---PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK---AIEELKKAKGKCPV 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 464 EMKKLNyEENKEEGLLEKRRQLSRDISRLKETYEALlarfpniqfayrdpeknwnRNCVKGLVASLISVKDTSTTTALEL 543
Cdd:PRK03918 441 CGRELT-EEHRKELLEEYTAELKRIEKELKEIEEKE-------------------RKLRKELRELEKVLKKESELIKLKE 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 544 VAgERLYNVVVDTEVTGKKLLEKGELKRRYTIIPLNKISARciapetlrvaqnlvgpnnvhvalsLVEYKPELQKAMEFV 623
Cdd:PRK03918 501 LA-EQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGE------------------------IKSLKKELEKLEELK 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 624 FGTTFVCNNMDNAKKVAfdKRIMTRTVTLGGEVFDphgTLSGGARSqAASILTKFQELKNVQDELRIKENELQSLDEEla 703
Cdd:PRK03918 556 KKLAELEKKLDELEEEL--AELLKELEELGFESVE---ELEERLKE-LEPFYNEYLELKDAEKELEREEKELKKLEEE-- 627
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 704 gLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSYHK-----------------QQEELDALKKTIEESEETLKNTKEIQ 766
Cdd:PRK03918 628 -LDKAFEELAETEKRLEELRKELEELEKKYSEEEYEElreeylelsrelaglraELEELEKRREEIKKTLEKLKEELEER 706
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 1952970885 767 KKAEEKYEVLENKMKNAEAERD--RELKDAQKKLDFAKTKADAS 808
Cdd:PRK03918 707 EKAKKELEKLEKALERVEELREkvKKYKALLKERALSKVGEIAS 750
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-123 |
4.20e-09 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 59.79 E-value: 4.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 1 MHVKSIILEGFKSYAqRTEVNgFDPLFNAITGLNGSGKSNILDSICFLlgiSNLSQVRASNLQDLVyKNGQAGitkASVS 80
Cdd:PRK00064 1 MYLTRLSLTDFRNYE-ELDLE-LSPGVNVLVGENGQGKTNLLEAIYLL---APGRSHRTARDKELI-RFGAEA---AVIH 71
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1952970885 81 ITFDNSdkkqsplGFEVHDEITVTRQvvigGRNKYLINGVNAN 123
Cdd:PRK00064 72 GRVEKG-------GRELPLGLEIDKK----GGRKVRINGEPQR 103
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
198-832 |
9.21e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 9.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 198 ILEE-EITPTIQKLKEERSSYLEYQKIM----REIEHLSRLYIAYQFLLAEDTKERSAEELKEM------QDKVVKLQEK 266
Cdd:COG4913 217 MLEEpDTFEAADALVEHFDDLERAHEALedarEQIELLEPIRELAERYAAARERLAELEYLRAAlrlwfaQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 267 LSENDKKIKALSHEIEELEKGKDkEIGGKLRSLEDALAEAqrvntksqsafDLKKKNLASEENKRTEleknmiedsRTLA 346
Cdd:COG4913 297 LEELRAELARLEAELERLEARLD-ALREELDELEAQIRGN-----------GGDRLEQLEREIERLE---------RELE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 347 AKEKEVKKITDGLNALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEAtlagqmmackndiskAQTEAKQAQMKLKHA 426
Cdd:COG4913 356 ERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE---------------ALAEAEAALRDLRRE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 427 QQELKTKQAEVKKMDSGYrkDQEALEAVKKLKEKLEAEMKKLNY--EenkeegLLEkrrqlsrdisrlketyeallarfp 504
Cdd:COG4913 421 LRELEAEIASLERRKSNI--PARLLALRDALAEALGLDEAELPFvgE------LIE------------------------ 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 505 niqfaYRDPEKNWnRNCVKGLVASLisvkdtstttALELVAGERLYNVVvdtevtgKKLLEKGELKRRytiIPLNKISAR 584
Cdd:COG4913 469 -----VRPEEERW-RGAIERVLGGF----------ALTLLVPPEHYAAA-------LRWVNRLHLRGR---LVYERVRTG 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 585 CIAPETLRVAQN-LVGpnnvhvalsLVEYKP-ELQKAMEFVFGTTF--VCnnMDNAKkvAFDKriMTRTVTLGGEVFDPH 660
Cdd:COG4913 523 LPDPERPRLDPDsLAG---------KLDFKPhPFRAWLEAELGRRFdyVC--VDSPE--ELRR--HPRAITRAGQVKGNG 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 661 GTLSGGARSQAAS-----------ILTKFQELKNVQDELRIKENELQSLDEELAGLKNTAEKYRQLKQQWEmktEEADLL 729
Cdd:COG4913 588 TRHEKDDRRRIRSryvlgfdnrakLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW---DEIDVA 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 730 QTKLQQSSYHKQQEELDA-------LKKTIEESEETLKNTKEIQKKAEEKYEVLENKMKNAEAERDRELKDAQKKLD--- 799
Cdd:COG4913 665 SAEREIAELEAELERLDAssddlaaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDlar 744
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1952970885 800 ----------FAKTKADASSKKMKEK-QQEVEAITLELEELKRE 832
Cdd:COG4913 745 lelralleerFAAALGDAVERELRENlEERIDALRARLNRAEEE 788
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
3-95 |
1.67e-08 |
|
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: 56.07 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 3 VKSIILEGFKSYAqRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVyKNGQagiTKASVSIT 82
Cdd:cd03276 1 IESITLKNFMCHR-HLQIE-FGPRVNFIVGNNGSGKSAILTALTIGLGGKASDTNRGSSLKDLI-KDGE---SSAKITVT 74
|
90
....*....|...
gi 1952970885 83 FDNSDKKQSPLGF 95
Cdd:cd03276 75 LKNQGLDANPLCV 87
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
694-868 |
4.53e-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: 55.32 E-value: 4.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 694 ELQSLDEELAGLKNTAEkyrqlkqqwEMKTEEADLlqtklqqssyhkqQEELDALKKTIEESEETLKNTKEIQKKAEEKY 773
Cdd:COG1579 11 DLQELDSELDRLEHRLK---------ELPAELAEL-------------EDELAALEARLEAAKTELEDLEKEIKRLELEI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 774 EVLENKMKNAEAERD-----RELKDAQKKLDFAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIK 848
Cdd:COG1579 69 EEVEARIKKYEEQLGnvrnnKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
|
170 180
....*....|....*....|
gi 1952970885 849 SYEVQIEAMAVEVAKNKESV 868
Cdd:COG1579 149 EELAELEAELEELEAEREEL 168
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
4-97 |
4.67e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 56.48 E-value: 4.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 4 KSIILEGFKSYaQRTEVNgFDPLfNAITGLNGSGKSNILDSICFL--LGISNLSQVRASN--LQDLVYKNGQAGITKASV 79
Cdd:COG4637 3 TRIRIKNFKSL-RDLELP-LGPL-TVLIGANGSGKSNLLDALRFLsdAARGGLQDALARRggLEELLWRGPRTITEPIRL 79
|
90
....*....|....*...
gi 1952970885 80 SITFDNSDkkQSPLGFEV 97
Cdd:COG4637 80 ELEFAEED--ERDLRYEL 95
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-109 |
5.37e-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: 54.54 E-value: 5.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 3 VKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICF-LLGISNLSQVRASNLQDLVYKngqaGITKASVSI 81
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIE-FFSPLTLIVGQNGAGKTTIIEALKYaLTGELPPNSKGGAHDPKLIRE----GEVRAQVKL 75
|
90 100
....*....|....*....|....*...
gi 1952970885 82 TFDNSDKKQsplgFEVHDEITVTRQVVI 109
Cdd:cd03240 76 AFENANGKK----YTITRSLAILENVIF 99
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
670-918 |
1.06e-07 |
|
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: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 670 QAASILTKFQELKNVQDELRIKENELQSLdeelAGLKNTAEKYRQLKqqwemktEEADLLQTKLQQSSYHKQQEELDALK 749
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDAREQIELL----EPIRELAERYAAAR-------ERLAELEYLRAALRLWFAQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 750 KTIEESEETLkntkeiqKKAEEKYEVLENKMKNAEAERDrELKDAqkkldfaktKADASSKKMKEKQQEVEAITLELEEL 829
Cdd:COG4913 295 AELEELRAEL-------ARLEAELERLEARLDALREELD-ELEAQ---------IRGNGGDRLEQLEREIERLERELEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 830 KREHTSYKQQLEAVneaiksyEVQIEAMAVEVAKNKESVNKAQEEVTKQKEviIAQDNVIKAKYAEVAVhKEQNNDSQLK 909
Cdd:COG4913 358 ERRRARLEALLAAL-------GLPLPASAEEFAALRAEAAALLEALEEELE--ALEEALAEAEAALRDL-RRELRELEAE 427
|
....*....
gi 1952970885 910 IKELDHNIS 918
Cdd:COG4913 428 IASLERRKS 436
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
685-849 |
1.66e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 685 QDELRIKENELQSLDEELAGLKntaEKYRQLKQQWEMKTEEADLLQTKLQQSSYhkqqEELDALKKTIEESEETLKNTKE 764
Cdd:COG4913 287 QRRLELLEAELEELRAELARLE---AELERLEARLDALREELDELEAQIRGNGG----DRLEQLEREIERLERELEERER 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 765 IQKKAEEKYEVLE----------NKMKNAEAERDRELKDAQKKLDFAKTKADASSKKMKEKQQEVEAitlELEELKREHT 834
Cdd:COG4913 360 RRARLEALLAALGlplpasaeefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA---EIASLERRKS 436
|
170
....*....|....*
gi 1952970885 835 SYKQQLEAVNEAIKS 849
Cdd:COG4913 437 NIPARLLALRDALAE 451
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-84 |
1.97e-07 |
|
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: 54.62 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 1 MHVKSIILEGFKSYaQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLqdlvYKNGQAGITKASVS 80
Cdd:COG3593 1 MKLEKIKIKNFRSI-KDLSIE-LSDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFDEEDF----YLGDDPDLPEIEIE 74
|
....
gi 1952970885 81 ITFD 84
Cdd:COG3593 75 LTFG 78
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
677-1053 |
2.16e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 677 KFQELKNVQDELRIKENELQSLDEelagLKNTAEKYRQlKQQWEMKTEEADLLQTKLQQSSYHKQQEELDALKKTIEESE 756
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAAKKKADE----AKKKAEEKKK-ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 757 ETLKNTKEIQKKAEEKYEVLENKMKNAEAERDRELKDAQKKLDFAKTKADA-SSKKMKEKQQEVEAITLE---------- 825
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAdEAKKAEEAKKADEAKKAEekkkadelkk 1553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 826 ------------LEELKREHTSYKQQLEAVNEAIKSYEVQIEAMAVEVAKNK----ESVNKAQEEVTKQKEVIIAQDNVI 889
Cdd:PTZ00121 1554 aeelkkaeekkkAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKkmkaEEAKKAEEAKIKAEELKKAEEEKK 1633
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 890 KAKYAEVAVHKEQNNDSQLKIKELDHNISKH--KREAEDAASKVSKMLK-DYDWINAEKHLFGQPNSAYDFKTNNPKEA- 965
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEELKKAEEENKIKAAeeAKKAEEDKKKAEEAKKaEEDEKKAAEALKKEAEEAKKAEELKKKEAe 1713
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 966 ----GQRLQKLQEMKEKLGRNVNMRAMNVLTEAEERYNDLMKKKRI----------VENDKSKILATIEDLDQKKNQALN 1031
Cdd:PTZ00121 1714 ekkkAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIahlkkeeekkAEEIRKEKEAVIEEELDEEDEKRR 1793
|
410 420
....*....|....*....|..
gi 1952970885 1032 IAWQKVNKDFGSIFSTLLPGAN 1053
Cdd:PTZ00121 1794 MEVDKKIKDIFDNFANIIEGGK 1815
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
986-1144 |
3.13e-07 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 53.46 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 986 RAMNVLTEAEERYNDLMKKKRIVENDKSKILATIEDLDQKKNQALNIAWQKVNKdfgsIFSTLLPGANAMLAPPEGQTVL 1065
Cdd:COG3950 97 RLKEEYFSRLDGYDSLLDEDSNLREFLEWLREYLEDLENKLSDELDEKLEAVRE----ALNKLLPDFKDIRIDRDPGRLV 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 1066 ----DGLEFkvalgntwkeNLTELSGGQRSLVAL--SLILSMLLFKPAP--------IYILDEVDAALDLSHTQNIGQML 1131
Cdd:COG3950 173 ildkNGEEL----------PLNQLSDGERSLLALvgDLARRLAELNPALenplegegIVLIDEIDLHLHPKWQRRILPDL 242
|
170
....*....|...
gi 1952970885 1132 RTHFTHSQFIVVS 1144
Cdd:COG3950 243 RKIFPNIQFIVTT 255
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
246-946 |
3.50e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 54.74 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 246 KERSAEELKEMQDKVVKLQEKLSEndkkikalSHEIEELEKGKDKE----IGGKLRSLE---DALAEAQRVNTKSQSAFD 318
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNE--------SNELHEKQKFYLRQsvidLQTKLQEMQmerDAMADIRRRESQSQEDLR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 319 LKKKNLASEENKRTELEKNMIEDSRT--------LAAKEKEVKKITDGLNALQEASNKDA-EALAAAQQHFNAVSAGLSS 389
Cdd:pfam15921 145 NQLQNTVHELEAAKCLKEDMLEDSNTqieqlrkmMLSHEGVLQEIRSILVDFEEASGKKIyEHDSMSTMHFRSLGSAISK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 390 ---NEDGAEATLAGQMMACKNDISKAQTE---------------------------------AKQAQMKLKHAQQELKTK 433
Cdd:pfam15921 225 ilrELDTEISYLKGRIFPVEDQLEALKSEsqnkielllqqhqdrieqliseheveitgltekASSARSQANSIQSQLEII 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 434 QAEVKKMDSGYRKDQEALEA-VKKLKEKLEaEMKKLnYEENKEEglLEKRRQLSRdiSRLKEtyeallARFPNIQFAYRd 512
Cdd:pfam15921 305 QEQARNQNSMYMRQLSDLEStVSQLRSELR-EAKRM-YEDKIEE--LEKQLVLAN--SELTE------ARTERDQFSQE- 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 513 peknwNRNCVKGLVASLISVKDTSTTTALELVAGERLYNVVVDTEVTGKKLleKGELKRRYTIIP-----LNKISARCIA 587
Cdd:pfam15921 372 -----SGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHL--RRELDDRNMEVQrlealLKAMKSECQG 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 588 PETLRVAQnLVGPNNVHVALSLVEYKPELQKAM--EFVFGTTFVCNNMDNAKKVAFDkriMTRTVTLGGEVFDPHGTLSG 665
Cdd:pfam15921 445 QMERQMAA-IQGKNESLEKVSSLTAQLESTKEMlrKVVEELTAKKMTLESSERTVSD---LTASLQEKERAIEATNAEIT 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 666 GARSQAASILTKFQELKNVQDELRIKENELQSLDEELAGLKNTAEKyrqLKQQWEmkteeaDLLQTKLQQS-SYHKQQEE 744
Cdd:pfam15921 521 KLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEI---LRQQIE------NMTQLVGQHGrTAGAMQVE 591
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 745 LDALKKTIEESEETLKNTKEIQKKAEEKYEVLEN----------KMKNAEAERDRELKDaqkkldfAKTKADASSKKMKE 814
Cdd:pfam15921 592 KAQLEKEINDRRLELQEFKILKDKKDAKIRELEArvsdlelekvKLVNAGSERLRAVKD-------IKQERDQLLNEVKT 664
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 815 KQQEVEAITLELEELKREHTSYKQQLEAVNEAIKsyeVQIEAMAVEVAKNKESVNKAQEEVTKQKEVIIAQDNVIKAKYA 894
Cdd:pfam15921 665 SRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLK---MQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRG 741
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 1952970885 895 EVavhkeqnNDSQLKIKELDHNISKHKREAEDAASKVSKMLKDYDWINAEKH 946
Cdd:pfam15921 742 QI-------DALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKN 786
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
709-905 |
7.63e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.89 E-value: 7.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 709 AEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEELDALKKTIEESEETLKnTKEIQKKAEEKYEVLENKMKNAEAERD 788
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLA-AQEQKKQAEEAAKQAALKQKQAEEAAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 789 RELKDAQKKLDFAKTKADASSKKMKE---KQQEVEAITLELEELKREHTSYKQQlEAVNEAIKSYEVQIEAMAVEVAKNK 865
Cdd:PRK09510 140 KAAAAAKAKAEAEAKRAAAAAKKAAAeakKKAEAEAAKKAAAEAKKKAEAEAAA-KAAAEAKKKAEAEAKKKAAAEAKKK 218
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1952970885 866 ESVNKAQEEVTKQKEVIIAQDNVIKAKYAEVAVHKEQNND 905
Cdd:PRK09510 219 AAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
680-897 |
8.31e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 8.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 680 ELKNVQDELRIKENELQSLDEELAGLKNTAEkyrQLKQQWEMKTEEADLLQTKLQQSsyhkqQEELDALKKTIEESEETL 759
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELE---ELNEEYNELQAELEALQAEIDKL-----QAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 760 KNTKEIQKKAEEKYEVLE------------------NKMKNAEAERDRELKDAQKKLDFAKTKADASSKKMKEKQQEVEA 821
Cdd:COG3883 89 GERARALYRSGGSVSYLDvllgsesfsdfldrlsalSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952970885 822 ITLELEELKREHTSYKQQLEAvneAIKSYEVQIEAMAVEVAKNKESVNKAQEEVTKQKEVIIAQDNVIKAKYAEVA 897
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSA---EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
668-1168 |
9.47e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 9.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 668 RSQAASILTKFQELKNVQDELRIKENELQSLDEELAGLKNTAEKYRQLKQqwemKTEEADLLQTKLQQSSYHKQQEELDA 747
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKA----KKEELERLKKRLTGLTPEKLEKELEE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 748 LKKTIEESEETLKNTK----EIQKKAEEK------------------YEVLENKMKNAEAERDRELKDAQKKLdfakTKA 805
Cdd:PRK03918 396 LEKAKEEIEEEISKITarigELKKEIKELkkaieelkkakgkcpvcgRELTEEHRKELLEEYTAELKRIEKEL----KEI 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 806 DASSKKMKEKQQEVEAITLELEELKREHTSYKQqLEAVNEAIKSYEVQ-IEAMAVEVAKNKESVNKAQ------------ 872
Cdd:PRK03918 472 EEKERKLRKELRELEKVLKKESELIKLKELAEQ-LKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKgeikslkkelek 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 873 -EEVTKQKEVIIAQDNVIKAKYAEV-----------------------AVHKEQNN--DSQLKIKELDHNISKHKREAED 926
Cdd:PRK03918 551 lEELKKKLAELEKKLDELEEELAELlkeleelgfesveeleerlkelePFYNEYLElkDAEKELEREEKELKKLEEELDK 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 927 AASKVSKMLKDYDWINAEKHLFGQPNSAYDF--KTNNPKEAGQRLQKLQEMKEKLGRNVNmRAMNVLTEAEERYNDLMKK 1004
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEELEKKYSEEEYeeLREEYLELSRELAGLRAELEELEKRRE-EIKKTLEKLKEELEEREKA 709
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 1005 KRIVENDKsKILATIEDLDQK----KNQALNIAWQKVNKDFGSIFSTLLPGANAmlappegQTVLDGLEFKVALGNTW-- 1078
Cdd:PRK03918 710 KKELEKLE-KALERVEELREKvkkyKALLKERALSKVGEIASEIFEELTEGKYS-------GVRVKAEENKVKLFVVYqg 781
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 1079 -KENLTELSGGQRSLVALS--LILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTH-SQFIVVSLKEGMFNNAN 1154
Cdd:PRK03918 782 kERPLTFLSGGERIALGLAfrLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERYLRKiPQVIIVSHDEELKDAAD 861
|
570
....*....|....
gi 1952970885 1155 VLFKTKFVDGVSTV 1168
Cdd:PRK03918 862 YVIRVSLEGGVSKV 875
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
662-981 |
1.02e-06 |
|
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: 53.30 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 662 TLSGGARS---QAASILTKFQELKN-VQDELRIKENELQSLDEELAGLKNTAekyrqlKQQWEMKTEEADLLQTKLQQ-- 735
Cdd:pfam12128 262 HLHFGYKSdetLIASRQEERQETSAeLNQLLRTLDDQWKEKRDELNGELSAA------DAAVAKDRSELEALEDQHGAfl 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 736 ----SSYHKQQEELDALKKTIEESEETLKNTKEIQKKAEEKYEVLENKMKnaeAERDRELKDAQKKLDfaktkadaSSKK 811
Cdd:pfam12128 336 dadiETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIK---EQNNRDIAGIKDKLA--------KIRE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 812 MKEKQQEVEAITLELEElkrehTSYKQQLEAVNEAIKSYEVQIEAMAVEVAKNKESVNKAQEEVTKQKeviIAQDNVIKA 891
Cdd:pfam12128 405 ARDRQLAVAEDDLQALE-----SELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLE---NFDERIERA 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 892 KYAEVAVHKEQNN--DSQLKIKELDHNISKHKREAEDAASKVSKMLKDydwinAEKHLFGQPNSAYDFKTNNPKEAGQRL 969
Cdd:pfam12128 477 REEQEAANAEVERlqSELRQARKRRDQASEALRQASRRLEERQSALDE-----LELQLFPQAGTLLHFLRKEAPDWEQSI 551
|
330
....*....|..
gi 1952970885 970 QKLQEmKEKLGR 981
Cdd:pfam12128 552 GKVIS-PELLHR 562
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
5-90 |
1.51e-06 |
|
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: 50.29 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 5 SIILEGFKSYAQrTEVNgFDPLFNAITGLNGSGKSNILDSICFLLG--ISNLSqvRASNLQDLVyKNGQagiTKASVSIT 82
Cdd:cd03277 5 RIKLENFVTYDE-TEFR-PGPSLNMIIGPNGSGKSSIVCAICLGLGgkPKLLG--RAKKVGEFV-KRGC---DEGTIEIE 76
|
....*....
gi 1952970885 83 -FDNSDKKQ 90
Cdd:cd03277 77 lYGNPGNIQ 85
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
8-89 |
1.85e-06 |
|
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: 49.96 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 8 LEGFKSYAQRTEVN----GFDPLFnAITGLNGSGKSNILDSICFLLgisnLSQVRASNLQDLVYKNGQAGITKASVSITF 83
Cdd:cd03279 8 LKNFGPFREEQVIDftglDNNGLF-LICGPTGAGKSTILDAITYAL----YGKTPRYGRQENLRSVFAPGEDTAEVSFTF 82
|
....*.
gi 1952970885 84 DNSDKK 89
Cdd:cd03279 83 QLGGKK 88
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
734-963 |
1.99e-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: 51.69 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 734 QQSSYHKQQEELDALKKTIEESEETLKNTKEIQKKAEEKYEVLENKMKNAEaerdRELKDAQKKLDFAKTKADASSKKMK 813
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA----RRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 814 EKQQEVEAITLELEELKRehTSYKQQL----------EAVNEAIKSYEVqIEAMAVEVAKNKESVNKAQEEVTKQKEVII 883
Cdd:COG4942 94 ELRAELEAQKEELAELLR--ALYRLGRqpplalllspEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 884 AQDNVIKAKYAEVAVHKE----QNNDSQLKIKELDHNISKHKREAEDAASKVSKMLKDYDWINAEKHLFGQPNSAYDFKT 959
Cdd:COG4942 171 AERAELEALLAELEEERAaleaLKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
....
gi 1952970885 960 NNPK 963
Cdd:COG4942 251 LKGK 254
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
679-864 |
2.18e-06 |
|
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: 52.16 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 679 QELKNVQDEL---RIKENELQSLDEELAGLKntaekyRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEeldalKKTIEES 755
Cdd:pfam09726 402 QDIKKLKAELqasRQTEQELRSQISSLTSLE------RSLKSELGQLRQENDLLQTKLHNAVSAKQKD-----KQTVQQL 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 756 EETLKNTKEIQKKAEEKY--EVLENKMKNAEAERDRELKDAQKkldfaKTKADASSKKMKEKQQEVEAITLEL---EELK 830
Cdd:pfam09726 471 EKRLKAEQEARASAEKQLaeEKKRKKEEEATAARAVALAAASR-----GECTESLKQRKRELESEIKKLTHDIklkEEQI 545
|
170 180 190
....*....|....*....|....*....|....
gi 1952970885 831 REHTSYKQQLEAVNEAIKSYEVQIEAMAVEVAKN 864
Cdd:pfam09726 546 RELEIKVQELRKYKESEKDTEVLMSALSAMQDKN 579
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
667-1025 |
3.24e-06 |
|
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: 51.36 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 667 ARSQAASIL-TKFQELKNVQDE----LRIKENELQSLDEELAGLkntAEKYRQLKQQWEMKTEEADLLQTKLQ--QSSYH 739
Cdd:pfam10174 335 AKEQRAAILqTEVDALRLRLEEkesfLNKKTKQLQDLTEEKSTL---AGEIRDLKDMLDVKERKINVLQKKIEnlQEQLR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 740 KQQEELDALKKTIEESEETLKNT-------KEIQKKAEEKYEVLENKMKNAEAERDRELKDAQKKLDFAKTKADASSKKM 812
Cdd:pfam10174 412 DKDKQLAGLKERVKSLQTDSSNTdtalttlEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPEL 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 813 KEKQQEveaitleLEELKREHTSYKQQLEAVNEAIKSYEVQIEAMAVEVAKNKESVNKAQE-EVTKQKEVIIAqdNVIKA 891
Cdd:pfam10174 492 TEKESS-------LIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNaEEAVRTNPEIN--DRIRL 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 892 KYAEVAVHKEQNNDSQLKIKELDHNISKHKREAEDAASKVSKMLKdydwiNAEKHLFGQPNSAYDFKTNNPKEagqRLQK 971
Cdd:pfam10174 563 LEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELES-----LTLRQMKEQNKKVANIKHGQQEM---KKKG 634
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1952970885 972 LQEMKEKLGRNVNMRAMNVLTEAEERYNDLMKKKRIVENDKSKILATIEDLDQK 1025
Cdd:pfam10174 635 AQLLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEK 688
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
679-923 |
5.17e-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: 50.88 E-value: 5.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 679 QELKNVQDEL----RIKENELQSLDEELAGLKNTAEKYrqLKQQWEMKTE--EADLLQTKLQQSS------YHKQQEELD 746
Cdd:pfam05483 432 EELKGKEQELifllQAREKEIHDLEIQLTAIKTSEEHY--LKEVEDLKTEleKEKLKNIELTAHCdkllleNKELTQEAS 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 747 ALKKTIEESEETLKNTKEIQKKAEEKYEVLENKMKNAEAERDRELKDAQKKLDFAKTKADASSKKM---------KEKQ- 816
Cdd:pfam05483 510 DMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENArsieyevlkKEKQm 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 817 -----------QEVEAITLELEELKREHTSYKQQLEAVNEAIKSYEVQIEAMAVEVAKNK----ESVNKAQEEVTKQKev 881
Cdd:pfam05483 590 kilenkcnnlkKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKqkfeEIIDNYQKEIEDKK-- 667
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1952970885 882 iIAQDNVI----KAKYA---EVAVHKEQNNDSQLKIKELDHNISKHKRE 923
Cdd:pfam05483 668 -ISEEKLLeeveKAKAIadeAVKLQKEIDKRCQHKIAEMVALMEKHKHQ 715
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
3-131 |
5.51e-06 |
|
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: 49.60 E-value: 5.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 3 VKSIILEGFKSYAqRTEVNgFDPLFNAITGLNGSGKSNILDSICFLlgiSNLSQVRASNLQDLVykngQAGITKASVSIT 82
Cdd:cd03242 1 LKSLELRNFRNYA-ELELE-FEPGVTVLVGENAQGKTNLLEAISLL---ATGKSHRTSRDKELI----RWGAEEAKISAV 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1952970885 83 FDNSdkkqsplGFEVHDEITVTRqvviGGRNKYLINGVNANnsRVQDLF 131
Cdd:cd03242 72 LERQ-------GGELALELTIRS----GGGRKARLNGIKVR--RLSDLL 107
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
685-927 |
5.53e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 5.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 685 QDELRIKENELQ-SLDEE---LAGLKNTAEKYR----QLKQQWEMKTEEADLLQTKLQ--QSSYHKQQEELDALKKTIEE 754
Cdd:PRK02224 316 REELEDRDEELRdRLEECrvaAQAHNEEAESLRedadDLEERAEELREEAAELESELEeaREAVEDRREEIEELEEEIEE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 755 SEETLKNTKEIQKKAEEKYEVLE---NKMKNAEAERDRELKDAQKKLDFAKTKADASskKMKEKQQEVEaitleleelKR 831
Cdd:PRK02224 396 LRERFGDAPVDLGNAEDFLEELReerDELREREAELEATLRTARERVEEAEALLEAG--KCPECGQPVE---------GS 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 832 EHTsykqqleavnEAIKSYEVQIEAMAVEVAKNKESVNKAQEEVTKQKEVIIAQDNV----IKAKYAE--VAVHKEQNND 905
Cdd:PRK02224 465 PHV----------ETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIerleERREDLEelIAERRETIEE 534
|
250 260
....*....|....*....|..
gi 1952970885 906 SQLKIKELDHNISKHKREAEDA 927
Cdd:PRK02224 535 KRERAEELRERAAELEAEAEEK 556
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
263-503 |
7.11e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 7.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 263 LQEKLSENDKKIKALSHEIEELEKgkdkeiggKLRSLEDALAEAQRvntksqsafdlkKKNLASEENKRTELEKNMIEDS 342
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRK--------ELEEAEAALEEFRQ------------KNGLVDLSEEAKLLLQQLSELE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 343 RTLAAKEKEVKKITDGLNALQEASNKDAEALAAAQQhfNAVSAGLSSNEDGAEATLAgqmmacknDISKAQTEAKQAQMK 422
Cdd:COG3206 226 SQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ--SPVIQQLRAQLAELEAELA--------ELSARYTPNHPDVIA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 423 LKHAQQELKTK-QAEVKKMDSGYRKDQEALEA----VKKLKEKLEAEMKKLNyeenkeeGLLEKRRQLSRDISRLKETYE 497
Cdd:COG3206 296 LRAQIAALRAQlQQEAQRILASLEAELEALQAreasLQAQLAQLEARLAELP-------ELEAELRRLEREVEVARELYE 368
|
....*.
gi 1952970885 498 ALLARF 503
Cdd:COG3206 369 SLLQRL 374
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-63 |
7.42e-06 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 49.23 E-value: 7.42e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952970885 1 MHVKSIILEGFKSYAQRtEVN-GFDPLFNAITGLNGSGKSNILDSICFLLG--ISNLSQVRASNLQ 63
Cdd:COG3950 1 MRIKSLTIENFRGFEDL-EIDfDNPPRLTVLVGENGSGKTTLLEAIALALSglLSRLDDVKFRKLL 65
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
632-1026 |
8.25e-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: 50.11 E-value: 8.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 632 NMDNAKKVAFDKRIMTRTVTLGGEVFDPHGTLSGGARSQAASILTKFQELKNVQDELrikenelqsLDEELAGLKNTAEK 711
Cdd:pfam05483 308 SMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEEL---------LRTEQQRLEKNEDQ 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 712 YRQLKQQWEMKTEEADLLqTKLQQSsyhkQQEELDALKKTIEESEETLKNTKEIQKKAEEkYEVLENKMKNAEAERDREL 791
Cdd:pfam05483 379 LKIITMELQKKSSELEEM-TKFKNN----KEVELEELKKILAEDEKLLDEKKQFEKIAEE-LKGKEQELIFLLQAREKEI 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 792 KDAQKKLDFAKTKADASSKKMKEKQQEVE--------------AITLELEELKREHTSYKQQLEAVNEAIKSYEVQIEAM 857
Cdd:pfam05483 453 HDLEIQLTAIKTSEEHYLKEVEDLKTELEkeklknieltahcdKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERM 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 858 AVEVAKNKESVNKAQEEVTKQKEVIIAQDNVIKAKYAEVAVHKEQNNDSQLK----IKELDHNISKHKREAEDAASKVSK 933
Cdd:pfam05483 533 LKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKkekqMKILENKCNNLKKQIENKNKNIEE 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 934 MLKDYDWINAEKHLFGQPNSAYDFKTNNPK-EAGQRLQKLQEMKEKLGRNVNMRAMnvlteAEERYNDLMKKKRIVENDK 1012
Cdd:pfam05483 613 LHQENKALKKKGSAENKQLNAYEIKVNKLElELASAKQKFEEIIDNYQKEIEDKKI-----SEEKLLEEVEKAKAIADEA 687
|
410
....*....|....
gi 1952970885 1013 SKILATIEDLDQKK 1026
Cdd:pfam05483 688 VKLQKEIDKRCQHK 701
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
710-870 |
9.30e-06 |
|
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: 50.03 E-value: 9.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 710 EKYRQLKQQWEMKTeeadlLQTKLQ--QSSYHKQQEELDALKKTIEESEETLKNTKEIQKKAEEKYEVLENKMKnaeaer 787
Cdd:pfam05667 326 EEELQQQREEELEE-----LQEQLEdlESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLD------ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 788 drELKDAQKKLDFAKTKADASSKKMKEKQQEVEA----ITLELEELKREHTSYKQQLEAVNEAIKSYEVQIEAMAVEvAK 863
Cdd:pfam05667 395 --LLPDAEENIAKLQALVDASAQRLVELAGQWEKhrvpLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEE-AK 471
|
....*..
gi 1952970885 864 NKESVNK 870
Cdd:pfam05667 472 QKEELYK 478
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
681-1033 |
9.85e-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: 50.12 E-value: 9.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 681 LKNVQDELRIKENELQSLDEELAGLKNTAEKyrQLKQQWEM------KTEEADLLQTKLQQSS--YHKQQEELDALKKTI 752
Cdd:pfam15921 414 IDHLRRELDDRNMEVQRLEALLKAMKSECQG--QMERQMAAiqgkneSLEKVSSLTAQLESTKemLRKVVEELTAKKMTL 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 753 EESEETLKntkEIQKKAEEKYEVLEnkMKNAEAERDRELKDAQ-KKLDFAKTKADasskKMKEKQQEVEAITLELEELKR 831
Cdd:pfam15921 492 ESSERTVS---DLTASLQEKERAIE--ATNAEITKLRSRVDLKlQELQHLKNEGD----HLRNVQTECEALKLQMAEKDK 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 832 EHTSYKQQLEAVNEAIKSYEVQIEAMAVEVAKNKESVNKAQEEVtkqKEVIIAQDnvikakyaevavhkeqNNDSqlKIK 911
Cdd:pfam15921 563 VIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLEL---QEFKILKD----------------KKDA--KIR 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 912 ELDHNISKHKREAEDAASKVSKMLKDYDWINAEKhlfgqpnsayDFKTNNPKEAGQRLQKLQEMKEKLGRNVNmramNVL 991
Cdd:pfam15921 622 ELEARVSDLELEKVKLVNAGSERLRAVKDIKQER----------DQLLNEVKTSRNELNSLSEDYEVLKRNFR----NKS 687
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1952970885 992 TEAEERYNDLMKKKRIVENDKSKILATIEDLDQKKNQALNIA 1033
Cdd:pfam15921 688 EEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVA 729
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1053-1133 |
1.07e-05 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 47.85 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 1053 NAMLAPPEGQTVLDGLEFKVALGNTWKENLTELSGGQRSLVALSLILSMllfKPaPIYILDEVDAALDLSHTQNIGQMLR 1132
Cdd:cd03225 103 NLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAM---DP-DILLLDEPTAGLDPAGRRELLELLK 178
|
.
gi 1952970885 1133 T 1133
Cdd:cd03225 179 K 179
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
678-1029 |
1.24e-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: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 678 FQELKNVQDELRIKENELQSLDEELAGLKNTAEKYRQLKQQWEmkteeadllqtklqqsSYHKQQEELDALKKTIEESEE 757
Cdd:pfam05622 96 VLELQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVE----------------TYKKKLEDLGDLRRQVKLLEE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 758 tlKNTKEIQKKAEekyevLENKMKNAEAERD------RELKDAQKKLDFAKTKADA---SSKKMKEK----QQEVEAITL 824
Cdd:pfam05622 160 --RNAEYMQRTLQ-----LEEELKKANALRGqletykRQVQELHGKLSEESKKADKlefEYKKLEEKlealQKEKERLII 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 825 E-------LEELKREHTSYKQQLEAVNEAIKSYE----VQIEAMAVEVaknKESVNKAQEEvtkQKEVIIAQDNVIKAKY 893
Cdd:pfam05622 233 ErdtlretNEELRCAQLQQAELSQADALLSPSSDpgdnLAAEIMPAEI---REKLIRLQHE---NKMLRLGQEGSYRERL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 894 AEVAVH-----------KEQNNDSQLKIKELDHNISKHKRE-------AEDAASKVSKMLKDYDWINaEKHLFGQPNSAY 955
Cdd:pfam05622 307 TELQQLledanrrknelETQNRLANQRILELQQQVEELQKAlqeqgskAEDSSLLKQKLEEHLEKLH-EAQSELQKKKEQ 385
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952970885 956 dFKTNNPKEAGQRLQKLQEMKEKL-GRNVNMRAMnvlteaEERYndlmkkKRIVENDKSkilaTIEDLDQKKNQA 1029
Cdd:pfam05622 386 -IEELEPKQDSNLAQKIDELQEALrKKDEDMKAM------EERY------KKYVEKAKS----VIKTLDPKQNPA 443
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
679-821 |
1.42e-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: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 679 QELKNVQDELRIKENELQSLDEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSS--------YHKQQEELDALKK 750
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnnkeYEALQKEIESLKR 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952970885 751 TIEESEETLKNTKEIQKKAEEKYEVLENKMKNAEAerdrELKDAQKKLDFAKTKADASSKKMKEKQQEVEA 821
Cdd:COG1579 104 RISDLEDEILELMERIEELEEELAELEAELAELEA----ELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
663-897 |
1.66e-05 |
|
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: 48.61 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 663 LSGGARSQAASILTKFQELKNVQDELRIKENELQSLDEELAGLkntAEKYRQLKQQWEMKTEEADLLQTKLQQssyhkQQ 742
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKAL---LKQLAALERRIAALARRIRALEQELAA-----LE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 743 EELDALKKTIEESEETLKNTKEIQKKAEEKYEVLENKMKNAEAERDRELKDAQKKLDFAKTKADASSKKMKEKQQEVEAI 822
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952970885 823 TLELEELKREHTSYKQQLEAVNEAIKSYEVQIEAMAVEVAKNKESVNKAQEEVTKQKEVIIAQDNVIKAKYAEVA 897
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
324-512 |
2.29e-05 |
|
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: 48.22 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 324 LASEENKRTELEKNMIEDSRTLAAKEKEVKKITDGLNALQEASNKDAEALAAAQQHFNAVSAGLSSNE---DGAEATLAG 400
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEkeiAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 401 QMMACKNDISKAQTEAKQAQMKLKHAQQELKTKQAEVKKMDSGYRKDQEALEAVKKLKEKLEAEMKKLNYEENKEEGLLE 480
Cdd:COG4942 102 QKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190
....*....|....*....|....*....|..
gi 1952970885 481 KRRQLSRDISRLKETYEALLARFPNIQFAYRD 512
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAA 213
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
668-882 |
2.31e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.60 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 668 RSQAASILTKFQELKNVQDELRikeNELQSLDEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEelda 747
Cdd:COG1340 63 REKRDELNEKVKELKEERDELN---EKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEE---- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 748 lKKTIEESEEtLKNTKEIQKKAEEKYEVLENKMKNAEAERDrELKDAQKKLDFAKTKADASSKKMKEKQQEVEAITLELE 827
Cdd:COG1340 136 -KELVEKIKE-LEKELEKAKKALEKNEKLKELRAELKELRK-EAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEAD 212
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 828 ELKREHTSYKQQLEAVNEAIKSY-----EVQIEAMAVEVAKNKESVNKAQEEVTKQKEVI 882
Cdd:COG1340 213 ELHKEIVEAQEKADELHEEIIELqkelrELRKELKKLRKKQRALKREKEKEELEEKAEEI 272
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1081-1143 |
2.53e-05 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 46.27 E-value: 2.53e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952970885 1081 NLTELSGGQRSLValslILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVV 1143
Cdd:cd03214 94 PFNELSGGERQRV----LLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVV 152
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
667-880 |
3.38e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.21 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 667 ARSQAASILTKFQELKNVQDELRIKENELQSLDEELAGLKN----TAEKYRQLKQQWEMKTEEADLLQTKlqQSSYHKQQ 742
Cdd:COG1340 38 LKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEerdeLNEKLNELREELDELRKELAELNKA--GGSIDKLR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 743 EELDALKKTIEESEETLKNTKEIQKKAEEKYEVLENKMKnaEAERDRELKDAQKKLDFAKTKADASSKKMKEKQQEVEAI 822
Cdd:COG1340 116 KEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKK--ALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQEL 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1952970885 823 TLELEELKREHTSYKQQLEAVNEAIKSYEVQIEAMAVEVAKNKESVNKAQEEVTKQKE 880
Cdd:COG1340 194 HEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRK 251
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
740-841 |
3.58e-05 |
|
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: 44.48 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 740 KQQEELDALKKTIEESEETLKNTKEIQKKAEEKYEVLENKMKNAEAERDRELKDAQKKLDFAKTKADASSKKMKEKQQEV 819
Cdd:pfam13863 3 EKKREMFLVQLALDAKREEIERLEELLKQREEELEKKEQELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEKEKEI 82
|
90 100
....*....|....*....|..
gi 1952970885 820 EAITLELEELKREHTSYKQQLE 841
Cdd:pfam13863 83 KKLTAQIEELKSEISKLEEKLE 104
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
23-376 |
3.84e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 47.76 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 23 FDPLFNAITGLNGSGKSNILDSICFLLGisnlsqVRASnlQDLVyKNGQAgitKASVSITFDNSDKKQ-----SPLGFEV 97
Cdd:COG0497 20 FGPGLTVLTGETGAGKSILLDALGLLLG------GRAD--ASLV-RHGAD---KAEVEAVFDLSDDPPlaawlEENGLDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 98 HD-EITVTRQVVIGGRNKYLINGVNANNSRVQDLFcsvglnvnnpHFLI-MQG-----RItkvlnMKPPEILSMIEEAAG 170
Cdd:COG0497 88 DDgELILRREISADGRSRAFINGRPVTLSQLRELG----------ELLVdIHGqhehqSL-----LDPDAQRELLDAFAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 171 TR--MYEYKkiAAQKTIEKKEAKLKEIKTILEEeitptiqklKEERSSYLEYQ---------------KIMREIEHLSR- 232
Cdd:COG0497 153 LEelLEEYR--EAYRAWRALKKELEELRADEAE---------RARELDLLRFQleeleaaalqpgeeeELEEERRRLSNa 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 233 ------LYIAYQfLLAEDtkERSAEE-LKEMQDKVvklqEKLSENDKKIKALSHEIE----ELEkgkdkEIGGKLRSLED 301
Cdd:COG0497 222 eklreaLQEALE-ALSGG--EGGALDlLGQALRAL----ERLAEYDPSLAELAERLEsaliELE-----EAASELRRYLD 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 302 AL----AEAQRVNTKSQSAFDLKKKN-------LASEENKRTELEKnmIEDS-RTLAAKEKEVKKITDGLN----ALQEA 365
Cdd:COG0497 290 SLefdpERLEEVEERLALLRRLARKYgvtveelLAYAEELRAELAE--LENSdERLEELEAELAEAEAELLeaaeKLSAA 367
|
410
....*....|.
gi 1952970885 366 SNKDAEALAAA 376
Cdd:COG0497 368 RKKAAKKLEKA 378
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
422-879 |
4.33e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 422 KLKHAQQELKTKQAEVKKmdsgYRKDQEALEAVKKLKEKLEAEMKKLNYEENKEEGLLE------KRRQLSRDISRLKET 495
Cdd:COG4717 72 ELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELREELEKLEKLLQllplyqELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 496 YEALLARFPNIQFAYRDPEKnwnrncvkglVASLISVKDTSTTTALELVAGERLYNVVVDTEVTGKKLLEKGELKRRyti 575
Cdd:COG4717 148 LEELEERLEELRELEEELEE----------LEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE--- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 576 ipLNKISARCiapETLRvaQNLVGPNNVHVALSLVEykpELQKAMEFVFGTTFVCnnmdnaKKVAFDKRIMTRTVTLGGE 655
Cdd:COG4717 215 --LEEAQEEL---EELE--EELEQLENELEAAALEE---RLKEARLLLLIAAALL------ALLGLGGSLLSLILTIAGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 656 VFDPHGTLSGGARSQAASILTKFQELKNVQDELRIKENELQSLDEELAGL--------KNTAEKYRQLKQQWEMKTEEAD 727
Cdd:COG4717 279 LFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALglppdlspEELLELLDRIEELQELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 728 lLQTKLQQSSYHKQQEELdaLKKTIEESEETLK---NTKEIQKKAEEKYEVLENKMKNAEAERDRELKDAQK-----KLD 799
Cdd:COG4717 359 -LEEELQLEELEQEIAAL--LAEAGVEDEEELRaalEQAEEYQELKEELEELEEQLEELLGELEELLEALDEeeleeELE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 800 FAKTKADASSKKMKEKQQEVEAITLELEELKREHTsykqqLEAVNEAIKSYEVQIEAMAVEVAKNK---ESVNKAQEEVT 876
Cdd:COG4717 436 ELEEELEELEEELEELREELAELEAELEQLEEDGE-----LAELLQELEELKAELRELAEEWAALKlalELLEEAREEYR 510
|
...
gi 1952970885 877 KQK 879
Cdd:COG4717 511 EER 513
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
735-1028 |
5.29e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 735 QSSYHKQQEELDALKKTIEESEETLKNTKEIQKKAEEKYEVLENKMKNAEAERDrELKDAQKKLDfaktkadasskKMKE 814
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISS-ELPELREELE-----------KLEK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 815 KQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYEVQIEAMAVEVAKNKESVNKAQEEVTKQKEVIIAQDNVIKAKYA 894
Cdd:PRK03918 229 EVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 895 EVAVHKEQNNDSQL--KIKELDHNISKHKREAEDAASKVSKMLKDYDWINAEKHLFgqpnsaydfktnnpKEAGQRLQKL 972
Cdd:PRK03918 309 LREIEKRLSRLEEEinGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELY--------------EEAKAKKEEL 374
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1952970885 973 QEMKEKLGrnvnmraMNVLTEAEERYNDLMKKKRIVENDKSKILATIEDLDQKKNQ 1028
Cdd:PRK03918 375 ERLKKRLT-------GLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
693-879 |
5.35e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.51 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 693 NELQSLDEELAGLkntAEKYRQLKQQW---EMKTEEADLLQTKLQQsSYHKQQEELDALKKTIEES-EETLKNTKEiqKK 768
Cdd:PRK00409 513 EDKEKLNELIASL---EELERELEQKAeeaEALLKEAEKLKEELEE-KKEKLQEEEDKLLEEAEKEaQQAIKEAKK--EA 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 769 AEEKYEVLENKMKNAEAERDRELKDAQKKLDFAKTKADASSKKMKEKQQEVEaitlELEELKREhtSYKQQ---LEAVNE 845
Cdd:PRK00409 587 DEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK----VGDEVKYL--SLGQKgevLSIPDD 660
|
170 180 190
....*....|....*....|....*....|....*
gi 1952970885 846 aiKSYEVQIEAMAVEV-AKNKESVNKAQEEVTKQK 879
Cdd:PRK00409 661 --KEAIVQAGIMKMKVpLSDLEKIQKPKKKKKKKP 693
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
181-337 |
5.35e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 181 AQKTIEKKEAKLKEIKT-----ILEEEITPTIQKLKEERSSYLEYQKIMREIEH--------LSRLYIAYQFLLAEDTKE 247
Cdd:COG3206 187 LRKELEEAEAALEEFRQknglvDLSEEAKLLLQQLSELESQLAEARAELAEAEArlaalraqLGSGPDALPELLQSPVIQ 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 248 RSAEELKEMQDKVVKLQEKLSENDKKIKALSHEIEELEKGKDKEIGGKLRSLEDALAEAQ-RVNTKSQSAFDLKKK--NL 324
Cdd:COG3206 267 QLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQaREASLQAQLAQLEARlaEL 346
|
170
....*....|...
gi 1952970885 325 ASEENKRTELEKN 337
Cdd:COG3206 347 PELEAELRRLERE 359
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
689-893 |
5.57e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.32 E-value: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 689 RIKEN--ELQSLDEELAGLK---NTAEKY--RQLKQQWEMKTEEADLLQTKLQQSSYHKQQ-----EELDALKKTIEESE 756
Cdd:PHA02562 175 KIRELnqQIQTLDMKIDHIQqqiKTYNKNieEQRKKNGENIARKQNKYDELVEEAKTIKAEieeltDELLNLVMDIEDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 757 ETLK--NTKEIQKKAE-----------EKYEVLENKMKNAEAERDR------ELKDAQKKLDFAKTKADasskKMKEKQQ 817
Cdd:PHA02562 255 AALNklNTAAAKIKSKieqfqkvikmyEKGGVCPTCTQQISEGPDRitkikdKLKELQHSLEKLDTAID----ELEEIMD 330
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952970885 818 EVEAITLELEELKREHTSYKQQLEAVNEAIKSYEVQIEAMAVEVAKNKESVNKAQEEVtkqKEVIIAQDNVIKAKY 893
Cdd:PHA02562 331 EFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDEL---DKIVKTKSELVKEKY 403
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
161-503 |
5.79e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 5.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 161 ILSMIEEAAGTRMYEY------KKIAAQKTIEKKEAKLKEIKTIlEEEITPTIQKLKEERSSYLEYQKIMREIEH-LSRL 233
Cdd:COG4717 43 IRAMLLERLEKEADELfkpqgrKPELNLKELKELEEELKEAEEK-EEEYAELQEELEELEEELEELEAELEELREeLEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 234 YIAYQFLLAEDTKERSAEELKEMQDKVVKLQEK---LSENDKKIKALSHEIEELEKGKDKEIGGKLRSLEDALAEAQRVN 310
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEELEERleeLRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 311 TKSQSAFDLKKKNLASEENKRTELEKNM--IEDSRTLAAKEKEVKKITDGLNALqeasnkdaeALAAAQQHFNAVSAGLS 388
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELeqLENELEAAALEERLKEARLLLLIA---------AALLALLGLGGSLLSLI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 389 SNEDGAEATLAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKTKQAEVKK-----MDSGYRKDQEALEAVKKLKEKLEA 463
Cdd:COG4717 273 LTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEEllaalGLPPDLSPEELLELLDRIEELQEL 352
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1952970885 464 EMKKLNYEENKEEGLLEKRRQ--LSRDISRLKETYEALLARF 503
Cdd:COG4717 353 LREAEELEEELQLEELEQEIAalLAEAGVEDEEELRAALEQA 394
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
221-903 |
5.81e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 5.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 221 QKIMREIEHLSRLYIAYQFLLA-EDTKERSAEELKEMQDKVVKLQEKLSENDKKIKALSHEIEELEKgKDKEIGGKLRSL 299
Cdd:PRK03918 148 EKVVRQILGLDDYENAYKNLGEvIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISS-ELPELREELEKL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 300 EDALAEAQrvntKSQSAFDLKKKNLASEENKRTELEKNMIEDSRTLAAKEKEVKKITDGLNALQEASNKDAEALaaaqqh 379
Cdd:PRK03918 227 EKEVKELE----ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYI------ 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 380 fnavsaglssnedgaeatlagqmmackndiskaqteakqaqmKLKHAQQELKTKQAEVKKMdsgyrkdqeaLEAVKKLKE 459
Cdd:PRK03918 297 ------------------------------------------KLSEFYEEYLDELREIEKR----------LSRLEEEIN 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 460 KLEAEMKKLNYEENKEEGLLEKRRQLSRDISRLKE---TYEALLARFPNIQfAYRDPEKNWNRNCVKGLVASLISVKDTS 536
Cdd:PRK03918 325 GIEERIKELEEKEERLEELKKKLKELEKRLEELEErheLYEEAKAKKEELE-RLKKRLTGLTPEKLEKELEELEKAKEEI 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 537 TTTALELV---------------AGERLYNVVVDTEVTGKKLLE--KGELKRRYTiIPLNKISA---------RCIAPET 590
Cdd:PRK03918 404 EEEISKITarigelkkeikelkkAIEELKKAKGKCPVCGRELTEehRKELLEEYT-AELKRIEKelkeieekeRKLRKEL 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 591 LRVAQNLVGPNNVHVALSLVEYKPELQKAMEFVfgttfvcnnmdNAKKVAFDKrimtrtvtlggEVFDPHGTLSGGARSQ 670
Cdd:PRK03918 483 RELEKVLKKESELIKLKELAEQLKELEEKLKKY-----------NLEELEKKA-----------EEYEKLKEKLIKLKGE 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 671 AASILTKFQELKNVQDELRIKENELQSLDEELAGLkntaekyrqLKQQWEMKTEEADLLQTKLQQ------------SSY 738
Cdd:PRK03918 541 IKSLKKELEKLEELKKKLAELEKKLDELEEELAEL---------LKELEELGFESVEELEERLKElepfyneylelkDAE 611
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 739 HKQQEELDALKKTIEESEETLKNTKEIQKKAEEKYEVLENKMKNAEAERDRELKDAQKKLDFAKTKADASSKKMKEKQQE 818
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREE 691
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 819 VEAITLELEELKREHTSYKQQLEAVNEAIKSYEVQIEamavevaKNKESVNKAQEEVTKQKEVIIAQ--DNVIKAKYAEV 896
Cdd:PRK03918 692 IKKTLEKLKEELEEREKAKKELEKLEKALERVEELRE-------KVKKYKALLKERALSKVGEIASEifEELTEGKYSGV 764
|
....*..
gi 1952970885 897 AVHKEQN 903
Cdd:PRK03918 765 RVKAEEN 771
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
698-1028 |
6.08e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.59 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 698 LDE--ELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSsyhkqQEELDALKKTIEESEETLKNTKEIQKKAEEKYEV 775
Cdd:PRK01156 155 LDEilEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSS-----NLELENIKKQIADDEKSHSITLKEIERLSIEYNN 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 776 LENKMKNAEAERDR--ELKDAQKKLDFAKTKADASSKKMKEKQQEVEAITLELEELK-----------REHTSYKQQLEA 842
Cdd:PRK01156 230 AMDDYNNLKSALNElsSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIIndpvyknrnyiNDYFKYKNDIEN 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 843 VNEAIKSYEVQIEAMAVEVAKNKESVNKAQEEVTKQKEViiaqdNVIKAKYAEVAVHKEQNNDSQLKIKELDHNISKHKR 922
Cdd:PRK01156 310 KKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRY-----DDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSK 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 923 EAEDAASKVSKMLKdYDWINAE--KHLFGQPNSAYDFKTNNPKEAGQRLQKLQEMKEKLGRNVNM-RAMNV-----LTEA 994
Cdd:PRK01156 385 NIERMSAFISEILK-IQEIDPDaiKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMlNGQSVcpvcgTTLG 463
|
330 340 350
....*....|....*....|....*....|....*...
gi 1952970885 995 EERYNDLMK----KKRIVENDKSKILATIEDLDQKKNQ 1028
Cdd:PRK01156 464 EEKSNHIINhyneKKSRLEEKIREIEIEVKDIDEKIVD 501
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
4-100 |
6.36e-05 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 46.58 E-value: 6.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 4 KSIILEGFKSYAQRTEVN----GFDPL-FNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYKNGQAGITKAS 78
Cdd:COG1106 3 ISFSIENFRSFKDELTLSmvasGLRLLrVNLIYGANASGKSNLLEALYFLRNLVLNSSQPGDKLVEPFLLDSESKNEPSE 82
|
90 100
....*....|....*....|..
gi 1952970885 79 VSITFdNSDKKQSPLGFEVHDE 100
Cdd:COG1106 83 FEILF-LLDGVRYEYGFELDKE 103
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
242-467 |
8.86e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 8.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 242 AEDTKERSAEELKEMQDKVVKLQEKLSENDKKIKALSHEIEELEKgKDKEIGGKLRSLEDALAEAQRVNTKSQSAfdLKK 321
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQA-ELEALQAEIDKLQAEIAEAEAEIEERREE--LGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 322 KNLASEENKRTELEKNMIEDSRTLAAkekevkkITDGLNALQEASNKDAEALAAAQQhfnavsaglssnedgAEATLAGQ 401
Cdd:COG3883 91 RARALYRSGGSVSYLDVLLGSESFSD-------FLDRLSALSKIADADADLLEELKA---------------DKAELEAK 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952970885 402 mmacKNDISKAQTEAKQAQMKLKHAQQELKTKQAEVKKMDSGYRKDQEALEAVKKLKEKLEAEMKK 467
Cdd:COG3883 149 ----KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
785-930 |
1.00e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 785 AERDRELKDAQKKLDFAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYEVQIEamavEVAKN 864
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG----NVRNN 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952970885 865 KEsVNKAQEEVTKQKEVIIAQDNVIKAKYAEVAVHKEQNNDSQLKIKELDHNISKHKREAEDAASK 930
Cdd:COG1579 89 KE-YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
692-913 |
1.07e-04 |
|
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: 46.87 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 692 ENELQSLDEELAglkntAEKYRQ--LKQQWEMKTEEADLLQTKLQQSSYH--------KQQEELDALKKTIEESEETLKN 761
Cdd:COG3096 291 RRELFGARRQLA-----EEQYRLveMARELEELSARESDLEQDYQAASDHlnlvqtalRQQEKIERYQEDLEELTERLEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 762 TKEIQKKAEEKYEVLENKMKNAEAERDR---ELKDAQKKLDFAKTKADA---SSKKMKEKQQEVEAITLELEELKREHTS 835
Cdd:COG3096 366 QEEVVEEAAEQLAEAEARLEAAEEEVDSlksQLADYQQALDVQQTRAIQyqqAVQALEKARALCGLPDLTPENAEDYLAA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 836 YKQQLEAVNEAIKSYEVQI---EAMAVEVAKNKESVNKAQEEVTKQ------KEVI---------IAQDNVIKAKYAEVa 897
Cdd:COG3096 446 FRAKEQQATEEVLELEQKLsvaDAARRQFEKAYELVCKIAGEVERSqawqtaRELLrryrsqqalAQRLQQLRAQLAEL- 524
|
250
....*....|....*.
gi 1952970885 898 vhkEQNNDSQLKIKEL 913
Cdd:COG3096 525 ---EQRLRQQQNAERL 537
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
687-851 |
1.13e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 687 ELRIKENELQSLDEELAGLKNT--AEKYR--QLKQQWEMKTEEADLLQTKLQQSSYH--------KQQEELDALKKTIEE 754
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQlaAEQYRlvEMARELAELNEAESDLEQDYQAASDHlnlvqtalRQQEKIERYQADLEE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 755 SEETLKNTKEIQKKAEEKYEVLENKMKNAEAERDR---ELKDAQKKLDFAKTKADA---SSKKMKEKQQEVEAITLELEE 828
Cdd:PRK04863 360 LEERLEEQNEVVEEADEQQEENEARAEAAEEEVDElksQLADYQQALDVQQTRAIQyqqAVQALERAKQLCGLPDLTADN 439
|
170 180
....*....|....*....|...
gi 1952970885 829 LKREHTSYKQQLEAVNEAIKSYE 851
Cdd:PRK04863 440 AEDWLEEFQAKEQEATEELLSLE 462
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
180-1026 |
1.37e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.19 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 180 AAQKTIEKKEAKLKEIKTILE--EEITPTIQKLKEERSSYLEYQKIMREIEHLSRLYIAYQFLLAE----DTKERSAEEL 253
Cdd:TIGR00606 235 SSREIVKSYENELDPLKNRLKeiEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDeqlnDLYHNHQRTV 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 254 KEMQDKVVKLQEKLSENDKKIKALSHEIEELE-----------------KGKDKEI-GGKLRSLEDALAEAQRVNTKSQS 315
Cdd:TIGR00606 315 REKERELVDCQRELEKLNKERRLLNQEKTELLveqgrlqlqadrhqehiRARDSLIqSLATRLELDGFERGPFSERQIKN 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 316 AFDLKKKNlasEENKRTELEKNMIEDSRTLAAKEKEVKKITDGLNALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAE 395
Cdd:TIGR00606 395 FHTLVIER---QEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 396 atlagqmmacknDISKAQTEAKQAQMKLKHAQqelKTKQAEVKKMDSGYRKDQEAleAVKKLKEKLEAEMKKLNYEENKE 475
Cdd:TIGR00606 472 ------------RILELDQELRKAERELSKAE---KNSLTETLKKEVKSLQNEKA--DLDRKLRKLDQEMEQLNHHTTTR 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 476 EGLL-------EKRRQLSRDISRLKETYEALLARFPNIQ-----FAYRDPEKNWNRNCVKGLVASLISV--------KDT 535
Cdd:TIGR00606 535 TQMEmltkdkmDKDEQIRKIKSRHSDELTSLLGYFPNKKqledwLHSKSKEINQTRDRLAKLNKELASLeqnknhinNEL 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 536 STTTALELVAGERLYNVV--VDTEVTGKKLLEKGElKRRYTIIPLNKISARCIAPETLRVAQNlvgPNNVHVALSLVEYK 613
Cdd:TIGR00606 615 ESKEEQLSSYEDKLFDVCgsQDEESDLERLKEEIE-KSSKQRAMLAGATAVYSQFITQLTDEN---QSCCPVCQRVFQTE 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 614 PELQKamefvfgttfVCNNMDNAKKVAFDKRIMTRTVTLGGEvfDPHGTLSGGARSQAASILTKFQELKNVQdelrikeN 693
Cdd:TIGR00606 691 AELQE----------FISDLQSKLRLAPDKLKSTESELKKKE--KRRDEMLGLAPGRQSIIDLKEKEIPELR-------N 751
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 694 ELQSLDEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLqqSSYHKQQEELDALKKTIEE------SEETLKNTKEIQK 767
Cdd:TIGR00606 752 KLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDV--TIMERFQMELKDVERKIAQqaaklqGSDLDRTVQQVNQ 829
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 768 KAEEKYEVLENKMKNAE------AERDRELKDAQKKLDFAKTKADASSKKMKEKQQ---EVEAITLELEELKREHTSYKQ 838
Cdd:TIGR00606 830 EKQEKQHELDTVVSKIElnrkliQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQfeeQLVELSTEVQSLIREIKDAKE 909
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 839 QLEAVNEAIKSYEVQIEAMaveVAKNKESVNKAQEEVTKQKEVIIAQDNVIKAKYAEVAVHKE-QNNDSQLKIKELDHNI 917
Cdd:TIGR00606 910 QDSPLETFLEKDQQEKEEL---ISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDdYLKQKETELNTVNAQL 986
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 918 SKHKREAEDAASKVSKMLKDYDWINAEKHLFgqpnsaydfktNNPKEAGQRLQKLQEMKEKLGRNVNMRAMNVLTEAEER 997
Cdd:TIGR00606 987 EECEKHQEKINEDMRLMRQDIDTQKIQERWL-----------QDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQE 1055
|
890 900
....*....|....*....|....*....
gi 1952970885 998 YNDLMKKKRIVENDKSKILATIEDLDQKK 1026
Cdd:TIGR00606 1056 HQKLEENIDLIKRNHVLALGRQKGYEKEI 1084
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
152-485 |
1.49e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 152 KVLNMKPPEILSMIEEAAGTRMY----EYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQKIMREI 227
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEEARIEEVMklyeEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 228 EHLSRLYIAYQFLLAEDTKERSAEELKEMQD----------------KVVKLQEKLSENDKKIKALSHEIEE----LEKG 287
Cdd:PTZ00121 1656 EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDekkaaealkkeaeeakKAEELKKKEAEEKKKAEELKKAEEEnkikAEEA 1735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 288 KDKEIGGKLRSLEDALAEAQRVNTKSQSAFDLKKKNLASEENKRTELEKNMIEDSRTLAAKEKEVKKITDGLNALQEASN 367
Cdd:PTZ00121 1736 KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGK 1815
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 368 KDAEALAAAQQHFNAVS--AGLSSNEDGAEATLAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKTKQAEVKKMDSGYR 445
Cdd:PTZ00121 1816 EGNLVINDSKEMEDSAIkeVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDK 1895
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1952970885 446 KDQEALEAVKKLKEK-LEAEMKKLNYEENKEEGLLEKRRQL 485
Cdd:PTZ00121 1896 DDIEREIPNNNMAGKnNDIIDDKLDKDEYIKRDAEETREEI 1936
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
679-879 |
1.53e-04 |
|
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: 46.26 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 679 QELKNVQDELRIKENELQSLDEElaglkntaekYRQLKQQWEMKTEEADLLQTKLQQSsyhkqqeeldaLKKTIEESEET 758
Cdd:pfam15921 653 QERDQLLNEVKTSRNELNSLSED----------YEVLKRNFRNKSEEMETTTNKLKMQ-----------LKSAQSELEQT 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 759 LKNTKEIQKKAEEKYEVLENKMKNAEAERDrELKDAQKKLDF---AKTKADASSKKMKEKQ----QEVEAITLELEELKR 831
Cdd:pfam15921 712 RNTLKSMEGSDGHAMKVAMGMQKQITAKRG-QIDALQSKIQFleeAMTNANKEKHFLKEEKnklsQELSTVATEKNKMAG 790
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1952970885 832 EHTSYKQQLEAVNEAIKSYEVQIEAMAVEVAKNKESVNKAQEEVTKQK 879
Cdd:pfam15921 791 ELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLK 838
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
688-1022 |
1.81e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.84 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 688 LRIKENELQSLDEELAGLKNTAEKYRQLKQQWEMKTEeadllqtklqqssyhkqqEELDALKKTIEESEETLKNTKEIQK 767
Cdd:COG5022 805 LLGSRKEYRSYLACIIKLQKTIKREKKLRETEEVEFS------------------LKAEVLIQKFGRSLKAKKRFSLLKK 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 768 kaEEKYEVLENKMKNAEaerdRELKDaqkkLDFAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKqqleavNEAI 847
Cdd:COG5022 867 --ETIYLQSAQRVELAE----RQLQE----LKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFK------TELI 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 848 KSYEVQIEAMAVEVAKNKE-----SVNKAQEEVTKQKEVIIAQDNVIKaKYAEvavHKEQNNDSQLKIKELDHNISKHKR 922
Cdd:COG5022 931 ARLKKLLNNIDLEEGPSIEyvklpELNKLHEVESKLKETSEEYEDLLK-KSTI---LVREGNKANSELKNFKKELAELSK 1006
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 923 EaEDAASKVSKMLKDYDWINAEKHlfgqpnSAYDFKTNNPKEAGQR--LQKLQEMKEKLGRNVNMRAMNVLT--EAEERY 998
Cdd:COG5022 1007 Q-YGALQESTKQLKELPVEVAELQ------SASKIISSESTELSILkpLQKLKGLLLLENNQLQARYKALKLrrENSLLD 1079
|
330 340
....*....|....*....|....
gi 1952970885 999 NDLMKKKRIVENDKSKILATIEDL 1022
Cdd:COG5022 1080 DKQLYQLESTENLLKTINVKDLEV 1103
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
685-984 |
1.89e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 685 QDELRIKENELQSLDEELAGLKNTAEKyrqLKQQWEMKTEEADLLQTKLQQSSYHKQQ--EELDALKKtiEESEETLKNT 762
Cdd:TIGR04523 238 QQEINEKTTEISNTQTQLNQLKDEQNK---IKKQLSEKQKELEQNNKKIKELEKQLNQlkSEISDLNN--QKEQDWNKEL 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 763 KEIQKKAEEKYEVLENKMKNAE---AERDRELKDAQKKLDFAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQ 839
Cdd:TIGR04523 313 KSELKNQEKKLEEIQNQISQNNkiiSQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQ 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 840 LEAVNEAIKSYEVQIEAMAVEVAKNKESVNKAQEEVTKQKEVIIAQDNVIKAKyaevavhKEQNNDSQLKIKELDHNISK 919
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL-------TNQDSVKELIIKNLDNTRES 465
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952970885 920 HKREAEDAASKVSKMLKDYDWINAEkhlFGQPNSAYDFKTNNPKEAGQRLQKLQEMKEKLGRNVN 984
Cdd:TIGR04523 466 LETQLKVLSRSINKIKQNLEQKQKE---LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE 527
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1062-1143 |
1.91e-04 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 44.02 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 1062 QTVLDGLEFKVALGNtwkENLtelSGGQRSLVALSLILsmllFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFI 1141
Cdd:cd03244 123 ESLPGGLDTVVEEGG---ENL---SVGQRQLLCLARAL----LRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVL 192
|
..
gi 1952970885 1142 VV 1143
Cdd:cd03244 193 TI 194
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
144-468 |
2.27e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.56 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 144 LIMQGRITKVLNMKPPEILSMIEEAAGT--------RMYEYKKiAAQKTIEKKEAKLKEIKTILEEE---ITPTIQKLKE 212
Cdd:PRK10246 152 LLSQGQFAAFLNAKPKERAELLEELTGTeiygqisaMVFEQHK-SARTELEKLQAQASGVALLTPEQvqsLTASLQVLTD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 213 ERSSYLEYQKIM-REIEHLSRLYIAYQFLLAEDTKERSA-EELKEMQDKVVKLQekLSENDKKIKALSHEIEELEKGkdk 290
Cdd:PRK10246 231 EEKQLLTAQQQQqQSLNWLTRLDELQQEASRRQQALQQAlAAEEKAQPQLAALS--LAQPARQLRPHWERIQEQSAA--- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 291 eiggklrsLEDALAEAQRVNTKSQSAFDLKKKNLASEENKRTELEKNMIEDSRTLAAKEK------EVKkitdGLNALQE 364
Cdd:PRK10246 306 --------LAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRfrqwnnELA----GWRAQFS 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 365 ASNKDAEALAAAQQHFNAVSAGLS---------SNEDGAEA--------TLAGQMMACKNDISKAQTEAKQAQMKLKHAQ 427
Cdd:PRK10246 374 QQTSDREQLRQWQQQLTHAEQKLNalpaitltlTADEVAAAlaqhaeqrPLRQRLVALHGQIVPQQKRLAQLQVAIQNVT 453
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1952970885 428 QELKTKQAEVKKMDSGYRKDQEALEAVKKLKEkLEAEMKKL 468
Cdd:PRK10246 454 QEQTQRNAALNEMRQRYKEKTQQLADVKTICE-QEARIKDL 493
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
675-979 |
2.32e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.40 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 675 LTKFQELKNVQDELRIKENELQSLDEELAGLKNtaeKYRQLKQQWEMKTEEADLLQTKLQ--QSSYHKQQEELDALKKTI 752
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKENQSYKQEIKNLES---QINDLESKIQNQEKLNQQKDEQIKklQQEKELLEKEIERLKETI 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 753 EESEETLKNTkeiqkkaEEKYEVLENKMKNAEAERDRElkdaqkkldfaKTKADASSKKMKEKQQEVEAITLELEELKRE 832
Cdd:TIGR04523 436 IKNNSEIKDL-------TNQDSVKELIIKNLDNTRESL-----------ETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 833 HTSYKQQLEAVNEAIKSYEVQIEAMAVEVAK-NKESVNKAQEEVTKQKEVIIAQDNVIKAKYAEVAVHKEQnndsqlKIK 911
Cdd:TIGR04523 498 LKKLNEEKKELEEKVKDLTKKISSLKEKIEKlESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNK------EIE 571
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952970885 912 ELDHNISKHKREAEDAASKVSKMLKDYDWINAEKHLFGQPNSAYDFKTNNPKEAGQRL----QKLQEMKEKL 979
Cdd:TIGR04523 572 ELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLssiiKNIKSKKNKL 643
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
180-378 |
2.35e-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: 44.75 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 180 AAQKTIEKKEAKLKEIKTILEEeITPTIQKLKEERSSYL-EYQKIMREIEHLSRLYIAYQFLLAEDTKE--RSAEELKEM 256
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAE-LEKELAALKKEEKALLkQLAALERRIAALARRIRALEQELAALEAElaELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 257 QDKVVKLQEKLSE-----------NDKKIKALSHEIEELEKGKD------KEIGGKLRSLEDALAEAQRVNTKSQSAFDL 319
Cdd:COG4942 96 RAELEAQKEELAEllralyrlgrqPPLALLLSPEDFLDAVRRLQylkylaPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1952970885 320 KKKNLASEENKRTELEKNMIEDSRTLAAKEKEVKKITDGLNALQEASNKDAEALAAAQQ 378
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
422-934 |
2.48e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 422 KLKHAQQELKTKQAEVKKMDSGYRKDQEALEAVKKLKEKLEAEMKKLNYEENKEEGLLEKRRQLSRDISRLKETYEALLA 501
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 502 RFPNIQFAYRD-PEKNWNRNCVKGLVASLISVKDTSTTTALELVAGERLYNVVV--------DTEVTGKKLLEKGELKRR 572
Cdd:PRK03918 274 EIEELEEKVKElKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEerikeleeKEERLEELKKKLKELEKR 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 573 YTIIP-----LNKISARCIAPETLRVAQNLVGPNNVHVALSLVE-YKPELQKAMEFVFGTTFVCNNMDNAKKVAFD--KR 644
Cdd:PRK03918 354 LEELEerhelYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEkAKEEIEEEISKITARIGELKKEIKELKKAIEelKK 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 645 IMTRTVTLGGEVFDPH-GTLSGGARSQAASILTKFQELKNVQDELRIKENELQSL---DEELAGLKNTAEKYRQLkqqwE 720
Cdd:PRK03918 434 AKGKCPVCGRELTEEHrKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVlkkESELIKLKELAEQLKEL----E 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 721 MKTEEADLLQTKLQQSSYHKQQEELDALKKTIEESEETLKNTKEIQKKAEEkyevLENKMKNAEAER------------- 787
Cdd:PRK03918 510 EKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAE----LEKKLDELEEELaellkeleelgfe 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 788 -------------------------DRELKDAQKKLDFAKTKADASSKKMKEKQQEVEAITLELEELKR-----EHTSYK 837
Cdd:PRK03918 586 sveeleerlkelepfyneylelkdaEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkyseeEYEELR 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 838 QQLEAVNEAIKSYEVQIEAMAVEVAKNKESVNKAQEEVTKQKEVIIAQDNVIKAKYaevavhkeqnndsqlKIKELDHNI 917
Cdd:PRK03918 666 EEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE---------------RVEELREKV 730
|
570
....*....|....*...
gi 1952970885 918 SKHKREAEDAA-SKVSKM 934
Cdd:PRK03918 731 KKYKALLKERAlSKVGEI 748
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
680-874 |
2.56e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 680 ELKNVQDELRIKENELQSLDEELaglkntaEKYRQLKQQWEMKTEEADLLQTklqqsSYHKQQEELDALKKTIEESEETl 759
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEI-------ERYEEQREQARETRDEADEVLE-----EHEERREELETLEAEIEDLRET- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 760 kntkeiqkKAEEKYEvlenkmKNAEAERDRELKDAQKKLDFAKTKADASSKKmkeKQQEVEAITLELEELKREHTSYKQQ 839
Cdd:PRK02224 267 --------IAETERE------REELAEEVRDLRERLEELEEERDDLLAEAGL---DDADAEAVEARREELEDRDEELRDR 329
|
170 180 190
....*....|....*....|....*....|....*
gi 1952970885 840 LEAVNEAIKSYEVQIEAMAVEVAKNKESVNKAQEE 874
Cdd:PRK02224 330 LEECRVAAQAHNEEAESLREDADDLEERAEELREE 364
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1081-1120 |
2.97e-04 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 43.94 E-value: 2.97e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1952970885 1081 NLTELSGGQRSLVALSLILSmllfKPAPIYILDEVDAALD 1120
Cdd:cd03237 112 EVPELSGGELQRVAIAACLS----KDADIYLLDEPSAYLD 147
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1079-1144 |
3.46e-04 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). 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: 213195 [Multi-domain] Cd Length: 171 Bit Score: 42.76 E-value: 3.46e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952970885 1079 KENLteLSGGQRSLVALSLilsMLLfKPAPIYILDEVDAALDlSHTQN-IGQMLRTHFTHSQFIVVS 1144
Cdd:cd03228 93 RENI--LSGGQRQRIAIAR---ALL-RDPPILILDEATSALD-PETEAlILEALRALAKGKTVIVIA 152
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
735-937 |
4.22e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 735 QSSYHKQQEELDALKKTIEES----EETLKNTKEIQKKAEEKYEVLENKMKNAEAERDRELKDAQKK----LDFAKTKAD 806
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELerelEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEaqqaIKEAKKEAD 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 807 ASSKKMKEKQQEvEAITLELEELKREHTSYKQQLEAVNEA-IKSYEVQIEAMAVEVAKNKESVNKAQ-EEVTKQKEVIIa 884
Cdd:PRK00409 588 EIIKELRQLQKG-GYASVKAHELIEARKRLNKANEKKEKKkKKQKEKQEELKVGDEVKYLSLGQKGEvLSIPDDKEAIV- 665
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952970885 885 QDNVIK--AKYAEVAVHKEQNNDSQLKIKELDHNISKHKRE-------AEDAASKVSKMLKD 937
Cdd:PRK00409 666 QAGIMKmkVPLSDLEKIQKPKKKKKKKPKTVKPKPRTVSLEldlrgmrYEEALERLDKYLDD 727
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
676-856 |
4.79e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 42.59 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 676 TKFQELKNVQDELRIKENEL-QSLDEELAGLKNTAEKYRQLKQQWEMKTEEadlLQTKLQQssyhkQQEELDALKKTIEE 754
Cdd:pfam13851 8 KAFNEIKNYYNDITRNNLELiKSLKEEIAELKKKEERNEKLMSEIQQENKR---LTEPLQK-----AQEEVEELRKQLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 755 SE---ETLKNTKEIQKKAEEK-------YEVLENKMKNAEAERD-------RELKDAQKKLDFaktKADASSKKMKEKQQ 817
Cdd:pfam13851 80 YEkdkQSLKNLKARLKVLEKElkdlkweHEVLEQRFEKVERERDelydkfeAAIQDVQQKTGL---KNLLLEKKLQALGE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1952970885 818 EVEAITLELEELKR----EHTSYKQQLEAVNEAIKSYEVQIEA 856
Cdd:pfam13851 157 TLEKKEAQLNEVLAaanlDPDALQAVTEKLEDVLESKNQLIKD 199
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1084-1144 |
5.11e-04 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 43.09 E-value: 5.11e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952970885 1084 ELSGGQRSLVALSLILSMllfKPaPIYILDEVDAALDLSHTQNIGQMLRT-HFTHSQFIVVS 1144
Cdd:COG1122 134 ELSGGQKQRVAIAGVLAM---EP-EVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVT 191
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1082-1132 |
5.12e-04 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 43.08 E-value: 5.12e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1952970885 1082 LTELSGGQRSLValslILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLR 1132
Cdd:PRK11231 136 LTDLSGGQRQRA----FLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMR 182
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
709-872 |
5.86e-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: 43.84 E-value: 5.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 709 AEKYRQLKQQWEMKTEEADLLQTKLQQSSYH----------KQQEELDALKK------------TIEESEETLKNTKEIQ 766
Cdd:pfam05262 212 AKRAQQLKEELDKKQIDADKAQQKADFAQDNadkqrdevrqKQQEAKNLPKPadtsspkedkqvAENQKREIEKAQIEIK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 767 KKAEEKYEVLENKMKNAEAERDRELKDAQKKLDFAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEA 846
Cdd:pfam05262 292 KNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDAIDSSNPVYGLKVVDPI 371
|
170 180
....*....|....*....|....*.
gi 1952970885 847 IKSYEVQIEAMAVEVAKNKESVNKAQ 872
Cdd:pfam05262 372 TNLSELVLIDLKTEVRLRESAQQTIR 397
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
666-880 |
6.46e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 6.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 666 GARSQAASILTkfqELKNVQDELRIKENELQSLDEELAGLK----NTAEKYRQLKQQWEMKTEEADLLQTKLQ------- 734
Cdd:PRK02224 360 ELREEAAELES---ELEEAREAVEDRREEIEELEEEIEELRerfgDAPVDLGNAEDFLEELREERDELREREAeleatlr 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 735 --QSSYHKQQEELDALK--------------KTIEESEETLKNTKEIQKKAEEKYEVLENKMKNAEaerdrELKDAQKKL 798
Cdd:PRK02224 437 taRERVEEAEALLEAGKcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLERAE-----DLVEAEDRI 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 799 DFAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYEVQIEAMAVEVAknkeSVNKAQEEVTKQ 878
Cdd:PRK02224 512 ERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVA----ELNSKLAELKER 587
|
..
gi 1952970885 879 KE 880
Cdd:PRK02224 588 IE 589
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
664-933 |
6.74e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 664 SGGARSQAASILTKFQELKNvqdELRIKENELQS----LDEELAGLKNTAEKYRQLKQQweMKTEEADLLQTKLQQSSYH 739
Cdd:pfam01576 217 STDLQEQIAELQAQIAELRA---QLAKKEEELQAalarLEEETAQKNNALKKIRELEAQ--ISELQEDLESERAARNKAE 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 740 KQQ----EELDALKKTIEESEETLKNTKEIQKKaeekyevlenkmknaeaeRDRELKDAQKKLDFAKTKADASSKKMKEK 815
Cdd:pfam01576 292 KQRrdlgEELEALKTELEDTLDTTAAQQELRSK------------------REQEVTELKKALEEETRSHEAQLQEMRQK 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 816 Q-QEVEAITLELEELKRehtsYKQQLEAVNEAiksyevqIEAMAVEVAKNKESVNKAQEEVTKQKEVIIAQDNVIKAKYA 894
Cdd:pfam01576 354 HtQALEELTEQLEQAKR----NKANLEKAKQA-------LESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLS 422
|
250 260 270
....*....|....*....|....*....|....*....
gi 1952970885 895 EVAVHKEQNNDSQLKIKELDHNISKHKREAEDAASKVSK 933
Cdd:pfam01576 423 ESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSK 461
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
740-997 |
6.80e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 6.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 740 KQQEELDALKKTIEESEETlkntkeiqkkaeEKYEVLeNKMKNAEAERDRELKDAQKKLDFAK-TKADASS--KKMKEKQ 816
Cdd:PRK02224 184 DQRGSLDQLKAQIEEKEEK------------DLHERL-NGLESELAELDEEIERYEEQREQAReTRDEADEvlEEHEERR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 817 QEVEAITLELEELK-------REHTSYKQQLEAVNEAIKSYEVQIEAMAVEVA---KNKESVNKAQEEVTKQKE------ 880
Cdd:PRK02224 251 EELETLEAEIEDLRetiaeteREREELAEEVRDLRERLEELEEERDDLLAEAGlddADAEAVEARREELEDRDEelrdrl 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 881 -----VIIAQDNVIKAKYAEVAVHKEQNNDSQLKIKELDHNISKHKREAEDAASKVSKMLKDYDWINAekhlfgqpnsAY 955
Cdd:PRK02224 331 eecrvAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE----------RF 400
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1952970885 956 DFKTNNPKEAGQRLQKLQEMKEKL-GRNVNMRAmnVLTEAEER 997
Cdd:PRK02224 401 GDAPVDLGNAEDFLEELREERDELrEREAELEA--TLRTARER 441
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
684-874 |
6.98e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 684 VQDELRIKENELQSLDEELAGLKNTAE----KYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEEldalkktieeseetl 759
Cdd:pfam01576 880 LQDEKRRLEARIAQLEEELEEEQSNTEllndRLRKSTLQVEQLTTELAAERSTSQKSESARQQLE--------------- 944
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 760 KNTKEIQKKAEEKYEVLENKMKNAEAERDRELKDAQKKLDFAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQ 839
Cdd:pfam01576 945 RQNKELKAKLQEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQ 1024
|
170 180 190
....*....|....*....|....*....|....*
gi 1952970885 840 LEAVNEAIKSYEVQIEAMAVEVAKNKESVNKAQEE 874
Cdd:pfam01576 1025 AEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRE 1059
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
190-390 |
7.14e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.76 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 190 AKLKEIKTI-LEEEITPTIQKLKE----------ERSSYLEYQKIMREIEHLSR-----------------LYIAYQFLL 241
Cdd:PRK05771 4 VRMKKVLIVtLKSYKDEVLEALHElgvvhiedlkEELSNERLRKLRSLLTKLSEaldklrsylpklnplreEKKKVSVKS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 242 AEDTKERSAEELKEMQDKVVKLQEKLSENDKKIKALSHEIEELEKGKD------KEIGGKL----------RSLEDALAE 305
Cdd:PRK05771 84 LEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEPWGNfdldlsLLLGFKYvsvfvgtvpeDKLEELKLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 306 AQRVNTKSQS---------AFDLKK-KNLASEENKRTELEKNMIEDSRT-----------LAAKEKEVKKITDGLNALQE 364
Cdd:PRK05771 164 SDVENVEYIStdkgyvyvvVVVLKElSDEVEEELKKLGFERLELEEEGTpselireikeeLEEIEKERESLLEELKELAK 243
|
250 260 270
....*....|....*....|....*....|
gi 1952970885 365 ASNKDA----EALAAAQQHFNAVSAGLSSN 390
Cdd:PRK05771 244 KYLEELlalyEYLEIELERAEALSKFLKTD 273
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
696-945 |
8.18e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 8.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 696 QSLDEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSsyhkqQEELDALKKTIEESEETLKNTKEIQKKAEEKYEV 775
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQA-----RSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 776 LENKMKNAEAERDR---ELKDAQKKLDFAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEA-----VNEAI 847
Cdd:COG4372 106 LQEEAEELQEELEElqkERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAlseaeAEQAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 848 KSYEVQIEAMAVEVAKNKESVNKAQEEVTKQKEVIIAQDNVIKAKYAEV-AVHKEQNNDSQLKIKELDHNISKHKREAED 926
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAlSALLDALELEEDKEELLEEVILKEIEELEL 265
|
250
....*....|....*....
gi 1952970885 927 AASKVSKMLKDYDWINAEK 945
Cdd:COG4372 266 AILVEKDTEEEELEIAALE 284
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
652-974 |
8.88e-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: 43.80 E-value: 8.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 652 LGGEVFDPHGTLSG-----GARSQAASILTKfQELKNVQDELRIKENELQSLDEELAGLKNTAEKYRQLKQqwemKTEEA 726
Cdd:TIGR00618 181 LALMEFAKKKSLHGkaellTLRSQLLTLCTP-CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKRE----AQEEQ 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 727 DLLQTKLQQSsyHKQQEELDALKKTIEESEETL-------------KNTKEIQKKAEEKYEVLENKMKNAEAERDRELKD 793
Cdd:TIGR00618 256 LKKQQLLKQL--RARIEELRAQEAVLEETQERInrarkaaplaahiKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAH 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 794 AQKKLDFAKTKadaSSKKMKEKQQEVEAITLELEELKREHTSYKQQLEavnEAIKSYEVQIEAMAVEVAKNKESVNKAQE 873
Cdd:TIGR00618 334 VKQQSSIEEQR---RLLQTLHSQEIHIRDAHEVATSIREISCQQHTLT---QHIHTLQQQKTTLTQKLQSLCKELDILQR 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 874 EVTKQKeviiAQDNVIKAKYAEVAVHKEQNNDSQLKIKELDHNISKHKREAEDAASKVSKMLKDYDwinAEKHLFGQPNS 953
Cdd:TIGR00618 408 EQATID----TRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLK---EREQQLQTKEQ 480
|
330 340
....*....|....*....|.
gi 1952970885 954 AYDFKTNNPKEAGQRLQKLQE 974
Cdd:TIGR00618 481 IHLQETRKKAVVLARLLELQE 501
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
785-945 |
8.91e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 8.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 785 AERDRELKDAQKKLDFAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYEVQIEAMAVEVAKN 864
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 865 KESVNKAQ------------EEVTKQKEVIIAQDNVIKAKYAEVAVHKEQNNDSQLKIKELDHNISKHKREAEDAASKVS 932
Cdd:COG3883 99 GGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170
....*....|...
gi 1952970885 933 KMLKDYDWINAEK 945
Cdd:COG3883 179 EQEALLAQLSAEE 191
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
679-880 |
9.02e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 42.32 E-value: 9.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 679 QELKNVQDELRIKENELQSLDEELAGLKNTAEKYRQLKQQWEMKTEEA-DLLQTKLQQ-SSYHKQQEELDALKKTIEES- 755
Cdd:pfam00261 8 EELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTeERLAEALEKlEEAEKAADESERGRKVLENRa 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 756 ----------EETLKNTKEIQKKAEEKYEVLENKMKNAEAERDRelkdaqkkldfAKTKADASSKKMKEKQQEVEAIT-- 823
Cdd:pfam00261 88 lkdeekmeilEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLER-----------AEERAELAESKIVELEEELKVVGnn 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952970885 824 ---LELEELK---REHtSYKQQLEAVNEAIKSYEVQIEAMAVEVAKNKESVNKAQEEVTKQKE 880
Cdd:pfam00261 157 lksLEASEEKaseRED-KYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKE 218
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
182-399 |
9.34e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 9.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 182 QKTIEKKEAKLKEIKTILEE--EITPTIQKLKEERSSYLEYQKIMREIEHLSRLYI---AYQFLLAEDTKERSA-----E 251
Cdd:COG4913 606 FDNRAKLAALEAELAELEEElaEAEERLEALEAELDALQERREALQRLAEYSWDEIdvaSAEREIAELEAELERldassD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 252 ELKEMQDKVVKLQEKLSENDKKIKALSHEIEELEKgKDKEIGGKLRSLEDALAEAQRVNTKSQSAFDLKKKNLASEENKR 331
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEK-ELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVE 764
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952970885 332 TELEKNMIEDSRTLAAKekevkkitdglnaLQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLA 399
Cdd:COG4913 765 RELRENLEERIDALRAR-------------LNRAEEELERAMRAFNREWPAETADLDADLESLPEYLA 819
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
711-945 |
9.68e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 9.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 711 KYRQLKQQWEMKTEEADLLQTKLQqsSYHKQQEELDALkktieeseetlknTKEIQKKAEEKYEVLENKMKNAEAERDrE 790
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIK--TYNKNIEEQRKK-------------NGENIARKQNKYDELVEEAKTIKAEIE-E 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 791 LKDAQKKLDFAKTKADASSKKMKekqQEVEAITLELEELKREHTSY---------KQQLEAVNEAIKSyevqIEAMAVEV 861
Cdd:PHA02562 239 LTDELLNLVMDIEDPSAALNKLN---TAAAKIKSKIEQFQKVIKMYekggvcptcTQQISEGPDRITK----IKDKLKEL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 862 AKNKESVNKAQEEVTKQKEVIIAQDNVIKAKYAEVAVHKEQNNDSQLKIKELDHNISKHKREAEDAASKVSKMLKDYDWI 941
Cdd:PHA02562 312 QHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
....
gi 1952970885 942 NAEK 945
Cdd:PHA02562 392 VKTK 395
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
674-933 |
1.02e-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: 43.47 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 674 ILTKFQELKNVQDELRIKENELQSLDEELAGLKNTAE--KYRQLKQQWEMKTEEADLL----QTKLQQSSYHKQQEELDA 747
Cdd:TIGR04523 49 LKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKdlNDKLKKNKDKINKLNSDLSkinsEIKNDKEQKNKLEVELNK 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 748 LKKTIEESEETL-KNTKEIQKKAEE------KYEVLENKMKNAEAERD---RELKDAQKKLDFAKTKADASS------KK 811
Cdd:TIGR04523 129 LEKQKKENKKNIdKFLTEIKKKEKEleklnnKYNDLKKQKEELENELNlleKEKLNIQKNIDKIKNKLLKLElllsnlKK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 812 MKEKQQEVEAITLELEE----LKREHTSYKQQLEAVNEAIKSYEVQIEAMAVEVAKNKESVNKAQEEVTKQKEVIIAQDN 887
Cdd:TIGR04523 209 KIQKNKSLESQISELKKqnnqLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEK 288
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1952970885 888 VIKAKYAEVAVHKEQNNdsQLKIKELDHNISKHKREAEDAASKVSK 933
Cdd:TIGR04523 289 QLNQLKSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQ 332
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
241-370 |
1.07e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 241 LAEDTKERSAEELKEMQDKVVKLQEKLSENDKKIKALSHEIEELEKgkdkeiggKLRSLEDALAEAQRVNTKSQSAFDLK 320
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEA--------EVEELEAELEEKDERIERLERELSEA 453
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1952970885 321 KKNLASEENKRTELEK--NMIED-SRTLAAKEKEVKKITDGLNALQEASNKDA 370
Cdd:COG2433 454 RSEERREIRKDREISRldREIERlERELEEERERIEELKRKLERLKELWKLEH 506
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
677-934 |
1.20e-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: 43.19 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 677 KFQELKnvQDELRIKENELQSLDEELAGLKNtAEKYRQLK---------QQWEMKTE-EADLLQTKLQQSSYHKQQEELD 746
Cdd:pfam17380 292 KFEKME--QERLRQEKEEKAREVERRRKLEE-AEKARQAEmdrqaaiyaEQERMAMErERELERIRQEERKRELERIRQE 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 747 ALKKTIEESEETLKNTKEIQKKAEEKYEVLENKMKNAEAERDRELKDAQKKLDFAKTKADASSKKMKEKQQEVEAITLEL 826
Cdd:pfam17380 369 EIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREM 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 827 EELKREHTSYKQQLeavnEAIKSYEVQIEAMAVEVAKNKESVNKAQEEVTK--QKEVIIAQDNVIKAKYAEVAVHKEQnN 904
Cdd:pfam17380 449 ERVRLEEQERQQQV----ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKilEKELEERKQAMIEEERKRKLLEKEM-E 523
|
250 260 270
....*....|....*....|....*....|
gi 1952970885 905 DSQLKIKEldhniSKHKREAEDAASKVSKM 934
Cdd:pfam17380 524 ERQKAIYE-----EERRREAEEERRKQQEM 548
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
724-1006 |
1.22e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.29 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 724 EEADLLQTKLQ-QSSYHKQQEE-LDALKKTIEESEETLKNTKEIQKKAEEKYEVLENKMKNAEAERDRELKDAQKKLDFA 801
Cdd:pfam12128 604 ERLDKAEEALQsAREKQAAAEEqLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANER 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 802 KTKADASSKKMKEKQQEVEAitlELEELKREHTSYKQQleavneaikSYEVQIEAMAVEVAKNKESVNKAQEEVTKQKEV 881
Cdd:pfam12128 684 LNSLEAQLKQLDKKHQAWLE---EQKEQKREARTEKQA---------YWQVVEGALDAQLALLKAAIAARRSGAKAELKA 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 882 IiaqdnvikakyaevavhkEQNNDSQLKIKELD-HNISKHKREA-------EDAASKVSKMLKDYDWINaekHLFGQPNS 953
Cdd:pfam12128 752 L------------------ETWYKRDLASLGVDpDVIAKLKREIrtlerkiERIAVRRQEVLRYFDWYQ---ETWLQRRP 810
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1952970885 954 AYDFKTNNPKEAGQRLQ---KLQEMKEKLGRNVNMRAMNVLTEAEERYNDLMKKKR 1006
Cdd:pfam12128 811 RLATQLSNIERAISELQqqlARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLR 866
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
667-856 |
1.34e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 667 ARSQAASILTKF--QELKNVQDELRIKENELQ---------SLDEE----LAGLKNTAEKYRQLKQQWEMKTEEADLLQT 731
Cdd:COG3206 168 LRREEARKALEFleEQLPELRKELEEAEAALEefrqknglvDLSEEakllLQQLSELESQLAEARAELAEAEARLAALRA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 732 KL----QQSSYHKQQEELDALKKTIEESEETLKNTKEIQKKAEEKYEVLENKMKNAEAERDRELK----DAQKKLDFAKT 803
Cdd:COG3206 248 QLgsgpDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQrilaSLEAELEALQA 327
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1952970885 804 KADASSKKMKEKQQEVEAIT---LELEELKREHTSYKQQLEAVNEaiKSYEVQIEA 856
Cdd:COG3206 328 REASLQAQLAQLEARLAELPeleAELRRLEREVEVARELYESLLQ--RLEEARLAE 381
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
243-519 |
1.45e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 243 EDTKERSAEELKEMQDKVVKLQEKLSENDKKIKALSHEIEELEKGKDKEIGGKLRSLEDALAEAQRVNTKSQSafdLKKK 322
Cdd:PRK01156 468 NHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINE---LKDK 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 323 NLASEENKrTELEKNMIEDSRTlaakekevkKITDGLNALQEASNKDAEALaaaQQHFNAVSAGLSSNEDGA---EATLA 399
Cdd:PRK01156 545 HDKYEEIK-NRYKSLKLEDLDS---------KRTSWLNALAVISLIDIETN---RSRSNEIKKQLNDLESRLqeiEIGFP 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 400 GQMMACKNDISKAQTEAKQAQMKLKHAqQELKTKQAEVKKMDSGYRKDQEALEAVKKLKEKLEAEMKKLNYEENKEEGLL 479
Cdd:PRK01156 612 DDKSYIDKSIREIENEANNLNNKYNEI-QENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKAL 690
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1952970885 480 EKrrqLSRDISRLKETYEALLARFPNIQFAYRDPEKNWNR 519
Cdd:PRK01156 691 DD---AKANRARLESTIEILRTRINELSDRINDINETLES 727
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1066-1120 |
1.49e-03 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 42.78 E-value: 1.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1952970885 1066 DGLEFKVAlgntwkENLTELSGGQRSLVALSlilsMLLFKPAPIYILDEVDAALD 1120
Cdd:TIGR02203 457 LGLDTPIG------ENGVLLSGGQRQRLAIA----RALLKDAPILILDEATSALD 501
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
680-840 |
1.50e-03 |
|
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: 42.89 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 680 ELKNVQDELRIKENELQSLDEELAGL--------KNTAEKYRQLKQ-QWEMKTEEADLLQTKLQQ------SSYHKQQEE 744
Cdd:pfam10174 580 EVERLLGILREVENEKNDKDKKIAELesltlrqmKEQNKKVANIKHgQQEMKKKGAQLLEEARRRednladNSQQLQLEE 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 745 L-DALKKTIEESEETLKNTKEIQKKAEEKyevlENKMKNAEAERDRELKDA----QKKLDFAKTKADA-------SSKKM 812
Cdd:pfam10174 660 LmGALEKTRQELDATKARLSSTQQSLAEK----DGHLTNLRAERRKQLEEIlemkQEALLAAISEKDAniallelSSSKK 735
|
170 180
....*....|....*....|....*...
gi 1952970885 813 KEKQQEVEAitleleeLKREHTSYKQQL 840
Cdd:pfam10174 736 KKTQEEVMA-------LKREKDRLVHQL 756
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1085-1134 |
1.51e-03 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 41.31 E-value: 1.51e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1952970885 1085 LSGGQRSLVALSLilsmLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTH 1134
Cdd:COG4133 132 LSAGQKRRVALAR----LLLSPAPLWLLDEPFTALDAAGVALLAELIAAH 177
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
675-802 |
1.59e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 39.98 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 675 LTKFQELKNVQDELRIKENELQSLDEELAGLKNTAEKYRQLKQQwemkteeADLLQTKLQQssyhkQQEELdalkktiEE 754
Cdd:pfam12718 31 LEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTN-------NENLTRKIQL-----LEEEL-------EE 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1952970885 755 SEETLKNTKEIQKKAEEKYEVLENKMKNAEAERD---RELKDAQKKLDFAK 802
Cdd:pfam12718 92 SDKRLKETTEKLRETDVKAEHLERKVQALEQERDeweKKYEELEEKYKEAK 142
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
27-100 |
1.61e-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: 41.99 E-value: 1.61e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952970885 27 FNAITGLNGSGKSNILDSICFLLGIsnlsqvrASNLQDLVYKNGQAGITKASVSITFDNSDKKQSPLGFEVHDE 100
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADF-------DALVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLE 67
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1081-1132 |
1.81e-03 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 41.57 E-value: 1.81e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1952970885 1081 NLTELSGGQRSLVAlsliLSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLR 1132
Cdd:COG1120 134 PVDELSGGERQRVL----IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLR 181
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1062-1114 |
1.83e-03 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 39.94 E-value: 1.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1952970885 1062 QTVLDGLEFKVALGNTWKENLTELSGGQRSLVAlsliLSMLLFKPAPIYILDE 1114
Cdd:pfam00005 99 EEALEKLGLGDLADRPVGERPGTLSGGQRQRVA----IARALLTKPKLLLLDE 147
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
674-930 |
1.84e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.65 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 674 ILTKFQELKNVQDELRIKENELQSLDEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQE---------E 744
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTaqceklekiH 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 745 LDALKKTIEESEETLKNTKEIQKKAEEKYEVlENKMKNAEAERDRELKDAQKKLDFAKTKAD---ASSKKMKEKQQEVEA 821
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHLQETRKKAV-VLARLLELQEEPCPLCGSCIHPNPARQDIDnpgPLTRRMQRGEQTYAQ 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 822 ITLELEELKREHTSYKQQLEAVNEAIKSYEVQIEAMAVEVAKNKESVNKAQEEVTKQKEVIIAQDNVIKAKYAEVAVHKE 901
Cdd:TIGR00618 540 LETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLR 619
|
250 260
....*....|....*....|....*....
gi 1952970885 902 QNNDSQLKIKELDHNISKHKREAEDAASK 930
Cdd:TIGR00618 620 KLQPEQDLQDVRLHLQQCSQELALKLTAL 648
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
673-1039 |
2.18e-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: 42.34 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 673 SILTKFQ-ELKNVQDELRIKENELQSLDEELAglkntaekYRQLKQQWEMKTEEADLLQTK--LQQSSYHKQQEELDALK 749
Cdd:TIGR00606 792 TIMERFQmELKDVERKIAQQAAKLQGSDLDRT--------VQQVNQEKQEKQHELDTVVSKieLNRKLIQDQQEQIQHLK 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 750 KTIEESE-------ETLKNTKEIQKKAEEKYEVLENKMKNAEAERDRELKDAQKKLDFAKTKADASSKKMKEKQQEVEAI 822
Cdd:TIGR00606 864 SKTNELKseklqigTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKV 943
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 823 TLELEELKREHTSYKQQLEAVNEAIKSY----EVQIEAMAVEVAKNKESVNKAQEEVTKQKEVIIAQDNVIKAKYAEVAV 898
Cdd:TIGR00606 944 NDIKEKVKNIHGYMKDIENKIQDGKDDYlkqkETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTL 1023
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 899 HKEQNndsqlKIKELDHNISKHKREAEDaaSKVSKMLKDYDWINAEKHLFGQPNSAYDFKTNNPKEagQRLQKLQEMKEK 978
Cdd:TIGR00606 1024 RKREN-----ELKEVEEELKQHLKEMGQ--MQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEK--EIKHFKKELREP 1094
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952970885 979 LGRNvnmramnvlteAEERYNDLMKKKRIVENDKSKILATIEDLDQKKNQALNIAWQKVNK 1039
Cdd:TIGR00606 1095 QFRD-----------AEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMKMEEINK 1144
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
180-494 |
2.30e-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: 42.41 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 180 AAQKTIEKKEAKLKEIKTILEEE---ITPTIQKLKEERSsylEYQKIMREIEHLsrlyiayqfllaedtkERSAEELKEM 256
Cdd:pfam15921 486 AKKMTLESSERTVSDLTASLQEKeraIEATNAEITKLRS---RVDLKLQELQHL----------------KNEGDHLRNV 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 257 QDKVVKLQEKLSENDKKIKALSHEIEELEK--GKDKEIGGKLRsLEDALAEAQ----RVNTKSQSAFDLKKKNLASE-EN 329
Cdd:pfam15921 547 QTECEALKLQMAEKDKVIEILRQQIENMTQlvGQHGRTAGAMQ-VEKAQLEKEindrRLELQEFKILKDKKDAKIRElEA 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 330 KRTELEKNMIEDSRTLAAKEKEVKKITDGLNALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLAGQMMACKNdi 409
Cdd:pfam15921 626 RVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKS-- 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 410 skAQTEAKQAQMKLK-------HA-------QQELKTKQAEVKKMDSGYRKDQEAL-------EAVKKLKEKLEAEMKKL 468
Cdd:pfam15921 704 --AQSELEQTRNTLKsmegsdgHAmkvamgmQKQITAKRGQIDALQSKIQFLEEAMtnankekHFLKEEKNKLSQELSTV 781
|
330 340
....*....|....*....|....*.
gi 1952970885 469 NYEENKEEGLLEKRRQLSRdisRLKE 494
Cdd:pfam15921 782 ATEKNKMAGELEVLRSQER---RLKE 804
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1064-1132 |
2.36e-03 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 40.59 E-value: 2.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952970885 1064 VLDGLEFkVALGNTWKENLTELSGGQRSLValslILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLR 1132
Cdd:cd03235 113 VDEALER-VGLSELADRQIGELSGGQQQRV----LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLR 176
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
692-916 |
2.38e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 692 ENELQSLDEELAGLKNTAEkyrqlkqqwEMKTEEADLLQTKLQQSSYHKQQEELDALKKTIEES-EETLKNTKEIQK-KA 769
Cdd:PRK11281 38 EADVQAQLDALNKQKLLEA---------EDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQApAKLRQAQAELEAlKD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 770 EEKYEVLE--NKMKNAE-----AERDRELKDAQKKLDFA-------KTKADASSKKMKEKQQEVEAITLELEELKRE--- 832
Cdd:PRK11281 109 DNDEETREtlSTLSLRQlesrlAQTLDQLQNAQNDLAEYnsqlvslQTQPERAQAALYANSQRLQQIRNLLKGGKVGgka 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 833 ------------------HTSYKQQLEAVNEAIKS-YEVQIEAMAVEVAKNKESVNKAQEEVTkQKEVIIAQDNVIKAKY 893
Cdd:PRK11281 189 lrpsqrvllqaeqallnaQNDLQRKSLEGNTQLQDlLQKQRDYLTARIQRLEHQLQLLQEAIN-SKRLTLSEKTVQEAQS 267
|
250 260
....*....|....*....|...
gi 1952970885 894 AEVAVHKEQNNdsqLKIKELDHN 916
Cdd:PRK11281 268 QDEAARIQANP---LVAQELEIN 287
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
803-939 |
2.57e-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: 41.06 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 803 TKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYEVQIEAMAVEVAKNKEsvnkAQEEVTKQKEvi 882
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE----QLGNVRNNKE-- 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1952970885 883 iaqdnvIKAKYAEVAVHKEQNNDSQLKIKELDHNISKHKREAEDAASKVSKMLKDYD 939
Cdd:COG1579 91 ------YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELE 141
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1084-1143 |
2.73e-03 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 40.54 E-value: 2.73e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 1084 ELSGGQRSLVALsliLSMLLFKPAPIyILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVV 1143
Cdd:COG4136 133 TLSGGQRARVAL---LRALLAEPRAL-LLDEPFSKLDAALRAQFREFVFEQIRQRGIPAL 188
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
144-493 |
2.80e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 41.96 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 144 LIMQGRItKVLNMKPPEILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKE------ERSSY 217
Cdd:PTZ00108 1020 HVINGEL-VITNAKKKDLVKELKKLGYVRFKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEELGAAVSydyllsMPIWS 1098
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 218 LEYQKIMREIEHLSRLYIAYQFLLAEDTKERSAEELKemqdkvvKLQEKLSENDKKIKALSHEIEELEKgKDKEIGGKLR 297
Cdd:PTZ00108 1099 LTKEKVEKLNAELEKKEKELEKLKNTTPKDMWLEDLD-------KFEEALEEQEEVEEKEIAKEQRLKS-KTKGKASKLR 1170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 298 SLEDALAEAQrvntKSQSAFDLKKKNLASEENKRTELEKnMIEDSRTLAAKEKEVKKITDGLNALQEASNKDAEALAAAQ 377
Cdd:PTZ00108 1171 KPKLKKKEKK----KKKSSADKSKKASVVGNSKRVDSDE-KRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKS 1245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 378 QHFNAVSAGLSSNEDGAEATLAGQmmACKNDISKAQTEAKQAQMKLKHAQQELKTKQAEVKKMDSGYRKDQEALEAVKKL 457
Cdd:PTZ00108 1246 KKNNSSKSSEDNDEFSSDDLSKEG--KPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSSPTKKKVKKRLEGSLAALKK 1323
|
330 340 350
....*....|....*....|....*....|....*.
gi 1952970885 458 KEKleAEMKKLNYEENKEEGLLEKRRQLSRDISRLK 493
Cdd:PTZ00108 1324 KKK--SEKKTARKKKSKTRVKQASASQSSRLLRRPR 1357
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1059-1143 |
3.10e-03 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 40.47 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 1059 PEGQTVLDGLE-FKVALgNTWKENLTELSGGQRSLVALsliLSMLLFKPApIYILDEVDAALDLSHTQNIGQMLrTHFTH 1137
Cdd:PRK10247 112 PDPAIFLDDLErFALPD-TILTKNIAELSGGEKQRISL---IRNLQFMPK-VLLLDEITSALDESNKHNVNEII-HRYVR 185
|
....*.
gi 1952970885 1138 SQFIVV 1143
Cdd:PRK10247 186 EQNIAV 191
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
708-930 |
3.31e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 41.96 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 708 TAEKYRQLKQQWEMKTEEADLLQTKLQQSSYhkqQEELDALKKTIEESEETLKNTKEIQKKAEEKyevlenKMKNAEAER 787
Cdd:PTZ00108 1100 TKEKVEKLNAELEKKEKELEKLKNTTPKDMW---LEDLDKFEEALEEQEEVEEKEIAKEQRLKSK------TKGKASKLR 1170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 788 DRELKDAQKKLDFAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEaiksyEVQIEAMAVEVAKNKES 867
Cdd:PTZ00108 1171 KPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDD-----EEQKTKPKKSSVKRLKS 1245
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952970885 868 VNKAQEEVTKQKEVIIAQDNVIKAKYAEVAVHKEQNNDSQLKIKELDHNISKHKREAEDAASK 930
Cdd:PTZ00108 1246 KKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSSPTKK 1308
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
175-354 |
3.35e-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: 41.65 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 175 EYKKIAAQKTIE----KKEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQKIMREIEHlsRLYIAYQFLLAEDTKERSA 250
Cdd:pfam17380 338 EQERMAMEREREleriRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQ--ELEAARKVKILEEERQRKI 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 251 EELKEMQDKVVKLQEKLSENDKKI----------------KALSHEIEEL----EKGKDKEIGGKLRSLEDALAEAQRVN 310
Cdd:pfam17380 416 QQQKVEMEQIRAEQEEARQREVRRleeeraremervrleeQERQQQVERLrqqeEERKRKKLELEKEKRDRKRAEEQRRK 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1952970885 311 TKSQSaFDLKKKNLASEENKRTELEKNMiEDSRTLAAKEKEVKK 354
Cdd:pfam17380 496 ILEKE-LEERKQAMIEEERKRKLLEKEM-EERQKAIYEEERRRE 537
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
684-838 |
4.35e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 41.36 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 684 VQDELRIKENELQSLDEELAGLKNTAEKYRQLKQQWEMKTEEA--DLLQTKLQQSSYHKQQEELDA----------LKKT 751
Cdd:NF012221 1611 ILEESRAVTKELTTLAQGLDALDSQATYAGESGDQWRNPFAGGllDRVQEQLDDAKKISGKQLADAkqrhvdnqqkVKDA 1690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 752 IEESEETLKNTKEIQKKAEEKYEVLENKMKNAEAERDRELKDAQKkldfAKTKADASSKKMKEK-QQEVEAITLELEELK 830
Cdd:NF012221 1691 VAKSEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQ----AESDANAAANDAQSRgEQDASAAENKANQAQ 1766
|
....*...
gi 1952970885 831 REHTSYKQ 838
Cdd:NF012221 1767 ADAKGAKQ 1774
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
641-874 |
4.63e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.43 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 641 FDKRIMTRTVTLGGEVFDPHGTLSGGARSQAASILTKFQELKNVQDELRIKENeLQSLDEELAGLKNTAEKYRQlkqqwe 720
Cdd:cd22656 63 FKDDTYPSIVSLAGDIYNYAQNAGGTIDSYYAEILELIDDLADATDDEELEEA-KKTIKALLDDLLKEAKKYQD------ 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 721 mkteEADLLQTKLQ--QSSYHKQQEELDALKKTI------EESEETLKNTKEIQKKAEEKYEVLENKMKNAEAERDRELK 792
Cdd:cd22656 136 ----KAAKVVDKLTdfENQTEKDQTALETLEKALkdlltdEGGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 793 DAQKKLDfAKTKADASSKKMKEK----QQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYEVQIEAMAVEvaknKESV 868
Cdd:cd22656 212 DDEAKLA-AALRLIADLTAADTDldnlLALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDISKIPAAILA----KLEL 286
|
....*.
gi 1952970885 869 NKAQEE 874
Cdd:cd22656 287 EKAIEK 292
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
408-482 |
5.08e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 5.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952970885 408 DISKAQTEAKQAQMKLKHAQQELKTKQAEVKKMDSGYRKDQEALEAVKKLKEKLEAEMKKLNYEENKEEGLLEKR 482
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
689-900 |
5.22e-03 |
|
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: 40.60 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 689 RIKENELQSLDEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEE--LDALKKTIEESEETLKNTKEIQ 766
Cdd:TIGR02794 54 RIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQaaKQAEEKQKQAEEAKAKQAAEAK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 767 KKAEEKYEVLENKMKNAEAERDRELK---DAQKKLDFAKTKADASSKKMKEKQQEVEAitlelEELKREHTSYKQQLEAv 843
Cdd:TIGR02794 134 AKAEAEAERKAKEEAAKQAEEEAKAKaaaEAKKKAEEAKKKAEAEAKAKAEAEAKAKA-----EEAKAKAEAAKAKAAA- 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1952970885 844 nEAIKSYEVQIEAMAVEVAKNKESVNKAQEEVTKQKEVIIAQDNVIKAKYAEVAVHK 900
Cdd:TIGR02794 208 -EAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-331 |
5.27e-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: 40.66 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 1 MHVKSIILEGFKSYaQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLgisNLSQVRASNLQDLVYKNGQAGITKASVS 80
Cdd:pfam13175 1 MKIKSIIIKNFRCL-KDTEID-LDEDLTVLIGKNNSGKSSILEALDIFL---NNKEKFFEDDFLVLYLKDVIKIDKEDLN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 81 ItFDNSDKKQSplgFEVHDEITVTRQVVIGGRNKYLIngvNANNSRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPPE 160
Cdd:pfam13175 76 I-FENISFSID---IEIDVEFLLILFGYLEIKKKYLC---LASKGKAKEYEKTLHPKGANKADLLLELKISDLKKYLKQF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 161 ILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQKIMREIEHLSRLYIAYQFL 240
Cdd:pfam13175 149 KIYIYNNYYLDEKKNVFDKKSKYELPSLKEEFLNSEKEEIKVDKEDLKKLINELEKSINYHENVLENLQIKKLLISADRN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 241 LAEDTKERSAEELKEMQDKvvKLQEKLSENDKKIKALSHEIEELEKgKDKEIGGKLR-SLEDALAEAQR--VNTKSQSAF 317
Cdd:pfam13175 229 ASDEDSEKINSLLGALKQR--IFEEALQEELELTEKLKETQNKLKE-IDKTLAEELKnILFKKIDKLKDfgYPPFLNPEI 305
|
330
....*....|....
gi 1952970885 318 DLKKKNLASEENKR 331
Cdd:pfam13175 306 EIKKDDEDLPLNKN 319
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
714-880 |
5.31e-03 |
|
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: 40.60 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 714 QLKQQW-EMKTEEADllQTKLQQSSYHKQQEELDALKKTIEESEETLKNTKEiQKKAEEKYEVLENKMKNAEAERDRELK 792
Cdd:TIGR02794 47 AVAQQAnRIQQQKKP--AAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQ-RAAAEKAAKQAEQAAKQAEEKQKQAEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 793 DAQKKLDFAKTKADASSKKMK----EKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYEVQIEAMAVEvAKNKESV 868
Cdd:TIGR02794 124 AKAKQAAEAKAKAEAEAERKAkeeaAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAK-AKAEAAK 202
|
170
....*....|..
gi 1952970885 869 NKAQEEVTKQKE 880
Cdd:TIGR02794 203 AKAAAEAAAKAE 214
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
281-502 |
5.32e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 281 IEELeKGKDKEIGGKLRSLEDALAEAQRVNTKSQSAFDLKKKNLASEENKRT-ELEKNMIEDSRTLAAKEKEVKKITDGL 359
Cdd:PRK04863 444 LEEF-QAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAwDVARELLRRLREQRHLAEQLQQLRMRL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 360 NALQEASNKDAEALAAAQQhFNAVSAGLSSNEDGAEAtLAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKTKQAEVKK 439
Cdd:PRK04863 523 SELEQRLRQQQRAERLLAE-FCKRLGKNLDDEDELEQ-LQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAA 600
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952970885 440 MDSGYRKDQEALEavkKLKEKLEAEMKKLNYEENKEEGLLEKRRQLSRDISRLKETYEALLAR 502
Cdd:PRK04863 601 RAPAWLAAQDALA---RLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEE 660
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
742-976 |
5.38e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 41.36 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 742 QEELDALKKTIEESEETlKNTKEIQKKAEEKYEVLENkmknaeaERDRELKD---AQKKLDfaktkADASSKKMKEKQQE 818
Cdd:NF012221 1541 SQQADAVSKHAKQDDAA-QNALADKERAEADRQRLEQ-------EKQQQLAAisgSQSQLE-----STDQNALETNGQAQ 1607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 819 VEAITLELEELKREHTSYKQQLEAVNE----AIKSYEVQIEAMAVEVAKNKESV-----NKAQEEVTKQKEVIIAQDNVI 889
Cdd:NF012221 1608 RDAILEESRAVTKELTTLAQGLDALDSqatyAGESGDQWRNPFAGGLLDRVQEQlddakKISGKQLADAKQRHVDNQQKV 1687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 890 KAKYAEVAVHKEQnndSQLKIKELDHNISKHKREAEdaASKVSKMLKDYDWINAEKhlfgQPNSAYdfktNNPKEAGQRL 969
Cdd:NF012221 1688 KDAVAKSEAGVAQ---GEQNQANAEQDIDDAKADAE--KRKDDALAKQNEAQQAES----DANAAA----NDAQSRGEQD 1754
|
....*..
gi 1952970885 970 QKLQEMK 976
Cdd:NF012221 1755 ASAAENK 1761
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
680-879 |
5.60e-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: 40.77 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 680 ELKNVQDELRIKENELQSLDEELAGLKNTaEKYRQLKQQWEMKTEEAdllqTKLQQSSYHKQQEELDALKKT---IEESE 756
Cdd:NF033838 175 ELEIAESDVEVKKAELELVKEEAKEPRDE-EKIKQAKAKVESKKAEA----TRLEKIKTDREKAEEEAKRRAdakLKEAV 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 757 ETLKNTKEIQK-KAEEKYEVL---------ENKMKNAEA------------ERDRELKDAQKKLDFAKTKADASSKKMKE 814
Cdd:NF033838 250 EKNVATSEQDKpKRRAKRGVLgepatpdkkENDAKSSDSsvgeetlpspslKPEKKVAEAEKKVEEAKKKAKDQKEEDRR 329
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952970885 815 KQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSyevqieamavevAKNKESVNKAQEEVTKQK 879
Cdd:NF033838 330 NYPTNTYKTLELEIAESDVKVKEAELELVKEEAKE------------PRNEEKIKQAKAKVESKK 382
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
800-882 |
5.78e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 800 FAKTKADASSKKMKEKQQEVEAITLELEELKrehtsykQQLEAVNEAIKSYEVQIEAMAVEVAKNKESVNKAQEEVTKQK 879
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQ-------AELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR 85
|
...
gi 1952970885 880 EVI 882
Cdd:COG3883 86 EEL 88
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
679-854 |
5.93e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 679 QELKNVQDELRIKENELQSLDEELAGLKNTAEKYRQLKQQWEMKTEEADLlQTKLQQ--SSYHKQQEELDALKKTIEESE 756
Cdd:COG3206 226 SQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAEL-EAELAElsARYTPNHPDVIALRAQIAALR 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 757 EtlkntkEIQKKAEEKYEVLENKMKNAEAeRDRELKDAQKKLDfaktkadASSKKMKEKQQEVEAITLELEELKREHTSY 836
Cdd:COG3206 305 A------QLQQEAQRILASLEAELEALQA-REASLQAQLAQLE-------ARLAELPELEAELRRLEREVEVARELYESL 370
|
170 180
....*....|....*....|
gi 1952970885 837 KQQLEA--VNEAIKSYEVQI 854
Cdd:COG3206 371 LQRLEEarLAEALTVGNVRV 390
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
242-399 |
6.25e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 242 AEDTKERSAEELKEMQDKVVKLQEKLSENDKKIKALSHEIEELEK---GKDKEIGGKLR-------------------SL 299
Cdd:COG3883 35 AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAeieERREELGERARalyrsggsvsyldvllgseSF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 300 EDALAEAQRVNT---KSQSAFDLKKKNLASEENKRTELEKNMiedsRTLAAKEKEVKKITDGLNALQEASNKDAEALAAA 376
Cdd:COG3883 115 SDFLDRLSALSKiadADADLLEELKADKAELEAKKAELEAKL----AELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190
|
170 180
....*....|....*....|...
gi 1952970885 377 QQHFNAVSAGLSSNEDGAEATLA 399
Cdd:COG3883 191 EAAAEAQLAELEAELAAAEAAAA 213
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
668-984 |
6.51e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.83 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 668 RSQAASILTKFQELKNvqdELRIKENELQSLDEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEELDA 747
Cdd:COG5022 813 RSYLACIIKLQKTIKR---EKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKI 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 748 LKKTIEESEET--------LKNTKEIQKKAEEKYEVLENKMKN-AEAERDRELKDAQKKlDFAKTKADAS----SKKMKE 814
Cdd:COG5022 890 DVKSISSLKLVnleleseiIELKKSLSSDLIENLEFKTELIARlKKLLNNIDLEEGPSI-EYVKLPELNKlhevESKLKE 968
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 815 KQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYEVQIEAMAVEVAKNKESVNKAQE---------EVTKQKEVIIAQ 885
Cdd:COG5022 969 TSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAElqsaskiisSESTELSILKPL 1048
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 886 DNVIKAKYAEVAVHKEQNNDSQLKiKELDHNISKHKREAEDAASKVSKmlkdydwINAEKHLFGQPNSAYD-FKTNNPKE 964
Cdd:COG5022 1049 QKLKGLLLLENNQLQARYKALKLR-RENSLLDDKQLYQLESTENLLKT-------INVKDLEVTNRNLVKPaNVLQFIVA 1120
|
330 340
....*....|....*....|
gi 1952970885 965 AGQRLQKLQEMKEKLGRNVN 984
Cdd:COG5022 1121 QMIKLNLLQEISKFLSQLVN 1140
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
794-870 |
6.88e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 6.88e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952970885 794 AQKKLDFAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYEVQIEAMAVEVAKNKESVNK 870
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
756-928 |
7.08e-03 |
|
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: 40.21 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 756 EETLKNTKEIQKKAEEKYEVLEnKMKNAEAERDRELKDAQKKLDFAKtKADASSKKMKEKQQEVEaitlelEELKREHTS 835
Cdd:TIGR02794 60 KPAAKKEQERQKKLEQQAEEAE-KQRAAEQARQKELEQRAAAEKAAK-QAEQAAKQAEEKQKQAE------EAKAKQAAE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 836 YKQQLEAVNEAIKSYEVQIEAMAVEVAKNKESVNKAQEEVTKQKEViiaqdnviKAKYAEVAVHKEQNNDSQLKIKEldh 915
Cdd:TIGR02794 132 AKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEA--------EAKAKAEAEAKAKAEEAKAKAEA--- 200
|
170
....*....|...
gi 1952970885 916 niSKHKREAEDAA 928
Cdd:TIGR02794 201 --AKAKAAAEAAA 211
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
679-811 |
7.14e-03 |
|
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: 40.21 E-value: 7.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 679 QELKNVQDELRIKENELQSLDEELAglkNTAEKYRQLKQQWEMKTEEAdllqtKLQQSSYHKQQEELDALKKTIEESEET 758
Cdd:TIGR02794 80 AEKQRAAEQARQKELEQRAAAEKAA---KQAEQAAKQAEEKQKQAEEA-----KAKQAAEAKAKAEAEAERKAKEEAAKQ 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1952970885 759 LKNTKEIQKKAEEKYEVLENKMKNAEAERDRELKDAQKKLDFAKTKADASSKK 811
Cdd:TIGR02794 152 AEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAK 204
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
406-1027 |
8.75e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.39 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 406 KNDISKAQTEAKQAQMKLKHAQQELKTKQAEVKKMDSGYRKDQEALEAVKKLKEKLEAEMKKLNYEENKEEGLLEKrrqL 485
Cdd:TIGR04523 25 KNIANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINK---L 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 486 SRDISRLKEtyeallarfpniQFAYRDPEKNWNRNCVKGLVASLISVKDTSTTTALELVAGERLYNVVVDTEVTGKKLLE 565
Cdd:TIGR04523 102 NSDLSKINS------------EIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 566 KGELKRRYTIIPLNKISarciapETLRVAQNLVgpNNVHVALSLVEYKPELQKAMEF----------VFGTTFVCNNMDN 635
Cdd:TIGR04523 170 ELENELNLLEKEKLNIQ------KNIDKIKNKL--LKLELLLSNLKKKIQKNKSLESqiselkkqnnQLKDNIEKKQQEI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 636 AKKVAFDKRIMTRTVTLGGEVFDPHGTLSggarsqaasilTKFQELKNVQDELRIKENELQSLDEELAGLKNTAEK--YR 713
Cdd:TIGR04523 242 NEKTTEISNTQTQLNQLKDEQNKIKKQLS-----------EKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwNK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 714 QLKQQWEMKTEEADLLQTKLQQS--SYHKQQEELDALKKTIEESEetlKNTKEIQKKAEEKYEVLEnKMKNAEAERDREL 791
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNnkIISQLNEQISQLKKELTNSE---SENSEKQRELEEKQNEIE-KLKKENQSYKQEI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 792 KDAQKKLDFAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIK---------------------SY 850
Cdd:TIGR04523 387 KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKdltnqdsvkeliiknldntreSL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 851 EVQIEAMAVEVAKNKESVNKAQEEVTKQKEVIIAQDNVIKAKYAEVAVHKEQNNDSQLKIKELDHNISKHKREAEDAASK 930
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 931 VSKMLKDYDWINAEKHLFGQPNSAYDFKTNNPKEAGQRLQKLQEMKEKLGRNVNMRamNVLTEAEERYNDLMKKKRIVEN 1010
Cdd:TIGR04523 547 LNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLI--KEIEEKEKKISSLEKELEKAKK 624
|
650
....*....|....*..
gi 1952970885 1011 DKSKILATIEDLDQKKN 1027
Cdd:TIGR04523 625 ENEKLSSIIKNIKSKKN 641
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
715-939 |
8.88e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 40.42 E-value: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 715 LKQQWEMKTEEAD--LLQTKLQQSSYHKQQEELDALKKTIEESEETLKNTKEIQKKAEEKYEVLENKMKNAEAERD---- 788
Cdd:TIGR01612 1470 LKIKKDNATNDHDfnINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAKTKKDseii 1549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 789 -RELKDAQKKLDFaktKADASSKKMKEKQQevEAITLELEELKREHTsykqqleavNEAIKSYEVQIEAMAVEVAKNKEs 867
Cdd:TIGR01612 1550 iKEIKDAHKKFIL---EAEKSEQKIKEIKK--EKFRIEDDAAKNDKS---------NKAAIDIQLSLENFENKFLKISD- 1614
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952970885 868 VNKAQEEVTKQKEVIIAQDNVIKAKYAEVAVHKEQNNDSQLK-----IKELDHNISKHKREAEDAASKVSKMLKDYD 939
Cdd:TIGR01612 1615 IKKKINDCLKETESIEKKISSFSIDSQDTELKENGDNLNSLQeflesLKDQKKNIEDKKKELDELDSEIEKIEIDVD 1691
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
698-842 |
8.91e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.06 E-value: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952970885 698 LDEeLAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSS-----YHKQQEELDALK------KTIEESEETLKNTKEIQ 766
Cdd:COG0497 147 LDA-FAGLEELLEEYREAYRAWRALKKELEELRADEAERAreldlLRFQLEELEAAAlqpgeeEELEEERRRLSNAEKLR 225
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952970885 767 KKAEEKYEVLENKMKNAEAerdrELKDAQKKLDfaktKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEA 842
Cdd:COG0497 226 EALQEALEALSGGEGGALD----LLGQALRALE----RLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEF 293
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
27-49 |
9.22e-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: 38.38 E-value: 9.22e-03
|
| |
