|
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 ... |
3-1206 |
1.04e-106 |
|
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: 363.91 E-value: 1.04e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 3 HLELLLVENFKSWRGRQVIGPFRRFTCIIGPNGSGKSNVMDALSFVMGEKIA-NLRVKNIQELIHgaHIGKPISSSASVK 81
Cdd:pfam02463 1 YLKRIEIEGFKSYAKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAkSLRSERLSDLIH--SKSGAFVNSAEVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 82 IIYVEESGEEKT-------FARIIRGGCSEFRFNDNLVSRSVYIAELEKIGIIVKAQNCLVFQGTVESISVKKPKERTQF 154
Cdd:pfam02463 79 ITFDNEDHELPIdkeevsiRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 155 FEEISTSGELIGEYEEKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAERYQSLLEELKMNKIQLQLFQLYHNEKK 234
Cdd:pfam02463 159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 235 IHLLNTKLEHVNRDLSVKRESLSHHENIVKARKKEHGMLTRQLQQTEKELKSVETLLNQKRPQYIKAKENTSHHLKKLDV 314
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 315 AKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEEILHKKRDIELEASQLDRYKELKEQVRKKVATMTQQLE 394
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 395 KLQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEKTKSRMSEVN 474
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQ 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 475 EELNLIRSELQNAGIDTHEGKRQQKRAEVLEHLKRLYPDSVFGRLFDLCHPIHKKYQLAVTKVFGRFITAIVVASEKVAK 554
Cdd:pfam02463 479 LVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATAD 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 555 DCIRFLKEERAEPETFLALDYLDIKPINERLRELKGCKMVIDVIKTQFPQLKKVIQFVCGNGLVCETMEEARHIALSGpE 634
Cdd:pfam02463 559 EVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTK-L 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 635 RQKTVALDGTLFLKSGVISGGSSDLKYKARcwdekelknlrdrrsqkiqelkglMKTLRKETDLKQIQTLIQGTQTRLKY 714
Cdd:pfam02463 638 KESAKAKESGLRKGVSLEEGLAEKSEVKAS------------------------LSELTKELLEIQELQEKAESELAKEE 693
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 715 SQNELEMIKKKhlvafyqEQSQLQSELLNIESQCIMLSEGIKERQRRIKEFQEKIDKVEDDIFQhfCEEIGVENIREFEN 794
Cdd:pfam02463 694 ILRRQLEIKKK-------EQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEE--EEEKSRLKKEEKEE 764
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 795 KHVKRQQEIDQKRLEFEKQKTRLNVQLEYsrshlKKKLNKINTLKETIQKGSEDIDHLKKAEENCLQTVNELMAKQQQLK 874
Cdd:pfam02463 765 EKSELSLKEKELAEEREKTEKLKVEEEKE-----EKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELA 839
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 875 dirvtQNSSAEKVQTQIEEERKKFLAVDREVGKLQKEVVSIQTSLEQKRLEKHNLLLDCKVQDIEIILLSGSLDDIIEVE 954
Cdd:pfam02463 840 -----LELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEE 914
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 955 MGTEAESTQATIDIYekeeafEIDYSSLKEDLKALQSDQEIEAHLRLLLQQVASQEDILLKTAAPNLRALENLKTVRDKF 1034
Cdd:pfam02463 915 KENEIEERIKEEAEI------LLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEE 988
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 1035 QESTDAFEASRKEARLCRQEFEQVKKRRYDLFTQCFEHVSISIDQIYKKLCRNNSAQAFLSPENPEEPYLEGISYNCVAP 1114
Cdd:pfam02463 989 RYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEISARPP 1068
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 1115 GKRFMPMDNLSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTNIGKVSSYIKEQTqDQFQMIVISLKEEFYSRAD 1194
Cdd:pfam02463 1069 GKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELS-KNAQFIVISLREEMLEKAD 1147
|
1210
....*....|..
gi 613410199 1195 ALIGIYPEYDDC 1206
Cdd:pfam02463 1148 KLVGVTMVENGV 1159
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-1199 |
4.27e-90 |
|
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: 316.62 E-value: 4.27e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 3 HLELLLVENFKSWRGRQVIGPFRRFTCIIGPNGSGKSNVMDALSFVMGEK-IANLRVKNIQELIHGAHIGKPiSSSASVK 81
Cdd:TIGR02169 1 YIERIELENFKSFGKKKVIPFSKGFTVISGPNGSGKSNIGDAILFALGLSsSKAMRAERLSDLISNGKNGQS-GNEAYVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 82 IIYVEESGEEKTFARIIR-------GGCSEFRFNDNLVSRSVYIAELEKIGIIVKAQNcLVFQGTVESISVKKPKERTQF 154
Cdd:TIGR02169 80 VTFKNDDGKFPDELEVVRrlkvtddGKYSYYYLNGQRVRLSEIHDFLAAAGIYPEGYN-VVLQGDVTDFISMSPVERRKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 155 FEEISTsgelIGEYEEKKRKLQKAEEDAQFNFNKKKNIAAERRQA----KLEKEEAERYQSLLEELkmnkiqlQLFQLYH 230
Cdd:TIGR02169 159 IDEIAG----VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQlerlRREREKAERYQALLKEK-------REYEGYE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 231 NEKKIHLLNTKLEHVNRDLSVKRESLSHhenivkarkkehgmLTRQLQQTEKELKSVETLLNQKRPQYIKAKENTSHHLK 310
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEK--------------LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 311 KldvakkSIKDSEKQCSKQEDDIKALETELADLDAAwrsfEKQIEEEILHKKRDIELEASQLDRYKELKEQVRKKVATMT 390
Cdd:TIGR02169 294 E------KIGELEAEIASLERSIAEKERELEDAEER----LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 391 QQLEKLQ------------WEQKTDEERLAFE--KRRHGEVQGNLK--------------QIKEQIEDHKKRIEKLEEYT 442
Cdd:TIGR02169 364 EELEDLRaeleevdkefaeTRDELKDYREKLEklKREINELKRELDrlqeelqrlseelaDLNAAIAGIEAKINELEEEK 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 443 KTCMDCLKEKKQQEETLVDEIEKTKSRMSEVNEELNLIRSELQNAG--IDTHEGKRQQKRAEVL-----EHLKRLYPDSV 515
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQreLAEAEAQARASEERVRggravEEVLKASIQGV 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 516 FGRLFDLCHpIHKKYQLAVTKVFGRFITAIVVASEKVAKDCIRFLKEERAEPETFLALDYLDIKPINERLRELKGC-KMV 594
Cdd:TIGR02169 524 HGTVAQLGS-VGERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGViGFA 602
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 595 IDVIKTQfPQLKKVIQFVCGNGLVCETMEEARhiALSGPERqkTVALDGTLFLKSGVISGGSsdLKYKARCWDEKELKNL 674
Cdd:TIGR02169 603 VDLVEFD-PKYEPAFKYVFGDTLVVEDIEAAR--RLMGKYR--MVTLEGELFEKSGAMTGGS--RAPRGGILFSRSEPAE 675
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 675 RDRRSQKIQELKGLMKTLRKETD-----LKQIQTLIQGTQTRLKYSQNELEMIKKKH------LVAFYQEQSQLQSELLN 743
Cdd:TIGR02169 676 LQRLRERLEGLKRELSSLQSELRrienrLDELSQELSDASRKIGEIEKEIEQLEQEEeklkerLEELEEDLSSLEQEIEN 755
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 744 IESQCIMLSEGIKERQRRIKEFQEKIDKVEDDIFQHFCEEIGVEnIREFENKHvkrqQEIDQKRLEFEKQKTRLNVQLEY 823
Cdd:TIGR02169 756 VKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAE-LSKLEEEV----SRIEARLREIEQKLNRLTLEKEY 830
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 824 SRSHLKKKLNKINTLKETIQKGSEDIDHLKKAEENCLQTVNELMAKQQQLkdirvtqnssaEKVQTQIEEERKKflaVDR 903
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL-----------ESRLGDLKKERDE---LEA 896
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 904 EVGKLQKEVVSIQTSLEQKRLekhnLLLDCKVQdieiillsgslddiievemgteAESTQATIDIYEKEEAFEIDYSSLK 983
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRK----RLSELKAK----------------------LEALEEELSEIEDPKGEDEEIPEEE 950
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 984 EDLKALQSD-QEIEAHLRLLlqqvasqEDIllktaapNLRALENLKTV---RDKFQESTDAFEASRKEARLCRQEFEQVK 1059
Cdd:TIGR02169 951 LSLEDVQAElQRVEEEIRAL-------EPV-------NMLAIQEYEEVlkrLDELKEKRAKLEEERKAILERIEEYEKKK 1016
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 1060 KrryDLFTQCFEHVSISIDQIYKKLcrnNSAQAFLSPENPEEPYLEGISYNCVAPGKRFMPMDNLSGGEKCVAALALLFA 1139
Cdd:TIGR02169 1017 R---EVFMEAFEAINENFNEIFAEL---SGGTGELILENPDDPFAGGLELSAKPKGKPVQRLEAMSGGEKSLTALSFIFA 1090
|
1210 1220 1230 1240 1250 1260
....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 1140 VHSFRPAPFFVLDEVDAALDNTNIGKVSSYIKEQTQDQfQMIVISLKEEFYSRADALIGI 1199
Cdd:TIGR02169 1091 IQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEA-QFIVVSLRSPMIEYADRAIGV 1149
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
4-148 |
7.99e-80 |
|
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: 262.12 E-value: 7.99e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 4 LELLLVENFKSWRGRQVIGPFRRFTCIIGPNGSGKSNVMDALSFVMGEKIANLRVKNIQELIHGAHIGKPISSSASVKII 83
Cdd:cd03275 1 LKRLELENFKSYKGRHVIGPFDRFTCIIGPNGSGKSNLMDAISFVLGEKSSHLRSKNLKDLIYRARVGKPDSNSAYVTAV 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613410199 84 YVEESGEEKTFARIIRGGCSEFRFNDNLVSRSVYIAELEKIGIIVKAQNCLVFQGTVESISVKKP 148
Cdd:cd03275 81 YEDDDGEEKTFRRIITGGSSSYRINGKVVSLKEYNEELEKINILVKARNFLVFQGDVESIASKNP 145
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
12-1199 |
5.40e-78 |
|
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: 281.17 E-value: 5.40e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 12 FKSWRGRQVIGPFRRFTCIIGPNGSGKSNVMDALSFVMGE-KIANLRVKNIQELIHGAHIGKPISSSASVKIIYVEESGE 90
Cdd:TIGR02168 10 FKSFADPTTINFDKGITGIVGPNGCGKSNIVDAIRWVLGEqSAKALRGGKMEDVIFNGSETRKPLSLAEVELVFDNSDGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 91 EKTFA--------RIIRGGCSEFRFNDNLVsRSVYIAEL--------EKIGIIVkaqnclvfQGTVESISVKKPKERTQF 154
Cdd:TIGR02168 90 LPGADyseisitrRLYRDGESEYFINGQPC-RLKDIQDLfldtglgkRSYSIIE--------QGKISEIIEAKPEERRAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 155 FEEisTSGelIGEYEEKKRKLQKAEEDAQFNFNKKKNIAAE--RRQAKLEK--EEAERYQSLLEELKMNKIQLQLFQLYH 230
Cdd:TIGR02168 161 FEE--AAG--ISKYKERRKETERKLERTRENLDRLEDILNEleRQLKSLERqaEKAERYKELKAELRELELALLVLRLEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 231 NEKKIHLLNTKLEHVNRDLSVKRESLSHHENIVKARKKEHGMLTRQLQQTEKELKSVETLLNQKRPQYIKAKENTSHHLK 310
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 311 KLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEeilhKKRDIELEASQLDRYKELKEQVRKKVATMT 390
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE----LEAELEELESRLEELEEQLETLRSKVAQLE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 391 QQLEKLQWEQKTDEERLAFEKRRHG----EVQGNLKQIKE-QIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEK 465
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRErlqqEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 466 TKSRMSEVNEELNLIRSELQN-AGIDTHEGKRQQKRAEVLEHLKRLypDSVFGRLFDLCHpIHKKYQLAVTKVFGRFITA 544
Cdd:TIGR02168 473 AEQALDAAERELAQLQARLDSlERLQENLEGFSEGVKALLKNQSGL--SGILGVLSELIS-VDEGYEAAIEAALGGRLQA 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 545 IVVASEKVAKDCIRFLKEERAEPETFLALDYLDIKPIN----ERLRELKGCKMVIDVIKTQFPQLKKVIQFVCGNGLVCE 620
Cdd:TIGR02168 550 VVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQgndrEILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVD 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 621 TMEEARHIALSGPERQKTVALDGTLFLKSGVISGGSSdlkykarcwdekELKNLRDRRSQKIQELKGLMKTLrkETDLKQ 700
Cdd:TIGR02168 630 DLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSA------------KTNSSILERRREIEELEEKIEEL--EEKIAE 695
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 701 IQTLIQGTQTRLKYSQNELEMIKKKhLVAFYQEQSQLQSELLNIESQCIMLSEGIKERQRRIKEFQEKIDKVEDDIFQHF 780
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKE-LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 781 ceeigvENIREFENKHVKRQQEIDQKRLEFEKQKTRLnvqleysrshlKKKLNKINTLKETIQKGSEDIDHLKKAEENCL 860
Cdd:TIGR02168 775 ------EELAEAEAEIEELEAQIEQLKEELKALREAL-----------DELRAELTLLNEEAANLRERLESLERRIAATE 837
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 861 QTVNELMAKQQQLKDIRVTQNSSAEKVQTQIEEERKKFLAVDREVGKLQKEVVSIQTSLEQKRLEKHNLLLDCKVQDIEI 940
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 941 ILLSGSLDDIIEVEMGTEAEstqatidIYEKEEAFEIDYSSLKEDLKALQSD-----QEIEAHLRLLLQQVASQEDIllk 1015
Cdd:TIGR02168 918 EELREKLAQLELRLEGLEVR-------IDNLQERLSEEYSLTLEEAEALENKieddeEEARRRLKRLENKIKELGPV--- 987
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 1016 taapNLRALENLKTVRDKF----QESTDAFEASRKEARLCRQEFEQVKKRrydlFTQCFEHVSISIDQIYKKLCRNNSAQ 1091
Cdd:TIGR02168 988 ----NLAAIEEYEELKERYdfltAQKEDLTEAKETLEEAIEEIDREARER----FKDTFDQVNENFQRVFPKLFGGGEAE 1059
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 1092 -AFLSPENPEEpylEGISYNCVAPGKRFMPMDNLSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTNIGKVSSYI 1170
Cdd:TIGR02168 1060 lRLTDPEDLLE---AGIEIFAQPPGKKNQNLSLLSGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDDANVERFANLL 1136
|
1210 1220
....*....|....*....|....*....
gi 613410199 1171 KEQTqDQFQMIVISLKEEFYSRADALIGI 1199
Cdd:TIGR02168 1137 KEFS-KNTQFIVITHNKGTMEVADQLYGV 1164
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1113-1216 |
6.25e-65 |
|
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: 220.14 E-value: 6.25e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 1113 APGKRFMPMDNLSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTNIGKVSSYIKEQTQDQFQMIVISLKEEFYSR 1192
Cdd:cd03275 145 PPGKRFRDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAGPNFQFIVISLKEEFFSK 224
|
90 100
....*....|....*....|....
gi 613410199 1193 ADALIGIYPEYdDCMFSRVLTLDL 1216
Cdd:cd03275 225 ADALVGVYRDQ-ECNSSKVLTLDL 247
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-771 |
8.76e-46 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 179.75 E-value: 8.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 3 HLELLLVENFKSWRGRQVIgPFRR-FTCIIGPNGSGKSNVMDALSFVMGE-KIANLRVKNIQELIH-GAHIGKPiSSSAS 79
Cdd:COG1196 2 RLKRLELAGFKSFADPTTI-PFEPgITAIVGPNGSGKSNIVDAIRWVLGEqSAKSLRGGKMEDVIFaGSSSRKP-LGRAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 80 VKIIYVEESG------EEKTFARII-RGGCSEFRFNDNLVSRSVyIAEL-EKIGIIVKAQNcLVFQGTVESISVKKPKER 151
Cdd:COG1196 80 VSLTFDNSDGtlpidyDEVTITRRLyRSGESEYYINGKPCRLKD-IQDLfLDTGLGPESYS-IIGQGMIDRIIEAKPEER 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 152 TQFFEEIStsGelIGEYEEKK----RKLQKAEEdaqfNFNKKKNIAAE--RRQAKLEK--EEAERYQSLLEELKMNKIQL 223
Cdd:COG1196 158 RAIIEEAA--G--ISKYKERKeeaeRKLEATEE----NLERLEDILGEleRQLEPLERqaEKAERYRELKEELKELEAEL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 224 QLFQLYHNEKKIHLLNTKLEHVNRDLSVKRESLSHHENIVKARKKEHGMLTRQLQQTEKELKSVETLLNQKRPQYIKAKE 303
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 304 NTSHHLKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEEILHKKRDIELEASQLDRYKELKEQVR 383
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 384 KKVATMTQQLEKLQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEI 463
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 464 EKTKSRMSEVNEELNLI-----RSELQNAGIDTHEGKRQQKRAEVLEHLKRLYPDSVFGRLFDLchpihKKYQLAVTKVF 538
Cdd:COG1196 470 EEAALLEAALAELLEELaeaaaRLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVE-----AAYEAALEAAL 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 539 GRFITAIVVASEKVAKDCIRFLKEERAEPETFLALD----YLDIKPINERLRELKGCKMVIDVIKTQFPQLKKVIQFVCG 614
Cdd:COG1196 545 AAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDkiraRAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLG 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 615 NGLVCETMEEARHIALSGPERQKTVALDGTLFLKSGVISGGSSDLKYKARcwdEKELKNLRDRRSQKIQELKGLMKTLRK 694
Cdd:COG1196 625 RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL---LEAEAELEELAERLAEEELELEEALLA 701
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613410199 695 ETDLKQIQTLIQGTQTRLKYSQNELEMIKKKHLVAFYQEQSQLQSELLNIESQCIMLSEGIKERQRRIKEFQEKIDK 771
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1113-1199 |
2.39e-28 |
|
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: 113.33 E-value: 2.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 1113 APGKRFMPMDNLSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTNIGKVSSYIKEQTqDQFQMIVISLKEEFYSR 1192
Cdd:cd03278 103 APGKKVQRLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFS-KETQFIVITHRKGTMEA 181
|
....*..
gi 613410199 1193 ADALIGI 1199
Cdd:cd03278 182 ADRLYGV 188
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
513-628 |
8.61e-27 |
|
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: 106.16 E-value: 8.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 513 DSVFGRLFDLCHpIHKKYQLAVTKVFGRFITAIVVASEKVAKDCIRFLKEERAEPETFLALDYLDIKPI-NERLRELK-- 589
Cdd:smart00968 1 PGVLGRVADLIS-VDPKYETALEAALGGRLQAVVVDTEETAKKAIEFLKKNRLGRATFLPLDKIKPRSPaGSKLREALlp 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 613410199 590 ---GCKMVIDVIKTQfPQLKKVIQFVCGNGLVCETMEEARHI 628
Cdd:smart00968 80 epgFVGPAIDLVEYD-PELRPALEYLLGNTLVVDDLETARRL 120
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1114-1204 |
1.03e-25 |
|
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: 106.23 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 1114 PGKRFMPMDNLSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTNIGKVSSYIKEQTQDQfQMIVISLKEEFYSRA 1193
Cdd:cd03274 118 PKKSWKNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNA-QFIVISLRNNMFELA 196
|
90
....*....|.
gi 613410199 1194 DALIGIYPEYD 1204
Cdd:cd03274 197 DRLVGIYKTNN 207
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1124-1200 |
1.53e-23 |
|
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: 98.92 E-value: 1.53e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613410199 1124 LSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTNIGKVSSYIKEQTQDQFQMIVISLKEEFYSRADALIGIY 1200
Cdd:cd03239 95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHTSQFIVITLKKEMFENADKLIGVL 171
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
4-144 |
3.40e-21 |
|
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: 93.13 E-value: 3.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 4 LELLLVENFKSWRGRQVIGPF-RRFTCIIGPNGSGKSNVMDALSFVMGEKIANLRVKNIQELIHGAHiGKPISSSASVKI 82
Cdd:cd03274 3 ITKLVLENFKSYAGEQVIGPFhKSFSAIVGPNGSGKSNVIDSMLFVFGFRASKMRQKKLSDLIHNSA-GHPNLDSCSVEV 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613410199 83 iyveesgeekTFARIIrggcsefrfNDNLvsrsvyiaeLEKIGIIVKAQNCLVFQGTVESIS 144
Cdd:cd03274 82 ----------HFQEII---------DKPL---------LKSKGIDLDHNRFLILQGEVEQIA 115
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
513-629 |
1.26e-20 |
|
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: 88.47 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 513 DSVFGRLFDLCHpIHKKYQLAVTKVFGRFITAIVVASEKVAKDCIRFLKEERAEPETFLALDYLDIKPINERLRELKGCK 592
Cdd:pfam06470 2 KGVLGRLADLIE-VDEGYEKAVEAALGGRLQAVVVDDEDDAKRAIEFLKKNKLGRATFLPLDRLKPRPRRPGADLKGGAG 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 613410199 593 MVIDVIKTQfPQLKKVIQFVCGNGLVCETMEEARHIA 629
Cdd:pfam06470 81 PLLDLVEYD-DEYRKALRYLLGNTLVVDDLDEALELA 116
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1124-1202 |
4.69e-20 |
|
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: 88.57 E-value: 4.69e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613410199 1124 LSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTNIGKVSSYIKEQTQDQFQMIVISLKEEFYSRADALIGIYPE 1202
Cdd:cd03227 78 LSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIKKV 156
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
4-95 |
7.22e-19 |
|
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: 85.44 E-value: 7.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 4 LELLLVENFKSWRGRQVIGPFRRFTCIIGPNGSGKSNVMDALSFVMGEKIANLRVKNIQELIHGAhiGKPISSSASVKII 83
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSNSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFLAGGG--VKAGINSASVEIT 78
|
90 100
....*....|....*....|....*
gi 613410199 84 Y-----------VEE--SGEEKTFA 95
Cdd:cd03239 79 FdksyflvlqgkVEQilSGGEKSLS 103
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
4-83 |
8.56e-18 |
|
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: 82.90 E-value: 8.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 4 LELLLVENFKSWRGRQVIgPF-RRFTCIIGPNGSGKSNVMDALSFVMGEKIA-NLRVKNIQELIHGAHIGKPISSSASVK 81
Cdd:cd03278 1 LKKLELKGFKSFADKTTI-PFpPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAkSLRGEKMSDVIFAGSETRKPANFAEVT 79
|
..
gi 613410199 82 II 83
Cdd:cd03278 80 LT 81
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
3-140 |
1.25e-17 |
|
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: 83.89 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 3 HLELLLVENFKSWRGRQVIGPF-RRFTCIIGPNGSGKSNVMDALSFVMG-EKIANLRVKNIQELIHgaHIGKPISSSASV 80
Cdd:cd03273 2 HIKEIILDGFKSYATRTVISGFdPQFNAITGLNGSGKSNILDAICFVLGiTNLSTVRASNLQDLIY--KRGQAGITKASV 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613410199 81 KIIYVEES------GEEK----TFARIIRGGCSEFRFNDNLVSRSVYIAEL-EKIGIIVKAQNCLVFQGTV 140
Cdd:cd03273 80 TIVFDNSDksqspiGFENypeiTVTRQIVLGGTNKYLINGHRAQQQRVQDLfQSVQLNVNNPHFLIMQGRI 150
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1124-1196 |
7.86e-15 |
|
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: 75.80 E-value: 7.86e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613410199 1124 LSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALD--NT-NIGKVssyIKEQ-TQDQFqmIVISLKEEFYSRADAL 1196
Cdd:cd03273 167 LSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDlsHTqNIGRM---IKTHfKGSQF--IVVSLKEGMFNNANVL 238
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1121-1199 |
3.86e-12 |
|
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: 67.67 E-value: 3.86e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613410199 1121 MDNLSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTNIGKVSSYIKEQTqDQFQMIVISLKEEFYSRADALIGI 1199
Cdd:cd03272 156 MQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELS-DGAQFITTTFRPELLEVADKFYGV 233
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
7-159 |
4.70e-12 |
|
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: 67.29 E-value: 4.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 7 LLVENFKSWRGRQVIGPFR-RFTCIIGPNGSGKSNVMDALSFVMGEKIANLRVKNIQELIH-GAhigKPISSSASVKII- 83
Cdd:cd03272 4 VIIQGFKSYKDQTVIEPFSpKHNVVVGRNGSGKSNFFAAIRFVLSDEYTHLREEQRQALLHeGS---GPSVMSAYVEIIf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 84 -----YVEESGEEKTFARIIRGGCSEFRFNDNLVSRSVYIAELEKIGI-------IVKaqnclvfQGTVESISVKKPKEr 151
Cdd:cd03272 81 dnsdnRFPIDKEEVRLRRTIGLKKDEYFLDKKNVTKNDVMNLLESAGFsrsnpyyIVP-------QGKINSLTNMKQDE- 152
|
....*...
gi 613410199 152 TQFFEEIS 159
Cdd:cd03272 153 QQEMQQLS 160
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
145-509 |
2.20e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.55 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 145 VKKPKERTQFFEEISTSGELIGEYEEKKRKL----QKAEEDAQFNFNKKKniAAERRQA---KLEKEEAERYQSLLEELK 217
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADELKKAAAAKKKAdeakKKAEEKKKADEAKKK--AEEAKKAdeaKKKAEEAKKAEEAKKKAE 1467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 218 MNKIQLQLFQLYHNEKKIHLLNTKLEHVNRDLSVKRESLSHHENIVKARKKEHGMLTRQLQQTEK-----ELKSVETLln 292
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEakkadEAKKAEEK-- 1545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 293 QKRPQYIKAKE-NTSHHLKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSfEKQIEEEILHKKRDIELEASQ 371
Cdd:PTZ00121 1546 KKADELKKAEElKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE-EKKMKAEEAKKAEEAKIKAEE 1624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 372 LDRYKELK---EQVRKKVATMTQQLEKLQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDC 448
Cdd:PTZ00121 1625 LKKAEEEKkkvEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA 1704
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613410199 449 LKEKKQQEEtlvdeiEKTKSRMSEVNEELNLIRSElqNAGIDTHEGKRQQKRAEVLEHLKR 509
Cdd:PTZ00121 1705 EELKKKEAE------EKKKAEELKKAEEENKIKAE--EAKKEAEEDKKKAEEAKKDEEEKK 1757
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
11-97 |
1.73e-09 |
|
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: 58.14 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 11 NFKSWRGRQVIGPFR-RFTCIIGPNGSGKSNVMDALSFVMGEKIANLRVKNiqelihGAHIGkPISSSASVKIIY--VEE 87
Cdd:cd03227 6 RFPSYFVPNDVTFGEgSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRS------GVKAG-CIVAAVSAELIFtrLQL 78
|
90
....*....|
gi 613410199 88 SGEEKTFARI 97
Cdd:cd03227 79 SGGEKELSAL 88
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
244-857 |
2.38e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 244 HVNRDLSVKRESLSHHENIvKARKKEHGmltRQLQQTEKELKSvetlLNQKRPQYIKAKENTSHHLKKLDVAKKSIKDSE 323
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENI-EELIKEKE---KELEEVLREINE----ISSELPELREELEKLEKEVKELEELKEEIEELE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 324 KQCSKQEDDIKALETELADLDAAWRSFEKQIE--EEILHKKRDIELEASQLDRYKELKEQVRKKVATMTQQLEKLQWEQK 401
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEelEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 402 TDEERLA---FEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEY--TKTCMDCLKEKKQQE--ETLVDEIEKTKSRMSEVN 474
Cdd:PRK03918 325 GIEERIKeleEKEERLEELKKKLKELEKRLEELEERHELYEEAkaKKEELERLKKRLTGLtpEKLEKELEELEKAKEEIE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 475 EELNLIRSELqnAGIDThEGKRQQKRAEVLEHLKRLYPdsVFGRLFDLCH--PIHKKYQLAVTKVFGRFITAivvasekv 552
Cdd:PRK03918 405 EEISKITARI--GELKK-EIKELKKAIEELKKAKGKCP--VCGRELTEEHrkELLEEYTAELKRIEKELKEI-------- 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 553 aKDCIRFLKEERAEPETFLaldyldikpinERLRELKGCKMVIDVIKTQFPQLKKViqfvcgnglVCETMEEARHialsg 632
Cdd:PRK03918 472 -EEKERKLRKELRELEKVL-----------KKESELIKLKELAEQLKELEEKLKKY---------NLEELEKKAE----- 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 633 pERQKTVALDGTLflkSGVISGGSSDLKykarcwDEKELKNLRDRRSQKIQELKGLMKTLrketdLKQIQTLIQGTQTRL 712
Cdd:PRK03918 526 -EYEKLKEKLIKL---KGEIKSLKKELE------KLEELKKKLAELEKKLDELEEELAEL-----LKELEELGFESVEEL 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 713 KYSQNELEMIKKKHLVAFYQEqSQLQSELLNIESQCIMLSEGIKERQRRIKEFQEKIDKVEDdifqhFCEEIGVENIREF 792
Cdd:PRK03918 591 EERLKELEPFYNEYLELKDAE-KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE-----LEKKYSEEEYEEL 664
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613410199 793 ENKHVKRQQEIDQKRLEFEkqktrlnvQLEYSRSHLKKKLNKINTLKETIQKGSEDIDHLKKAEE 857
Cdd:PRK03918 665 REEYLELSRELAGLRAELE--------ELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE 721
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
145-476 |
9.17e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 9.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 145 VKKPKERTQFFEEISTSGELIGEYEEKKRK---LQKAEEDAQFNFNKKKniAAERRQAKLEKEEAERYQSLLEELKMNKi 221
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAKKKAEEAKKAeeaKKKAEEAKKADEAKKK--AEEAKKADEAKKKAEEAKKKADEAKKAA- 1506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 222 qlqlfqlyHNEKKIHLLNTKLEHVNRDLSVKRESLSHHENIVKARKKEHGMLTRQLQQTEK--ELKSVEtllnQKRpqyi 299
Cdd:PTZ00121 1507 --------EAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKaeEKKKAE----EAK---- 1570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 300 KAKENTSHHLKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEEILHKKRDIEL---------EAS 370
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLkkkeaeekkKAE 1650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 371 QLDRYKEL----KEQVRKKVATMTQQLEKLQWEQKtDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKL---EEYTK 443
Cdd:PTZ00121 1651 ELKKAEEEnkikAAEEAKKAEEDKKKAEEAKKAEE-DEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELkkaEEENK 1729
|
330 340 350
....*....|....*....|....*....|....*...
gi 613410199 444 TCMDCLK-----EKKQQEETLVDEIEKTKSRMSEVNEE 476
Cdd:PTZ00121 1730 IKAEEAKkeaeeDKKKAEEAKKDEEEKKKIAHLKKEEE 1767
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
4-48 |
1.45e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 58.40 E-value: 1.45e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 613410199 4 LELLLVENFKSWRgrQVIGPFRRFTCIIGPNGSGKSNVMDALSFV 48
Cdd:COG4637 2 ITRIRIKNFKSLR--DLELPLGPLTVLIGANGSGKSNLLDALRFL 44
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
276-476 |
1.59e-08 |
|
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: 58.24 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 276 QLQQTEKELKSVETLLNQKRPQYIKAKENTSHHLKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIE 355
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 356 E---------------------EILHKKRDIELEASQLDRYKELKEQVRKKVATMTQQLEKLQWEQKTDEERLAFEKRRH 414
Cdd:COG4942 101 AqkeelaellralyrlgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613410199 415 GEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEKTKSRMSEVNEE 476
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
330-511 |
1.67e-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: 56.47 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 330 EDDIKALEtELADLDAAWRSFEKQIEE---EILHKKRDIELEASQLDRYKELKEQVRKKVATMTQQLEKLQWEQKTDEER 406
Cdd:COG1579 3 PEDLRALL-DLQELDSELDRLEHRLKElpaELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 407 LafekrrhGEVQGN--LKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEKTKSRMSEVNEELNLIRSEL 484
Cdd:COG1579 82 L-------GNVRNNkeYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
170 180
....*....|....*....|....*..
gi 613410199 485 QNAgIDTHEGKRQQKRAEVLEHLKRLY 511
Cdd:COG1579 155 EAE-LEELEAEREELAAKIPPELLALY 180
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
169-469 |
3.13e-08 |
|
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: 58.43 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 169 EEKKRKLQKAEEDAQFNFNKKKNIAAER-RQAKL--EKEEAERYQSLLE-ELKMNKIQLQLFQ--LYHNEKkihllntkL 242
Cdd:COG3096 278 NERRELSERALELRRELFGARRQLAEEQyRLVEMarELEELSARESDLEqDYQAASDHLNLVQtaLRQQEK--------I 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 243 EHVNRDLSVKRESLSHHENIVKARKKEHGMLTRQLQQTEKELKSVETLL---------NQKRP-QY---IKAKENTSHHL 309
Cdd:COG3096 350 ERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLadyqqaldvQQTRAiQYqqaVQALEKARALC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 310 KKLDVAKKSIKDSEKQCSKQEDDIK----ALETELADLDAAWRSFEKQIEeeiLHKKRDIELEASQ--------LDRYKE 377
Cdd:COG3096 430 GLPDLTPENAEDYLAAFRAKEQQATeevlELEQKLSVADAARRQFEKAYE---LVCKIAGEVERSQawqtarelLRRYRS 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 378 LKEQVrKKVATMTQQLEKL--QWEQKTDEERLA--FEKRRHGEVQGNLkQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKK 453
Cdd:COG3096 507 QQALA-QRLQQLRAQLAELeqRLRQQQNAERLLeeFCQRIGQQLDAAE-ELEELLAELEAQLEELEEQAAEAVEQRSELR 584
|
330
....*....|....*.
gi 613410199 454 QQEETLVDEIEKTKSR 469
Cdd:COG3096 585 QQLEQLRARIKELAAR 600
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
9-214 |
3.60e-08 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 55.02 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 9 VENFKSWRGRQVIgPFRR-FTCIIGPNGSGKSNVMDALSFVMGEKiANLRVKNIQELIHGAhigkpiSSSASVKIIYvee 87
Cdd:COG0419 7 LENFRSYRDTETI-DFDDgLNLIVGPNGAGKSTILEAIRYALYGK-ARSRSKLRSDLINVG------SEEASVELEF--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 88 SGEEKTFaRIIRggcsefrfndnlvsrsvyiaelekigiivkaqnclvFQGTVESISVKKPKERTQFFEEIStsgeLIGE 167
Cdd:COG0419 76 EHGGKRY-RIER------------------------------------RQGEFAEFLEAKPSERKEALKRLL----GLEI 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 613410199 168 YEEKKRKLQKAEEDAQfnfnkkkniAAERRQAKLEKEEAERYQSLLE 214
Cdd:COG0419 115 YEELKERLKELEEALE---------SALEELAELQKLKQEILAQLSG 152
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
298-929 |
4.42e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 4.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 298 YIKAKENTSHHLKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLdaawrsfEKQIEEeILHKKRDIELEASQLDRYKE 377
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEV-------LREINE-ISSELPELREELEKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 378 LKEQVRKKVATMTQQLEKLQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKtcmdcLKEKKQQEE 457
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK-----LSEFYEEYL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 458 TLVDEIEKTKSRMSevnEELNLIRSELQNAGIDTHE-GKRQQKRAEVLEHLKRLYPDSvfgRLFDLCHPIHKKYQLAVTK 536
Cdd:PRK03918 307 DELREIEKRLSRLE---EEINGIEERIKELEEKEERlEELKKKLKELEKRLEELEERH---ELYEEAKAKKEELERLKKR 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 537 VFGRFItaivvasEKVAKDcIRFLKEERAEPEtflaldyLDIKPINERLRELKGckmVIDVIKTQFPQLK--KVIQFVCG 614
Cdd:PRK03918 381 LTGLTP-------EKLEKE-LEELEKAKEEIE-------EEISKITARIGELKK---EIKELKKAIEELKkaKGKCPVCG 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 615 NglvcETMEEARHIALSgperqktvaldgtlflksgvisggssdlKYKARCWD-EKELKNLRDRRSQKIQELKGLMKTLR 693
Cdd:PRK03918 443 R----ELTEEHRKELLE----------------------------EYTAELKRiEKELKEIEEKERKLRKELRELEKVLK 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 694 KETDLKQIQTLIQgtqtRLKYSQNELEMIKKKHLVAFYQEQSQLQSELLNIESQCimlsEGIKERQRRIKEFQEKIDKVE 773
Cdd:PRK03918 491 KESELIKLKELAE----QLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEI----KSLKKELEKLEELKKKLAELE 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 774 DDIfqHFCEEIGVENIREFENKHVKRQQEIDQKRLEFEKQKTRLnVQLEYSRSHLKKKLNKINTLKETIQKGSEDIDHLK 853
Cdd:PRK03918 563 KKL--DELEEELAELLKELEELGFESVEELEERLKELEPFYNEY-LELKDAEKELEREEKELKKLEEELDKAFEELAETE 639
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613410199 854 KAEENCLQTVNELMAKQQQlkdirvtqnSSAEKVQTQIEEERKKFLAVDREVGKLQKEVVSIQTSLEQKRLEKHNL 929
Cdd:PRK03918 640 KRLEELRKELEELEKKYSE---------EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
146-499 |
1.53e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.80 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 146 KKPKERTQFFEEISTSGELIGEYEEKKRKLQKAEEDAQFNFNKKKN------------IAAERRQAKLEKE--EAERYQS 211
Cdd:TIGR04523 149 KKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNkllklelllsnlKKKIQKNKSLESQisELKKQNN 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 212 LLE---ELKMNKIQLQLFQLYHNEKKIHLLNTKLEHVNRDLSVKRESLSHHENIVKArkkehgmLTRQLQQTEKELksvE 288
Cdd:TIGR04523 229 QLKdniEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE-------LEKQLNQLKSEI---S 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 289 TLLNQKRPQYIKA-KENTSHHLKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEeilhKKRDIEL 367
Cdd:TIGR04523 299 DLNNQKEQDWNKElKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE----KQNEIEK 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 368 EASQLDRYKELKEQVRKKVATMTQQLEKLQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEE------- 440
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNqdsvkel 454
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 613410199 441 YTKTCMDCLKEKKQQEETLVDEIEKTKSRMSEVNEELNLIRSELQNAGIDTHEGKRQQK 499
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK 513
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
270-771 |
1.97e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 270 HGMLTRQLQQTEKELKSVetllnQKRPQYIKAKEntshhLKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAwrs 349
Cdd:COG4717 44 RAMLLERLEKEADELFKP-----QGRKPELNLKE-----LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAE--- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 350 fekqiEEEILHKKRDIELEASQLDRYKELkEQVRKKVATMTQQLEKLQWEQKTDEERLAfekrrhgevqgNLKQIKEQIE 429
Cdd:COG4717 111 -----LEELREELEKLEKLLQLLPLYQEL-EALEAELAELPERLEELEERLEELRELEE-----------ELEELEAELA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 430 DHKKRIEKLEEYTKTcmdclkEKKQQEETLVDEIEKTKSRMSEVNEELNLIRSELQNAGIDTHEGKRQQKRAEVLEHLKR 509
Cdd:COG4717 174 ELQEELEELLEQLSL------ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 510 LYPDS-VFGRLFDLCHPIHKKYQLAVTkvFGRFITAIVVASEKVAKDCIRFLKEERAEPETFLALDYLDIKPINERLREL 588
Cdd:COG4717 248 ARLLLlIAAALLALLGLGGSLLSLILT--IAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 589 KGCKMVIDVIKTQFPQLKKVIQFVCGNGLVCETMEEARHIALSGPERQKtvaldgtLFLKSGVISggSSDLKYKARCWDE 668
Cdd:COG4717 326 AALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAA-------LLAEAGVED--EEELRAALEQAEE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 669 -KELKNLRDRRSQKIQELKGLMKTLRKETDLKQIQTLIQGTQTRLKYSQNELEMIKkkhlvafyQEQSQLQSELLNIESQ 747
Cdd:COG4717 397 yQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELR--------EELAELEAELEQLEED 468
|
490 500
....*....|....*....|....
gi 613410199 748 cIMLSEGIKERQRRIKEFQEKIDK 771
Cdd:COG4717 469 -GELAELLQELEELKAELRELAEE 491
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
169-505 |
3.04e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 169 EEKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAERYQSLLEELKM----NKIQLQLFQLYHNEKKIHLLNTKLEH 244
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKaaaaKKKADEAKKKAEEKKKADEAKKKAEE 1442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 245 VNR--DLSVKRESLSHHENIVK----ARKKEHGMLTRQLQQTEKELKSVETLLNQKRPQYIKAKE--NTSHHLKKLDVAK 316
Cdd:PTZ00121 1443 AKKadEAKKKAEEAKKAEEAKKkaeeAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEakKKADEAKKAEEAK 1522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 317 KSIKDSEKQCSKQEDDI-KALETELADLDAAWRSFEKQIEEEILHKKRDIELEASQLDRYKELKEQVRKK----VATMTQ 391
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAkKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEArieeVMKLYE 1602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 392 QLEKLQWEQ--KTDEERLAFEK-RRHGEVQGNLKQIKEQIEDHKKRIEKL---EEYTKTCMDCLKEKKQQEETLVDEIEK 465
Cdd:PTZ00121 1603 EEKKMKAEEakKAEEAKIKAEElKKAEEEKKKVEQLKKKEAEEKKKAEELkkaEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 613410199 466 TKSRMSEVNEELNLIRSELQNAGIDTHEGKRQQKRAEVLE 505
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELK 1722
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
3-114 |
3.14e-07 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 54.01 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 3 HLELLLVENFKSWRgRQVIGPFRRFTCIIGPNGSGKSNVMDALSFV-MGEkiaNLRVKNIQELI-HGAhigkpisSSASV 80
Cdd:COG1195 1 RLKRLSLTNFRNYE-SLELEFSPGINVLVGPNGQGKTNLLEAIYLLaTGR---SFRTARDAELIrFGA-------DGFRV 69
|
90 100 110
....*....|....*....|....*....|....
gi 613410199 81 KIIYVEESGEEKTFARIIRGGCSEFRFNDNLVSR 114
Cdd:COG1195 70 RAEVERDGREVRLGLGLSRGGKKRVRINGKPVRR 103
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
156-477 |
4.47e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.26 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 156 EEISTSGELIGEYEEKKRKLQKAEEDAQFNFNKKKNIAAER----RQAKLEKEEAERYQSLLEELKmNKIQLQLFQLYHN 231
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLnnkyNDLKKQKEELENELNLLEKEK-LNIQKNIDKIKNK 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 232 EKKIHLLNTKLEHVNRDLSVKRESLSHHENIVKARKKEHGMLTRQLQQTEKELKSVETLLNQKRPQYIKAKENTSHHLKK 311
Cdd:TIGR04523 196 LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 312 LDVAKKSIKDSEKQCSKQEDDIKALETE-LADLDAAWRSFEKQIEEEILHKKRDIELEASQLDRYKELKEQVRKKVATMT 390
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQLKSEISDLNNQkEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 391 QQLEKLQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEKTKSRM 470
Cdd:TIGR04523 356 SENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETI 435
|
....*..
gi 613410199 471 SEVNEEL 477
Cdd:TIGR04523 436 IKNNSEI 442
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
194-431 |
5.38e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 5.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 194 AERRQAKLE--KEEAERYQSLLEELKMNKIQLQLFQLYHNEKKIHLLNTKLEHVNRDLSVKRESLSHHENIVKARKKEHG 271
Cdd:COG4913 247 AREQIELLEpiRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 272 MLTRQLQQtekelksvetllnqkrpqyikakentsHHLKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSfe 351
Cdd:COG4913 327 ELEAQIRG---------------------------NGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA-- 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 352 kqiEEEILHKKRdiELEASQLDRYKELKEQVRKKVATMTQQLEKLQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDH 431
Cdd:COG4913 378 ---SAEEFAALR--AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1124-1199 |
6.96e-07 |
|
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: 50.32 E-value: 6.96e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613410199 1124 LSGGEKCVAALALLFAvhsfRPAPFFVLDEVDAALDNTNIGKVSSYIKEQTQDQFQMIVISLKEEFYSRA-DALIGI 1199
Cdd:cd00267 81 LSGGQRQRVALARALL----LNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVL 153
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
18-893 |
7.52e-07 |
|
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: 53.90 E-value: 7.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 18 RQVIGPFRRFTCIIGPNGSGKSNVMDALSFVMGEKIANLRVKNiqELIHGAHIGKPISSSASVKIIYVEESGEEKTFARI 97
Cdd:TIGR00606 21 KQIIDFFSPLTILVGPNGAGKTTIIECLKYICTGDFPPGTKGN--TFVHDPKVAQETDVRAQIRLQFRDVNGEECAVVRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 98 I----RGGCSEFRFNDNLVSR---------SVYIAELEK-----IGIIVKAQNCLVFQGTVESI-SVKKPKERTQFFEEI 158
Cdd:TIGR00606 99 MvctqKTKKTEFKTLEGVITRykhgekvslSSKCAEIDRemishLGVSKAVLNNVIFCHQEDSNwPLSEGKALKQKFDEI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 159 STSGELIGEYE-------EKKRKLQKAEEDAQFNFNKKKNIAAERRQ--AKLEKEEAERYQSLLEELKMNKIQLQLFQLY 229
Cdd:TIGR00606 179 FSATRYIKALEtlrqvrqTQGQKVQEHQMELKYLKQYKEKACEIRDQitSKEAQLESSREIVKSYENELDPLKNRLKEIE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 230 HNEKKIHLLNTKL----------EHVNRDLSVKRESL------------SHHENIVKARKKEHGMLTRQLQQTEKELKsv 287
Cdd:TIGR00606 259 HNLSKIMKLDNEIkalksrkkqmEKDNSELELKMEKVfqgtdeqlndlyHNHQRTVREKERELVDCQRELEKLNKERR-- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 288 etLLNQKRPQYIkaKENTSHHLKKLDVAKKSIK-DSEKQCSKQEDDIKALETElADLDAAWRSFEKQIEEEILHKKRDIE 366
Cdd:TIGR00606 337 --LLNQEKTELL--VEQGRLQLQADRHQEHIRArDSLIQSLATRLELDGFERG-PFSERQIKNFHTLVIERQEDEAKTAA 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 367 LEASQLDRYKELKEQ------VRKKVATMTQQLEKLQWEQKTDEerLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEE 440
Cdd:TIGR00606 412 QLCADLQSKERLKQEqadeirDEKKGLGRTIELKKEILEKKQEE--LKFVIKELQQLEGSSDRILELDQELRKAERELSK 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 441 YTKTCM-DCLKEKKQQEETLVDEIEKTKSRMSEVNEELNLIRSELQNAGIDThegKRQQKRAEVLEHLKRLYPDSVFGRL 519
Cdd:TIGR00606 490 AEKNSLtETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLT---KDKMDKDEQIRKIKSRHSDELTSLL 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 520 FDLchpihkKYQLAVTKVFGRFITAIVVASEKVAKDCIRFLKEERAEPETFLALDYLD--IKPINERLRELKGCKMV--- 594
Cdd:TIGR00606 567 GYF------PNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEeqLSSYEDKLFDVCGSQDEesd 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 595 IDVIKTQFPQLKKVIQFVCGnglvcETMEEARHIALSGPERQKTVALDGTLFLKSGVISGGSSDLKYKARCWD------E 668
Cdd:TIGR00606 641 LERLKEEIEKSSKQRAMLAG-----ATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPdklkstE 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 669 KELKNLRDRRSQKIQELKGLMKTL-RKETDLKQIQTLIQGTQTRLKYSQNELEmikkkhlvafyQEQSQLQSELLNIESQ 747
Cdd:TIGR00606 716 SELKKKEKRRDEMLGLAPGRQSIIdLKEKEIPELRNKLQKVNRDIQRLKNDIE-----------EQETLLGTIMPEEESA 784
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 748 CIMLSE-GIKERqrrikeFQEKIDKVEDDIFQHFCEEIGVENIREFEnkHVKRQQEIDQKRLEFEKQKTRLNVQLEYSRS 826
Cdd:TIGR00606 785 KVCLTDvTIMER------FQMELKDVERKIAQQAAKLQGSDLDRTVQ--QVNQEKQEKQHELDTVVSKIELNRKLIQDQQ 856
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613410199 827 ----HLKKKLNKINTLKETIQKGSEDIDHLKKAEENCLQTVNELMAKQQQLKDIRVTQNSSAEKVQTQIEE 893
Cdd:TIGR00606 857 eqiqHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEE 927
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
259-896 |
9.03e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 9.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 259 HENIVKARKKEHgmLTRQLQQTEKELKSVETLLNQKRpqYIKAKENTSHHLKKLDVAKKSIKDSEKQCSKQEDDIKALET 338
Cdd:COG4913 241 HEALEDAREQIE--LLEPIRELAERYAAARERLAELE--YLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 339 ELADLDAAWRSFEKQI-----------EEEILHKKRDieleasqldrykelKEQVRKKVATMTQQLEKLQWEQKTDEERL 407
Cdd:COG4913 317 RLDALREELDELEAQIrgnggdrleqlEREIERLERE--------------LEERERRRARLEALLAALGLPLPASAEEF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 408 AfekrrhgEVQGNLKQIKEQIEDHKKRIEklEEYTKTcMDCLKEKKQQEETLVDEIEKTKSRMSEVNEELNLIRSEL-QN 486
Cdd:COG4913 383 A-------ALRAEAAALLEALEEELEALE--EALAEA-EAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALaEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 487 AGIDTHEgkrqqkraevlehLKrlypdsVFGRLFDLcHPIHKKYQLAVTKVFGRFITAIVVaSEKVAKDCIRFLKEERAE 566
Cdd:COG4913 453 LGLDEAE-------------LP------FVGELIEV-RPEEERWRGAIERVLGGFALTLLV-PPEHYAAALRWVNRLHLR 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 567 petfLALDYLDIKPINERLRELKG------CKMVIDV------IKTqfpQLKKVIQFVCgnglvCETMEEARH----IAL 630
Cdd:COG4913 512 ----GRLVYERVRTGLPDPERPRLdpdslaGKLDFKPhpfrawLEA---ELGRRFDYVC-----VDSPEELRRhpraITR 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 631 SGPERQKTVA--LDGTLFLKSGVISGGSSDLKYKARcwdEKELKNLRDRRSQ---KIQELKGLMKTLRKE-TDLKQIQTL 704
Cdd:COG4913 580 AGQVKGNGTRheKDDRRRIRSRYVLGFDNRAKLAAL---EAELAELEEELAEaeeRLEALEAELDALQERrEALQRLAEY 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 705 ------IQGTQTRLKYSQNELEMIKK--KHLVAFYQEQSQLQSELLNIESQCIMLSEGIKERQRRIKEFQEKIDKVEdDI 776
Cdd:COG4913 657 swdeidVASAEREIAELEAELERLDAssDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ-DR 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 777 FQHFCEEIGVENIREFENK--HVKRQQEIDQKRLEFEKQKTRLNVQLEYSRSHLKKKLNKINTL-KETIQKGSEDIDHLK 853
Cdd:COG4913 736 LEAAEDLARLELRALLEERfaAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREwPAETADLDADLESLP 815
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 613410199 854 KAEENCLQTVNE-LMAKQQQLKDiRVTQNSSAEKV--QTQIEEERK 896
Cdd:COG4913 816 EYLALLDRLEEDgLPEYEERFKE-LLNENSIEFVAdlLSKLRRAIR 860
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
7-190 |
1.01e-06 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 50.57 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 7 LLVENFKSWRGrQVIGPFRRFTCIIGPNGSGKSNVMDALSFVMGEKIANL-RVKNIQELIHGAHIGKPISSSASVKIIYV 85
Cdd:pfam13476 1 LTIENFRSFRD-QTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLkRKSGGGFVKGDIRIGLEGKGKAYVEITFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 86 EESGE-----EKTFARIIRGGCSEFRFNDNLVSRSVYIAELEKIGIIVKAQNCLVFQGTVESISVKKPKERTQFFEEISt 160
Cdd:pfam13476 80 NNDGRytyaiERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILPLLVFLGQEREEEFERKEKKERLEELE- 158
|
170 180 190
....*....|....*....|....*....|
gi 613410199 161 sgELIGEYEEKKRKLQKAEEDAQFNFNKKK 190
Cdd:pfam13476 159 --KALEEKEDEKKLLEKLLQLKEKKKELEE 186
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
275-487 |
1.32e-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: 52.07 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 275 RQLQQTEKELKSVETLLNQKRPQYIKAKENTSHHLKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQI 354
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 355 EE--------------EILHKKRDIELEASQLDRYKELKEQVRKKVATMTQQLEKLQweqktdeerlafekrrhgevqgn 420
Cdd:COG4942 107 AEllralyrlgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA----------------------- 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613410199 421 lkQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEKTKSRMSEVNEELNLIRSELQNA 487
Cdd:COG4942 164 --ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
145-515 |
1.42e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 145 VKKPKERTQFFEEISTSGELIGEYEEKKRKLQKAEEDAQfnfNKKKNIAAERRQAKLEKEEAERYQSLLEELKMNKIQlq 224
Cdd:PTZ00121 1301 KKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAE---EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE-- 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 225 lfqlyhNEKKIHLLNTKLEHVNRDLSVKRESLSHHENIVKARKKEHG-MLTRQLQQTEKELKSVETLlnQKRPQYIKAKE 303
Cdd:PTZ00121 1376 ------AKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAkKKADEAKKKAEEKKKADEA--KKKAEEAKKAD 1447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 304 NTSHHLKKLDVAKKSIKDSEKQCSKQEDDIKALETELADlDAAWRSFEKQIEEEILHKKRDIELEASQLDRYKELK--EQ 381
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD-EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKkaDE 1526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 382 VRK-KVATMTQQLEKLQWEQKTDEERLAFEKRRHGEVQgNLKQIKEQIEDHKKRIEKLEEYTKTcmdclkEKKQQEETLV 460
Cdd:PTZ00121 1527 AKKaEEAKKADEAKKAEEKKKADELKKAEELKKAEEKK-KAEEAKKAEEDKNMALRKAEEAKKA------EEARIEEVMK 1599
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 613410199 461 DEIEKTKSRMSEVNEElnlirselQNAGIDTHEGKRQQKRAEVLEHLKRLYPDSV 515
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKA--------EEAKIKAEELKKAEEEKKKVEQLKKKEAEEK 1646
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
162-440 |
2.47e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 162 GELIGEY-------EEKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAERYQSLLEELKmnkiQLQLFQLYHNEKK 234
Cdd:PRK03918 451 KELLEEYtaelkriEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLK----KYNLEELEKKAEE 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 235 IHLLNTKLEHVNRDLSVKRESLSHheniVKARKKEHGMLTRQLQQTEKELKSVETLLNQKRPQYIKAKENTSHHLKK--- 311
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEK----LEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPfyn 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 312 ----LDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEeiLHKKRDIELEASQLDRYKELkeqvRKKVA 387
Cdd:PRK03918 603 eyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE--LEKKYSEEEYEELREEYLEL----SRELA 676
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 613410199 388 TMTQQLEKLQWEQKTDEERLAFEKRRHGEvqgnLKQIKEQIEDHKKRIEKLEE 440
Cdd:PRK03918 677 GLRAELEELEKRREEIKKTLEKLKEELEE----REKAKKELEKLEKALERVEE 725
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
4-510 |
2.56e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 4 LELLLVENFKSWRGRQVigPFRR-FTCIIGPNGSGKSNVMDA----LSFVMGEKIANLRVKNIQElihgahigkpISSSA 78
Cdd:PRK03918 3 IEELKIKNFRSHKSSVV--EFDDgINLIIGQNGSGKSSILEAilvgLYWGHGSKPKGLKKDDFTR----------IGGSG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 79 SVKIIYVEESGEEKTFARIIRGGCSEFRFND---NLVSRSVYIAE-LEKIGIIVKAQNCL-VFQGTVESIsVKKPKERTQ 153
Cdd:PRK03918 71 TEIELKFEKNGRKYRIVRSFNRGESYLKYLDgseVLEEGDSSVREwVERLIPYHVFLNAIyIRQGEIDAI-LESDESREK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 154 FFEEISTsgelIGEYEekkrklqkaeedaqfnfNKKKNIAAERRQAKLEKEEAERYQSLLEELKmNKIQLQLFQLYHNEK 233
Cdd:PRK03918 150 VVRQILG----LDDYE-----------------NAYKNLGEVIKEIKRRIERLEKFIKRTENIE-ELIKEKEKELEEVLR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 234 KIHLLNTKLehvnRDLSVKRESLSHHENIVKARKKEHGMLTRQLQQTEKELKSVETLLNQKRpQYIKAKENTSHHLKKLD 313
Cdd:PRK03918 208 EINEISSEL----PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE-ERIEELKKEIEELEEKV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 314 VAKKSIKDSEKQ-------CSKQEDDIKALETELADLDAAWRSFEKQIEE---------EILHKKRDIELEASQLDRYKE 377
Cdd:PRK03918 283 KELKELKEKAEEyiklsefYEEYLDELREIEKRLSRLEEEINGIEERIKEleekeerleELKKKLKELEKRLEELEERHE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 378 LKEQVRKKVATMTQQLEKLQWEQKTD-EERLAFEKRRHGEVQGNLKQIKEQI-------EDHKKRIEKLEEYTKTCMDCL 449
Cdd:PRK03918 363 LYEEAKAKKEELERLKKRLTGLTPEKlEKELEELEKAKEEIEEEISKITARIgelkkeiKELKKAIEELKKAKGKCPVCG 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613410199 450 KE-----KKQQEETLVDEIEKTKSRMSEVNEELNLIRSELQNAGIDTHEGKRQQKRAEVLEHLKRL 510
Cdd:PRK03918 443 RElteehRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKEL 508
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
4-96 |
3.40e-06 |
|
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: 49.14 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 4 LELLLVENFKSWRGRQVIGPFRRFTCIIGPNGSGKSNVMDALSFVM-GEKIANLRvkniqeliHGAHIGKPI---SSSAS 79
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALtGELPPNSK--------GGAHDPKLIregEVRAQ 72
|
90
....*....|....*..
gi 613410199 80 VKIIYVEESGEEKTFAR 96
Cdd:cd03240 73 VKLAFENANGKKYTITR 89
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
9-48 |
4.33e-06 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 50.43 E-value: 4.33e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 613410199 9 VENFKSWRGRQVI------GPFRRFTCIIGPNGSGKSNVMDALSFV 48
Cdd:COG1106 7 IENFRSFKDELTLsmvasgLRLLRVNLIYGANASGKSNLLEALYFL 52
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
755-1050 |
4.37e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 755 IKERQRRIKEFQEKIDKVEDDIfqhfcEEIGvENIrefenKHVKRQQEIDQKRLEFEKQKTRLNVQLeysrshlkkKLNK 834
Cdd:COG1196 174 KEEAERKLEATEENLERLEDIL-----GELE-RQL-----EPLERQAEKAERYRELKEELKELEAEL---------LLLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 835 INTLKETIQKGSEDIDHLKKAEEnclqtvnELMAKQQQLKDIRVTQNSSAEKVQTQIEEERKKFLAVDREVGKLQKEVVS 914
Cdd:COG1196 234 LRELEAELEELEAELEELEAELE-------ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 915 IQTSLEQKRLEKHNLLLDCKVQDIEIILLSGSLDDIIEVEMGTEAESTQATIDIYEKEEAFEIDYSSLKEDLKALQSDQE 994
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 613410199 995 IEAHLRLLLQQVASQEDILLKTAAPNLRALENLKTVRDKFQESTDAFEASRKEARL 1050
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
7-1008 |
1.12e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.97 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 7 LLVENFKSWRGRQVI--GPFRRFTCIIGPNGSGKSNVMDALSFVMGEKIAnlRVKNIQELIHGAHIGKPISSSASVKIIY 84
Cdd:TIGR00618 6 LTLKNFGSYKGTHTIdfTALGPIFLICGKTGAGKTTLLDAITYALYGKLP--RRSEVIRSLNSLYAAPSEAAFAELEFSL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 85 veesgeektfariirgGCSEFRFNDNLVSRSVYIAELEKIGIIVKAQNclvFQGTVESISVKKPKERtqffeeISTSGEL 164
Cdd:TIGR00618 84 ----------------GTKIYRVHRTLRCTRSHRKTEQPEQLYLEQKK---GRGRILAAKKSETEEV------IHDLLKL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 165 IGEYEEKKRKLQKAEEDAQFNFNKKkniaaERRQAKLEKEEAERYQSLLEELKMNKIQLqlfqlyhnEKKIHLLNTKLEH 244
Cdd:TIGR00618 139 DYKTFTRVVLLPQGEFAQFLKAKSK-----EKKELLMNLFPLDQYTQLALMEFAKKKSL--------HGKAELLTLRSQL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 245 VNRDLSVKRESLshhenivkarkkehgmlTRQLQQTEKELKSVETLLNQKRpqyikakeNTSHHLKKLDVAKKSIKDSEK 324
Cdd:TIGR00618 206 LTLCTPCMPDTY-----------------HERKQVLEKELKHLREALQQTQ--------QSHAYLTQKREAQEEQLKKQQ 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 325 QCSKQEDDIKALETELADLDAAW--RSFEKQIEEEILHKKRDIELEASQLDRYKELKEQVRKKVATMTQQLEKLQWEQKT 402
Cdd:TIGR00618 261 LLKQLRARIEELRAQEAVLEETQerINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSI 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 403 DEERLAFEK--------RRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEKTKSRMSEVN 474
Cdd:TIGR00618 341 EEQRRLLQTlhsqeihiRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFR 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 475 -EELNLIRSELQNAGIDTHEGKRQQKRAEVLEHLKRLYPDSVfgRLFDLCHpiHKKYQLAVTKVfgrfitaIVVASEKVA 553
Cdd:TIGR00618 421 dLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQ--ESAQSLK--EREQQLQTKEQ-------IHLQETRKK 489
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 554 KDCIRFLKEERAEPetflaldyldiKPINERLRELKGCKMVIDVIKTQFPQLKKVIQFVCGNGlvcETMEEARHIALSGP 633
Cdd:TIGR00618 490 AVVLARLLELQEEP-----------CPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLE---TSEEDVYHQLTSER 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 634 ERQKTvaldgtlflksgvisggssdLKYKARCWDEKELKnlrdrRSQKIQELKGLMKTLRKETDLKQIQTLIQGTQTRLK 713
Cdd:TIGR00618 556 KQRAS--------------------LKEQMQEIQQSFSI-----LTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDML 610
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 714 YSQNELEMIKKKHLVAFYQ--------EQSQLQSELLNIESQCIMLSEGIKERQRRIKEFQE--------KIDKVEDDIF 777
Cdd:TIGR00618 611 ACEQHALLRKLQPEQDLQDvrlhlqqcSQELALKLTALHALQLTLTQERVREHALSIRVLPKellasrqlALQKMQSEKE 690
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 778 QHFCEEIGVENIREFENKHVKRQQEIDQKRLEFEKQKTRLNVQLEYSRSHLKKKLNKINTLKETIQKGSEDIDHLKK--- 854
Cdd:TIGR00618 691 QLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNeev 770
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 855 -AEENCLQTVNELMAKQQQLKDIRVTQNSSAEKVQTQIEEERKKF-LAVDREVGKLQKEVVSIQTSLEQKRLEKHNL--- 929
Cdd:TIGR00618 771 tAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDeDILNLQCETLVQEEEQFLSRLEEKSATLGEIthq 850
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 930 ---LLDCKVQDIEIILLSGSLDDIIEVEMGTEAESTQATIDIYEKEEAfEIDYSSLKEdlkaLQSDQEIEAHLRLLLQQV 1006
Cdd:TIGR00618 851 llkYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLH-EITLYANVR----LANQSEGRFHGRYADSHV 925
|
..
gi 613410199 1007 AS 1008
Cdd:TIGR00618 926 NA 927
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
156-469 |
1.20e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 156 EEISTSGELIGEYEEKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAERyqslLEELKMNKIQLQLFQLYHNE--K 233
Cdd:PTZ00121 1227 EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK----ADELKKAEEKKKADEAKKAEekK 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 234 KIHLLNTKLEHVNRDLSVKRESLSHHENIVKARKK-EHGMLTRQLQQTEKELKSVETLLNQKRPQyiKAKENTSHHLKKL 312
Cdd:PTZ00121 1303 KADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKaEEAKKAAEAAKAEAEAAADEAEAAEEKAE--AAEKKKEEAKKKA 1380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 313 DVAKKSIKDSEK---------QCSKQEDDIKALETELADLDAAWRSFEKQIEEEILHKKRDielEASQLDRYKELKEQVR 383
Cdd:PTZ00121 1381 DAAKKKAEEKKKadeakkkaeEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE---EAKKADEAKKKAEEAK 1457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 384 KkvatmTQQLEKlqweqKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEI 463
Cdd:PTZ00121 1458 K-----AEEAKK-----KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEA 1527
|
....*.
gi 613410199 464 EKTKSR 469
Cdd:PTZ00121 1528 KKAEEA 1533
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
260-441 |
1.42e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 260 ENIVKARKKEHGMLTRQLQQTEKELKSVETLLNQKRpQYIKAKENTSHHLKKLDVAKKSIKDSEKQCSKQED------DI 333
Cdd:COG4717 56 DELFKPQGRKPELNLKELKELEEELKEAEEKEEEYA-ELQEELEELEEELEELEAELEELREELEKLEKLLQllplyqEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 334 KALETELADLDAAWRSFEKQIEE--EILHKKRDIELEASQLDR-----YKELKEQVRKKVATMTQQLEKLQWEQKTDEER 406
Cdd:COG4717 135 EALEAELAELPERLEELEERLEElrELEEELEELEAELAELQEeleelLEQLSLATEEELQDLAEELEELQQRLAELEEE 214
|
170 180 190
....*....|....*....|....*....|....*
gi 613410199 407 LAFEKRRHGEVQGNLKQIKEQIEDHKKRiEKLEEY 441
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALE-ERLKEA 248
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
3-52 |
1.64e-05 |
|
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: 48.46 E-value: 1.64e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 613410199 3 HLELLLVENFKSWRgRQVIGPFRRFTCIIGPNGSGKSNVMDALSFVMGEK 52
Cdd:COG3593 2 KLEKIKIKNFRSIK-DLSIELSDDLTVLVGENNSGKSSILEALRLLLGPS 50
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
168-505 |
1.87e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 49.05 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 168 YEEKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAERYQSLLEElKMNKIQLQLF----QLYHNEKKIHLLNTKLE 243
Cdd:pfam10174 354 LEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQK-KIENLQEQLRdkdkQLAGLKERVKSLQTDSS 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 244 HVNRDLSVKRESLSHHENIVKARKKEHGMLTRQ----LQQTEKELKSVETLLNQKRPQ-------YIKAKENTSHHLKKL 312
Cdd:pfam10174 433 NTDTALTTLEEALSEKERIIERLKEQREREDRErleeLESLKKENKDLKEKVSALQPEltekessLIDLKEHASSLASSG 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 313 DVAKKSIKDSEKQCSKQEDDIKALETELadLDAAWRSFEKQIEEEILHKKRDIELEASqldRYKELKEQVRKKVATMTQQ 392
Cdd:pfam10174 513 LKKDSKLKSLEIAVEQKKEECSKLENQL--KKAHNAEEAVRTNPEINDRIRLLEQEVA---RYKEESGKAQAEVERLLGI 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 393 LEKLQWEQKTDEERLA-FEK---RRHGEVQGNLKQIKE-QIEDHKKRIEKLEEYTKTCMDCL-KEKKQQEETLVDEIEKT 466
Cdd:pfam10174 588 LREVENEKNDKDKKIAeLESltlRQMKEQNKKVANIKHgQQEMKKKGAQLLEEARRREDNLAdNSQQLQLEELMGALEKT 667
|
330 340 350
....*....|....*....|....*....|....*....
gi 613410199 467 KSRMSEVNEELNLIRSELQNAgiDTHEGKRQQKRAEVLE 505
Cdd:pfam10174 668 RQELDATKARLSSTQQSLAEK--DGHLTNLRAERRKQLE 704
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
146-486 |
2.65e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 146 KKPKERTQFFEEISTSGELIGEYEEKKRK---LQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAERYQSL--LEELKMNK 220
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADEAKKKAEEAKKKadeAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAkkAEEKKKAD 1549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 221 IQLQLFQLYHNEKKIHLLNTKLEHVNRDLSVKRESLShhENIVKARKKEHGMLTRQLQQTEKELKSVETLLNQKRPQYIK 300
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA--KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 301 AKENTSHHLKKLDVAKKSIKDSEkQCSKQEDDIKALETELADLDAAwrsfEKQIEEEILHKKRDIELEASQLDRYKELK- 379
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAE-ELKKAEEENKIKAAEEAKKAEE----DKKKAEEAKKAEEDEKKAAEALKKEAEEAk 1702
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 380 --EQVRKKVATMTQQLEKLQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEE 457
Cdd:PTZ00121 1703 kaEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
330 340
....*....|....*....|....*....
gi 613410199 458 TLVDeiEKTKSRMSEVNEELNLIRSELQN 486
Cdd:PTZ00121 1783 EELD--EEDEKRRMEVDKKIKDIFDNFAN 1809
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1120-1197 |
3.54e-05 |
|
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: 46.06 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 1120 PMDNLSGGEKCVAALALLFAVHSFRPA--PFFVLDEVDAALDNTNI-GKVSSYIKEQ-TQDQFQMIVISLKEEFYSRADA 1195
Cdd:cd03240 112 MRGRCSGGEKVLASLIIRLALAETFGSncGILALDEPTTNLDEENIeESLAEIIEERkSQKNFQLIVITHDEELVDAADH 191
|
..
gi 613410199 1196 LI 1197
Cdd:cd03240 192 IY 193
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
751-1050 |
4.13e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 751 LSEGIKERQ-----RRIKEFQEKIDKVEDDIfqhfceEIGVENIREFENKHVKRQQEIDQKRLEFEKQKTRLNVQLEysr 825
Cdd:COG1196 218 LKEELKELEaelllLKLRELEAELEELEAEL------EELEAELEELEAELAELEAELEELRLELEELELELEEAQA--- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 826 shlkkklnKINTLKETIQKGSEDIDHLKKAEENCLQTVNELMAKQQQLKDIRVTQNSSAEKVQTQIEEERKKFLAVDREV 905
Cdd:COG1196 289 --------EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 906 GKLQKEVVSIQTSLEQKRLEKHNL---LLDCKVQDIEIILLSGSLDDIIEVEMGTEAESTQATIDIYEKEEAFEIDYSSL 982
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELaeeLLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613410199 983 KEDLKA-------LQSDQEIEAHLRLLLQQVASQEDILLKTAAPNLRALENLKTVRDKFQESTDAFEASRKEARL 1050
Cdd:COG1196 441 EEALEEaaeeeaeLEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
774-1199 |
7.02e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.20 E-value: 7.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 774 DDIFQHFCEEIG--VENIREFENKhvkrQQEIDQKRLEFEKQKTRLNV-----------QLEYSRSHLKKKLNKINTLKE 840
Cdd:PRK01156 468 NHIINHYNEKKSrlEEKIREIEIE----VKDIDEKIVDLKKRKEYLESeeinksineynKIESARADLEDIKIKINELKD 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 841 TIQKGSEDIDHLKKAEENCLQTVNElmakqQQLKDIRVTQNSSAEKVQTQIEEERKKFLAVDREVGKLQKEVVSIQTSLE 920
Cdd:PRK01156 544 KHDKYEEIKNRYKSLKLEDLDSKRT-----SWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYID 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 921 Q--KRLEKHNLLLDCKVQDIE-----IILLSGSLDDIIEVEMGT-EAESTQATIDIyeKEEAFEIDYSSLKEDLKALQSD 992
Cdd:PRK01156 619 KsiREIENEANNLNNKYNEIQenkilIEKLRGKIDNYKKQIAEIdSIIPDLKEITS--RINDIEDNLKKSRKALDDAKAN 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 993 Q-EIEAHLRLLLQQVASQEDIL------LKTAAPNLRALENLKTVRDKFqeSTDAFEAS-RKEArlcrQEFEQVKKRRYd 1064
Cdd:PRK01156 697 RaRLESTIEILRTRINELSDRIndinetLESMKKIKKAIGDLKRLREAF--DKSGVPAMiRKSA----SQAMTSLTRKY- 769
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 1065 LFTQCFEHVSISIDQIYK-KLCRNNSAQAflspenpeepylegisyncvapgkrfmpMDNLSGGEKCVAALALLFAVHSF 1143
Cdd:PRK01156 770 LFEFNLDFDDIDVDQDFNiTVSRGGMVEG----------------------------IDSLSGGEKTAVAFALRVAVAQF 821
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613410199 1144 RPA--PFFVLDEVDAALDN---TNIGKVSSYIKEQTQDQFQMIVISLKEEFYSRADALIGI 1199
Cdd:PRK01156 822 LNNdkSLLIMDEPTAFLDEdrrTNLKDIIEYSLKDSSDIPQVIMISHHRELLSVADVAYEV 882
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
1121-1162 |
8.15e-05 |
|
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: 44.90 E-value: 8.15e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 613410199 1121 MDNLSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTN 1162
Cdd:cd03276 107 VKTLSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVN 148
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
27-235 |
8.75e-05 |
|
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: 45.84 E-value: 8.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 27 FTCIIGPNGSGKSNVMDALSFVMGEKIANLRVKNIQELIHGAHIGKPISSSASVKIIYVEESGEEKTFARIIRggcSEFR 106
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLEDGVRYR---YGLD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 107 FNDNLVSRSVY-IAELEKIGIIVKAQNClvFQGTVESISVKKPKERTQFFEEISTSGELIGEYEEKKRKLQKAEEDAQFN 185
Cdd:pfam13304 78 LEREDVEEKLSsKPTLLEKRLLLREDSE--EREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 613410199 186 FNKKKNIAAERRQAKLEKEEAeRYQSLLEELK--MNKIQLQLFQLYHNEKKI 235
Cdd:pfam13304 156 LLDEGLLLEDWAVLDLAADLA-LFPDLKELLQrlVRGLKLADLNLSDLGEGI 206
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
666-929 |
9.74e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.55 E-value: 9.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 666 WDEKELKNLrdrrSQKIQELKGLMKTLrkETDLKQIQTLIQGTQTRLKYSQNELEMIKKK--HLVAFYQEQSQLQSELLN 743
Cdd:TIGR04523 149 KKEKELEKL----NNKYNDLKKQKEEL--ENELNLLEKEKLNIQKNIDKIKNKLLKLELLlsNLKKKIQKNKSLESQISE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 744 IESQCIMLSEGIKERQRRIKEFQEKIDKVEDDIFQHFCEEIgvENIREFENKhvkrQQEIDQ---KRLEFEKQKTRLNVQ 820
Cdd:TIGR04523 223 LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN--KIKKQLSEK----QKELEQnnkKIKELEKQLNQLKSE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 821 LEYSRShlKKKLNKINTLKETIQKGSEDIDHLKKAEENCLQTVNELMAKQQQLKDIRVTQNSSAEKVQTQIEEERKkfla 900
Cdd:TIGR04523 297 ISDLNN--QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQN---- 370
|
250 260
....*....|....*....|....*....
gi 613410199 901 vdrEVGKLQKEVVSIQTSLEQKRLEKHNL 929
Cdd:TIGR04523 371 ---EIEKLKKENQSYKQEIKNLESQINDL 396
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
170-457 |
1.30e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 46.27 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 170 EKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKE-EAERYQSL-----LEELKMNKIQLQLFQLYHNEKKIHLLNTKLE 243
Cdd:pfam17380 313 ERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERErELERIRQEerkreLERIRQEEIAMEISRMRELERLQMERQQKNE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 244 HVNRDLSVKREslshheniVKARKKEHgmlTRQLQQTEKELKSVETLLNQKRPQYIKA-KENTSHHLKKLDVAKKSIKDS 322
Cdd:pfam17380 393 RVRQELEAARK--------VKILEEER---QRKIQQQKVEMEQIRAEQEEARQREVRRlEEERAREMERVRLEEQERQQQ 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 323 EKQCSKQEDDIKALETELADldaawRSFEKQIEEEILHKKRDIELEAsqldRYKELKEQVRKKVATMTQQLEKLQWEQKT 402
Cdd:pfam17380 462 VERLRQQEEERKRKKLELEK-----EKRDRKRAEEQRRKILEKELEE----RKQAMIEEERKRKLLEKEMEERQKAIYEE 532
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 613410199 403 DEERLAFEKRRHGEVQGNLKQIKEQI---EDHKKRIEKLEEYTKTCMDCLKEKKQQEE 457
Cdd:pfam17380 533 ERRREAEEERRKQQEMEERRRIQEQMrkaTEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
137-509 |
1.40e-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: 46.58 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 137 QGTVESISVKKPKERTQFFEEISTSGELIG----EYEEKKRKLQKAEEDAQfnfNKKKNIAAERRQAKLEKEEAERYQSL 212
Cdd:TIGR00606 711 LKSTESELKKKEKRRDEMLGLAPGRQSIIDlkekEIPELRNKLQKVNRDIQ---RLKNDIEEQETLLGTIMPEEESAKVC 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 213 LEELKMnkIQLQLFQLYHNEKKIHLLNTKLEHVNRDLSVKRESLSHHENIVKARK-KEHGMLTRQLQQTEkelksvetll 291
Cdd:TIGR00606 788 LTDVTI--MERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTvVSKIELNRKLIQDQ---------- 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 292 nQKRPQYIKAKENtshhlkKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEEILHKKRDIELEASQ 371
Cdd:TIGR00606 856 -QEQIQHLKSKTN------ELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEEL 928
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 372 LDRYKELKEQVRKKVATMTQQLEKLQWEQKTDEERLAFEKRRH-GEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLK 450
Cdd:TIGR00606 929 ISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYlKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDID 1008
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613410199 451 EKKQQEETLVDEIEKTKSR--MSEVNEELNLIRSELQNAGIdTHEGKRQQKRAEVLEHLKR 509
Cdd:TIGR00606 1009 TQKIQERWLQDNLTLRKREneLKEVEEELKQHLKEMGQMQV-LQMKQEHQKLEENIDLIKR 1068
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
167-484 |
1.53e-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: 46.17 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 167 EYEEKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAERYQSLLEElKMNKIQLQLFQLyHNEKK---IHLLNTKLE 243
Cdd:TIGR04523 240 EINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEK-QLNQLKSEISDL-NNQKEqdwNKELKSELK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 244 HVNRDLSVKRESLSHHENIVKARKKEHGMLTRQLQQTEKELKSVETLLNQKRPQYIKAKENTSHHLKKLDVAKKSIKDSE 323
Cdd:TIGR04523 318 NQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 324 KQCSKQEDDIKALETELADLDAAWRSFEKQIEEeilhKKRDIELEASQLDRYKELKEQVRKKVatmtQQLEKLQWEQKTD 403
Cdd:TIGR04523 398 SKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER----LKETIIKNNSEIKDLTNQDSVKELII----KNLDNTRESLETQ 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 404 EERLafeKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEKTKSRMSEVNEELNLIRSE 483
Cdd:TIGR04523 470 LKVL---SRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546
|
.
gi 613410199 484 L 484
Cdd:TIGR04523 547 L 547
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
159-483 |
1.77e-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: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 159 STSGELIGEYEEKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAERYQSLLEElKMNKIQLQLFQLYHNEKKIHLL 238
Cdd:TIGR04523 356 SENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDE-QIKKLQQEKELLEKEIERLKET 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 239 NTKLEHVNRDL----SVKRESLSHHENIVKARKKEHGMLTRQ-------LQQTEKELKSVETLLNQKRPQYIKAKENTSH 307
Cdd:TIGR04523 435 IIKNNSEIKDLtnqdSVKELIIKNLDNTRESLETQLKVLSRSinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKD 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 308 HLKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSfeKQIEEEILHKKRDIE--------LEASQlDRYKELK 379
Cdd:TIGR04523 515 LTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKK--ENLEKEIDEKNKEIEelkqtqksLKKKQ-EEKQELI 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 380 EQVRKKVATMTQQLEKLQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETL 459
Cdd:TIGR04523 592 DQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKES 671
|
330 340
....*....|....*....|....
gi 613410199 460 VDEIEKTKSRMSEVNEELNLIRSE 483
Cdd:TIGR04523 672 KTKIDDIIELMKDWLKELSLHYKK 695
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
679-923 |
2.01e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 679 SQKIQELKGLMKTLRKEtdLKQIQTLIQGTQTRLKYSQNELEMIKKKhlvafyqeQSQLQSELLNIESQCIMLSEGIKER 758
Cdd:COG4942 19 ADAAAEAEAELEQLQQE--IAELEKELAALKKEEKALLKQLAALERR--------IAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 759 QRRIKEFQEKIDKVEDDIFQHFceeigvenirefenkhVKRQQEIDQKRLEF---EKQKTRLNVQLEYSRSHLKKKLNKI 835
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELL----------------RALYRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 836 NTLKETIQKGSEDIDHLKKAEENCLQTVNELMAKQQQLKDIRVTQNSSAEKVQTQIEEERKKFLAVDREVGKLQKEVVSI 915
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
....*...
gi 613410199 916 QTSLEQKR 923
Cdd:COG4942 233 EAEAAAAA 240
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
187-509 |
2.38e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 187 NKKKNIAAERRQAKLEKEEAERYQSLLEELKmNKIQLQLFQLYHNEKKIHLLNTKLehvnRDLSVKRESLSHHENIVKAR 266
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIE-ELIKEKEKELEEVLREINEISSEL----PELREELEKLEKEVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 267 KKEHGMLTRQLQQTEKELKSVETLLNQKRpQYIKAKENTSHHLKKLDVAKKSIKDSEKQ-------CSKQEDDIKALETE 339
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIRELE-ERIEELKKEIEELEEKVKELKELKEKAEEyiklsefYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 340 LADLDAAWRSFEKQIEE---------EILHKKRDIELEASQLDRYKELKEQVRKKVATMTQ---------------QLEK 395
Cdd:PRK03918 316 LSRLEEEINGIEERIKEleekeerleELKKKLKELEKRLEELEERHELYEEAKAKKEELERlkkrltgltpeklekELEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 396 LQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKK----------------RIEKLEEYTKTCMDCLKEKKQQEE-- 457
Cdd:PRK03918 396 LEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteehRKELLEEYTAELKRIEKELKEIEEke 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 458 ------------------------TLVDEIEKTKSRMSEVN---------------EELNLIRSELQNAGIDTHEGKRQQ 498
Cdd:PRK03918 476 rklrkelrelekvlkkeseliklkELAEQLKELEEKLKKYNleelekkaeeyeklkEKLIKLKGEIKSLKKELEKLEELK 555
|
410
....*....|.
gi 613410199 499 KRAEVLEHLKR 509
Cdd:PRK03918 556 KKLAELEKKLD 566
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
149-485 |
2.52e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 149 KERTQFFEEISTSGELIGEYEEKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAERYQSLLEELKMNKIQLQLFQL 228
Cdd:PRK03918 300 EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKK 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 229 YHNEKKIHLLNTKLEHVNRdlsvKRESLSHHENIVKARKkehgmltRQLQQTEKEL-KSVETLLNQKRPQYIKAKENTSH 307
Cdd:PRK03918 380 RLTGLTPEKLEKELEELEK----AKEEIEEEISKITARI-------GELKKEIKELkKAIEELKKAKGKCPVCGRELTEE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 308 HLKKLdvakksIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEEilhkkrdieleaSQLDRYKELKEQVRKkva 387
Cdd:PRK03918 449 HRKEL------LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKE------------SELIKLKELAEQLKE--- 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 388 tMTQQLEKLqweqktDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEKTK 467
Cdd:PRK03918 508 -LEEKLKKY------NLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELE 580
|
330
....*....|....*...
gi 613410199 468 SRMSEVNEELNLIRSELQ 485
Cdd:PRK03918 581 ELGFESVEELEERLKELE 598
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
183-401 |
2.74e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.12 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 183 QFNFNKKKNIAAERRQAKLEKEEAERYQSLLEELKMNKIQLQlfqlyhnekkihllntKLEHVNRDLSVKRESLSHHENI 262
Cdd:pfam05557 42 QLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKK----------------YLEALNKKLNEKESQLADAREV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 263 VKARKKEHGMLTRQLQQTEKELKSVET----------LLNQKRPQYIKAKENTSHHLKKLDVAKKSIKDSEKQCSKQEDD 332
Cdd:pfam05557 106 ISCLKNELSELRRQIQRAELELQSTNSeleelqerldLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQD 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613410199 333 ---IKALETELADLdAAWRSFEKQIEEEILH---KKRDIELEASQLDRYK---ELKEQVRKKVATMTQQLEKLQWEQK 401
Cdd:pfam05557 186 seiVKNSKSELARI-PELEKELERLREHNKHlneNIENKLLLKEEVEDLKrklEREEKYREEAATLELEKEKLEQELQ 262
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
169-546 |
2.92e-04 |
|
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: 45.21 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 169 EEKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAERYQSL-LEELKMNKIQL-QLFQLYHNEKKihllnTKLEHVN 246
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFaRTALKNARLDLrRLFDEKQSEKD-----KKNKALA 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 247 RDLSVKRESLSHHENIVKARKKEHGMLtrqLQQTEKELKSVETLLNQKRPQYIKAKENTSHHLKK-LDVAKKSIKDSEKQ 325
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQLDKKHQAW---LEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAaIAARRSGAKAELKA 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 326 CSKQED-DIKAL---ETELADLDAAWRSFEKQIEE------EILHKKRDI-ELEASQLDRYKELKEQVRKKVATMTQQLE 394
Cdd:pfam12128 752 LETWYKrDLASLgvdPDVIAKLKREIRTLERKIERiavrrqEVLRYFDWYqETWLQRRPRLATQLSNIERAISELQQQLA 831
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 395 KLQWEQKTDeeRLAFEKRRHG------EVQGNLKQIKEQIE-----DHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEI 463
Cdd:pfam12128 832 RLIADTKLR--RAKLEMERKAsekqqvRLSENLRGLRCEMSklatlKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESV 909
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 464 EKTKSRMSEVNEELNliRSEL----QNAGIDTHEgkrQQKRAEVLEHLKRLYPdsVFGRLFDLCHPIHKKYQLAVTKVFG 539
Cdd:pfam12128 910 KKYVEHFKNVIADHS--GSGLaetwESLREEDHY---QNDKGIRLLDYRKLVP--YLEQWFDVRVPQSIMVLREQVSILG 982
|
....*..
gi 613410199 540 RFITAIV 546
Cdd:pfam12128 983 VDLTEFY 989
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
230-923 |
3.88e-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: 44.72 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 230 HNEKKIHL------LNTKLEhvnrDLSVKRESLShheNIVKARKKEHGMLTRQLQQTEKELKSV----ETLLNQKRPQYI 299
Cdd:pfam15921 101 HEKQKFYLrqsvidLQTKLQ----EMQMERDAMA---DIRRRESQSQEDLRNQLQNTVHELEAAkclkEDMLEDSNTQIE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 300 KAKENTSHHLKKLDVAKKSIKDSEKQCSKQEDDIKALET-ELADLDAAWRSFEKQIEEEILH-KKRDIELEasqlDRYKE 377
Cdd:pfam15921 174 QLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTmHFRSLGSAISKILRELDTEISYlKGRIFPVE----DQLEA 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 378 LKEQVRKKVATMTQQ----LEKLQWEQKTD----EERLAFEKRRHGEVQGNLKQIKEQIED----HKKRIEKLEEYTKTC 445
Cdd:pfam15921 250 LKSESQNKIELLLQQhqdrIEQLISEHEVEitglTEKASSARSQANSIQSQLEIIQEQARNqnsmYMRQLSDLESTVSQL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 446 MDCLKEKKQQEETLVDEIEKtksrmsevneELNLIRSELQNAgiDTHEGKRQQKRAEVLEHLKRLYPDsvfgrlfdlchp 525
Cdd:pfam15921 330 RSELREAKRMYEDKIEELEK----------QLVLANSELTEA--RTERDQFSQESGNLDDQLQKLLAD------------ 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 526 IHKKyqlavtkvfgrfitaivvasEKVakdcirfLKEERAEPETFLALDYLDIKPINERLRELKGCKMVIDVIKTQFPQL 605
Cdd:pfam15921 386 LHKR--------------------EKE-------LSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAM 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 606 KKViqfvcgnglvCETMEEARHIALSGperqKTVALDGTLFLKSgvisggssdlkykarcwdekELKNLRDRRSQKIQEL 685
Cdd:pfam15921 439 KSE----------CQGQMERQMAAIQG----KNESLEKVSSLTA--------------------QLESTKEMLRKVVEEL 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 686 KGLMKTLRK-ETDLKQIQTLIQGTQTRLKYSQNELEMIKKKHLVAFyQEQSQLQSE---LLNIESQCIMLSEGIKERQRR 761
Cdd:pfam15921 485 TAKKMTLESsERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKL-QELQHLKNEgdhLRNVQTECEALKLQMAEKDKV 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 762 IKEFQEKIDKVEDDIFQHFceeigvENIREFENKHVKRQQEIDQKRLEFEKQKTrLNVQLEYSRSHLKKKLNKINTLK-E 840
Cdd:pfam15921 564 IEILRQQIENMTQLVGQHG------RTAGAMQVEKAQLEKEINDRRLELQEFKI-LKDKKDAKIRELEARVSDLELEKvK 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 841 TIQKGSEDIDHLKKAEENCLQTVNELMAKQQQLkdirvtqNSSAEKVQTQIEEERKKFLAVDREVGKLQKEVVSIQTSLE 920
Cdd:pfam15921 637 LVNAGSERLRAVKDIKQERDQLLNEVKTSRNEL-------NSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELE 709
|
...
gi 613410199 921 QKR 923
Cdd:pfam15921 710 QTR 712
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
4-49 |
4.26e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 39.51 E-value: 4.26e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 613410199 4 LELLLVENFKSWRGRQVIGPFRRFTCIIGPNGSGKSNVMDALSFVM 49
Cdd:pfam13555 1 LTRLQLINWGTFDGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLL 46
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
227-1015 |
4.36e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.71 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 227 QLYHNEKKIHLLNTKLEhvnRDLSVKRESLSHHENIVKARKKEHGMLtrQLQQTEKELKSVETLlnQKRPQYIKAKENTS 306
Cdd:pfam05483 82 KLYKEAEKIKKWKVSIE---AELKQKENKLQENRKIIEAQRKAIQEL--QFENEKVSLKLEEEI--QENKDLIKENNATR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 307 HHLKKLdvakksikdsEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEEIL-HKKRDIELEASQLDRYKELKEQvRKK 385
Cdd:pfam05483 155 HLCNLL----------KETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILaFEELRVQAENARLEMHFKLKED-HEK 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 386 VATMTQQLEKlqwEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEK 465
Cdd:pfam05483 224 IQHLEEEYKK---EINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELED 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 466 TKSRMSEVNEELNLIRSELQNAGIDTHEgKRQQKRAEVLEHLKrlypdsvfgrlfdlchpihkkyqlavTKVFGRFITAI 545
Cdd:pfam05483 301 IKMSLQRSMSTQKALEEDLQIATKTICQ-LTEEKEAQMEELNK--------------------------AKAAHSFVVTE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 546 VVASEKVAKDCIRFLKEERAEPETFLALDYLDIKPINERLRELkgckmvidvikTQFPQLKKViqfvcgnglvceTMEEA 625
Cdd:pfam05483 354 FEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEM-----------TKFKNNKEV------------ELEEL 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 626 RhialsgperqKTVALDGTLFlksgvisggssdlkykarcWDEKELKNLRDRRSQKIQELKGLMKTLRKETDLKQIQtlI 705
Cdd:pfam05483 411 K----------KILAEDEKLL-------------------DEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQ--L 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 706 QGTQTRLKYSQNELEMIKkkhlvafyqeqSQLQSE-LLNIE--SQCIMLSEGIKERQRRIKEFQEKIDKVEDDIFQH-FC 781
Cdd:pfam05483 460 TAIKTSEEHYLKEVEDLK-----------TELEKEkLKNIEltAHCDKLLLENKELTQEASDMTLELKKHQEDIINCkKQ 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 782 EEIGVENIREFENKHVKRQQEIDQKRLEFEKQKTRLNVQLEYSRSHLKKKLNKINTLKETIQKGSEDIDHLKKAEENCLQ 861
Cdd:pfam05483 529 EERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNK 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 862 TVNELMAKQQQLKdirvtQNSSAEKVQTQIEEERKKFLAVDREVGKLQKEVV--SIQTSLEQKRLEKHNLLLD---CKVQ 936
Cdd:pfam05483 609 NIEELHQENKALK-----KKGSAENKQLNAYEIKVNKLELELASAKQKFEEIidNYQKEIEDKKISEEKLLEEvekAKAI 683
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 937 DIEIILLSGSLD-----DIIEVEMGTEAESTQ---------ATIDIYEKEE--------AFEIDYSSLKEDLKALQSDQE 994
Cdd:pfam05483 684 ADEAVKLQKEIDkrcqhKIAEMVALMEKHKHQydkiieerdSELGLYKNKEqeqssakaALEIELSNIKAELLSLKKQLE 763
|
810 820
....*....|....*....|.
gi 613410199 995 IEAHLRLLLQQVASQEDILLK 1015
Cdd:pfam05483 764 IEKEEKEKLKMEAKENTAILK 784
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
149-510 |
4.55e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 149 KERTQFFEEISTSGELIGEYEEKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAERYQSLLE-ELKMNKIQLQLFQ 227
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAlEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 228 LYHNEKKIHLLNTKLEHVNRDLSVKRESLSHHENIVKARKKEhgmltrQLQQTEKELKSVETLLNQKRPQYIKAKENTSH 307
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE------ELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 308 HLKKLD-VAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEE--------------EILHKKRDIELEASQL 372
Cdd:COG4717 225 LEEELEqLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlgllalLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 373 DRYKELKEQVRKKVATMTQQLEKLQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHkkrieKLEEYTKTCMDCLKEK 452
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL-----QLEELEQEIAALLAEA 379
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 613410199 453 KQQEETLVDEIEKTKSRMSEVNEELNLIRSELQNAGIDTHEGKRQQKRAEVLEHLKRL 510
Cdd:COG4717 380 GVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEEL 437
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1050-1202 |
4.83e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 42.31 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 1050 LCRQEFEQVKKRRYDLFTQCFEHVS-ISIDQIyKKLCRNnsaqaflspenpeepyleGISYncVAPGKrfmPMDNLSGGE 1128
Cdd:cd03238 37 LVNEGLYASGKARLISFLPKFSRNKlIFIDQL-QFLIDV------------------GLGY--LTLGQ---KLSTLSGGE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613410199 1129 KCVAALALLFAVHSFRPapFFVLDEVDAALDNTNIGKVSSYIKEQTQDQFQMIVISLKEEFYSRADALIGIYPE 1202
Cdd:cd03238 93 LQRVKLASELFSEPPGT--LFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDFGPG 164
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
257-491 |
5.27e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 257 SHHENIVKARKKEHGMLTR------QLQQTEKELKSVETLLNQKRPQYIKAKENTSHHLKKLDVAKKSIKDSEKQCSKqe 330
Cdd:PHA02562 199 TYNKNIEEQRKKNGENIARkqnkydELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQK-- 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 331 ddikaleteladldaawrsfekqiEEEILHKKRDIELEASQLDRYKELKEQVRKKVATMTQQLEKLQWEQKTDEER---L 407
Cdd:PHA02562 277 ------------------------VIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEImdeF 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 408 AFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEKTKSRMSEVNEE---LNLIRSEL 484
Cdd:PHA02562 333 NEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEkyhRGIVTDLL 412
|
....*..
gi 613410199 485 QNAGIDT 491
Cdd:PHA02562 413 KDSGIKA 419
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
163-486 |
5.27e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 163 ELIGEYEEKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAERY-----QSLLEELKMNKIQLQLFQLYHNEKKIHL 237
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAELKRIEKELKE 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 238 LNTKLEHVNRDLSVKRESLSHHENIVKARKkehgmLTRQLQQTEKELKSVET-LLNQKRPQYIKAKENtshhLKKLDVAK 316
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESELIKLKE-----LAEQLKELEEKLKKYNLeELEKKAEEYEKLKEK----LIKLKGEI 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 317 KSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEEILHKKRDIELEASQL----DRYKELKEqVRKKVATMTQQ 392
Cdd:PRK03918 542 KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELepfyNEYLELKD-AEKELEREEKE 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 393 LEKLQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQI--EDHKKRIEKLEEYTKTcMDCLKEKKQQEETLVDEIEKTKSRM 470
Cdd:PRK03918 621 LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYseEEYEELREEYLELSRE-LAGLRAELEELEKRREEIKKTLEKL 699
|
330
....*....|....*.
gi 613410199 471 SEVNEELNLIRSELQN 486
Cdd:PRK03918 700 KEELEEREKAKKELEK 715
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
28-486 |
7.61e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 7.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 28 TCIIGPNGSGKSNVMDALSFVMgekIANLRVKNIQELIhgahigKPISSSASVKIIYVEESGEEKTFARIIRGGC----- 102
Cdd:PRK01156 26 NIITGKNGAGKSSIVDAIRFAL---FTDKRTEKIEDMI------KKGKNNLEVELEFRIGGHVYQIRRSIERRGKgsrre 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 103 SEFRFNDNLVSRSV-----YIaELEKIGII--VKAQNCLVFQGTVESISVKKPKERTQFFEEISTsgelIGEYEEKKRKL 175
Cdd:PRK01156 97 AYIKKDGSIIAEGFddttkYI-EKNILGISkdVFLNSIFVGQGEMDSLISGDPAQRKKILDEILE----INSLERNYDKL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 176 QKAEEDAQFNFNKKKNIaaerrqakleKEEAERYQSLLEELKMnkiqlqlfQLYHNEKKIHLLNTKLEHVNRDLSVKRES 255
Cdd:PRK01156 172 KDVIDMLRAEISNIDYL----------EEKLKSSNLELENIKK--------QIADDEKSHSITLKEIERLSIEYNNAMDD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 256 LSHheniVKARKKEHGMLTRQLQQTEKELKSVETLLNQKRPQYIKAKENTSHHLKKLDVAKKSIKDSEKQCSKQEDDIKA 335
Cdd:PRK01156 234 YNN----LKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIEN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 336 LETELADLDAAWRSFEKqieeeiLHKKrdieLEASQLDRYKELKEQVRKkvatmtQQLEKLQWEQKTDEErlafekrrhg 415
Cdd:PRK01156 310 KKQILSNIDAEINKYHA------IIKK----LSVLQKDYNDYIKKKSRY------DDLNNQILELEGYEM---------- 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613410199 416 evqgNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIektKSRMSEVNEELNLIRSELQN 486
Cdd:PRK01156 364 ----DYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAI---KKELNEINVKLQDISSKVSS 427
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
3-65 |
7.79e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 42.68 E-value: 7.79e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613410199 3 HLELLLVENFKSWRGRQV-IGPFRRFTCIIGPNGSGKSNVMDALSFVMGEKIANLRVKNIQELI 65
Cdd:COG3950 2 RIKSLTIENFRGFEDLEIdFDNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLL 65
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
218-386 |
8.56e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 8.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 218 MNKIQLQLFQLYHNEKKIHLLNTKLEHVNRDLSVKRESLSHHENIVKARKKEHGMLTRQLQQTEKELKSVETLLNQKRPQ 297
Cdd:COG1579 2 MPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 298 YIKAKENT--SHHLKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEEIlhKKRDIELEA--SQLD 373
Cdd:COG1579 82 LGNVRNNKeyEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK--AELDEELAEleAELE 159
|
170
....*....|...
gi 613410199 374 RYKELKEQVRKKV 386
Cdd:COG1579 160 ELEAEREELAAKI 172
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
757-926 |
9.12e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.57 E-value: 9.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 757 ERQRRIKEFQEKIDKVEDDIFQHfcEEIGVE--NIREFENKHVKRQQEIDQKRLEFEKQKTRLNVQLEYSRSHLKKKLNK 834
Cdd:pfam17380 345 ERERELERIRQEERKRELERIRQ--EEIAMEisRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEM 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 835 INTLKETIQKGSEDIDHLKKAEENCLQTVN-ELMAKQQQLKDIRVTQNSSAEKVQTQIEEERKKFLAVDREVGKLQKEV- 912
Cdd:pfam17380 423 EQIRAEQEEARQREVRRLEEERAREMERVRlEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELe 502
|
170
....*....|....
gi 613410199 913 VSIQTSLEQKRLEK 926
Cdd:pfam17380 503 ERKQAMIEEERKRK 516
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
245-510 |
9.15e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 9.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 245 VNRDLSVKRESLSHHENIVKArkKEHGMLTRQLQQTEKELKSVETLL---NQKRPQYIKAKENTSHHLKKLDVAKKSIKD 321
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEE--KEEKDLHERLNGLESELAELDEEIeryEEQREQARETRDEADEVLEEHEERREELET 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 322 SEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEeiLHKKRDIELEASQLDRYkelkeqvrkkvatmtqqleklqwEQK 401
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEE--LEEERDDLLAEAGLDDA-----------------------DAE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 402 TDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEKTKSRMSEVNEELNLIR 481
Cdd:PRK02224 311 AVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELE 390
|
250 260 270
....*....|....*....|....*....|....
gi 613410199 482 SELQN-----AGIDTHEGKRQQKRAEVLEHLKRL 510
Cdd:PRK02224 391 EEIEElrerfGDAPVDLGNAEDFLEELREERDEL 424
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
7-47 |
1.04e-03 |
|
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: 41.87 E-value: 1.04e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 613410199 7 LLVENFKSWRGRQVI----GPFRRFTCIIGPNGSGKSNVMDALSF 47
Cdd:cd03279 6 LELKNFGPFREEQVIdftgLDNNGLFLICGPTGAGKSTILDAITY 50
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
153-405 |
1.09e-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: 43.08 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 153 QFFEEISTSGELIGEYE------EKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAeryqslleELKMNKIQLQLF 226
Cdd:NF033838 129 QFKKDTLEPGKKVAEATkkveeaEKKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKA--------ELELVKEEAKEP 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 227 QlyhNEKKIHLLNTKLEHvnrdlsvKRESLSHHENIVKARKKEHGMLTRQLQQTEKEL--KSVETLLNQKRPQYIK---- 300
Cdd:NF033838 201 R---DEEKIKQAKAKVES-------KKAEATRLEKIKTDREKAEEEAKRRADAKLKEAveKNVATSEQDKPKRRAKrgvl 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 301 -------AKENTSHHL-----------------KKLDVAKKSIKDSEKQCSKQEDD---------IKALETELADLDAAW 347
Cdd:NF033838 271 gepatpdKKENDAKSSdssvgeetlpspslkpeKKVAEAEKKVEEAKKKAKDQKEEdrrnyptntYKTLELEIAESDVKV 350
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 613410199 348 RSFEKQIEEEILHKKRDIEleasqldRYKELKEQVRKKVATMTqQLEKLQWEQKTDEE 405
Cdd:NF033838 351 KEAELELVKEEAKEPRNEE-------KIKQAKAKVESKKAEAT-RLEKIKTDRKKAEE 400
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
210-477 |
1.34e-03 |
|
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: 43.09 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 210 QSLLEELKMNKIQLQLFQLYHNEKKIHLLNTKLEHVNRDLSVKRESLSHHeniVKARKKEHGMLTRQLQQTEKELKSVET 289
Cdd:pfam05667 206 PSLLERNAAELAAAQEWEEEWNSQGLASRLTPEEYRKRKRTKLLKRIAEQ---LRSAALAGTEATSGASRSAQDLAELLS 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 290 LLNQKRP-QYIKAKENTSHHLKKLDVAK---------KSIKDSEKQC-SKQEDDIKALETELADLDA----------AWR 348
Cdd:pfam05667 283 SFSGSSTtDTGLTKGSRFTHTEKLQFTNeapaatsspPTKVETEEELqQQREEELEELQEQLEDLESsiqelekeikKLE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 349 SFEKQIEEEIlhkkRDIELEASQLDRYKELKEQVRKKVATMTQQLEKLQWEQKTDEERLAfekrrhgevqgnlkQIKEQI 428
Cdd:pfam05667 363 SSIKQVEEEL----EELKEQNEELEKQYKVKKKTLDLLPDAEENIAKLQALVDASAQRLV--------------ELAGQW 424
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 613410199 429 EDHKKR-IEKLEEYTKTCMDCLKEKKQQeetlVDEIEKTKSRMSEVNEEL 477
Cdd:pfam05667 425 EKHRVPlIEEYRALKEAKSNKEDESQRK----LEEIKELREKIKEVAEEA 470
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
213-883 |
1.38e-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: 43.18 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 213 LEELK---MNKIQLQLFQlyhNEKKIHLLNTKLEHVNRDLSVKRESLSHHENIVKAR--------KKEHGMLTRQLQQTE 281
Cdd:pfam15921 247 LEALKsesQNKIELLLQQ---HQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQleiiqeqaRNQNSMYMRQLSDLE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 282 KELKSVETLLNQKRPQYIKAKENTSHHLKKLDVAKKSIKDSEKQCSKQEDDIK-ALETELADLDAawRSFEKQIEEE--- 357
Cdd:pfam15921 324 STVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDdQLQKLLADLHK--REKELSLEKEqnk 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 358 ------------ILHKKRDIELEASQLDRYKELKEQVRKKV-ATMTQQLEKLQWEQKTDEERLAFEKRRHgEVQGNLKQI 424
Cdd:pfam15921 402 rlwdrdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSECqGQMERQMAAIQGKNESLEKVSSLTAQLE-STKEMLRKV 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 425 KEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEKTKSRMSEVNEELNLIRSE---LQNAGIDTHEGKRQQ-KR 500
Cdd:pfam15921 481 VEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMaEK 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 501 AEVLEHLKRlypdsvfgrlfdlchPIHKKYQLAVTKvfGRFITAIVVasekvakdcirflkeERAEPEtflaldyldiKP 580
Cdd:pfam15921 561 DKVIEILRQ---------------QIENMTQLVGQH--GRTAGAMQV---------------EKAQLE----------KE 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 581 INERLRELKGCKMVIDVIKTQFPQLKkviqfvcgnGLVCETMEEARHIALSGPERQKTValdgtlflksgvisggsSDLK 660
Cdd:pfam15921 599 INDRRLELQEFKILKDKKDAKIRELE---------ARVSDLELEKVKLVNAGSERLRAV-----------------KDIK 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 661 yKARCWDEKELKNLRDRRSQKIQELKGLMKTLRKETDlkQIQTLIQGTQTRLKYSQNELEmikkkhlvafyQEQSQLQSe 740
Cdd:pfam15921 653 -QERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSE--EMETTTNKLKMQLKSAQSELE-----------QTRNTLKS- 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 741 LLNIESQCIMLSEGIkerQRRIKEFQEKIDKVEDDIfqHFCEEIGVENIREfenKHVKRQQ--EIDQKRLEFEKQKTRLN 818
Cdd:pfam15921 718 MEGSDGHAMKVAMGM---QKQITAKRGQIDALQSKI--QFLEEAMTNANKE---KHFLKEEknKLSQELSTVATEKNKMA 789
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613410199 819 VQLEYSRSHLKKKLNKINTLKETIQKGS----EDIDHLKKAEENCLQTVNELMAKQQQLKDIRVTQNSS 883
Cdd:pfam15921 790 GELEVLRSQERRLKEKVANMEVALDKASlqfaECQDIIQRQEQESVRLKLQHTLDVKELQGPGYTSNSS 858
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
669-923 |
1.43e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 669 KELKNLRDRRSQKIQELKGLMKTLRKETDLKQIQ-TLIQGTQTRLK---YSQNELEMIKKKhlvaFYQEQSQLQSELLNI 744
Cdd:pfam01576 152 KERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHeAMISDLEERLKkeeKGRQELEKAKRK----LEGESTDLQEQIAEL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 745 ESQcimLSEGIKERQRRIKEFQEKIDKVEDDIFQhfcEEIGVENIREFENKHVKRQQEIDQKRL---EFEKQKTRLNVQL 821
Cdd:pfam01576 228 QAQ---IAELRAQLAKKEEELQAALARLEEETAQ---KNNALKKIRELEAQISELQEDLESERAarnKAEKQRRDLGEEL 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 822 EYSRSHLKKKLNKINTLKETIQKGSEDIDHLKKAEEnclqtvNELMAKQQQLKDIRVTQNSSAEKVQTQIEEER------ 895
Cdd:pfam01576 302 EALKTELEDTLDTTAAQQELRSKREQEVTELKKALE------EETRSHEAQLQEMRQKHTQALEELTEQLEQAKrnkanl 375
|
250 260 270
....*....|....*....|....*....|..
gi 613410199 896 -KKFLAVDREVGKLQKEVVSIQTS---LEQKR 923
Cdd:pfam01576 376 eKAKQALESENAELQAELRTLQQAkqdSEHKR 407
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
149-478 |
1.55e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 149 KERTQFFEEISTSGELIGEYEEKKRKLQKAEEdaqfnfnKKKNIaaERRQAKLEK--EEAERYQSLLEELKMNKIQLQLF 226
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERLEELKK-------KLKEL--EKRLEELEErhELYEEAKAKKEELERLKKRLTGL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 227 QLYHNEKKIHLLNTKLEHVNRDLSVKRESLSHHENIVKARKKEHGMLT----------RQL-QQTEKELKSVETLLNQKR 295
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgRELtEEHRKELLEEYTAELKRI 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 296 PQYIKAKENTSHHLKKLDVAKKSIKDSEKQCSKQE---DDIKALETELA-----DLDAAWRSFEKqIEEEILHKKRDIEL 367
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEKVLKKESELIKLKelaEQLKELEEKLKkynleELEKKAEEYEK-LKEKLIKLKGEIKS 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 368 EASQLDRYKELKEQvRKKVATMTQQLEKLQWEQKTDEERLAFEKRRhgEVQGNLKQIKE------QIEDHKKRIEKLEEY 441
Cdd:PRK03918 544 LKKELEKLEELKKK-LAELEKKLDELEEELAELLKELEELGFESVE--ELEERLKELEPfyneylELKDAEKELEREEKE 620
|
330 340 350
....*....|....*....|....*....|....*..
gi 613410199 442 TKTCMDCLKEKKQQEETLVDEIEKTKSRMSEVNEELN 478
Cdd:PRK03918 621 LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS 657
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
251-506 |
1.62e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 251 VKRESLSHHENIVKARKKEHGMLTRQLQQTEKEL---KSVETLLN--QKRPQYiKAKENTSHHLKKLDVAKKSIkdseKQ 325
Cdd:COG5022 760 LRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWrlfIKLQPLLSllGSRKEY-RSYLACIIKLQKTIKREKKL----RE 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 326 CSKQEDDIKALETeladLDAAWRSFEKQIEEEILHKKRDIELEASQLD----RYKELKEQVrKKVATMTQQLEKLQWE-- 399
Cdd:COG5022 835 TEEVEFSLKAEVL----IQKFGRSLKAKKRFSLLKKETIYLQSAQRVElaerQLQELKIDV-KSISSLKLVNLELESEii 909
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 400 -----QKTDE-ERLAFEKRRHGEVQGNLK--QIKEQIEDHKKRIEKLEEYTKTCMDcLKEKKQQEETLVDEIEKTKSRMS 471
Cdd:COG5022 910 elkksLSSDLiENLEFKTELIARLKKLLNniDLEEGPSIEYVKLPELNKLHEVESK-LKETSEEYEDLLKKSTILVREGN 988
|
250 260 270
....*....|....*....|....*....|....*
gi 613410199 472 EVNEELNLIRSELQNAGIDTHEGKRQQKRAEVLEH 506
Cdd:COG5022 989 KANSELKNFKKELAELSKQYGALQESTKQLKELPV 1023
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
310-509 |
2.15e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 310 KKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIeeeilhkkRDIELEASQLdrykelkeqvRKKVATM 389
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI--------RALEQELAAL----------EAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 390 TQQLEKLQWEQKTDEERLA------FEKRRHGEVQGNLKQikEQIEDHKKRIEKLEEYT---KTCMDCLKEKKQQEETLV 460
Cdd:COG4942 89 EKEIAELRAELEAQKEELAellralYRLGRQPPLALLLSP--EDFLDAVRRLQYLKYLAparREQAEELRADLAELAALR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 613410199 461 DEIEKTKSRMSEVNEELNLIRSELQNAgidthegkrQQKRAEVLEHLKR 509
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEAL---------KAERQKLLARLEK 206
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
3-47 |
2.19e-03 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 41.68 E-value: 2.19e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 613410199 3 HLELLLVENFKSWRgRQVIGPFRRFTCIIGPNGSGKSNVMDALSF 47
Cdd:PRK00064 2 YLTRLSLTDFRNYE-ELDLELSPGVNVLVGENGQGKTNLLEAIYL 45
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
141-509 |
2.37e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 141 ESISVKKPKERTQFFEEISTSGELIGEYEEKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAERYQSLLEELKMNK 220
Cdd:PTZ00121 1086 DNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARK 1165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 221 IQLQlfQLYHNEKKIHLLNtKLEHVNRDLSVKR-------ESLSHHENIVK---------ARKKEHGMLTRQLQQTEKEL 284
Cdd:PTZ00121 1166 AEEA--RKAEDAKKAEAAR-KAEEVRKAEELRKaedarkaEAARKAEEERKaeearkaedAKKAEAVKKAEEAKKDAEEA 1242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 285 KSVETLLNQ---------------KRPQYIKAKE-NTSHHLKKLDVAKKS--IKDSEKQCSKQEDDIKALETELADlDAA 346
Cdd:PTZ00121 1243 KKAEEERNNeeirkfeearmahfaRRQAAIKAEEaRKADELKKAEEKKKAdeAKKAEEKKKADEAKKKAEEAKKAD-EAK 1321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 347 WRSFEKQIEEEILHKKRDielEASQLDRYKELKEQVRKKVATMTQQLEKLQWEQKTDEERLAFEKRRHGEVQGNLKQIKE 426
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAE---EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKK 1398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 427 QIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEKTKSRMSEVNEELNLIRSELQNAgidtHEGKRQQKRAEVLEH 506
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKA----EEAKKKAEEAKKADE 1474
|
...
gi 613410199 507 LKR 509
Cdd:PTZ00121 1475 AKK 1477
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
26-99 |
2.37e-03 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 39.92 E-value: 2.37e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613410199 26 RFTCIIGPNGSGKSNVMDALSFVmgekianLRVKNIQELIHGAHIGKPISSSASVKIIYVEE-SGEEKTFARIIR 99
Cdd:cd00267 26 EIVALVGPNGSGKSTLLRAIAGL-------LKPTSGEILIDGKDIAKLPLEELRRRIGYVPQlSGGQRQRVALAR 93
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
9-53 |
3.22e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 41.11 E-value: 3.22e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 613410199 9 VENFKSWRGRQVigPFRRFTCIIGPNGSGKSNVMDALSFVMGEKI 53
Cdd:COG4938 6 IKNFGPFKEAEL--ELKPLTLLIGPNGSGKSTLIQALLLLLQSNF 48
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
181-408 |
3.23e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 181 DAQFNFNKKKNIAAERRQAKLEKEeaerYQSLLEELkmNKIQLQLFQLyhnEKKIHLLNTKLEHVNRDLSVKRESLSHHE 260
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAE----LDALQAEL--EELNEEYNEL---QAELEALQAEIDKLQAEIAEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 261 NIVKARkkehgmlTRQLQQTEKELKSVETLLNQkrpqyikakENTSHHLKKLDVAKKSIKDSEKQCSKQEDDIKALETEL 340
Cdd:COG3883 86 EELGER-------ARALYRSGGSVSYLDVLLGS---------ESFSDFLDRLSALSKIADADADLLEELKADKAELEAKK 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613410199 341 ADLDAAWRSFEKQIEEEILHKKrdiELEAsQLDRYKELKEQVRKKVATMTQQLEKLQWEQKTDEERLA 408
Cdd:COG3883 150 AELEAKLAELEALKAELEAAKA---ELEA-QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
190-510 |
3.32e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 190 KNIAAERRQAKLEKEEAERYQSLLE---ELKMNKIQLQLFQLYHNEKKIHLLNTKLEHVNRDLSVKRESLSHHENI---V 263
Cdd:TIGR00606 698 SDLQSKLRLAPDKLKSTESELKKKEkrrDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLlgtI 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 264 KARKKEHGMLTRQ---LQQTEKELKSVETLLNQKRPQ---------YIKAKENTSHHLKKLDVAKKSIKDSEKQCSKQED 331
Cdd:TIGR00606 778 MPEEESAKVCLTDvtiMERFQMELKDVERKIAQQAAKlqgsdldrtVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQE 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 332 DIKALETELADLDAAWRSFEKQIEEEILHKKRDIELEASQLDRYKELKeQVRKKVATMTQQLEKLQWEQKTDEERLAFEK 411
Cdd:TIGR00606 858 QIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIK-DAKEQDSPLETFLEKDQQEKEELISSKETSN 936
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 412 RRHGEVQGNLKQIKEQIEDHKKRIEKleEYTKTCMDCLKEKKQQEETLVDEIEKTKSRMSEVNEELNLIRSELQNAGIDT 491
Cdd:TIGR00606 937 KKAQDKVNDIKEKVKNIHGYMKDIEN--KIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQE 1014
|
330
....*....|....*....
gi 613410199 492 HEGKRQQKRAEVLEHLKRL 510
Cdd:TIGR00606 1015 RWLQDNLTLRKRENELKEV 1033
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
315-477 |
3.36e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.45 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 315 AKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEeiLHKKRDIELEASQLDRYKelkeQVRKKVATMTQQLE 394
Cdd:PRK05771 84 LEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIER--LEPWGNFDLDLSLLLGFK----YVSVFVGTVPEDKL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 395 KLQwEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLE------EYTKTCMDCLKEKKQQEETLVDEIEKTKS 468
Cdd:PRK05771 158 EEL-KLESDVENVEYISTDKGYVYVVVVVLKELSDEVEEELKKLGferlelEEEGTPSELIREIKEELEEIEKERESLLE 236
|
....*....
gi 613410199 469 RMSEVNEEL 477
Cdd:PRK05771 237 ELKELAKKY 245
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
820-1048 |
3.88e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 820 QLEYSRSHLKKKLNKINTLKETIQKGSEDIDhlkKAEENCLQTVNELMAKQQQLKDIrvtqNSSAEKVQTQIEEERKkfl 899
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELE---ELNEEYNELQAELEALQAEIDKL----QAEIAEAEAEIEERRE--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 900 avdrevgKLQKEVVSIQTSLEQkrlekhnllldckVQDIEIILLSGSLDDIIE--VEMGTEAESTQATIDiyekeeafei 977
Cdd:COG3883 87 -------ELGERARALYRSGGS-------------VSYLDVLLGSESFSDFLDrlSALSKIADADADLLE---------- 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613410199 978 DYSSLKEDLKALQSD-QEIEAHLRLLLQQVASQEDILLKTAAPNLRALENLKTVRDKFQESTDAFEASRKEA 1048
Cdd:COG3883 137 ELKADKAELEAKKAElEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
149-397 |
4.08e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 149 KERTQFFEEistsgeligEYEEKKRKLQKAEEDAQfNFNKKKNIAAERRQAKLEKEEAERYQSLLEELKMNKIQLQlfql 228
Cdd:COG3206 174 RKALEFLEE---------QLPELRKELEEAEAALE-EFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAE---- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 229 yhnekkihllnTKLEHVNRDLSVKRESLSHHENIVKARKkehgmLTRQLQQTEKELKSVETLLNQKRPQYIKAKEntshh 308
Cdd:COG3206 240 -----------ARLAALRAQLGSGPDALPELLQSPVIQQ-----LRAQLAELEAELAELSARYTPNHPDVIALRA----- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 309 lkKLDVAKKSIKDSEKQcskqedDIKALETELADLDAAWRSFEKQIEEEilhkKRDIELEASQLDRYKELKEQVRKKVAT 388
Cdd:COG3206 299 --QIAALRAQLQQEAQR------ILASLEAELEALQAREASLQAQLAQL----EARLAELPELEAELRRLEREVEVAREL 366
|
....*....
gi 613410199 389 MTQQLEKLQ 397
Cdd:COG3206 367 YESLLQRLE 375
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
232-456 |
4.11e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.26 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 232 EKKIHLLNTKLEHV---NRDLSVKRESLSHHENIVKARKKEHGMLTRQLQqteKELKSVETLLNQKRPQYIKAKENTSHH 308
Cdd:pfam05557 33 EKKASALKRQLDREsdrNQELQKRIRLLEKREAEAEEALREQAELNRLKK---KYLEALNKKLNEKESQLADAREVISCL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 309 LKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEeiLHKKRDIELEASQ----LDRYKELKEQVRK 384
Cdd:pfam05557 110 KNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQN--LEKQQSSLAEAEQrikeLEFEIQSQEQDSE 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613410199 385 KVATMTQQLEKLQwEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEY--TKTCMDCLKEKKQQE 456
Cdd:pfam05557 188 IVKNSKSELARIP-ELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYreEAATLELEKEKLEQE 260
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
655-895 |
4.22e-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: 41.36 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 655 GSSDLKYKARCwDEKELKNLRDRRSQKIQELKGLMKTLRKETDLKQIQTLI---------QGTQTRLKYSQNELEMIKKK 725
Cdd:pfam12128 284 TSAELNQLLRT-LDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAfldadietaAADQEQLPSWQSELENLEER 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 726 HlVAFYQEQSQLQSEL----LNIESQCIMLSEGIKERQRRIKEFQEKIDKVEDDIFQHFCEEIgvenirefenkhvkrQQ 801
Cdd:pfam12128 363 L-KALTGKHQDVTAKYnrrrSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESEL---------------RE 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 802 EIDQKRLEFEKQKTRLNVQLEysrsHLKKKLNKINT---LKETIQKGSEDIDHLKKAEENCLQTVNELMAKQQQLKDIRV 878
Cdd:pfam12128 427 QLEAGKLEFNEEEYRLKSRLG----ELKLRLNQATAtpeLLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRD 502
|
250
....*....|....*..
gi 613410199 879 TQNSSAEKVQTQIEEER 895
Cdd:pfam12128 503 QASEALRQASRRLEERQ 519
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
170-474 |
4.41e-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: 41.58 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 170 EKKRKLQKAEEDAQFNFNKKKNiaaerrqakleKEEAERYQSLLEELKMNKIQLQLFQLYHNEKKIHLLNTKLEHVNRDL 249
Cdd:TIGR01612 974 DKINELDKAFKDASLNDYEAKN-----------NELIKYFNDLKANLGKNKENMLYHQFDEKEKATNDIEQKIEDANKNI 1042
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 250 SvkRESLSHHENIVKARKKEHGMLTRQLQQTEKE-LKSVETLLNQ--KRPQYIK-------AKENTSHHLKKLDVAKKSI 319
Cdd:TIGR01612 1043 P--NIEIAIHTSIYNIIDEIEKEIGKNIELLNKEiLEEAEINITNfnEIKEKLKhynfddfGKEENIKYADEINKIKDDI 1120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 320 KDSEKQC-----------SKQEDDIKALETELADL-DAAWRSFEKQIEEEILHKKRDIeleASQLDRYKELKEQVrKKVA 387
Cdd:TIGR01612 1121 KNLDQKIdhhikaleeikKKSENYIDEIKAQINDLeDVADKAISNDDPEEIEKKIENI---VTKIDKKKNIYDEI-KKLL 1196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 388 TMTQQLEKlqweQKTDEERLAFEKRRHGEVQGNLkqIKEQIEDHKKR----IEKLEEYTKTcMDCLKEKKQQEETLVDEI 463
Cdd:TIGR01612 1197 NEIAEIEK----DKTSLEEVKGINLSYGKNLGKL--FLEKIDEEKKKsehmIKAMEAYIED-LDEIKEKSPEIENEMGIE 1269
|
330
....*....|.
gi 613410199 464 EKTKSRMSEVN 474
Cdd:TIGR01612 1270 MDIKAEMETFN 1280
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
169-357 |
4.56e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 169 EEKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAERYQSLLEElKMNKIQLQLFQLyhnEKKIHLLNTKLEHVNRD 248
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR-RIRALEQELAAL---EAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 249 LSVKRESLSH--------------------------------HENIVKARKKehgmLTRQLQQTEKELKSVETLLNQKRP 296
Cdd:COG4942 99 LEAQKEELAEllralyrlgrqpplalllspedfldavrrlqyLKYLAPARRE----QAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613410199 297 QYIKAKENTSHHLKKLDVAKKS----IKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEE 357
Cdd:COG4942 175 ELEALLAELEEERAALEALKAErqklLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
1125-1182 |
4.71e-03 |
|
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: 39.89 E-value: 4.71e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 613410199 1125 SGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTNIGKVssyikeqtqdqFQMIV 1182
Cdd:cd03277 128 SGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKV-----------FDMLV 174
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
297-486 |
4.82e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 297 QYIKAKENTSHHLK-KLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEEILHKKRDIELEASQLDRy 375
Cdd:PHA02562 181 QQIQTLDMKIDHIQqQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNK- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 376 kelkeqVRKKVATMTQQLEKLQWEQKTDEErlafekrrHGEVqgnlKQIKEQIEDHKKRIEKLEEYTKTC---MDCLKEK 452
Cdd:PHA02562 260 ------LNTAAAKIKSKIEQFQKVIKMYEK--------GGVC----PTCTQQISEGPDRITKIKDKLKELqhsLEKLDTA 321
|
170 180 190
....*....|....*....|....*....|....
gi 613410199 453 KQQEETLVDEIEKTKSRMSEVNEELNLIRSELQN 486
Cdd:PHA02562 322 IDELEEIMDEFNEQSKKLLELKNKISTNKQSLIT 355
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
372-510 |
5.54e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 372 LDRYKELKEQVRKKV----------------ATMTQQLEKLQWEQKTDEERLAFEKRRHGEVQGNLKQikEQIEDHKKRI 435
Cdd:COG2433 345 YDAYKNKFERVEKKVppdvdrdevkarvirgLSIEEALEELIEKELPEEEPEAEREKEHEERELTEEE--EEIRRLEEQV 422
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613410199 436 EKLEEYTKTCMDCLKEKKQQEETLVDEIEKTKSRMSE---VNEELNLIRSELQNAgidTHEGKRQQKRAEVLE-HLKRL 510
Cdd:COG2433 423 ERLEAEVEELEAELEEKDERIERLERELSEARSEERReirKDREISRLDREIERL---ERELEEERERIEELKrKLERL 498
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
668-921 |
6.22e-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: 40.77 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 668 EKELKNLRDRRSQKIQELKGLMKTLR-KETDLKQIQTLIQGTQTRLKYSQNELEMIKkkhlvafyQEQSQLQSELLNIES 746
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSvKELIIKNLDNTRESLETQLKVLSRSINKIK--------QNLEQKQKELKSKEK 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 747 QCIMLSEGIKERQRRIKEFQEKIDKVEddifqhfceeigvENIREFENKHVKRQQEIDQKRLEFEKQKTRLNvqleysRS 826
Cdd:TIGR04523 497 ELKKLNEEKKELEEKVKDLTKKISSLK-------------EKIEKLESEKKEKESKISDLEDELNKDDFELK------KE 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 827 HLKKKLNKINtlkETIQKGSEDIDHLKKAEENCLQTVNELMAKQQQLKDIRVTQNSSAEKVQTQIEEERKKFLAVDREVG 906
Cdd:TIGR04523 558 NLEKEIDEKN---KEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIK 634
|
250
....*....|....*
gi 613410199 907 KLQKEVVSIQTSLEQ 921
Cdd:TIGR04523 635 NIKSKKNKLKQEVKQ 649
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
260-474 |
6.65e-03 |
|
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: 40.78 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 260 ENIVKARKKEHGMLTRQLQQT-------EKELKSVETLLNQKRPQYIKAKENTSHHLKKLDVAKKSIK---DSEKQCSKQ 329
Cdd:pfam05667 327 EELQQQREEELEELQEQLEDLessiqelEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDllpDAEENIAKL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 330 EDDIKALETELADLDAAWrsfEKqieeeilHKKRDIEleasqldRYKELKEQVRKKVATMTQQLEKLQwEQKTDEERLAF 409
Cdd:pfam05667 407 QALVDASAQRLVELAGQW---EK-------HRVPLIE-------EYRALKEAKSNKEDESQRKLEEIK-ELREKIKEVAE 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613410199 410 EKRRHGEVQgnlKQIKEQIEDHKKRIEKlEEYTKTCMDCLKEKKQQEETLVDEIEKTKSRMSEVN 474
Cdd:pfam05667 469 EAKQKEELY---KQLVAEYERLPKDVSR-SAYTRRILEIVKNIKKQKEEITKILSDTKSLQKEIN 529
|
|
| cdk7 |
TIGR00570 |
CDK-activating kinase assembly factor MAT1; All proteins in this family for which functions ... |
310-476 |
6.78e-03 |
|
CDK-activating kinase assembly factor MAT1; All proteins in this family for which functions are known are cyclin dependent protein kinases that are components of TFIIH, a complex that is involved in nucleotide excision repair and transcription initiation. Also known as MAT1 (menage a trois 1). 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: 129661 [Multi-domain] Cd Length: 309 Bit Score: 40.17 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 310 KKLDVAKKSIKDSekqcSKQEDDIKALeteladldAAWRSFEKQIEEEILHKKRDIELEASQ--LDRYKELKEQVRKKva 387
Cdd:TIGR00570 70 KEVDIRKRVLKIY----NKREEDFPSL--------REYNDYLEEVEDIVYNLTNNIDLENTKkkIETYQKENKDVIQK-- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 388 tmtqQLEKLQWEQKTDEERLAFEkrrhgevqgnlkqiKEQIEDHKKRIEKLEEYTKtcmdclKEKKQQEETLVDEIEKTK 467
Cdd:TIGR00570 136 ----NKEKSTREQEELEEALEFE--------------KEEEEQRRLLLQKEEEEQQ------MNKRKNKQALLDELETST 191
|
....*....
gi 613410199 468 SRMSEVNEE 476
Cdd:TIGR00570 192 LPAAELIAQ 200
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
201-473 |
6.79e-03 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 39.94 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 201 LEKEEA--ERYQSLLEELKMNKIQLQLfqlyhNEKKIHLLNTKLEHVnrdlsvkresLSHHENIVKARKKEHGmLTRQLQ 278
Cdd:pfam09728 17 EEKLAAlcKKYAELLEEMKRLQKDLKK-----LKKKQDQLQKEKDQL----------QSELSKAILAKSKLEK-LCRELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 279 QTEKELKsvETLLNQKRPQYIKAKENTSHHLKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEei 358
Cdd:pfam09728 81 KQNKKLK--EESKKLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEK-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 359 LHKKRDIE-------LEASQLDRYKELKEQVRKKVATMTQQLEKLQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDH 431
Cdd:pfam09728 157 LLKTKELEvqlaeakLQQATEEEEKKAQEKEVAKARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFTTF 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 613410199 432 KKRIEKLeeyTKTCMDCLKE----KKQQEET---LVDEIEKTKSRMSEV 473
Cdd:pfam09728 237 KKEMEKM---SKKIKKLEKEnltwKRKWEKSnkaLLEMAEERQKLKEEL 282
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
288-487 |
7.10e-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: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 288 ETLLNQKRPQYIKAKENTSHHLKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLdaawrsfEKQIEeeilhkkrdiEL 367
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL-------QAEIA----------EA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 368 EASQLDRYKELKEQVR------------------KKVATMTQQLEKLQWEQKTDEERLAfekrrhgevqgNLKQIKEQIE 429
Cdd:COG3883 78 EAEIEERREELGERARalyrsggsvsyldvllgsESFSDFLDRLSALSKIADADADLLE-----------ELKADKAELE 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 613410199 430 DHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEKTKSRMSEVNEELNLIRSELQNA 487
Cdd:COG3883 147 AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAE 204
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
149-510 |
7.12e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 149 KERTQFFEEISTSGELIGEYEEKKRKLQKAEEDaqfnfnkkkniaAERRQAKLEKEEAERyQSLLEELKMNKIQLQlfql 228
Cdd:PRK02224 227 EQREQARETRDEADEVLEEHEERREELETLEAE------------IEDLRETIAETERER-EELAEEVRDLRERLE---- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 229 yhnekkihllntKLEHVNRDLSVKRESLSHHENIVKARKKEhgmLTRQLQQTEKELKSVETLLNQKRPQYIKAKENTSHH 308
Cdd:PRK02224 290 ------------ELEEERDDLLAEAGLDDADAEAVEARREE---LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 309 LKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEEilhkkrDIELEASQ--LDRYKELKEQVRKKV 386
Cdd:PRK02224 355 EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA------PVDLGNAEdfLEELREERDELRERE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 387 ATMTQQL----------EKLQWEQKTDE-----------ERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTC 445
Cdd:PRK02224 429 AELEATLrtarerveeaEALLEAGKCPEcgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAE 508
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613410199 446 --MDCLKEKKQQEETLVDEIEKTKSRMSEVNEELNLIRSELQNAGiDTHEGKRQQKRAEVLEHLKRL 510
Cdd:PRK02224 509 drIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEA-EEKREAAAEAEEEAEEAREEV 574
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
162-510 |
8.53e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.26 E-value: 8.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 162 GELIGEYEEKKRKLQKAEEDaqfnfNKKKNIAAERRQAKLE------KEEAERYQSLLEELKMNKIQLQLFQLYHNEKKI 235
Cdd:pfam07888 44 AELLQAQEAANRQREKEKER-----YKRDREQWERQRRELEsrvaelKEELRQSREKHEELEEKYKELSASSEELSEEKD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 236 HLLNTKLEHVNR------DLSVKRESLSHHENIVKARKKEHGMLTRQLQQTEKELKSVETLLNQkrpqyikaKENTSHHL 309
Cdd:pfam07888 119 ALLAQRAAHEARireleeDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQ--------TEEELRSL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 310 -KKLDVAKKSIKDSEKQCSKQEDDIKALETEladLDAAWRsfeKQIEEEILHK-------------------KRDIELEA 369
Cdd:pfam07888 191 sKEFQELRNSLAQRDTQVLQLQDTITTLTQK---LTTAHR---KEAENEALLEelrslqerlnaserkveglGEELSSMA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 370 SQLDRYKELKEQVRKKVATMTQQLEKLQWEQKtdEERLAFEKRRHGeVQGNLKQIKEQIEDHKKRIEKLEEYtktcmdcL 449
Cdd:pfam07888 265 AQRDRTQAELHQARLQAAQLTLQLADASLALR--EGRARWAQERET-LQQSAEADKDRIEKLSAELQRLEER-------L 334
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613410199 450 KEKKQQEETLVDEI--EKTKSR--MSEVNEELNLIRSELQNAgiDTHEGKRQQKRAEVLEHLKRL 510
Cdd:pfam07888 335 QEERMEREKLEVELgrEKDCNRvqLSESRRELQELKASLRVA--QKEKEQLQAEKQELLEYIRQL 397
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
331-501 |
8.69e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 331 DDIKALETELADLDAAWRSFEKQIEeeiLHKKRDIELEASQ---LDRYKELKEQVRKKVATMTQQLEKLQweqktdEERL 407
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQIK---TYNKNIEEQRKKNgenIARKQNKYDELVEEAKTIKAEIEELT------DELL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 408 AFEKRRhGEVQGNLK-------QIKEQIEDHKKRIEKLEEYTkTCMDClkekKQQEETLVDEIEKTKSRMSEVNEELNLI 480
Cdd:PHA02562 245 NLVMDI-EDPSAALNklntaaaKIKSKIEQFQKVIKMYEKGG-VCPTC----TQQISEGPDRITKIKDKLKELQHSLEKL 318
|
170 180
....*....|....*....|.
gi 613410199 481 RSELQNAGIDTHEGKRQQKRA 501
Cdd:PHA02562 319 DTAIDELEEIMDEFNEQSKKL 339
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
630-927 |
8.77e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 8.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 630 LSGPERQKTVAlDgtlFLKSGVISGGSSDLKYKARCWDE--KELKNLRDRRSQKIQELKGLMKTLRKETDLKQiqtliqg 707
Cdd:PHA02562 147 LSAPARRKLVE-D---LLDISVLSEMDKLNKDKIRELNQqiQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENI------- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 708 TQTRLKYSQNeLEMIKKKHlvafyQEQSQLQSELLNIESQCIMLSEGIKERQRRIKEFQEKIDKVEDDIfqHFCEEIGV- 786
Cdd:PHA02562 216 ARKQNKYDEL-VEEAKTIK-----AEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVI--KMYEKGGVc 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 787 ----ENIREFENKHVKRQQEIDQKRLEFEKQKTRlnvqleysRSHLKKKLNKINTLKetiqkgsedidhlkkaeenclQT 862
Cdd:PHA02562 288 ptctQQISEGPDRITKIKDKLKELQHSLEKLDTA--------IDELEEIMDEFNEQS---------------------KK 338
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613410199 863 VNELMAKQQQLKDIRVTQNSSAEKVQTQIEEERKKFLAVDREVGKLQKEVVSIQTSLEQKRLEKH 927
Cdd:PHA02562 339 LLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKY 403
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
26-65 |
8.91e-03 |
|
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: 38.57 E-value: 8.91e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 613410199 26 RFTCIIGPNGSGKSNVMDALS----------FVMGEKIANLRVKNIQELI 65
Cdd:cd03214 26 EIVGILGPNGAGKSTLLKTLAgllkpssgeiLLDGKDLASLSPKELARKI 75
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
160-495 |
8.92e-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: 40.42 E-value: 8.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 160 TSGELIGEYEEKKRKLQKAEEDAQFNfnkkkniaaeRRQAKLEKEEAERYQSLLEELKMNKIQL--QLFQLYHNEKKIHL 237
Cdd:TIGR00606 823 TVQQVNQEKQEKQHELDTVVSKIELN----------RKLIQDQQEQIQHLKSKTNELKSEKLQIgtNLQRRQQFEEQLVE 892
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 238 LNTKLEHVNRDLSVKRESLSHHEnivkarkkehgmltrqlQQTEKELKSVETLLNQKRPQYIKAKENTSHHLKKLDVAKK 317
Cdd:TIGR00606 893 LSTEVQSLIREIKDAKEQDSPLE-----------------TFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHG 955
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 318 SIKDSEKQCSKQEDD-IKALETELADLDAAWRSFEK---QIEEEILHKKRDIELEASQ-------------LDRYKELKE 380
Cdd:TIGR00606 956 YMKDIENKIQDGKDDyLKQKETELNTVNAQLEECEKhqeKINEDMRLMRQDIDTQKIQerwlqdnltlrkrENELKEVEE 1035
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 381 QVRKKVATMTQ-QLEKLQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEkleeyTKTCMDClkEKKQQEETL 459
Cdd:TIGR00606 1036 ELKQHLKEMGQmQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELR-----EPQFRDA--EEKYREMMI 1108
|
330 340 350
....*....|....*....|....*....|....*.
gi 613410199 460 VDEIEKtksrmsEVNEELNLIRSELQNAGIDTHEGK 495
Cdd:TIGR00606 1109 VMRTTE------LVNKDLDIYYKTLDQAIMKFHSMK 1138
|
|
| |
