|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
250-380 |
1.13e-37 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 137.79 E-value: 1.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 250 YFVAPAKFLGNQQVSYGQSLSFDYRVD---RGGRQPSAYDVILEGAGLQIRAPLMAPGKTLPcGITKTYTFRLNEHpssH 326
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEplpGGGSLNSEPDVILEGNGLRLSYSSPDQPPPDP-GQEQTYSVRLHEE---N 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 327 W----SPQLSYFEYRRLLRNLTALLIRATYGEYSTG-YIDNVTLVSARP-VSGAPAPWVE 380
Cdd:pfam00052 77 WrdsdGAPVSREDFMMVLANLTAILIRATYSTGSGQvSLSNVSLDSAVPgGSGPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
245-370 |
5.35e-37 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 135.47 E-value: 5.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 245 RSDPVYFVAPAKFLGNQQVSYGQSLSFDYRVD--RGGRQPSAYDVILEGAGLQIRAPLMAPgkTLPC-GITKTYTFRLNE 321
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDgrRGGTHVSAPDVILEGNGLRISHPAEGP--PLPDeLTTVEVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 110624798 322 HPSSHWSPQLSYfEYRRLLRNLTALLIRATYGEYSTG-YIDNVTLVSARP 370
Cdd:smart00281 79 WQYYGGRPVTRE-DLMMVLANLTAILIRATYSQQMAGsRLSDVSLEVAVP 127
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
83-127 |
2.81e-13 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 65.07 E-value: 2.81e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 110624798 83 PCNCHSKGSLSAGCD-NSGQCRCKPGVTGQRCDRCQPGFHMLTDAG 127
Cdd:cd00055 1 PCDCNGHGSLSGQCDpGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
84-128 |
3.63e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 64.64 E-value: 3.63e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 110624798 84 CNCHSKGSLSAGCD-NSGQCRCKPGVTGQRCDRCQPGFHMLTDAGC 128
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
84-123 |
2.20e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 62.76 E-value: 2.20e-12
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 110624798 84 CNCHSKGSLSAGCD-NSGQCRCKPGVTGQRCDRCQPGFHML 123
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGL 41
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
139-184 |
6.97e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 61.22 E-value: 6.97e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 110624798 139 CDCDPAGISGP-CDS--GRCVCKPAVTGERCDRCRPGYYHLDRANPEGC 184
Cdd:pfam00053 1 CDCNPHGSLSDtCDPetGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
139-184 |
3.80e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.86 E-value: 3.80e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 110624798 139 CDCDPAG-ISGPCD--SGRCVCKPAVTGERCDRCRPGYYhldRANPEGC 184
Cdd:smart00180 1 CDCDPGGsASGTCDpdTGQCECKPNVTGRRCDRCAPGYY---GDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
139-185 |
1.25e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 57.75 E-value: 1.25e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 110624798 139 CDCDPAG-ISGPCD--SGRCVCKPAVTGERCDRCRPGYYHLDRaNPEGCT 185
Cdd:cd00055 2 CDCNGHGsLSGQCDpgTGQCECKPNTTGRRCDRCAPGYYGLPS-QGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
517-564 |
7.92e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 55.44 E-value: 7.92e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 110624798 517 CQCNNNVDPnaSGNCDQLTGRCLkCIYNTAGVYCDQCKAGYFGDPLAP 564
Cdd:pfam00053 1 CDCNPHGSL--SDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDP 45
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
614-1181 |
1.06e-09 |
|
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: 63.15 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 614 YNQVKIQMDQFTQQLQSLEALVSkaqggggggtvpsgELEGRMQQAEQALRDILREAQisEGAMRALGFRLAKARSQEND 693
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLE--------------RLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEE 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 694 YKTRLDDLKMTAERIRALGSQHQNRVQDTSRLISQMRLSLAGSEASLQNtniHSSEhyvgPNGFKSLAQEATRLADSHA- 772
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN---LEGF----SEGVKALLKNQSGLSGILGv 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 773 -----------ESA------NAMKQLARETEDYSKQALSLARKALSGGGGSGVLDS-----------------SVVQGLM 818
Cdd:TIGR02168 525 lselisvdegyEAAieaalgGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSikgteiqgndreilkniEGFLGVA 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 819 GKLEKT-----KSLSQQLSR-----EGTQAdIEADRSYQHSLRL--LDS-----------ASQLQGVSDLSFQVEAKRIR 875
Cdd:TIGR02168 605 KDLVKFdpklrKALSYLLGGvlvvdDLDNA-LELAKKLRPGYRIvtLDGdlvrpggvitgGSAKTNSSILERRREIEELE 683
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 876 QKADSLSNLVTRQTDAFTRVRNNLGNWEKETRQLLQTGKDRRQTSDQLLSRANLAKNRAQEALSMGNATFYEVENILKNL 955
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 956 REFDLQVEDRKAEAEEAMKRLSSISQKVADASDKTQQAETALGSA------------------------TADTQR----- 1006
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELraeltllneeaanlrerleslerrIAATERrledl 843
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1007 AKNAAREALEISS-------------EIEQEIGSLNLEANVTADGALAMEKGLATLKSEMREMEGElaRKELEFDTDKDT 1073
Cdd:TIGR02168 844 EEQIEELSEDIESlaaeieeleelieELESELEALLNERASLEEALALLRSELEELSEELRELESK--RSELRRELEELR 921
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1074 VQLVITEAQQADARATSAgvTIQDTLN-----TLDGILHLidQPGSVDEEgmMLLEQGLFQAKTQINsRLRP--LMS--- 1143
Cdd:TIGR02168 922 EKLAQLELRLEGLEVRID--NLQERLSeeyslTLEEAEAL--ENKIEDDE--EEARRRLKRLENKIK-ELGPvnLAAiee 994
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 110624798 1144 --DLEER---VRRQRNHL----HLLETSIDGILADVKNL-----ENIRDNLP 1181
Cdd:TIGR02168 995 yeELKERydfLTAQKEDLteakETLEEAIEEIDREARERfkdtfDQVNENFQ 1046
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
620-1099 |
6.85e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 6.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 620 QMDQFTQQLQSLEALVSKAQGGGGGGTvpsgELEGRMQQAEQALRDILREAQISEGAMRALGF--RLAKARSQENDYKTR 697
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELE----ELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 698 LDDLKMTAERIRALgsqhQNRVQDTSRLISQMRLSLagsEASLQNTNIHSSEHyvgpngFKSLAQEATRLADSHAESANA 777
Cdd:COG4717 148 LEELEERLEELREL----EEELEELEAELAELQEEL---EELLEQLSLATEEE------LQDLAEELEELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 778 MKQLARETEDYSKQALSLARKALSGGggsgvldssvvqglmgKLEKTKSLSQQLSREGTQADIEA--DRSYQHSLRLLDS 855
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAA----------------LEERLKEARLLLLIAAALLALLGlgGSLLSLILTIAGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 856 ASQLQGVSDLSFQVEAK------RIRQKADSLSNLVTRQTDAFTRVRNNLGNWEKETRQLLQTGKDRRQTSDQLLSRANL 929
Cdd:COG4717 279 LFLVLGLLALLFLLLARekaslgKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 930 AKNRAQealsmgnatfyeVENILKNLREFdlqVEDRKAEAEEAMKRLssisqkvADASDKTQQAETALGSATADTQRAKN 1009
Cdd:COG4717 359 LEEELQ------------LEELEQEIAAL---LAEAGVEDEEELRAA-------LEQAEEYQELKEELEELEEQLEELLG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1010 AAREALEISS--EIEQEIGSLNLEANVTADGALAMEKGLATLKSEMREME--GELARKELEFDTDKDTvqlvITEAQQAD 1085
Cdd:COG4717 417 ELEELLEALDeeELEEELEELEEELEELEEELEELREELAELEAELEQLEedGELAELLQELEELKAE----LRELAEEW 492
|
490
....*....|....
gi 110624798 1086 ARATSAGVTIQDTL 1099
Cdd:COG4717 493 AALKLALELLEEAR 506
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
516-565 |
1.09e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 52.36 E-value: 1.09e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 110624798 516 RCQCNNNVDPNasGNCDQLTGRCLkCIYNTAGVYCDQCKAGYFGDPLAPN 565
Cdd:cd00055 1 PCDCNGHGSLS--GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGG 47
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
649-1180 |
2.52e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 649 SGELEGRMQQAEQALRDILREAQISEGAMRALGFRLAKARSqendyktRLDDLKMTAERIRALGSQHQNRVQDTSRL--- 725
Cdd:PRK03918 188 TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEK-------EVKELEELKEEIEELEKELESLEGSKRKLeek 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 726 ISQMRLSLAGSEASLQNTnihssEHYVGP-NGFKSLAQEATRLADSHAESANAMKQLARETEDYSKQAlslarkalsggg 804
Cdd:PRK03918 261 IRELEERIEELKKEIEEL-----EEKVKElKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEI------------ 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 805 gsgvldsSVVQGLMGKLEKTKSLSQQLS--REGTQADIEA----DRSYQHSLRLLDsasQLQGVSDLSFQVEAKRIRQKA 878
Cdd:PRK03918 324 -------NGIEERIKELEEKEERLEELKkkLKELEKRLEEleerHELYEEAKAKKE---ELERLKKRLTGLTPEKLEKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 879 DSLSNLVTRQTDAFTRVRNNLGNWEKETRQL------LQTGKDRRQTSDQLLS---RANL-AKNRAqealsmgnatfyEV 948
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELkkaieeLKKAKGKCPVCGRELTeehRKELlEEYTA------------EL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 949 ENILKNLREFDLQVEDRKAEAEEAMKRLSSISQ--KVADASDKTQQAETALGSATA-DTQRAKNAAREALEISSEIEQEI 1025
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLeELEKKAEEYEKLKEKLIKLKGEI 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1026 GSLNLEANVTADgalaMEKGLATLKSEMREMEGELAR-----KELEFDTDKDtVQLVITEAQQADAR---ATSAGVTIQD 1097
Cdd:PRK03918 542 KSLKKELEKLEE----LKKKLAELEKKLDELEEELAEllkelEELGFESVEE-LEERLKELEPFYNEyleLKDAEKELER 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1098 TLNTLDGILHLIDQPgsvdEEGMMLLEQGLFQAKTQINS-----------RLRPLMSDLEERVRRQRNHLHLLETSIDGI 1166
Cdd:PRK03918 617 EEKELKKLEEELDKA----FEELAETEKRLEELRKELEElekkyseeeyeELREEYLELSRELAGLRAELEELEKRREEI 692
|
570
....*....|....
gi 110624798 1167 LADVKNLENIRDNL 1180
Cdd:PRK03918 693 KKTLEKLKEELEER 706
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
517-561 |
5.16e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.31 E-value: 5.16e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 110624798 517 CQCNnnVDPNASGNCDQLTGRCLkCIYNTAGVYCDQCKAGYFGDP 561
Cdd:smart00180 1 CDCD--PGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
653-1087 |
3.41e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 51.75 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 653 EGRMQQAEQALRDILREAQ--ISEgAMRALGFRLAKARSQeNDYKTRlddlkmTAERIRALGSQHQNRVQDTSRLISQMR 730
Cdd:NF041483 264 EQRMQEAEEALREARAEAEkvVAE-AKEAAAKQLASAESA-NEQRTR------TAKEEIARLVGEATKEAEALKAEAEQA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 731 LSLAGSEAslqntnihssehyvgpngfKSLAQEATRLADSHA--ESANAMKQLARETEDYSKQALSLARkalsggggsgv 808
Cdd:NF041483 336 LADARAEA-------------------EKLVAEAAEKARTVAaeDTAAQLAKAARTAEEVLTKASEDAK----------- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 809 ldssvvqglmgklEKTKSLSQQLSREGTQADIEADRsyqhsLR--LLDSASQLQGVSD----------LSFQVEAKRIRQ 876
Cdd:NF041483 386 -------------ATTRAAAEEAERIRREAEAEADR-----LRgeAADQAEQLKGAAKddtkeyraktVELQEEARRLRG 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 877 KADSL------------------------------SNLVTR-QTDAFTRVRNNLGNWEK-ETRQLLQTGKDRRQTSDQL- 923
Cdd:NF041483 448 EAEQLraeavaegerirgearreavqqieeaartaEELLTKaKADADELRSTATAESERvRTEAIERATTLRRQAEETLe 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 924 LSRANLAKNRAqEALSMGNATFYEVENILKNLR-EFDLQVEDRKAEAEEAMKRLSsisqkvADASDKTQQAETALGSATA 1002
Cdd:NF041483 528 RTRAEAERLRA-EAEEQAEEVRAAAERAARELReETERAIAARQAEAAEELTRLH------TEAEERLTAAEEALADARA 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1003 DTQRAKNAAREALE------------ISSEIEQEIGSLNLEANVTADGALAMEKGLAT-LKSEMREmEGELARKELefdt 1069
Cdd:NF041483 601 EAERIRREAAEETErlrteaaerirtLQAQAEQEAERLRTEAAADASAARAEGENVAVrLRSEAAA-EAERLKSEA---- 675
|
490
....*....|....*...
gi 110624798 1070 dKDTVQLVITEAQQADAR 1087
Cdd:NF041483 676 -QESADRVRAEAAAAAER 692
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
461-509 |
3.63e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 45.04 E-value: 3.63e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 110624798 461 PCPCHNGFSCSVMPETEEVVCNnCPPGVTGARCELCADGFFGDPFGERG 509
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
904-1062 |
4.82e-06 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 48.91 E-value: 4.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 904 KETRQLLQTGKDRRQTSDQLLSRANLAK---NRAQEALSMGN-----ATFYEVENILKNLREFDLQVEDRKAEAEEAMKR 975
Cdd:pfam04012 40 KARQALAQTIARQKQLERRLEQQTEQAKkleEKAQAALTKGNeelarEALAEKKSLEKQAEALETQLAQQRSAVEQLRKQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 976 LSSISQKVADASDKTQ----QAETALGSATADTQRAKNAAREALEISSEIEQEIgsLNLEANVTADGALAMEKGL-ATLK 1050
Cdd:pfam04012 120 LAALETKIQQLKAKKNllkaRLKAAKAQEAVQTSLGSLSTSSATDSFERIEEKI--EEREARADAAAELASAVDLdAKLE 197
|
170
....*....|....*
gi 110624798 1051 SEMREMEG---ELAR 1062
Cdd:pfam04012 198 QAGIQMEVsedVLAR 212
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
462-507 |
1.15e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 43.45 E-value: 1.15e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 110624798 462 CPCHNGFSCSVMPETEEVVCNnCPPGVTGARCELCADGFFGDPFGE 507
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
572-604 |
1.60e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 43.11 E-value: 1.60e-05
10 20 30
....*....|....*....|....*....|....
gi 110624798 572 ACNCSPMGSEPGEC-RGDGSCVCKPGFGGLNCDH 604
Cdd:cd00055 1 PCDCNGHGSLSGQCdPGTGQCECKPNTTGRRCDR 34
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
914-1032 |
1.23e-04 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 43.20 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 914 KDRRQTSDQLLSRANLAKNRAQEALSmgnatfyEVENILKNLREfdlQVEDRKAEAEEAMKRLssISQKVADAsdkTQQA 993
Cdd:cd06503 29 DEREEKIAESLEEAEKAKEEAEELLA-------EYEEKLAEARA---EAQEIIEEARKEAEKI--KEEILAEA---KEEA 93
|
90 100 110
....*....|....*....|....*....|....*....
gi 110624798 994 ETALGSATADTQRAKNAAREaleissEIEQEIGSLNLEA 1032
Cdd:cd06503 94 ERILEQAKAEIEQEKEKALA------ELRKEVADLAVEA 126
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
658-1059 |
1.53e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 46.36 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 658 QAEQalrdILREAQISEGAMRALGFR-LAKARSQendyktrlddlkmtAERIRALGSQHQNRVQ---DTSRLISQMRLSL 733
Cdd:NF041483 73 QAEQ----LLRNAQIQADQLRADAEReLRDARAQ--------------TQRILQEHAEHQARLQaelHTEAVQRRQQLDQ 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 734 AGSEASlQNTNIHSSEHYVGPNGFKS-LAQEATRLAD-SHAESANAMKQLARETEDYSKQALslarkalsggggsgvlds 811
Cdd:NF041483 135 ELAERR-QTVESHVNENVAWAEQLRArTESQARRLLDeSRAEAEQALAAARAEAERLAEEAR------------------ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 812 svvQGLMGKLEKTKSLSQQLSREGtQADIEadrsyqhslRLLDSAS-QLQGVSDLSFQV------EAKRIRQKADSLSNL 884
Cdd:NF041483 196 ---QRLGSEAESARAEAEAILRRA-RKDAE---------RLLNAAStQAQEATDHAEQLrsstaaESDQARRQAAELSRA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 885 V-TRQTDAFTRVRNNLGNWEKETRQLLQTGKDRRQTSD-QLLSRANLAKNR----AQEALSMGNATFYEVENILKNLREf 958
Cdd:NF041483 263 AeQRMQEAEEALREARAEAEKVVAEAKEAAAKQLASAEsANEQRTRTAKEEiarlVGEATKEAEALKAEAEQALADARA- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 959 dlQVEDRKAEAEEAmKRLSSISQKVADASDKTQQAETALGSATADTQRA-KNAAREALEISSEIEQEIGSLNLEANVTAD 1037
Cdd:NF041483 342 --EAEKLVAEAAEK-ARTVAAEDTAAQLAKAARTAEEVLTKASEDAKATtRAAAEEAERIRREAEAEADRLRGEAADQAE 418
|
410 420 430
....*....|....*....|....*....|....
gi 110624798 1038 GAlameKGLAT------------LKSEMREMEGE 1059
Cdd:NF041483 419 QL----KGAAKddtkeyraktveLQEEARRLRGE 448
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
28-86 |
1.75e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 40.41 E-value: 1.75e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110624798 28 CDCNG---KSRQCvfdqelHRQTGsgfRCLnCNDNTAGVHCERCREGFYRHRdrdRCLPCNC 86
Cdd:pfam00053 1 CDCNPhgsLSDTC------DPETG---QCL-CKPGVTGRHCDRCKPGYYGLP---SDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
573-604 |
2.12e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.99 E-value: 2.12e-04
10 20 30
....*....|....*....|....*....|...
gi 110624798 573 CNCSPMGSEPGEC-RGDGSCVCKPGFGGLNCDH 604
Cdd:smart00180 1 CDCDPGGSASGTCdPDTGQCECKPNVTGRRCDR 33
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
573-604 |
2.52e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 39.64 E-value: 2.52e-04
10 20 30
....*....|....*....|....*....|...
gi 110624798 573 CNCSPMGSEPGEC-RGDGSCVCKPGFGGLNCDH 604
Cdd:pfam00053 1 CDCNPHGSLSDTCdPETGQCLCKPGVTGRHCDR 33
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
28-74 |
1.57e-03 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 37.72 E-value: 1.57e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 110624798 28 CDCNG---KSRQCvfdqelHRQTGsgfRCLnCNDNTAGVHCERCREGFYR 74
Cdd:cd00055 2 CDCNGhgsLSGQC------DPGTG---QCE-CKPNTTGRRCDRCAPGYYG 41
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
484-506 |
3.20e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 36.56 E-value: 3.20e-03
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
250-380 |
1.13e-37 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 137.79 E-value: 1.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 250 YFVAPAKFLGNQQVSYGQSLSFDYRVD---RGGRQPSAYDVILEGAGLQIRAPLMAPGKTLPcGITKTYTFRLNEHpssH 326
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEplpGGGSLNSEPDVILEGNGLRLSYSSPDQPPPDP-GQEQTYSVRLHEE---N 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 327 W----SPQLSYFEYRRLLRNLTALLIRATYGEYSTG-YIDNVTLVSARP-VSGAPAPWVE 380
Cdd:pfam00052 77 WrdsdGAPVSREDFMMVLANLTAILIRATYSTGSGQvSLSNVSLDSAVPgGSGPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
245-370 |
5.35e-37 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 135.47 E-value: 5.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 245 RSDPVYFVAPAKFLGNQQVSYGQSLSFDYRVD--RGGRQPSAYDVILEGAGLQIRAPLMAPgkTLPC-GITKTYTFRLNE 321
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDgrRGGTHVSAPDVILEGNGLRISHPAEGP--PLPDeLTTVEVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 110624798 322 HPSSHWSPQLSYfEYRRLLRNLTALLIRATYGEYSTG-YIDNVTLVSARP 370
Cdd:smart00281 79 WQYYGGRPVTRE-DLMMVLANLTAILIRATYSQQMAGsRLSDVSLEVAVP 127
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
83-127 |
2.81e-13 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 65.07 E-value: 2.81e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 110624798 83 PCNCHSKGSLSAGCD-NSGQCRCKPGVTGQRCDRCQPGFHMLTDAG 127
Cdd:cd00055 1 PCDCNGHGSLSGQCDpGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
84-128 |
3.63e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 64.64 E-value: 3.63e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 110624798 84 CNCHSKGSLSAGCD-NSGQCRCKPGVTGQRCDRCQPGFHMLTDAGC 128
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
84-123 |
2.20e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 62.76 E-value: 2.20e-12
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 110624798 84 CNCHSKGSLSAGCD-NSGQCRCKPGVTGQRCDRCQPGFHML 123
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGL 41
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
139-184 |
6.97e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 61.22 E-value: 6.97e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 110624798 139 CDCDPAGISGP-CDS--GRCVCKPAVTGERCDRCRPGYYHLDRANPEGC 184
Cdd:pfam00053 1 CDCNPHGSLSDtCDPetGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
139-184 |
3.80e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.86 E-value: 3.80e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 110624798 139 CDCDPAG-ISGPCD--SGRCVCKPAVTGERCDRCRPGYYhldRANPEGC 184
Cdd:smart00180 1 CDCDPGGsASGTCDpdTGQCECKPNVTGRRCDRCAPGYY---GDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
139-185 |
1.25e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 57.75 E-value: 1.25e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 110624798 139 CDCDPAG-ISGPCD--SGRCVCKPAVTGERCDRCRPGYYHLDRaNPEGCT 185
Cdd:cd00055 2 CDCNGHGsLSGQCDpgTGQCECKPNTTGRRCDRCAPGYYGLPS-QGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
517-564 |
7.92e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 55.44 E-value: 7.92e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 110624798 517 CQCNNNVDPnaSGNCDQLTGRCLkCIYNTAGVYCDQCKAGYFGDPLAP 564
Cdd:pfam00053 1 CDCNPHGSL--SDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDP 45
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
614-1181 |
1.06e-09 |
|
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: 63.15 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 614 YNQVKIQMDQFTQQLQSLEALVSkaqggggggtvpsgELEGRMQQAEQALRDILREAQisEGAMRALGFRLAKARSQEND 693
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLE--------------RLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEE 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 694 YKTRLDDLKMTAERIRALGSQHQNRVQDTSRLISQMRLSLAGSEASLQNtniHSSEhyvgPNGFKSLAQEATRLADSHA- 772
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN---LEGF----SEGVKALLKNQSGLSGILGv 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 773 -----------ESA------NAMKQLARETEDYSKQALSLARKALSGGGGSGVLDS-----------------SVVQGLM 818
Cdd:TIGR02168 525 lselisvdegyEAAieaalgGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSikgteiqgndreilkniEGFLGVA 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 819 GKLEKT-----KSLSQQLSR-----EGTQAdIEADRSYQHSLRL--LDS-----------ASQLQGVSDLSFQVEAKRIR 875
Cdd:TIGR02168 605 KDLVKFdpklrKALSYLLGGvlvvdDLDNA-LELAKKLRPGYRIvtLDGdlvrpggvitgGSAKTNSSILERRREIEELE 683
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 876 QKADSLSNLVTRQTDAFTRVRNNLGNWEKETRQLLQTGKDRRQTSDQLLSRANLAKNRAQEALSMGNATFYEVENILKNL 955
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 956 REFDLQVEDRKAEAEEAMKRLSSISQKVADASDKTQQAETALGSA------------------------TADTQR----- 1006
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELraeltllneeaanlrerleslerrIAATERrledl 843
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1007 AKNAAREALEISS-------------EIEQEIGSLNLEANVTADGALAMEKGLATLKSEMREMEGElaRKELEFDTDKDT 1073
Cdd:TIGR02168 844 EEQIEELSEDIESlaaeieeleelieELESELEALLNERASLEEALALLRSELEELSEELRELESK--RSELRRELEELR 921
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1074 VQLVITEAQQADARATSAgvTIQDTLN-----TLDGILHLidQPGSVDEEgmMLLEQGLFQAKTQINsRLRP--LMS--- 1143
Cdd:TIGR02168 922 EKLAQLELRLEGLEVRID--NLQERLSeeyslTLEEAEAL--ENKIEDDE--EEARRRLKRLENKIK-ELGPvnLAAiee 994
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 110624798 1144 --DLEER---VRRQRNHL----HLLETSIDGILADVKNL-----ENIRDNLP 1181
Cdd:TIGR02168 995 yeELKERydfLTAQKEDLteakETLEEAIEEIDREARERfkdtfDQVNENFQ 1046
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
620-1099 |
6.85e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 6.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 620 QMDQFTQQLQSLEALVSKAQGGGGGGTvpsgELEGRMQQAEQALRDILREAQISEGAMRALGF--RLAKARSQENDYKTR 697
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELE----ELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 698 LDDLKMTAERIRALgsqhQNRVQDTSRLISQMRLSLagsEASLQNTNIHSSEHyvgpngFKSLAQEATRLADSHAESANA 777
Cdd:COG4717 148 LEELEERLEELREL----EEELEELEAELAELQEEL---EELLEQLSLATEEE------LQDLAEELEELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 778 MKQLARETEDYSKQALSLARKALSGGggsgvldssvvqglmgKLEKTKSLSQQLSREGTQADIEA--DRSYQHSLRLLDS 855
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAA----------------LEERLKEARLLLLIAAALLALLGlgGSLLSLILTIAGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 856 ASQLQGVSDLSFQVEAK------RIRQKADSLSNLVTRQTDAFTRVRNNLGNWEKETRQLLQTGKDRRQTSDQLLSRANL 929
Cdd:COG4717 279 LFLVLGLLALLFLLLARekaslgKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 930 AKNRAQealsmgnatfyeVENILKNLREFdlqVEDRKAEAEEAMKRLssisqkvADASDKTQQAETALGSATADTQRAKN 1009
Cdd:COG4717 359 LEEELQ------------LEELEQEIAAL---LAEAGVEDEEELRAA-------LEQAEEYQELKEELEELEEQLEELLG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1010 AAREALEISS--EIEQEIGSLNLEANVTADGALAMEKGLATLKSEMREME--GELARKELEFDTDKDTvqlvITEAQQAD 1085
Cdd:COG4717 417 ELEELLEALDeeELEEELEELEEELEELEEELEELREELAELEAELEQLEedGELAELLQELEELKAE----LRELAEEW 492
|
490
....*....|....
gi 110624798 1086 ARATSAGVTIQDTL 1099
Cdd:COG4717 493 AALKLALELLEEAR 506
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
516-565 |
1.09e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 52.36 E-value: 1.09e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 110624798 516 RCQCNNNVDPNasGNCDQLTGRCLkCIYNTAGVYCDQCKAGYFGDPLAPN 565
Cdd:cd00055 1 PCDCNGHGSLS--GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGG 47
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
650-1180 |
2.24e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 650 GELEGRMQ----QAEQA-----LRDILREAQISEGAMR--ALGFRLAKARSQENDYKTRLDDLkmtAERIRALGSQHqnr 718
Cdd:TIGR02168 196 NELERQLKslerQAEKAerykeLKAELRELELALLVLRleELREELEELQEELKEAEEELEEL---TAELQELEEKL--- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 719 vqDTSRL-ISQMRLSLAGSEASLQNTNIHSSEHyvgpNGFKSLAQEatRLADSHAESANAMKQLAREtedysKQALSLAR 797
Cdd:TIGR02168 270 --EELRLeVSELEEEIEELQKELYALANEISRL----EQQKQILRE--RLANLERQLEELEAQLEEL-----ESKLDELA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 798 KALSGGGGSGVLDSSVVQGLMGKLEKTKSLSQQLSR--EGTQADIEADRS--YQHSLRLLDSASQLQGVSDLSFQVEAKR 873
Cdd:TIGR02168 337 EELAELEEKLEELKEELESLEAELEELEAELEELESrlEELEEQLETLRSkvAQLELQIASLNNEIERLEARLERLEDRR 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 874 IRQKADSLSNLVTRQTDAFTRVRNNLGNWEKETRQLLQTGKDRRQ---TSDQLLSRANLAKNRAQEALSMGNATFYEVEN 950
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEaleELREELEEAEQALDAAERELAQLQARLDSLER 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 951 ILKNLREFDLQVEDRKAEAEEAMKRLSSISQKVADASDKTQQAETALGS-ATADTQRAKNAAREAleISSEIEQEIGSLN 1029
Cdd:TIGR02168 497 LQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGrLQAVVVENLNAAKKA--IAFLKQNELGRVT 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1030 -LEANVTADGALAMEKGlatlksEMREMEGELARKELEFDTDKDTVQLVITeaqqadarATSAGVTIQDTLNTLDGILHL 1108
Cdd:TIGR02168 575 fLPLDSIKGTEIQGNDR------EILKNIEGFLGVAKDLVKFDPKLRKALS--------YLLGGVLVVDDLDNALELAKK 640
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110624798 1109 IDQPGS-VDEEGMMLLEQGL--FQAKTQINSRL--RPLMSDLEERVRRQRNHLHLLETSIDGILADVKNLENIRDNL 1180
Cdd:TIGR02168 641 LRPGYRiVTLDGDLVRPGGVitGGSAKTNSSILerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL 717
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
657-1133 |
2.97e-08 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 57.99 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 657 QQAEQALRDILREAQISEGAMRalGFR-------LAKARSQENDYKTRLDDLKMT-------AERIRALGSQHQNRVQDT 722
Cdd:COG5278 46 YEVLRALEELLSALLDAETGQR--GYLltgdesfLEPYEEARAEIDELLAELRSLtadnpeqQARLDELEALIDQWLAEL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 723 SRLISQMRLSlaGSEASLQntnihssehYVGPNGFKSLAQEATRLADSHAESANAMKQLARETEDYSKQALSLARKALSG 802
Cdd:COG5278 124 EQVIALRRAG--GLEAALA---------LVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 803 GGGSGVLDSSVVQGLMGKLEKTKSLSQQLSREGTQADIEADRSYQHSLRLLDSASQLQGVSDLSFQVEAKRIRQKADSLS 882
Cdd:COG5278 193 LLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 883 NLVTRQTDAFTRVRNNLGNWEKETRQLLQTGKDRRQTSDQLLSRANLAKNRAQEALSMGNATFYEVENILKNLREFDLQV 962
Cdd:COG5278 273 LLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLA 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 963 EDRKAEAEEAMKRLSSISQKVADASDKTQQAETALGSATADTQRAKNAAREALEISSEIEQEIGSLNLEANVTADGALAM 1042
Cdd:COG5278 353 EAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEAL 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1043 EKGLATLKSEMREMEGELARKELEFDTDKDTVQLVITEAQQADARATSAGVTIQDTLNTLDGILHLIDQPGSVDEEGMML 1122
Cdd:COG5278 433 ALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAA 512
|
490
....*....|.
gi 110624798 1123 LEQGLFQAKTQ 1133
Cdd:COG5278 513 AEAALAAALAA 523
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
620-1062 |
1.06e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 620 QMDQFTQQLQSLEALVSKAQGGGGggtvpsgELEGRMQQAEQALRDILREAQISEGAMRALGFRLAKARSQENDYKTRLD 699
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELE-------EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 700 DLKMTAERIRALGSQHQNRVQD--------------TSRLISQMRLSLAGSEASLQNTNIHSSEHYVGPNGFKSLAQEAT 765
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEEleealaeleeeeeeEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 766 RLADSHAESANAMKQLARETEDYSKQALSLARKALSGGGGSGVLDSSVVQGLMGKLEKTkSLSQQLSREGTQADIEADRS 845
Cdd:COG1196 484 EELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEA-ALAAALQNIVVEDDEVAAAA 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 846 YQHSLRLLDSA-----SQLQGVSDLSFQVEAKRIRQKADSLSNLVTRQTDAFTRVRNNLGNWEKETRQLLQTGKDRRQTS 920
Cdd:COG1196 563 IEYLKAAKAGRatflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTL 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 921 DQLLSRANLAKNRAQEALSMGNATFYEVENILKNLREFDLQVEDRKAEAEEAMKRLssiSQKVADASDKTQQAETALGSA 1000
Cdd:COG1196 643 AGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEA---LLAEEEEERELAEAEEERLEE 719
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110624798 1001 TADTQRAKNAAREALEISSEIEQEIGSLNLEAnvtADGALAMEKGLATLKSEMREMEGELAR 1062
Cdd:COG1196 720 ELEEEALEEQLEAEREELLEELLEEEELLEEE---ALEELPEPPDLEELERELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
829-1091 |
1.19e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 829 QQLSREGTQADIEA----DRSYQHSLRLLDSASQLQgvsdlsfQVEAKRIRQKADSLSNLVTRQTDAFTRVRNNLgnweK 904
Cdd:COG1196 216 RELKEELKELEAELlllkLRELEAELEELEAELEEL-------EAELEELEAELAELEAELEELRLELEELELEL----E 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 905 ETRQLLQTGKDRRQTSDQLLSRANLAKNRAQEALsmgnatfyevENILKNLREFDLQVEDRKAEAEEAMKRLSSISQKVA 984
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLEERRRELEERL----------EELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 985 DASDKTQQAETALGSATADTQRAKNAAREALEISSEIEQEIgslnLEANVTADGALAMEKGLATLKSEMREMEGELARKE 1064
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA----AELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260
....*....|....*....|....*..
gi 110624798 1065 LEFDTDKDTVQLVITEAQQADARATSA 1091
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEE 457
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
870-1180 |
1.89e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.91 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 870 EAKRIRQKADSLSNLVTRQTDAFTRVRNNLgnwEKETRQLLQTGKDRRQTSDQLlSRANLAKNRAQEALSmgnatfyEVE 949
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEEL---EQARSELEQLEEELEELNEQL-QAAQAELAQAQEELE-------SLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 950 NILKNLREfdlQVEDRKAEAEEAMKRLSSISQKVADASDKTQQAETALGSATADTQRAKNAArEALEIS------SEIEQ 1023
Cdd:COG4372 108 EEAEELQE---ELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL-AALEQElqalseAEAEQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1024 EIGSLNLEANVTADGALAMEKGLATLKSEMR---EMEGELARKELEFDTDKDTVQLVITEAQQADARATSAGVTIQDTLN 1100
Cdd:COG4372 184 ALDELLKEANRNAEKEEELAEAEKLIESLPRelaEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1101 TLDGILHLIDQPGSVDEEGMMLLEQGLFQAKTQINSRLRPLMSDLEERVRRQRNHLHLLETSIDGILADVKNLENIRDNL 1180
Cdd:COG4372 264 ELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLL 343
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
649-1180 |
2.52e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 649 SGELEGRMQQAEQALRDILREAQISEGAMRALGFRLAKARSqendyktRLDDLKMTAERIRALGSQHQNRVQDTSRL--- 725
Cdd:PRK03918 188 TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEK-------EVKELEELKEEIEELEKELESLEGSKRKLeek 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 726 ISQMRLSLAGSEASLQNTnihssEHYVGP-NGFKSLAQEATRLADSHAESANAMKQLARETEDYSKQAlslarkalsggg 804
Cdd:PRK03918 261 IRELEERIEELKKEIEEL-----EEKVKElKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEI------------ 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 805 gsgvldsSVVQGLMGKLEKTKSLSQQLS--REGTQADIEA----DRSYQHSLRLLDsasQLQGVSDLSFQVEAKRIRQKA 878
Cdd:PRK03918 324 -------NGIEERIKELEEKEERLEELKkkLKELEKRLEEleerHELYEEAKAKKE---ELERLKKRLTGLTPEKLEKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 879 DSLSNLVTRQTDAFTRVRNNLGNWEKETRQL------LQTGKDRRQTSDQLLS---RANL-AKNRAqealsmgnatfyEV 948
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELkkaieeLKKAKGKCPVCGRELTeehRKELlEEYTA------------EL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 949 ENILKNLREFDLQVEDRKAEAEEAMKRLSSISQ--KVADASDKTQQAETALGSATA-DTQRAKNAAREALEISSEIEQEI 1025
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLeELEKKAEEYEKLKEKLIKLKGEI 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1026 GSLNLEANVTADgalaMEKGLATLKSEMREMEGELAR-----KELEFDTDKDtVQLVITEAQQADAR---ATSAGVTIQD 1097
Cdd:PRK03918 542 KSLKKELEKLEE----LKKKLAELEKKLDELEEELAEllkelEELGFESVEE-LEERLKELEPFYNEyleLKDAEKELER 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1098 TLNTLDGILHLIDQPgsvdEEGMMLLEQGLFQAKTQINS-----------RLRPLMSDLEERVRRQRNHLHLLETSIDGI 1166
Cdd:PRK03918 617 EEKELKKLEEELDKA----FEELAETEKRLEELRKELEElekkyseeeyeELREEYLELSRELAGLRAELEELEKRREEI 692
|
570
....*....|....
gi 110624798 1167 LADVKNLENIRDNL 1180
Cdd:PRK03918 693 KKTLEKLKEELEER 706
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
762-1118 |
3.28e-07 |
|
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: 55.07 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 762 QEATRLAD--SHAESANAMKQLARETEDY----SKQALSLARKALSGGggsgvldssvVQGLMGKLEKTKSLSQQLSREg 835
Cdd:TIGR02169 198 QQLERLRRerEKAERYQALLKEKREYEGYellkEKEALERQKEAIERQ----------LASLEEELEKLTEEISELEKR- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 836 tQADIEADRSyQHSLRL--LDSASQLQGVSDL-SFQVEAKR----IRQKADSLSNLVTRQTDAFTRVRNNLGNWEKETRQ 908
Cdd:TIGR02169 267 -LEEIEQLLE-ELNKKIkdLGEEEQLRVKEKIgELEAEIASlersIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 909 LLQTGKDRRQTSDQLlsranlaKNRAQEAlsmgNATFYEVENILKNLREFDLQVEDRKAEAEEAMKRLSSISQKVADASD 988
Cdd:TIGR02169 345 IEEERKRRDKLTEEY-------AELKEEL----EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 989 KTQQAETALGSATADTQRAKNAAREALEISSEIEQEIGSLNLEANVTADGALAMEKGLATLKSEMREMEGELARKELEFD 1068
Cdd:TIGR02169 414 ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 110624798 1069 tdkdtvqlvITEAQQADARATSAG-VTIQDTLN-TLDGILHLIDQPGSVDEE 1118
Cdd:TIGR02169 494 ---------EAEAQARASEERVRGgRAVEEVLKaSIQGVHGTVAQLGSVGER 536
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
517-561 |
5.16e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.31 E-value: 5.16e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 110624798 517 CQCNnnVDPNASGNCDQLTGRCLkCIYNTAGVYCDQCKAGYFGDP 561
Cdd:smart00180 1 CDCD--PGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
896-1193 |
1.81e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.83 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 896 RNNLGNWEKETRQLLQTGKDRRQTSDQLLSRANLAKNRAQEalsmgnatfyEVENILKNLREFDLQVEDRKAEAEEAMKR 975
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLRE----------ELEQAREELEQLEEELEQARSELEQLEEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 976 LSSISQKVADASDKTQQAETALGSAtadtQRAKNAAREALEissEIEQEIGSLNLEANvtadgalAMEKGLATLKSEMRE 1055
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESL----QEEAEELQEELE---ELQKERQDLEQQRK-------QLEAQIAELQSEIAE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1056 MEGELarKELEfdtdkdtVQLVITEAQQADARATSAGVTIQDTLNTLDGILHLIDQPGSVDEEGMMLLEQGLFQAKTQIN 1135
Cdd:COG4372 148 REEEL--KELE-------EQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAE 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 110624798 1136 SRLRPLMSDLEERVRRQRNHLHLLETSIDGILADVKNLENIRDNLPPGCYNTQALEQQ 1193
Cdd:COG4372 219 ELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEE 276
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
653-1087 |
3.41e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 51.75 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 653 EGRMQQAEQALRDILREAQ--ISEgAMRALGFRLAKARSQeNDYKTRlddlkmTAERIRALGSQHQNRVQDTSRLISQMR 730
Cdd:NF041483 264 EQRMQEAEEALREARAEAEkvVAE-AKEAAAKQLASAESA-NEQRTR------TAKEEIARLVGEATKEAEALKAEAEQA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 731 LSLAGSEAslqntnihssehyvgpngfKSLAQEATRLADSHA--ESANAMKQLARETEDYSKQALSLARkalsggggsgv 808
Cdd:NF041483 336 LADARAEA-------------------EKLVAEAAEKARTVAaeDTAAQLAKAARTAEEVLTKASEDAK----------- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 809 ldssvvqglmgklEKTKSLSQQLSREGTQADIEADRsyqhsLR--LLDSASQLQGVSD----------LSFQVEAKRIRQ 876
Cdd:NF041483 386 -------------ATTRAAAEEAERIRREAEAEADR-----LRgeAADQAEQLKGAAKddtkeyraktVELQEEARRLRG 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 877 KADSL------------------------------SNLVTR-QTDAFTRVRNNLGNWEK-ETRQLLQTGKDRRQTSDQL- 923
Cdd:NF041483 448 EAEQLraeavaegerirgearreavqqieeaartaEELLTKaKADADELRSTATAESERvRTEAIERATTLRRQAEETLe 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 924 LSRANLAKNRAqEALSMGNATFYEVENILKNLR-EFDLQVEDRKAEAEEAMKRLSsisqkvADASDKTQQAETALGSATA 1002
Cdd:NF041483 528 RTRAEAERLRA-EAEEQAEEVRAAAERAARELReETERAIAARQAEAAEELTRLH------TEAEERLTAAEEALADARA 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1003 DTQRAKNAAREALE------------ISSEIEQEIGSLNLEANVTADGALAMEKGLAT-LKSEMREmEGELARKELefdt 1069
Cdd:NF041483 601 EAERIRREAAEETErlrteaaerirtLQAQAEQEAERLRTEAAADASAARAEGENVAVrLRSEAAA-EAERLKSEA---- 675
|
490
....*....|....*...
gi 110624798 1070 dKDTVQLVITEAQQADAR 1087
Cdd:NF041483 676 -QESADRVRAEAAAAAER 692
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
461-509 |
3.63e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 45.04 E-value: 3.63e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 110624798 461 PCPCHNGFSCSVMPETEEVVCNnCPPGVTGARCELCADGFFGDPFGERG 509
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
947-1088 |
4.66e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.15 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 947 EVENILKNLREFDLQVEDRKAEAEEAMKRLSSISQKVADASDKTQQAETALGSAtadtqraKNAaREALEISSEIEQ--- 1023
Cdd:COG1579 32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-------RNN-KEYEALQKEIESlkr 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110624798 1024 EIGSLN---LEANVTADgalAMEKGLATLKSEMREMEGELARKELEFDTdkdtvQLVITEAQQADARA 1088
Cdd:COG1579 104 RISDLEdeiLELMERIE---ELEEELAELEAELAELEAELEEKKAELDE-----ELAELEAELEELEA 163
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
904-1062 |
4.82e-06 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 48.91 E-value: 4.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 904 KETRQLLQTGKDRRQTSDQLLSRANLAK---NRAQEALSMGN-----ATFYEVENILKNLREFDLQVEDRKAEAEEAMKR 975
Cdd:pfam04012 40 KARQALAQTIARQKQLERRLEQQTEQAKkleEKAQAALTKGNeelarEALAEKKSLEKQAEALETQLAQQRSAVEQLRKQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 976 LSSISQKVADASDKTQ----QAETALGSATADTQRAKNAAREALEISSEIEQEIgsLNLEANVTADGALAMEKGL-ATLK 1050
Cdd:pfam04012 120 LAALETKIQQLKAKKNllkaRLKAAKAQEAVQTSLGSLSTSSATDSFERIEEKI--EEREARADAAAELASAVDLdAKLE 197
|
170
....*....|....*
gi 110624798 1051 SEMREMEG---ELAR 1062
Cdd:pfam04012 198 QAGIQMEVsedVLAR 212
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
903-1180 |
6.46e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 6.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 903 EKETRQLLQTGKDRRQtsdqLLSRANLAKNRAQEALSmgnatfyEVENILKNLREFDLQVEDRKAEAEEAMKRLSSISQK 982
Cdd:COG1196 221 ELKELEAELLLLKLRE----LEAELEELEAELEELEA-------ELEELEAELAELEAELEELRLELEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 983 VADASDKTQQAETALgsaTADTQRAKNAAREALEISSEIEQEIGSLNLEANVTADgALAMEKGLATLKSEMREMEGELAR 1062
Cdd:COG1196 290 EYELLAELARLEQDI---ARLEERRRELEERLEELEEELAELEEELEELEEELEE-LEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1063 KELEFDTDKDTVQLVITEAQQADARATSAGVTIQDTLNTLDGILHLIDQpgsvDEEGMMLLEQGLFQAKTQINSRLRPLM 1142
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE----RLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270
....*....|....*....|....*....|....*...
gi 110624798 1143 SDLEERVRRQRNHLHLLETSIDGILADVKNLENIRDNL 1180
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
|
| TNFRSF4 |
cd13406 |
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; ... |
437-501 |
9.28e-06 |
|
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; TNFRSF4 (also known as OX40, ACT35, CD134, IMD16, TXGP1L) activates NF-kappaB through its interaction with adaptor proteins TRAF2 and TRAF5. It also promotes the expression of apoptosis inhibitors BCL2 and BCL2lL1/BCL2-XL, and thus suppresses apoptosis. It is primarily expressed on activated CD4+ and CD8+ T cells, where it is transiently expressed and upregulated on the most recently antigen-activated T cells within inflammatory lesions. This makes it an attractive target to modulate immune responses, i.e. TNFRSF4 (OX40) blocking agents to inhibit adverse inflammation or agonists to enhance immune responses. An artificially created biologic fusion protein, OX40-immunoglobulin (OX40-Ig), prevents OX40 from reaching the T-cell receptors, thus reducing the T-cell response. Some single nucleotide polymorphisms (SNPs) of its natural ligand OX40 ligand (OX40L, CD252), which is also found on activated T cells, have been associated with systemic lupus erythematosus.
Pssm-ID: 276911 [Multi-domain] Cd Length: 142 Bit Score: 46.62 E-value: 9.28e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110624798 437 NPDIECADCPIGFYNDPHDPRSCKPCPCHNGFSCSVMPE----TEEVVCnNCPPGVT-------GARCELCADGFF 501
Cdd:cd13406 31 TQDTVCSPCEPGFYNEAVNYEPCKPCTQCNQRSGSEEKQkctkTSDTVC-RCRPGTQpldsykpGVDCVPCPPGHF 105
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
760-1154 |
1.07e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 760 LAQEATRLADSHAESANAMKQLARETEDYSKQALSLARKALSGGGGSGVLDSsvvqglmgKLEKTKSlsQQLSREGTQAD 839
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELES--------ELEEARE--AVEDRREEIEE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 840 IEADRSyQHSLRLLDSASQLQGVSDLSFQVEAKR--IRQKADSLSnlVTRQTdaftrVRNNLgnweKETRQLLQTGK--- 914
Cdd:PRK02224 389 LEEEIE-ELRERFGDAPVDLGNAEDFLEELREERdeLREREAELE--ATLRT-----ARERV----EEAEALLEAGKcpe 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 915 ---------------DRRQTSDQLlsRANLAKNRAQ--------EALSMGNATFYEVENILKNLREFDLQVEDRKAEAEE 971
Cdd:PRK02224 457 cgqpvegsphvetieEDRERVEEL--EAELEDLEEEveeveerlERAEDLVEAEDRIERLEERREDLEELIAERRETIEE 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 972 AMKRLSSISQKVADASDKTQQAETAlgsATADTQRAKNAAREALEISS---EIEQEIGSLNLEANVTADGALAME----- 1043
Cdd:PRK02224 535 KRERAEELRERAAELEAEAEEKREA---AAEAEEEAEEAREEVAELNSklaELKERIESLERIRTLLAAIADAEDeierl 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1044 ----KGLATLKSEMREMEGELA--RKELEFDTDKDTVQlvitEAQQADARATSAGVTIQDTLNTL----DGILHLIdqpG 1113
Cdd:PRK02224 612 rekrEALAELNDERRERLAEKRerKRELEAEFDEARIE----EAREDKERAEEYLEQVEEKLDELreerDDLQAEI---G 684
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 110624798 1114 SVDEEGMMLLEqgLFQAKTQINSR---LRPLMSDLEE------RVR---RQRN 1154
Cdd:PRK02224 685 AVENELEELEE--LRERREALENRveaLEALYDEAEElesmygDLRaelRQRN 735
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
462-507 |
1.15e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 43.45 E-value: 1.15e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 110624798 462 CPCHNGFSCSVMPETEEVVCNnCPPGVTGARCELCADGFFGDPFGE 507
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
572-604 |
1.60e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 43.11 E-value: 1.60e-05
10 20 30
....*....|....*....|....*....|....
gi 110624798 572 ACNCSPMGSEPGEC-RGDGSCVCKPGFGGLNCDH 604
Cdd:cd00055 1 PCDCNGHGSLSGQCdPGTGQCECKPNTTGRRCDR 34
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
651-869 |
1.80e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 651 ELEGRMQQAEQALRDILREAQISEGAMRALGF--RLAKARSQENDYKTRLDDLKMTAERIRALGSQHQNRVQD--TSRLI 726
Cdd:COG3206 186 ELRKELEEAEAALEEFRQKNGLVDLSEEAKLLlqQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEllQSPVI 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 727 SQMRLSLAGSEAslqntnihssehyvgpngfkSLAQEATRLADSHAEsanaMKQLARETEDYSKQALSLARKALSGGGGS 806
Cdd:COG3206 266 QQLRAQLAELEA--------------------ELAELSARYTPNHPD----VIALRAQIAALRAQLQQEAQRILASLEAE 321
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110624798 807 GVLDSSVVQGLMGKLEKTKSLSQQLSREGTQA-----DIEADRS-YQHSLRLLDSASQLQGVSDLSFQV 869
Cdd:COG3206 322 LEALQAREASLQAQLAQLEARLAELPELEAELrrlerEVEVARElYESLLQRLEEARLAEALTVGNVRV 390
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
614-1175 |
3.33e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 614 YNQVKIQMDQFTQQLQSLEALVSKAQGGGGggtvpsgELEGRMQQAEQALRDILREAQISEGAMR-------ALGFRLAK 686
Cdd:TIGR02169 289 QLRVKEKIGELEAEIASLERSIAEKERELE-------DAEERLAKLEAEIDKLLAEIEELEREIEeerkrrdKLTEEYAE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 687 ARSQENDYKTRLDDLKMTAERIRALGSQHQNRVQDTSRLISQMRLSLAGSEASLQNTNIHSSEHYvgpNGFKSLAQEATR 766
Cdd:TIGR02169 362 LKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN---AAIAGIEAKINE 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 767 LADSHAESANAMKQLARETEDYSKQALSLARKALSGGGGSGVLDS--SVVQGLMGKLEKTKSLSQQLSRE---------- 834
Cdd:TIGR02169 439 LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKelSKLQRELAEAEAQARASEERVRGgraveevlka 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 835 ------GTQAD-IEADRSYQHSL------RL--------LDSASQLQGVSDL--------------SFQVEAKRIRQKA- 878
Cdd:TIGR02169 519 siqgvhGTVAQlGSVGERYATAIevaagnRLnnvvveddAVAKEAIELLKRRkagratflplnkmrDERRDLSILSEDGv 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 879 -DSLSNLVT---RQTDAF------TRVRNNLgnwEKETRQLLQ-----------------TGKDRRQTSDQLLSRANLAK 931
Cdd:TIGR02169 599 iGFAVDLVEfdpKYEPAFkyvfgdTLVVEDI---EAARRLMGKyrmvtlegelfeksgamTGGSRAPRGGILFSRSEPAE 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 932 nraqeaLSMGNATFYEveniLKNLREFdLQVEDRKAEaeeamKRLSSISQKVADASDKTQQAETALGSATADTQRAKNAA 1011
Cdd:TIGR02169 676 ------LQRLRERLEG----LKRELSS-LQSELRRIE-----NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL 739
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1012 REALEISSEIEQEIgsLNLEANVTA-DGALA-MEKGLATLKSEMREMEGELARKelEFDTDKDTVQLVITEAQQADARat 1089
Cdd:TIGR02169 740 EELEEDLSSLEQEI--ENVKSELKElEARIEeLEEDLHKLEEALNDLEARLSHS--RIPEIQAELSKLEEEVSRIEAR-- 813
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1090 sagvtiqdtLNTLDGILHLIDQPGSVDEEGMMLLEQGLFQAKTQINSR------LRPLMSDLEERVRRQRNHLHLLETSI 1163
Cdd:TIGR02169 814 ---------LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIekeienLNGKKEELEEELEELEAALRDLESRL 884
|
650
....*....|..
gi 110624798 1164 DGILADVKNLEN 1175
Cdd:TIGR02169 885 GDLKKERDELEA 896
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
952-1182 |
3.88e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 952 LKNLREF-------DLQVEDRKAEAEEAMKRLSSISQKVADAsdkTQQAETaLGSATADTQRAKNAAREAleisSEIEQE 1024
Cdd:COG4913 206 IGDLDDFvreymleEPDTFEAADALVEHFDDLERAHEALEDA---REQIEL-LEPIRELAERYAAARERL----AELEYL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1025 IGSLNLEANVTADGALAMEkgLATLKSEMREMEGELARKELEFDTDKDTVQLVITEAQQAD-----------ARATSAGV 1093
Cdd:COG4913 278 RAALRLWFAQRRLELLEAE--LEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgdrleqlereiERLERELE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1094 TIQDTLNTLDGILHLIDQPGSVDEEGMMLLEQGLFQAKTQINSRLRPLMSDLEERVRRQRNhlhlLETSIDGILADVKNL 1173
Cdd:COG4913 356 ERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD----LRRELRELEAEIASL 431
|
....*....
gi 110624798 1174 ENIRDNLPP 1182
Cdd:COG4913 432 ERRKSNIPA 440
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
614-991 |
5.04e-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: 47.66 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 614 YNQVKIQMDQFTQQLQSLEALVSKAQGGGGGGTVPSGELEG---RMQQAEQA--------------LRDILREAQISEGA 676
Cdd:TIGR00618 485 ETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPltrRMQRGEQTyaqletseedvyhqLTSERKQRASLKEQ 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 677 MRALGFRLAKARSQENDYKTRLDDLKMTAERIRALGsQHQNRVQDTSRLISQMRLSLAGSEASLQNTNIHSSehyvgpNG 756
Cdd:TIGR00618 565 MQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLT-EKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQ------QC 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 757 FKSLAQEATRLadsHAESANAMKQLARETEDYSK--QALSLARKALSGGGGsgvldSSVVQGLMGKLEkTKSLSQQLSRE 834
Cdd:TIGR00618 638 SQELALKLTAL---HALQLTLTQERVREHALSIRvlPKELLASRQLALQKM-----QSEKEQLTYWKE-MLAQCQTLLRE 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 835 GTQADIEADRSYQHSLRLLDSA-SQLQGVSDLSFQVEAKRIRQKADSLSNLVTRQTDAFTRVRNNL--GNWEKETRQLLQ 911
Cdd:TIGR00618 709 LETHIEEYDREFNEIENASSSLgSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALqtGAELSHLAAEIQ 788
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 912 TGKDRRQTSDQLLsrANLAKNRAQEALSMGNATFYEVENILKNLREFD-----------------LQVEDRKAEAEEAMK 974
Cdd:TIGR00618 789 FFNRLREEDTHLL--KTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLsrleeksatlgeithqlLKYEECSKQLAQLTQ 866
|
410
....*....|....*..
gi 110624798 975 RLSSISQKVADASDKTQ 991
Cdd:TIGR00618 867 EQAKIIQLSDKLNGINQ 883
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
870-1192 |
5.57e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.73 E-value: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 870 EAKRIRQKADSLSNLvTRQTDAFTRVRNNLGNWEKETR------QLLQTGKDRR-QTSDQLLSRANLA------------ 930
Cdd:TIGR00606 167 EGKALKQKFDEIFSA-TRYIKALETLRQVRQTQGQKVQehqmelKYLKQYKEKAcEIRDQITSKEAQLessreivksyen 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 931 -----KNRAQEALSMgNATFYEVENILKNLREFDLQVEDRKAEAEEAM-KRLSSISQKVADASDKTQQAETALGSATADT 1004
Cdd:TIGR00606 246 eldplKNRLKEIEHN-LSKIMKLDNEIKALKSRKKQMEKDNSELELKMeKVFQGTDEQLNDLYHNHQRTVREKERELVDC 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1005 QR--AKN--AAREALEISSEIEQEIGSLNLEANVTADGALAMEkglatlkSEMREMEGELARKELEFDTD-----KDTVQ 1075
Cdd:TIGR00606 325 QRelEKLnkERRLLNQEKTELLVEQGRLQLQADRHQEHIRARD-------SLIQSLATRLELDGFERGPFserqiKNFHT 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1076 LVItEAQQADARATSAGVT-IQDTLNT----LDGILHLIDQPGSVDEEGMMLLEQGLFQAKTQIN--SRLRPLMSDL--- 1145
Cdd:TIGR00606 398 LVI-ERQEDEAKTAAQLCAdLQSKERLkqeqADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKelQQLEGSSDRIlel 476
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 110624798 1146 EERVRRQRNHLHLLE--TSIDGILADVKNLENIR-DNLPPGCYNTQALEQ 1192
Cdd:TIGR00606 477 DQELRKAERELSKAEknSLTETLKKEVKSLQNEKaDLDRKLRKLDQEMEQ 526
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
993-1180 |
6.78e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 6.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 993 AETALGSATADTQRAKNAAR--EALEISSEIEQEIGSLNLEANVTADGALAMEKGLATLKSEMREMEGELARKELEFDTD 1070
Cdd:COG3883 5 ALAAPTPAFADPQIQAKQKElsELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1071 KDTVQLVITEAQQADARATSAGV-----TIQDTLNTLDGILHLIDQpgsvDEEgmmLLEQgLFQAKTQIN---SRLRPLM 1142
Cdd:COG3883 85 REELGERARALYRSGGSVSYLDVllgseSFSDFLDRLSALSKIADA----DAD---LLEE-LKADKAELEakkAELEAKL 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 110624798 1143 SDLEERVRRQRNHLHLLETSIDGILADVKNLENIRDNL 1180
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAA 194
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
946-1168 |
8.43e-05 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 45.48 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 946 YEVENILKNLREFDLQVEDRKAEAEEAMKRLSSISQ-------KVADASDKTQQ----AETALGSATADTQRAKNAAREA 1014
Cdd:pfam06008 19 YNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQeteelqkKATQTLAKAQQvnaeSERTLGHAKELAEAIKNLIDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1015 LEISSEIEQeigsLNLEANVTADGALamEKGLATLKSEMREMegelarKELEFDTDKDTVQLVITEAQQADARATSAGVT 1094
Cdd:pfam06008 99 KEINEKVAT----LGENDFALPSSDL--SRMLAEAQRMLGEI------RSRDFGTQLQNAEAELKAAQDLLSRIQTWFQS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1095 IQDTLNTL-DGILHLIDQpgsvDEEGMMLLEQGLFQA--KTQ----INSRLRPLMSDLE---ERVRRQRNHLHLLETSID 1164
Cdd:pfam06008 167 PQEENKALaNALRDSLAE----YEAKLSDLRELLREAaaKTRdanrLNLANQANLREFQrkkEEVSEQKNQLEETLKTAR 242
|
....
gi 110624798 1165 GILA 1168
Cdd:pfam06008 243 DSLD 246
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
914-1032 |
1.23e-04 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 43.20 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 914 KDRRQTSDQLLSRANLAKNRAQEALSmgnatfyEVENILKNLREfdlQVEDRKAEAEEAMKRLssISQKVADAsdkTQQA 993
Cdd:cd06503 29 DEREEKIAESLEEAEKAKEEAEELLA-------EYEEKLAEARA---EAQEIIEEARKEAEKI--KEEILAEA---KEEA 93
|
90 100 110
....*....|....*....|....*....|....*....
gi 110624798 994 ETALGSATADTQRAKNAAREaleissEIEQEIGSLNLEA 1032
Cdd:cd06503 94 ERILEQAKAEIEQEKEKALA------ELRKEVADLAVEA 126
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
658-1059 |
1.53e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 46.36 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 658 QAEQalrdILREAQISEGAMRALGFR-LAKARSQendyktrlddlkmtAERIRALGSQHQNRVQ---DTSRLISQMRLSL 733
Cdd:NF041483 73 QAEQ----LLRNAQIQADQLRADAEReLRDARAQ--------------TQRILQEHAEHQARLQaelHTEAVQRRQQLDQ 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 734 AGSEASlQNTNIHSSEHYVGPNGFKS-LAQEATRLAD-SHAESANAMKQLARETEDYSKQALslarkalsggggsgvlds 811
Cdd:NF041483 135 ELAERR-QTVESHVNENVAWAEQLRArTESQARRLLDeSRAEAEQALAAARAEAERLAEEAR------------------ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 812 svvQGLMGKLEKTKSLSQQLSREGtQADIEadrsyqhslRLLDSAS-QLQGVSDLSFQV------EAKRIRQKADSLSNL 884
Cdd:NF041483 196 ---QRLGSEAESARAEAEAILRRA-RKDAE---------RLLNAAStQAQEATDHAEQLrsstaaESDQARRQAAELSRA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 885 V-TRQTDAFTRVRNNLGNWEKETRQLLQTGKDRRQTSD-QLLSRANLAKNR----AQEALSMGNATFYEVENILKNLREf 958
Cdd:NF041483 263 AeQRMQEAEEALREARAEAEKVVAEAKEAAAKQLASAEsANEQRTRTAKEEiarlVGEATKEAEALKAEAEQALADARA- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 959 dlQVEDRKAEAEEAmKRLSSISQKVADASDKTQQAETALGSATADTQRA-KNAAREALEISSEIEQEIGSLNLEANVTAD 1037
Cdd:NF041483 342 --EAEKLVAEAAEK-ARTVAAEDTAAQLAKAARTAEEVLTKASEDAKATtRAAAEEAERIRREAEAEADRLRGEAADQAE 418
|
410 420 430
....*....|....*....|....*....|....
gi 110624798 1038 GAlameKGLAT------------LKSEMREMEGE 1059
Cdd:NF041483 419 QL----KGAAKddtkeyraktveLQEEARRLRGE 448
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
850-1164 |
1.71e-04 |
|
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: 46.20 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 850 LRLLDSASQ-LQGVSDLSFQVEA--KRIRQKAdslsnlvtRQTDAFTRVRNNLGNWEKE--TRQLLQTGKDRRQTSDQLl 924
Cdd:TIGR02168 178 ERKLERTREnLDRLEDILNELERqlKSLERQA--------EKAERYKELKAELRELELAllVLRLEELREELEELQEEL- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 925 SRANLAKNRAQEALSMgnatfYEVEnilknLREFDLQVEDRKAEAEEAMKRLSSISQKVAD-------ASDKTQQAETAL 997
Cdd:TIGR02168 249 KEAEEELEELTAELQE-----LEEK-----LEELRLEVSELEEEIEELQKELYALANEISRleqqkqiLRERLANLERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 998 GSATADTQRAKNAAREALEISSEIEQEIGSLNLEANvtadgalAMEKGLATLKSEMREMEG--ELARKELEfdtdkdtvq 1075
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELE-------SLEAELEELEAELEELESrlEELEEQLE--------- 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1076 lviteaQQADARAtsagvtiqdtlntldgilhlidqpgsvdeegmmLLEQGLFQAKTQInSRLRPLMSDLEERVRRQRNH 1155
Cdd:TIGR02168 383 ------TLRSKVA---------------------------------QLELQIASLNNEI-ERLEARLERLEDRRERLQQE 422
|
....*....
gi 110624798 1156 LHLLETSID 1164
Cdd:TIGR02168 423 IEELLKKLE 431
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
28-86 |
1.75e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 40.41 E-value: 1.75e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110624798 28 CDCNG---KSRQCvfdqelHRQTGsgfRCLnCNDNTAGVHCERCREGFYRHRdrdRCLPCNC 86
Cdd:pfam00053 1 CDCNPhgsLSDTC------DPETG---QCL-CKPGVTGRHCDRCKPGYYGLP---SDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
573-604 |
2.12e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.99 E-value: 2.12e-04
10 20 30
....*....|....*....|....*....|...
gi 110624798 573 CNCSPMGSEPGEC-RGDGSCVCKPGFGGLNCDH 604
Cdd:smart00180 1 CDCDPGGSASGTCdPDTGQCECKPNVTGRRCDR 33
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
573-604 |
2.52e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 39.64 E-value: 2.52e-04
10 20 30
....*....|....*....|....*....|...
gi 110624798 573 CNCSPMGSEPGEC-RGDGSCVCKPGFGGLNCDH 604
Cdd:pfam00053 1 CDCNPHGSLSDTCdPETGQCLCKPGVTGRHCDR 33
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
652-1029 |
2.89e-04 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 45.01 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 652 LEGRMQQAEQALRDILREAQISEGAMRALGFRLAKARSQENDYKTRLDDLKMTAERIRALGSQHQNRVQDTSRLISQMRL 731
Cdd:COG0840 12 LALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALLLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 732 SLAGSEASLQNTNIHSSEHYVGPNGFKSLAQEATRLADSHAESANAMKQLARETEDYSKQALSLARKALSGGGGSGVLDS 811
Cdd:COG0840 92 LLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 812 SVVQGLMGKLEKTKSLSQQLSREGTQADIEADRSYQHSLR-LLDSASQL-QGvsDLSFQVEAKR---IRQKADSLSNLVT 886
Cdd:COG0840 172 LALAAAALALALLAAALLALVALAIILALLLSRSITRPLReLLEVLERIaEG--DLTVRIDVDSkdeIGQLADAFNRMIE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 887 RQTDAFTRVRNNlgnwekeTRQLlqtgkdrRQTSDQLLSRANLAKNRAQEALSmgnatfyEVEnilknlrefdlqvedrk 966
Cdd:COG0840 250 NLRELVGQVRES-------AEQV-------ASASEELAASAEELAAGAEEQAA-------SLE----------------- 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110624798 967 aEAEEAMKRLSSISQKVADasdKTQQAETALGSATADTQRAKNAAREALEISSEIEQEIGSLN 1029
Cdd:COG0840 292 -ETAAAMEELSATVQEVAE---NAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETA 350
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
867-1096 |
5.63e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 867 FQVEAKRIRQKADSLSNLVTrqtdAFtRVRNNLGNWEKETRQLLQTGKD---RRQTSDQLLSRANLAKNRAQEALSMGNA 943
Cdd:COG3206 180 LEEQLPELRKELEEAEAALE----EF-RQKNGLVDLSEEAKLLLQQLSElesQLAEARAELAEAEARLAALRAQLGSGPD 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 944 TFYEVENilknlrefDLQVEDRKAEAEEAMKRLSSISQKVADASDKTQQAETALgsATADTQRAKNAAREALEISSEIEQ 1023
Cdd:COG3206 255 ALPELLQ--------SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQI--AALRAQLQQEAQRILASLEAELEA 324
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110624798 1024 eigslnLEANVTAdgalaMEKGLATLKSEMREM---EGELARKELEFDTDKDTVQLVITEAQQADARATSAGVTIQ 1096
Cdd:COG3206 325 ------LQAREAS-----LQAQLAQLEARLAELpelEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
824-985 |
5.93e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 44.27 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 824 TKSLSQQLSREG----------TQADIEaDRSYQHSLRLLDSASQLQGvsdlsfqvEAKRIRQKADSLSNLVTRQTDA-- 891
Cdd:PRK10929 81 SAELRQQLNNERdeprsvppnmSTDALE-QEILQVSSQLLEKSRQAQQ--------EQDRAREISDSLSQLPQQQTEArr 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 892 -FTRVRNNLG-----NWEKETRQL--LQTGKDRRQTSDQLLSRANLAKNRAQEALSMgnatfyEVENILKNLREFDLQVE 963
Cdd:PRK10929 152 qLNEIERRLQtlgtpNTPLAQAQLtaLQAESAALKALVDELELAQLSANNRQELARL------RSELAKKRSQQLDAYLQ 225
|
170 180 190
....*....|....*....|....*....|
gi 110624798 964 D--------RKAEAEEAMKRLSSISQKVAD 985
Cdd:PRK10929 226 AlrnqlnsqRQREAERALESTELLAEQSGD 255
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
903-1160 |
6.64e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 903 EKETRQLLQTGKDRRQTSDQLLSRANLAKNRAQEALSMGNATFYEVENILKNLREFDLQVEDRKAEAEEAMKRLSSISQK 982
Cdd:PRK02224 201 EKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 983 VADASDKTQQ---------AETALGSATADT---QRAKNAAREAlEISSEIEQE---IGSLNLEANVTADGALAMEKGLA 1047
Cdd:PRK02224 281 VRDLRERLEEleeerddllAEAGLDDADAEAveaRREELEDRDE-ELRDRLEECrvaAQAHNEEAESLREDADDLEERAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1048 TLKSEMREMEGELARKELEFDTDKDTVQLVITEAQQADARATSAGVtiqdtlntldgilhlidQPGSVDEEGMMLLEqgl 1127
Cdd:PRK02224 360 ELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV-----------------DLGNAEDFLEELRE--- 419
|
250 260 270
....*....|....*....|....*....|...
gi 110624798 1128 fqAKTQINSRLRPLMSDLEERVRRQRNHLHLLE 1160
Cdd:PRK02224 420 --ERDELREREAELEATLRTARERVEEAEALLE 450
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
826-1064 |
8.38e-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: 43.21 E-value: 8.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 826 SLSQQLSREGTQADIEA-DRSYQHSLRLLDSASQLQGvsdlSFQVEAKRIRQKADSLSNLVTRQTDAFTRVRNNLGNWEK 904
Cdd:COG4942 15 AAAQADAAAEAEAELEQlQQEIAELEKELAALKKEEK----ALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 905 ETRQLLQTGKDRRQTSDQLLSRANLAKNRAQEALSMGNATFYEVENILKNLREFDLQVEDRKAEAEEAMKRLSSISQKVA 984
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 985 DASDKTQQAETALGSATADTQRAKNAAREALeisSEIEQEIGSLNLEANvtadgalAMEKGLATLKSEMREMEGELARKE 1064
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLL---ARLEKELAELAAELA-------ELQQEAEELEALIARLEAEAAAAA 240
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
921-1062 |
8.91e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.12 E-value: 8.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 921 DQLLSRANLAKNRAQEALSMGNatfyevENI----LKNLREFDLQVEDRKAEAEEAMKRLSSISQKVADASDKTQQAETA 996
Cdd:COG1842 61 EELEAEAEKWEEKARLALEKGR------EDLareaLERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 997 LGS--ATADTQRAKNAAREALE-ISSE--------IEQEIgsLNLEANVTADGALAMEKGLAtlkSEMREMEG------E 1059
Cdd:COG1842 135 KDTlkARAKAAKAQEKVNEALSgIDSDdatsalerMEEKI--EEMEARAEAAAELAAGDSLD---DELAELEAdsevedE 209
|
...
gi 110624798 1060 LAR 1062
Cdd:COG1842 210 LAA 212
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
822-1099 |
1.38e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 822 EKTKSLSQQLSREGTQADIEADRS--YQHSLRLLDSASQLQGVSDLsfqveakrirqkadSLSNLVTRQtDAFTrvrnnl 899
Cdd:PRK04863 390 EEVDELKSQLADYQQALDVQQTRAiqYQQAVQALERAKQLCGLPDL--------------TADNAEDWL-EEFQ------ 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 900 gNWEKE-TRQLLQTGkdrrqtsdQLLSRANLAKNRAQEALSMGNATFYEVE--NILKNLREFDLQVEDRKAEAEeamkRL 976
Cdd:PRK04863 449 -AKEQEaTEELLSLE--------QKLSVAQAAHSQFEQAYQLVRKIAGEVSrsEAWDVARELLRRLREQRHLAE----QL 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 977 SSISQKVADA---SDKTQQAETALGSATADTQRAKNAAREALEISSEIEQEIGSLNLEANVTADGALAMEKGLATLKSEM 1053
Cdd:PRK04863 516 QQLRMRLSELeqrLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARI 595
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 110624798 1054 RemegELARKELEFDTDKDTV-QLvitEAQQADARATSAGVT--IQDTL 1099
Cdd:PRK04863 596 Q----RLAARAPAWLAAQDALaRL---REQSGEEFEDSQDVTeyMQQLL 637
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
680-937 |
1.52e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 680 LGFRLAKARSQENDYKTRLDDLKMTAERIRALGSQHQNRVQDTSRLISQMRLSLAGSEASLQNTNihssehyvgpngfKS 759
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALE-------------QE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 760 LAQEATRLADSHAESANAMKQLARETEDYSKQALSLARKALSGGGGSGVLDSSVVQGLMgklektkslSQQLSREGTQAD 839
Cdd:COG4942 78 LAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVR---------RLQYLKYLAPAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 840 IEADRSYQHSLRLLDSASQLQGVSDLSFQVEAKRIRQKADSLSNLVTRQTDAFTRVRNNLGNWEKETRQLLQTGKDRRQT 919
Cdd:COG4942 149 REQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
250
....*....|....*...
gi 110624798 920 SDQLLSRANLAKNRAQEA 937
Cdd:COG4942 229 IARLEAEAAAAAERTPAA 246
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
28-74 |
1.57e-03 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 37.72 E-value: 1.57e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 110624798 28 CDCNG---KSRQCvfdqelHRQTGsgfRCLnCNDNTAGVHCERCREGFYR 74
Cdd:cd00055 2 CDCNGhgsLSGQC------DPGTG---QCE-CKPNTTGRRCDRCAPGYYG 41
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
946-1103 |
1.90e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.96 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 946 YEVENILKNLREFDLQVEDRKAEAEEAMKRLSSISQKVADasdKTQQAETALgsatadtQRAK-NAAREALEISSEIEQE 1024
Cdd:COG1842 30 QAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEK---WEEKARLAL-------EKGReDLAREALERKAELEAQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1025 IGSLNLEANVTADGALAMEKGLATLKSEMREMEgelARKElefdtdkdtvqLVITEAQQADARA----TSAGVTIQDTLN 1100
Cdd:COG1842 100 AEALEAQLAQLEEQVEKLKEALRQLESKLEELK---AKKD-----------TLKARAKAAKAQEkvneALSGIDSDDATS 165
|
...
gi 110624798 1101 TLD 1103
Cdd:COG1842 166 ALE 168
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
615-1180 |
2.39e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.34 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 615 NQVKIQMDQFTQQLQSLEALVSKAQGGGGGGTVPSGELEG---RMQQAEQALRDILRE-------AQISEGAMRALGFR- 683
Cdd:TIGR00606 429 DEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGssdRILELDQELRKAERElskaeknSLTETLKKEVKSLQn 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 684 -----------LAKARSQENDYKTRLDDLKMTA-------ERIRALGSQHQNRV-------------QDT----SRLISQ 728
Cdd:TIGR00606 509 ekadldrklrkLDQEMEQLNHHTTTRTQMEMLTkdkmdkdEQIRKIKSRHSDELtsllgyfpnkkqlEDWlhskSKEINQ 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 729 MRLSLAGSEASLQN--TNIHsseHYvgPNGFKSLAQEATRLAD-------SHAESANaMKQLARETEDYSKQALSLARKA 799
Cdd:TIGR00606 589 TRDRLAKLNKELASleQNKN---HI--NNELESKEEQLSSYEDklfdvcgSQDEESD-LERLKEEIEKSSKQRAMLAGAT 662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 800 lsggggsGVLDSSVvqglmgklektkslsQQLSREGTQADIEADRSYQHSLRLLDSASQLQGVSDL------SFQVEAKR 873
Cdd:TIGR00606 663 -------AVYSQFI---------------TQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLapdklkSTESELKK 720
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 874 IRQKADSLSNLVTRQTDAFTRVrnnlgnwEKETRQLLQtgKDRRQTSDQLLSRANLAKNRAQeaLSMGNATFYEVENILK 953
Cdd:TIGR00606 721 KEKRRDEMLGLAPGRQSIIDLK-------EKEIPELRN--KLQKVNRDIQRLKNDIEEQETL--LGTIMPEEESAKVCLT 789
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 954 N---LREFDLQVEDRKAEAEEAMKRLSSI--SQKVADASDKTQQAETALGSATADTQRAKNAAREALEISSEIE---QEI 1025
Cdd:TIGR00606 790 DvtiMERFQMELKDVERKIAQQAAKLQGSdlDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKsktNEL 869
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1026 GSLNLEANVTADGALAMEKGLATLKSEMREMEGELARKELEFDTDKDTVQLVITEAQQADARATSAGVTIQDTLNTL--- 1102
Cdd:TIGR00606 870 KSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIkek 949
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 1103 --DGILHLIDQPGSVdEEGMmllEQGLFQAKTQINSrLRPLMSDLEERVRRQRNHLHLLETSIDG------ILADVKNLE 1174
Cdd:TIGR00606 950 vkNIHGYMKDIENKI-QDGK---DDYLKQKETELNT-VNAQLEECEKHQEKINEDMRLMRQDIDTqkiqerWLQDNLTLR 1024
|
....*.
gi 110624798 1175 NIRDNL 1180
Cdd:TIGR00606 1025 KRENEL 1030
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
484-506 |
3.20e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 36.56 E-value: 3.20e-03
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
967-1067 |
3.53e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 967 AEAEEAMKRLSSISQKVADASDKTQQaetalgsatadTQRAKNAAREALEissEIEQEIGSLNLEANVTADGALAMEKGL 1046
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAA-----------LKKEEKALLKQLA---ALERRIAALARRIRALEQELAALEAEL 85
|
90 100
....*....|....*....|.
gi 110624798 1047 ATLKSEMREMEGELARKELEF 1067
Cdd:COG4942 86 AELEKEIAELRAELEAQKEEL 106
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
914-1028 |
5.16e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 39.00 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 914 KDRRQTSDQLLSRANLAKNRAQEALSmgnatfyEVENILKNLREfdlQVEDRKAEAEEAMKRLssISQKVADAsdkTQQA 993
Cdd:COG0711 30 DERQEKIADGLAEAERAKEEAEAALA-------EYEEKLAEARA---EAAEIIAEARKEAEAI--AEEAKAEA---EAEA 94
|
90 100 110
....*....|....*....|....*....|....*
gi 110624798 994 ETALGSATADTQRAKNAAREaleissEIEQEIGSL 1028
Cdd:COG0711 95 ERIIAQAEAEIEQERAKALA------ELRAEVADL 123
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
947-1070 |
5.87e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.68 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 947 EVENILKNLREFDL-QVEDRKAEAE-EAMKRLSSISQKVADASDKTQQAETALGSA-----TADTQRAKNAAREALEISS 1019
Cdd:PRK05771 17 YKDEVLEALHELGVvHIEDLKEELSnERLRKLRSLLTKLSEALDKLRSYLPKLNPLreekkKVSVKSLEELIKDVEEELE 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 110624798 1020 EIEQEIGSLnleanvtadgalamEKGLATLKSEMREMEGELarKELE----FDTD 1070
Cdd:PRK05771 97 KIEKEIKEL--------------EEEISELENEIKELEQEI--ERLEpwgnFDLD 135
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
870-1067 |
7.83e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 870 EAKRIRQKADSLSNLVTRQTDAFTRVRNNlgNWEKetrqllqtgKDRRQTSDQLLsranlAKNRAQEALSMGNATfyeve 949
Cdd:COG4913 628 EAEERLEALEAELDALQERREALQRLAEY--SWDE---------IDVASAEREIA-----ELEAELERLDASSDD----- 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110624798 950 niLKNLREfdlQVEDRKAEAEEAMKRLSSISQKVADASDKTQQAETALGSATADTQRAKNAAREALEisSEIEQEIGSLN 1029
Cdd:COG4913 687 --LAALEE---QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR--ALLEERFAAAL 759
|
170 180 190
....*....|....*....|....*....|....*...
gi 110624798 1030 LEAnVTADGALAMEKGLATLKSEMREMEGELARKELEF 1067
Cdd:COG4913 760 GDA-VERELRENLEERIDALRARLNRAEEELERAMRAF 796
|
|
| |
