|
Name |
Accession |
Description |
Interval |
E-value |
| tape_meas_TP901 |
TIGR01760 |
phage tail tape measure protein, TP901 family, core region; This model represents a reasonably ... |
322-669 |
9.86e-111 |
|
phage tail tape measure protein, TP901 family, core region; This model represents a reasonably well conserved core region of a family of phage tail proteins. The member from phage TP901-1 was characterized as a tail length tape measure protein in that a shortened form of the protein leads to phage with proportionately shorter tails. [Mobile and extrachromosomal element functions, Prophage functions]
Pssm-ID: 273790 [Multi-domain] Cd Length: 350 Bit Score: 357.05 E-value: 9.86e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 322 STPITLGLGAALKTSADFEGQMSRVGAIAQAS-SKDLKSMSNQAVDLGAKTSKSANEVAKGMEELAALGFNAKQTMEAMP 400
Cdd:TIGR01760 1 SAALGGGLVAAVKAAIEFEDAMSGVRAVVDGSrTKEFEDLSNQARDLGDETPFSAAQIAGAMTALARAGISAKDLLGATP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 401 GVISAAEASGAEMATTATVMASAINSFGLKASDANHVADLLARSANDSAADIQYMGDALKYAGTPAKALGVSIEDTSAAI 480
Cdd:TIGR01760 81 TALKLAAASDLTAEEAASILAKIMNAFGLTAKDSEKVADVLNYTANNSAATTRDMGDALQYAGPVAKSLGVSLEETAAAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 481 EVLSNSGLEGSQAGTALRASFIRLANPSKNTAKEMKKLGIHLSDAKGQFVGMGELIRQFQDNMKGMTREQKLATVATIVG 560
Cdd:TIGR01760 161 AALASAGIEGEIAGTALKAMLSRLAAPTGKAAKALKKLGIQTRDAKGNMKGLLDVLKELQKLTKGMGTEQQAAKLKTIFG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 561 TEAASGFLALIEAGPD-KINSYSKSLKNSNGESKKAADLMKDNLKGALEQLGGAFESLAIEVGKDLTPMIRAGAEGLTKL 639
Cdd:TIGR01760 241 VEASSALATLLTAGSKlSLAKNAKSLANSNGSAKKEADKMLDTLKGQLKLLQNAVENAFIELGEALLPALRELAQALTKL 320
|
330 340 350
....*....|....*....|....*....|
gi 215401158 640 VDGFTHLPGWVRKASVGLALFGAAIGPAVL 669
Cdd:TIGR01760 321 INAINGLAKGNPQLAVTLAAVAAAILALTA 350
|
|
| YqbO |
COG5280 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
301-1121 |
9.76e-94 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444091 [Multi-domain] Cd Length: 962 Bit Score: 328.04 E-value: 9.76e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 301 KKFSSIGDKMTSLGRTMTMGVSTPITLGLGAALKTSADFEGQMSRVGAIAQASSKDLKSMSNQAVDLGAKTSKSANEVAK 380
Cdd:COG5280 35 EKMDRAGKKMKSIGAALTAGVTAALVAAGAAAVKAAADFEKAMSTVQAVTGATGEELEALEQLAKELGATTGESAAEVAE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 381 GMEELAALGFNAKQTMEAMPGVISAAEASGAEMATTATVMASAINSFGLKASDANHVADLLARSANDSAADIQYMGDALK 460
Cdd:COG5280 115 ALGSVAQAGLSGDELIAVTEGALVLAAATGVDLNEAAEIVASAMNAFGLSADEASRVADLLAAGAQAGNTTSDELADALK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 461 YAGTPAKALGVSIEDTSAAIEVLSNSGLEGSQAGTALRASFIRLANPSKNTAKEMKKLGIHLSDAKGQFVGMGELIRQFQ 540
Cdd:COG5280 195 EYAPLAAALGFSLEETLAALALLANAGIKGSDAGTALKEFLIRLADPSKTAAEALEELGINVFDASGKLKGLSEILGELA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 541 DNMKGMTREQKLATVATIVGTEAASGFLALIEAGPDKINSYSKSLKNSNGESKKAADLMKDNLKGALEQLGGAFESLAIE 620
Cdd:COG5280 275 KKFAGLGEAARAAVLAAIFGDDAGRAAIALLLFGTDWYAKLTAALKNSAGAADEAAATMQDNLAGALESLKSALEGLAIT 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 621 VGKDLTPMIRAGAEGLTKLVDGFTHLPGWVRKASVGLALFGAAIGPAVLAGGLLIRTVGSAAKGYASLnrriaentilsn 700
Cdd:COG5280 355 IGETLLPALRDAVEALTGLADWFNELSPAVQELIIAIAGLVAALGPLLLILGALITGIGALAGAFGIL------------ 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 701 tnSKAMKSLGLQTLFlgSTTGKTSKGFKGLAGAMMFNLKPINVLKNSAKLAILPFKLLKNGLGLAAKSLFAVSGGARFAG 780
Cdd:COG5280 423 --STALAKAKGALLA--GPIGIVIAAIAALAAALVLLYKNWDTIKEFLTGLWNSIKEAIGGVWDGIKTSVEGLKGAAGAA 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 781 valrfLTGPIGATITAITIAYKVFKTAYDRVEWFRNGINGLGETIKFFGGKIIGGAVRKLGEfknylgSIGKSFKEKFSK 860
Cdd:COG5280 499 -----LSAAAGKAIEALAGISVDALKQGVILSGTISMLWGAAGTEVSLKGGAAQDNVSDAAS------SAGDGALAIINS 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 861 DMKDGYKSLSDDDLLKVGVNKFKGFMQTMGTASKKASDTVKVLGKGVSKETEKALEKYVHYSEENSRIMEKVRlNSGQIS 940
Cdd:COG5280 568 AEQAIIGLAAALKTASTSSALQASTKAAAATKAEKTILAIAMATVKGVTSATAALANAAGVILQGAIKNGISG-ALDSAG 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 941 EDKAKKLLKIETDLSNNLIAEIEKRNKKELEKTQELIDKYSAFDEQEKQNILTRTKEKNDLRIKKEQELNQ-KIKELKEK 1019
Cdd:COG5280 647 ATTVAKLAEEEAINEKIVELLKAAANGANKEAVANALLLDAAAKQNINGQEAILEGITAKGVQTDELQDSDaIQAKFQFE 726
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1020 ALSDGQISENERKEIEKLENQRRDITVKELSKTEKEQERILV-RMQRNRNAYsIDEASKAIKEAEKARKARKKEVDKQYE 1098
Cdd:COG5280 727 ELSEGAKATINAINGNGVLGGIIADGIKTNSAELKAAANELKgDINRVAAAI-NSLAEAGAEEIKSEAKEAGSDKAITGE 805
|
810 820
....*....|....*....|...
gi 215401158 1099 DDVIAIKNNVNLSKSEKDKLLAI 1121
Cdd:COG5280 806 AGQAALELAVARVNALISRVTKN 828
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
201-889 |
1.11e-75 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 269.03 E-value: 1.11e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 201 LKVQNDNLSKSNDKIESSYAKTNTKLKQTEKEFNDLNNTIKNHSANVAKAETAVNKEKAALNNLERSIDKASSEMKTFNK 280
Cdd:COG5283 5 LGAVDKPFKSALESAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALDQAGIDTRQLSA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 281 EQMIAQSHFGKLASQADVMSKKFSSIGDKMTSLGRT--------MTMGVSTPITLGLGAALKTSADFEGQMSRVGAIAQA 352
Cdd:COG5283 85 AQRRLRSSLEQTNRQLERQQQRLARLGARQDRLKAArarlqrlaGAGAAAAAIGAALAASVKPAIDFEDAMADVAATVDL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 353 --SSKDLKSMSNQAVDLGAKTSKSANEVAKGMEELAALGFNAKQTMEAMPGVISAAEASGAEMATTATVMASAINSFGLK 430
Cdd:COG5283 165 dkSSEQFKALGKQARELSAQTPQSADDIAAGQAALAQAGVSAEDILAFTPTAAKLATAFDTDAEEAAEIAAKILNAFKLP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 431 ASDANHVADLLARSANDSAADIQYMGDALKYAGTPAKALGVSIEDTSAAIEVLSNSGLEGSQAGTALRASFIRLANPSKN 510
Cdd:COG5283 245 ADDVERLGDALNYAGNNGATSLADLADALPYVGPVAKALGVSGKEAAALGAALADAGIEGEEAGTALRNMLTRLTSPTKA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 511 TAKEMKKLGIHLSDAKGQFVGM------------GELIRQFQDNMKGMTREQKLATVATIVGTEAASGFLALIEAGPD-K 577
Cdd:COG5283 325 AAKALKKLGIDTQDSKGNLRGLakilakqmqkdaQGALAELLKALKKLDAAKRAAALKQLFGEEAVSALAPLLQNGDElR 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 578 INSYSKSLKNSNGESKKAADLMKDNLKGALEQLGGAFESLAIEVGKDLTPMIRAGAEGLTKLVDGFTHLPGWVRKASVGL 657
Cdd:COG5283 405 KQLAVAEAAAAQGSMDKEAAKRTDTLAGQLKLLKNALENLGISIGEALLPALRELAQALTPVVGKLADWAKANPGLIKTI 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 658 ALFGAAIGPAVLAGGLLIRTVGSAAKGYASLNRRIAentilsntnskamkslglqtLFLGSTTGKTSKGFKGLAgammfn 737
Cdd:COG5283 485 VKVAAALAGLKAALGALRLALALLLSPLAALKAAAA--------------------LLGGGGLGGAGRGAGALA------ 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 738 lkpinvlknsaklailpfkllknGLGlAAKSLFAVSGGARFAGVALrfLTGPIGATITAITI-AYKVFKTaydrveWfrn 816
Cdd:COG5283 539 -----------------------ALG-GAKGLKLAGGAVLWLGRAL--LANPIGLVIAAIAAaAYLIYKY------W--- 583
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 215401158 817 ginglgETIKFFGGKIIGGavrklgeFKNYLGSIGKSFKEKFSKDMKDGYKSLSDDDLLKVGVNKFKGFMQTM 889
Cdd:COG5283 584 ------EPIKAFFKGVWEG-------IKAAFSPAWEAIKALISNWLGPVWDGLAIAGAGAGEAAAAAAVAGAQ 643
|
|
| PhageMin_Tail |
pfam10145 |
Phage-related minor tail protein; Members of this family are found in putative phage tail tape ... |
361-560 |
4.51e-52 |
|
Phage-related minor tail protein; Members of this family are found in putative phage tail tape measure proteins.
Pssm-ID: 462962 [Multi-domain] Cd Length: 201 Bit Score: 182.50 E-value: 4.51e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 361 SNQAVDLGAKTSKSANEVAKGMEELAALGFNAKQTMEAMPGVISAAEASGA-EMATTATVMASAINSFGLKASDANHVAD 439
Cdd:pfam10145 1 RDAALELGETTGFSATDAAEAMAALASAGLSAEELLSATEGALKLAVAGGAtDAAEAAEALAAAMNAFGLSADDAEEAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 440 LLARSANDSAADIQYMGDALKYAGTPAKALGVSIEDTSAAIEVLSNSGLEGSQAGTALRASFIRLANPSKNTAKEMKKLG 519
Cdd:pfam10145 81 VLAAAANNGATEVGDLADALKEVGPVAKAAGLSGEETAAALALLAAAGISGSEAGTALKNFLTRLAAPTKEAAKALKKLG 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 215401158 520 IHLSDAKGQFVGMGELIRQFQDNMKGMTREQKLATVATIVG 560
Cdd:pfam10145 161 ISAKDANGKMKSLSEILEELAQALKGLTDAQRAAALSALFG 201
|
|
| LT_TF-like |
cd13402 |
lytic transglycosylase-like domain of tail fiber-like proteins and similar domains; These tail ... |
1851-1972 |
9.39e-44 |
|
lytic transglycosylase-like domain of tail fiber-like proteins and similar domains; These tail fiber-like proteins are multi-domain proteins that include a lytic transglycosylase (LT) domain. Members of the LT family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, and the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL). LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.
Pssm-ID: 381605 [Multi-domain] Cd Length: 117 Bit Score: 155.05 E-value: 9.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1851 VGNIISLIQHESGGNAGITQssaLRDINVLQGNPAKGLLQYIPQTFRHYAVRGHNNIYSGYDQLLAFFNNRYWRSQFnPR 1930
Cdd:cd13402 1 LNALLRQIQTESGGNPNAIN---NWDSNAKAGHPSKGLMQVIPPTFAAYAPPGHGNILNPLDNILAAINYAKARYGS-GF 76
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 215401158 1931 GGWSPSGPRRYANGGLITKHqLAEVGEGDKQEMVIPLTRRKR 1972
Cdd:cd13402 77 ALAAGGGGGGYANGGIVTKG-LAEVGEGNKPEEVIPLDPAKR 117
|
|
| NlpD |
COG0739 |
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ... |
1691-1812 |
1.23e-30 |
|
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440502 [Multi-domain] Cd Length: 196 Bit Score: 120.85 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1691 QRFGRYTGGLNFNGGRHYGIDFGMPSGTNVYAVKGGIADKVWTDYGGGNSIQIKTGANEWNWYMHLSKQLARQGQRIKAG 1770
Cdd:COG0739 81 SGFGYRRHPVTGRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVIIDHGNGYTTLYAHLSSILVKVGQRVKAG 160
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 215401158 1771 QLIGKSGATGNfVRGAHLHFQLMQgshpgNDTAKDPEKWLKS 1812
Cdd:COG0739 161 QVIGYVGNTGR-STGPHLHFEVRV-----NGKPVDPLPFLPA 196
|
|
| Peptidase_M23 |
pfam01551 |
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ... |
1705-1798 |
9.13e-28 |
|
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins such as Swiss:P33648 for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.
Pssm-ID: 460250 [Multi-domain] Cd Length: 96 Bit Score: 108.79 E-value: 9.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1705 GRHYGIDFGMPSGTNVYAVKGGIADKVWTDYGGGNSIQIKTGANEWNWYMHLSKQLARQGQRIKAGQLIGKSGATGNfVR 1784
Cdd:pfam01551 1 RFHKGIDIAAPTGTPVYAAADGVVVFAGWLGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGR-ST 79
|
90
....*....|....
gi 215401158 1785 GAHLHFQLMQGSHP 1798
Cdd:pfam01551 80 GPHLHFEIRKNGKP 93
|
|
| M23_peptidase |
cd12797 |
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ... |
1707-1792 |
3.62e-27 |
|
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.
Pssm-ID: 410984 [Multi-domain] Cd Length: 85 Bit Score: 106.52 E-value: 3.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1707 HYGIDFGMPSGTNVYAVKGGIADKVWTDYGGGNSIQIKTGANEWNWYMHLSKQLARQGQRIKAGQLIGKSGATGNfVRGA 1786
Cdd:cd12797 1 HNGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGR-STGP 79
|
....*.
gi 215401158 1787 HLHFQL 1792
Cdd:cd12797 80 HLHFEI 85
|
|
| SLT |
COG3953 |
SLT domain protein [Mobilome: prophages, transposons]; |
1711-1945 |
4.14e-26 |
|
SLT domain protein [Mobilome: prophages, transposons];
Pssm-ID: 443153 [Multi-domain] Cd Length: 325 Bit Score: 111.35 E-value: 4.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1711 DFGMPSGTNVYAVKGGIADKVWTDYGGGNSIQIKTGANEWNWYMHLSKQLARQGQRIKAGQLIGK-----SGATGNFVRG 1785
Cdd:COG3953 93 SGAGPTSGGGAAAAGIGAGGAGNWLGNQAASGSSGAIGVAGGGKKVAGAANKAAKASSKAVAKGKtkavkGGGGISSGSG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1786 AHLHFQLMQGSHPGNDTAKDPEKWlkslKGSGVRSGSGVNKAASAWAGDIRRAAKrMGVNVTSGDVGNIISLIQHESGGN 1865
Cdd:COG3953 173 GGAQAATGKGGGGLGKGASKALGG----AGAGAGGGGGVGGGAGGWGIDIRQAAA-LGVPVSEAWVDGILRIIQHESGGN 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1866 AGITQssaLRDINVLQGNPAKGLLQYIPQTFRHYAVRGHNNIYSGYDQLLAFFNnrYWRSqfnpRGGWSPSGPRRYANGG 1945
Cdd:COG3953 248 PNAIN---LWDSNAAAGTPSKGLMQVIPPTFNAYKLPGHGNIYNPVDNILAGIN--YAKS----RYGSSDNVPGLASLGQ 318
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1691-1811 |
5.27e-16 |
|
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: 82.12 E-value: 5.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1691 QRFGRYTGGlnfnGGRHYGIDFGMPSGTNVYAVKGGIADKVWTDYGGGNSIQIKTGANEWNWYMHLSKQLARQGQRIKAG 1770
Cdd:COG4942 265 RRFGERDGG----GGRNKGIDIAAPPGAPVRAVADGTVVYAGWLRGYGNLVIIDHGGGYLTLYAHLSSLLVKVGQRVKAG 340
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 215401158 1771 QLIGKSGATGNfVRGAHLHFQLMQgshpgNDTAKDPEKWLK 1811
Cdd:COG4942 341 QPIGTVGSSGG-QGGPTLYFELRK-----NGKPVDPLPWLA 375
|
|
| SpoIIQ2 |
COG5821 |
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell ... |
1707-1811 |
2.31e-14 |
|
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444523 [Multi-domain] Cd Length: 200 Bit Score: 73.91 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1707 HYGIDFGMPSGTNVYAVKGGIADKVWTDYGGGNSIQIKTGANEWNWYMHL-SKQLARQGQRIKAGQLIGKSGATGNFVR- 1784
Cdd:COG5821 97 HTGIDIAAKEGTPVKAAADGVVVEVGKDPKYGITVVIDHGNGIKTVYANLdSKIKVKVGQKVKKGQVIGKVGSTALFESs 176
|
90 100
....*....|....*....|....*...
gi 215401158 1785 -GAHLHFQLMQgshpgNDTAKDPEKWLK 1811
Cdd:COG5821 177 eGPHLHFEVLK-----NGKPVDPMKYLK 199
|
|
| PRK11649 |
PRK11649 |
putative peptidase; Provisional |
1701-1806 |
4.37e-13 |
|
putative peptidase; Provisional
Pssm-ID: 236946 [Multi-domain] Cd Length: 439 Bit Score: 73.93 E-value: 4.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1701 NFNGGR----------HYGIDFGMPSGTNVYAVKGGiaDKVWTDYGG--GNSIQIKTGANEWNWYMHLSKQLARQGQRIK 1768
Cdd:PRK11649 297 NFNPRRlnpvtgrvapHRGVDFAMPVGTPVLAVGDG--EVVVAKRSGaaGNYVAIRHGRQYTTRYMHLRKLLVKPGQKVK 374
|
90 100 110
....*....|....*....|....*....|....*....
gi 215401158 1769 AGQLIGKSGATGNFVrGAHLHFQLMQGSHPGND-TAKDP 1806
Cdd:PRK11649 375 RGDRIALSGNTGRST-GPHLHYEVWINQQAVNPlTAKLP 412
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-280 |
1.05e-10 |
|
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: 67.39 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 3 EKVEGMTLELKLDHLGVQEGMKGLKRQLGVVNSEMKAnlsafdkSEKSMEKYQARIKGLNDRLKVQKKMYSQVEDELKQV 82
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE-------AEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 83 NANYQKAKSSVKDVEKAylklVEANKKEKLALDKSKEALKSSNTELKKAENQYKRTNQRKQDAYQKLKQLRDAEQ----K 158
Cdd:TIGR02168 816 NEEAANLRERLESLERR----IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEealaL 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 159 LKNSNQATTAQLKRASDAVQKQSAKHKALVEQYKQEGNQVQKLKVQNDNL--------SKSNDKIESSYAKTNTKLKQTE 230
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLqerlseeySLTLEEAEALENKIEDDEEEAR 971
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 215401158 231 KEFNDLNNTIK-----NHSA-----NVAKAETAVNKEKA----ALNNLERSIDKASSEMK-----TFNK 280
Cdd:TIGR02168 972 RRLKRLENKIKelgpvNLAAieeyeELKERYDFLTAQKEdlteAKETLEEAIEEIDREARerfkdTFDQ 1040
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
19-264 |
2.65e-10 |
|
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: 65.85 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 19 VQEGMKGLKRQLGVVNSEMKANLSAFDKSEKSMEKYQARIKGLN---DRLKVQKKMYS----QVEDELKQVNANYQKAKS 91
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAneiSRLEQQKQILRerlaNLERQLEELEAQLEELES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 92 SVKDVEKAylklVEANKKEKLALDKSKEALKSsntELKKAENQYKRTNQRKQDAYQKLKQLRDAEQKLKNSNQATTAQLK 171
Cdd:TIGR02168 331 KLDELAEE----LAELEEKLEELKEELESLEA---ELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 172 RASDavQKQSAKHKalVEQYKQEGNQVQKLKVQNDnlsksNDKIESSYAKTNTKLKQTEKEFNDLNNTIKNHSANVAKAE 251
Cdd:TIGR02168 404 RLEA--RLERLEDR--RERLQQEIEELLKKLEEAE-----LKELQAELEELEEELEELQEELERLEEALEELREELEEAE 474
|
250
....*....|...
gi 215401158 252 TAVNKEKAALNNL 264
Cdd:TIGR02168 475 QALDAAERELAQL 487
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
28-281 |
9.22e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 63.89 E-value: 9.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 28 RQLGVVNSEMKANLSAFDK--SEKSMEKYQARIKGLNDRLKVQKKMysqvedeLKQVNANYQKAKSSVK-DVEKAYLKLV 104
Cdd:TIGR04523 52 KEKELKNLDKNLNKDEEKInnSNNKIKILEQQIKDLNDKLKKNKDK-------INKLNSDLSKINSEIKnDKEQKNKLEV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 105 EANKKEKlALDKSKEALKSSNTELKKAENQ-------YKRTNQRKQDAYQKLKQLRDAEQKLKNSNQATTAQLKRasdaV 177
Cdd:TIGR04523 125 ELNKLEK-QKKENKKNIDKFLTEIKKKEKEleklnnkYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLK----L 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 178 QKQSAKHKALVEQYKQEGNQVQKLKVQNDNLSKSNDKIESSYAKTNTKLKQTEKEFNDLNNTIKNHSANVAKAETAVNKE 257
Cdd:TIGR04523 200 ELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN 279
|
250 260
....*....|....*....|....
gi 215401158 258 KAALNNLERSIDKASSEMKTFNKE 281
Cdd:TIGR04523 280 NKKIKELEKQLNQLKSEISDLNNQ 303
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
910-1140 |
9.39e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 63.99 E-value: 9.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 910 ETEKALEKYvhYSEENSRIMEKVRLNSGQISEDKAKKL--LKIETDLSNnliaeieKRNKKELEKTQelidKYSAFDEQE 987
Cdd:pfam17380 345 ERERELERI--RQEERKRELERIRQEEIAMEISRMRELerLQMERQQKN-------ERVRQELEAAR----KVKILEEER 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 988 KQNILTRTKEKNDLRIKKE---QELNQKIKELKEKALSDGQISENERK-EIEKLENQRRDITVKELSKtEKEQERILVRM 1063
Cdd:pfam17380 412 QRKIQQQKVEMEQIRAEQEearQREVRRLEEERAREMERVRLEEQERQqQVERLRQQEEERKRKKLEL-EKEKRDRKRAE 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1064 QRNRNAY--SIDEASKAIKEAEKARKARKKEVDKQyeDDVIAIKNNVNLSKSEKDKLLAIADQRH-KDEVRKA---KSKK 1137
Cdd:pfam17380 491 EQRRKILekELEERKQAMIEEERKRKLLEKEMEER--QKAIYEEERRREAEEERRKQQEMEERRRiQEQMRKAteeRSRL 568
|
...
gi 215401158 1138 DAV 1140
Cdd:pfam17380 569 EAM 571
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
96-274 |
1.11e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 62.61 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 96 VEKAYLKLVEANKKEKLALDKSKEALKSSNTELKKAENQYKRTNQRKQDAYQKLKQLRDAEQKLKNSNQATTAQLKRASD 175
Cdd:COG4372 8 VGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 176 AVQKQSAKHKALVEQ-------YKQEGNQVQKLKVQNDNLSKSNDKIESSYAKTNTKLKQTEKEFNDLNNTIKNHSANVA 248
Cdd:COG4372 88 QLQAAQAELAQAQEEleslqeeAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELA 167
|
170 180
....*....|....*....|....*.
gi 215401158 249 KAETAVNKEKAAlnNLERSIDKASSE 274
Cdd:COG4372 168 ALEQELQALSEA--EAEQALDELLKE 191
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
19-237 |
1.35e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 62.23 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 19 VQEGMKGLKRQLGVVNSEMKANLSAFDKSEKSMEKYQARIKGLNDRLKVQKKMYSQVEDELKQVNANYQKAKSSVKDVEK 98
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 99 AYLKLVEANKKEKLALDKSKEALKSSNTELKKAENQYKRTNQRKQDAYQKLKQLRDAEqklknSNQATTAQLKRASDAVQ 178
Cdd:COG4372 123 ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE-----AEQALDELLKEANRNAE 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 215401158 179 KQSAKHKALVEQYKQEGNQVQKLKVQNDNLSKSNDKIESSYAKTNTKLKQTEKEFNDLN 237
Cdd:COG4372 198 KEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
893-1227 |
2.13e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 893 SKKASDTVKVLGKGVSKETEKALEkyVHYSEENSRIMEKVRL----NSGQISEDKAKKLLKIETDLSNNLIAEIEKRNKK 968
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADELKKAEE--LKKAEEKKKAEEAKKAeedkNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 969 ELEKTQELIDKYSAF-DEQEKQNILTRTKEKNDLRIKKEQELNQKIKELKEKALSDGQISENERKEIEKLENQRRDITVK 1047
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA 1690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1048 ELSKTEKEQERILVRMQRNRNAYSIDEASKaIKEAEKARKARKKEVDKQYEDDVIAIKnNVNLSKSEKDKLLAIADQRHK 1127
Cdd:PTZ00121 1691 AEALKKEAEEAKKAEELKKKEAEEKKKAEE-LKKAEEENKIKAEEAKKEAEEDKKKAE-EAKKDEEEKKKIAHLKKEEEK 1768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1128 DEVRKAKSKKDAVVDVVKKQNKDIDKEMDLSSGRVYKNTEKWWNGLKSwWSNFREDQKKKSDKYAKEQEETARRNRENIK 1207
Cdd:PTZ00121 1769 KAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKE-GNLVINDSKEMEDSAIKEVADSKNMQLEEAD 1847
|
330 340
....*....|....*....|....*
gi 215401158 1208 -----KWFGNAWDGVKSKTGEAFSK 1227
Cdd:PTZ00121 1848 afekhKFNKNNENGEDGNKEADFNK 1872
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
894-1208 |
2.77e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.85 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 894 KKASDTVKVLGKGVSKETEKALEKYVHYSEENSRIMEKVRLNSGQISEDKAKKLLKiETDLSNNLIAEIEKRNKKELEKT 973
Cdd:PTZ00121 1284 KKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAE-EAKKAAEAAKAEAEAAADEAEAA 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 974 QEL--IDKYSAFDEQEKQNILTRTKE---KNDLRIKKEQELNQKIKELKEKALSDGQISENERKEIE---------KLEN 1039
Cdd:PTZ00121 1363 EEKaeAAEKKKEEAKKKADAAKKKAEekkKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEkkkadeakkKAEE 1442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1040 QRRDITVKELSKTEKEQERILVRMQRNRNAysiDEASKAIKEAEKARKARKK-EVDKQYEDDVI----AIKNNVNLSKSE 1114
Cdd:PTZ00121 1443 AKKADEAKKKAEEAKKAEEAKKKAEEAKKA---DEAKKKAEEAKKADEAKKKaEEAKKKADEAKkaaeAKKKADEAKKAE 1519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1115 K----DKLLAIADQRHKDEVRKAKSKKDA--------------VVDVVKKQNKDIDKEMDLSSGRVYKNTEKwwNGLKSW 1176
Cdd:PTZ00121 1520 EakkaDEAKKAEEAKKADEAKKAEEKKKAdelkkaeelkkaeeKKKAEEAKKAEEDKNMALRKAEEAKKAEE--ARIEEV 1597
|
330 340 350
....*....|....*....|....*....|..
gi 215401158 1177 WSNFREDQKKKSDKYAKEQEEtaRRNRENIKK 1208
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEA--KIKAEELKK 1627
|
|
| COG5412 |
COG5412 |
Phage-related protein [Mobilome: prophages, transposons]; |
408-861 |
5.13e-09 |
|
Phage-related protein [Mobilome: prophages, transposons];
Pssm-ID: 444167 [Multi-domain] Cd Length: 704 Bit Score: 61.64 E-value: 5.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 408 ASGAEMATTATVMASAINSFGLKASDANHVADLLARSANDSAADIQYMGDALK-YAGTPAKALGVSIEDTSAAIEVLSNS 486
Cdd:COG5412 2 AAADASAKEAASAALLLAQAKAADSELTAASGGVVSAAAKAQGSIAQLGKIGAaAGAEAALADSSLAFATLAAALGATVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 487 GLEGSQAGTALRASFIRLANPSKNTAKEMKKLGIHLSDAKGQFVGMGELIRQFQDNMKGMTREQKLATVATIVGTEAASG 566
Cdd:COG5412 82 GASLLLAAGGARAKGSAAAAAALGAVAAAAKVLNGALAAAGAALAATQALAAAATGAKGEANAAAKAGGAAALASAGLAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 567 FLALIEAgpDKINSYSKSLKNSNGESKKAADLMKDNLKGALEQLGGAFESLAIEVGKDLTPMIRAGAEGLTKLvdgfthl 646
Cdd:COG5412 162 AGAAAAA--SALAAAGAIAKAILSASKLSGQALAGQSAAAGGALEAAAAAAAGAAAAGAAAAAATAASALLAL------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 647 pgwvrKASVGLALFGAAIGPAVLAGGLLIRTVGSAAKGYASLNRRIAENTILSNTNSKAMKSLGLQTLFLGSTTGKTSKG 726
Cdd:COG5412 233 -----AALQGLAAGAATGAAAGAAGAAGLGAAGAGAGQAAALLGLVAGAEASGGTAGGAVAGLAAGLAAAAGASANLGAA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 727 FKGLAGA-MMFNLKPINVLKNSAKLAILPFKLLKNGLGLAAKSLFAVSGG-------------ARFAGVALRFLTGPIGA 792
Cdd:COG5412 308 AAASFGAsLAASAGVDTAAAALAAAEAIADGSLVAGLGSAGTVLSTLSGAvgglegaigqlgaAGGLGSALGGLTGPIGI 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 215401158 793 TITAITIAYKVFKTAYDRVEWFRNGINGLGETIKFfgGKIIGGAVRKLGEFknyLGSIGKSFKEKFSKD 861
Cdd:COG5412 388 VIAAIAALIAAFVALWKNSETFRNLVQGVWELNAI--KTAIEGVVSAIVTF---ISALWEAIKALLTAI 451
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
93-388 |
6.35e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 6.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 93 VKDVEKAYLKLVEANKKEKLALDKSKEALKSSNTELKKAENQYKRTNQRKQDAYQKLKQLRDAEQKLKNSNQATTAQLKR 172
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 173 ASDAVQKQSAKHK---------ALVEQYKQEGNQVQKLKVQNDNLSKSNDKIESSYAKTNTklkQTEKEFNDLNNTIKNH 243
Cdd:COG4717 128 LPLYQELEALEAElaelperleELEERLEELRELEEELEELEAELAELQEELEELLEQLSL---ATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 244 SANVAKAETAVNKEKAALNNLERSIDKASSEMKTFNKEQMIAQ--SHFGKLASQADVMSKKFSSIGDKMTSLGrtMTMGV 321
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEarLLLLIAAALLALLGLGGSLLSLILTIAG--VLFLV 282
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 215401158 322 STPITLGLGAALKTSADFEGQMSRVGAIAQASSKDLKSMSNQAVDLGAKTSKSANEVAKGMEELAAL 388
Cdd:COG4717 283 LGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL 349
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
52-287 |
1.12e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 52 EKYQARIKGLNDRLKVQKKmySQVEDELKQVNANYQKAKSSVKDVEKAYLKLVEANKKEKLALDKSKEALKSSNTELKKA 131
Cdd:COG1196 223 KELEAELLLLKLRELEAEL--EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 132 ENQYKRTNQRKQDAYQKLKQLRDAEQKLKNSNQATTAQLKRASDAVQKQSAKHKALVEQYKQEGNQVQKLKVQNDNLSKS 211
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 215401158 212 NDKIESSYAKTNTKLKQTEKEFNDLNNTIKNHSANVAKAETAVNKEKAALNNLERSIDKASSEMKTFNKEQMIAQS 287
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
941-1145 |
1.50e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 57.63 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 941 EDKAKKLLKI-ETDLSnnlIAEIEKRNKKELEKTQELIDKYsafdEQEKQNILTRTKEKNDLRIKKEQ------ELNQKI 1013
Cdd:COG1579 3 PEDLRALLDLqELDSE---LDRLEHRLKELPAELAELEDEL----AALEARLEAAKTELEDLEKEIKRleleieEVEARI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1014 KELKEKAlsdGQISENE-----RKEIEKLEnqrrditvKELSKTEKEQERILVRmqrnrnaysIDEASKAIKEAEKARKA 1088
Cdd:COG1579 76 KKYEEQL---GNVRNNKeyealQKEIESLK--------RRISDLEDEILELMER---------IEELEEELAELEAELAE 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 215401158 1089 RKKEVD---KQYEDDVIAIKNNVNLSKSEKDKLLAIADQRHKDEVRKAKSKKD--AVVDVVK 1145
Cdd:COG1579 136 LEAELEekkAELDEELAELEAELEELEAEREELAAKIPPELLALYERIRKRKNglAVVPVEG 197
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
45-259 |
1.76e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 45 DKSEKSMEKYQARIKGLNDRLKVQKKMYSQVEDELKQVNANYQKAKSSVKDVEKAYLKL---VEANKKEKLALDKSKEAL 121
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALeaeLAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 122 KSSNTELKKAenQYKRTNQRK-------QDAYQK------LKQLRDAEQKLKNSNQATTAQLKRASDAVQKQSAKHKALV 188
Cdd:COG4942 103 KEELAELLRA--LYRLGRQPPlalllspEDFLDAvrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215401158 189 EQYKQEGNQVQKLKVQNDNLSKSNDKIESSYAKTNTKLKQTEKEFNDLNNTIKNHSANVAKAETAVNKEKA 259
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
106-398 |
2.03e-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: 59.69 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 106 ANKKEKLALDKSKEALKSSNTELKKAENQYKRTNQRKQdayQKLKQLRDAEQklknsnqattaQLKRASDAVQKQSAKHK 185
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELE---EELEQLRKELE-----------ELSRQISALRKDLARLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 186 ALVEQYKQegnQVQKLKVQNDNLSKSNDKIESSYAKTNTKLKQTEKEFNDLNNTIKNHSANVAKAETAVNKEKAALNNLE 265
Cdd:TIGR02168 740 AEVEQLEE---RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 266 RSIDKASSEMKTFNKEQMIAQSHFGKLASQADVMSKKFSSIGDKMTSLGRTMtmgvsTPITLGLGAALKTSADFEGQMSR 345
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI-----EELESELEALLNERASLEEALAL 891
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 215401158 346 VGAIAQASSKDLKSMSNQAVDLGAKTSKSANEVAKGMEELAALGFNAKQTMEA 398
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
23-281 |
3.71e-08 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 56.19 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 23 MKGLKRQLGVVNSEMKANLSAFDKSEKSMEKYQARIKGLNDRLkvqkkmySQVEDELKQVNanyqkakssvKDVEKAYLK 102
Cdd:pfam00261 3 MQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRI-------QLLEEELERTE----------ERLAEALEK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 103 LVEANKkeklALDKSKEALKS-SNTELK------KAENQYKRTNQRKQDAyqkLKQLRDAEQKLKnsnqATTAQLKRASD 175
Cdd:pfam00261 66 LEEAEK----AADESERGRKVlENRALKdeekmeILEAQLKEAKEIAEEA---DRKYEEVARKLV----VVEGDLERAEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 176 AVQKQSAKHKALVEQYKQEGNQVQKLKVQNDNLSKSNDKIESSYAKTNTKLKQTEkefndlnntiknhsANVAKAETAVN 255
Cdd:pfam00261 135 RAELAESKIVELEEELKVVGNNLKSLEASEEKASEREDKYEEQIRFLTEKLKEAE--------------TRAEFAERSVQ 200
|
250 260
....*....|....*....|....*.
gi 215401158 256 KEKAALNNLERSIDKASSEMKTFNKE 281
Cdd:pfam00261 201 KLEKEVDRLEDELEAEKEKYKAISEE 226
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
908-1208 |
3.75e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 908 SKETEKALEKYVHYSEENSRIMEKVRLNSGQISED--KAKKLLKIEtdlsnnliaeiEKRNKKELEKTQELidkySAFDE 985
Cdd:PTZ00121 1242 AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEarKADELKKAE-----------EKKKADEAKKAEEK----KKADE 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 986 QEKQnilTRTKEKNDLRIKKEQELNQKIKELKEKALSDGQISENERKEIEKlenqrrdiTVKELSKTEKEQERilVRMQR 1065
Cdd:PTZ00121 1307 AKKK---AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEA--------AADEAEAAEEKAEA--AEKKK 1373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1066 NRNAYSIDEASKAIKEAEKARKARKK-EVDKQYEDDViaikNNVNLSKSEKDKLLAIADQRHKDEVRKAKSKKDAVVDVV 1144
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKKKADEAKKKaEEDKKKADEL----KKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEA 1449
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 215401158 1145 KKQNKDIDKEMDLSSgrvyKNTEKwwngLKSWWSNFREDQKKKSDKYAKEQEETARRNRENIKK 1208
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKK----KAEEA----KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA 1505
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
912-1132 |
6.19e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 56.85 E-value: 6.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 912 EKALEKYVHYSEENSRIMEKVRLnsgQISEDKAKKLLKIE--TDLSNNLIAEIEKRNK-KELEKTQELID---------- 978
Cdd:pfam13868 87 QKRQEEYEEKLQEREQMDEIVER---IQEEDQAEAEEKLEkqRQLREEIDEFNEEQAEwKELEKEEEREEderileylke 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 979 ---KYSAFDEQEKQNILTRTKEKNDLRikKEQELNQKIKELKEKALSDGQISENER----KEIEKLENQRRDitVKELSK 1051
Cdd:pfam13868 164 kaeREEEREAEREEIEEEKEREIARLR--AQQEKAQDEKAERDELRAKLYQEEQERkerqKEREEAEKKARQ--RQELQQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1052 TEKEQERILVRMQRnrnaysideaskaiKEAEKARKARKKEVDKQYEDDVIAIKNNvnlsksEKDKLLaiaDQRHKDEVR 1131
Cdd:pfam13868 240 AREEQIELKERRLA--------------EEAEREEEEFERMLRKQAEDEEIEQEEA------EKRRMK---RLEHRRELE 296
|
.
gi 215401158 1132 K 1132
Cdd:pfam13868 297 K 297
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
11-275 |
7.32e-08 |
|
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: 58.13 E-value: 7.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 11 ELKLDHLGVQEGMKGLKRQLGVVNSEMKANLSAfdkSEKSMEKYQARIKGLNDRLKVQKKMYSQVEDELKQVNANYQKAK 90
Cdd:TIGR00606 391 QIKNFHTLVIERQEDEAKTAAQLCADLQSKERL---KQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLE 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 91 SSVKDVekayLKLVEANKKEKLALDKskeALKSSNTELKKAENQYKRTNQRKQDayqklKQLRDAEQKLKNSNQATTAQL 170
Cdd:TIGR00606 468 GSSDRI----LELDQELRKAERELSK---AEKNSLTETLKKEVKSLQNEKADLD-----RKLRKLDQEMEQLNHHTTTRT 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 171 KRASDAVQKQSA-------KHKALVEQYKQEGNQVQKLKVQNDNLSKSNDK--IESSYAKTNTKLKQTEKEFNDLNNTIK 241
Cdd:TIGR00606 536 QMEMLTKDKMDKdeqirkiKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEInqTRDRLAKLNKELASLEQNKNHINNELE 615
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 215401158 242 NHSANVAKAETAV------NKEKAALNNLERSIDKASSEM 275
Cdd:TIGR00606 616 SKEEQLSSYEDKLfdvcgsQDEESDLERLKEEIEKSSKQR 655
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
938-1209 |
7.37e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 58.06 E-value: 7.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 938 QISEDKAKKLLKIETDLSNNLIAEIEKRNKKELEKTQelidkysafdEQEKQNILTRTKEKNDLRIKKEQELNQKIKE-- 1015
Cdd:pfam02463 146 IIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEET----------ENLAELIIDLEELKLQELKLKEQAKKALEYYql 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1016 -LKEKALSDGQISENERKEIEKLENQRRDITVKELSKTEKEQERIlvrmqrnrnaysIDEASKAIKEAEKARKARKKEVD 1094
Cdd:pfam02463 216 kEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEI------------EKEEEKLAQVLKENKEEEKEKKL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1095 KQYEDDVIAIKNNVNLSKSEKDKLLAIADQRHKDEVRKAKSKKDAVVDVVKKQNKDIDKEMDLSSGRVYKNTEKWWNGLK 1174
Cdd:pfam02463 284 QEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEK 363
|
250 260 270
....*....|....*....|....*....|....*
gi 215401158 1175 swwsNFREDQKKKSDKYAKEQEETARRNRENIKKW 1209
Cdd:pfam02463 364 ----LQEKLEQLEEELLAKKKLESERLSSAAKLKE 394
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
55-282 |
7.88e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 7.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 55 QARIKGLNDRLKVQKKMYSQVEDELKQVNANYQKAKSSVKDVEKaylklveankkeklALDKSKEALKSSNTELKKAENQ 134
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER--------------RIAALARRIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 135 YKRTNQRKQDAYQKLKQLRDAEQKL-----KNSNQATTAQLKRASDAvqKQSAKHKALVEQYKQE-GNQVQKLKVQNDNL 208
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELlralyRLGRQPPLALLLSPEDF--LDAVRRLQYLKYLAPArREQAEELRADLAEL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 215401158 209 SKSNDKIESSYAKTNTKLKQTEKEFNDLNNTIKNHSANVAKAETAVNKEKAALNNLERSIDKASSEMKTFNKEQ 282
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
923-1208 |
8.65e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 8.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 923 EENSRIMEKVRLNSGQISEDKaKKLLKIETDLSNNLIaEIEKrnkkELEKTQELIDKYSAFDEQEkqNILTRTKEKNDLR 1002
Cdd:PRK03918 448 EHRKELLEEYTAELKRIEKEL-KEIEEKERKLRKELR-ELEK----VLKKESELIKLKELAEQLK--ELEEKLKKYNLEE 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1003 IKKEQELNQKIKELKEKALSDGQISENERKEIEKLENQRRDITvKELSKTEKEQERILVRMqRNRNAYSIDEASKAIKEA 1082
Cdd:PRK03918 520 LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELE-KKLDELEEELAELLKEL-EELGFESVEELEERLKEL 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1083 EKARKARKKEVDKQYEddviaIKNNVNLSKSEKDKLlaiadqrhkDEVRKAKSKKDAVVDVVKKQNKDIDKEMD------ 1156
Cdd:PRK03918 598 EPFYNEYLELKDAEKE-----LEREEKELKKLEEEL---------DKAFEELAETEKRLEELRKELEELEKKYSeeeyee 663
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 215401158 1157 -----LSSGRVYKNTEKWWNGLKSwwsnfREDQKKKSDKYAKEQEETARRNRENIKK 1208
Cdd:PRK03918 664 lreeyLELSRELAGLRAELEELEK-----RREEIKKTLEKLKEELEEREKAKKELEK 715
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
892-1241 |
9.46e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 9.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 892 ASKKASDTVKVLGKGVSKETEKALEkyVHYSEENSRIMEKVRLNSGQISED--KAKKLLKIETDLSnnliaEIEKRNKKE 969
Cdd:PTZ00121 1120 AKKKAEDARKAEEARKAEDARKAEE--ARKAEDAKRVEIARKAEDARKAEEarKAEDAKKAEAARK-----AEEVRKAEE 1192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 970 LEKTQEL--IDKYSAFDEQEKQNILTRTKEKNDLR-IKKEQELNQKIKELK--EKALSDGQISENERKEIEKLENQRRDI 1044
Cdd:PTZ00121 1193 LRKAEDArkAEAARKAEEERKAEEARKAEDAKKAEaVKKAEEAKKDAEEAKkaEEERNNEEIRKFEEARMAHFARRQAAI 1272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1045 TVKELSKTEK----EQERILVRMQRNRNAYSIDEASKAIKEAEKARKARKK---------EVDKQYEDDVIAIKNNVNLS 1111
Cdd:PTZ00121 1273 KAEEARKADElkkaEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKaeeakkkadAAKKKAEEAKKAAEAAKAEA 1352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1112 KSEKDKLLAIADQRHKDEVRKAKSKKDAvvDVVKKQNKDIDKEMDLSsgRVYKNTEKWWNGLKSwwsnfREDQKKKSDKY 1191
Cdd:PTZ00121 1353 EAAADEAEAAEEKAEAAEKKKEEAKKKA--DAAKKKAEEKKKADEAK--KKAEEDKKKADELKK-----AAAAKKKADEA 1423
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 215401158 1192 AKEQEETARRNRENIKKWFGNAWDGVKSKTGEAfsKMGRNANHFGGEMKK 1241
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA--KKAEEAKKKAEEAKK 1471
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
26-414 |
1.16e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 57.44 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 26 LKRQLGVVNSEMKaNLSAFDKSEKS-----MEKYQARIKGLNDRLKVQKKMYSQVEdelkqvnanyqkaksSVKDVEKay 100
Cdd:pfam15921 417 LRRELDDRNMEVQ-RLEALLKAMKSecqgqMERQMAAIQGKNESLEKVSSLTAQLE---------------STKEMLR-- 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 101 lKLVEANKKEKLALDKSKEALKSSNTELKKAENQYKRTN-------QRKQDAYQKLKQLRDAEQKLKNSN---QATTAQL 170
Cdd:pfam15921 479 -KVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNaeitklrSRVDLKLQELQHLKNEGDHLRNVQtecEALKLQM 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 171 KRASDAVQKQSAKHKALVEQYKQEGNQVQKLKVQNDNLSKS-NDK------IESSYAKTNTKLKQTEKEFNDLN-NTIK- 241
Cdd:pfam15921 558 AEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEiNDRrlelqeFKILKDKKDAKIRELEARVSDLElEKVKl 637
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 242 -NHSANVAKAETAVNKEKAALNN------------------LERSIDKASSEMK-TFNKEQMIAQSHFGKLASQADVMSK 301
Cdd:pfam15921 638 vNAGSERLRAVKDIKQERDQLLNevktsrnelnslsedyevLKRNFRNKSEEMEtTTNKLKMQLKSAQSELEQTRNTLKS 717
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 302 KFSSIGDKMtslgrTMTMGVSTPITLGLGA--ALKTSADF-EGQMSRvgaiAQASSKDLKSMSNQavdLGAKTSKSANEV 378
Cdd:pfam15921 718 MEGSDGHAM-----KVAMGMQKQITAKRGQidALQSKIQFlEEAMTN----ANKEKHFLKEEKNK---LSQELSTVATEK 785
|
410 420 430
....*....|....*....|....*....|....*.
gi 215401158 379 AKGMEELAALGFNAKQTMEAMPGVISAAEASGAEMA 414
Cdd:pfam15921 786 NKMAGELEVLRSQERRLKEKVANMEVALDKASLQFA 821
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
909-1159 |
1.46e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 909 KETEKALEKYVHYSEENSRIMEKVRlnsgqisedKAKKLLKIETDLSNNLIAEIEKRNKKE------LEKTQELIDKYSA 982
Cdd:PRK03918 286 KELKEKAEEYIKLSEFYEEYLDELR---------EIEKRLSRLEEEINGIEERIKELEEKEerleelKKKLKELEKRLEE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 983 FDE------------QEKQNILTRTKEKNDLRIKKE--------QELNQKIKELKEKALSDGQISENERKEIEKLENQRR 1042
Cdd:PRK03918 357 LEErhelyeeakakkEELERLKKRLTGLTPEKLEKEleelekakEEIEEEISKITARIGELKKEIKELKKAIEELKKAKG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1043 DITV--KELskTEKEQERILVRMQRNRNaySIDEASKAIKEAEKARKARKKEVDK--QYEDDVIAIKNNVNLSKSEKDKL 1118
Cdd:PRK03918 437 KCPVcgREL--TEEHRKELLEEYTAELK--RIEKELKEIEEKERKLRKELRELEKvlKKESELIKLKELAEQLKELEEKL 512
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 215401158 1119 LAIADQ---RHKDEVRKAKSKKDAVVDVVKKQNKDIDKEMDLSS 1159
Cdd:PRK03918 513 KKYNLEeleKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKK 556
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
47-260 |
1.57e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 47 SEKSMEKYQARIKGLNDRLKVQKKMYSQVEDELKQV----NANYQKAKSSVKDVEKAYLKLVEANKKEKLAlDKSKEALK 122
Cdd:PTZ00121 1251 NEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAeekkKADEAKKAEEKKKADEAKKKAEEAKKADEAK-KKAEEAKK 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 123 SSNTELKKAENQYKRTNQRKQDAYQKLKQLRDAEQKLKNSNQATTAQLKRASDAVQKQSAKHKA-----LVEQYKQEGNQ 197
Cdd:PTZ00121 1330 KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAdeakkKAEEDKKKADE 1409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 215401158 198 VQKLKVQNDNLSKSNDKIESSYAKTNTKLKQTEKEFNDlnnTIKNHSANVAKAETAVNKEKAA 260
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKAD---EAKKKAEEAKKAEEAKKKAEEA 1469
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
36-296 |
1.78e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 36 EMKANLSAFDKSEKSMEKYQARIKGLNDRLKVQKKmysQVEDELKQVNANYQKAKSSVKDVEKAYLKLVEANKKEKlALD 115
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA---KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAE-AKK 1510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 116 KSKEALKSSNT----ELKKAENQYKRTNQRKQDAYQKLKQLRDAEQKLKNSNQATTAQLKRASDAVQKQSAKHKALVEQY 191
Cdd:PTZ00121 1511 KADEAKKAEEAkkadEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAE 1590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 192 KQEGNQVQKLKVQNDNLSKSNDKIESSYAKTNTKLKQTEKEFNDLNNTIKNHSANVAKAETAVNKE------KAALNNLE 265
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEeenkikAAEEAKKA 1670
|
250 260 270
....*....|....*....|....*....|.
gi 215401158 266 RSIDKASSEMKTFNKEQMIAQSHFGKLASQA 296
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDEKKAAEALKKEAEEA 1701
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
26-282 |
1.86e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.57 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 26 LKRQLGVVNSEMKANLSAFDKSEKSMEKYQARIKGLNDRLKVQKKMYSQVEDELKQVNANYQKakssvkdVEKAYLKLVE 105
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL-------LEKEIERLKE 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 106 ANKKEKlaldKSKEALKSSNTELKKaenQYKRTNQRKQDAYQKLKQLRDAEQKLKNSNQATTAQLKRasdavqkQSAKHK 185
Cdd:TIGR04523 434 TIIKNN----SEIKDLTNQDSVKEL---IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS-------KEKELK 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 186 ALVEQYKQEGNQVQKLKVQNDNLSKSNDKIESSYAKTNTKLKQTEKEFNDLNNTIKNhsANVAKAETAVNKE----KAAL 261
Cdd:TIGR04523 500 KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKK--ENLEKEIDEKNKEieelKQTQ 577
|
250 260
....*....|....*....|....*...
gi 215401158 262 NNLERS-------IDKASSEMKTFNKEQ 282
Cdd:TIGR04523 578 KSLKKKqeekqelIDQKEKEKKDLIKEI 605
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
52-281 |
1.96e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.18 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 52 EKYQARIKGLNDRLKVQKKMYSQVEDELKQVNANYQKAKSSVKDVEKAyLKLVEANKKEKlaldksKEALKSSNTELKKA 131
Cdd:TIGR04523 303 QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKE-LTNSESENSEK------QRELEEKQNEIEKL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 132 ENQykrtNQRKQDAYQKLK-QLRDAEQKLKNSNQattaqlkrasDAVQKQSaKHKALVEQYKQEGNQVQKLKVQNdnlSK 210
Cdd:TIGR04523 376 KKE----NQSYKQEIKNLEsQINDLESKIQNQEK----------LNQQKDE-QIKKLQQEKELLEKEIERLKETI---IK 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215401158 211 SNDKIESSYAKTNTKlkqtEKEFNDLNNTIKNHSANVAKAETAVNKEKAALNNLERSIDKASSEMKTFNKE 281
Cdd:TIGR04523 438 NNSEIKDLTNQDSVK----ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE 504
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
55-234 |
2.31e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 55 QARIKGLNDRLKvqkkmysQVEDELKQVNANYQKAKSSVKDVEK---AYLKLVEAN---------KKEKLALDKSKEALK 122
Cdd:COG4913 609 RAKLAALEAELA-------ELEEELAEAEERLEALEAELDALQErreALQRLAEYSwdeidvasaEREIAELEAELERLD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 123 SSNTELKKAENQYKRTNQRKQDAYQKLKQLRDAEQKLKNSNQATTAQLKRASDAVQ-----KQSAKHKALVEQYKQEG-- 195
Cdd:COG4913 682 ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEaaedlARLELRALLEERFAAALgd 761
|
170 180 190
....*....|....*....|....*....|....*....
gi 215401158 196 NQVQKLKvqnDNLSKSNDKIESSYAKTNTKLKQTEKEFN 234
Cdd:COG4913 762 AVERELR---ENLEERIDALRARLNRAEEELERAMRAFN 797
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
891-1202 |
3.86e-07 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 55.40 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 891 TASKKASDTVKVLGKGVSKETEKALEKyVHYSEENSRIMEKVRLNsgqisedkaKKLLKIETDLSNNLIAEIEKRNKKEL 970
Cdd:NF033838 47 TVTSSGNESQKEHAKEVESHLEKILSE-IQKSLDKRKHTQNVALN---------KKLSDIKTEYLYELNVLKEKSEAELT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 971 EKTQELIDkySAFdEQEKQNILTRTKEKNDLRiKKEQELNQKIKELKEKALSDgqISENERKEIEkLENQRRDITVKEls 1050
Cdd:NF033838 117 SKTKKELD--AAF-EQFKKDTLEPGKKVAEAT-KKVEEAEKKAKDQKEEDRRN--YPTNTYKTLE-LEIAESDVEVKK-- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1051 kteKEQERILVRMQRNRNAYSIDEAsKAIKEAEKARKARKKEV--DKQYEDDVIAIKNNVNLSKSEKDKLLAIADQRHKD 1128
Cdd:NF033838 188 ---AELELVKEEAKEPRDEEKIKQA-KAKVESKKAEATRLEKIktDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKR 263
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 215401158 1129 EVRKAKSKKDAVVDvvKKQNKDidKEMDLSSGRVYKNTEKWWNGLKSwwsnfREDQKKK--SDKYAKEQEETARRN 1202
Cdd:NF033838 264 RAKRGVLGEPATPD--KKENDA--KSSDSSVGEETLPSPSLKPEKKV-----AEAEKKVeeAKKKAKDQKEEDRRN 330
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
922-1157 |
4.92e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 55.36 E-value: 4.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 922 SEENSRIMEKVRLNSGQISEDKAKKLLKIETDLSNNLIAEIEKRNKKELEKTQELIDKYSAFDEQEKQNILTRTKEKNDL 1001
Cdd:pfam02463 792 KEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQE 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1002 RIKKEQELNQKIKELKEKALSDGQisENERKEIEKLENQRRDITVKELSKTEKEQERILVRMQRNRNAYSIDEASKAIKE 1081
Cdd:pfam02463 872 LLLKEEELEEQKLKDELESKEEKE--KEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKE 949
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 215401158 1082 AEKARKARKKEVDKQYEDDVIAIKNNVNLSKSEKDKLLAIADQRHKDEVRKAKSKKDAVVDVVKKQNKDIDKEMDL 1157
Cdd:pfam02463 950 KEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLEL 1025
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
910-1147 |
8.47e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 8.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 910 ETEKALEKYVHYSEENSRIMEKVRLNSGQISEDKAKKLLKIETDLSNNLIAEIEKRNKKELEKTQELIDKYSAFDEQEKQ 989
Cdd:COG1196 266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 990 niLTRTKEKNDLRIKKEQELNQKIKELKEKALSDGQISENERKEIEKLENQRRDITvKELSKTEKEQERILVRMQRNRNA 1069
Cdd:COG1196 346 --LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA-AQLEELEEAEEALLERLERLEEE 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 215401158 1070 ysIDEASKAIKEAEKARKARKKEVDKQYEDDVIAIKNNVNLSKSEKDKLLAIADQRHKDEVRKAKSKKDAVVDVVKKQ 1147
Cdd:COG1196 423 --LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
72-274 |
9.46e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 9.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 72 YSQVEDElKQVNANYQKAKSSVKDVEKAYLKLVEANKKEKL--ALDKSKEALKSsnTELKKAENQYKRTNQRKQDAYQKL 149
Cdd:COG4913 214 REYMLEE-PDTFEAADALVEHFDDLERAHEALEDAREQIELlePIRELAERYAA--ARERLAELEYLRAALRLWFAQRRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 150 KQLRDAEQKLKNSNQATTAQLKRASDAVQKQSAKHKALVEQYKQ-EGNQVQKLKVQNDNLSKSNDKIESSYAKTNTKLKQ 228
Cdd:COG4913 291 ELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERERRRARLEALLAA 370
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 215401158 229 -------TEKEFNDLNNTIKNHSANVAKAETAVNKE----KAALNNLERSIDKASSE 274
Cdd:COG4913 371 lglplpaSAEEFAALRAEAAALLEALEEELEALEEAlaeaEAALRDLRRELRELEAE 427
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
907-1143 |
9.59e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 9.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 907 VSKETEKALEKYVHYSEENSRIMEKVRLNSGQISEDKaKKLLKIETDL--SNNLIAEIEKR------NKKELEKTQELID 978
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELE-EEIEELQKELyaLANEISRLEQQkqilreRLANLERQLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 979 KYSAFDEQEKQNILTR----TKEKNDLRIKKE------QELNQKIKELKEKALSDGQISENERKEIEKLENQRRDITvKE 1048
Cdd:TIGR02168 323 AQLEELESKLDELAEElaelEEKLEELKEELEsleaelEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN-NE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1049 LSKTEKEQERILVRMQRNRNaySIDEASKAIKEAEKARKARKKEVDKQYEDDVIAIKNNVNLSKSEKDKLLAIADQR--- 1125
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQ--EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAlda 479
|
250
....*....|....*...
gi 215401158 1126 HKDEVRKAKSKKDAVVDV 1143
Cdd:TIGR02168 480 AERELAQLQARLDSLERL 497
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
38-377 |
1.35e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.98 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 38 KANLSAFDKSEKSMEKyqarIKGLNDRLKVQKKMYSQVEDELKQVNANYQKAKSSVKDVEKaylKLVEANKKeklaLDKS 117
Cdd:COG4372 10 KARLSLFGLRPKTGIL----IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEE---ELEQARSE----LEQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 118 KEALKSSNTELKKAENQYKRTNQRKQDAYQKLKQLRDAEQKLKNSNQATTAQLKRASDAVQKQSAKHKALVEQYKQEGNQ 197
Cdd:COG4372 79 EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 198 VQKL--KVQNDNLSKSNDKIESSYAKTNTKLKQTEKEFNDLNNTIKNHSANVAKAETAVNKEKAALNNLERSIDKASSEM 275
Cdd:COG4372 159 LESLqeELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 276 KTFNKEQMIAQSH-FGKLASQADVMSKKFSSIGDKMTSLGRTMTMGVSTPITLGLGAALKTSADFEGQMSRVGAIAQASS 354
Cdd:COG4372 239 LDALELEEDKEELlEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALL 318
|
330 340
....*....|....*....|...
gi 215401158 355 KDLKSMSNQAVDLGAKTSKSANE 377
Cdd:COG4372 319 AALLELAKKLELALAILLAELAD 341
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
908-1200 |
1.60e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 908 SKETEKAlEKYVHYSEENSRIMEKVRLNSGQISEdkaKKLLKIETDlsnnlIAEIEKrnkkELEKTQELIDKYSAFDEQE 987
Cdd:TIGR02169 204 RREREKA-ERYQALLKEKREYEGYELLKEKEALE---RQKEAIERQ-----LASLEE----ELEKLTEEISELEKRLEEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 988 KQNILTRTKEKNDLRIKKEQELNQKIKELK-EKALSDGQISENERkEIEKLENQRRdITVKELSKTEKEQERILVRMQR- 1065
Cdd:TIGR02169 271 EQLLEELNKKIKDLGEEEQLRVKEKIGELEaEIASLERSIAEKER-ELEDAEERLA-KLEAEIDKLLAEIEELEREIEEe 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1066 NRNAYSIDEASKAIKEAEKARKARKKEVD----------KQYEDDVIAIKNNVNLSKSEKDKLLAIADQRH------KDE 1129
Cdd:TIGR02169 349 RKRRDKLTEEYAELKEELEDLRAELEEVDkefaetrdelKDYREKLEKLKREINELKRELDRLQEELQRLSeeladlNAA 428
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 215401158 1130 VRKAKSKKDAVVDVVKKQNKDIDK-EMDLSSGRVYKNTEkwwnglKSWWSNFREDQKKKSDKYAKEQEETAR 1200
Cdd:TIGR02169 429 IAGIEAKINELEEEKEDKALEIKKqEWKLEQLAADLSKY------EQELYDLKEEYDRVEKELSKLQRELAE 494
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1-281 |
2.15e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.80 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1 MNEKVEGMTLELKLDHLGVQEGM---KGLKRQLGV-------VNSEMKANLSAFDKSEKS----MEKYQARIKGLNDRLK 66
Cdd:pfam05483 287 LIEKKDHLTKELEDIKMSLQRSMstqKALEEDLQIatkticqLTEEKEAQMEELNKAKAAhsfvVTEFEATTCSLEELLR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 67 VQKKMYSQVEDELKQVNANYQKAKSSV---------KDVEKAYLKLVEANKK----EKLALDKSKEALKSSNTEL----- 128
Cdd:pfam05483 367 TEQQRLEKNEDQLKIITMELQKKSSELeemtkfknnKEVELEELKKILAEDEklldEKKQFEKIAEELKGKEQELifllq 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 129 ------KKAENQYKRTNQRKQDAYQKLKQLRDAEQKLKNSNQATTAQLKRASDAVQKQSAKHKALVEQYKQEGNQVQKLK 202
Cdd:pfam05483 447 arekeiHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCK 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 203 VQNDNLSKSNDKIESSYAKTNTKLKQTEKEFNDLNNTIK-----------NHSANVAKAETAVNKEKAALNNLERSIDKA 271
Cdd:pfam05483 527 KQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKckldkseenarSIEYEVLKKEKQMKILENKCNNLKKQIENK 606
|
330
....*....|
gi 215401158 272 SSEMKTFNKE 281
Cdd:pfam05483 607 NKNIEELHQE 616
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
19-275 |
2.35e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 19 VQEGMKGLKRQLGVVNSEMKANLSAFDKSE--KSMEKYQARIKGLNDRLKVQKKMYSQV--EDELKQVNANyQKAKSSVK 94
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEelKKAEEEKKKVEQLKKKEAEEKKKAEELkkAEEENKIKAA-EEAKKAEE 1672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 95 DVEKAylklvEANKKEKLALDKSKEALKSSNTELKKAENQYKRTNQRKQDAyqklKQLRDAEQKlknsNQATTAQLKRAS 174
Cdd:PTZ00121 1673 DKKKA-----EEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA----EELKKAEEE----NKIKAEEAKKEA 1739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 175 DAVQKQSAKHKalVEQykQEGNQVQKLKVQNDNLSKSNDKIESSYAKTNTKlKQTEKEFNDLNNTIKNHSANVAKAETAV 254
Cdd:PTZ00121 1740 EEDKKKAEEAK--KDE--EEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD-EEDEKRRMEVDKKIKDIFDNFANIIEGG 1814
|
250 260
....*....|....*....|.
gi 215401158 255 NKEKAALNNLERSIDKASSEM 275
Cdd:PTZ00121 1815 KEGNLVINDSKEMEDSAIKEV 1835
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1-266 |
2.91e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.83 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1 MNEKVEGMTLELKLDHLGVQEGMKGLKRQLGVVNSEMKANLSAFDKSEKSMEKYQARIKGLNDRLKVQKKMYSQVEDELK 80
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 81 QVNANYQKAKSSVKDVEKAylklVEANKKEKLALDKSKEALKSSNTELKKAENQYKRT-NQRKQDAYQKLKQLRDAEQKL 159
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEE----LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQiAELQSEIAEREEELKELEEQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 160 kNSNQATTAQLKRASDAVQKQSAKHKalVEQYKQEGNQVQKLKVQNDNLSKSNDKIESSYAKTNTKLKQTEKEFNDLNNT 239
Cdd:COG4372 160 -ESLQEELAALEQELQALSEAEAEQA--LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALS 236
|
250 260
....*....|....*....|....*..
gi 215401158 240 IKNHSANVAKAETAVNKEKAALNNLER 266
Cdd:COG4372 237 ALLDALELEEDKEELLEEVILKEIEEL 263
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
50-316 |
3.28e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.33 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 50 SMEKYQARIKGLNDRLKVQKKMYSQVEDELKQVNANYQKAKSSVKDVEKAYLKLVEANKKEKLALDKSKEALKSSNTELK 129
Cdd:TIGR04523 205 NLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIK 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 130 KAENQYKR--------TNQRKQDAYQKLK-QLRDAEQKLKNsnqattaqlkrasdaVQKQSAKHKALVEQYKQegnQVQK 200
Cdd:TIGR04523 285 ELEKQLNQlkseisdlNNQKEQDWNKELKsELKNQEKKLEE---------------IQNQISQNNKIISQLNE---QISQ 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 201 LKVQNDNLSKSNDKIESSYAKTNTKLKQTEKEFNDLNNTIKNHSANVAKAETAVNKEKAALNNLERSIDKASSEMKTFNK 280
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
250 260 270
....*....|....*....|....*....|....*.
gi 215401158 281 EQMIAQSHFGKLASQADVMSKKFSSIGDKMTSLGRT 316
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNT 462
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
922-1118 |
3.86e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.03 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 922 SEENSRIMEKVRLnsgqisedKAKKLLKIETDLSNNLIAEIEKRNK--KELEKTQELIDKYSAfDEQEKQNILTRTKEKN 999
Cdd:pfam05483 571 SEENARSIEYEVL--------KKEKQMKILENKCNNLKKQIENKNKniEELHQENKALKKKGS-AENKQLNAYEIKVNKL 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1000 DLRIKKEQELNQKIKELKEKALSDGQIS-ENERKEIEKLEnqrrdITVKELSKTEKE-----QERI---LVRMQRNRNAY 1070
Cdd:pfam05483 642 ELELASAKQKFEEIIDNYQKEIEDKKISeEKLLEEVEKAK-----AIADEAVKLQKEidkrcQHKIaemVALMEKHKHQY 716
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 215401158 1071 S--IDEASKAI-----KEAEKARKARKKEVD-KQYEDDVIAIKNNVNLSKSEKDKL 1118
Cdd:pfam05483 717 DkiIEERDSELglyknKEQEQSSAKAALEIElSNIKAELLSLKKQLEIEKEEKEKL 772
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
893-1168 |
4.38e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.03 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 893 SKKASDTVKVLGKGVSKETEkaLEKYVHYSEENSRIMEKVRLNSGQISEDKAKKLLKIETDLSNN--LIAEIEKRN---- 966
Cdd:pfam05483 81 SKLYKEAEKIKKWKVSIEAE--LKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENkdLIKENNATRhlcn 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 967 --KKELEKTQELIDKYSAFDEQEKQ-------NILTRTKEKNDLRIKKEQ---ELNQKIKELKEKAlsdGQISENERKEI 1034
Cdd:pfam05483 159 llKETCARSAEKTKKYEYEREETRQvymdlnnNIEKMILAFEELRVQAENarlEMHFKLKEDHEKI---QHLEEEYKKEI 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1035 EKLENQRRDITVKELSKTEKEQERILVRMQRNRNAYSIDEASKAIKEAEKARKARKKEVDKQYEDDVIAIKNNVNLSKSE 1114
Cdd:pfam05483 236 NDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKAL 315
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 215401158 1115 KDKL---------LAIADQRHKDEVRKAKSKKDAVVDVVKKQNKDIDKEMDLSSGRVYKNTEK 1168
Cdd:pfam05483 316 EEDLqiatkticqLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQ 378
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
941-1204 |
4.51e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 941 EDKAKKLLKIETDLsNNLIAEIEKRNKKElEKTQELIDKysafDEQEKQNILTRTKEKNDLRIKKEQELNQKIKELKEka 1020
Cdd:PRK03918 161 ENAYKNLGEVIKEI-KRRIERLEKFIKRT-ENIEELIKE----KEKELEEVLREINEISSELPELREELEKLEKEVKE-- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1021 lsdgqiSENERKEIEKLEnqrrditvKELSKTEKEQERILVRMQRNRNaySIDEASKAIKEAEKARKARK--KEVDKQYE 1098
Cdd:PRK03918 233 ------LEELKEEIEELE--------KELESLEGSKRKLEEKIRELEE--RIEELKKEIEELEEKVKELKelKEKAEEYI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1099 dDVIAIKNNVNLSKSEKDKLLAIADQRHKDEVRKAK--SKKDAVVDVVKKQNKDIDKEMDlssgrVYKNTEKWWNGLKSW 1176
Cdd:PRK03918 297 -KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKelEEKEERLEELKKKLKELEKRLE-----ELEERHELYEEAKAK 370
|
250 260 270
....*....|....*....|....*....|..
gi 215401158 1177 WSNFREDQKKKS----DKYAKEQEETARRNRE 1204
Cdd:PRK03918 371 KEELERLKKRLTgltpEKLEKELEELEKAKEE 402
|
|
| Lyz-like |
cd00442 |
lysozyme-like domains; This family contains several members, including soluble lytic ... |
1853-1913 |
5.12e-06 |
|
lysozyme-like domains; This family contains several members, including soluble lytic transglycosylases (SLT), goose egg-white lysozymes (GEWL), hen egg-white lysozymes (HEWL), chitinases, bacteriophage lambda lysozymes, endolysins, autolysins, chitosanases, and pesticin. Typical members are involved in the hydrolysis of beta-1,4- linked polysaccharides.
Pssm-ID: 381596 [Multi-domain] Cd Length: 59 Bit Score: 45.48 E-value: 5.12e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215401158 1853 NIISLIQHESGGNAGItqssalrdiNVLQGNPAKGLLQYIPQTFRHYAVRGHNNIYSGYDQ 1913
Cdd:cd00442 1 VLAAIIGQESGGNKPA---------NAGSGSGAAGLFQFMPGTWKAYGKNSSSDLNDPEAS 52
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
28-277 |
6.82e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 28 RQLGVVNSEMKANLSAFDKSEKSMEKYQARIKGLNDRLKVQKKMYSQVEDELKQVNANYQKAKSSVKDVEKAYLKLVEAn 107
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEL- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 108 KKEKLALDKSKEAL-----------KSSNTELKKAENQYKRTNQRKQDA--YQKLKQLRDAEQKLKNSNQATTAQLKRAS 174
Cdd:PRK03918 244 EKELESLEGSKRKLeekireleeriEELKKEIEELEEKVKELKELKEKAeeYIKLSEFYEEYLDELREIEKRLSRLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 175 DAVQKQSAKHKALVEQYKQEGNQVQKLKVQNDNLSKSNDKIESSYAKTNtKLKQTEKEFNDLN-NTIKNHSANVAKAETA 253
Cdd:PRK03918 324 NGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE-ELERLKKRLTGLTpEKLEKELEELEKAKEE 402
|
250 260
....*....|....*....|....
gi 215401158 254 VNKEKAALNNLERSIDKASSEMKT 277
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKELKK 426
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
24-315 |
7.62e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 7.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 24 KGLKRQLgvvnSEMKANLSAFDKS---EKSMEKYQARIKG-----LNDRLKVQKKMYSQVEDELKQVNANYQKAKSSVKD 95
Cdd:PRK03918 348 KELEKRL----EELEERHELYEEAkakKEELERLKKRLTGltpekLEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 96 VEKAYLKLVEANKK-----EKLALDKSKEALKSSNTELKKAENQYKRTNQRKQDA--------------------YQKLK 150
Cdd:PRK03918 424 LKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLrkelrelekvlkkeseliklKELAE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 151 QLRDAEQKLKNSNQATTAQLKRASDAVQKQSAKHKALVEQYKQEGNQVQKLKVQNDNLSKSNDKIESSYAKTNTKLKQTE 230
Cdd:PRK03918 504 QLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELG 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 231 -KEFNDLNNTIKNHSANVAKAETAVNKEKaALNNLERSIDKASSEMKTFNKEQMIAQSHFGKLASQADVMSKKFS----- 304
Cdd:PRK03918 584 fESVEELEERLKELEPFYNEYLELKDAEK-ELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSeeeye 662
|
330
....*....|.
gi 215401158 305 SIGDKMTSLGR 315
Cdd:PRK03918 663 ELREEYLELSR 673
|
|
| SpoIVFA |
COG5833 |
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, ... |
1707-1797 |
8.18e-06 |
|
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444535 [Multi-domain] Cd Length: 219 Bit Score: 49.22 E-value: 8.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1707 HYGIDFGMPSGTNVYAVKGGIADKVWTDYGGGNSIQIKTGANEWNWYMHLSKQLARQGQRIKAGQLIGKSGATGNfvRGA 1786
Cdd:COG5833 120 GKGVDIETPGGANVKAVKEGYVIFAGKDEETGKTVIIQHADGSESWYGNLSSIDVKLYDFVEAGQKIGTVPATEG--EEG 197
|
90
....*....|.
gi 215401158 1787 HLHFQLMQGSH 1797
Cdd:COG5833 198 TFYFAIKKGGK 208
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
873-1175 |
8.21e-06 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 50.73 E-value: 8.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 873 DLLKVGVNKFKGFMQTMGTASKKASDTVKVLGKGVSKETEKALEKYVHYSEENSRIMEKVRLNSGQisEDKAKKLLKIET 952
Cdd:COG5185 186 LGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQT--SDKLEKLVEQNT 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 953 DLSNNLIAEIEKRNKKELEKTQELIDKYsafdEQEKQNILTRTKEkndlrIKKEQELNQKIKELKEKALSDgQISENERK 1032
Cdd:COG5185 264 DLRLEKLGENAESSKRLNENANNLIKQF----ENTKEKIAEYTKS-----IDIKKATESLEEQLAAAEAEQ-ELEESKRE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1033 EIEKLENQRRDITvKELSKTEKEQERILVRMQRNRNAYSIDEASKAIKEAEKARKARKKEVDKQYEDdvIAIKNNVNLSK 1112
Cdd:COG5185 334 TETGIQNLTAEIE-QGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQN--QRGYAQEILAT 410
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 215401158 1113 SEKDKLLAIAD-QRHKDEVRKAKSKKDAVVDVVKKQNKDIDKEMDLSSGRVYKNTEKWWNGLKS 1175
Cdd:COG5185 411 LEDTLKAADRQiEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINR 474
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
909-1154 |
8.76e-06 |
|
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: 51.12 E-value: 8.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 909 KETEKALEKYVHYSEENSRIMEKVRLNSGQIseDKAKKLLKIETDLSNNLIAEIEKRnKKELEKT-QELIDKYSafDEQE 987
Cdd:TIGR00618 166 KELLMNLFPLDQYTQLALMEFAKKKSLHGKA--ELLTLRSQLLTLCTPCMPDTYHER-KQVLEKElKHLREALQ--QTQQ 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 988 KQNILTRTKEKNDLRIKKEQELNQKIKELKEkalsdgqiSENERKEIEKLE---NQRRDIT-----VKELSKTEKEQERI 1059
Cdd:TIGR00618 241 SHAYLTQKREAQEEQLKKQQLLKQLRARIEE--------LRAQEAVLEETQeriNRARKAAplaahIKAVTQIEQQAQRI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1060 LVRMQRNRN--AYSIDEASKAIKEAEKARKARKKEVDKQYEDDVIAIKNNVNLSksekdkLLAIADQRHKDE--VRKAKS 1135
Cdd:TIGR00618 313 HTELQSKMRsrAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATS------IREISCQQHTLTqhIHTLQQ 386
|
250
....*....|....*....
gi 215401158 1136 KKDAVVDVVKKQNKDIDKE 1154
Cdd:TIGR00618 387 QKTTLTQKLQSLCKELDIL 405
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
41-315 |
9.62e-06 |
|
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: 51.12 E-value: 9.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 41 LSAFDKSEKsmEKYQARIKGLNDRLKVQKKMYSQVEdelkqvNANYQKAKSSVKdvEKAYLKLVEANKKEKLAL---DKS 117
Cdd:TIGR00618 120 ILAAKKSET--EEVIHDLLKLDYKTFTRVVLLPQGE------FAQFLKAKSKEK--KELLMNLFPLDQYTQLALmefAKK 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 118 KEALKSSNTELKKAENQYKRTNQRKQDAYQK-------LKQLRDAEQKLknsnQATTAQLKRASDAVQKQSAKHKALVEQ 190
Cdd:TIGR00618 190 KSLHGKAELLTLRSQLLTLCTPCMPDTYHERkqvlekeLKHLREALQQT----QQSHAYLTQKREAQEEQLKKQQLLKQL 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 191 YKQEgnqvQKLKVQNDNLSKSNDKIESS-----YAKTNTKLKQTEKEFNDLNNTIKN----------HSANVAKAETAVN 255
Cdd:TIGR00618 266 RARI----EELRAQEAVLEETQERINRArkaapLAAHIKAVTQIEQQAQRIHTELQSkmrsrakllmKRAAHVKQQSSIE 341
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 215401158 256 KEKAALNNL-------ERSIDKASSEMKTFNKEQMIAQsHFGKLASQADVMSKKFSSIGDKMTSLGR 315
Cdd:TIGR00618 342 EQRRLLQTLhsqeihiRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKTTLTQKLQSLCKELDILQR 407
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
45-281 |
9.98e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.79 E-value: 9.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 45 DKSEKSMEKYQARIKGLNDRLKVQKKMYSQVEDELKQVNANYQKAKSSVKDVEKAYLKLVEanKKEKLALDKSK--EALK 122
Cdd:TIGR04523 464 ESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKE--KIEKLESEKKEkeSKIS 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 123 SSNTELKKAENQYKRTNQRKQ-DAYQK-LKQLRDAEQKLKNSNqattaqlKRASDAVQKQSAKHKALVEQYKQEGNQVQK 200
Cdd:TIGR04523 542 DLEDELNKDDFELKKENLEKEiDEKNKeIEELKQTQKSLKKKQ-------EEKQELIDQKEKEKKDLIKEIEEKEKKISS 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 201 LKVQNDNLSKSN-------DKIESSYAKTNTKLKQTEKEFndlnNTIKNHSAN-VAKAETAVNKekaalnnlersIDKAS 272
Cdd:TIGR04523 615 LEKELEKAKKENeklssiiKNIKSKKNKLKQEVKQIKETI----KEIRNKWPEiIKKIKESKTK-----------IDDII 679
|
....*....
gi 215401158 273 SEMKTFNKE 281
Cdd:TIGR04523 680 ELMKDWLKE 688
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
901-1057 |
1.00e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 50.89 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 901 KVLGKGVSKETEKALEKYVH-YSEENSRIMEKVRLNS-----------GQISEDKAKKLLK-----------------IE 951
Cdd:pfam17380 419 KVEMEQIRAEQEEARQREVRrLEEERAREMERVRLEEqerqqqverlrQQEEERKRKKLELekekrdrkraeeqrrkiLE 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 952 TDLSNNLIAEIEKRNK-KELEKtqELIDKYSAFDEQEKqniltRTKEKNDLRIKKEQELNQKIKELKEKAlsdgqisENE 1030
Cdd:pfam17380 499 KELEERKQAMIEEERKrKLLEK--EMEERQKAIYEEER-----RREAEEERRKQQEMEERRRIQEQMRKA-------TEE 564
|
170 180
....*....|....*....|....*...
gi 215401158 1031 RKEIEKLENQRRDI-TVKELSKTEKEQE 1057
Cdd:pfam17380 565 RSRLEAMEREREMMrQIVESEKARAEYE 592
|
|
| PRK06148 |
PRK06148 |
hypothetical protein; Provisional |
1706-1792 |
1.15e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 180426 [Multi-domain] Cd Length: 1013 Bit Score: 50.79 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1706 RHYGIDFGMPSGTNVYAvkgGIADKVWT--------DYGGGNSIQIKT--GANEWNWYMHLSKQ-LAR--QGQRIKAGQL 1772
Cdd:PRK06148 440 VHLGVDLFAPAGTPVYA---PLAGTVRSveieavplGYGGLVALEHETpgGDPFYTLYGHLAHEaVSRlkPGDRLAAGEL 516
|
90 100
....*....|....*....|.
gi 215401158 1773 IGKSGATG-NFVRGAHLHFQL 1792
Cdd:PRK06148 517 FGAMGDAHeNGGWAPHLHFQL 537
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
27-281 |
1.21e-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: 50.82 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 27 KRQLGVVNSEMKANLsaFDKSEKSMEKYQARIKGLNDRLKVQKKMYSQVEDELKQVNANYQKAKSSVKDV---EKAYLKL 103
Cdd:TIGR00606 724 RRDEMLGLAPGRQSI--IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVtimERFQMEL 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 104 VEANKKeklaldKSKEALKSSNTELKKAENQYKRTNQRKQDAYQK-------LKQLRDAEQKLKNSNQATTAQLKRASDA 176
Cdd:TIGR00606 802 KDVERK------IAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTvvskielNRKLIQDQQEQIQHLKSKTNELKSEKLQ 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 177 VQKQSAKHKALVEQYKQEGNQVQKL---------KVQNDNLSKSNDKIESSY--AKTNTKLKQTEKEFNDLNNTIKN--- 242
Cdd:TIGR00606 876 IGTNLQRRQQFEEQLVELSTEVQSLireikdakeQDSPLETFLEKDQQEKEEliSSKETSNKKAQDKVNDIKEKVKNihg 955
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 215401158 243 HSANVAK------------AETAVNKEKAALNNLERSIDKASSEMKTFNKE 281
Cdd:TIGR00606 956 YMKDIENkiqdgkddylkqKETELNTVNAQLEECEKHQEKINEDMRLMRQD 1006
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
923-1139 |
1.23e-05 |
|
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: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 923 EENSRIMEKVRLNSGQISEDKAKKLLKIETDLSNNLIAEIEKRNKKELEKTQELIDKYSAFDEQEKQ--NILTRTKEKND 1000
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAllEAEAELAEAEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1001 LRIKKEQELNQKIKELKEKALSDGQISENERKEIEKLENQRRDITVKELSKTEKEQERILVRMQRNRNAYSIDEASKAIK 1080
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1081 EAEKARKARKKEvDKQYEDDVIAIKNNVNLSKSEKDKLLAIADQR-HKDEVRKAKSKKDA 1139
Cdd:COG1196 460 ALLELLAELLEE-AALLEAALAELLEELAEAAARLLLLLEAEADYeGFLEGVKAALLLAG 518
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
26-230 |
1.31e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 26 LKRQLGvvnsEMKANLsafDKSEKSMEKYQAR--IKGLNDRLKVQKKMYSQVEDELKQVNANYQKAKSSVKDVEKAylkl 103
Cdd:COG3206 180 LEEQLP----ELRKEL---EEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQ---- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 104 vEANKKEKLALDKSKEALKSSNTELKKAENQYKRTNQRKQDAYQKLKQLR----DAEQKLKNSNQATTAQLKRASDAVQK 179
Cdd:COG3206 249 -LGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRaqiaALRAQLQQEAQRILASLEAELEALQA 327
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 215401158 180 QSAKHKALVEQYKQEGNQVQKLKVQNDNLSKSNDKIESSYAKTNTKLKQTE 230
Cdd:COG3206 328 REASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
941-1153 |
1.59e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.02 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 941 EDKAKKLLKIETDLSNN---------LIAEIEK----------RNKKELEKTQELIDKYSAFDEQEKQNILTRTKEKNDL 1001
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNnkiisqlneQISQLKKeltnsesensEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1002 RIK------KEQELNQKIKEL-KEKALSDGQIS------ENERKEIEKLENQ--RRDITVKELSKTEKEQERIL--VRMQ 1064
Cdd:TIGR04523 397 ESKiqnqekLNQQKDEQIKKLqQEKELLEKEIErlketiIKNNSEIKDLTNQdsVKELIIKNLDNTRESLETQLkvLSRS 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1065 RNRNAYSIDEASKAIKEAEKARKARKKEVdKQYEDDVIAIKNNVNLSKSEKDKLLAIADQRH------KDEVRKAKS--K 1136
Cdd:TIGR04523 477 INKIKQNLEQKQKELKSKEKELKKLNEEK-KELEEKVKDLTKKISSLKEKIEKLESEKKEKEskisdlEDELNKDDFelK 555
|
250
....*....|....*..
gi 215401158 1137 KDAVVDVVKKQNKDIDK 1153
Cdd:TIGR04523 556 KENLEKEIDEKNKEIEE 572
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
41-281 |
1.70e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.01 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 41 LSAFDKSEKSmekyqaRIKGLNDRLKVQKKMYSQVEDELK--QVNANYQKAKSS--VKDVEKAYLKLVEANKKEKLALDK 116
Cdd:PHA02562 165 LSEMDKLNKD------KIRELNQQIQTLDMKIDHIQQQIKtyNKNIEEQRKKNGenIARKQNKYDELVEEAKTIKAEIEE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 117 SKEALKSSNTELKKAENQYKRTNQRKQDAYQKLKQLrDAEQKLKNSNQ---ATTAQLKRASDAVQKQSAKHKALVEQYKQ 193
Cdd:PHA02562 239 LTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQF-QKVIKMYEKGGvcpTCTQQISEGPDRITKIKDKLKELQHSLEK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 194 EGNQVQKLKVQNDnlsksndkiessyaktntKLKQTEKEFNDLNNTIKNHSANVAKAETAVNKEKAALNNLERSIDKASS 273
Cdd:PHA02562 318 LDTAIDELEEIMD------------------EFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAE 379
|
....*...
gi 215401158 274 EMKTFNKE 281
Cdd:PHA02562 380 ELAKLQDE 387
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
11-213 |
1.71e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 11 ELKLDHLGVQEGMKGLKRQLGVVNSEMKANLSAFDKSEKSMEKYQARIKGLNDRLKVQKKMYSQVEDEL-KQVNANYQKA 89
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALyRLGRQPPLAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 90 KSSVKDVEKA-----YLKLVEANKKEKLaldkskEALKSSNTELKKAENQYKRTNQRKQDAYQKLKQLRDAEQKLKNSNQ 164
Cdd:COG4942 125 LLSPEDFLDAvrrlqYLKYLAPARREQA------EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQ 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 215401158 165 ATTAQLKRASDAVQKQSAKHKALVEQYKQEGNQVQKLKVQNDNLSKSND 213
Cdd:COG4942 199 KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
42-231 |
1.84e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 42 SAFDKSEKSMEKYQArikglnDRLKVQKKmySQVEDELKQVNANYQKAKSSVKDVEKAYLKLVEANKKEklALDKSKEAL 121
Cdd:PTZ00121 1354 AAADEAEAAEEKAEA------AEKKKEEA--KKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAA--AAKKKADEA 1423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 122 KSSNTELKKAENQYKRTNQRKQ--DAYQKLKQLRDAEQKLKNSNQATTAQ--LKRASDAVQKQSAKHKAlvEQYKQEGNQ 197
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEEAKKadEAKKKAEEAKKAEEAKKKAEEAKKADeaKKKAEEAKKADEAKKKA--EEAKKKADE 1501
|
170 180 190
....*....|....*....|....*....|....
gi 215401158 198 VQKlkvQNDNLSKSNDKIESSYAKTNTKLKQTEK 231
Cdd:PTZ00121 1502 AKK---AAEAKKKADEAKKAEEAKKADEAKKAEE 1532
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
87-276 |
1.89e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 87 QKAKSSVKDVEKAYLKLVEANKKEKLALDKSKEALKSSNTELKKAENQYKRTNQRKQDAYQKLKQLRDAEQKLKNSNQAT 166
Cdd:PTZ00121 1230 KKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKK 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 167 TAQLKRASDAVQKQSAKHKALVEQYKQEGNQVQKL-KVQNDNLSKSNDKIESSYAKTNTKLKQTEKEfNDLNNTIKNHSA 245
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAaEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA-KKKADAAKKKAE 1388
|
170 180 190
....*....|....*....|....*....|.
gi 215401158 246 NVAKAETAVNKEKAALNNLERsIDKASSEMK 276
Cdd:PTZ00121 1389 EKKKADEAKKKAEEDKKKADE-LKKAAAAKK 1418
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
910-1094 |
2.25e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.79 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 910 ETEKA-LEKYVHYSEENSRIMEKvRLNSGQISEDKAKKllKIETDLSN-NLIAEIEKRNKKELE-KTQELIDKYSAFDEQ 986
Cdd:pfam01576 495 EDERNsLQEQLEEEEEAKRNVER-QLSTLQAQLSDMKK--KLEEDAGTlEALEEGKKRLQRELEaLTQQLEEKAAAYDKL 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 987 EKQNilTRTK-EKNDLRI-------------KKEQELNQKIKElkEKALSDGQISENERKEIEKLENQRRDITV----KE 1048
Cdd:pfam01576 572 EKTK--NRLQqELDDLLVdldhqrqlvsnleKKQKKFDQMLAE--EKAISARYAEERDRAEAEAREKETRALSLaralEE 647
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 215401158 1049 LSKTEKEQERI--LVRMQRNRNAYSIDEASKAIKEAEKARKARKKEVD 1094
Cdd:pfam01576 648 ALEAKEELERTnkQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVE 695
|
|
| COG5412 |
COG5412 |
Phage-related protein [Mobilome: prophages, transposons]; |
248-867 |
2.69e-05 |
|
Phage-related protein [Mobilome: prophages, transposons];
Pssm-ID: 444167 [Multi-domain] Cd Length: 704 Bit Score: 49.31 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 248 AKAETAVNKEKAALNNLERSIDKASSEMKTFNKEQMIAQSHF----GKLASQADVMSKKFSSIGDKMTSLGRTMTMGVST 323
Cdd:COG5412 4 ADASAKEAASAALLLAQAKAADSELTAASGGVVSAAAKAQGSiaqlGKIGAAAGAEAALADSSLAFATLAAALGATVAGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 324 PITLGLGAALKTSADFEGQMSRVGAIAQASSKDLKSMSNQAVDLGAKTSKSANEVAKGMEELAALGFNAKQTME--AMPG 401
Cdd:COG5412 84 SLLLAAGGARAKGSAAAAAALGAVAAAAKVLNGALAAAGAALAATQALAAAATGAKGEANAAAKAGGAAALASAglAAAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 402 VISAAEASGAEMATTATVMASAINSFGLKASDANHVADLLArSANDSAADIQYMGDALKyAGTPAKALGVSIEDTSAAIE 481
Cdd:COG5412 164 AAAAASALAAAGAIAKAILSASKLSGQALAGQSAAAGGALE-AAAAAAAGAAAAGAAAA-AATAASALLALAALQGLAAG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 482 VLSNSGLEGSQAGTALRASFIRLANPSKNTAKEMKKLGIH-LSDAKGQFVGMGELIRQFQDNMKGMTREQKLAT-VATIV 559
Cdd:COG5412 242 AATGAAAGAAGAAGLGAAGAGAGQAAALLGLVAGAEASGGtAGGAVAGLAAGLAAAAGASANLGAAAAASFGASlAASAG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 560 GTEAASGFLALIEAGPDKINSYSKSLKNSNGESKKAADLMKDNL--KGALEQLGGAFESLAIEVG---KDLTPMIRAG-- 632
Cdd:COG5412 322 VDTAAAALAAAEAIADGSLVAGLGSAGTVLSTLSGAVGGLEGAIgqLGAAGGLGSALGGLTGPIGiviAAIAALIAAFva 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 633 ----AEGLTKLVDG---FTHLPGWVRKASVGLALF---------------GAAIGPAVLAGGLLIRTVGSAAKGYASLNR 690
Cdd:COG5412 402 lwknSETFRNLVQGvweLNAIKTAIEGVVSAIVTFisalweaikalltaiGGALPQLIAAVWNGIVQFISAIITNLPLIL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 691 RIAENTILS------NTNSKAMKSL-----GLQTLFLGSTTGKTSK----GFKGLAGAMMFNLKPI-NVLKNSAKLAILP 754
Cdd:COG5412 482 QAALQLIKAlikglwTAIKGVIQGAieiitGIIQFITALLTGDWSGiiweGIKQLVSGIVEIIPNIvAAVPQGGIAALWD 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 755 -----FKLLKNGLGLAAKSLFavSGGARFAGVALRFLTGPIGATITAITIAYKVFKTAYDR----VEWFRNGINGLGETI 825
Cdd:COG5412 562 aikgfFPGLIEAIVQLVSNII--NAIISIISSILNAAGSIISSIWNAIKSAVSSIISAKSIgkniVNGLWNGIKSAAGAV 639
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 215401158 826 KFFGGKIIGGAVRKLGEFKN------YLGSIGKSFKEKFSKDMKDGYK 867
Cdd:COG5412 640 TDKVKDIVGGIVDGIKGALGihspsrKFLEIGKMIVAGLAKGIEDAFS 687
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
948-1234 |
2.95e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 948 LKIETDLSNNLIAEIEKRNKKELEKTQELIDKYSAfDEQEKQNILTRTKEKNDLRIKKEQELNQKIKELKEKALSDGQIS 1027
Cdd:COG4372 18 LRPKTGILIAALSEQLRKALFELDKLQEELEQLRE-ELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1028 ENERKEIEKLENQRRDITvKELSKTEKEQERIlvRMQRNRNAYSIDEASKAIKEAEKARKARKKEVDKQyEDDVIAIKNN 1107
Cdd:COG4372 97 AQAQEELESLQEEAEELQ-EELEELQKERQDL--EQQRKQLEAQIAELQSEIAEREEELKELEEQLESL-QEELAALEQE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1108 VN-----LSKSEKDKLLAIADQRHKDEVRKAKSKKDAVVDVVKKQNKDIDKEMDLSSGRVYKNTEKWWNGLKSWWSNFRE 1182
Cdd:COG4372 173 LQalseaEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELL 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 215401158 1183 DQKKKSDKYAKEQEETARRNRENIKKWFGNAWDGVKSKTGEAFSKMGRNANH 1234
Cdd:COG4372 253 EEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNL 304
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
23-276 |
3.52e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 23 MKGLKRQLGVVNSEMKANLSAFDKSE---KSMEKYQARIKGLNDRLKVQKKMYSQVEDELKQVNANYQKAKSSVKDVEKA 99
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEekkKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEA 1341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 100 YLKLVEANKKEKLALDKSKEALKSSNTELKKAENQYKRTNQRKQDAYQKlkqlRDAEQKLKNSNQATtaqlKRASDAVQK 179
Cdd:PTZ00121 1342 KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK----KKADEAKKKAEEDK----KKADELKKA 1413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 180 QSAKHKAlvEQYKQEGNQVQK---LKVQNDNLSKSND---KIESSYAKTNTKLKQTEKEFNDlnnTIKNHSANVAKAETA 253
Cdd:PTZ00121 1414 AAAKKKA--DEAKKKAEEKKKadeAKKKAEEAKKADEakkKAEEAKKAEEAKKKAEEAKKAD---EAKKKAEEAKKADEA 1488
|
250 260
....*....|....*....|...
gi 215401158 254 VNKEKAALNNLERSIDKASSEMK 276
Cdd:PTZ00121 1489 KKKAEEAKKKADEAKKAAEAKKK 1511
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
35-283 |
4.03e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 35 SEMKANLSAFDKSEKSME----KYQARIKGLNDRLKVQKKMYSQVEDELKQVNANYQKAKSS------VKDVEKAYLKLV 104
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKadaaKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAkkkaeeKKKADEAKKKAE 1441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 105 EANKKEKLAlDKSKEALKSSNT-----------ELKKAENQYKRTNQRK---QDAYQKLKQLRDAEQKLKNSNQATTAQL 170
Cdd:PTZ00121 1442 EAKKADEAK-KKAEEAKKAEEAkkkaeeakkadEAKKKAEEAKKADEAKkkaEEAKKKADEAKKAAEAKKKADEAKKAEE 1520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 171 KRASDAVQKQSAKHKALVEQYKQEGNQVQKLKvQNDNLSKSNDKiessyaktnTKLKQTEKEFNDLNNTIKnhsanvaKA 250
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADEAKKAEEKKKADELK-KAEELKKAEEK---------KKAEEAKKAEEDKNMALR-------KA 1583
|
250 260 270
....*....|....*....|....*....|...
gi 215401158 251 ETAVNKEKAALnnleRSIDKASSEMKTFNKEQM 283
Cdd:PTZ00121 1584 EEAKKAEEARI----EEVMKLYEEEKKMKAEEA 1612
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
19-313 |
5.65e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.51 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 19 VQEGMKGLKRQLGVVNSEMkanlsafDKSEKSMEKyqarIKGLNDRLKVQKKMYSQVEDelKQVNANYQKAKSSvkdveK 98
Cdd:TIGR01612 1367 VKEYTKEIEENNKNIKDEL-------DKSEKLIKK----IKDDINLEECKSKIESTLDD--KDIDECIKKIKEL-----K 1428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 99 AYLKLVEANKKE--KLALDKSKE-ALKSSNTELKKAENQYKRTNQRKQDAYQKLKQLRDAEQKLKNSNQAttaqlKRASD 175
Cdd:TIGR01612 1429 NHILSEESNIDTyfKNADENNENvLLLFKNIEMADNKSQHILKIKKDNATNDHDFNINELKEHIDKSKGC-----KDEAD 1503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 176 AVQKQSAKHKALVEQYKQEG----NQVQKLKVQNDNLSKSND------KIESSYAKTNTKLKQTEKEFNDLNN---TIKN 242
Cdd:TIGR01612 1504 KNAKAIEKNKELFEQYKKDVtellNKYSALAIKNKFAKTKKDseiiikEIKDAHKKFILEAEKSEQKIKEIKKekfRIED 1583
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 215401158 243 HSANVAKAETAVNKEKAALNNLERSIDKASSEMKTFNKEQMIAQSHFGKLAS-QADVMSKKFSSIGDKMTSL 313
Cdd:TIGR01612 1584 DAAKNDKSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETESIEKKISSfSIDSQDTELKENGDNLNSL 1655
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
21-306 |
5.71e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 21 EGMKGLKRQLGVVNSEmkanlsafdKSEKSMEKYQarikGLNDRLKVQKKMYSQVEDELKQVNANYQKAKSSVKDVEKAY 100
Cdd:PRK03918 503 EQLKELEEKLKKYNLE---------ELEKKAEEYE----KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELE 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 101 LKLVEANKKEKLALDKSKEALKSSNTELKKAENQYKRTNQRKQDAYQKLKQLRDAEQKLKnsnqATTAQLKRASDAVQKQ 180
Cdd:PRK03918 570 EELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELD----KAFEELAETEKRLEEL 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 181 SAKHKALVEQYKQEgnqvqklkvQNDNLSKSNDKIESSYAKTNTKLKQTEKEFNDLNNTIKNHSANVAKAETA---VNKE 257
Cdd:PRK03918 646 RKELEELEKKYSEE---------EYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAkkeLEKL 716
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 215401158 258 KAALNNLERSIDKAsSEMKTFNKEQmiAQSHFGKLASQ--ADVMSKKFSSI 306
Cdd:PRK03918 717 EKALERVEELREKV-KKYKALLKER--ALSKVGEIASEifEELTEGKYSGV 764
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
3-282 |
5.78e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.43 E-value: 5.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 3 EKVEGMTLELKLDHLgvQEGMKGLKRQLGVVNSEMKANLSAFDKSEKSMEKYQARIKGLNDRLKVQKKMYSQVEDELKQV 82
Cdd:pfam02463 221 LEEEYLLYLDYLKLN--EERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEEL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 83 NANYQKAKSSVKDVEKAYLKLVEANKKEKLALDKSKEALKSSNTELKKAENQYKRTNQRKQDAYQKLKQLRDAEQKLKNS 162
Cdd:pfam02463 299 KSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAK 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 163 NQATTAQLKRAsdavqkqsakhKALVEQYKQEGNQVQKLKVQNDNLSKSNDKIESSYAKTNTKLKQTEKEFNDLNNtikn 242
Cdd:pfam02463 379 KKLESERLSSA-----------AKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ---- 443
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 215401158 243 hsANVAKAETAVNKEKAALNNLERSIDKASSEMKTFNKEQ 282
Cdd:pfam02463 444 --GKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVK 481
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
48-145 |
6.21e-05 |
|
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras
Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 47.73 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 48 EKSMEKYQARIKGLNDRLKVQKKMYsqveDELKQVNANYQKAKSSV-KDVEKAYLKlVEANKKEKLALDKSKEALKSSNT 126
Cdd:smart00435 276 EKSMEKLQEKIKALKYQLKRLKKMI----LLFEMISDLKRKLKSKFeRDNEKLDAE-VKEKKKEKKKEEKKKKQIERLEE 350
|
90
....*....|....*....
gi 215401158 127 ELKKAENQYKRTNQRKQDA 145
Cdd:smart00435 351 RIEKLEVQATDKEENKTVA 369
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
844-1197 |
6.68e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.51 E-value: 6.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 844 KNYLGSIGKSFKEK--------FSKDMKDGYKSLSDDDLLKVGVNKFKGFMQTMGTASKKasdtvKVLGKGVSKETEKAL 915
Cdd:TIGR01612 423 NNFHKTIERLIFEKpdpnnnniFKDDFDEFNKPIPKSKLKALEKRFFEIFEEEWGSYDIK-----KDIDENSKQDNTVKL 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 916 ekYVHYSEENSRIMEKVRLNSGQISEDKAKKLLKIETDLSNNLIAEIEKrnkkELEKTQELIDKYsafdEQEKQNILTRT 995
Cdd:TIGR01612 498 --ILMRMKDFKDIIDFMELYKPDEVPSKNIIGFDIDQNIKAKLYKEIEA----GLKESYELAKNW----KKLIHEIKKEL 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 996 KEKNDLRIKKEQElnqkIKELKEKALSdgQISENERKEIEKLENQRRditVKELS-KTEKEQERI-LVRMQRNRNAYsID 1073
Cdd:TIGR01612 568 EEENEDSIHLEKE----IKDLFDKYLE--IDDEIIYINKLKLELKEK---IKNISdKNEYIKKAIdLKKIIENNNAY-ID 637
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1074 EASKA--------IKEAEKARKARKKEVDKQYEDDVIAIKNNVNLSKSEKDkllaIADQRHKDEVRKAKSKKDAVVDvvK 1145
Cdd:TIGR01612 638 ELAKIspyqvpehLKNKDKIYSTIKSELSKIYEDDIDALYNELSSIVKENA----IDNTEDKAKLDDLKSKIDKEYD--K 711
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 215401158 1146 KQNKDIDK-EMDLSSGRVYKN--------TEKWWNG-----LKSWWSNFREDQKKKSDK---YAKEQEE 1197
Cdd:TIGR01612 712 IQNMETATvELHLSNIENKKNelldiiveIKKHIHGeinkdLNKILEDFKNKEKELSNKindYAKEKDE 780
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
917-1392 |
7.15e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.12 E-value: 7.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 917 KYVHYSEENSRIMEKVRLNSGQISEDKAKKLLKIETDLSNNLIAEIEKrNKKELEKTQELIDKY--------SAFDEQEK 988
Cdd:TIGR01612 1457 KNIEMADNKSQHILKIKKDNATNDHDFNINELKEHIDKSKGCKDEADK-NAKAIEKNKELFEQYkkdvtellNKYSALAI 1535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 989 QNILTRTKEKNDLRIKKeqelnqkIKELKEKALSDGQISENERKEI----------------------------EKLENQ 1040
Cdd:TIGR01612 1536 KNKFAKTKKDSEIIIKE-------IKDAHKKFILEAEKSEQKIKEIkkekfrieddaakndksnkaaidiqlslENFENK 1608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1041 RRDIT---------VKELSKTEKEQERILVRMQRNR------NAYSIDEASKAIKEAEKARKARKKEVD------KQYED 1099
Cdd:TIGR01612 1609 FLKISdikkkindcLKETESIEKKISSFSIDSQDTElkengdNLNSLQEFLESLKDQKKNIEDKKKELDeldseiEKIEI 1688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1100 DVIAIKNNVNLSKSEKDKLLAIADqrhKDEVRKAK-SKKDAVVDVVKKQNKD----IDKEMDLSS-----GRVYKNTEKW 1169
Cdd:TIGR01612 1689 DVDQHKKNYEIGIIEKIKEIAIAN---KEEIESIKeLIEPTIENLISSFNTNdlegIDPNEKLEEynteiGDIYEEFIEL 1765
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1170 WNGLkswwSNFREDQKKKSDKYakEQEETARRNREN-------IKKWFGNAWDGVKSKtgeafsKMGRNANHFggemkkm 1242
Cdd:TIGR01612 1766 YNII----AGCLETVSKEPITY--DEIKNTRINAQNeflkiieIEKKSKSYLDDIEAK------EFDRIINHF------- 1826
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1243 wsgikgiPSKLSSGWSSAKSSVGYHTKAIANstgkwFGKAWQSVKSTTG-----SIYNQTKQKYSDASDKAWAHSKSiwr 1317
Cdd:TIGR01612 1827 -------KKKLDHVNDKFTKEYSKINEGFDD-----ISKSIENVKNSTDenllfDILNKTKDAYAGIIGKKYYSYKD--- 1891
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 215401158 1318 GTSKWFSNAYKSAKGWLTDMANKSRAK-WDNISSTAWSNAKSVWKGTSKWFSNSYKSlkdwtGDMYSRAHDRFDAI 1392
Cdd:TIGR01612 1892 EAEKIFINISKLANSINIQIQNNSGIDlFDNINIAILSSLDSEKEDTLKFIPSPEKE-----PEIYTKIRDSYDTL 1962
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
56-200 |
7.49e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 7.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 56 ARIKGLNDRLKVQKKMYSQVEDELKQVNANYQKAKSSVKDVEKAYLKLvEANKKEKLA-LDKSKEALKS--SNTELKKAE 132
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRL-ELEIEEVEArIKKYEEQLGNvrNNKEYEALQ 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 215401158 133 NQYKRTNQRKQDAYQKLKQLRDAEQKLKNSNQATTAQLKRASDAVQKQSAKHKALVEQYKQEGNQVQK 200
Cdd:COG1579 96 KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
27-259 |
7.59e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.86 E-value: 7.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 27 KRQLGVVNSEMKANLSAFDKSEKSMEK----YQARIKGLNDRLKVQKKMYSQVEDELKQVNANYQKAKSSVKDVEK--AY 100
Cdd:pfam01576 154 RKLLEERISEFTSNLAEEEEKAKSLSKlknkHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAqiAE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 101 LKLVEANKKEKL--ALDKSKEALKSSNTELKK----------------AENQYK-RTNQRKQDAYQKLKQLR-------- 153
Cdd:pfam01576 234 LRAQLAKKEEELqaALARLEEETAQKNNALKKireleaqiselqedleSERAARnKAEKQRRDLGEELEALKteledtld 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 154 --DAEQKLKNSNQATTAQLKRasdAVQKQSAKHKALVEQYKQEGNQ-VQKLKVQNDNLSKSNDKIEssyaktntKLKQT- 229
Cdd:pfam01576 314 ttAAQQELRSKREQEVTELKK---ALEEETRSHEAQLQEMRQKHTQaLEELTEQLEQAKRNKANLE--------KAKQAl 382
|
250 260 270
....*....|....*....|....*....|
gi 215401158 230 EKEFNDLNNTIKnhSANVAKAETAVNKEKA 259
Cdd:pfam01576 383 ESENAELQAELR--TLQQAKQDSEHKRKKL 410
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
20-281 |
7.65e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.86 E-value: 7.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 20 QEGMKGLKRQLGVVNSEMKANLSAFDKSEKSMEKYQARIKGLNDRLKVQKKMYSQVE---DELKQVNANYQKAKSSVKDv 96
Cdd:pfam01576 804 QAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQqerDELADEIASGASGKSALQD- 882
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 97 EKAYL-----KLVEANKKEKLALDKSKEALKSSNTELKKAENQY---KRTNQRKQDAYQKL-KQLRDAEQKLKNSNQATT 167
Cdd:pfam01576 883 EKRRLeariaQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELaaeRSTSQKSESARQQLeRQNKELKAKLQEMEGTVK 962
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 168 AQLKRASDAVQkqsAKHKALVEQYKQEGNQVQ-----------KLK---VQNDNLSKSNDKIESSYAKTNTKLKQTEKEF 233
Cdd:pfam01576 963 SKFKSSIAALE---AKIAQLEEQLEQESRERQaanklvrrtekKLKevlLQVEDERRHADQYKDQAEKGNSRMKQLKRQL 1039
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 215401158 234 NDlnntiknhsanvakAETAVNKEKAALNNLERSIDKASSEMKTFNKE 281
Cdd:pfam01576 1040 EE--------------AEEEASRANAARRKLQRELDDATESNESMNRE 1073
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
910-1106 |
8.38e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.74 E-value: 8.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 910 ETEKALEKYVHYSEENSRIMEKV--RLNSGQISEDKAKKLLKIETDLSNNLIAEIEKRNKKELEKTQELIDKYSAFDEQE 987
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLaaEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 988 KQNILTRTKeKNDLRIKKeQELNQKIKELKEKALSDGQISEnerKEIEKLENQRrditVKELSKTEKEQERIlvRMQRNR 1067
Cdd:TIGR02168 915 RELEELREK-LAQLELRL-EGLEVRIDNLQERLSEEYSLTL---EEAEALENKI----EDDEEEARRRLKRL--ENKIKE 983
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 215401158 1068 ----NAYSIDEAskaikeaeKARKARKKEVDKQYEDDVIAIKN 1106
Cdd:TIGR02168 984 lgpvNLAAIEEY--------EELKERYDFLTAQKEDLTEAKET 1018
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
940-1095 |
8.94e-05 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 47.56 E-value: 8.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 940 SEDKAKKLLKIETDLSNNLIAEIEKRNKKELEKTQELIDKYSAFDEQEKQNILTRTKEKNDLRIKKEQELNQKIKEL--K 1017
Cdd:PRK00106 51 AERDAEHIKKTAKRESKALKKELLLEAKEEARKYREEIEQEFKSERQELKQIESRLTERATSLDRKDENLSSKEKTLesK 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 215401158 1018 EKALSDGQISENER-KEIEKLENQRRDITVKELSKTEKEQERILVRMQRNRNAYSIdeASKaIKEAEKARKARKKEVDK 1095
Cdd:PRK00106 131 EQSLTDKSKHIDEReEQVEKLEEQKKAELERVAALSQAEAREIILAETENKLTHEI--ATR-IREAEREVKDRSDKMAK 206
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
9-357 |
9.88e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 47.53 E-value: 9.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 9 TLELKLDHLGVqegmkglkrqlGVVNSEMKanlsafdkSEKSMEKYQARIKGLNDRLKVQKKMYSQVEDELKQ----VNA 84
Cdd:pfam12128 255 SAELRLSHLHF-----------GYKSDETL--------IASRQEERQETSAELNQLLRTLDDQWKEKRDELNGelsaADA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 85 NYQKAKSSVKDVEKAYLKLVEANKkEKLALDKSKEALKSSNTELKKAENQYKRTNQRK-QDAYQKLKQLRDAE------- 156
Cdd:pfam12128 316 AVAKDRSELEALEDQHGAFLDADI-ETAAADQEQLPSWQSELENLEERLKALTGKHQDvTAKYNRRRSKIKEQnnrdiag 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 157 --QKLKNSNQATTAQLKRASDAVQKQSAKHKALVEQYKQEGNQVQKLkvqndnlsksndkIESSYAKTNTKLKQTekefn 234
Cdd:pfam12128 395 ikDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYR-------------LKSRLGELKLRLNQA----- 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 235 dlnntiknhsanVAKAETAVNKEkaalNNLERsIDKASSEMKTFNKEQMIAQSHFGKLASQADVMSKKFSSIGDKM---- 310
Cdd:pfam12128 457 ------------TATPELLLQLE----NFDER-IERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLeerq 519
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 215401158 311 TSLGRTMTMGVSTPITLgLGAALKTSADFEGQMSRVGAIAQASSKDL 357
Cdd:pfam12128 520 SALDELELQLFPQAGTL-LHFLRKEAPDWEQSIGKVISPELLHRTDL 565
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
909-1092 |
1.02e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.84 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 909 KETEKALEKyvhysEENSRIMEKVRLNSGQISEDKAKKL-LKIETDLSNNLIAEIEKRNKKELEKTQELIDKYsAFDEQE 987
Cdd:pfam13868 143 KELEKEEER-----EEDERILEYLKEKAEREEEREAEREeIEEEKEREIARLRAQQEKAQDEKAERDELRAKL-YQEEQE 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 988 KQNiltrtkekndlRIKKEQELNQKIKELKE--KALSDGQISENERKEIEKLENQRRDITVKELSKTEKEQERILVRMQR 1065
Cdd:pfam13868 217 RKE-----------RQKEREEAEKKARQRQElqQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRR 285
|
170 180
....*....|....*....|....*..
gi 215401158 1066 NRNAYSIDEASKAIKEAEKARKARKKE 1092
Cdd:pfam13868 286 MKRLEHRRELEKQIEEREEQRAAEREE 312
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
774-1155 |
1.12e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 774 GGARFAGVALRFLTGPIGATITAItiaykvfktaydRVEWFRNGINGLGETIKFFGgkIIGGAVRkLGEFKNYLGSIGK- 852
Cdd:COG4913 94 PGDTWSAIAATFANDGSGQTVTLA------------QVFWLKGDASSLGDVKRFFV--IADGPLD-LEDFEEFAHGFDIr 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 853 SFKEKFSKDMKDGYKSLSdddllkvgvnKFKG-FMQTMGTASKKASDTvkvLGKGVS------------------KETEK 913
Cdd:COG4913 159 ALKARLKKQGVEFFDSFS----------AYLArLRRRLGIGSEKALRL---LHKTQSfkpigdlddfvreymleePDTFE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 914 ALEKYVHYSEENSRI---MEKVRlnsgqiseDKAKKLLKIETDlsnnliAEIEKRNKKELEKTQELIDKYSAFDEQEKQN 990
Cdd:COG4913 226 AADALVEHFDDLERAheaLEDAR--------EQIELLEPIREL------AERYAAARERLAELEYLRAALRLWFAQRRLE 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 991 ILTRTKEKNDLRIkkeQELNQKIKELKEKAlsdgqisENERKEIEKLENQRRDI---TVKELSKTEKEQERILVRMQRNR 1067
Cdd:COG4913 292 LLEAELEELRAEL---ARLEAELERLEARL-------DALREELDELEAQIRGNggdRLEQLEREIERLERELEERERRR 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1068 NAYsiDEASKAIKEAEKARkarkkevdkqyEDDVIAIKNNVNLSKSEKDKLLAIADQ---RHKDEVRKAKSKKDAV---V 1141
Cdd:COG4913 362 ARL--EALLAALGLPLPAS-----------AEEFAALRAEAAALLEALEEELEALEEalaEAEAALRDLRRELRELeaeI 428
|
410
....*....|....
gi 215401158 1142 DVVKKQNKDIDKEM 1155
Cdd:COG4913 429 ASLERRKSNIPARL 442
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
937-1091 |
1.17e-04 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 44.26 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 937 GQISEDKAKKLLkietdlsnnliaeIEKRNKKELEKTQElidkysafdEQEKQniltrtkEKNDLRIKKEQELNQKIKEL 1016
Cdd:pfam05672 5 GTTDAEEAARIL-------------AEKRRQAREQRERE---------EQERL-------EKEEEERLRKEELRRRAEEE 55
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 215401158 1017 KEKALSDGQISENERKEIEklENQRRDITVKELSKTEKEQERiLVRMQRNRnaysiDEA-SKAIKEAEKARKARKK 1091
Cdd:pfam05672 56 RARREEEARRLEEERRREE--EERQRKAEEEAEEREQREQEE-QERLQKQK-----EEAeAKAREEAERQRQEREK 123
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
922-1123 |
1.21e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 922 SEENSRIMEKVRLNSGQISE-DKAKKLLKIETDLSNNLIAEIEKRNKKELEKTQELIDKYSAFDEQEKQNILTRTKEKND 1000
Cdd:PHA02562 166 SEMDKLNKDKIRELNQQIQTlDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1001 LRIKKE------QELNQKIKELK---------EKALSDG--------QISENERKeIEKLENQRRDITVK---------E 1048
Cdd:PHA02562 246 LVMDIEdpsaalNKLNTAAAKIKskieqfqkvIKMYEKGgvcptctqQISEGPDR-ITKIKDKLKELQHSlekldtaidE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1049 LSKTEKEQERILVRMQRNRNAYS------------IDEASKAIKEAEKARKARKKEVdKQYEDDVIAIKNNVNLSKSEKD 1116
Cdd:PHA02562 325 LEEIMDEFNEQSKKLLELKNKIStnkqslitlvdkAKKVKAAIEELQAEFVDNAEEL-AKLQDELDKIVKTKSELVKEKY 403
|
....*..
gi 215401158 1117 KLLAIAD 1123
Cdd:PHA02562 404 HRGIVTD 410
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
29-328 |
1.32e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 47.35 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 29 QLGVVNSEMKANLSAFDKSEKSMEK-YQA--RIKGLNDRLKVQKKMYSQVED------ELKQV-NANYQKAKSSvKDVEK 98
Cdd:TIGR01612 884 KLNDYEKKFNDSKSLINEINKSIEEeYQNinTLKKVDEYIKICENTKESIEKfhnkqnILKEIlNKNIDTIKES-NLIEK 962
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 99 AYLKLVE---ANKK---EKLALDKSKEALKSSNTELKKAENQYK------RTNQRKQDAYQKLKQLRDAEQKLKNSNQ-- 164
Cdd:TIGR01612 963 SYKDKFDntlIDKInelDKAFKDASLNDYEAKNNELIKYFNDLKanlgknKENMLYHQFDEKEKATNDIEQKIEDANKni 1042
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 165 -----ATTAQLKRASDAVQKQSAKHKALVEQykqegNQVQKLKVQNDNLSKSNDKIE----SSYAKTNTkLKQTEkEFND 235
Cdd:TIGR01612 1043 pnieiAIHTSIYNIIDEIEKEIGKNIELLNK-----EILEEAEINITNFNEIKEKLKhynfDDFGKEEN-IKYAD-EINK 1115
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 236 LNNTIKNHSANV-----------AKAETAVNKEKAALNNLERSIDKASS--EMKTFNKEQMIAQSHFGKLASQADVMSKK 302
Cdd:TIGR01612 1116 IKDDIKNLDQKIdhhikaleeikKKSENYIDEIKAQINDLEDVADKAISndDPEEIEKKIENIVTKIDKKKNIYDEIKKL 1195
|
330 340
....*....|....*....|....*....
gi 215401158 303 FSSIGD---KMTSLGRTMTMGVSTPITLG 328
Cdd:TIGR01612 1196 LNEIAEiekDKTSLEEVKGINLSYGKNLG 1224
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
90-243 |
1.68e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 45.13 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 90 KSSVKDVEKAYLKLVEANKKEKLALDKSKEALKSSNTELKKAENQYKRTNQRKQDAYQKLKQLRDAEQKLKN-SNQATTA 168
Cdd:cd00176 53 EERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEkEAALASE 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 215401158 169 QLKRASDAVQKQSAKHKALVEQYKQEGNQVQKLKVQNDNLSKSNdkIESSYAKTNTKLKQTEKEFNDLNNTIKNH 243
Cdd:cd00176 133 DLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEG--HPDADEEIEEKLEELNERWEELLELAEER 205
|
|
| MltE |
COG0741 |
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ... |
1803-1915 |
1.71e-04 |
|
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin domain) [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440504 [Multi-domain] Cd Length: 244 Bit Score: 45.37 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1803 AKDPEKWLKSLKGSGVRSGSGVNKAASAWAGDIRRAAKRMGVnvtsgDVGNIISLIQHESGGNAGITqSSAlrdinvlqg 1882
Cdd:COG0741 75 ALAAFAAIAALAAELLALAALLLRRPLPYLPLIEEAAKKYGV-----DPALVLALIRQESAFNPNAV-SPA--------- 139
|
90 100 110
....*....|....*....|....*....|...
gi 215401158 1883 nPAKGLLQYIPQTFRHYAVRGhnNIYSGYDQLL 1915
Cdd:COG0741 140 -GARGLMQLMPATARRLGLKL--GLGPSPDDLF 169
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
955-1095 |
1.71e-04 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 44.29 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 955 SNNLIAEIEKRNKKELEKTQELIDKYSAFD--EQEKQNILTRTKE-----KNDLRIKKEQELNQKIKELKEKalsdgqis 1027
Cdd:pfam11600 3 SQKSVQSQEEKEKQRLEKDKERLRRQLKLEaeKEEKERLKEEAKAekeraKEEARRKKEEEKELKEKERREK-------- 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 215401158 1028 eNERKEIEKLENQRrditVKELSKTEKeQERILVRMQRNRNaysiDEASKAIKEAEKARKARKKEVDK 1095
Cdd:pfam11600 75 -KEKDEKEKAEKLR----LKEEKRKEK-QEALEAKLEEKRK----KEEEKRLKEEEKRIKAEKAEITR 132
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
942-1132 |
1.73e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.67 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 942 DKAKKLLKiETDLSNNLIAEIEKRNKKELEKTQELIDKYSAFDEQEKQNI---------------LTRTKEKNDLRIKKE 1006
Cdd:COG1340 57 EEAQELRE-KRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNkaggsidklrkeierLEWRQQTEVLSPEEE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1007 QELNQKIKELKEKA-LSDGQISENE-----RKEIEKLENQRRDITvKELSKTEKEQERILVRMQRNRNAY-----SIDEA 1075
Cdd:COG1340 136 KELVEKIKELEKELeKAKKALEKNEklkelRAELKELRKEAEEIH-KKIKELAEEAQELHEEMIELYKEAdelrkEADEL 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 215401158 1076 SKAIKEAEKARKARKKEVDKQYEDdviaIKNNVNLSKSEKDKLLAIADQRHKDEVRK 1132
Cdd:COG1340 215 HKEIVEAQEKADELHEEIIELQKE----LRELRKELKKLRKKQRALKREKEKEELEE 267
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
938-1155 |
1.81e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.07 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 938 QISEDKAKKLLKIETDLSNNLIAEI--------------------------------EKRNKKELEKTQELIDK------ 979
Cdd:pfam13868 27 QIAEKKRIKAEEKEEERRLDEMMEEereraleeeeekeeerkeerkryrqeleeqieEREQKRQEEYEEKLQEReqmdei 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 980 ---YSAFDEQEKQNILTRTKEK-------NDLRIK-------KEQELNQKIKE-LKEKALSDGQIsENERKEIEKLENQR 1041
Cdd:pfam13868 107 verIQEEDQAEAEEKLEKQRQLreeidefNEEQAEwkelekeEEREEDERILEyLKEKAEREEER-EAEREEIEEEKERE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1042 RDITVKELSKTEKEQERI-LVRMQRNRNAYSIDEASKAIKEAEKaRKARKKEVDKQYEDDVIaiknnvnlsksEKDKLLA 1120
Cdd:pfam13868 186 IARLRAQQEKAQDEKAERdELRAKLYQEEQERKERQKEREEAEK-KARQRQELQQAREEQIE-----------LKERRLA 253
|
250 260 270
....*....|....*....|....*....|....*
gi 215401158 1121 IADQRHKDEVRKakskkdavvdVVKKQNKDIDKEM 1155
Cdd:pfam13868 254 EEAEREEEEFER----------MLRKQAEDEEIEQ 278
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
996-1209 |
1.99e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 45.68 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 996 KEKNDLRIKKEQELNQKIKELKEKALsdgqiseNERKEIEKLENQRRDITVKELSK--TEKEQERILVRMQRNRNAYSID 1073
Cdd:pfam13868 32 KRIKAEEKEEERRLDEMMEEERERAL-------EEEEEKEEERKEERKRYRQELEEqiEEREQKRQEEYEEKLQEREQMD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1074 EASKAIKEAEKARKARKKEVDKQYEDDVIAIKNNVNLSKSEKDKLLAIADQRhkdeVRKAKSKKDAVVDVVKKQNKDIDK 1153
Cdd:pfam13868 105 EIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDER----ILEYLKEKAEREEEREAEREEIEE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 215401158 1154 EMDLSSGRVYKNTEKwwnglkswwsnfREDQKKKSDK--YAKEQEETARRNRENIKKW 1209
Cdd:pfam13868 181 EKEREIARLRAQQEK------------AQDEKAERDElrAKLYQEEQERKERQKEREE 226
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
48-315 |
2.27e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 48 EKSMEKYQARIKGLNDRLKVQKKMYSQVE-DELKQVNANYQKAKSSVKDVEKAYLKLVE-ANKKEKLALDKSK------E 119
Cdd:PRK01156 482 EEKIREIEIEVKDIDEKIVDLKKRKEYLEsEEINKSINEYNKIESARADLEDIKIKINElKDKHDKYEEIKNRykslklE 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 120 ALKSSNTELKKAENQYK----RTNQRKQDayQKLKQLRDAEQKLK-------NSNQATTAQLKRASDAVQ------KQSA 182
Cdd:PRK01156 562 DLDSKRTSWLNALAVISlidiETNRSRSN--EIKKQLNDLESRLQeieigfpDDKSYIDKSIREIENEANnlnnkyNEIQ 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 183 KHKALVEQYKQEGNQVQKLKVQNDNLSKSNDKIESSYAKTNTKLKQTEKEFNDLNNTIKNHSANVAKAETAVNKEKAALN 262
Cdd:PRK01156 640 ENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRIN 719
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 215401158 263 NLERSIDKASSEMKTFNKEQMIAQShFGKLASQAdvMSKKfsSIGDKMTSLGR 315
Cdd:PRK01156 720 DINETLESMKKIKKAIGDLKRLREA-FDKSGVPA--MIRK--SASQAMTSLTR 767
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
45-266 |
2.34e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 45 DKSEKSMEKYQARIKGLNDRLKVQKKMYS---QVEDELKQVNANYQKAKSSVKDVEKAYLKL---VEANKKEKLALDKSK 118
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKrteNIEELIKEKEKELEEVLREINEISSELPELreeLEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 119 EALKSSNTELKKAENQYKRTNQRKQDAYQKLKQLRDAEQKLKnSNQATTAQLKRasdaVQKQSAKHKALVEQYKQEGNQV 198
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE-EKVKELKELKE----KAEEYIKLSEFYEEYLDELREI 312
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 215401158 199 QKLKVQNDNLSKSNDKIESSYAKTNTKLKQTEKEFNDLnntiKNHSANVAKAETAVNKEKAALNNLER 266
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKEL----EKRLEELEERHELYEEAKAKKEELER 376
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
942-1051 |
2.73e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 45.39 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 942 DKAKKLLKIETDLSNNLIAEIEKRnKKELEKTQELIDKYSAFDEQEKQNILTRTKEK-------NDLRIKKEQELNQKIK 1014
Cdd:smart00787 157 KEDYKLLMKELELLNSIKPKLRDR-KDALEEELRQLKQLEDELEDCDPTELDRAKEKlkkllqeIMIKVKKLEELEEELQ 235
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 215401158 1015 ELKEKaLSDG--QISE--NERKEIEKLENQRRDITVKELSK 1051
Cdd:smart00787 236 ELESK-IEDLtnKKSElnTEIAEAEKKLEQCRGFTFKEIEK 275
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
71-257 |
2.77e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 71 MYSQVEDELKQVNA---------NYQKAKSSVKDVE--KAYLKLVEANKKEKL---ALDKSKEALKSSNTELKKAENQYK 136
Cdd:COG4913 240 AHEALEDAREQIELlepirelaeRYAAARERLAELEylRAALRLWFAQRRLELleaELEELRAELARLEAELERLEARLD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 137 RTNQRKQDAYQKL------------KQLRDAEQKLKN--------SNQATTAQLKRASDA--VQKQSAKHKALVEQYKQE 194
Cdd:COG4913 320 ALREELDELEAQIrgnggdrleqleREIERLERELEErerrrarlEALLAALGLPLPASAeeFAALRAEAAALLEALEEE 399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 215401158 195 GNQVQKLKvqndnlsksnDKIESSYAKTNTKLKQTEKEFNDLNNTIKNHSANVAKAETAVNKE 257
Cdd:COG4913 400 LEALEEAL----------AEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
52-236 |
2.78e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 45.39 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 52 EKYQARIKGLNDRLKVQKKMYSQVEdelKQVNAN-------YQKAKSSVKDVEKAYLKLVEAN-----KKE--------- 110
Cdd:smart00787 66 ELYQFSCKELKKYISEGRDLFKEIE---EETLINnpplfkeYFSASPDVKLLMDKQFQLVKTFarleaKKMwyewrmkll 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 111 ---KLALDKSKEALKSSNTELKKAENQYKRTNQRKQDAYQKL-KQLRDAEQKLKNSNQATTAQLKRASDAVQKQSAKHKA 186
Cdd:smart00787 143 eglKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALeEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMI 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 215401158 187 LVEQYKQEGNQVQKLKVQNDNLSKSNDKIESSYAKTNTKLKQ----TEKEFNDL 236
Cdd:smart00787 223 KVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQcrgfTFKEIEKL 276
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
126-276 |
2.90e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 126 TELKKAENQYKRTNQRKQDAYQKLKQLRDAEQKLKNSNQATTAQLKRASDAVQKqsakHKALVEQYKQEGNQVQKLKVQN 205
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEE----VEARIKKYEEQLGNVRNNKEYE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215401158 206 DnLSKsndKIESsyakTNTKLKQTEKEFNDLNNTIKNHSANVAKAETAVNKEKAALNNLERSIDKASSEMK 276
Cdd:COG1579 93 A-LQK---EIES----LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
|
| F-BAR_PSTPIP1 |
cd07671 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ... |
78-243 |
2.91e-04 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Proline-Serine-Threonine Phosphatase-Interacting Protein 1 (PSTPIP1), also known as CD2 Binding Protein 1 (CD2BP1), is mainly expressed in hematopoietic cells. It is a binding partner of the cell surface receptor CD2 and PTP-PEST, a tyrosine phosphatase which functions in cell motility and Rac1 regulation. It also plays a role in the activation of the Wiskott-Aldrich syndrome protein (WASP), which couples actin rearrangement and T cell activation. Mutations in the gene encoding PSTPIP1 cause the autoinflammatory disorder known as PAPA (pyogenic sterile arthritis, pyoderma gangrenosum, and acne) syndrome. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153355 [Multi-domain] Cd Length: 242 Bit Score: 44.57 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 78 ELKQVNANYQKAKSSVKDVEKAYLKLVEANKKEKLALDKSKEALKSSNtelKKAENQYKRTNQRKQDAYQK-LKQLRDAE 156
Cdd:cd07671 54 EINTLKASFDQLKQQIENIGNSHIQLAGMLREELKSLEEFRERQKEQR---KKYEAVMERVQKSKVSLYKKtMESKKTYE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 157 QKLKNSNQATTAQLKRASDAVQKQSAKHKALVEQYKQEGNQVQKLKVQN-DNLSKSNDKIESSYAKTNTKLKQTEKE-FN 234
Cdd:cd07671 131 QRCREADEAEQTFERSSSTGNPKQSEKSQNKAKQCRDAATEAERVYKQNiEQLDKARTEWETEHILTCEVFQLQEDDrIT 210
|
....*....
gi 215401158 235 DLNNTIKNH 243
Cdd:cd07671 211 ILRNALWVH 219
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
941-1153 |
2.95e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.19 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 941 EDKAKKLLKIETDLSNNLIAEIEKRNKKELEKtQELIDKYSAFDEQEKQNILTRT-------KEKNDLRIKKEQELNQKI 1013
Cdd:TIGR00606 905 KDAKEQDSPLETFLEKDQQEKEELISSKETSN-KKAQDKVNDIKEKVKNIHGYMKdienkiqDGKDDYLKQKETELNTVN 983
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1014 KELKEkalsdgqiSENERKEIEK-LENQRRDItvkelsKTEKEQERI----LVRMQRNRNAYSIDEASKA-IKEAEKARK 1087
Cdd:TIGR00606 984 AQLEE--------CEKHQEKINEdMRLMRQDI------DTQKIQERWlqdnLTLRKRENELKEVEEELKQhLKEMGQMQV 1049
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 215401158 1088 ARKKEVDKQYEDDVIAIKNNVNLSKS-----EKDKLLAIADQRHKdEVRKAKSK-KDAVVD--VVKKQNKDIDK 1153
Cdd:TIGR00606 1050 LQMKQEHQKLEENIDLIKRNHVLALGrqkgyEKEIKHFKKELREP-QFRDAEEKyREMMIVmrTTELVNKDLDI 1122
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
19-197 |
3.08e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 19 VQEGMKGLKRQLGVVNSEMKANLSAFDKSEKSMEKYQARIKGLNDRLKVQKkmysqveDELKQVNANYQKAKSSVKDVE- 97
Cdd:COG3883 35 AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR-------EELGERARALYRSGGSVSYLDv 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 98 --------------KAYLKLVEANKKEKLALDKSKEALKSSNTELKKAENQYKRTNQRKQDAYQKLKQLRDAEQKLKNSN 163
Cdd:COG3883 108 llgsesfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQL 187
|
170 180 190
....*....|....*....|....*....|....
gi 215401158 164 QATTAQLKRASDAVQKQSAKHKALVEQYKQEGNQ 197
Cdd:COG3883 188 SAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
908-1167 |
3.37e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 908 SKETE-KALEKYVHYSEENSRIMEKvRLNSGQISEDKAKKLLKIETDLSNNLiaeieKRNKKELE-KTQELIDKYSAFde 985
Cdd:TIGR04523 451 VKELIiKNLDNTRESLETQLKVLSR-SINKIKQNLEQKQKELKSKEKELKKL-----NEEKKELEeKVKDLTKKISSL-- 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 986 QEKQNILtrTKEKNdlrikkeqELNQKIKELKEKALSDGQISENERKEIEKLENQrrditvKELSKTEKEQERILVrmqr 1065
Cdd:TIGR04523 523 KEKIEKL--ESEKK--------EKESKISDLEDELNKDDFELKKENLEKEIDEKN------KEIEELKQTQKSLKK---- 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1066 nrnaySIDEASKAIKEAEKARKARKKEVDKqYEDDVIAIKNNVNLSKSEKDKLLAIadqrhkdeVRKAKSKKDAVVDVVK 1145
Cdd:TIGR04523 583 -----KQEEKQELIDQKEKEKKDLIKEIEE-KEKKISSLEKELEKAKKENEKLSSI--------IKNIKSKKNKLKQEVK 648
|
250 260
....*....|....*....|..
gi 215401158 1146 KQNKDIDKEMDLSSGRVYKNTE 1167
Cdd:TIGR04523 649 QIKETIKEIRNKWPEIIKKIKE 670
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
941-1118 |
3.52e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 941 EDKAKKLLKIETDLSNNLIAEIEK--RNKKELEKT----QELIDKYSAFDEQ--EKQNILTRTKEKNDL--RIKKEQELN 1010
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKEleEELKEAEEKeeeyAELQEELEELEEEleELEAELEELREELEKleKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1011 QKIKELKEKALSDGQISENERKEIEKLENQRRDItvKELSKTEKEQERILVRMQRNRNAYSIDEASKAIKEAEKARKARk 1090
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEEEL--EELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL- 208
|
170 180
....*....|....*....|....*...
gi 215401158 1091 kevdKQYEDDVIAIKNNVNLSKSEKDKL 1118
Cdd:COG4717 209 ----AELEEELEEAQEELEELEEELEQL 232
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
957-1204 |
3.61e-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: 45.82 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 957 NLIAEIEKRNKKELEKTQELIDKYSAFDEqekqniltRTKEKNDLRiKKEQELNQKIKELKEKAlsdgqisENERKEIEK 1036
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEE--------LEEELEQLR-KELEELSRQISALRKDL-------ARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1037 LENQRRDItvkELSKTEKEQERILVRMQRNrnaysidEASKAIKEAEKARKARKKEVDKQyeddviaiKNNVNLSKSEKD 1116
Cdd:TIGR02168 745 LEERIAQL---SKELTELEAEIEELEERLE-------EAEEELAEAEAEIEELEAQIEQL--------KEELKALREALD 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1117 KLLAIAdQRHKDEVRKAKSKKDAV---VDVVKKQNKDIDKEMDLSSGRVYKNTEKwWNGLKSWWSNFREDQKKKSDKYAK 1193
Cdd:TIGR02168 807 ELRAEL-TLLNEEAANLRERLESLerrIAATERRLEDLEEQIEELSEDIESLAAE-IEELEELIEELESELEALLNERAS 884
|
250
....*....|.
gi 215401158 1194 EQEETARRNRE 1204
Cdd:TIGR02168 885 LEEALALLRSE 895
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
954-1098 |
3.81e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 954 LSNNLIAEIEKRNKKELEKTQELIDKYSafdEQEKQniltrTKEKNDLRIKKEQELNQKIKELKEKALsdgQISENERKE 1033
Cdd:PRK00409 499 LPENIIEEAKKLIGEDKEKLNELIASLE---ELERE-----LEQKAEEAEALLKEAEKLKEELEEKKE---KLQEEEDKL 567
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 215401158 1034 IEKLENQRRDItVKELSKTEKEQERILVRMQR----NRNAYSIDEASKAIKEAEKARKARKKEVDKQYE 1098
Cdd:PRK00409 568 LEEAEKEAQQA-IKEAKKEADEIIKELRQLQKggyaSVKAHELIEARKRLNKANEKKEKKKKKQKEKQE 635
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
953-1154 |
3.85e-04 |
|
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: 45.83 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 953 DLSNNLIAEIEKRNKKELEKTQELIDKYSAFDEQEKQ-NILTRTKEKNDLRIK--------KEQELNQKIKELK--EKAL 1021
Cdd:TIGR02169 688 RELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEiEQLEQEEEKLKERLEeleedlssLEQEIENVKSELKelEARI 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1022 SDGQIS-ENERKEIEKLE----NQRRDITVKELSKTEKEQERILVRMQR-----NRNAYSIDEASKAIKEAEKAR---KA 1088
Cdd:TIGR02169 768 EELEEDlHKLEEALNDLEarlsHSRIPEIQAELSKLEEEVSRIEARLREieqklNRLTLEKEYLEKEIQELQEQRidlKE 847
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215401158 1089 RKKEVDKQYEDDVIAIKnnvNLSKSEKDKLLAIAD--QRHKD---EVRKAKSKKDAVVDVVKKQNKDIDKE 1154
Cdd:TIGR02169 848 QIKSIEKEIENLNGKKE---ELEEELEELEAALRDleSRLGDlkkERDELEAQLRELERKIEELEAQIEKK 915
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
24-276 |
4.65e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 24 KGLKRQLGVVNSEMKANLSAFDKSEKSMEKYQARIKGLNDRLkvqkkmysqveDELKQVNANYQKAKSSVKDVEKAYLKL 103
Cdd:COG1340 53 KELREEAQELREKRDELNEKVKELKEERDELNEKLNELREEL-----------DELRKELAELNKAGGSIDKLRKEIERL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 104 VEANKKEKLALDKSKEALKssntELKKAENQYKrtnqrkqdayqKLKQLRDAEQKLKNsnqaTTAQLKRASDAVQKQSAK 183
Cdd:COG1340 122 EWRQQTEVLSPEEEKELVE----KIKELEKELE-----------KAKKALEKNEKLKE----LRAELKELRKEAEEIHKK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 184 HKALVEQYKQEGNQVQKLKVQNDNLSKSNDKIESSYAKTNTKLKQTEKEFNDLNNTIKnhsanvaKAETAVNKEKAALNN 263
Cdd:COG1340 183 IKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELR-------ELRKELKKLRKKQRA 255
|
250
....*....|...
gi 215401158 264 LERSIDKASSEMK 276
Cdd:COG1340 256 LKREKEKEELEEK 268
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
36-297 |
4.81e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 36 EMKANLSAFDKSEKSMEKYQARIKGLNDRLKVQKKMYSQVEDELKQVNANYQKAKSSVKDVEKAYLKLVEANKKEKlALD 115
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE-ELK 1708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 116 KSKEALKSSNTELKKAENQYK-RTNQRKQDAYQKLKQLRDAEQKLKNSNQATTAQLKRASDAVQKQSAKHKALVEQYKQE 194
Cdd:PTZ00121 1709 KKEAEEKKKAEELKKAEEENKiKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 195 GNQVQKLKVQNDNLSKSNDKIESSYAKTNT----KLKQTE----KEFNDLNNTIKNHSANVAKAETAVNKEKAALNNLEr 266
Cdd:PTZ00121 1789 DEKRRMEVDKKIKDIFDNFANIIEGGKEGNlvinDSKEMEdsaiKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKE- 1867
|
250 260 270
....*....|....*....|....*....|.
gi 215401158 267 sidkASSEMKTFNKEQMIAQSHFGKLASQAD 297
Cdd:PTZ00121 1868 ----ADFNKEKDLKEDDEEEIEEADEIEKID 1894
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
908-1156 |
5.15e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 908 SKETEKALEKYVHYSEENSRIMEKVRLNSGQISEDKAKKLLKIETDLSNNLIaeiekrnKKELEKTQELIDKYsafdEQE 987
Cdd:TIGR04523 508 LEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENL-------EKEIDEKNKEIEEL----KQT 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 988 KQNILTRTKEKNDLRIKKEQELNQKIKELKEKAlsdgqisenerKEIEKLEnqrrditvKELSKTEKEQERILVRMQRNR 1067
Cdd:TIGR04523 577 QKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKE-----------KKISSLE--------KELEKAKKENEKLSSIIKNIK 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1068 NAY-SIDEASKAIKEAEKARKARKKEVDKQYEDDVIAIKNNVNLSKSEKDKLLA-----IADQRHKDEVRKAKSKKDAVV 1141
Cdd:TIGR04523 638 SKKnKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLhykkyITRMIRIKDLPKLEEKYKEIE 717
|
250
....*....|....*
gi 215401158 1142 DVVKKQnKDIDKEMD 1156
Cdd:TIGR04523 718 KELKKL-DEFSKELE 731
|
|
| F-BAR_PSTPIP |
cd07647 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ... |
64-193 |
5.42e-04 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Vetebrates contain two Proline-Serine-Threonine Phosphatase-Interacting Proteins (PSTPIPs), PSTPIP1 and PSTPIP2. PSTPIPs are mainly expressed in hematopoietic cells and are involved in the regulation of cell adhesion and motility. Mutations in PSTPIPs have been shown to cause autoinflammatory disorders. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain, while PSTPIP2 contains only the N-terminal F-BAR domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153331 [Multi-domain] Cd Length: 239 Bit Score: 43.62 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 64 RLKVQKKMYSQVEDELKQ---VNANYQKA-----------------KSS-------VKDVEKAYLKLVEANKKEklaLDK 116
Cdd:cd07647 13 RLKEGKKMCKELEDFLKQrakAEEDYGKAllklsksagpgdeigtlKSSwdslrkeTENVANAHIQLAQSLREE---AEK 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 215401158 117 SKEALKSSNTELKKAENQYKRTNQRKQDAYQKLKQLRDA-EQKLKNSNQATTAQLKRASDAVQKQSAKHKALVEQYKQ 193
Cdd:cd07647 90 LEEFREKQKEERKKTEDIMKRSQKNKKELYKKTMKAKKSyEQKCREKDKAEQAYEKSSSGAQPKEAEKLKKKAAQCKT 167
|
|
| YkyA |
pfam10368 |
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ... |
36-236 |
5.45e-04 |
|
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein signal and a hydrolase domain. It is similar to cell wall binding proteins and might also be recognisable by a host immune defence system. It is thus likely to belong to pathways important for pathogenicity.
Pssm-ID: 431235 [Multi-domain] Cd Length: 185 Bit Score: 42.96 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 36 EMKANLSAFDKSEKSMEKYQariKGLNDRLKVQKKMYSQV----EDELKQVNANYQKAKSSVKDVEKAYlklveanKKEK 111
Cdd:pfam10368 5 KIYDHLEEAVELEKPFEEQQ---EPLVELEKKEQELYEEIielgMDEFDEIKKLSDEALENVEEREELL-------EKEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 112 LALDKSKEALKSSNTELKKAENqykrtnqrkqdayqklKQLRDAEQKLKNSNQATTAQLKRASDAVQKQSAKHKALVEQY 191
Cdd:pfam10368 75 ESIEEAKEEFKKIKEIIEEIED----------------EELKKEAEELIDAMEERYEAYDELYDAYKKALELDKELYEML 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 215401158 192 KQEGNQVQKLKVQNDNLSKSNDKIEssyaKTNTKLKQTEKEFNDL 236
Cdd:pfam10368 139 KDEDLTLEELQEQIEKINESYEEVK----EANEQFNEYTKQYNEL 179
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
3-270 |
5.82e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.83 E-value: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 3 EKVEGMTLELKLDHlgVQEGMKGLKRQL----GVVNSEMKAnlsafdksEKSMEKYQARIKglnDRLKVQKKMYSQVEDE 78
Cdd:PRK04778 266 DENLALLEELDLDE--AEEKNEEIQERIdqlyDILEREVKA--------RKYVEKNSDTLP---DFLEHAKEQNKELKEE 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 79 LKQVNANY----------QKAKSSVKDVEKAYLKLVEANKKEKLALDKSKEALKSSNTELKKAENQYKRTNQ-----RK- 142
Cdd:PRK04778 333 IDRVKQSYtlneselesvRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEmlqglRKd 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 143 -QDAYQKL----KQLRDAEQKLKNSN------------QATTAQLKRAS----------DAVQKQSAKHKALVEQYKQEG 195
Cdd:PRK04778 413 eLEAREKLeryrNKLHEIKRYLEKSNlpglpedylemfFEVSDEIEALAeeleekpinmEAVNRLLEEATEDVETLEEET 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 196 NQVqklkVQNDNLSK-----SNdKIESSYAKTNTKLKQTEKEFNDLnntikNHSANVAKAETAVNK-EKAALNNLERSID 269
Cdd:PRK04778 493 EEL----VENATLTEqliqyAN-RYRSDNEEVAEALNEAERLFREY-----DYKAALEIIATALEKvEPGVTKRIEDSYE 562
|
.
gi 215401158 270 K 270
Cdd:PRK04778 563 K 563
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
985-1156 |
5.84e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 985 EQEKQNILTRTKEKNDLRIKKEQELNQKIKELKEkalSDGQISENERKeIEKLENQRRDITvKELSKTEKEQERILVRMQ 1064
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAA---LERRIAALARR-IRALEQELAALE-AELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1065 RNRNAY--------------------SIDEASKAIKEAE------KARKARKKEVDKQYEdDVIAIKNNVNLSKSEKDKL 1118
Cdd:COG4942 101 AQKEELaellralyrlgrqpplalllSPEDFLDAVRRLQylkylaPARREQAEELRADLA-ELAALRAELEAERAELEAL 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 215401158 1119 LAIADQRhKDEVRKAKSKKDAVVDVVKKQNKDIDKEMD 1156
Cdd:COG4942 180 LAELEEE-RAALEALKAERQKLLARLEKELAELAAELA 216
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
913-1088 |
6.53e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 913 KALEKYVHYSEENSRIMEKvRLNSGQISEDKAKKLLKIETDLSNNLIAEIEKRNK-------------KELEKTQELIDK 979
Cdd:COG4942 65 AALARRIRALEQELAALEA-ELAELEKEIAELRAELEAQKEELAELLRALYRLGRqpplalllspedfLDAVRRLQYLKY 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 980 YSAFDEQEKQNILTRTKEKNDLRIKKEQELNQKIKELKEKalsdgqisENERKEIEKLENQRRDiTVKELSKTEKEQERI 1059
Cdd:COG4942 144 LAPARREQAEELRADLAELAALRAELEAERAELEALLAEL--------EEERAALEALKAERQK-LLARLEKELAELAAE 214
|
170 180
....*....|....*....|....*....
gi 215401158 1060 LVRMQRNRNAYSiDEASKAIKEAEKARKA 1088
Cdd:COG4942 215 LAELQQEAEELE-ALIARLEAEAAAAAER 242
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
46-319 |
7.21e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 44.73 E-value: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 46 KSEKSMEKYQARIKGLNDRLKVQKKMYSQVEdelkQVNANYQKAKSSVKDVE------------KAYLKLVEANKKEKLA 113
Cdd:pfam05557 122 RAELELQSTNSELEELQERLDLLKAKASEAE----QLRQNLEKQQSSLAEAEqrikelefeiqsQEQDSEIVKNSKSELA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 114 ----LDKSKEALKSSNTELkkaeNQYKRTN----------QRKQDAYQKLK--------QLRDAEQKLK---NSNQATTA 168
Cdd:pfam05557 198 ripeLEKELERLREHNKHL----NENIENKlllkeevedlKRKLEREEKYReeaatlelEKEKLEQELQswvKLAQDTGL 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 169 QLKRASDAVQKqsakhkalVEQYKQEgNQVqkLKVQNDNLSKSNDKIESSYAKTNTKLKQTEKEFNDLNNTIKNHSANV- 247
Cdd:pfam05557 274 NLRSPEDLSRR--------IEQLQQR-EIV--LKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVr 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 248 --AKAETAVNKEKAALNNLERSIDKASSEMKTFNK--------EQMI--AQSHFGKLASQADVMSKKFSSIGDKMTSLGR 315
Cdd:pfam05557 343 rlQRRVLLLTKERDGYRAILESYDKELTMSNYSPQllerieeaEDMTqkMQAHNEEMEAQLSVAEEELGGYKQQAQTLER 422
|
....
gi 215401158 316 TMTM 319
Cdd:pfam05557 423 ELQA 426
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
105-287 |
7.71e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.58 E-value: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 105 EANKKEKLALDKSKEALKSSNTELKKAENQYKRT---NQRKQDAYQKLKQLRDAEQKLKNSNQATtaQLKRASDAVQKQS 181
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLkeqAKKALEYYQLKEKLELEEEYLLYLDYLK--LNEERIDLLQELL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 182 AKHKALVEQYKQEGNQVQKLKVQNDNLSKSNDKIESS----YAKTNTKLKQTEKEF-------NDLNNTIKNHSANVAKA 250
Cdd:pfam02463 247 RDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLqeeeLKLLAKEEEELKSELlklerrkVDDEEKLKESEKEKKKA 326
|
170 180 190
....*....|....*....|....*....|....*..
gi 215401158 251 ETAVNKEKAALNNLErsIDKASSEMKTFNKEQMIAQS 287
Cdd:pfam02463 327 EKELKKEKEEIEELE--KELKELEIKREAEEEEEEEL 361
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
58-266 |
8.04e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 8.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 58 IKGLNDRLKVQKKMYSQVEDELKQVNANYQkakssvkDVEKAYLKLVEANKKEKLALDKS-KEALKssntELKKAENQY- 135
Cdd:PRK00409 522 IASLEELERELEQKAEEAEALLKEAEKLKE-------ELEEKKEKLQEEEDKLLEEAEKEaQQAIK----EAKKEADEIi 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 136 --KRTNQRKQDAYQKLKQLRDAEQKLKNSNQATTAQLK---------RASDAVQKQSAKHKALVEQYKQEGN-QVQ---- 199
Cdd:PRK00409 591 keLRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKkqkekqeelKVGDEVKYLSLGQKGEVLSIPDDKEaIVQagim 670
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215401158 200 KLKVQNDNLSKSND--KIESSYAKTNTKLKQTEKefndlnNTIKNHSANVAKAETAVNK--EKAALNNLER 266
Cdd:PRK00409 671 KMKVPLSDLEKIQKpkKKKKKKPKTVKPKPRTVS------LELDLRGMRYEEALERLDKylDDALLAGYGE 735
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
917-1208 |
1.04e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 917 KYVHYSEENSRIMEKVRLNSGQISEdKAKKLLKIETDLsNNLIAEIEKRNKKELEKTQELIDKYSAFDEQEKQnILTRTK 996
Cdd:TIGR04523 219 QISELKKQNNQLKDNIEKKQQEINE-KTTEISNTQTQL-NQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQ-LNQLKS 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 997 EKNDLRIKKEQELNQKIKEL-----KEKALSDGQISENERK------EIEKLENQRRDITVKELSK----TEKEQERILV 1061
Cdd:TIGR04523 296 EISDLNNQKEQDWNKELKSElknqeKKLEEIQNQISQNNKIisqlneQISQLKKELTNSESENSEKqrelEEKQNEIEKL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1062 RMQRNRNAYSIDEASKAIKEAEkaRKARKKEVDKQYEDDVIAIKnnvnlsKSEKDKLlaiaDQRHKDeVRKAKSKKDAVV 1141
Cdd:TIGR04523 376 KKENQSYKQEIKNLESQINDLE--SKIQNQEKLNQQKDEQIKKL------QQEKELL----EKEIER-LKETIIKNNSEI 442
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 215401158 1142 DVVKKQNKDIDKEmdlssgrvYKNTEkwwnglkswwsNFREDQKKKSDKYAKEQEETaRRNRENIKK 1208
Cdd:TIGR04523 443 KDLTNQDSVKELI--------IKNLD-----------NTRESLETQLKVLSRSINKI-KQNLEQKQK 489
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
76-302 |
1.07e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 76 EDELKQVNANYQKAKSSVKDVEKAYLKLVE--------------------------ANKKEKLaldksKEALKSSNTELK 129
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEeknalqeqlqaetelcaeaeemrarlAARKQEL-----EEILHELESRLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 130 KAE-------NQYKRTNQRKQDAYQKLKQLRDAEQKLKNSNQATTAQLKR-------ASDAVQKQSAKHKALVEQYKQEG 195
Cdd:pfam01576 86 EEEersqqlqNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKleedillLEDQNSKLSKERKLLEERISEFT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 196 NQVQKLKVQNDNLSKSNDKIESSYAKTNTKLKQTEK--------------EFNDLNNTIKNHSANVAKAETAVNKEKAAL 261
Cdd:pfam01576 166 SNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKgrqelekakrklegESTDLQEQIAELQAQIAELRAQLAKKEEEL 245
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 215401158 262 NNLERSIDKASSEMKTFNKEQMIAQSHFGKLasQADVMSKK 302
Cdd:pfam01576 246 QAALARLEEETAQKNNALKKIRELEAQISEL--QEDLESER 284
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
143-271 |
1.09e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 143 QDAYQKLKQLRDAEQKLK---NSNQATTAQLKRASDAVQKQSAKHKALVEQYKQE------GNQVQKLKVQNDNLSKSND 213
Cdd:COG4913 606 FDNRAKLAALEAELAELEeelAEAEERLEALEAELDALQERREALQRLAEYSWDEidvasaEREIAELEAELERLDASSD 685
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215401158 214 KI---ESSYAKTNTKLKQTEKEFNDLNNTIKNHSANVAKAETAVNKEKAALNNLERSIDKA 271
Cdd:COG4913 686 DLaalEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746
|
|
| CENP-F_N |
pfam10481 |
Cenp-F N-terminal domain; Mitosin or centromere-associated protein-F (Cenp-F) is found bound ... |
145-267 |
1.16e-03 |
|
Cenp-F N-terminal domain; Mitosin or centromere-associated protein-F (Cenp-F) is found bound across the centromere as one of the proteins of the outer layer of the kinetochore. Most of the kinetochore/centromere functions appear to depend upon binding of the C-terminal par to f the molecule, whereas the N-terminal part, here, may be a cytoplasmic player in controlling the function of microtubules and dynein.
Pssm-ID: 463106 [Multi-domain] Cd Length: 304 Bit Score: 43.27 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 145 AYQKLKQLRDAEQKLKNSNQATTAQLKRASDAVQKQsaKHKAlveqyKQEGNQVQKLKVQNDNLSKSNDKIESSYAKTNT 224
Cdd:pfam10481 16 ALQKIQELESQLDKLKKERQQKQFQLESLEAALQKQ--KQKV-----ENEKNEGSALKRENQSLMESCDNLEKSRQKISH 88
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 215401158 225 KLKQTEKEFNDLNNTIKNHSANVAKAETAVNKEKaalNNLERS 267
Cdd:pfam10481 89 DLQVKESQVNFLEGQLNSSKKQIEKLEQELKRYK---SELERS 128
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
940-1208 |
1.30e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.86 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 940 SEDKAKKLLKIETD------LSNNLIAEIEKRNKKELEKTQELIDKYSAFDEQEKqNILTRTKEKNDLRIKKEQELNQKI 1013
Cdd:TIGR04523 52 KEKELKNLDKNLNKdeekinNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLS-KINSEIKNDKEQKNKLEVELNKLE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1014 KELKE-KALSDGQISE--NERKEIEKLENQRRDITV------KELSKTEKEQERILVRMQRNRNAYSIDEASKAIKeaeK 1084
Cdd:TIGR04523 131 KQKKEnKKNIDKFLTEikKKEKELEKLNNKYNDLKKqkeeleNELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNL---K 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1085 ARKARKKEVDKQYED---DVIAIKNNVNLSKSEKDKLLAIAdQRHKDEVRKAKSKKDAVVDVVKKQNKDIDKemdlsSGR 1161
Cdd:TIGR04523 208 KKIQKNKSLESQISElkkQNNQLKDNIEKKQQEINEKTTEI-SNTQTQLNQLKDEQNKIKKQLSEKQKELEQ-----NNK 281
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 215401158 1162 VYKNTEKWWNGLKSWWSNFREDQKKKSDKYAKEQEETARRNRENIKK 1208
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQN 328
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
68-317 |
1.32e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.79 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 68 QKKMYSQVEDELKQVNANYQKAKSSVKDVEKAYLKLVEANKK-------------EKLALDKSKEALKSSNTELKKAENQ 134
Cdd:COG5185 223 EKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDlrleklgenaessKRLNENANNLIKQFENTKEKIAEYT 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 135 YKRTNQRKQDAYQKLKQLRDAEQKL-------KNSNQATTAQLKRASDAVQKQSAKHKALVEQYKQEGNQVQKLKvqndN 207
Cdd:COG5185 303 KSIDIKKATESLEEQLAAAEAEQELeeskretETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSE----E 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 208 LSKSNDKIESSYAKTNTKLKQTEKEFND----LNNTIKNHSANVAKAETAVNKE-------KAALNNLERSIDKASSEMK 276
Cdd:COG5185 379 LDSFKDTIESTKESLDEIPQNQRGYAQEilatLEDTLKAADRQIEELQRQIEQAtssneevSKLLNELISELNKVMREAD 458
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 215401158 277 TFNKEQMI--AQSHFGKLASQADVMSKKFSSIGDKMTSLGRTM 317
Cdd:COG5185 459 EESQSRLEeaYDEINRSVRSKKEDLNEELTQIESRVSTLKATL 501
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
113-307 |
1.32e-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: 43.21 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 113 ALDKSKEALKSSNTELKKAENQYKRTNQRKQDAYQKLKQLRD----AEQKLKNSNQ---ATTAQLKRASDAVQKQSAKHK 185
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERriaaLARRIRALEQelaALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 186 ALVEQYKQEGNQVQK-------------------------LKVQNDNLSKSNDKIESSYAKTNTKLKQTEKEFNDLNNTI 240
Cdd:COG4942 101 AQKEELAELLRALYRlgrqpplalllspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 215401158 241 KNHSANVAKAETAVNKEKAALNNLERSIDKASSEMKTFNKEQMIAQSHFGKLASQADVMSKKFSSIG 307
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| secA |
PRK12903 |
preprotein translocase subunit SecA; Reviewed |
842-1099 |
1.33e-03 |
|
preprotein translocase subunit SecA; Reviewed
Pssm-ID: 237258 [Multi-domain] Cd Length: 925 Bit Score: 43.89 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 842 EFKNYlgsIGKSFKEKFSKDMKDGYKSLSDDDLLKVGVNKFKGF-----MQTMGTASKKASDTVKVLGKGVSketekaLE 916
Cdd:PRK12903 671 DFENY---HKEELAQYLIEALNEIYFKKRQVILDKIALNTFFESeryiiLSALDKYWQNHIDTMDKLRSGVN------LV 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 917 KYVH------YSEENSRIMEKVRLNsgqISEDKAKKLLKIETDLSNNLIAEIEK---RNKKELEKTQELIDKYSAFDEQ- 986
Cdd:PRK12903 742 QYSQknpyqvYTEEGTKKFNILLQE---IAYDVIVSLFNNPNAEKILIITEILSdgiNNSDINDRPQELIDQIIESEEEr 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 987 -EKQNILTRTKEKNDLRIKKEQELNQKIKELKEKALSDGQISENERKEIEKLENQRRDITVKELSKTEKEQERILVRMQR 1065
Cdd:PRK12903 819 lKALRIQREEMLMRPEELELINEEQKNLKQEIKLELSEIQEAEEEIQNINENKNEFVEFKNDPKKLNKLIIAKDVLIKLV 898
|
250 260 270
....*....|....*....|....*....|....
gi 215401158 1066 NRnaySIDEAskaiKEAEKARKARKKEVDKQYED 1099
Cdd:PRK12903 899 IS---SDEIK----QDEKTTKKKKKDLEKTDEEA 925
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
46-280 |
1.54e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.89 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 46 KSEKSmEKYQARIKGLNDRLK--VQKKMYSQVEDELK------QVNANYQKAKSSVKDVEKAYLKLVEANKKEKLA---- 113
Cdd:TIGR01612 662 KSELS-KIYEDDIDALYNELSsiVKENAIDNTEDKAKlddlksKIDKEYDKIQNMETATVELHLSNIENKKNELLDiive 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 114 ------------LDKSKEALKSSNTELKKAENQYKRTNQRKQDAYQKLKQLRDAEQKLKNSNQATTAQLKRASDAVQKQS 181
Cdd:TIGR01612 741 ikkhihgeinkdLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYI 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 182 AKHKALVEQYKQEGNQVQKLKvqNDNLSKSNDKI--ESSYAKtntKLKQTEKEFNDLNNTIKNHSAN--VAKAETAVNKE 257
Cdd:TIGR01612 821 KTISIKEDEIFKIINEMKFMK--DDFLNKVDKFInfENNCKE---KIDSEHEQFAELTNKIKAEISDdkLNDYEKKFNDS 895
|
250 260
....*....|....*....|...
gi 215401158 258 KAALNNLERSIDKASSEMKTFNK 280
Cdd:TIGR01612 896 KSLINEINKSIEEEYQNINTLKK 918
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
41-284 |
1.65e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.89 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 41 LSAFDKSEKSMEKYQA--RIKGLNDRLKVQK-KMYSQVE------DELKQVNANYQKAKSSVKDVEKAYLKLVEAN---K 108
Cdd:TIGR01612 1980 LNIIFENQQLYEKIQAsnELKDTLSDLKYKKeKILNDVKlllhkfDELNKLSCDSQNYDTILELSKQDKIKEKIDNyekE 2059
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 109 KEKLALDKS----KEALKSSNTELKKAENQYKRTNQRKQDAYQKLKQLRDAEQKLKNSNQATTAQLKRASDAVQKQSAKH 184
Cdd:TIGR01612 2060 KEKFGIDFDvkamEEKFDNDIKDIEKFENNYKHSEKDNHDFSEEKDNIIQSKKKLKELTEAFNTEIKIIEDKIIEKNDLI 2139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 185 KALVEQYKQ-----EGNQVQKLKVQ----------------------NDNLSKSNDKIESsyAKTNTKLKQTEKEFNDLN 237
Cdd:TIGR01612 2140 DKLIEMRKEcllfsYATLVETLKSKvinhsefitsaakfskdffefiEDISDSLNDDIDA--LQIKYNLNQTKKHMISIL 2217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 215401158 238 NTIKNHSANVakaetaVNKEKAA---LNNLER--SIDKASSEMKT--FNKEQMI 284
Cdd:TIGR01612 2218 ADATKDHNNL------IEKEKEAtkiINNLTElfTIDFNNADADIlhNNKIQII 2265
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
47-274 |
1.67e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 47 SEKSMEKYQARIKGLNDRLKVQKKMYSQVEDELKQVNANYQKAKSSVKDVEKaylklveankkeklALDKSKEALKSSNT 126
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA--------------EIDKLQAEIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 127 ELKKAENQYKrtnQRKQDAYQKLKQLRDAEQkLKNSNQATTAqLKRAsDAVQKQSAKHKALVEQYKQegnQVQKLKVQND 206
Cdd:COG3883 80 EIEERREELG---ERARALYRSGGSVSYLDV-LLGSESFSDF-LDRL-SALSKIADADADLLEELKA---DKAELEAKKA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 215401158 207 NLSKSNDKIESSYAKTNTKLKQTEKEFNDLNNTIKNHSANVAKAETAVNKEKAALNNLERSIDKASSE 274
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
97-280 |
1.75e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.42 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 97 EKAYLKLVEANKKEKLALDKskealkssNTELKKAENQYKRTNQRKQDAYQKLKQLRDAEQKLKNSNQATtaQLKRASDA 176
Cdd:pfam02463 172 KEALKKLIEETENLAELIID--------LEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK--LNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 177 VQKQSAKHKALVEQYKQEGNQVQKLKVQNDNLSKSNDKIESS----YAKTNTKLKQTEKEFNDLNNTIKNHSANVAKAET 252
Cdd:pfam02463 242 LQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLqeeeLKLLAKEEEELKSELLKLERRKVDDEEKLKESEK 321
|
170 180
....*....|....*....|....*...
gi 215401158 253 AVNKEKAALNNLERSIDKASSEMKTFNK 280
Cdd:pfam02463 322 EKKKAEKELKKEKEEIEELEKELKELEI 349
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
910-1163 |
1.78e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.38 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 910 ETEKALEKYVHYSEEN----SRIMEKVRLNSGQISEDKAKKLLKIETDLSNnLIAEIE--KRNKKELEKTQELIDKYSAF 983
Cdd:PRK05771 54 KLSEALDKLRSYLPKLnplrEEKKKVSVKSLEELIKDVEEELEKIEKEIKE-LEEEISelENEIKELEQEIERLEPWGNF 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 984 D-----EQEKQNI------LTRTKEKNDLRIKkEQELNQKIKELKEK----ALSDGQISENERKEIEKLENQRRDITVKE 1048
Cdd:PRK05771 133 DldlslLLGFKYVsvfvgtVPEDKLEELKLES-DVENVEYISTDKGYvyvvVVVLKELSDEVEEELKKLGFERLELEEEG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1049 LSKTEkeqerilvrmqrnrnaysIDEASKAIKEAEKARKARK---KEVDKQYEDDVIAIKNnvnlsksekdkLLAIADQR 1125
Cdd:PRK05771 212 TPSEL------------------IREIKEELEEIEKERESLLeelKELAKKYLEELLALYE-----------YLEIELER 262
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 215401158 1126 HKDEVRKAKSKKDAVVD--VVKKQNKDIDKEMD-LSSGRVY 1163
Cdd:PRK05771 263 AEALSKFLKTDKTFAIEgwVPEDRVKKLKELIDkATGGSAY 303
|
|
| COG5325 |
COG5325 |
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion]; |
88-288 |
1.88e-03 |
|
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion];
Pssm-ID: 227635 [Multi-domain] Cd Length: 283 Bit Score: 42.52 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 88 KAKSSVKDVEKAYLKLVEANKKEKLALDKSKEAL-KSSNTELKKAENQYKRTNQRKQDAYQKLKQLRDaeqklkNSNQAT 166
Cdd:COG5325 49 AVRRSISRLGKVYAKHTEPSFSDKSEKEDEIDELsKKVNQDLQRCEKILKTKYKNLQSSFLQSKLLRD------LNTECM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 167 TAQlkrasdAVQKQSAKhkalveQYKQEGNQVQKLKVQNDNLSKSNDK-----IESSYAK-TNTKLKQTEKEFNDLNNTI 240
Cdd:COG5325 123 EGQ------RIQQKSAQ------FRKYQVLQAKFLRNKNNDQHPLEEEedeesLSSLGSQqTLQQQGLSNEELEYQQILI 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 215401158 241 KNHSANVAKAETAVN-------------KEKAAL-NNLERSIDKASSEMKTFNKEQMIAQSH 288
Cdd:COG5325 191 TERDEEIKNLARGIYelneifrdlgslvGEQGELvDRIDFNIENTSDNLKNANKELEKAPAH 252
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
114-274 |
1.90e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 114 LDKSKEALKSSNTELKKAENQYKRTNQRKQDAYQKLKQLRDAEQKLKNsnqattaQLKRASDAVQKQSAKHKALVEQYKQ 193
Cdd:TIGR04523 42 LKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLND-------KLKKNKDKINKLNSDLSKINSEIKN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 194 EGNQVQKLKVQNDNLSKSNDKIESSYAKTNTKLKQTEKEFNDLNNTIKNHSANVAKAETAVNKEKAALNNLERSIDKASS 273
Cdd:TIGR04523 115 DKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKN 194
|
.
gi 215401158 274 E 274
Cdd:TIGR04523 195 K 195
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
60-271 |
2.01e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.29 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 60 GLNDRLK-VQKKMYSQVEDELK----QVNANYQKAKSSVKDVEKAylkLVEANKKeklaLDKSKEALKSSNTELKKA-EN 133
Cdd:pfam12128 582 GVKLDLKrIDVPEWAASEEELRerldKAEEALQSAREKQAAAEEQ---LVQANGE----LEKASREETFARTALKNArLD 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 134 QYKRTNQRKQDAYQKlkqlrdaeqklknsNQATTAQLKRASDAVQKQSA-------KHKALVEQYKQE-----GNQVQKL 201
Cdd:pfam12128 655 LRRLFDEKQSEKDKK--------------NKALAERKDSANERLNSLEAqlkqldkKHQAWLEEQKEQkrearTEKQAYW 720
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 215401158 202 KV----QNDNLSKSNDKIESSYAKTNTKLKQTEKEFndlnntiKNHSANVAKAETAVNKEKAALNNLERSIDKA 271
Cdd:pfam12128 721 QVvegaLDAQLALLKAAIAARRSGAKAELKALETWY-------KRDLASLGVDPDVIAKLKREIRTLERKIERI 787
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
89-309 |
2.07e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 43.28 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 89 AKSSVKDVEKAYLKLVEANKKEKLAL-DKskealkssntelKKAENQYKRTNQRKQDAYQKL----KQLRDAEQ-KLKNS 162
Cdd:NF012221 1536 ATSESSQQADAVSKHAKQDDAAQNALaDK------------ERAEADRQRLEQEKQQQLAAIsgsqSQLESTDQnALETN 1603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 163 NQATTAQLKRASDAVQKQSAKHKALVEQYKQEGNQVQKLKVQNDN------LSKSNDKIESSYAKTNTKLKQTEKEFNDL 236
Cdd:NF012221 1604 GQAQRDAILEESRAVTKELTTLAQGLDALDSQATYAGESGDQWRNpfagglLDRVQEQLDDAKKISGKQLADAKQRHVDN 1683
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 215401158 237 NNTIKNhsaNVAKAETAVNKEKAALNNLERSIDKASSEMKTFNKEQMIAQSHFGKLASQADVMSKKFSSIGDK 309
Cdd:NF012221 1684 QQKVKD---AVAKSEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQ 1753
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
985-1139 |
2.09e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 42.53 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 985 EQEKQNILTRTKEKNDLRIKKEQelnQKIKELKEKALSDGQISENERKEIEKLENQRRDITVKELSKTEKEQERILVRMQ 1064
Cdd:TIGR02794 66 EQERQKKLEQQAEEAEKQRAAEQ---ARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAER 142
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 215401158 1065 RnrnaysidEASKAIKEAEKARKARKKEVDKQYEDDVIAIKNNVNLSKSEKDKLLAIADQRHKDEVRKAKSKKDA 1139
Cdd:TIGR02794 143 K--------AKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEA 209
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1007-1127 |
2.29e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.15 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1007 QELNQKIKEL---KEKALSDGQISENER-----KEIEKLENQRRDITVKELSKTEKEQERILVRMQRNRNAYSIDEASKA 1078
Cdd:COG0542 414 DELERRLEQLeieKEALKKEQDEASFERlaelrDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKE 493
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 215401158 1079 IKEAEKARKARKK----EVDKqyED--DVIAIKNNVNLSK---SEKDKLLAIADQRHK 1127
Cdd:COG0542 494 LAELEEELAELAPllreEVTE--EDiaEVVSRWTGIPVGKlleGEREKLLNLEEELHE 549
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
945-1118 |
2.35e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 42.31 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 945 KKLLK-IETDLSNNLiaEIEKRNKKELEKTQELI--------DKYSAFdeQEKQNILTrtKEKNDLRIKKEQELNQkike 1015
Cdd:smart00787 139 MKLLEgLKEGLDENL--EGLKEDYKLLMKELELLnsikpklrDRKDAL--EEELRQLK--QLEDELEDCDPTELDR---- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1016 LKEKALSDGQISENERKEIEKLENQRRDITVKELSKTEKEQErilvrmqrnrnaySIDEASKAIKEAEKARKARKKEVdK 1095
Cdd:smart00787 209 AKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSE-------------LNTEIAEAEKKLEQCRGFTFKEI-E 274
|
170 180
....*....|....*....|....*
gi 215401158 1096 QYEDDVIAIKN--NVNLSKSEKDKL 1118
Cdd:smart00787 275 KLKEQLKLLQSltGWKITKLSGNTL 299
|
|
| FCH_F-BAR |
cd07610 |
The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a ... |
903-1069 |
2.39e-03 |
|
The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a dimerization module that binds and bends membranes; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. F-BAR domain containing proteins, also known as Pombe Cdc15 homology (PCH) family proteins, include Fes and Fer tyrosine kinases, PACSINs/Syndapins, FCHO, PSTPIP, CIP4-like proteins and srGAPs. Many members also contain an SH3 domain and play roles in endocytosis. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules. These tubules have diameters larger than those observed with N-BARs. The F-BAR domains of some members such as NOSTRIN and Rgd1 are important for the subcellular localization of the protein.
Pssm-ID: 153294 [Multi-domain] Cd Length: 191 Bit Score: 41.17 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 903 LGKGVSKETEKALEKYVHYSEENSRIMEKVRLNSGQISEDK------AKKLLKIETDLSNNLIAEIEKRnkkeleKTQEL 976
Cdd:cd07610 11 LGLDLLKDLREFLKKRAAIEEEYAKNLQKLAKKFSKKPESGktslgtSWNSLREETESAATVHEELSEK------LSQLI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 977 IDKYSAFDEQEKQNiltRTKEKNDLRiKKEQELNQKIKELKEKALSDgqisenERKEIEKLENQRRDITVKELSKTEKEQ 1056
Cdd:cd07610 85 REPLEKVKEDKEQA---RKKELAEGE-KLKKKLQELWAKLAKKADEE------YREQVEKLNPAQSEYEEEKLNKIQAEQ 154
|
170
....*....|...
gi 215401158 1057 ERILVRMQRNRNA 1069
Cdd:cd07610 155 EREEERLEILKDN 167
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
19-199 |
2.40e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 19 VQEGMKGLKRQLGVVNSEMKANLSAFDKSEKSMEKYQARIKGLNDRLKVQKKMYSQVEDELKQVNANYQKAKSS------ 92
Cdd:COG3883 28 LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSvsyldv 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 93 ----------------VKDVEKAYLKLVE---------ANKKEKlaLDKSKEALKSSNTELKKAENQYKRTNQRKQDAYQ 147
Cdd:COG3883 108 llgsesfsdfldrlsaLSKIADADADLLEelkadkaelEAKKAE--LEAKLAELEALKAELEAAKAELEAQQAEQEALLA 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 215401158 148 KLKQLRDAEQKLKNSNQATTAQLKRASDAVQKQSAKHKALVEQYKQEGNQVQ 199
Cdd:COG3883 186 QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
922-1113 |
2.74e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 922 SEENSRIMEKVRLNSGQIS--EDKAKKLLKIETDlSNNLIAEIEKRNKKE------LEKT-----------QELIDKYSA 982
Cdd:pfam01576 151 SKERKLLEERISEFTSNLAeeEEKAKSLSKLKNK-HEAMISDLEERLKKEekgrqeLEKAkrklegestdlQEQIAELQA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 983 FDEQEKQNILTRTKEKNDLRIKKEQELNQKIKELKEKALSDGQISE------NERKEIEKLENQRRDITvKELS--KTEK 1054
Cdd:pfam01576 230 QIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISElqedleSERAARNKAEKQRRDLG-EELEalKTEL 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 215401158 1055 E---------QErilVRMQRNRnaySIDEASKAIKEAEKARKA-----RKK------EVDKQYEDdviAIKNNVNLSKS 1113
Cdd:pfam01576 309 EdtldttaaqQE---LRSKREQ---EVTELKKALEEETRSHEAqlqemRQKhtqaleELTEQLEQ---AKRNKANLEKA 378
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1-272 |
2.74e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1 MNEKVEGMTLELKldhlGVQEGMKGLKRQLGVVNSEMKANLSAFDKSEKSMEKYQARIKGLNDRLKVQKKMYSQVEDELK 80
Cdd:pfam01576 529 MKKKLEEDAGTLE----ALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQK 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 81 QVNANYQKAKS-SVKDVEKAYLKLVEANKKEKLALDKSKEAlkssnTELKKAENQYKRTNqrkqdayqklKQLRDAEQKL 159
Cdd:pfam01576 605 KFDQMLAEEKAiSARYAEERDRAEAEAREKETRALSLARAL-----EEALEAKEELERTN----------KQLRAEMEDL 669
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 160 KNSNQAT---TAQLKRASDAVQKQSAKHKALVEQYKQEGN-----------QVQKLKVQND-NLSKSNDKIESsyaktnt 224
Cdd:pfam01576 670 VSSKDDVgknVHELERSKRALEQQVEEMKTQLEELEDELQatedaklrlevNMQALKAQFErDLQARDEQGEE------- 742
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 215401158 225 KLKQTEKEFNDLNNTIKNHSANVAKAETAVNKEKAALNNLERSIDKAS 272
Cdd:pfam01576 743 KRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAAN 790
|
|
| COG5644 |
COG5644 |
U3 small nucleolar RNA-associated protein 14 [Function unknown]; |
941-1219 |
2.75e-03 |
|
U3 small nucleolar RNA-associated protein 14 [Function unknown];
Pssm-ID: 227931 [Multi-domain] Cd Length: 869 Bit Score: 42.77 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 941 EDKAKKLLKIETDlsnnliaEIEKRNKKELEKTQELIDKYSafDEQEKQNILTRTKEKNDLRIKKEQELNqkiKELKEKA 1020
Cdd:COG5644 389 ERKAKRVAKIKSK-------TYRKIRKNRKEKEMALIPKSE--DLENEKSEEARALERMTQRHKNTSSWT---RKMLERA 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1021 LSDGQISENERKEIEKLENQRRDITVKELSKTEKEQERILVRMQRNRNaysIDEASKAIKEAE-----------KARKAR 1089
Cdd:COG5644 457 SHGEGTREAVNEQIRKGDELMQRIHGKEIMDGEDVSEFSDSDYDTNEQ---VSTAFEKIRNEEelkgvlgmkfmRDASNR 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1090 KKEVDKQYEDDVIAIKNNVNLSKSEKDKLLAIADQrhkdevrkAKSKKDAVVDVVKKQNKDID---KEMDLSSGRVYKNT 1166
Cdd:COG5644 534 QMAASKISVADLVKVENGDDIDVGELDEVGGDAIY--------ANAGRREVFPVVEQRRKLAPrkrKEDFVTPSTSLEKS 605
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 215401158 1167 EKWWNglkswwsnfrEDQKKKSDkyAKEQEETARRNRENIKKWFGNAWDGVKS 1219
Cdd:COG5644 606 MDRIL----------HGQKKRAE--GAVVFEKPLEATENFNPWLDRKMRRIKR 646
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
901-1055 |
3.08e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 901 KVLGKGVSKETEKALEKYVHYSEENSRIMEKVRLNSGQIsedkakKLLKIETDLSNNLIAEIEKRNKkELEKTQELIDKy 980
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQV------ERLEAEVEELEAELEEKDERIE-RLERELSEARS- 455
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 215401158 981 SAFDEQEKQNILTRTKEKNDlRIKKE-QELNQKIKELKEKalsdgqisENERKEIEKLENQRRDITVKELSKTEKE 1055
Cdd:COG2433 456 EERREIRKDREISRLDREIE-RLERElEEERERIEELKRK--------LERLKELWKLEHSGELVPVKVVEKFTKE 522
|
|
| MapZ_EC1 |
pfam18041 |
MapZ extracellular domain 1; This is the extracellular domain 1 (MapZextra1) found in ... |
118-218 |
3.39e-03 |
|
MapZ extracellular domain 1; This is the extracellular domain 1 (MapZextra1) found in Streptococcus pneumoniae cell division site positioning protein MapZ. MapZ ensures accurate placement of the bacterial division site. The domain is a rigid four alpha-helices with two flexible linkers. The N-terminal end of MapZextra1 is connected to the trans-membrane segment of MapZ whilst the C-terminal is linked to MapZextra2 via a serine rich linker (SRL).The highly conserved residues are not accessible at the surface but are directly involved in many inter-helices interactions allowing for rigidity.
Pssm-ID: 465625 [Multi-domain] Cd Length: 129 Bit Score: 39.62 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 118 KEALKSSNTELKKAENQYKRTNQRKQDAYqklkqLRDAEQKLKNSNqaTTAQLkrasDAVQKQSAKHKAlVEQYKQEGNQ 197
Cdd:pfam18041 1 QESETASSQELKKEDANLDAFEKEYDAFY-----TDDEHTFLKNSE--FAAQL----SKLQKQLEKLKD-SKYYDKLKTK 68
|
90 100
....*....|....*....|.
gi 215401158 198 VQKLKVQNDNLSKSNDKIESS 218
Cdd:pfam18041 69 LDSLKDQIAAIQKVNGKFTSP 89
|
|
| PLN02372 |
PLN02372 |
violaxanthin de-epoxidase |
950-1058 |
3.96e-03 |
|
violaxanthin de-epoxidase
Pssm-ID: 215212 [Multi-domain] Cd Length: 455 Bit Score: 42.14 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 950 IETDLSNNLIAEIEKRNKKELEKTQELIDKYSAFDEQE--KQNILTRTKEKNDLrikKEQELNQKIKELKEKALSDGQ-I 1026
Cdd:PLN02372 350 VRTDNTCGPEPPLLERLEKDVEEGEKTIVKEARQIEEEleKEVEKLGKEEESLF---KRVALEEGLKELEQDEENFLKeL 426
|
90 100 110
....*....|....*....|....*....|..
gi 215401158 1027 SENERKEIEKLEnqrrditvKELSKTEKEQER 1058
Cdd:PLN02372 427 SKEEKELLEKLK--------MEASEVEKLFGR 450
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
49-214 |
4.52e-03 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 40.43 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 49 KSMEKYQARIKGLNDRLKVQKKMYSQvedELKQVNANYQKAKSSVKDVEKAYLKLVEANKKEKLALdkskEALKSSNTEL 128
Cdd:pfam05010 43 KIVAEFEKTIAQMIEEKQKQKELEHA---EIQKVLEEKDQALADLNSVEKSFSDLFKRYEKQKEVI----SGYKKNEESL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 129 KKAENQYKRTNQRKQDAYQKLKQlrDAEQKLKNSNqATTAQLKRasdavqKQSAKHKALVEQYKQEGNQVQKLKVQNDNL 208
Cdd:pfam05010 116 KKCAQDYLARIKKEEQRYQALKA--HAEEKLDQAN-EEIAQVRS------KAKAETAALQASLRKEQMKVQSLERQLEQK 186
|
....*.
gi 215401158 209 SKSNDK 214
Cdd:pfam05010 187 TKENEE 192
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
19-285 |
4.56e-03 |
|
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: 42.36 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 19 VQEGMKGLKRQLGVVNSEMKANLSAFDKSEKSMEKYQARIKGLNDRLKvqkkmysqvEDELKQVNANYQKAKSSVKDVEK 98
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS---------HSRIPEIQAELSKLEEEVSRIEA 812
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 99 AylkLVEANKKEKlALDKSKEALkssntelkkaenqykrtnqrkQDAYQKLKQLRDAEQKLKNSNQATTAQLKRASDAVQ 178
Cdd:TIGR02169 813 R---LREIEQKLN-RLTLEKEYL---------------------EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 179 KQSAKHKALVEQYkqeGNQVQKLKVQNDNLSKSNDKIESSYAKTNTKLKQTEKEFNDLNNTIKNHSANVAKAETAVNKEK 258
Cdd:TIGR02169 868 EELEELEAALRDL---ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
250 260 270
....*....|....*....|....*....|...
gi 215401158 259 ------AALNNLERSIDKASSEMKTFNKEQMIA 285
Cdd:TIGR02169 945 eipeeeLSLEDVQAELQRVEEEIRALEPVNMLA 977
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
6-222 |
4.65e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 6 EGMTLELKLDHlgVQEGMKGLKRQLGVVNSEMKANL----SAFDKSEKSMEKYQARIKGLNDRLKVQKKMYSQVEDELKQ 81
Cdd:PHA02562 182 QIQTLDMKIDH--IQQQIKTYNKNIEEQRKKNGENIarkqNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNK 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 82 VNANYQKAKSSVKD---VEKAYLK----------------LVEANKKEKLALDKSKEALKSSNTELKKAENQYKRTNQRK 142
Cdd:PHA02562 260 LNTAAAKIKSKIEQfqkVIKMYEKggvcptctqqisegpdRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 143 QDAYQKLKQLRDAEQKLKNSNQATTAQLKRASDAVQKQSAKHKALVEQYKQEGNQVQKLKVQNDNLSKSNDKIESSYAKT 222
Cdd:PHA02562 340 LELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRGIVTDLLKDSGIKA 419
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
909-1138 |
4.70e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 41.78 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 909 KETEKALEKYVHYSEENSRIMEKVRLNSGQISEDKAK---KLLKIETDLSNNLIAEIEKRNKKELEKTQELIDKYSAFDE 985
Cdd:pfam02029 77 KRLQEALERQKEFDPTIADEKESVAERKENNEEEENSsweKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 986 QEKQNILTRTKEKNDLRIKKEQELNQKIKELKEKALSDGQISENERKEIEKLENQRRDITVKELSKTEKEQERILVRMQR 1065
Cdd:pfam02029 157 EEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQER 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1066 NRNAYSIDEASKAIKE-----AEKARKARKKEVDKQYEddviAIKNNVNLSKS--EKDKLLAIADQRHKDEVRKAKSKKD 1138
Cdd:pfam02029 237 EEEAEVFLEAEQKLEElrrrrQEKESEEFEKLRQKQQE----AELELEELKKKreERRKLLEEEEQRRKQEEAERKLREE 312
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
75-272 |
4.93e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 41.94 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 75 VEDELKQVNANYQKAKS----SVKDVEKAYLKLVEANKK-EKLA--LDKSKEALKSSNTELKKAENQYKRTN-QRKQDAY 146
Cdd:pfam05701 143 VKEELESLRKEYASLVSerdiAIKRAEEAVSASKEIEKTvEELTieLIATKESLESAHAAHLEAEEHRIGAAlAREQDKL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 147 QKLKQLRDAEQKLKNSNQATTAQ------LKRASDAVQKQSAKHKALVEqykqegNQVQKLKVQNDNLSKSNDKIESsya 220
Cdd:pfam05701 223 NWEKELKQAEEELQRLNQQLLSAkdlkskLETASALLLDLKAELAAYME------SKLKEEADGEGNEKKTSTSIQA--- 293
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 215401158 221 ktntKLKQTEKEFNDLNntiknhsANVAKAETAVN--------------KEKAALNNLERSIDKAS 272
Cdd:pfam05701 294 ----ALASAKKELEEVK-------ANIEKAKDEVNclrvaaaslrseleKEKAELASLRQREGMAS 348
|
|
| Ax_dynein_light |
pfam10211 |
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in ... |
74-172 |
4.98e-03 |
|
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in flagellar and cilia motility. Eukaryotic cilia and flagella are complex organelles consisting of a core structure, the axoneme, which is composed of nine microtubule doublets forming a cylinder that surrounds a pair of central singlet microtubules. This ultra-structural arrangement seems to be one of the most stable micro-tubular assemblies known and is responsible for the flagellar and ciliary movement of a large number of organizms ranging from protozoan to mammals. This light chain interacts directly with the N-terminal half of the heavy chains.
Pssm-ID: 463000 [Multi-domain] Cd Length: 187 Bit Score: 40.25 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 74 QVEDELKQVNANYQK-AKSSV----KDVEKAYLKLVEANKKEKlALDKSKEALKSSNTELKKAENQYKRTNQRKQDAYQK 148
Cdd:pfam10211 87 RVRDELRMTIAAYQTlYESSVafgmRKALQAEQGKAELEKKIA-DLEEEKEELEKQVAELKAKCEAIEKREEERRQAEEK 165
|
90 100
....*....|....*....|....
gi 215401158 149 LKQlrDAEQKLKNSNQATTAQLKR 172
Cdd:pfam10211 166 KHA--EEIAFLKKTNQQLKAQLER 187
|
|
| Utp11 |
pfam03998 |
Utp11 protein; This protein is found to be part of a large ribonucleoprotein complex ... |
984-1164 |
5.03e-03 |
|
Utp11 protein; This protein is found to be part of a large ribonucleoprotein complex containing the U3 snoRNA. Depletion of the Utp proteins impedes production of the 18S rRNA, indicating that they are part of the active pre-rRNA processing complex. This large RNP complex has been termed the small subunit (SSU) processome.
Pssm-ID: 461122 [Multi-domain] Cd Length: 241 Bit Score: 40.68 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 984 DEQEKQNILTRTKEK----ND-------LRIKKEQELNQKIKELKEKALSDGQIS--------------ENERKEIEKLE 1038
Cdd:pfam03998 31 DYHKKQATLKALREKaaerNPdefyfgmISSKTDDGVHVLVNKDRGNALSVDQVKllktqdlgyvrtkrQIERKKIEKLE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1039 NQRRDITVkELSKTEKEQERILVRMQRNRNAYSIDEASKAIKEAEKARKARKKEVDKQYEDDVIAIKNNVNLSKSEKDKL 1118
Cdd:pfam03998 111 EELHLLDA-GVKNEKKNKHTVFVDSEEEVKNFDPAEYFDTDPELLDRRENRLKKEQLESNSLTAATLKKLDKKKEKLYKE 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 215401158 1119 LAIADQRHKD--------EVRKAKSKKDAVVDVVKKQNKdidkemdlsSGRVYK 1164
Cdd:pfam03998 190 LKARLEREKElkkaeqklELQRALMKKGAKKKVKGGTTK---------KGPVYK 234
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
185-271 |
5.16e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 41.25 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 185 KALVEQYKQEGNQVQKLKVQNDNLSKSNDKIESSYAKTNTKLKQTEKEFNDLNNT--------IKNHSANVAKAETAVNK 256
Cdd:TIGR04320 257 AALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQalqtaqnnLATAQAALANAEARLAK 336
|
90
....*....|....*
gi 215401158 257 EKAALNNLERSIDKA 271
Cdd:TIGR04320 337 AKEALANLNADLAKK 351
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
929-1100 |
5.20e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.13 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 929 MEKVRLNSGQISEDKAK-KLLKIETDL--SNNLIAEIEKR---NKKELEKTQ-ELIDKYSAFdEQEKQNILTRTKEKNDL 1001
Cdd:pfam12128 587 LKRIDVPEWAASEEELReRLDKAEEALqsAREKQAAAEEQlvqANGELEKASrEETFARTAL-KNARLDLRRLFDEKQSE 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1002 RIKKEQELNQKIKELKEKALS-DGQISENERKEIEKLENQRRDItvKELSkTEKEQERILVRMQRNRNAYSIDEAskaIK 1080
Cdd:pfam12128 666 KDKKNKALAERKDSANERLNSlEAQLKQLDKKHQAWLEEQKEQK--REAR-TEKQAYWQVVEGALDAQLALLKAA---IA 739
|
170 180
....*....|....*....|
gi 215401158 1081 EAEKARKARKKEVDKQYEDD 1100
Cdd:pfam12128 740 ARRSGAKAELKALETWYKRD 759
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
939-1159 |
5.23e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 939 ISEDKAKK---LLKIEtDLSNNL------IAEIEKR--------NK----KELEKTQELIDKYSAF--------DEQEKQ 989
Cdd:COG1196 167 ISKYKERKeeaERKLE-ATEENLerlediLGELERQleplerqaEKaeryRELKEELKELEAELLLlklreleaELEELE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 990 NILTRTKEKNDLRIKKEQELNQKIKELKEKALSDGQ----ISENERKEIEKLENQRRDITVKELSKTEKEQERILVRMQR 1065
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELeleeAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1066 NRNAYSIDEASKAIKEAEKARKARKKEVDkqyeddviAIKNNVNLSKSEKDKLLAIADQRHKDEVRKAKSKKDAVVDVVK 1145
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELE--------EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
250
....*....|....
gi 215401158 1146 KQNKDIDKEMDLSS 1159
Cdd:COG1196 398 LAAQLEELEEAEEA 411
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
46-276 |
5.23e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 46 KSEKSMEKYQARIKGlnDRLKVQKKMYSQVEDELKQVNANYQKAKSSVKDVEKAylKLVEANKKEKL----ALDKSKEAL 121
Cdd:PTZ00121 1471 KADEAKKKAEEAKKA--DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK--KADEAKKAEEAkkadEAKKAEEKK 1546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 122 KSSNT----ELKKAEN-----QYKRTNQRKQDAYQKLKQLRDAEQK--------LKNSNQATTAQLKRASDA-------- 176
Cdd:PTZ00121 1547 KADELkkaeELKKAEEkkkaeEAKKAEEDKNMALRKAEEAKKAEEArieevmklYEEEKKMKAEEAKKAEEAkikaeelk 1626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 177 ----VQKQSAKHKALVEQYKQEGNQVQK----LKVQNDNLSKSND----------KIESSYAKTNTKLKQTEKEFNDLNN 238
Cdd:PTZ00121 1627 kaeeEKKKVEQLKKKEAEEKKKAEELKKaeeeNKIKAAEEAKKAEedkkkaeeakKAEEDEKKAAEALKKEAEEAKKAEE 1706
|
250 260 270
....*....|....*....|....*....|....*...
gi 215401158 239 TIKNHSANVAKAETAVNKEKAALNNLERSIDKASSEMK 276
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK 1744
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
224-503 |
5.31e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 224 TKLKQTEKEFNDLNNTIKNHSANVAKAETAVNKEKAALNNLERSIDKASSEMKTFNKEQMIAQShfgKLASQADVMSKKF 303
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA---EIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 304 SSI---GDKMTSLgrtmtmgvstpitlglgAALKTSADFEGQMSRVGAIAQASSKDLKSMSNQAVDLGAKTSKSAnEVAK 380
Cdd:COG3883 93 RALyrsGGSVSYL-----------------DVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKA-ELEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 381 GMEELAALGFNAKQTMEAMPGVISAAEASGAEMATTATVMASAINSFGLKASDANHVADLLARSANDSAADIQYMGDALK 460
Cdd:COG3883 155 KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 215401158 461 YAGTPAKAlGVSIEDTSAAIEVLSNSGLEGSQAGTALRASFIR 503
Cdd:COG3883 235 AAAAAAAA-AASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGA 276
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
27-318 |
5.36e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.13 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 27 KRQLGVVNSEMKANLSAFDKSEKSMEKYQARIKGLNDRLKVQKKMYSQVEDELKQV------------NANYQKAKSSVK 94
Cdd:PTZ00440 2208 KKKNIINNIYKKINFIKLQEIENSSEKYNDISKLFNNVVETQKKKLLDNKNKINNIkdkindkekeliNVDSSFTLESIK 2287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 95 DVEKAYLKLVEANKKEKLALDKSKEALKSSNTELKKAENQYKRTNQRKQDA--YQKLKQLRDAEQKLKNSNQATTAQLKR 172
Cdd:PTZ00440 2288 TFNEIYDDIKSNIGDLYKLEDTNNDELKKVKLYIENITHLLNRINTLINDLdnYQDENYGKDKNIELNNENNSYIIKTKE 2367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 173 ASDAVQKQSAKHKALVEQYKQEGNQVQKLKVQNDNLSKSNDKIE--SSYAKTNTKLKQTEKEFNDLNN------TIKNHS 244
Cdd:PTZ00440 2368 KINNLKEEFSKLLKNIKRNNTLCNNNNIKDFISNIGKSVETIKQrfSSNLPEKEKLHQIEENLNEIKNimnetkRISNVD 2447
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 215401158 245 ANVAKAETAVNKEKAALNNLE--RSIDKASSEMKTFNKEqmiAQSHFgklaSQADVMSKKFSSIGDKMTSLGRTMT 318
Cdd:PTZ00440 2448 AFTNKILQDIDNEKNKENNNMnaEKIDDLIENVTSHNEK---IKSEL----LIINDALRRVKEKKDEMNKLFNSLT 2516
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
949-1138 |
5.41e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 41.56 E-value: 5.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 949 KIETDLSNNLIAEIEKRNKKELEKTQELIdKYSA----FDEQEKQNILTR--TKEKNDLRIKKEQELNQKIK--ELKEKA 1020
Cdd:pfam15558 150 RLEEACHKRQLKEREEQKKVQENNLSELL-NHQArkvlVDCQAKAEELLRrlSLEQSLQRSQENYEQLVEERhrELREKA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1021 lsdgqiseneRKEIEKLENQRRdiTVKELSKTEKEQERILVRM--QRNRNAYSIdeASKAIKeaEKARKARKKEVDKQye 1098
Cdd:pfam15558 229 ----------QKEEEQFQRAKW--RAEEKEEERQEHKEALAELadRKIQQARQV--AHKTVQ--DKAQRARELNLERE-- 290
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 215401158 1099 ddviaiKNN-VNLSKSEKDkllaiaDQRHKDEVRKAKSKKD 1138
Cdd:pfam15558 291 ------KNHhILKLKVEKE------EKCHREGIKEAIKKKE 319
|
|
| YscO-like |
pfam16789 |
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ... |
927-1059 |
5.84e-03 |
|
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. The family includes Chlamydia trachomatis CT670 which is found in a type III secretion gene cluster. CT670 interacts with CT671, a putative YscP homolog and CT670 and CT671 may form a chaperone-effector pair.
Pssm-ID: 435583 [Multi-domain] Cd Length: 160 Bit Score: 39.43 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 927 RIMEKVRLNSGQISEDKaKKLLKIETDLSNNLIAEIEKRNKKELEKTQELIDKYSAFDEQEKQNILTRTKEKNDLRIKKE 1006
Cdd:pfam16789 10 DIKKKRVEEAEKVVKDK-KRALEKEKEKLAELEAERDKVRKHKKAKMQQLRDEMDRGTTSDKILQMKRYIKVVKERLKQE 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 215401158 1007 QELNQKIKELKEKALSDGQISENE----RKEIEKLENQRRDItVKELSKTEKEQERI 1059
Cdd:pfam16789 89 EKKVQDQKEQVRTAARNLEIAREElkkkRQEVEKLEKHKKEW-VKEMKKEEEDQEER 144
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
50-300 |
5.92e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.96 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 50 SMEKYQ------ARIKGLNDRLKVQKKMYSQVEDELKQvnaNYQKAKSSVKDVEKAYLKLVEANKKeKLALDKSKEALKS 123
Cdd:TIGR01612 511 FMELYKpdevpsKNIIGFDIDQNIKAKLYKEIEAGLKE---SYELAKNWKKLIHEIKKELEEENED-SIHLEKEIKDLFD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 124 SNTELKKaENQYkrTNQRKQDAYQKLKQLRDaeqklKNSnqattaQLKRASDAvqkqsakhKALVEQYKQEGNQVQKLK- 202
Cdd:TIGR01612 587 KYLEIDD-EIIY--INKLKLELKEKIKNISD-----KNE------YIKKAIDL--------KKIIENNNAYIDELAKISp 644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 203 VQNDNLSKSNDKIESSYAKTNTKLKQ--TEKEFNDLNNTIKnhsanvakaETAVN--KEKAALNNLERSIDKASSEMKtf 278
Cdd:TIGR01612 645 YQVPEHLKNKDKIYSTIKSELSKIYEddIDALYNELSSIVK---------ENAIDntEDKAKLDDLKSKIDKEYDKIQ-- 713
|
250 260
....*....|....*....|..
gi 215401158 279 NKEQMIAQSHFGKLASQADVMS 300
Cdd:TIGR01612 714 NMETATVELHLSNIENKKNELL 735
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
168-271 |
6.09e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.22 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 168 AQLKrasDAVQKQSAKHKALVEQYKQEGNQVQKLKVQndnlsksndkiESSYAKTNTKLKQTEKEFNDLNNTIKNHSANV 247
Cdd:PRK11637 47 DQLK---SIQQDIAAKEKSVRQQQQQRASLLAQLKKQ-----------EEAISQASRKLRETQNTLNQLNKQIDELNASI 112
|
90 100
....*....|....*....|....
gi 215401158 248 AKAETavnKEKAALNNLERSIDKA 271
Cdd:PRK11637 113 AKLEQ---QQAAQERLLAAQLDAA 133
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
938-1139 |
6.31e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 41.40 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 938 QISEDKAKKLLKIETDLSNNLiaeieKRNKKELE--KTQELIDKYSAFDEQEKQNIltrTKEKNDLRIKK-EQELNQKIk 1014
Cdd:COG2268 144 ELNEDREKFAEKVQEVAGTDL-----AKNGLELEsvAITDLEDENNYLDALGRRKI---AEIIRDARIAEaEAERETEI- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1015 elkekalsdgQISENERKEIEKLENQRRDITVKELSKTEKEQERILVRMQRNRNAYSIdeasKAIKEAEKARKARKKEVD 1094
Cdd:COG2268 215 ----------AIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARA----EAEAAYEIAEANAEREVQ 280
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 215401158 1095 KQYEddVIAIKNNVNLSKSEKDKLLA--IADQRHKDEVRKAKSKKDA 1139
Cdd:COG2268 281 RQLE--IAEREREIELQEKEAEREEAelEADVRKPAEAEKQAAEAEA 325
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
961-1151 |
6.34e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 41.39 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 961 EIEKRNKKELEKTQELIDKYSAFDEQEKQNILTRTKEKNDLRIKKEQELNQKIKELKEKALSDGQISENERKEIEKLEN- 1039
Cdd:pfam02029 34 ESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENs 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1040 --QRRDITVKELSKTEKEQERILVRmQRNRNAYSIDEASKAIKEAEKARKARK-KEVDKQYEDDVIAIKNNVNLSKSEKD 1116
Cdd:pfam02029 114 swEKEEKRDSRLGRYKEEETEIREK-EYQENKWSTEVRQAEEEGEEEEDKSEEaEEVPTENFAKEEVKDEKIKKEKKVKY 192
|
170 180 190
....*....|....*....|....*....|....*
gi 215401158 1117 KLLAIADQRHKDEVRKAKSKKDAVVDVVKKQNKDI 1151
Cdd:pfam02029 193 ESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQ 227
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
26-300 |
6.74e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 26 LKRQLGVVNSEMKANLSAFDKSEKSMEKYQARIKGLNDRLKVQKKMYSQVEDELKQVNANYQKAKssvkdveKAYLKLVE 105
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKN-------RYESEIKT 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 106 ANKKEKLALDKSKEaLKSSNTELKKAENQYKRTNQRKQDAYQKLK-QLRDAEQKLKNSNqattAQLKRASDAVQKqSAKH 184
Cdd:PRK01156 261 AESDLSMELEKNNY-YKELEERHMKIINDPVYKNRNYINDYFKYKnDIENKKQILSNID----AEINKYHAIIKK-LSVL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 185 KALVEQYKQEGNQVQKLKVQNDNLSKSNDKIES---SYAKTNTKLKQTEKEFNDLNNTIknhSANVAKAETAVNKEKAAL 261
Cdd:PRK01156 335 QKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSylkSIESLKKKIEEYSKNIERMSAFI---SEILKIQEIDPDAIKKEL 411
|
250 260 270
....*....|....*....|....*....|....*....
gi 215401158 262 NNLERSIDKASSEMKTFNKEQMIAQSHFGKLASQADVMS 300
Cdd:PRK01156 412 NEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLN 450
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
114-428 |
7.83e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 114 LDKSKEALKSSNTELKKAENQYKRTNQRKQDAYQKLKQLRdaeqklknsnqattAQLKRASDAVQKQSAKHKALVEQYKQ 193
Cdd:COG3883 32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQ--------------AEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 194 EGNQVQKLKV--QNDNLSKSNDKIESS---YAKTNTKLKQTEKEFNDLNNTIKNHSANVAKAETAVNKEKAALNNLERSI 268
Cdd:COG3883 98 SGGSVSYLDVllGSESFSDFLDRLSALskiADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 269 DKASSEMKTFNKEQMIAQSHFGKLASQADVMSKKFSSIGDKMTSLGRTMTMGVSTPITLGLGAALKTSADFEGQMSRVGA 348
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 349 IAQASSKDLKSMSNQAVDLGAKTSKSANEVAKGMEELAALGFNAKQTMEAMPGVISAAEASGAEMATTATVMASAINSFG 428
Cdd:COG3883 258 AAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGG 337
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
985-1153 |
8.23e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 985 EQEKQNILTRTKEKNDLRIKKEQELNQKIKELKEKAlsdGQISENE------RKEIEKLENQRRDITvKELSKTEKE--- 1055
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKE---EEYAELQeeleelEEELEELEAELEELR-EELEKLEKLlql 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1056 ----QERILVRMQRNRNAYSIDEAS---KAIKEAEKARKARKKEVdKQYEDDVIAIKNNVNLSKSEKDKLLAIADQRHKD 1128
Cdd:COG4717 128 lplyQELEALEAELAELPERLEELEerlEELRELEEELEELEAEL-AELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180
....*....|....*....|....*
gi 215401158 1129 EVRKAKSKKDAVVDVVKKQNKDIDK 1153
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQ 231
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
170-282 |
8.77e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 8.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 170 LKRASDAVQKQsAKHKA--LVEQYKQEGNQVQKLKV--QNDNLSKSNDKIESSYAKTNTKLKQTEKEFNDLNNTIKNHSA 245
Cdd:PRK12704 25 RKKIAEAKIKE-AEEEAkrILEEAKKEAEAIKKEALleAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110
....*....|....*....|....*....|....*..
gi 215401158 246 NVAKAETAVNKEKAALNNLERSIDKASSEMKTFNKEQ 282
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQ 140
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
55-183 |
8.97e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 40.67 E-value: 8.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 55 QARIKGLNDRLKVQKKMY--------SQVEDELKQV---NANYQKAKSSVKDVEKAYLKLVEANKKE------------K 111
Cdd:pfam00038 123 EAKIESLKEELAFLKKNHeeevrelqAQVSDTQVNVemdAARKLDLTSALAEIRAQYEEIAAKNREEaeewyqskleelQ 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 112 LALDKSKEALKSSNTELkkaeNQYKRTNQRKQ---DAYQKLK-----QLRDAEQKLknSNQATTAQLKRASDAVQKQSAK 183
Cdd:pfam00038 203 QAAARNGDALRSAKEEI----TELRRTIQSLEielQSLKKQKaslerQLAETEERY--ELQLADYQELISELEAELQETR 276
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
945-1167 |
9.30e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 40.99 E-value: 9.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 945 KKLLKIETDLSNNL--IAEIE-KRNKKELEKTQELIDK-YSAFdEQE---KQNIltrtkEKNDLRIKKE-QELNQKIKEL 1016
Cdd:pfam06160 237 KEIQQLEEQLEENLalLENLElDEAEEALEEIEERIDQlYDLL-EKEvdaKKYV-----EKNLPEIEDYlEHAEEQNKEL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1017 KEK--ALSDG-QISENERKEIEKLEnqrrditvKELSKTEKEQERILVRMQRNRNAYS--------IDEASKAIKE---- 1081
Cdd:pfam06160 311 KEEleRVQQSyTLNENELERVRGLE--------KQLEELEKRYDEIVERLEEKEVAYSelqeeleeILEQLEEIEEeqee 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 1082 -AEKARKARKKEVD-----KQYEDDVIAIK---NNVNLSKSEKDKLLAIADQRHK-DEVRKAKSKKDAVVDVVKKQNKDI 1151
Cdd:pfam06160 383 fKESLQSLRKDELEareklDEFKLELREIKrlvEKSNLPGLPESYLDYFFDVSDEiEDLADELNEVPLNMDEVNRLLDEA 462
|
250
....*....|....*.
gi 215401158 1152 DKEMDlssgRVYKNTE 1167
Cdd:pfam06160 463 QDDVD----TLYEKTE 474
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
36-318 |
9.35e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 9.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 36 EMKANLSAFDKSEKSMEKYQARIKglndrlKVQKKMYSQVEDELKQVNANYQkakSSVKDVEKaylKLVEANKK-EKlaL 114
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELE------LKMEKVFQGTDEQLNDLYHNHQ---RTVREKER---ELVDCQRElEK--L 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 115 DKSKEALKSSNTELkkaENQYKRTnQRKQDAYQKLKQLRDAEqKLKNSNQATTAQLKRASDAVQKQSAKHKALVEQYKQE 194
Cdd:TIGR00606 332 NKERRLLNQEKTEL---LVEQGRL-QLQADRHQEHIRARDSL-IQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215401158 195 GNQV--------QKLKVQNDNLSKSNDKIESSYAKTNTKLKQTEKEFNDLNNTIKNHSANVAKAETAVNKEKaALNNLER 266
Cdd:TIGR00606 407 AKTAaqlcadlqSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQ-ELRKAER 485
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 215401158 267 SIDKA--SSEMKTFNKEQMIAQShfgklaSQADVMsKKFSSIGDKMTSLGRTMT 318
Cdd:TIGR00606 486 ELSKAekNSLTETLKKEVKSLQN------EKADLD-RKLRKLDQEMEQLNHHTT 532
|
|
|