|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
2-97 |
3.45e-49 |
|
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 (FHAD1) and similar proteins; FHAD1, also called FHA domain-containing protein 1, is an uncharacterized FHA domain-containing protein. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438752 [Multi-domain] Cd Length: 96 Bit Score: 169.36 E-value: 3.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 2 KAYLKSPDGFFVLK-KSTTIGKHEdSDLVLQSSDIDNHHALIEFNEAEGTFVLQDFNTRNGTFVNECHIQNVAVKLIPGD 80
Cdd:cd22700 1 KGYLKSSDGIFQLDpKVTTIGREG-CDLVLQSPGVEEQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAPGD 79
|
90
....*....|....*..
gi 1958778178 81 ILRFGSSGPTYELVIEN 97
Cdd:cd22700 80 VLRFGFGGLPYELVVDN 96
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
229-1056 |
2.33e-20 |
|
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: 97.82 E-value: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 229 INRLSD--FEMESKYKDaviMNLQAEIA----DLSQRLSEMAAVVAAARqsnrcdprFQDLDEGDDHRQKEIESMKSQIN 302
Cdd:TIGR02168 188 LDRLEDilNELERQLKS---LERQAEKAerykELKAELRELELALLVLR--------LEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 303 ALQKgysqvlsqTLAERNTEIESLKNEGENLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEVNQLRIQNKEKEYQLEAL 382
Cdd:TIGR02168 257 ELTA--------ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 383 TSRCSKLKEDLrkeeaqkERREAQEKELKLCRSQMQDMEKEVKKLREELKKnytgqnviskTLREKNKVEEKLQEDSRRK 462
Cdd:TIGR02168 329 ESKLDELAEEL-------AELEEKLEELKEELESLEAELEELEAELEELES----------RLEELEEQLETLRSKVAQL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 463 LLQLQEMGNRENLIKMNLERAVGQLENFRSQVIKAtfgktkpfrDKPVTDQQLIERIVQVTEDNlsfqqrkwtlQRETHL 542
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEEL---------LKKLEEAELKELQAELEELE----------EELEEL 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 543 HSKQEEVVHNVEKLRVLLDKCQACMRDSCNSMD-LKKEVELLQHLQLSppVLGLQKAVLNILRvSLSWLEETEQLLGDLn 621
Cdd:TIGR02168 453 QEELERLEEALEELREELEEAEQALDAAERELAqLQARLDSLERLQEN--LEGFSEGVKALLK-NQSGLSGILGVLSEL- 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 622 IElsdSDKGFSLCL-IYLLEHYKKIMIQSEelraqvNASLETQQSLQEENLAEKEKLTEKLEQEEKLKAR---IQQLTEE 697
Cdd:TIGR02168 529 IS---VDEGYEAAIeAALGGRLQAVVVENL------NAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNdreILKNIEG 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 698 KAALEESVAEEKNKLQGDLEMTQARVH---ELENDLACQKE-------------------------VLESSVTQEKRKMR 749
Cdd:TIGR02168 600 FLGVAKDLVKFDPKLRKALSYLLGGVLvvdDLDNALELAKKlrpgyrivtldgdlvrpggvitggsAKTNSSILERRREI 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 750 EVLEAERRKAQDLENQLTQQKEISESNTYEklkMRDTLEKEKRRIQDLENRLTKQREEIELKGQKEDILNNKLKDALLLV 829
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEE---LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 830 EDAQQMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDRLKLQQQSMKALQDERESQKHGF---EEEITEYKEQIKQH 906
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAAT 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 907 SQTIVNLEERLSQVTQYYRKIEGEIATLKDSDSAQKEEVPQEftivpSLDSSAKEIACDHLIDDLLMAQKEILSQQEIIM 986
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL-----LNERASLEEALALLRSELEELSEELRELESKRS 911
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 987 KLRTDLGEAHTRMSDLRGELSEKQKTELERQVALVRQQNSELSILKAKVVQTTGLVEKKDRELKVLREAL 1056
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
18-84 |
1.90e-16 |
|
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 74.53 E-value: 1.90e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958778178 18 TTIGKHEDSDLVLQSSDIDNHHALIEFNEaEGTFVLQDFNTRNGTFVNECHIQNVAVKLIPGDILRF 84
Cdd:pfam00498 1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDG-GGRFYLEDLGSTNGTFVNGQRLGPEPVRLKDGDVIRL 66
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
11-87 |
5.65e-16 |
|
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.
Pssm-ID: 438714 [Multi-domain] Cd Length: 92 Bit Score: 74.23 E-value: 5.65e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958778178 11 FFVLKKSTTIGKHEDSDLVLQSSDIDNHHALIEFNeaEGTFVLQDFNTRNGTFVNECHIQNvAVKLIPGDILRFGSS 87
Cdd:cd00060 14 FPLTKGVVTIGRSPDCDIVLDDPSVSRRHARIEVD--GGGVYLEDLGSTNGTFVNGKRITP-PVPLQDGDVIRLGDT 87
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
640-919 |
1.42e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.29 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 640 EHYKKIMIQSEELRAQVNA----SLETQQSLQEENLAEKEKLTEKLEQE-EKLKARIQQLTEEKAALEESVAEeknkLQG 714
Cdd:COG1196 213 ERYRELKEELKELEAELLLlklrELEAELEELEAELEELEAELEELEAElAELEAELEELRLELEELELELEE----AQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 715 DLEMTQARVHELENDLACQKEVLESSVTQEKRKMREVLEAERRKAQDLENQLTQQKEISESNTYEKLKMRDTLEKEKRRI 794
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 795 QDLENRLTKQREEIELKGQKEDILNNKLKDALLLVEDAQQMRTAESTRAEklslkLKETLAELEITKAKMIMAEDRLKLQ 874
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER-----LEEELEELEEALAELEEEEEEEEEA 443
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1958778178 875 QQSMKALQDERESQKHGFEEEITEYKEQIKQHSQTIVNLEERLSQ 919
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
648-1140 |
1.56e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.91 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 648 QSEELRAQVNASLETQQSLQEENLAEKEKLTEKLEQEEKLKARIQQLTEEKAALEE----------SVAEEKNKLQGDLE 717
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEErrreleerleELEEELAELEEELE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 718 MTQARVHELENDLACQKEVLESSVTQEKRKMREVLEAERRKAQDLENQLTQQKEISESNTyEKLKMRDTLEKEKRRIQDL 797
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR-AAAELAAQLEELEEAEEAL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 798 ENRLTKQREEIELKGQKEDILNNKLKDALLLVEDAQQMRTAESTRAEKLSLKLKETLAELEITKAKMImAEDRLKLQQQS 877
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA-ELLEELAEAAA 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 878 MKALQDERESQKHGFEEEITEYKEQIKQHS----------------------------QTIVNLEERLSQVTQYYRKIEG 929
Cdd:COG1196 492 RLLLLLEAEADYEGFLEGVKAALLLAGLRGlagavavligveaayeaaleaalaaalqNIVVEDDEVAAAAIEYLKAAKA 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 930 EIATLKDSDSAQKEEVPQEFTIVPSLDSSAKEIACD--------HLIDDLL----MAQKEILSQQEIIMKLRTDLGEAHT 997
Cdd:COG1196 572 GRATFLPLDKIRARAALAAALARGAIGAAVDLVASDlreadaryYVLGDTLlgrtLVAARLEAALRRAVTLAGRLREVTL 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 998 RMSDLRGELSEKQKTELERQVALVRQQNSELSILKAKVVQTTGLVEKKDRELKVLREALRASQEKPRPYLSTEQKPRNLS 1077
Cdd:COG1196 652 EGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE 731
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958778178 1078 QKCDISLQIEPAHPDsfssFQEEQFFSDLGAkckgsrhEEVIQRQKKALSELRTRIKELEKAN 1140
Cdd:COG1196 732 AEREELLEELLEEEE----LLEEEALEELPE-------PPDLEELERELERLEREIEALGPVN 783
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
225-936 |
3.68e-15 |
|
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: 80.88 E-value: 3.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 225 LGREINRLSDFEMESKYKD-----AVIMNLQAEIADLSQRLSEMAAVVAAAR-QSNRCDPRFQDLDEGDDHRQKEIESMK 298
Cdd:TIGR02169 277 LNKKIKDLGEEEQLRVKEKigeleAEIASLERSIAEKERELEDAEERLAKLEaEIDKLLAEIEELEREIEEERKRRDKLT 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 299 SQINALQKGY-------------SQVLSQTLAERNTEIESLKNEGENLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEV 365
Cdd:TIGR02169 357 EEYAELKEELedlraeleevdkeFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 366 NQLRIQNKEKEYQLEALTSRCSKLKEDLRKEEAQKERReaqekelklcRSQMQDMEKEVKKLREELKKNYTGQNVISKTL 445
Cdd:TIGR02169 437 NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL----------KEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 446 REKNKVEEKLQEDSRRKLLQLQEMGNRENLIKMNLERAVGQLENF-----------------RSQVIKATFGKTKPFRDK 508
Cdd:TIGR02169 507 RGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNvvveddavakeaiellkRRKAGRATFLPLNKMRDE 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 509 PVTDQQL-----IERIVQVTEDNLSFQQRKWTLQREThlhskqeEVVHNVEKLRVLLDKCQACMRDScnsmdlkkevELL 583
Cdd:TIGR02169 587 RRDLSILsedgvIGFAVDLVEFDPKYEPAFKYVFGDT-------LVVEDIEAARRLMGKYRMVTLEG----------ELF 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 584 QHlqlSPPVLGLQKAVLNILRVSLSWLEETEQL---LGDLNIELSDsdkgfslcLIYLLEHYKKIMIQSEELRAQVNASL 660
Cdd:TIGR02169 650 EK---SGAMTGGSRAPRGGILFSRSEPAELQRLrerLEGLKRELSS--------LQSELRRIENRLDELSQELSDASRKI 718
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 661 ETQQSLQEENLAEKEKLTEKLEQeekLKARIQQLTEEKAALEesvaEEKNKLQGDLEMTQARVHELENDLACQKEVLESS 740
Cdd:TIGR02169 719 GEIEKEIEQLEQEEEKLKERLEE---LEEDLSSLEQEIENVK----SELKELEARIEELEEDLHKLEEALNDLEARLSHS 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 741 VTQEKRKMREVLEAERRKaqdLENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQDLENRLTKQREEIE-LKGQKEDiLN 819
Cdd:TIGR02169 792 RIPEIQAELSKLEEEVSR---IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEnLNGKKEE-LE 867
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 820 NKLKdalllvEDAQQMRTAESTRAEklslkLKETLAELEITKAKMIMAEDRLKLQQQSMKALQDERESQKHGFEEEITEY 899
Cdd:TIGR02169 868 EELE------ELEAALRDLESRLGD-----LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
|
730 740 750
....*....|....*....|....*....|....*..
gi 1958778178 900 KEQIKQhSQTIVNLEERLSQVTQYYRKIEGEIATLKD 936
Cdd:TIGR02169 937 EDPKGE-DEEIPEEELSLEDVQAELQRVEEEIRALEP 972
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
11-93 |
1.23e-14 |
|
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 70.76 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 11 FFVLKKSTTIGKHEDSDLVLQSSDIDNHHALIEFNeaEGTFVLQDFNTRNGTFVNECHIQNvAVKLIPGDILRFGSSGPT 90
Cdd:COG1716 16 FPLDGGPLTIGRAPDNDIVLDDPTVSRRHARIRRD--GGGWVLEDLGSTNGTFVNGQRVTE-PAPLRDGDVIRLGKTELR 92
|
...
gi 1958778178 91 YEL 93
Cdd:COG1716 93 FRL 95
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
4-93 |
5.57e-14 |
|
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) family; The Cep170 family includes Cep170 and Cep170B. Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438756 [Multi-domain] Cd Length: 102 Bit Score: 68.89 E-value: 5.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 4 YLKSPDG-FFVLKKSTTIGKHEDSDLVLQSSDIDNHHALIEFNEAEGTFVLQDFNTRNGTFVNECHI-QNVAVKLIPGDI 81
Cdd:cd22704 3 CLVSSDGtRHRLPRSMLFVGREDCDLILQSRSVDKQHAVITYDQIDNEFKIKDLGSLNGTFVNDSRIpEQTYITLKLGDS 82
|
90
....*....|..
gi 1958778178 82 LRFGSSGPTYEL 93
Cdd:cd22704 83 IRFGYDTNVYRF 94
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
250-858 |
9.16e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.05 E-value: 9.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 250 QAEIA----DLSQRLSEMAAVVAAARqsnrcdprfqdldegDDHRQKEIESMKSQINALQKGySQVLSQTLAERNTEIES 325
Cdd:COG1196 208 QAEKAeryrELKEELKELEAELLLLK---------------LRELEAELEELEAELEELEAE-LEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 326 LKNEGENLKRDqaitsgmVTSLQKDVSARNEQVQQLQEEVNQLRIQNKEKEYQLEALTSRCSKLKEDLRKEEAQKERREA 405
Cdd:COG1196 272 LRLELEELELE-------LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 406 QEKELKLCRSQMQDMEKEVKKLREELKKNYTGQNVISKTLREKNKVEEKLQEDSRRKLLQLQEMGNRENLIKMNLERAVG 485
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 486 QLENFRSQVIKATFGKTKPFRDKPVTDQQLIERIVQVTEDNLsfQQRKWTLQRETHLHSKQEEVVHNVEKLRVLLDkcqa 565
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA--ELLEEAALLEAALAELLEELAEAAARLLLLLE---- 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 566 cMRDscnSMDLKKEVELLQHLQLSPPVLGLQKAVLNILRVSLSWLEETEQLLGDLNIELSDSDKGfslcliyllehykKI 645
Cdd:COG1196 499 -AEA---DYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVA-------------AA 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 646 MIQSEELRAQVNASLETQQSLQEENLAEKEKLTEKLEQEEKLKARIQQLTEEKAALEESVAEEKNKLQGDLEMTQARVHE 725
Cdd:COG1196 562 AIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVT 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 726 LENDLAC----QKEVLESSVTQEKRKMREVLEAERRKAQDLENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQDLENRL 801
Cdd:COG1196 642 LAGRLREvtleGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEEL 721
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958778178 802 TKQREEIELKGQKEDILNNKLKDALLLVEDAQQMRTAESTRAEklslkLKETLAELE 858
Cdd:COG1196 722 EEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE-----LERELERLE 773
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
18-85 |
1.16e-11 |
|
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; MDC1, also called nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438717 [Multi-domain] Cd Length: 97 Bit Score: 62.25 E-value: 1.16e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 18 TTIGKHEDSDLVLQSSDIDNHHALIEFneAEGTFVLQDFNTRNGTFVNECHI--QNVAVKLIPGDILRFG 85
Cdd:cd22665 23 NVIGRDPSCSVVLPDKSVSKQHACIEV--DGGTHLIEDLGSTNGTRIGNKVRlkPNVRYELIDGDLLLFG 90
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
225-1058 |
2.69e-11 |
|
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: 68.22 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 225 LGREINRLSDFEMESK-YKDAVIMNLQAEIADLSQRLSEMAAVVAAARQS-----NRCDPRFQDLDEGDDHRQKEIESMK 298
Cdd:pfam15921 90 LQRRLNESNELHEKQKfYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSqedlrNQLQNTVHELEAAKCLKEDMLEDSN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 299 SQINALQK---GYSQVLSQTlaeRNTEIESLKNEGENLKRDQAITSGMVTSLQkdvSARNEQVQQLQEEVNQLRIQNKEK 375
Cdd:pfam15921 170 TQIEQLRKmmlSHEGVLQEI---RSILVDFEEASGKKIYEHDSMSTMHFRSLG---SAISKILRELDTEISYLKGRIFPV 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 376 EYQLEALTSRCSKLKEDLRKEEAQKERREAQEKELklcrsQMQDMEKEVKKLREELKKNYTGQNVISKTLREKNKVEEKL 455
Cdd:pfam15921 244 EDQLEALKSESQNKIELLLQQHQDRIEQLISEHEV-----EITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQ 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 456 QEDSRRKLLQLQ-EMGNRENLIKMNLERAVGQLENFRSQVIKATFGKTKPFRDKPVTDQQLIERIVQV----TEDNLSFQ 530
Cdd:pfam15921 319 LSDLESTVSQLRsELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLhkreKELSLEKE 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 531 QRKWTLQRET-------HLHSKQEEVVHNVEKLRVLL----DKCQACMRDSCNSMDLKKE-VELLQHL--QLSPPVLGLQ 596
Cdd:pfam15921 399 QNKRLWDRDTgnsitidHLRRELDDRNMEVQRLEALLkamkSECQGQMERQMAAIQGKNEsLEKVSSLtaQLESTKEMLR 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 597 KAVLNILRVSLSwLEETEQLLGDLNIELSDSDKGFSLCLIYLLEHYKKIMIQSEELRAQVNASlETQQSLQEENLAEKEK 676
Cdd:pfam15921 479 KVVEELTAKKMT-LESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEG-DHLRNVQTECEALKLQ 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 677 LTEKLEQEEKLKARIQQLTEekaaleesVAEEKNKLQGDLEMTQARVHELENDLacQKEVLESSVTQEKR--KMREvLEA 754
Cdd:pfam15921 557 MAEKDKVIEILRQQIENMTQ--------LVGQHGRTAGAMQVEKAQLEKEINDR--RLELQEFKILKDKKdaKIRE-LEA 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 755 errKAQDLEnqltqqkeisesntYEKLKMRDTLEKEKRRIQDLEnrltKQREEI--ELKGQKEDiLNNKLKDALLLVEDA 832
Cdd:pfam15921 626 ---RVSDLE--------------LEKVKLVNAGSERLRAVKDIK----QERDQLlnEVKTSRNE-LNSLSEDYEVLKRNF 683
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 833 QQMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDR--------LKLQQQ--SMKALQDERESQKHGFEEEITEYKEQ 902
Cdd:pfam15921 684 RNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSdghamkvaMGMQKQitAKRGQIDALQSKIQFLEEAMTNANKE 763
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 903 IKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKDSDSAQKEEVPQeftIVPSLDSSAKEIA-CDHLIddllmaQKEilSQ 981
Cdd:pfam15921 764 KHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVAN---MEVALDKASLQFAeCQDII------QRQ--EQ 832
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 982 QEIIMKLRTDL------GEAHTRMSDLRGELSekQKTELERQVALVRQQNSELSILKAKVVQTTGLVEKKDRELKVLREA 1055
Cdd:pfam15921 833 ESVRLKLQHTLdvkelqGPGYTSNSSMKPRLL--QPASFTRTHSNVPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQE 910
|
...
gi 1958778178 1056 LRA 1058
Cdd:pfam15921 911 LRS 913
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
19-87 |
5.20e-11 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaB and similar proteins; FhaB, also called FtsZ-interacting protein A (FipA), is a putative virulence factor involved in regulating cell shape. It can interact with polyketide-associated protein PapA5, a putative membrane protein involved in the biosynthesis of virulence enhancing lipids. FhaB regulates growth and cell division. It is probably required for divisomal protein assembly under oxidative stress. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438745 [Multi-domain] Cd Length: 91 Bit Score: 60.01 E-value: 5.20e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958778178 19 TIGKHEDSDLVLQSSDIDNHHALIEFNEaeGTFVLQDFNTRNGTFVNECHIqNVAVKLIPGDILRFGSS 87
Cdd:cd22693 21 TIGRADDNDLVLSDDFVSSRHARIYLQG--SSWYLEDLGSTNGTFVNGNRV-TQPVVVQPGDTIRIGAT 86
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
319-947 |
8.57e-11 |
|
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: 66.58 E-value: 8.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 319 RNTEIESLKNEGENLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEVNQLRIQNKEKEYQLEALTSRCSKLKEDLRKeea 398
Cdd:TIGR04523 31 QDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSK--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 399 qkerreaQEKELKLCRSQMQDMEKEVKKLREELKKNYTGQNVISKTLREKNKVEEKLQEDSRRKLLQLQEMGNRENLIKM 478
Cdd:TIGR04523 108 -------INSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 479 NLERAVGQLENFRSQVIKATFG----KTKPFRDKPVTDQQL-IERIVQVTEDNLSFQQRKWTlQRETHLHSKQEEVVHNV 553
Cdd:TIGR04523 181 EKLNIQKNIDKIKNKLLKLELLlsnlKKKIQKNKSLESQISeLKKQNNQLKDNIEKKQQEIN-EKTTEISNTQTQLNQLK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 554 EKLRVLLDKCQACMRDSCNSMDLKKEVE-LLQHLQLSPPVLGLQKAVlNILRVSLSWLEETEQLLGDLNIELSDSDKGFS 632
Cdd:TIGR04523 260 DEQNKIKKQLSEKQKELEQNNKKIKELEkQLNQLKSEISDLNNQKEQ-DWNKELKSELKNQEKKLEEIQNQISQNNKIIS 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 633 lcliyllehykkimiqseELRAQVNASLETQQSLQEENLAEKEKLTEKLEQEEKLKARIQQLTEEKAALEESVAEEKNKL 712
Cdd:TIGR04523 339 ------------------QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 713 QGDLEMTQARVHELENdLACQKEVLEssvtQEKRKMREVLEAERRKAQDLENQLTQQKEISESNTYEKLKMRDTLEKEKR 792
Cdd:TIGR04523 401 QNQEKLNQQKDEQIKK-LQQEKELLE----KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 793 RIQDLENRLTKQREEIELKGQKEDILNNKLKDALLLVEDAQQMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDR-- 870
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFElk 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 871 -----------------LKLQQQSMKALQDERESQKHGFEEEITEYKEQIKQHSQTIVNLEERLSQVTQYYRKIEGEIAT 933
Cdd:TIGR04523 556 kenlekeideknkeieeLKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKN 635
|
650
....*....|....
gi 1958778178 934 LKDSDSAQKEEVPQ 947
Cdd:TIGR04523 636 IKSKKNKLKQEVKQ 649
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
650-948 |
8.93e-11 |
|
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: 66.63 E-value: 8.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 650 EELRAQVNASLETQQSLQEEnlaeKEKLTEKLEQEEKLKARIQQLTEEKAA-LEESVAEEKNKLQGDLEMTQARVHELEN 728
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEE----LEKLTEEISELEKRLEEIEQLLEELNKkIKDLGEEEQLRVKEKIGELEAEIASLER 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 729 DLACQKEVLESSVTQEkRKMREVLEAERRKAQDLENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQDLENRLTKQREEI 808
Cdd:TIGR02169 309 SIAEKERELEDAEERL-AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 809 ELKGQKEDILNNKLkdalllvEDAQQMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDRLKLQQQSMKALQDERESQ 888
Cdd:TIGR02169 388 KDYREKLEKLKREI-------NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 889 KhgfeEEITEYKEQIKQHSQTIVNLEERLSQVTQYYRKIEgeiATLKDSDSAQKEEVPQE 948
Cdd:TIGR02169 461 A----ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAE---AQARASEERVRGGRAVE 513
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
351-907 |
1.30e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.86 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 351 VSARNEQVQQLQEEVNQLRIQNKEKEYQLEALTSRCSKLKEDLRKEEAQKERREAQEKELKlcrsQMQDMEKEVKKLREE 430
Cdd:PRK03918 226 LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK----ELKEKAEEYIKLSEF 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 431 LKKNYTGQNVISKTL----REKNKVEEKLQEDSRRKlLQLQEMGNRENLIKMNLERAVGQLENF-RSQVIKATFGKTKPf 505
Cdd:PRK03918 302 YEEYLDELREIEKRLsrleEEINGIEERIKELEEKE-ERLEELKKKLKELEKRLEELEERHELYeEAKAKKEELERLKK- 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 506 RDKPVTDQQLIERIVQVTEDNLSFQ-QRKWTLQRETHLHSKQEEVVHNVEKLRVLLDKCQACMRDscnsMDLKKEVELLQ 584
Cdd:PRK03918 380 RLTGLTPEKLEKELEELEKAKEEIEeEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRE----LTEEHRKELLE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 585 HLQLSppvlglqkavlniLRVSLSWLEETEQLLGDLNIELSDSDKgfslcliyLLEHYKKImIQSEELRAQVNaslETQQ 664
Cdd:PRK03918 456 EYTAE-------------LKRIEKELKEIEEKERKLRKELRELEK--------VLKKESEL-IKLKELAEQLK---ELEE 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 665 SLQEENLaekEKLTEKLEQEEKLKARIQQLTEEKAALEESVaEEKNKLQGDLEMTQARVHELENDLACQKEVLE----SS 740
Cdd:PRK03918 511 KLKKYNL---EELEKKAEEYEKLKEKLIKLKGEIKSLKKEL-EKLEELKKKLAELEKKLDELEEELAELLKELEelgfES 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 741 VTQEKRKMREVLEAERR--KAQDLENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQDLENRLtkqrEEIELKGQKEDil 818
Cdd:PRK03918 587 VEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL----EELEKKYSEEE-- 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 819 NNKLKDALLLVEDAQQMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDRLKLQQQSMKALQDEResqkhgfeEEITE 898
Cdd:PRK03918 661 YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELR--------EKVKK 732
|
....*....
gi 1958778178 899 YKEQIKQHS 907
Cdd:PRK03918 733 YKALLKERA 741
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
281-1034 |
2.25e-10 |
|
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: 65.38 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 281 QDLDEGDDHRQKEIESMKSQINALQKGYSQVLSQTLAERNTEIESLKNEGENLKRDQAITSGMVTSLQKDVSARNEQVQQ 360
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKK 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 361 LQEEVNQLRIQNKEKEYQLEALTSRCSKLKEDLRKEEAQKERREAQEKELKLCRSQMQDMEKEVKKLREELKKNYTGQNV 440
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLE 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 441 ISKTLREKNKVEEKLQEDSRRKLLQLQEMGNRENLIKMNLERAVGQLENFRSQVIKATFGKTKPFRDKPV-TDQQLIERI 519
Cdd:pfam02463 413 LARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLqEQLELLLSR 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 520 VQVTEDNLSFQQRKWTLQRETHLHSKQEEVVHNVEKLR-------VLLDKCQACMRDSCNSMDLKKEVELLQHLQLSPPV 592
Cdd:pfam02463 493 QKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRlgdlgvaVENYKVAISTAVIVEVSATADEVEERQKLVRALTE 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 593 LGLQKAVLNILRVSLSWleeteqllgdlnIELSDSDKGFSLCLIYLLEHYKKIMIQSEELRAQVNASLETQQSLQEENLA 672
Cdd:pfam02463 573 LPLGARKLRLLIPKLKL------------PLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKES 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 673 EKEKLTEK-----LEQEEKLKARIQQLTEEKAALEESVAEEKNKLQGDLEMTQARVHELENDLACQKEVLES-SVTQEKR 746
Cdd:pfam02463 641 AKAKESGLrkgvsLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELkKLKLEAE 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 747 KMREVLEAERRKAQDLENQLTQQKEISESNTYEKLKM-RDTLEKEKRRIQDLENRLTKQREEIELKGQKEDILNNKLKDA 825
Cdd:pfam02463 721 ELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLkKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQE 800
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 826 LLLVEDAQQMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDRLKLQQ--------QSMKALQDERESQKHGFEEEIT 897
Cdd:pfam02463 801 EELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKlaeeelerLEEEITKEELLQELLLKEEELE 880
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 898 EYKEQIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKD-SDSAQKEEVPQEFTIVPSLDSSAKEIACDHLIDDLLMAQK 976
Cdd:pfam02463 881 EQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIeERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEE 960
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958778178 977 EILSQQEIIMKLRTDLGEAHTRMSDLRgELSEKQKTELERQVALVRQQNSELSILKAK 1034
Cdd:pfam02463 961 RNKRLLLAKEELGKVNLMAIEEFEEKE-ERYNKDELEKERLEEEKKKLIRAIIEETCQ 1017
|
|
| FHA_Ki67 |
cd22673 |
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ... |
11-85 |
7.70e-10 |
|
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar proteins; Ki-67, also called antigen identified by monoclonal antibody Ki-67, antigen KI-67, or antigen Ki67, acts as a biological surfactant to disperse mitotic chromosomes. It is required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. Ki-67 binds DNA with a preference for supercoiled DNA and AT-rich DNA. It may also play a role in chromatin organization. Ki-67 contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438725 [Multi-domain] Cd Length: 95 Bit Score: 56.84 E-value: 7.70e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958778178 11 FFVLKKSTTIGKHEDSDLVLQSSDIDNHHALIEFNEaEGTFVLQDFNTRNGTFVNECHIQNvAVKLIPGDILRFG 85
Cdd:cd22673 16 FPLTKKSCTFGRDLSCDIRIQLPGVSREHCRIEVDE-NGKAYLENLSTTNPTLVNGKAIEK-SAELKDGDVITIG 88
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
674-1058 |
1.13e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 674 KEKLTEKLEQ-EEKLkARIQQLTEEKAA----LEE--SVAEEKNKLQGDLEMTQARVHELENDLACQKEVLESSVTQEKR 746
Cdd:COG1196 174 KEEAERKLEAtEENL-ERLEDILGELERqlepLERqaEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 747 KMREVLEAERRKaqdLENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQDLENRLTKQREEIELKGQKEDILNNKLKDAL 826
Cdd:COG1196 253 AELEELEAELAE---LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 827 LLVEDAQQMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDRLKLQQQSMKALQDERESQkhgfEEEITEYKEQIKQH 906
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA----LRAAAELAAQLEEL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 907 SQTIVNLEERLSQVTQYYRKIEGEIATLKDSDSAQKEEVpqeftivpsldssakeiacDHLIDDLLMAQKEILSQQEIIM 986
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL-------------------EEAAEEEAELEEEEEALLELLA 466
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958778178 987 KLRTDLGEAHTRMSDLRGELSEKQKTELERQVALVRQQNSELSILKAKVVQTTGLVEKKDRELKVLREALRA 1058
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA 538
|
|
| FHA_DUN1-like |
cd22683 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ... |
15-85 |
1.85e-09 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein kinase DUN1 and similar proteins; DUN1 is a protein kinase that controls the DNA damage response in yeast. It phosphorylates SML1 on serine residues and cooperates with the PAN deadenylation complex in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438735 [Multi-domain] Cd Length: 96 Bit Score: 55.96 E-value: 1.85e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958778178 15 KKSTTIGKHEDSDLVLQSSDIDNHHALIEFnEAEGTFVLqDFNTRNGTFVNECHIQNVAVKLIPGDILRFG 85
Cdd:cd22683 20 RNVTTIGRSRSCDLVLSDPSISRFHAELRL-EQNGINVI-DNNSANGTFINGKRIKGKTYILKNGDIIVFG 88
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
672-1155 |
1.92e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 672 AEKEKLTEKLEQEEKLKARIQQLTEEKAALEESVAE---EKNKLQGDLEMTQARVHELE------NDLACQKEVLESSVT 742
Cdd:PRK03918 176 RRIERLEKFIKRTENIEELIKEKEKELEEVLREINEissELPELREELEKLEKEVKELEelkeeiEELEKELESLEGSKR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 743 QEKRKMREV---LEAERRKAQDLENQLTQQKEISES-NTYEKL-KMRDTLEKEKRRIQDLENRLTKQREEIELKGQKedi 817
Cdd:PRK03918 256 KLEEKIRELeerIEELKKEIEELEEKVKELKELKEKaEEYIKLsEFYEEYLDELREIEKRLSRLEEEINGIEERIKE--- 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 818 LNNKlkdalllvedaqqmrtaeSTRAEKLSLKLKETLAELEITKAKMIMAEDrlklqqqsMKALQDERESQKHGFE-EEI 896
Cdd:PRK03918 333 LEEK------------------EERLEELKKKLKELEKRLEELEERHELYEE--------AKAKKEELERLKKRLTgLTP 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 897 TEYKEQIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKDS------------------DSAQKEEVPQEFTIvpSLDSS 958
Cdd:PRK03918 387 EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAieelkkakgkcpvcgrelTEEHRKELLEEYTA--ELKRI 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 959 AKEIA-CDHLIDDLLMAQKEI---LSQQEIIMKLRTDLGEahtrMSDLRGELSEKQKTELERQVALVRQQNSELSILKAK 1034
Cdd:PRK03918 465 EKELKeIEEKERKLRKELRELekvLKKESELIKLKELAEQ----LKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 1035 VVQTTGLVEKKDRELKVLREALRASQEKPRPYLSTEQKPRNLSQKCDISL-----QIEPAHPDSFSSFQEEQFFSDLGAK 1109
Cdd:PRK03918 541 IKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELeerlkELEPFYNEYLELKDAEKELEREEKE 620
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1958778178 1110 CKGSRHE-----EVIQRQKKALSELRTRIKELEKANSSNHKDHVNESFLEL 1155
Cdd:PRK03918 621 LKKLEEEldkafEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLEL 671
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
358-808 |
3.92e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 3.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 358 VQQLQEEVNQL-RIQNKEKEYQLEALtsrcSKLKEDLRKEEAQKERREAQEKELKLCRSQMQDMEKEVKKLREELKKnYT 436
Cdd:COG4717 48 LERLEKEADELfKPQGRKPELNLKEL----KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK-LE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 437 GQNVISKTLREKNKVEEKLQEDSRRKLLQLQEMGNRENLIKmnleravgQLENFRSQVIKATFGKTKPFRDKPVTDQQLI 516
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEE--------ELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 517 ERIVQVTEDnlsFQQRKWTLQREthLHSKQEEvvhnVEKLRVLLDKCQACMRDSCNSMDLKKEVELL------------- 583
Cdd:COG4717 195 QDLAEELEE---LQQRLAELEEE--LEEAQEE----LEELEEELEQLENELEAAALEERLKEARLLLliaaallallglg 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 584 -QHLQLSPPVLGLQKAVLNILRVSLSWLEETEQLLGDLNIELSDSDKGFSLCLIYLLEHYKKIMIQSEELRAQVNASLET 662
Cdd:COG4717 266 gSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDR 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 663 QQSLQEEnLAEKEKLTEKLEQEEkLKARIQQLTEEKAALEESVAEEKNKLQGDLEMTQARVHELENDLACQ-KEVLESSV 741
Cdd:COG4717 346 IEELQEL-LREAEELEEELQLEE-LEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELlGELEELLE 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958778178 742 TQEKRKMREVLEAERRKAQDLENQLTQ-QKEISE-SNTYEKLKMRDTLEKEKRRIQDLENRLTKQREEI 808
Cdd:COG4717 424 ALDEEELEEELEELEEELEELEEELEElREELAElEAELEQLEEDGELAELLQELEELKAELRELAEEW 492
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
592-1161 |
4.92e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.82 E-value: 4.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 592 VLGLQKAVLNILRVSLSWLEETE--QLLGDLNIELSDSDKgfslcliyLLEHYkkimiqsEELRAQVNASLETQQSLQEE 669
Cdd:PRK02224 181 VLSDQRGSLDQLKAQIEEKEEKDlhERLNGLESELAELDE--------EIERY-------EEQREQARETRDEADEVLEE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 670 NLAEKEKLTEkLEQE-EKLKARIQQLTEEKAALEESVAEEKNKLQGDLEMTQARVHELENDLACQKEVLESSVTQEKRK- 747
Cdd:PRK02224 246 HEERREELET-LEAEiEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDe 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 748 -MREVLEAERRKAQDLENQltqqkeiSESNTYEKLKMRDTLEKEKRRIQDLENRLTKQREEIELKGQKEDILNNKLKDAL 826
Cdd:PRK02224 325 eLRDRLEECRVAAQAHNEE-------AESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELR 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 827 LLVEDAQQMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDRLKLQQQsmkaLQDERESQKHGFEEEITEYKEQIKQH 906
Cdd:PRK02224 398 ERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA----LLEAGKCPECGQPVEGSPHVETIEED 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 907 SQTIVNLEERLSQVTQYYRKIEGEIATLKDSDSAQKEevpqeftiVPSLDSSAKEIacDHLIDDllmAQKEILSQQEIIM 986
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDR--------IERLEERREDL--EELIAE---RRETIEEKRERAE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 987 KLRTDLGEAHTRMSDLRgELSEKQKTELERQVALVRQQNSELSILK------AKVVQTTGLVEKKDRELKVLREALRASQ 1060
Cdd:PRK02224 541 ELRERAAELEAEAEEKR-EAAAEAEEEAEEAREEVAELNSKLAELKerieslERIRTLLAAIADAEDEIERLREKREALA 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 1061 EKprpylsTEQKPRNLSQKCDISLQIEpahpdsfSSFQEEQFfsdLGAKCKGSRHEEVIQRQKKALSELRTRIKELEKAN 1140
Cdd:PRK02224 620 EL------NDERRERLAEKRERKRELE-------AEFDEARI---EEAREDKERAEEYLEQVEEKLDELREERDDLQAEI 683
|
570 580
....*....|....*....|.
gi 1958778178 1141 SSnhkdhVNESFLELKTLRME 1161
Cdd:PRK02224 684 GA-----VENELEELEELRER 699
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
317-887 |
5.05e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.82 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 317 AERNTEIESLKNEGENLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEVNQLRIQNKEKEYQLEALtsrcsklkeDLRKE 396
Cdd:PRK02224 247 EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAV---------EARRE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 397 EAQKERREAQEkELKLCRSQMQDMEKEVKKLREELKKNYTGqnviSKTLREKNKVEEKLQEDSRRKLlqlqemgnrenli 476
Cdd:PRK02224 318 ELEDRDEELRD-RLEECRVAAQAHNEEAESLREDADDLEER----AEELREEAAELESELEEAREAV------------- 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 477 kmnlERAVGQLENFRSQVIKATfgktKPFRDKPVTDQQLIERIVQVTEDnlsfqqRKWTLQRETHLHSKQEEVVHNVEKL 556
Cdd:PRK02224 380 ----EDRREEIEELEEEIEELR----ERFGDAPVDLGNAEDFLEELREE------RDELREREAELEATLRTARERVEEA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 557 RVLLD--KCQACMrdscnsmdlkkevellQHLQLSPPVLGLqkavlnilrvslswlEETEQLLGDLNIELSDsdkgfslc 634
Cdd:PRK02224 446 EALLEagKCPECG----------------QPVEGSPHVETI---------------EEDRERVEELEAELED-------- 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 635 liyllehykkimiqseelraqvnasLETQQSLQEENLAEKEKLTEkleqeekLKARIQQLTEEKAALEESVAEEKNKLQG 714
Cdd:PRK02224 487 -------------------------LEEEVEEVEERLERAEDLVE-------AEDRIERLEERREDLEELIAERRETIEE 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 715 D---LEMTQARVHELENDLACQKEvlessvtqEKRKMREVLEAERRKAQDLENQLTQQKEISES-NTYEKL-----KMRD 785
Cdd:PRK02224 535 KrerAEELRERAAELEAEAEEKRE--------AAAEAEEEAEEAREEVAELNSKLAELKERIESlERIRTLlaaiaDAED 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 786 TLEKEKRRIQDLENRLTKQREEIELKGQKEDILNNKLKDAllLVEDAQQMRTAESTRAEKLSLKLKETLAELEITKAKMI 865
Cdd:PRK02224 607 EIERLREKREALAELNDERRERLAEKRERKRELEAEFDEA--RIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIG 684
|
570 580
....*....|....*....|..
gi 1958778178 866 MAEDRLKlqqqSMKALQDERES 887
Cdd:PRK02224 685 AVENELE----ELEELRERREA 702
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
227-928 |
8.70e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 8.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 227 REINRLSDFEMESKYKDAVIMNLQAEIADLSQRLSemaavvaaarqsnrcdpRFQDLDEGDDHRQKEIESMKSQINALQK 306
Cdd:PRK03918 152 RQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIK-----------------RTENIEELIKEKEKELEEVLREINEISS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 307 GYSQVLSQ--TLAERNTEIESLKNEGENLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEVNQLRIQNKE-KEYQLEALT 383
Cdd:PRK03918 215 ELPELREEleKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElKELKEKAEE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 384 -SRCSKLKEDLRKEEAQKERREAQ-EKELKLCRSQMQDMEKEVKKLREELKKnytgqnvISKTLREKNKVEEKLQ--EDS 459
Cdd:PRK03918 295 yIKLSEFYEEYLDELREIEKRLSRlEEEINGIEERIKELEEKEERLEELKKK-------LKELEKRLEELEERHElyEEA 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 460 RRKLLQLQEMgnRENLIKMNLERAVGQLENFRsqvikatfgktkpfrdkpvtdqqliERIVQVTEDNLSFQQRKwtlqre 539
Cdd:PRK03918 368 KAKKEELERL--KKRLTGLTPEKLEKELEELE-------------------------KAKEEIEEEISKITARI------ 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 540 THLHSKQEEVVHNVEKLRVLLDKCQACMRdscnsmdlkkevELLQhlqlsppvlglqkavlnilrvslswlEETEQLLGD 619
Cdd:PRK03918 415 GELKKEIKELKKAIEELKKAKGKCPVCGR------------ELTE--------------------------EHRKELLEE 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 620 LNIELSDsdkgfslcliyLLEHYKKIMIQSEELRAQVnASLETQQSLQEENLAEKEKLTEKLEQEEKLKARIQQLTEEKA 699
Cdd:PRK03918 457 YTAELKR-----------IEKELKEIEEKERKLRKEL-RELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKA 524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 700 ALEESVAEEKNKLQGDLEMTQARVHELEnDLACQKEVLESSVTQEKRKMREVLEAERRKA----QDLENQLTQQKEISes 775
Cdd:PRK03918 525 EEYEKLKEKLIKLKGEIKSLKKELEKLE-ELKKKLAELEKKLDELEEELAELLKELEELGfesvEELEERLKELEPFY-- 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 776 NTYEKLK-MRDTLEKEKRRIQDLENRLTKQREEIELKGQKEDILNNKLKDALLLVEDAqqmrtaESTRAEKLSLKLKETL 854
Cdd:PRK03918 602 NEYLELKdAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE------EYEELREEYLELSREL 675
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958778178 855 AeleitkakmimaedrlklqqqsmkalqderesqkhGFEEEITEYKEQIKQHSQTIVNLEERLSQVTQYYRKIE 928
Cdd:PRK03918 676 A-----------------------------------GLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE 714
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
743-1070 |
1.34e-08 |
|
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: 59.31 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 743 QEKRKMRE----VLEAERRKAQDLEN--QLTQQKEISESNTYEKLKMRDTLEKEK----------RRIQDLE-------- 798
Cdd:TIGR02169 153 VERRKIIDeiagVAEFDRKKEKALEEleEVEENIERLDLIIDEKRQQLERLRRERekaeryqallKEKREYEgyellkek 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 799 NRLTKQREEI--ELKGQKEDI--LNNKLKDALLLVEDAQQMRTAESTRAEKLS----LKLKETLAELEITKAKMIMAEDR 870
Cdd:TIGR02169 233 EALERQKEAIerQLASLEEELekLTEEISELEKRLEEIEQLLEELNKKIKDLGeeeqLRVKEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 871 LKLQQQSMKALQDERESQKHGFEEEITEYKEQIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKDSDSAQKEEVPQEFT 950
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 951 IVPSLDSSAKEI--ACDHLIDDLLMAQKEILSQQEIIMKLRTDLGEAHTRMSDLRGELsEKQKTELERQVALVRQQNSEL 1028
Cdd:TIGR02169 393 KLEKLKREINELkrELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI-KKQEWKLEQLAADLSKYEQEL 471
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1958778178 1029 SILKAKVVQTTGLVEKKDRELKVLREALRASQEKPRPYLSTE 1070
Cdd:TIGR02169 472 YDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVE 513
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
313-807 |
2.42e-08 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 58.21 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 313 SQTLAERNTEIESLKNEGENLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEVNQLRIQNKEKEYQLEALTSRCSKLKEd 392
Cdd:pfam05557 96 ESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKE- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 393 LRKEEAQKERREAQEKELKLCRSQMQDMEKEVKKLREELKKnytgqnvISKTLREKNKVEEKLqEDSRRKLLQLQEMgnR 472
Cdd:pfam05557 175 LEFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNKH-------LNENIENKLLLKEEV-EDLKRKLEREEKY--R 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 473 ENLIKMNLERAVGQLENFRSQVIKATFGKTKpfrdkpVTDQQLIERIVQVTEDNLSFQQRKWTLQRET-HLHSKQEEVVH 551
Cdd:pfam05557 245 EEAATLELEKEKLEQELQSWVKLAQDTGLNL------RSPEDLSRRIEQLQQREIVLKEENSSLTSSArQLEKARRELEQ 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 552 nveKLRVLLDKCQacmrdscnsmDLKKEVELLQHLqlsppVLGLQKAVLNILRVSLSWLEETEQLLGDLNieLSDSDKGF 631
Cdd:pfam05557 319 ---ELAQYLKKIE----------DLNKKLKRHKAL-----VRRLQRRVLLLTKERDGYRAILESYDKELT--MSNYSPQL 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 632 SLCLIYLLEHYKKIMIQSEELRAQVNASLET-------------------QQSLQEENLAEKEKLTEKLEQEEKLKARIQ 692
Cdd:pfam05557 379 LERIEEAEDMTQKMQAHNEEMEAQLSVAEEElggykqqaqtlerelqalrQQESLADPSYSKEEVDSLRRKLETLELERQ 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 693 QLTEEKAALEESVaeEKNKLQGDLEMTQARVHELENDLACQKEvlessvtQEKRKMREVLEAE--------RRKAQDLEN 764
Cdd:pfam05557 459 RLREQKNELEMEL--ERRCLQGDYDPKKTKVLHLSMNPAAEAY-------QQRKNQLEKLQAEierlkrllKKLEDDLEQ 529
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1958778178 765 QLTQQKEISESNTYEKLKMRDTLEKEKRRIQDLENRLTKQREE 807
Cdd:pfam05557 530 VLRLPETTSTMNFKEVLDLRKELESAELKNQRLKEVFQAKIQE 572
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
317-707 |
2.86e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 317 AERNTEIESLKNEGENLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEVNQLR-------IQNKEKEYQLEALTSRCSKL 389
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRkeleelsRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 390 KEDLRKEEAQKERREAQEKELKLCRSQMQDMEKEVKKLREELKKNYTGQN----VISKTLREKNKVEEKLQEDSRRKLLQ 465
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKeelkALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 466 LQEMGNRENLIKMNLERAVGQLENFRSQVIKATfgktkpfrdKPVTDQQliERIVQVTEDNLSFQQRKWTLQRETHLHSK 545
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLA---------AEIEELE--ELIEELESELEALLNERASLEEALALLRS 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 546 QEEVVhnVEKLRVLLDKCQacmrdscnsmDLKKEVELLQHlQLSPPVLGLQKAVLNILRVslswleeTEQLLGDLNIELS 625
Cdd:TIGR02168 895 ELEEL--SEELRELESKRS----------ELRRELEELRE-KLAQLELRLEGLEVRIDNL-------QERLSEEYSLTLE 954
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 626 DsdkgfslcliyLLEHYKKIMIQSEELRAQVnASLETQ-QSLQEENLAEKEKLTEKLEQEEKLKARIQQLTEEKAALEES 704
Cdd:TIGR02168 955 E-----------AEALENKIEDDEEEARRRL-KRLENKiKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEA 1022
|
...
gi 1958778178 705 VAE 707
Cdd:TIGR02168 1023 IEE 1025
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
5-94 |
3.11e-08 |
|
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the first FHA domain. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438746 [Multi-domain] Cd Length: 93 Bit Score: 52.33 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 5 LKSPDGFFVLK--KSTTIGKHEDSDLVLQSSDIDNHHALIEFneAEGTFVLQDFNTRNGTFVNECHIQnvAVKLIPGDIL 82
Cdd:cd22694 3 IRIPGGELRFDpgSSVRIGRDPDADVRLDDPRVSRRHALLEF--DGDGWVYTDLGSRNGTYLNGRRVQ--QVKLSDGTRV 78
|
90
....*....|....
gi 1958778178 83 RFG--SSGPTYELV 94
Cdd:cd22694 79 RLGdpTDGPALTVV 92
|
|
| FHA_Cep170B |
cd22725 |
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) ... |
24-93 |
4.07e-08 |
|
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) and similar proteins; Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438777 [Multi-domain] Cd Length: 106 Bit Score: 52.62 E-value: 4.07e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958778178 24 EDSDLVLQSSDIDNHHALIEFNEAEGTFVLQDFNTRNGTFVNECHIQN---VAVKLipGDILRFGSSGPTYEL 93
Cdd:cd22725 28 EDCELMLQSRSVDKQHAVINYDQDTDEHWVKDLGSLNGTFVNDVRIPDqkyITLKL--NDVIRFGYDSNMYVL 98
|
|
| FHA_Cep170A |
cd22724 |
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar ... |
24-85 |
4.61e-08 |
|
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar proteins; Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438776 [Multi-domain] Cd Length: 106 Bit Score: 52.28 E-value: 4.61e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958778178 24 EDSDLVLQSSDIDNHHALIEFNEAEGTFVLQDFNTRNGTFVNECHI-QNVAVKLIPGDILRFG 85
Cdd:cd22724 28 DDCELMLQSRSVDKQHAVINYDASTDEHKVKDLGSLNGTFVNDVRIpEQTYITLKLDDKLRFG 90
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
317-901 |
5.29e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 5.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 317 AERNTEIESLKNEGENLKR-DQAITSGMVTSLQKDVSARNEQVQQLQEEVNQLRIQNKEKEYQLEALTSRCSKLKEDLRK 395
Cdd:PTZ00121 1298 AEEKKKADEAKKKAEEAKKaDEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 396 EEAQKERREAQEK----ELKLCRSQMQDMEKEVKKLREELKKNYTGQNV---ISKTLREKNKVEEKLQEDSRRKllQLQE 468
Cdd:PTZ00121 1378 KKADAAKKKAEEKkkadEAKKKAEEDKKKADELKKAAAAKKKADEAKKKaeeKKKADEAKKKAEEAKKADEAKK--KAEE 1455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 469 MGNRENLIKMNLE-RAVGQLENFRSQVIKATFGKTKPFRDKPVTDQ--------QLIERIVQVTEDNLSFQQRKWTLQRE 539
Cdd:PTZ00121 1456 AKKAEEAKKKAEEaKKADEAKKKAEEAKKADEAKKKAEEAKKKADEakkaaeakKKADEAKKAEEAKKADEAKKAEEAKK 1535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 540 THLHSKQEEV-----VHNVEKLRVLLDKCQAcmrdscnsmDLKKEVELLQHLQLSPPVLGLQKAVLNILRVSLSWLEETE 614
Cdd:PTZ00121 1536 ADEAKKAEEKkkadeLKKAEELKKAEEKKKA---------EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKK 1606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 615 QLLGDLNIELSDSDKGFSLcliYLLEHYKKIMIQSEELRAQVNASLETQQSLQEENLAEKEKLTEKLEQEEKLKARIQQL 694
Cdd:PTZ00121 1607 MKAEEAKKAEEAKIKAEEL---KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA 1683
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 695 TEEKAALEESVAEEKNKLQGDLEMTQARVHELENDLACQKEVLESSVTQEKRKMREvlEAERRKAQDL------ENQLTQ 768
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEA--EEDKKKAEEAkkdeeeKKKIAH 1761
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 769 QKEISESNTYEKLKMRDTLEKEKRRIQDLENRLTKQREEIELKGQKEDILNNKlKDALLLVEDAQQMRTAESTRAEKLSL 848
Cdd:PTZ00121 1762 LKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGG-KEGNLVINDSKEMEDSAIKEVADSKN 1840
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1958778178 849 KLKETLAELEitkaKMIMAEDRLKLQQQSMKALQDERESQKHGFEEEITEYKE 901
Cdd:PTZ00121 1841 MQLEEADAFE----KHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADE 1889
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
730-946 |
5.68e-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: 56.31 E-value: 5.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 730 LACQKEVLESSVTQEKRKMREVLEAERRKAQDLENQLTQQKEISESntyEKLKMRDTLEKEKRRIQDLENRLTKQREEIE 809
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLK---QLAALERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 810 LKGQKEDILNNKLK----------------------DALLLVEDAQQM-RTAESTRAekLSLKLKETLAELEITKAKMIM 866
Cdd:COG4942 87 ELEKEIAELRAELEaqkeelaellralyrlgrqpplALLLSPEDFLDAvRRLQYLKY--LAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 867 AEDRLKLQQQSMKALQDERESQKHGFEEEITEYKEQIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKDSDSAQKEEVP 946
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
324-433 |
1.09e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 56.02 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 324 ESLKNEGENLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEVNQLRIQNKEKEYQLEALTSRCSKLKEDLRKEEaqKERR 403
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREI--RKDR 465
|
90 100 110
....*....|....*....|....*....|..
gi 1958778178 404 EAQ--EKELKLCRSQMQDMEKEVKKLREELKK 433
Cdd:COG2433 466 EISrlDREIERLERELEEERERIEELKRKLER 497
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
648-948 |
1.35e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 648 QSEELRAQVNASLETQQSLQEENLAEKEKLTEKLEQEEKLKARIQQLTEEKAALEEsvAEEKNKLQGDLEMTQARVHELE 727
Cdd:PTZ00121 1426 KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE--AKKADEAKKKAEEAKKKADEAK 1503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 728 NDLACQKEVLESSVTQEKRKMREVLEAERRKAQDLENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQDLENRLTKQREE 807
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA 1583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 808 IELKGQKEdilnNKLKDALLLVEDAQQMRTAESTRAEKLSLKLKETLAELEITKA----KMIMAEDRLKLQQ----QSMK 879
Cdd:PTZ00121 1584 EEAKKAEE----ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKveqlKKKEAEEKKKAEElkkaEEEN 1659
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958778178 880 ALQDERESQKhgfEEEITEYKEQIKQHSQTIVNLEERLSQVTQYYRKIEgEIATLKDSDSAQKEEVPQE 948
Cdd:PTZ00121 1660 KIKAAEEAKK---AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE-ELKKKEAEEKKKAEELKKA 1724
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
15-87 |
1.72e-07 |
|
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also called human lung cancer oncogene 3 protein (HLC-3), kidney anion exchanger adapter protein, or solute carrier family 4 anion exchanger member 1 adapter protein (SLC4A1AP), is a nuclear protein widely expressed in mammalian tissues. It was originally isolated as a kidney Cl-/HCO3- anion exchanger 1 (kAE1)-binding protein. It is a highly mobile nucleocytoplasmic shuttling and multilocalizing protein. Its role in mammalian cells remains unclear. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438729 [Multi-domain] Cd Length: 106 Bit Score: 50.63 E-value: 1.72e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958778178 15 KKSTTIGKHEDSDLVLQSSDIDNHHALIEFN----EAEGTFVLQDFNTRNGTFVNECHIQ-NVAVKLIPGDILRFGSS 87
Cdd:cd22677 21 KSFYVFGRLPGCDVVLEHPSISRYHAVLQYRgdadDHDGGFYLYDLGSTHGTFLNKQRIPpKQYYRLRVGHVLKFGGS 98
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
18-65 |
2.16e-07 |
|
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.
Pssm-ID: 214578 [Multi-domain] Cd Length: 52 Bit Score: 48.71 E-value: 2.16e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1958778178 18 TTIGKHE-DSDLVLQSSDIDNHHALIEFNEaEGTFVLQDFNTRNGTFVN 65
Cdd:smart00240 1 VTIGRSSeDCDIQLDGPSISRRHAVIVYDG-GGRFYLIDLGSTNGTFVN 48
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
227-1060 |
2.18e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 55.44 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 227 REINRLSDFEMESKYKDAVIMNLQAEIADLSQRLSEMAAVVAAARQSNRCDPRFQDLDEGDDhRQKEIESMKSQINALQK 306
Cdd:TIGR00606 326 RELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPF-SERQIKNFHTLVIERQE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 307 GYSQVLSQTLAERnTEIESLKNEGENLKRDQAITSGMVTSLQKDVsarneqvqqLQEEVNQLRIQNKEKEyQLEALTSRC 386
Cdd:TIGR00606 405 DEAKTAAQLCADL-QSKERLKQEQADEIRDEKKGLGRTIELKKEI---------LEKKQEELKFVIKELQ-QLEGSSDRI 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 387 SKLKEDLRKEEAQKERREAQekelklcrSQMQDMEKEVKKLreelkknytgQNVISKTLREKNKVEEKLQEDSRRKLLQL 466
Cdd:TIGR00606 474 LELDQELRKAERELSKAEKN--------SLTETLKKEVKSL----------QNEKADLDRKLRKLDQEMEQLNHHTTTRT 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 467 Q-EMGNRENLIKMNleravgQLENFRSQVIKATFGKTKPFRDKPVTDQQL--IERIVQVTEDNLSFQQRKWTLQRETHLH 543
Cdd:TIGR00606 536 QmEMLTKDKMDKDE------QIRKIKSRHSDELTSLLGYFPNKKQLEDWLhsKSKEINQTRDRLAKLNKELASLEQNKNH 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 544 SKQEEvvhnvEKLRVLLDKCQACMRDSCNSMDLKKEVELLQHlqlsppvlGLQKAvlnilRVSLSWLEETEQLLGDLNIE 623
Cdd:TIGR00606 610 INNEL-----ESKEEQLSSYEDKLFDVCGSQDEESDLERLKE--------EIEKS-----SKQRAMLAGATAVYSQFITQ 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 624 LSDSDKGF-SLCliyllehykKIMIQSEELRAQVNASLETQQSLQEENLAEKEKLTEKLEQEEKLkarIQQLTEEKAALE 702
Cdd:TIGR00606 672 LTDENQSCcPVC---------QRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDE---MLGLAPGRQSII 739
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 703 ESVAEEKNKLQGDLEMTQARVHELENDLACQKEVLESSVTQEKRK---MREVLEAERRKAQDLENQLTQQKEISESNTYE 779
Cdd:TIGR00606 740 DLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAkvcLTDVTIMERFQMELKDVERKIAQQAAKLQGSD 819
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 780 KLKMRDTLEKEKrriQDLENRLTKQREEIEL-----KGQKEDILN-----NKLKDALLLVEDAQQMRTAESTRAEKLSLK 849
Cdd:TIGR00606 820 LDRTVQQVNQEK---QEKQHELDTVVSKIELnrkliQDQQEQIQHlksktNELKSEKLQIGTNLQRRQQFEEQLVELSTE 896
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 850 LKETLAELEITKAKMIMAEDRLKLQQQSMKALQDERESQKHGFEEEITEYKEQIKQHSQTIVNLEERLSQVTQYYRK--- 926
Cdd:TIGR00606 897 VQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKqke 976
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 927 --IEGEIATLKDSDSAQKEEVPQEFTIVPSLDSSAKeiacdhliddllmaQKEILSQQEIIMKLRTDLGEAHTRMSDLRG 1004
Cdd:TIGR00606 977 teLNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKI--------------QERWLQDNLTLRKRENELKEVEEELKQHLK 1042
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958778178 1005 ELSEKQKTELERQvalVRQQNSELSILKAKVVQTTGLVEKKDRELKVLREALRASQ 1060
Cdd:TIGR00606 1043 EMGQMQVLQMKQE---HQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
660-950 |
2.58e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 54.90 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 660 LETQQSLQEENLAEKEKLTEKLEQEEKlkariqqlteEKAALEESVAEEKNKLQGDLEMTQARVHELENDLAC------Q 733
Cdd:pfam07888 78 LESRVAELKEELRQSREKHEELEEKYK----------ELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTltqrvlE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 734 KEVLESSVTQEKRKMREVLEAERRKAQDLENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQDLENRLTKQREEIELKGQ 813
Cdd:pfam07888 148 RETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 814 KEDILNNKLKDALLLVEDAQ-QMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDRLKLQQQSMKALQD------ERE 886
Cdd:pfam07888 228 KEAENEALLEELRSLQERLNaSERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGrarwaqERE 307
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958778178 887 SQKHGFEEEiteyKEQIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKDSDSAQKEEVPQEFT 950
Cdd:pfam07888 308 TLQQSAEAD----KDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQ 367
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
640-1163 |
2.78e-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: 55.12 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 640 EHYKKIMiqsEELRAQVNaslETQQSLQEEN-LAEKEKLTEKlEQEEKLKARIQQLTEEKAALEEsVAEEKNKLQGDLE- 717
Cdd:pfam15921 74 EHIERVL---EEYSHQVK---DLQRRLNESNeLHEKQKFYLR-QSVIDLQTKLQEMQMERDAMAD-IRRRESQSQEDLRn 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 718 MTQARVHELENDLACQKEVLESSVTQEKrKMREVLEAERRKAQDLENQLTQQKEISESNTYEK---------------LK 782
Cdd:pfam15921 146 QLQNTVHELEAAKCLKEDMLEDSNTQIE-QLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHdsmstmhfrslgsaiSK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 783 MRDTLEKE----KRRIQDLENRLTKQREE----IELKGQK-----EDILNNKLKDALLLVEDAQQMRTAESTRAEKLSLK 849
Cdd:pfam15921 225 ILRELDTEisylKGRIFPVEDQLEALKSEsqnkIELLLQQhqdriEQLISEHEVEITGLTEKASSARSQANSIQSQLEII 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 850 LKET----------LAELEITKAKMimaEDRLKLQQQSMKALQDERESQKHGFEEEITEYKEQIKQHSQTIVNLEERLSQ 919
Cdd:pfam15921 305 QEQArnqnsmymrqLSDLESTVSQL---RSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQK 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 920 VTQYYRKIEGEIATLKDSDSAQKEEvpqeftivpsldSSAKEIACDHLIDDLLMAQKEILSQQEIIMKLRTDL-GEAHTR 998
Cdd:pfam15921 382 LLADLHKREKELSLEKEQNKRLWDR------------DTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECqGQMERQ 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 999 MSDLRGelsekQKTELERQVALVRQQNSELSILKAKVVQTTG---LVEKKDRELKVLREALrasQEKPRPYLSTEQKPRN 1075
Cdd:pfam15921 450 MAAIQG-----KNESLEKVSSLTAQLESTKEMLRKVVEELTAkkmTLESSERTVSDLTASL---QEKERAIEATNAEITK 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 1076 LSQKCDISLQiEPAHPDSfssfqEEQFFSDLGAKCKGSRHE--------EVIQRQKKALSEL---RTRIKELEKANSSNH 1144
Cdd:pfam15921 522 LRSRVDLKLQ-ELQHLKN-----EGDHLRNVQTECEALKLQmaekdkviEILRQQIENMTQLvgqHGRTAGAMQVEKAQL 595
|
570
....*....|....*....
gi 1958778178 1145 KDHVNESFLELKTLRMEKN 1163
Cdd:pfam15921 596 EKEINDRRLELQEFKILKD 614
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
668-1062 |
3.84e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 668 EENLAEKEKLTEKLEQEEKLKARIQQLTEEKAALE-ESVAEEKNKLQGDLEMTQARVHELENDLAcqkevlessvtqEKR 746
Cdd:PRK03918 358 EERHELYEEAKAKKEELERLKKRLTGLTPEKLEKElEELEKAKEEIEEEISKITARIGELKKEIK------------ELK 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 747 KMREVLEAERRKAQDLENQLTQQ--KEISESNTYEKLKMRDTLEKEKRRIQDLENRLTKQreEIELKGQKEDILNNKLKD 824
Cdd:PRK03918 426 KAIEELKKAKGKCPVCGRELTEEhrKELLEEYTAELKRIEKELKEIEEKERKLRKELREL--EKVLKKESELIKLKELAE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 825 ALLLVEDAQQMRTAES-TRAEKLSLKLKETLAELeitKAKMIMAEDRLKLQQQSMKALQdERESQKHGFEEEITEYKEQI 903
Cdd:PRK03918 504 QLKELEEKLKKYNLEElEKKAEEYEKLKEKLIKL---KGEIKSLKKELEKLEELKKKLA-ELEKKLDELEEELAELLKEL 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 904 KQHS-QTIVNLEERLSQVTQYYRkiegEIATLKDSDSAQKEEvpqeftivpsldssakeiacdhliddllmaQKEILSQQ 982
Cdd:PRK03918 580 EELGfESVEELEERLKELEPFYN----EYLELKDAEKELERE------------------------------EKELKKLE 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 983 EIIMKLRTDLGEAHTRMSDLRGELSEKQKT----ELERQVALVRQQNSELSILKAKVVQTTGLVEKKDRELKVLREALRA 1058
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEELEKKyseeEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE 705
|
....
gi 1958778178 1059 SQEK 1062
Cdd:PRK03918 706 REKA 709
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
290-511 |
4.26e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 4.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 290 RQKEIESMKSQINALQKgysqvlsqTLAERNTEIESLKNEGENLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEVNQLR 369
Cdd:COG4942 25 AEAELEQLQQEIAELEK--------ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 370 IQNKEKEYQLEAL------TSRCSKLKEDLRKE----------------EAQKERREAQEKELKLCRSQMQDMEKEVKKL 427
Cdd:COG4942 97 AELEAQKEELAELlralyrLGRQPPLALLLSPEdfldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 428 REELKKNYTGQNVISKTLREKNKVEEKLQEDSRRKLLQLQEMGNRENLIKMNLERAVGQLENFRSQVIKATFGKTKPFRD 507
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256
|
....
gi 1958778178 508 KPVT 511
Cdd:COG4942 257 WPVS 260
|
|
| FHA_PS1-like |
cd22691 |
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) ... |
5-93 |
5.55e-07 |
|
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) and similar proteins; PS1 is an FHA domain-containing protein required for normal spindle orientation at male meiosis II and normal formation of tetrad of microspores. It is not involved in female meiosis. Mutations in PS1 lead to the production of diploid pollen grains. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438743 [Multi-domain] Cd Length: 113 Bit Score: 49.34 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 5 LKSPDGFFVLKKSTTIGKHEDSDLVLQSSDIDNHHALIEFNEAEGTFVLQDFNTRNGTFVNECHIQ-NVAVKLIPGDILR 83
Cdd:cd22691 18 LHGKFSKSEEEDILVVGRHPDCDIVLDHPSISRFHLEIRIIPSRRKITLTDLSSVHGTWVNGQRIEpGVPVELEEGDTVR 97
|
90
....*....|
gi 1958778178 84 FGSSGPTYEL 93
Cdd:cd22691 98 LGASTRVYRL 107
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
656-1087 |
5.66e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.96 E-value: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 656 VNASLETQQSLQEENLAEKEKLTEKleQEEKLKARIQQLTEEKAALEESVAEEKNKlQGDLEMTQARVHELENDLACQKE 735
Cdd:pfam05483 350 VVTEFEATTCSLEELLRTEQQRLEK--NEDQLKIITMELQKKSSELEEMTKFKNNK-EVELEELKKILAEDEKLLDEKKQ 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 736 V--LESSVTQEKRKMREVLEAERRKAQDLENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQD---------LENRLTKQ 804
Cdd:pfam05483 427 FekIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIEltahcdkllLENKELTQ 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 805 REE---IELKGQKEDILNNKlkdalllvedaqqmrtaestRAEKLSLKLKETLAELEIT-KAKMIMAEDRLKLQQQSMKA 880
Cdd:pfam05483 507 EASdmtLELKKHQEDIINCK--------------------KQEERMLKQIENLEEKEMNlRDELESVREEFIQKGDEVKC 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 881 LQDERESQKHGFEEEITEYKEQIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKDSDSAQKEEVPQEFTIVPSLD---S 957
Cdd:pfam05483 567 KLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLElelA 646
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 958 SAKEiACDHLIDDLlmaQKEILSQQEIIMKLRTDLGEAHTRMSD---LRGELSEKQKTELERQVALVRQQNSELSILKAK 1034
Cdd:pfam05483 647 SAKQ-KFEEIIDNY---QKEIEDKKISEEKLLEEVEKAKAIADEavkLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEE 722
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1958778178 1035 VVQTTGLVEKKDRELKVLREALRASQEKPRPYLSTEQKPRNLSQKCDISLQIE 1087
Cdd:pfam05483 723 RDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKME 775
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
733-868 |
7.90e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 53.24 E-value: 7.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 733 QKEVLEssVTQEKRKMREVLEAE----RRKAQDLENQLTQQKEISEsntyeklKMRDTLEKEKRRIQDLENRLTKQREEI 808
Cdd:PRK12704 56 KEALLE--AKEEIHKLRNEFEKElrerRNELQKLEKRLLQKEENLD-------RKLELLEKREEELEKKEKELEQKQQEL 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 809 ELKGQKEDILNNKLKDAL-----LLVEDAQQM---RTAESTRAEKLSL-KLKETLAELEITK-AKMIMAE 868
Cdd:PRK12704 127 EKKEEELEELIEEQLQELerisgLTAEEAKEIlleKVEEEARHEAAVLiKEIEEEAKEEADKkAKEILAQ 196
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
322-1029 |
9.65e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 53.30 E-value: 9.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 322 EIESLKNEGENLKRDQA---ITSGMVTSLQKDVSARNEQVQQLQEEVNQLRIQnKEKEYQ--LEALTSRCSKLKEDLRKE 396
Cdd:pfam12128 242 EFTKLQQEFNTLESAELrlsHLHFGYKSDETLIASRQEERQETSAELNQLLRT-LDDQWKekRDELNGELSAADAAVAKD 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 397 EAQKERREAQEK--------ELKLCRSQMQDMEKEVKKLREELKKNYTGQNVISktlREKNKVEEKLQEDSRRKLLQL-Q 467
Cdd:pfam12128 321 RSELEALEDQHGafldadieTAAADQEQLPSWQSELENLEERLKALTGKHQDVT---AKYNRRRSKIKEQNNRDIAGIkD 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 468 EMGNRENLIKMNLERAVGQLENFRSQVIKATFGKTKPFRDKpvtDQQLIERI---------VQVTEDNLSFQQRKwtLQR 538
Cdd:pfam12128 398 KLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEE---EYRLKSRLgelklrlnqATATPELLLQLENF--DER 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 539 ETHLHSKQEEVVHNVE-------KLRVLLDKCQACMRDsCNSMDLKKEVELLQ-HLQLSPPVLGLqkavLNILRV----- 605
Cdd:pfam12128 473 IERAREEQEAANAEVErlqselrQARKRRDQASEALRQ-ASRRLEERQSALDElELQLFPQAGTL----LHFLRKeapdw 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 606 --SLSWLEETEQLL-GDLNIELSDSDKGFSLCLIYLLEHYKKImiqseelraQVNASLETQQSLQEENLAEKEKLTeklE 682
Cdd:pfam12128 548 eqSIGKVISPELLHrTDLDPEVWDGSVGGELNLYGVKLDLKRI---------DVPEWAASEEELRERLDKAEEALQ---S 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 683 QEEKLKARIQQLTEEKAALEESvaeeknklqgDLEMTQARVHELENDLACQKevLESSVTQEKRKMREVLEAERRKAQDL 762
Cdd:pfam12128 616 AREKQAAAEEQLVQANGELEKA----------SREETFARTALKNARLDLRR--LFDEKQSEKDKKNKALAERKDSANER 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 763 ENQLTQQKEISEsntyekLKMRDTLEKEKRriQDLENRLTKQREEIELKGQKEDILNnklkdalLLVEDAQQMRTAESTR 842
Cdd:pfam12128 684 LNSLEAQLKQLD------KKHQAWLEEQKE--QKREARTEKQAYWQVVEGALDAQLA-------LLKAAIAARRSGAKAE 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 843 AEKLSLKLKETLAELEITKAKMI-MAEDRLKLQQQSMKALQDERES------QKHGFEEEITEYKEQIKQHSQTIVNLEE 915
Cdd:pfam12128 749 LKALETWYKRDLASLGVDPDVIAkLKREIRTLERKIERIAVRRQEVlryfdwYQETWLQRRPRLATQLSNIERAISELQQ 828
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 916 RLSQVTQYYRKIEGEIATLKDSDSAQKEEVPQEFTIVPSLDSSAKEIACDHLIDDLLMAQKEILSQ-QEIIMKLRTDLGE 994
Cdd:pfam12128 829 QLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQlEDLKLKRDYLSES 908
|
730 740 750
....*....|....*....|....*....|....*
gi 1958778178 995 AHTRMSDLRGELSEKQKTELERQVALVRQQNSELS 1029
Cdd:pfam12128 909 VKKYVEHFKNVIADHSGSGLAETWESLREEDHYQN 943
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
19-87 |
1.04e-06 |
|
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 (AtPP2C70) and similar proteins; AtPP2C70, also called kinase-associated protein phosphatase, or protein ROOT ATTENUATED GROWTH 1, dephosphorylates the serine/threonine receptor-like kinase RLK5. It may function as a signaling component in a pathway involving RLK5. It acts as a negative regulator of the CLAVATA1 signaling in plant development by binding and dephosphorylating CLAVATA1. It is also a component of a signaling pathway which mediates adaptation to NaCl stress. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438730 [Multi-domain] Cd Length: 102 Bit Score: 48.13 E-value: 1.04e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958778178 19 TIGKHEDSDLVLQSSDIDNHHALIEFNEAEGTFVLQDFNTRNGTFVN--ECHIQNVAVKLIPGDILRFGSS 87
Cdd:cd22678 26 TIGRIQRGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNgeSISPNGRPVVLSSGDVITLGSE 96
|
|
| FHA_SNIP1_DDL-like |
cd22676 |
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA ... |
20-93 |
1.49e-06 |
|
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA domain-containing protein DDL, and similar proteins; SNIP1 is an FHA domain-containing protein required for pre-mRNA splicing as a component of the spliceosome. It inhibits NF-kappaB signaling by competing for its binding to the C/H1 domain of CBP/p300 transcriptional co-activators. It is involved in microRNA (miRNA) biogenesis. SNIP1 is a regulator of the cell cycle and cyclin D1 expression and may be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. This family also includes Arabidopsis thaliana FHA domain-containing protein DDL and similar proteins. DDL, also called protein DAWDLE, is involved in the microRNA (miRNA) and short interfering RNA (siRNA) biogenesis. It may facilitate DCL1 to access or recognize primary miRNAs. DDL binds RNA non-specifically. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438728 [Multi-domain] Cd Length: 111 Bit Score: 48.06 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 20 IGKHED-SDLVLQSSDIDNHHALIEF----NEAEGTFVLQ------DFNTRNGTFVNECHIQ-NVAVKLIPGDILRFGSS 87
Cdd:cd22676 25 IGRDRRvADIPLDHPSCSKQHAVIQFreveKRNEGDVIENirpyiiDLGSTNGTFLNGEKIEpRRYYELREKDVLKFGLS 104
|
....*.
gi 1958778178 88 GPTYEL 93
Cdd:cd22676 105 TREYVL 110
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
648-848 |
1.71e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.69 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 648 QSEELRAQVNASLETQQSLQEENLAEKEKLTEKLEQeekLKARIQQLTEEKAALEEsvaeEKNKLQGDLEMTQARVHELE 727
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA---LERRIAALARRIRALEQ----ELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 728 NDLACQKEVLE----------------------------------SSVTQEKRKMREVLEAERRKAQDLENQLTQQKEIS 773
Cdd:COG4942 97 AELEAQKEELAellralyrlgrqpplalllspedfldavrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958778178 774 ESNTYEKLKMRDTLEKEKRR----IQDLENRLTKQREEIELKGQKEDILNNKLKDALLLVEDAQQMRTAESTRAEKLSL 848
Cdd:COG4942 177 EALLAELEEERAALEALKAErqklLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
648-1150 |
1.72e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 648 QSEELRAQVNASLETQQSLQEENLAEKEKLTEKLEQEEKLKARIQQLTEEKAALEESVAEEKNK---------------- 711
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKadaakkkaeekkkade 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 712 LQGDLEMTQARVHELENDLACQKEVLESsvtqeKRKMREVLEAE--RRKAQDLENQLTQQKEISESNTYEKLKMRdtlEK 789
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEA-----KKKAEEKKKADeaKKKAEEAKKADEAKKKAEEAKKAEEAKKK---AE 1467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 790 EKRRIQDLENRLTKQREEIELKGQKEDILN--NKLKDALLLVEDAQQMRTAESTRAEKLSLKLKETLAELEITKAKMIMA 867
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKkaDEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK 1547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 868 EDRLKLQQQSMKALQDERESQKHGFEEEITEYKEQIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKDSDSAQKEEVPQ 947
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 948 EFTIVPSLDSSAKEIACDhliddllMAQKEILSQQEIIMKLRTDlgeahtrmSDLRGELSEKQKTELERQVALVRQQNSE 1027
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEE-------KKKAEELKKAEEENKIKAA--------EEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 1028 LSILKAKVVQTTGLVEKKDRELKVLREALRASQEKPRPYLSTEQKPRNLSQKCDISLQIEPAHPDSFSSF--QEEQFFSD 1105
Cdd:PTZ00121 1693 ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLkkEEEKKAEE 1772
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1958778178 1106 LGAKCKGSRHEEVIQRQKKALSELRTRIKELeKANSSNHKDHVNE 1150
Cdd:PTZ00121 1773 IRKEKEAVIEEELDEEDEKRRMEVDKKIKDI-FDNFANIIEGGKE 1816
|
|
| FHA_GarA_OdhI-like |
cd22684 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium ... |
18-85 |
2.14e-06 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium glutamicum OdhI and similar proteins; This family includes Mycobacterium tuberculosis glycogen accumulation regulator GarA and Corynebacterium glutamicum oxoglutarate dehydrogenase inhibitor (OdhI). GarA is involved in the regulation of glutamate metabolism. It acts as a phosphorylation-dependent molecular switch that modulates the activities of Kgd, Gdh and GltB. GarA binds to Kgd, Gdh, GltB, PknB, and the N-terminal region of PknG via its FHA domain. OdhI is an essential component of the PknG signaling pathway. It can inhibit the activity of 2-oxoglutarate dehydrogenase only when it is unphosphorylated. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438736 [Multi-domain] Cd Length: 94 Bit Score: 46.99 E-value: 2.14e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958778178 18 TTIGKHEDSDLVLQSSDIDNHHAliEFNEAEGTFVLQDFNTRNGTFVNECHIQnvAVKLIPGDILRFG 85
Cdd:cd22684 23 TTAGRHPESDIFLDDVTVSRRHA--EFRRAEGGFVVRDVGSLNGTYVNRERID--SAVLRNGDEVQIG 86
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
355-1050 |
2.24e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.04 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 355 NEQVQQLQEEVNQL-RIQNKEKEYQLEALTSRCSKLKEDLRKEEAQKE--RREAQEKELklCRSQMQDMEKEV---KKLR 428
Cdd:pfam15921 84 SHQVKDLQRRLNESnELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADirRRESQSQED--LRNQLQNTVHELeaaKCLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 429 EELKKNYTGQnviSKTLREKNKVEEKLQEDSRRKLLQLQEMGNR-----ENLIKM---NLERAVGQLenFRSQVIKATFG 500
Cdd:pfam15921 162 EDMLEDSNTQ---IEQLRKMMLSHEGVLQEIRSILVDFEEASGKkiyehDSMSTMhfrSLGSAISKI--LRELDTEISYL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 501 KTKPFrdkPVTDQqlierivqvTEDNLSFQQRKWTLQRETHlHSKQEEVVHNVEKLRVLLDKCQACMRDSCNSMDLKKEV 580
Cdd:pfam15921 237 KGRIF---PVEDQ---------LEALKSESQNKIELLLQQH-QDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEI 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 581 ellqhlqlsppvlgLQKAVLNILRVSLSWLEETEQLLGDLNIELSDSDKGFSlclIYLLEHYKKIMIQSEELR------- 653
Cdd:pfam15921 304 --------------IQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYE---DKIEELEKQLVLANSELTearterd 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 654 --AQVNASLETQQSLQEENLAEKEK-LTEKLEQEEKLKAR--------------IQQLTEEKAALEESVAEEKNKLQGDL 716
Cdd:pfam15921 367 qfSQESGNLDDQLQKLLADLHKREKeLSLEKEQNKRLWDRdtgnsitidhlrreLDDRNMEVQRLEALLKAMKSECQGQM 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 717 EMTQA----------RVHELENDLACQKEVLEsSVTQEKRKMREVLEAERRKAQDLENQLTQQKEISESNTYEKLKMRDT 786
Cdd:pfam15921 447 ERQMAaiqgknesleKVSSLTAQLESTKEMLR-KVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSR 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 787 LEKEKRRIQDLENRLTKQR------EEIELKGQKED----ILNNKLKDALLLVedAQQMRTAESTRAEKLSLK-----LK 851
Cdd:pfam15921 526 VDLKLQELQHLKNEGDHLRnvqtecEALKLQMAEKDkvieILRQQIENMTQLV--GQHGRTAGAMQVEKAQLEkeindRR 603
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 852 ETLAELEITK----AKMIMAEDR---LKLQQQSMKALQDERESQKHGFEEEITEYKEQIKQHSQTIVNLEERLSQVTQYY 924
Cdd:pfam15921 604 LELQEFKILKdkkdAKIRELEARvsdLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNF 683
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 925 RKIEGEIAT----LKDSDSAQKEEVPQEFTIVPSLDSSAkeiacDHLIDDLLMAQKEILSQQEIIMKLRTDLGEAHTRMS 1000
Cdd:pfam15921 684 RNKSEEMETttnkLKMQLKSAQSELEQTRNTLKSMEGSD-----GHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMT 758
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1958778178 1001 DlrgelSEKQKTELERQVALVRQQNSELSILKAKVVQTTGLVEKKDRELK 1050
Cdd:pfam15921 759 N-----ANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLK 803
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
209-482 |
2.44e-06 |
|
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: 52.05 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 209 MDQDLGQQDKDDiillLGREINRLSDFEMESKYKDAViMNLQAEIADLSQRLsemaavvaaARQSNRCDPRFQDLD---E 285
Cdd:pfam17380 296 MEQERLRQEKEE----KAREVERRRKLEEAEKARQAE-MDRQAAIYAEQERM---------AMERERELERIRQEErkrE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 286 GDDHRQKEIESMKSQINALQKgySQVLSQTLAER-NTEIESLKN----EGENLKRDQAITSGMVTSLQKDVSARNEQVQQ 360
Cdd:pfam17380 362 LERIRQEEIAMEISRMRELER--LQMERQQKNERvRQELEAARKvkilEEERQRKIQQQKVEMEQIRAEQEEARQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 361 LQEE----VNQLRIQNKEKEYQLEAL--------TSRCSKLKEDLRKEEAQKERREAQEKELKLCRSQMQDMEKEVKKLR 428
Cdd:pfam17380 440 LEEErareMERVRLEEQERQQQVERLrqqeeerkRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLE 519
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958778178 429 EELKKNytgQNVISKTLREKNKVEE--KLQEDSRRKLLQLQEMG---NRENLIKMNLER 482
Cdd:pfam17380 520 KEMEER---QKAIYEEERRREAEEErrKQQEMEERRRIQEQMRKateERSRLEAMERER 575
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
291-1069 |
2.49e-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: 51.99 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 291 QKEIESMKSQINALQKGYSQvLSQTLAERNTEIESL-KNEGENLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEVNQLR 369
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEE-IEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLE 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 370 IQNKEKEYQLEALTSRcskLKEDLRKEEAQKERREAQEKELKLCRSQMQDMEKEVKKLREELKKNytgQNVISKTLREKN 449
Cdd:TIGR02169 329 AEIDKLLAEIEELERE---IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY---REKLEKLKREIN 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 450 KveekLQEDSRRKLLQLQEMGNRENLIKMNLERAVGQLENFRSQvikatfgkTKPFRDKPVTDQQLIERIVQVTED-NLS 528
Cdd:TIGR02169 403 E----LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEE--------KEDKALEIKKQEWKLEQLAADLSKyEQE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 529 FQQRKWTLQR-ETHLHSKQEEvvhnveklrvlLDKCQACMRDSCNSMDLKKEVELLqhlqLSPPVLGLQKAVLNILRVSL 607
Cdd:TIGR02169 471 LYDLKEEYDRvEKELSKLQRE-----------LAEAEAQARASEERVRGGRAVEEV----LKASIQGVHGTVAQLGSVGE 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 608 SWLEETEQLLGD-LNIELSDSDKGFSLCLIYLLEHykkimiqseelraqvNASLETQQSLQEenLAEKEKLTEKLEQEEK 686
Cdd:TIGR02169 536 RYATAIEVAAGNrLNNVVVEDDAVAKEAIELLKRR---------------KAGRATFLPLNK--MRDERRDLSILSEDGV 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 687 LKARIQQLTEE-------KAALEESVAEEKNKLQGDLeMTQARVHELENDLacqkevLESS--VTQEKRKMREvleAERR 757
Cdd:TIGR02169 599 IGFAVDLVEFDpkyepafKYVFGDTLVVEDIEAARRL-MGKYRMVTLEGEL------FEKSgaMTGGSRAPRG---GILF 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 758 KAQDLEnqltqqkeisesntyEKLKMRDTLEKEKRriqdLENRLTKQREEIElkgqkedilnNKLKDALLLVEDAQQMRT 837
Cdd:TIGR02169 669 SRSEPA---------------ELQRLRERLEGLKR----ELSSLQSELRRIE----------NRLDELSQELSDASRKIG 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 838 AESTRAEKLslklketlaELEITKAKMIMAEDRLKLQQQSMKALQDERESQKhgFEEEITEYKEQIKQHSQTIVNLEERL 917
Cdd:TIGR02169 720 EIEKEIEQL---------EQEEEKLKERLEELEEDLSSLEQEIENVKSELKE--LEARIEELEEDLHKLEEALNDLEARL 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 918 SQvtQYYRKIEGEIatlkdsdSAQKEEVPQEFTIVPSLDSSAKEiacdhLIDDLLMAQKEILSQQEIIMKLRTDLGEAHT 997
Cdd:TIGR02169 789 SH--SRIPEIQAEL-------SKLEEEVSRIEARLREIEQKLNR-----LTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958778178 998 RMSDLRGELsEKQKTELERQVALVRQQNSELSILKAKVVQttglVEKKDRELKVLREALRASQEKPRPYLST 1069
Cdd:TIGR02169 855 EIENLNGKK-EELEEELEELEAALRDLESRLGDLKKERDE----LEAQLRELERKIEELEAQIEKKRKRLSE 921
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
321-1040 |
2.73e-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: 51.89 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 321 TEIESLKNEGENLKRDqaiTSGMVTSLQKDVSARNEQVQQLQEEVNQLRIqnkekeyQLEALTSRCSKLKEDLRKEEAQK 400
Cdd:TIGR00618 194 GKAELLTLRSQLLTLC---TPCMPDTYHERKQVLEKELKHLREALQQTQQ-------SHAYLTQKREAQEEQLKKQQLLK 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 401 ERReAQEKELklcrsqmQDMEKEVKKLREELKknytgQNVISKTLREKNKVEEKLQEDSRRKLLQLQEMGNRENLIKMNL 480
Cdd:TIGR00618 264 QLR-ARIEEL-------RAQEAVLEETQERIN-----RARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 481 ERAVGQLENFRSQvikatfgktkpfRDKPVTDQQLIERIVQVTEDNLSF-QQRKWTLQRETHLHSKQEEVVHNVEKLRVL 559
Cdd:TIGR00618 331 AAHVKQQSSIEEQ------------RRLLQTLHSQEIHIRDAHEVATSIrEISCQQHTLTQHIHTLQQQKTTLTQKLQSL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 560 LDKCQACMRDSCNSMDLKKEVELLQ-HLQLSPPVLGLQKAVLNILRVSlswLEETEQLLGDLNIELSDSDKGFSlCLIYL 638
Cdd:TIGR00618 399 CKELDILQREQATIDTRTSAFRDLQgQLAHAKKQQELQQRYAELCAAA---ITCTAQCEKLEKIHLQESAQSLK-EREQQ 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 639 LEHYKKIMIQSEELRAQVNASLETQQSLQ---EENLAEKEKLTEKLEQEEKLKARIQQLTEEKAALEESvaEEKNKLQGD 715
Cdd:TIGR00618 475 LQTKEQIHLQETRKKAVVLARLLELQEEPcplCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETS--EEDVYHQLT 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 716 LEMTQARVHELENDLACQKE-VLESSVTQEKRKMREVLEAERRKAQDLENQLTQQKEISESNTYEKLKMRDTLEKEKRRI 794
Cdd:TIGR00618 553 SERKQRASLKEQMQEIQQSFsILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRL 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 795 QDLENRLTKQREEIELKGQKEDILNNKLKDALLLVEDAQ----QMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDR 870
Cdd:TIGR00618 633 HLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPkellASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETH 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 871 LKL-------QQQSMKALQDERESQKHGFEEEITEYKEQIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKDSDSAQKE 943
Cdd:TIGR00618 713 IEEydrefneIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNR 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 944 EVPQEFTIVPSLDSSAKEIACDHLidDLLMAQKEILSQQEiiMKLRTDLGEAHTRMSDLRGELSE-----KQKTELERQV 1018
Cdd:TIGR00618 793 LREEDTHLLKTLEAEIGQEIPSDE--DILNLQCETLVQEE--EQFLSRLEEKSATLGEITHQLLKyeecsKQLAQLTQEQ 868
|
730 740
....*....|....*....|..
gi 1958778178 1019 ALVRQQNSELSILKAKVVQTTG 1040
Cdd:TIGR00618 869 AKIIQLSDKLNGINQIKIQFDG 890
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
648-1064 |
3.44e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 648 QSEELRAQVNASLETQQSLQEENLAEKEKLTEKLEQEEKLKA-RIQQLTEEKAALEESVAEEKNKL----QGDLEMTQAR 722
Cdd:PTZ00121 1239 AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAdELKKAEEKKKADEAKKAEEKKKAdeakKKAEEAKKAD 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 723 VHELENDLACQKEVLESSVTQEKRKMREVLEAERRKAQDLENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQDLEnRLT 802
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD-EAK 1397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 803 KQREEIELKGQKEDILNNKLKDALLLVEDAQQMRTAESTRAEKLSLKLKETLAELEITKAKmimAEDRLKLQQQSMKALQ 882
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK---AEEAKKKAEEAKKADE 1474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 883 DERESQKHGFEEEITEYKEQIKQHSQTIVNLEERLSQVTQYYRKIEGEIA-TLKDSDSAQKEEVPQEFTIVPSLDS---- 957
Cdd:PTZ00121 1475 AKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAdEAKKAEEAKKADEAKKAEEKKKADElkka 1554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 958 ----------SAKEIACDHLIDDLLMAQKEILSQQE---IIMKLRTDLGEAHTRMSDLRGELSEKQKTELERQVALVRQQ 1024
Cdd:PTZ00121 1555 eelkkaeekkKAEEAKKAEEDKNMALRKAEEAKKAEearIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK 1634
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1958778178 1025 NSELSILKAKVVQTTGLVEKKDRELKVLREALRASQEKPR 1064
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
639-915 |
3.56e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 51.44 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 639 LEHYKKIMIQSEELRAQVNAsLETQQSLQEEN--LAEKEKL-TEKLE-QEEKLKARIQQLTEEKAALEESVAEEKNKLQG 714
Cdd:PLN02939 155 LEDLEKILTEKEALQGKINI-LEMRLSETDARikLAAQEKIhVEILEeQLEKLRNELLIRGATEGLCVHSLSKELDVLKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 715 DLEMTQARVHELENDLACQKEVLESSVTQEKRkmREVLEAERRkaqDLENQL-TQQKEISESNTYEKlkmrDTLEKEKRR 793
Cdd:PLN02939 234 ENMLLKDDIQFLKAELIEVAETEERVFKLEKE--RSLLDASLR---ELESKFiVAQEDVSKLSPLQY----DCWWEKVEN 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 794 IQDLENRLTKQREEIELKGQKEDILNNKLKdalllvedaqqmrtaestraeklslKLKETLAELEITKakmiMAEDRLKL 873
Cdd:PLN02939 305 LQDLLDRATNQVEKAALVLDQNQDLRDKVD-------------------------KLEASLKEANVSK----FSSYKVEL 355
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958778178 874 QQQSMKALQDERESQKHGFEEEITEYKEQIKQHSQTIVNLEE 915
Cdd:PLN02939 356 LQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKE 397
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
688-902 |
4.31e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 4.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 688 KARIQQLTEEKAALEESVAEEKNKLQgDLEMTQARVHELENDLACQKEVLESSVtqekrkmrEVLEAERRkAQDLENQLT 767
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLE-ALEAELDALQERREALQRLAEYSWDEI--------DVASAERE-IAELEAELE 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 768 QqkeISESNtyeklkmrDTLEKEKRRIQDLENRLTKQREEIELKGQKEDILNNKLKDALLLVEDAQ-QMRTAESTRAEKL 846
Cdd:COG4913 679 R---LDASS--------DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQdRLEAAEDLARLEL 747
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958778178 847 SLKLKETLAELEITKAkmiMAEDRLKLQQQsMKALQDERESQKHGFEEEITEYKEQ 902
Cdd:COG4913 748 RALLEERFAAALGDAV---ERELRENLEER-IDALRARLNRAEEELERAMRAFNRE 799
|
|
| FHA_AGGF1 |
cd22686 |
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ... |
11-87 |
5.43e-06 |
|
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 (AGGF1) and similar proteins; AGGF1, also called angiogenic factor VG5Q, or G patch domain-containing protein 7 (GPATC7), or vasculogenesis gene on 5q protein, is an angiogenic factor involved in vascular development, angiogenesis, specification of hemangioblasts, and differentiation of veins. It promotes angiogenesis and the proliferation of endothelial cells. It inhibits inflammatory effect and preserve vascular integrity in non-nervous system diseases. Mutated AGGF1 causes susceptibility to Klippel-Trenaunay syndrome, a vascular disorder. Increased AGGF1 expression is associated with tumor angiogenesis. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438738 [Multi-domain] Cd Length: 123 Bit Score: 46.89 E-value: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 11 FFVLKKSTTIGKHEDSDLVLQSSD--IDNHHALIEFNEAEGTFVLQDFNTRNGTFVNECHIQNVAVKLIP-----GDILR 83
Cdd:cd22686 21 FIVTATGATIGREKDHGHTIRIPElgVSKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPyplthGDELK 100
|
....
gi 1958778178 84 FGSS 87
Cdd:cd22686 101 IGET 104
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
19-96 |
5.46e-06 |
|
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal transduction mechanisms, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442679 [Multi-domain] Cd Length: 402 Bit Score: 50.15 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 19 TIGKHEDSDLVLQSSD--IDNHHALIEFneAEGTFVLQDfNTRNGTFVNECHI---QNVAVKLIPGDILRFGSsgptYEL 93
Cdd:COG3456 29 TIGRSADCDWVLPDPDrsVSRRHAEIRF--RDGAFCLTD-LSTNGTFLNGSDHplgPGRPVRLRDGDRLRIGD----YEI 101
|
...
gi 1958778178 94 VIE 96
Cdd:COG3456 102 RVE 104
|
|
| FHA_MEK1-like |
cd22670 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ... |
18-87 |
6.29e-06 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine/threonine-protein kinase MEK1 and similar proteins; MEK1 (EC 2.7.11.1), also known as MRE4, is a meiosis-specific protein kinase required for chromosome synapsis and meiotic recombination. The recruitment and activation of MEK1 require the phosphorylation of the chromosome axis protein Hop1 at Thr318 (pT318), which is necessary for recognition by the MEK1 FHA domain. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438722 [Multi-domain] Cd Length: 105 Bit Score: 46.07 E-value: 6.29e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958778178 18 TTIGKHEDSDLVLQSSDIDNHHALIE---FNEAEGTFV-LQDfNTRNGTFVNECHI-QNVAVKLIPGDILRFGSS 87
Cdd:cd22670 24 ITIGRSPSCDIVINDPFVSRTHCRIYsvqFDESSAPLVyVED-LSSNGTYLNGKLIgRNNTVLLSDGDVIEIAHS 97
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
640-1141 |
6.96e-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: 50.40 E-value: 6.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 640 EHYKKIMIQSEELRAQVNASLETQQSLQEENLAEKEKLTEKLEQEEKLKARIQQLTEEKAALEE--SVAEEKNKLQGDLE 717
Cdd:TIGR04523 138 KNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELllSNLKKKIQKNKSLE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 718 mtqARVHELENdlacQKEVLESSVTQEKRKMREvLEAERRKAQDLENQLTQQKEISESNTYEKLKmrdTLEKEKRRIQDL 797
Cdd:TIGR04523 218 ---SQISELKK----QNNQLKDNIEKKQQEINE-KTTEISNTQTQLNQLKDEQNKIKKQLSEKQK---ELEQNNKKIKEL 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 798 ENRLTKQREEIE-LKGQKEDILNNKLKDALLLVEDAQQMRTAESTRAEKLSLKLKETLAELEitKAKMIMAEDRLKLQQQ 876
Cdd:TIGR04523 287 EKQLNQLKSEISdLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLK--KELTNSESENSEKQRE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 877 smkalQDERESQKHGFEEEITEYKEQIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKdsdsAQKEEVPQEFTIVPSLD 956
Cdd:TIGR04523 365 -----LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ----QEKELLEKEIERLKETI 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 957 SSAKEIacdhlIDDLlmaQKEILSQQEIIMKLRTDLGEAHTRMSDLRGELsEKQKTELERQVALVRQQNSELSILKAKVV 1036
Cdd:TIGR04523 436 IKNNSE-----IKDL---TNQDSVKELIIKNLDNTRESLETQLKVLSRSI-NKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 1037 QttglVEKKDRELKVLREALRASQEKprpyLSTE--QKPRNLSQKCDISLQIEpahpdsfssfqeeqffSDLgakcKGSR 1114
Cdd:TIGR04523 507 E----LEEKVKDLTKKISSLKEKIEK----LESEkkEKESKISDLEDELNKDD----------------FEL----KKEN 558
|
490 500
....*....|....*....|....*..
gi 1958778178 1115 HEEVIQRQKKALSELRTRIKELEKANS 1141
Cdd:TIGR04523 559 LEKEIDEKNKEIEELKQTQKSLKKKQE 585
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
316-1062 |
7.44e-06 |
|
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: 50.44 E-value: 7.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 316 LAERNTEIESLKNEGENLKRDQAITSgMVTSLQKDVSARneQVQQLQEEVNQLRIQNKEKEYQLEALTSRCSKLKEDL-- 393
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAERYKELKA-ELRELELALLVL--RLEELREELEELQEELKEAEEELEELTAELQELEEKLee 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 394 ---RKEEAQKERREAQeKELKLCRSQMQDMEKEVKKLREELKKNYTGQNVISKTLREKNKVEEKLQEDsrrkllqLQEMG 470
Cdd:TIGR02168 272 lrlEVSELEEEIEELQ-KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE-------LAELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 471 NRENLIKMNLERAVGQLENFRSQVikatfgktKPFRDKPVTDQQLIErivqvtednlsfqqrkwTLQRETHLHSKQEEVV 550
Cdd:TIGR02168 344 EKLEELKEELESLEAELEELEAEL--------EELESRLEELEEQLE-----------------TLRSKVAQLELQIASL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 551 HNveklrvlldkcqacmrdscnsmDLKKEVELLQHLQLSppvlglqkavlnilrvslswLEETEQLLGDLNIELSDSDKg 630
Cdd:TIGR02168 399 NN----------------------EIERLEARLERLEDR--------------------RERLQQEIEELLKKLEEAEL- 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 631 fslcliyllehyKKIMIQSEELRAQVNASLETQQSLQEENLAEKEKLTEKLEQEEKLKARIQQLTEEKAALEESVAEEKN 710
Cdd:TIGR02168 436 ------------KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 711 KLQGDLEMTQARvHELENDLACQKEVLE--------------------------------SSVTQEKRKMREVLEAERRK 758
Cdd:TIGR02168 504 FSEGVKALLKNQ-SGLSGILGVLSELISvdegyeaaieaalggrlqavvvenlnaakkaiAFLKQNELGRVTFLPLDSIK 582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 759 AQDLENQLTQQKE------------ISESNTYEK--------LKMRDTLE------KEKRR------------------- 793
Cdd:TIGR02168 583 GTEIQGNDREILKniegflgvakdlVKFDPKLRKalsyllggVLVVDDLDnalelaKKLRPgyrivtldgdlvrpggvit 662
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 794 ---------IQDLENRLTKQREEIELKGQKEDILNNKLKDALLLVEDAQQMRTAESTRAEKLSLKLKETLAELEITKAKM 864
Cdd:TIGR02168 663 ggsaktnssILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 865 IMAEDRLKLQQQSMKALQDERESQkhgfEEEITEYKEQIKQHSQTIVNLEERLSQvtqyyrkIEGEIATLKDSDSAQKEE 944
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEEL----EERLEEAEEELAEAEAEIEELEAQIEQ-------LKEELKALREALDELRAE 811
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 945 VPQEftivpSLDSSAKEIACDHLIDDLLMAQKEILSQQEIIMKLRTDLGEAHTRMSDLRgELSEKQKTELERQVALVRQQ 1024
Cdd:TIGR02168 812 LTLL-----NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE-ELIEELESELEALLNERASL 885
|
810 820 830
....*....|....*....|....*....|....*...
gi 1958778178 1025 NSELSILKAKVVQTTGLVEKKDRELKVLREALRASQEK 1062
Cdd:TIGR02168 886 EEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
283-1062 |
7.90e-06 |
|
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: 50.56 E-value: 7.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 283 LDEGDDHRQKEIESMKSqINALQKGYSQVLSQtLAERNTEIESLKNEGENLKRdqaitsgmvtSLQKDVSARNEQVQQLQ 362
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKS-LSKLKNKHEAMISD-LEERLKKEEKGRQELEKAKR----------KLEGESTDLQEQIAELQ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 363 EEVNQLRIQNKEKEYQLEALTSRCSKlkEDLRKEEAQKERREAQ------EKELKLCRSQMQDMEKEVKKLREELKKNYT 436
Cdd:pfam01576 229 AQIAELRAQLAKKEEELQAALARLEE--ETAQKNNALKKIRELEaqiselQEDLESERAARNKAEKQRRDLGEELEALKT 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 437 -----------GQNVISKTLREKNKVEEKLQEDSRRKLLQLQEMGNRENL--------------IKMNLERAVGQLENFR 491
Cdd:pfam01576 307 eledtldttaaQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQaleelteqleqakrNKANLEKAKQALESEN 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 492 SQVIKA----TFGKTKPFRDKPVTDQQLIERIVQVTEdnlSFQQRKWTLQRETHLHSKQEEVVHNVEKLRvllDKCQACM 567
Cdd:pfam01576 387 AELQAElrtlQQAKQDSEHKRKKLEGQLQELQARLSE---SERQRAELAEKLSKLQSELESVSSLLNEAE---GKNIKLS 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 568 RD-SCNSMDLKKEVELLQH-----LQLSPPVLGLQKAVlNILRVSLSWLEET----EQLLGDLNIELSDSDKGfslcliy 637
Cdd:pfam01576 461 KDvSSLESQLQDTQELLQEetrqkLNLSTRLRQLEDER-NSLQEQLEEEEEAkrnvERQLSTLQAQLSDMKKK------- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 638 lLEHYKKIMIQSEELRAQVNASLETQQSLQEENLAEKEKL---TEKLEQE------------------EKLKARIQQLTE 696
Cdd:pfam01576 533 -LEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLektKNRLQQElddllvdldhqrqlvsnlEKKQKKFDQMLA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 697 EKAALEESVAEEKNKLQGDLEMTQARVHELENDLacqkevlessvtQEKRKMREVLEAERRKAQDLENQLTQQKEISESN 776
Cdd:pfam01576 612 EEKAISARYAEERDRAEAEAREKETRALSLARAL------------EEALEAKEELERTNKQLRAEMEDLVSSKDDVGKN 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 777 TYEKLKMRDTLEKE----KRRIQDLENRLT-----KQREEIELKG-----------------QKEDILNNKLKDALLLVE 830
Cdd:pfam01576 680 VHELERSKRALEQQveemKTQLEELEDELQatedaKLRLEVNMQAlkaqferdlqardeqgeEKRRQLVKQVRELEAELE 759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 831 DAQQMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDRLKLQQQSMKALQDERESQKHGFEEEITEYKE---QIKQHS 907
Cdd:pfam01576 760 DERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKEsekKLKNLE 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 908 QTIVNLEERLSQVTQYYRKIEG-------EIATLKDSDSAQKEEVPQEFTIVPSLDSSAKEIACDhliddllmaqKEILS 980
Cdd:pfam01576 840 AELLQLQEDLAASERARRQAQQerdeladEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSN----------TELLN 909
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 981 QqeiimKLRTDLGEAHTRMSDLRGELSEKQKTE-----LERQVALVRQQNSEL------------SILKAKVVQTTGLVE 1043
Cdd:pfam01576 910 D-----RLRKSTLQVEQLTTELAAERSTSQKSEsarqqLERQNKELKAKLQEMegtvkskfkssiAALEAKIAQLEEQLE 984
|
890
....*....|....*....
gi 1958778178 1044 KKDRELKVLREALRASQEK 1062
Cdd:pfam01576 985 QESRERQAANKLVRRTEKK 1003
|
|
| FHA_EspA-like |
cd22698 |
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ... |
15-87 |
8.50e-06 |
|
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA is a histidine protein kinase with a fork head-associated (FHA) domain at the N-terminus and a receiver domain at the C-terminus. It functions as an inhibitor of sporulation during early fruiting body development while cells are aggregating into raised mounds. EspA is part of a two-component signal transduction system that regulates the timing of sporulation initiation. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438750 [Multi-domain] Cd Length: 93 Bit Score: 45.48 E-value: 8.50e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958778178 15 KKSTTIGKHEDSDLVLQSSDIDNHHALIEfnEAEGTFVLQDFNTRNGTFVNECHIQNVAVKliPGDILRFGSS 87
Cdd:cd22698 20 QDEFTIGRSSNNDIRLNDHSVSRHHARIV--RQGDKCNLTDLGSTNGTFLNGIRVGTHELK--HGDRIQLGET 88
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
685-933 |
1.08e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 685 EKLKARIQQLTEEKAALEEsvAEEKNKLQGDLEMTQARVHELENDLACQKEVLESSVTQEKRKMREVLEAERRKAQDLEN 764
Cdd:COG4913 228 DALVEHFDDLERAHEALED--AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 765 QLTQQkeisesntyeklkmRDTLEKEKRRIQDLENRLTKQREEIelKGQKEDILNNKLKDALLLVEDAQQMRTAESTRAE 844
Cdd:COG4913 306 RLEAE--------------LERLEARLDALREELDELEAQIRGN--GGDRLEQLEREIERLERELEERERRRARLEALLA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 845 KLSLKLKETLAELEITKAkmimaedRLKLQQQSMKALQDERESQKHGFEEEITEYKEQIKQHSQTIVNLEERLSQVTQYY 924
Cdd:COG4913 370 ALGLPLPASAEEFAALRA-------EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442
|
....*....
gi 1958778178 925 RKIEGEIAT 933
Cdd:COG4913 443 LALRDALAE 451
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
263-473 |
2.14e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 263 MAAVVAAARQSNRCDPRFQDLDEGDDHRQKEIESMKSQINALQKGYSQVLSQtLAERNTEIESLKNE----GENLKRDQA 338
Cdd:COG3883 8 APTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE-LEALQAEIDKLQAEiaeaEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 339 ITSGMVTSLQKDVSARNE-----QVQQLQEEVNQLRIQNKEKEYQLEALTSrcskLKEDLRKEEAQKERREAQEKELKLC 413
Cdd:COG3883 87 ELGERARALYRSGGSVSYldvllGSESFSDFLDRLSALSKIADADADLLEE----LKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 414 RSQMQDMEKEVKKLREELkknytgQNVISKTLREKNKVEEKLQEDSRRKLLQLQEMGNRE 473
Cdd:COG3883 163 KAELEAAKAELEAQQAEQ------EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
361-1183 |
2.20e-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: 48.81 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 361 LQEEVNQLRIQNKEKEYQLEALTSRcskLKEDLRKEEAQKERREAQEKELKLCRSQMQDMEKEVKKLREELKKNYTGQNv 440
Cdd:pfam02463 140 QGGKIEIIAMMKPERRLEIEEEAAG---SRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQL- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 441 isktLREKNKVEEKLQEDSRRKLLQLQEMGNRENLikmNLERAVGQLENFRSQVIKATFGKTKPFRDKPVTDQQLIERIV 520
Cdd:pfam02463 216 ----KEKLELEEEYLLYLDYLKLNEERIDLLQELL---RDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEEL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 521 QVTEDNLSFQQRKWTLQRETHlHSKQEEVVHNVEKLRVLLDKCQACMRDSCNSMDLKKEVELLQHLQLSPPVLGLQKAVL 600
Cdd:pfam02463 289 KLLAKEEEELKSELLKLERRK-VDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEK 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 601 NILRvslswLEETEQLLGDLNIELSDSDKGFSLCLIYLLEHYKKIMIQSEELRAQVNASLETQQSLQEENLAEKEKLTEK 680
Cdd:pfam02463 368 LEQL-----EEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELK 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 681 LEQEEKLKARIQQLTEEKAALEESVAEEKNKLQGDLEMTQARVHELENDLacQKEVLESSVTQEKRKMREVLEAERRKAQ 760
Cdd:pfam02463 443 QGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSR--QKLEERSQKESKARSGLKVLLALIKDGV 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 761 DLENQLTQQKEISESNTYEKLK--------------MRDTLEKEKRRIQDLENRLTKQREEIEL-KGQKEDILNNKLKDA 825
Cdd:pfam02463 521 GGRIISAHGRLGDLGVAVENYKvaistavivevsatADEVEERQKLVRALTELPLGARKLRLLIpKLKLPLKSIAVLEID 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 826 LLLVEDAQQMRTAESTRAEK--LSLKLKETLAELEITKAKMIMAEDRLKLQQQSMKALQDERESQKHGFEEEITEYKEQI 903
Cdd:pfam02463 601 PILNLAQLDKATLEADEDDKraKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQE 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 904 KQHSQTIVNLEERLSQVTQYYRKIEGEIATLKDSDSAQKEEVPQEFTIVPSLDSSAKEIACDHLIDDllmaqkEILSQQE 983
Cdd:pfam02463 681 LQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDE------EEEEEEK 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 984 IIMKLRTDLGEAHTRMSDLRGELSEKQKTELERQVALVRQQNSELSILKAKVVQTTGLVEKKDRELKVLREALRASQEKP 1063
Cdd:pfam02463 755 SRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEE 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 1064 RPYLSTEQKPRNLSQKCDISLQIEpahpdsfssFQEEQFFSDLGAKCKGSRHEEVIQRQKKALSELRTRIKELEKANSSN 1143
Cdd:pfam02463 835 LEELALELKEEQKLEKLAEEELER---------LEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEE 905
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 1958778178 1144 HKDHVNESFLELKTLRMEKNVQKILLDAKPDLTTFSRVEI 1183
Cdd:pfam02463 906 SQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEA 945
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
622-843 |
2.91e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 48.39 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 622 IELSDSDKGFSL------------CLIYLLEHYKKIMIQSEELRAQVNASLETQQSLQEENLAEKEK-LTEKLEQEEKLK 688
Cdd:PRK05771 34 EDLKEELSNERLrklrslltklseALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKeIKELEEEISELE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 689 ARIQQLTEEKAALE--ESVaEEKNKLQGDLEMTQARVHELENDLACQKEVLESS-----VTQEKRKMREVLEAERRKAQD 761
Cdd:PRK05771 114 NEIKELEQEIERLEpwGNF-DLDLSLLLGFKYVSVFVGTVPEDKLEELKLESDVenveyISTDKGYVYVVVVVLKELSDE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 762 LENQLtQQKEISESNTYEKLKMRDTLEKEKRRIQDLENRLTKQREEIELKGQKEDILNNKLKDALLLVEDAQQM--RTAE 839
Cdd:PRK05771 193 VEEEL-KKLGFERLELEEEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLEIELERAEAlsKFLK 271
|
....
gi 1958778178 840 STRA 843
Cdd:PRK05771 272 TDKT 275
|
|
| FHA_FhaA-like |
cd22668 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
17-87 |
2.94e-05 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaA and similar proteins; FhaA regulates cell growth and peptidoglycan synthesis by binding to MviN. It may inhibit the late stages of peptidoglycan synthesis. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438720 [Multi-domain] Cd Length: 91 Bit Score: 43.99 E-value: 2.94e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958778178 17 STTIGKHEDSDLVLQSSDIDNHHALIEFNeaEGTFVLQDFNTRNGTFVNECHIQnVAVKLIPGDILRFGSS 87
Cdd:cd22668 19 SNIIGRGSDADFRLPDTGVSRRHAEIRWD--GQVAHLTDLGSTNGTTVNNAPVT-PEWRLADGDVITLGHS 86
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
405-731 |
3.08e-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: 48.51 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 405 AQEKELKLCRSQMQDMEKEVKKLREELKKNYTGQNVISKTLREKNKVEEKLQEDSRRKLLQLQEMGNRENLIKMNLERAV 484
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 485 GQLENFRSQvikatfgKTKPFRDKPVTDQQLIERIVQVTEDNLSFQQRKWTLQRETHLHSKQEEVVHNV-EKLRVLLDKC 563
Cdd:TIGR02168 754 KELTELEAE-------IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLnEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 564 QACMRdscNSMDLKKEVELLQhlqlsppvlgLQKAVLN--ILRVSLSwLEETEQLLGDLNIELSDsdkgfslcliyLLEH 641
Cdd:TIGR02168 827 ESLER---RIAATERRLEDLE----------EQIEELSedIESLAAE-IEELEELIEELESELEA-----------LLNE 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 642 YKKIMIQSEELRAQVNASLETQQSLQEENLAEKEKLTEKLEQEEKLKARIQ-----------QLTEEKAALEESVAEEKN 710
Cdd:TIGR02168 882 RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEglevridnlqeRLSEEYSLTLEEAEALEN 961
|
330 340
....*....|....*....|.
gi 1958778178 711 KLQGDLEMTQARVHELENDLA 731
Cdd:TIGR02168 962 KIEDDEEEARRRLKRLENKIK 982
|
|
| Yop-YscD_cpl |
pfam16697 |
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ... |
19-86 |
3.48e-05 |
|
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.
Pssm-ID: 465238 [Multi-domain] Cd Length: 94 Bit Score: 43.79 E-value: 3.48e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958778178 19 TIGKHEDSDLVLQSSDIDNHHALIEFnEAEGtFVLQDFNTRNGTFVNECHIQNVAVKLIPGDILRFGS 86
Cdd:pfam16697 20 RIGSDPDCDIVLSDKEVSRVHLKLEV-DDEG-WRLDDLGSGNGTLVNGQRVTELGIALRPGDRIELGQ 85
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
640-817 |
3.52e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 640 EHYKKIMIQSEELRAQVNA--------SLETQQSLQEENLAEKEKLTEKLEQeekLKARIQQLTEEKAALEESVAE---- 707
Cdd:COG4913 262 ERYAAARERLAELEYLRAAlrlwfaqrRLELLEAELEELRAELARLEAELER---LEARLDALREELDELEAQIRGnggd 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 708 EKNKLQGDLEMTQARVHELENDLACQKEVLEsSVTQEKRKMREVLEAERRKAQDLENQLTQQKEisesntyeklKMRDTL 787
Cdd:COG4913 339 RLEQLEREIERLERELEERERRRARLEALLA-ALGLPLPASAEEFAALRAEAAALLEALEEELE----------ALEEAL 407
|
170 180 190
....*....|....*....|....*....|.
gi 1958778178 788 EKEKRRIQDLENRLTKQREEIE-LKGQKEDI 817
Cdd:COG4913 408 AEAEAALRDLRRELRELEAEIAsLERRKSNI 438
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
740-1136 |
4.31e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 48.15 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 740 SVTQEKRKMREVLEAERRKAQDLENQLT-QQKEISE------------SNTYEKLKMRDTLEKEKRRIQDLENRLTKQRE 806
Cdd:COG5022 804 SLLGSRKEYRSYLACIIKLQKTIKREKKlRETEEVEfslkaevliqkfGRSLKAKKRFSLLKKETIYLQSAQRVELAERQ 883
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 807 EIELKGQKE------DILNNKLKDALLLVEDAQQMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDRLKLQQqsmka 880
Cdd:COG5022 884 LQELKIDVKsisslkLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNK----- 958
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 881 LQDERESQKhgfeEEITEYKEQIKQHSQTIVNLEERLSQVTQYYRKIeGEIATLKDSDSAQKEEVPQEFTIVPSLDSSAK 960
Cdd:COG5022 959 LHEVESKLK----ETSEEYEDLLKKSTILVREGNKANSELKNFKKEL-AELSKQYGALQESTKQLKELPVEVAELQSASK 1033
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 961 eiacdhliddLLMAQKEILSQQEIIMKLRTDLGEA--HTRMSDLRGELSEKQKTELERQVALVRQQNSELSILKAKVVQT 1038
Cdd:COG5022 1034 ----------IISSESTELSILKPLQKLKGLLLLEnnQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEV 1103
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 1039 TGL-VEKKDRELKVLREALRASQEKPRPYLSTEQKPRNLSQK--------------CDISLQIEPAHPDSFSSFQEEQFF 1103
Cdd:COG5022 1104 TNRnLVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVfqklsvlqleldglFWEANLEALPSPPPFAALSEKRLY 1183
|
410 420 430
....*....|....*....|....*....|...
gi 1958778178 1104 SDLGAKCKGSRHEEVIQRQKKALSELRTRIKEL 1136
Cdd:COG5022 1184 QSALYDEKSKLSSSEVNDLKNELIALFSKIFSG 1216
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
744-960 |
4.41e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 744 EKRKMREVLEAERRKAQDLENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQDLENRLTKQREEIElkgQKEDILNNKLK 823
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE---ERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 824 ------------DALL-------LVEDAQQMRTAESTRAEKLSlKLKETLAELEITKAKMIMAEDRLKLQQQSMKALQDE 884
Cdd:COG3883 94 alyrsggsvsylDVLLgsesfsdFLDRLSALSKIADADADLLE-ELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958778178 885 RESQKHGFEEEITEYKEQIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKDSDSAQKEEVPQEFTIVPSLDSSAK 960
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
661-810 |
5.16e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 47.25 E-value: 5.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 661 ETQQSLQEENLAEKEKLTEKLEQE-----EKLKARIQQLTEEKAALEESvaEEKNKLQgdLEMTQARVHELENDLACQKE 735
Cdd:pfam15709 358 EEQRRLQQEQLERAEKMREELELEqqrrfEEIRLRKQRLEEERQRQEEE--ERKQRLQ--LQAAQERARQQQEEFRRKLQ 433
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958778178 736 VLESSVTQEKrkmREVLEAERRKAQDLENQLT-QQKEISESNTYEKLK-MRDTLEKEKRRIQDLENRLTKQREEIEL 810
Cdd:pfam15709 434 ELQRKKQQEE---AERAEAEKQRQKELEMQLAeEQKRLMEMAEEERLEyQRQKQEAEEKARLEAEERRQKEEEAARL 507
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
249-429 |
7.02e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 7.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 249 LQAEIADLSQRLSEMAAVVAAARQSNrcdpRFQDLDEGDDHRQKEIESMKSQINALQ------KGYSQVLSQTLAERNTE 322
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKN----GLVDLSEEAKLLLQQLSELESQLAEARaelaeaEARLAALRAQLGSGPDA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 323 IESLKNEGE--NLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEVNQLRIQ-NKEKEYQLEALTSRCSKLKEDLRKEEAQ 399
Cdd:COG3206 256 LPELLQSPViqQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQlQQEAQRILASLEAELEALQAREASLQAQ 335
|
170 180 190
....*....|....*....|....*....|
gi 1958778178 400 KERREAQEKELKLCRSQMQDMEKEVKKLRE 429
Cdd:COG3206 336 LAQLEARLAELPELEAELRRLEREVEVARE 365
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
639-1056 |
7.07e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.20 E-value: 7.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 639 LEHYKKIMIQSEELRAQVNASLETQQSLQEEN-----LAEKE-KLTEKLEQEEKLKARIQQLTEEKAALEESVAEEKNKL 712
Cdd:PRK01156 321 INKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNnqileLEGYEmDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQ 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 713 QGDLEMTQARVHELENDLAcQKEVLESSVTQEKRKMREVLEAERRKAQDLENQ---------LTQQK--EISESNTYEKL 781
Cdd:PRK01156 401 EIDPDAIKKELNEINVKLQ-DISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcgttLGEEKsnHIINHYNEKKS 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 782 KMRDTLEKEKRRIQDLENRLT--KQREEIELKGQKEDILN--NKLKDALLLVEDaqqMRTAESTraeklsLKLKETLAEL 857
Cdd:PRK01156 480 RLEEKIREIEIEVKDIDEKIVdlKKRKEYLESEEINKSINeyNKIESARADLED---IKIKINE------LKDKHDKYEE 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 858 EITKAKMIMAEDRLKLQQQSMKALQD----ERESQKHGFEEEITEYKEQIKQHSQTIVNLEERLSQVTQYYRKIEGEIAT 933
Cdd:PRK01156 551 IKNRYKSLKLEDLDSKRTSWLNALAVisliDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANN 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 934 LKDSDSAQKEEVPQEFTIVPSLDSSAKEIAcdhLIDDLLMAQKEILSQqeiIMKLRTDLGEAHTRMSDLRGELSEKQKTe 1013
Cdd:PRK01156 631 LNNKYNEIQENKILIEKLRGKIDNYKKQIA---EIDSIIPDLKEITSR---INDIEDNLKKSRKALDDAKANRARLEST- 703
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1958778178 1014 lerqVALVRQQNSELSILKA---KVVQTTGLVEKKDRELKVLREAL 1056
Cdd:PRK01156 704 ----IEILRTRINELSDRINdinETLESMKKIKKAIGDLKRLREAF 745
|
|
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
38-85 |
1.15e-04 |
|
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and similar proteins; SLMAP, also called sarcolemmal-associated protein (SLAP), is a tail-anchored protein involved in fundamental cellular processes, such as myoblast fusion, cell cycle progression, and chromosomal inheritance. It is a cardiac membrane protein that plays an important role in E-C coupling and the adrenergic response of the heart. Overexpression of the SLMAP gene has been associated with diabetes and endothelial dysfunction of macro- and micro-blood vessels. SLMAP contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438731 [Multi-domain] Cd Length: 126 Bit Score: 43.03 E-value: 1.15e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1958778178 38 HHALIEFNEaeGTFVLQDFNTRNGTFVNECHIQ-----NVAVKLIPGDILRFG 85
Cdd:cd22679 52 NHALLWYDD--GKFYLQDTKSSNGTFVNNQRLSkgseeSEPRELHSGDIVQFG 102
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
741-1035 |
1.17e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 46.75 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 741 VTQEKRKMREVLEAERRKAQDLENQLTQQKEISESNTY----EKLKMRDTLEKEKRRIQDLENRLTKQREEIELKGQKED 816
Cdd:PTZ00440 1075 IKEEIKLLEEKVEALLKKIDENKNKLIEIKNKSHEHVVnadkEKNKQTEHYNKKKKSLEKIYKQMEKTLKELENMNLEDI 1154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 817 ILNN----KLKDALLLVEDAQQMRTAESTRAEKLSLKLKETLAELEITKAKMImAEDRLKLQQQSMKALQDERESQKHGF 892
Cdd:PTZ00440 1155 TLNEvneiEIEYERILIDHIVEQINNEAKKSKTIMEEIESYKKDIDQVKKNMS-KERNDHLTTFEYNAYYDKATASYENI 1233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 893 EEEITEYK--EQIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKDSDSAQKEEvpQEFTIVPSLDSSAKEIA-----CD 965
Cdd:PTZ00440 1234 EELTTEAKglKGEANRSTNVDELKEIKLQVFSYLQQVIKENNKMENALHEIKNM--YEFLISIDSEKILKEILnstkkAE 1311
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 966 HLIDDllmAQKEILSQQEIIMKLRTDLGEAHTRMSDLRGELSEKQkteLERQVALVRQQNSELSILKAKV 1035
Cdd:PTZ00440 1312 EFSND---AKKELEKTDNLIKQVEAKIEQAKEHKNKIYGSLEDKQ---IDDEIKKIEQIKEEISNKRKEI 1375
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
246-458 |
1.31e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.17 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 246 IMNLQAEIADLSQRLSEmaavvaAARQSNRCDPRFQDLDEGDDHRQKEIESMKSQINALQKGYSQvLSQTLAERNTEIES 325
Cdd:TIGR04523 386 IKNLESQINDLESKIQN------QEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD-LTNQDSVKELIIKN 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 326 LKNEGENLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEVNQLRIQNKEKEYQLEALTSRCSKLKEDLRKEEAQKERREa 405
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKE- 537
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958778178 406 qekelklcrSQMQDMEKEVKKLREELKKnytgqNVISKTLREKNKVEEKLQED 458
Cdd:TIGR04523 538 ---------SKISDLEDELNKDDFELKK-----ENLEKEIDEKNKEIEELKQT 576
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
641-1064 |
1.31e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 641 HYKKImiqseELRAQVNA------------------SLETQQSLQEENLAEKEKLTE--KLEQEEKLKARIQQLTEEKAA 700
Cdd:PTZ00121 1056 HEGKA-----EAKAHVGQdeglkpsykdfdfdakedNRADEATEEAFGKAEEAKKTEtgKAEEARKAEEAKKKAEDARKA 1130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 701 LEESVAEEKNKLQGDLEMTQARVHELENDLACQKEVLESSVTQEKRKMREVLEAER-RKAQDLEnQLTQQKEISESNTYE 779
Cdd:PTZ00121 1131 EEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEvRKAEELR-KAEDARKAEAARKAE 1209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 780 KLKMRDTLEK--EKRRIQDLEnRLTKQREEIELKGQKEDILNNKLKDALLLVEDAQQMRTAESTRAEklslklkETLAEL 857
Cdd:PTZ00121 1210 EERKAEEARKaeDAKKAEAVK-KAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE-------EARKAD 1281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 858 EITKAKMIMAEDRLKLQQQSMKALQDERESQKHGFEEEITEYKEQIKQHSQTIVNLEERlsqvtqyyRKIEGEIATLKDS 937
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEE--------AKKAAEAAKAEAE 1353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 938 DSAQKEEVPQEFTIVPSLDSSAKEIACDHLiddllmaqKEILSQQEIIMKLRTDLGEAHTRMSDLRGELSEKQKTELERQ 1017
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAA--------KKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKK 1425
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1958778178 1018 VALVRQQNSELSiLKAKVVQTTGLVEKKDRELKVLREALRASQEKPR 1064
Cdd:PTZ00121 1426 KAEEKKKADEAK-KKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
|
| FHA_NBN |
cd22667 |
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ... |
11-91 |
1.33e-04 |
|
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also called cell cycle regulatory protein p95, or Nijmegen breakage syndrome protein 1 (NBS1), is a novel DNA double-strand break repair protein that is mutated in Nijmegen breakage syndrome. It is a component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. Nibrin modulates the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-dependent protein kinase catalytic subunit (DNA-PKcs) to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. Nibrin also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. Nibrin is a major player in the control of intra-S-phase checkpoint. This subfamily also includes Schizosaccharomyces pombe DNA repair and telomere maintenance protein Nbs1 and Arabidopsis thaliana AtNbs1. SpNbs1 is an FHA domain-containing protein required for DNA damage repair and S-phase DNA damage checkpoint. It is involved in telomere length maintenance and maintenance of chromatin structure. AtNbs1 is a component of MRN complex. It also functions in the very early stages of meiosis. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438719 [Multi-domain] Cd Length: 108 Bit Score: 42.31 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 11 FFVLKKSTTIGKHEDSDLVLQSSDIDNHHALI-----EFNEAEG----TFVLQDFNtRNGTFVNECHIQNVA-VKLIPGD 80
Cdd:cd22667 15 YLLPGGEYTVGRKDCDIIIVDDSSISRKHATLtvlhpEANLSDPdtrpELTLKDLS-KYGTFVNGEKLKGGSeVTLKDGD 93
|
90
....*....|.
gi 1958778178 81 ILRFGSSGPTY 91
Cdd:cd22667 94 VITFGVLGSKF 104
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
249-437 |
1.73e-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: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 249 LQAEIADLSQRLSEMAAVVAAAR-QSNRCDPRFQDLDEGDDHR---------QKEIESMKSQINALQKGYSQV--LSQTL 316
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEaELDALQERREALQRLAEYSwdeidvasaEREIAELEAELERLDASSDDLaaLEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 317 AERNTEIESLKNEGENLKRDQAitsgmvtSLQKDVSARNEQVQQLQEEVNqlRIQNKEKEYQLEALTSRCsklkEDLRKE 396
Cdd:COG4913 695 EELEAELEELEEELDELKGEIG-------RLEKELEQAEEELDELQDRLE--AAEDLARLELRALLEERF----AAALGD 761
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958778178 397 EAQKERREAQEKELKLCRSQMQDMEKEVKKLREELKKNYTG 437
Cdd:COG4913 762 AVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPA 802
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
222-434 |
1.73e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 222 ILLLGREINRLSDFEMESKYKDAVIMNLQAEIADLSQRLSEMAavvaaarqsnrcdprFQDLDEgDDHRQKEIESMKSQI 301
Cdd:PRK03918 541 IKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELG---------------FESVEE-LEERLKELEPFYNEY 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 302 NALQKGYSQvlsqtLAERNTEIESLKNEGENLKRDQAITSGMVTSLQKDVSARN-----EQVQQLQEEVNQLRIQNKEKE 376
Cdd:PRK03918 605 LELKDAEKE-----LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEkkyseEEYEELREEYLELSRELAGLR 679
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958778178 377 YQLEALTSRCSKLKEDLRKEEAQKERREAQEKELKL---CRSQMQDMEKEVKKLREELKKN 434
Cdd:PRK03918 680 AELEELEKRREEIKKTLEKLKEELEEREKAKKELEKlekALERVEELREKVKKYKALLKER 740
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
348-469 |
1.82e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.97 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 348 QKDVSARNEQVQQLQEEVNQLRIQNKEKEYQLEALTSRCSKLKEDLrkeEAQKERREAQEKELKlcrsqmQDMEKEVKKL 427
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEEL---EEKKEKLQEEEDKLL------EEAEKEAQQA 578
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1958778178 428 REELKKNytgQNVISKTLREKNK-----VEEKLQEDSRRKLLQLQEM 469
Cdd:PRK00409 579 IKEAKKE---ADEIIKELRQLQKggyasVKAHELIEARKRLNKANEK 622
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
648-1071 |
1.98e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.73 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 648 QSEELRAQVNASLETQQSLQEENLAEKEKLTEKLEQEEKLKARI------QQLTEEKAALEESVAEEKNKLQGDLEMTQA 721
Cdd:TIGR00618 188 KKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLrealqqTQQSHAYLTQKREAQEEQLKKQQLLKQLRA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 722 RVHELEN------------DLACQKEVL---ESSVTQEKRKMREVL-----------------------EAERRKAQDLE 763
Cdd:TIGR00618 268 RIEELRAqeavleetqeriNRARKAAPLaahIKAVTQIEQQAQRIHtelqskmrsrakllmkraahvkqQSSIEEQRRLL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 764 NQLTQQKEISESNTYEKLKMRDTLEKEKrriqDLENRLTKQREEIELKGQKEDILNNKLK---------DALLLVEDAQQ 834
Cdd:TIGR00618 348 QTLHSQEIHIRDAHEVATSIREISCQQH----TLTQHIHTLQQQKTTLTQKLQSLCKELDilqreqatiDTRTSAFRDLQ 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 835 MRTAESTRAEKLSLKLKE-------------TLAELEITKAKMIMAEDRLKLQQQSMKALQDERESQKHG-----FEEEI 896
Cdd:TIGR00618 424 GQLAHAKKQQELQQRYAElcaaaitctaqceKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLarlleLQEEP 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 897 TEYKEQIKQHSQTIVNLEE------RLSQVTQYYRKIEGEIATLKD----------SDSAQKEEVPQEFTIVPSLDSSAK 960
Cdd:TIGR00618 504 CPLCGSCIHPNPARQDIDNpgpltrRMQRGEQTYAQLETSEEDVYHqltserkqraSLKEQMQEIQQSFSILTQCDNRSK 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 961 EIacdhlIDDLLMAQKEILSQQEIIMKLRTDLGEAhtrmsdLRGELSEKQKTELERQVALVRQQNSELSILKAKVVQTTG 1040
Cdd:TIGR00618 584 ED-----IPNLQNITVRLQDLTEKLSEAEDMLACE------QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQ 652
|
490 500 510
....*....|....*....|....*....|.
gi 1958778178 1041 LVEKKDRElkvlREALRASQEKPRPYLSTEQ 1071
Cdd:TIGR00618 653 LTLTQERV----REHALSIRVLPKELLASRQ 679
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
246-479 |
2.07e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.58 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 246 IMNLQAEIADLSQRLSEMA-AVVAAARQSNRCDPRFQDLDEGDDHRQKEIESMKSQINALQKgysqvlsqtlaERNTEIE 324
Cdd:pfam10174 403 IENLQEQLRDKDKQLAGLKeRVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDR-----------ERLEELE 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 325 SLKNEGENLKRDqaitsgmVTSLQKDVSARNEQVQQLQEEVNQLRIQNKEKEYQLEALTSRCSKLKEDLRKEEAQKERRE 404
Cdd:pfam10174 472 SLKKENKDLKEK-------VSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAH 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 405 AQEKELKLC---RSQMQDMEKEVKKLREELKKNYTGQNVISKTLR----EKNKVEEKLQEDSRRKLLQLQEMGNRENLIK 477
Cdd:pfam10174 545 NAEEAVRTNpeiNDRIRLLEQEVARYKEESGKAQAEVERLLGILRevenEKNDKDKKIAELESLTLRQMKEQNKKVANIK 624
|
..
gi 1958778178 478 MN 479
Cdd:pfam10174 625 HG 626
|
|
| FHA_GarA-like |
cd22720 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis glycogen accumulation ... |
11-65 |
2.51e-04 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis glycogen accumulation regulator GarA and similar proteins; GarA is an FHA domain-containing protein involved in the regulation of glutamate metabolism. It acts as a phosphorylation-dependent ON/OFF molecular switch that modulates the activities of KGD, GDH and GltB. Its FHA domain has dual specificity. It binds to both phosphorylated upstream partners, such as the kinases PknB and PknG, and nonphosphorylated downstream partners, such as the 2-oxoglutarate decarboxylase KGD. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438772 [Multi-domain] Cd Length: 100 Bit Score: 41.53 E-value: 2.51e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1958778178 11 FFVLKKSTTIGKHEDSDLVLQSSDIDNHHAliEFNEAEGTFVLQDFNTRNGTFVN 65
Cdd:cd22720 19 FLLDQAITSAGRHPDSDIFLDDVTVSRRHA--EFRLENNEFNVVDVGSLNGTYVN 71
|
|
| FHA_OdhI-like |
cd22721 |
forkhead associated (FHA) domain found in Corynebacterium glutamicum oxoglutarate ... |
11-65 |
2.55e-04 |
|
forkhead associated (FHA) domain found in Corynebacterium glutamicum oxoglutarate dehydrogenase inhibitor (OdhI) and similar proteins; OdhI is an essential component of the PknG signaling pathway. It regulates glutamate production under biotin non-limiting conditions. It can inhibit the activity of 2-oxoglutarate dehydrogenase only when it is unphosphorylated. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438773 [Multi-domain] Cd Length: 102 Bit Score: 41.61 E-value: 2.55e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1958778178 11 FFVLKKSTTIGKHEDSDLVLQSSDIDNHHAliEFNEAEGTFVLQDFNTRNGTFVN 65
Cdd:cd22721 24 FLLDQPTTTAGRHPESDIFLDDVTVSRRHA--EFRINEGEFEVVDVGSLNGTYVN 76
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
672-959 |
2.59e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 672 AEKEKLTEKLEQEEKLKARIQQLTEEKAALEEsvaeEKNKLQGDLEMTQARVHELENDLAcqkeVLESSVTQEKRKMREV 751
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNE----EYNELQAELEALQAEIDKLQAEIA----EAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 752 LEAerrkaqdlenqltQQKEISESNTYEKLKMRDTLEKEKRRIQDLENRLTKQREEIElkgqkedilnnKLKDALLLVED 831
Cdd:COG3883 92 ARA-------------LYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLE-----------ELKADKAELEA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 832 AQQMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDRLKLQQQSMKALQDERESQKHGFEEEITEYKEQIKQHSQTIV 911
Cdd:COG3883 148 KKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1958778178 912 NLEERLSQVTQYYRKIEGEIATLKDSDSAQKEEVPQEFTIVPSLDSSA 959
Cdd:COG3883 228 AAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAG 275
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
576-721 |
2.92e-04 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 45.05 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 576 LKKEVELLQhLQLSPPVLGLQKAVLNiLRVSLSWLEETEQLLGDLNIELSDSDKGFSLC---LIYLLEHYKKIMIQSEEL 652
Cdd:pfam05911 686 LKEEFEQLK-SEKENLEVELASCTEN-LESTKSQLQESEQLIAELRSELASLKESNSLAetqLKCMAESYEDLETRLTEL 763
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958778178 653 RAQVNASLETQQSL----QEENLAEKEKLTEKLEQEEKLkariqQLTEEKAALEESVAEEKNKLQGDLEMTQA 721
Cdd:pfam05911 764 EAELNELRQKFEALevelEEEKNCHEELEAKCLELQEQL-----ERNEKKESSNCDADQEDKKLQQEKEITAA 831
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
4-85 |
3.01e-04 |
|
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing protein ArnA and similar proteins; ArnA is an FHA domain-containing protein from Sulfolobus acidocaldarius that was shown to strongly interact with ArnB, a von Willebrand domain-containing protein. They act synergistically and negatively to modulate motility. ArnA is involved in regulating archaella expression in S. acidocaldarius. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438732 [Multi-domain] Cd Length: 96 Bit Score: 41.17 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 4 YLKSPDgfFVLKK------STTIGKHEDSDLVLQSSDIDNHHALIEFNEaeGTFVLQDFNTRNGTFVNECHIQNVAVKLI 77
Cdd:cd22680 5 ILSSPN--LTGKKfpfdfsSVSIGRDPENVIVIPDPFVSRNHARITVDS--NEIYIEDLGSTNGTFVNDFKRIKGPAKLH 80
|
....*...
gi 1958778178 78 PGDILRFG 85
Cdd:cd22680 81 PNDIIKLG 88
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
600-1167 |
3.06e-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: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 600 LNILRVSLSWLEETEQLLGDLNIELSDSDKGFSLcliyLLEHYKKIMIQSEELRAQVNASLETQQSLQEENLAEKEKLTE 679
Cdd:TIGR04523 196 LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQ----LKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 680 KLEQEEKLKARIQQLTEEKAALEESVAEEKN--------KLQGDLEMTQARVHELENDLAcQKEVLESSVTQEKRKMREV 751
Cdd:TIGR04523 272 KQKELEQNNKKIKELEKQLNQLKSEISDLNNqkeqdwnkELKSELKNQEKKLEEIQNQIS-QNNKIISQLNEQISQLKKE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 752 LEAERRKAQDLENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQDLENRLTKQREEIELKGQKEDilnnKLKDALLLVED 831
Cdd:TIGR04523 351 LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIK----KLQQEKELLEK 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 832 AQQMRTAESTRAEKLSLKLKETLAELEITKAKMimaEDRLKLQQQSMKALQDERESQKHGFEE----------EITEYKE 901
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNQDSVKELIIKNL---DNTRESLETQLKVLSRSINKIKQNLEQkqkelkskekELKKLNE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 902 QIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKDSDSAQKEEVpqeFTIVPSLDSSAKEIACDHL---IDDLLMAQKEI 978
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDEL---NKDDFELKKENLEKEIDEKnkeIEELKQTQKSL 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 979 LSQQEiimKLRTDLGEAHTRMSDLRGELSEKQKT--ELERQVALVRQQNSELSILKAKVVQTTglvEKKDRELKVLREAL 1056
Cdd:TIGR04523 581 KKKQE---EKQELIDQKEKEKKDLIKEIEEKEKKisSLEKELEKAKKENEKLSSIIKNIKSKK---NKLKQEVKQIKETI 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 1057 RASQEKprpYLSTEQKPRNLSQKCDislqiepahpdsfssfqeeqffsdlgakckgsrheEVIQRQKKALSELRTRIKEl 1136
Cdd:TIGR04523 655 KEIRNK---WPEIIKKIKESKTKID-----------------------------------DIIELMKDWLKELSLHYKK- 695
|
570 580 590
....*....|....*....|....*....|.
gi 1958778178 1137 ekaNSSNHKDHVNESFLELKTLRMEKNVQKI 1167
Cdd:TIGR04523 696 ---YITRMIRIKDLPKLEEKYKEIEKELKKL 723
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
661-919 |
3.28e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 661 ETQQSLQEENLAEKEKLTEKLEQEEKLKARIQQLTEEKAALEEsvaeeknKLQGDLEMTqARVHELENDLACQKEVLEss 740
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQE-------QLQAETELC-AEAEEMRARLAARKQELE-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 741 vtqekrkmrEVLeaerrkaQDLENQLTQQKEISESNTYEKLKMrdtlekeKRRIQDLENRLTKQ---REEIELKGQKEDI 817
Cdd:pfam01576 75 ---------EIL-------HELESRLEEEEERSQQLQNEKKKM-------QQHIQDLEEQLDEEeaaRQKLQLEKVTTEA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 818 LNNKLKDALLLVEDAQQMRTAESTRAEKLSLKLKETLAELEiTKAKMImaeDRLKLQQQSMKALQDER-----------E 886
Cdd:pfam01576 132 KIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEE-EKAKSL---SKLKNKHEAMISDLEERlkkeekgrqelE 207
|
250 260 270
....*....|....*....|....*....|...
gi 1958778178 887 SQKHGFEEEITEYKEQIKQHSQTIVNLEERLSQ 919
Cdd:pfam01576 208 KAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
292-769 |
3.36e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.81 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 292 KEIESMKSQINALQKGYSQvLSQTLAERNTEIESLKNEGENLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEVNQLRIQ 371
Cdd:pfam10174 275 KQMEVYKSHSKFMKNKIDQ-LKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLR 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 372 NKEKEY-------QLEALTSRCSKLK---EDLRKEEAQKERR-EAQEKELKLCRSQMQDMEKEVKKLREELKKNYTGQN- 439
Cdd:pfam10174 354 LEEKESflnkktkQLQDLTEEKSTLAgeiRDLKDMLDVKERKiNVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSn 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 440 ------VISKTLREKNKVEEKLQE--------------DSRRKLLQLQEMGNRENLIKMNLERAVGQLENFRSQVIKATF 499
Cdd:pfam10174 434 tdtaltTLEEALSEKERIIERLKEqreredrerleeleSLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGL 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 500 GKTKPFRDKPVTDQQLIERIVQVTEDNLSFQQRKWTLQRETHLHSKQEEVVHNVEKLRVLLDKCQAcmrDSCNSMDLKKE 579
Cdd:pfam10174 514 KKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQA---EVERLLGILRE 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 580 VELLQHLQlsppvlglQKAVLNIlrVSLSWLEETEQLLGDLNIELSDSdkgfslcliylLEHYKKIMIQSEELRAQVNAS 659
Cdd:pfam10174 591 VENEKNDK--------DKKIAEL--ESLTLRQMKEQNKKVANIKHGQQ-----------EMKKKGAQLLEEARRREDNLA 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 660 LETQQSLQEENLAEKEKLTEKLEQ-EEKLKARIQQLTEEKAALEESVAEEKNKLQGDLEMTQ----ARVHELENDLAcqk 734
Cdd:pfam10174 650 DNSQQLQLEELMGALEKTRQELDAtKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQeallAAISEKDANIA--- 726
|
490 500 510
....*....|....*....|....*....|....*
gi 1958778178 735 eVLESSVTQEKRKMREVLeAERRKAQDLENQLTQQ 769
Cdd:pfam10174 727 -LLELSSSKKKKTQEEVM-ALKREKDRLVHQLKQQ 759
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
236-810 |
3.53e-04 |
|
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227569 [Multi-domain] Cd Length: 669 Bit Score: 44.68 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 236 EMESKYKDAVIMNLQAEIADLSQRLSEmaAVVAAARQSNRCDPRFQDLDEGDDHRQKEIESMKSQINALQKGYSQVLSQT 315
Cdd:COG5244 104 EDRIHFEESKIRRLEETIEALKSTEKE--EIVELRRENEELDKINLSLRERISSEEPELNKDGSKLSYDELKEFVEESRV 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 316 LAERNTEIESLKNEGENLKRD-------QAITSGMVTSLQKDVSARNEQVQQLQEEVNQLRIQnkekeyqleaLTSRCSK 388
Cdd:COG5244 182 QVYDMVELVSDISETLNRNGSiqrssvrECERSNIHDVLFLVNGILDGVIDELNGELERLRRQ----------LVSLMSS 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 389 LkedlrkeEAQKERREAQEKELKlcrsQMQDMEKEVKKLREELKKNytgqnvisKTLREKNKVEEKLQEDSRRKLLQ-LQ 467
Cdd:COG5244 252 H-------GIEVEENSRLKATLE----KFQSLELKVNTLQEELYQN--------KLLKKFYQIYEPFAQAALSSQLQyLA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 468 EMGNRENLIKMNLERaVGQLENFRSQVIKATFGKTKPFRDK-PVTDQQLIERIVQVTEDNLSFQQRKWTLQRETHLHSKQ 546
Cdd:COG5244 313 EVIESENFGKLENIE-IHIILKVLSSISYALHIYTIKNTPDhLETTLQCFVNIAPISMWLSEFLQRKFSSKQETAFSICQ 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 547 -----EEVVHNVEKLRVLLDKcqacmrdscNSMDLKKEVELLQHLQlSPPVLGLQKAVLNILRVS-LSWLEETEQLLGDL 620
Cdd:COG5244 392 flednKDVTLILKILHPILET---------TVPKLLAFLRTNSNFN-DNDTLCLIGSLYEIARIDkLIGKEEISKQDNRL 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 621 NIelsdsdkgFSLCLIYLLEHYKKIMIQSEELRAQVNASLETQQSLQEENLAEKEKLTEKLEQEEKLKARiqqLTEEKAA 700
Cdd:COG5244 462 FL--------YPSCDITLSSILTILFSDKLEVFFQGIESLLENITIFPEQPSQQTSDSENIKENSLLSDR---LNEENIR 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 701 LEESVAEEKNKLQgdlemtqarvHELENDLACQKEVLESSVTQEKRKMREVLEAERRKAQD--------LENQLTQQKEI 772
Cdd:COG5244 531 LKEVLVQKENMLT----------EETKIKIIIGRDLERKTLEENIKTLKVELNNKNNKLKEenfnlvnrLKNMELKLYQI 600
|
570 580 590
....*....|....*....|....*....|....*...
gi 1958778178 773 SESNTYEKLKMrdTLEKEKRRIQDLENRLTKQREEIEL 810
Cdd:COG5244 601 KDNNTLNKIYL--DLVSEIMELRETIRRQIKEQKRVSI 636
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
648-760 |
4.15e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.48 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 648 QSEELRAQVNASLETQQSLQEENLAEKEKLTEKLEQEEKLKARIqqlteEKAALEESVAEEKNKLQGDLEMtQARVHELE 727
Cdd:COG2268 216 IAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAET-----ARAEAEAAYEIAEANAEREVQR-QLEIAERE 289
|
90 100 110
....*....|....*....|....*....|...
gi 1958778178 728 NDLACQKEVLESSVTQEKRKMREVLEAERRKAQ 760
Cdd:COG2268 290 REIELQEKEAEREEAELEADVRKPAEAEKQAAE 322
|
|
| PLN02829 |
PLN02829 |
Probable galacturonosyltransferase |
593-796 |
4.76e-04 |
|
Probable galacturonosyltransferase
Pssm-ID: 215443 [Multi-domain] Cd Length: 639 Bit Score: 44.45 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 593 LGLQKAVLNIL-RVSLSWLEETEQLLGDLNIELSDSDKGFSLCLIYLLEHYKKIMIQSEE-LRAQVNASLE--TQQSLQE 668
Cdd:PLN02829 49 LGGDASKLNVLpQESSSSLKEPIGIVYSDNSSKTIEPDSQDLLLDKRGEHKARVLSATDDdTHSQTDDIIKqvTQKAGQD 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 669 ENLAEKEKLTEKLEQEEKLKARIQQ--LTEEKAALEESVAEEKNKLQGDLEMTQARVHELENDLACQKEVLESSVTQEKR 746
Cdd:PLN02829 129 DSDQQEKNSQSQSASQAESLEHVQQsaQTSEKVDEKEPLLTKTDKQTDQTVMPDARVRQLRDQLIKAKVYLSLPATKANP 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958778178 747 KMREVLEAERRKAQDLENQLTQQKEISEsNTYEKLK-MRDTLEKEKrRIQD 796
Cdd:PLN02829 209 HFTRELRLRIKEVQRVLGDASKDSDLPK-NANEKLKaMEQTLAKGK-QMQD 257
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
15-86 |
5.22e-04 |
|
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar proteins; ZEP, also called protein ABA DEFICIENT 1, ABA1, protein IMPAIRED IN BABA-INDUCED STERILITY 3, protein LOW EXPRESSION OF OSMOTIC STRESS-RESPONSIVE GENES 6, or protein NON-PHOTOCHEMICAL QUENCHING 2, plays an important role in the xanthophyll cycle and abscisic acid (ABA) biosynthesis. It converts zeaxanthin into antheraxanthin and subsequently violaxanthin. ZEP is required for resistance to osmotic and drought stresses, ABA-dependent stomatal closure, seed development and dormancy, modulation of defense gene expression, and disease resistance and non-photochemical quencing (NPQ). The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438754 [Multi-domain] Cd Length: 123 Bit Score: 41.26 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 15 KKSTTIGK--HEDSD---LVLQSSDIDNHHALIEFNEaeGTFVLQDFNTRNGTFVNECHIQ------NVAVKLIPGDILR 83
Cdd:cd22702 31 KQPCIIGSdpHQAISgisVVIPSPQVSELHARITCKN--GAFFLTDLGSEHGTWINDNEGRryrappNFPVRLHPSDVIE 108
|
...
gi 1958778178 84 FGS 86
Cdd:cd22702 109 FGS 111
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
648-845 |
6.12e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 648 QSEELRAQVNASLETQQSLQEENLAEKEKLTEKLEQEEKLKARIQQLTEEKAALEESVAEEKNKLQgdleMTQARVHELE 727
Cdd:COG3883 31 ELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY----RSGGSVSYLD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 728 --------NDLACQKEVLESSVTQEKRKMREvLEAERRKAQDLENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQDLEN 799
Cdd:COG3883 107 vllgsesfSDFLDRLSALSKIADADADLLEE-LKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLA 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958778178 800 RLTKQREEIELKGQKEDILNNKLKDALLLVEDAQQMRTAESTRAEK 845
Cdd:COG3883 186 QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
281-434 |
9.10e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 43.48 E-value: 9.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 281 QDLDEGDDHRQKEIESMKSQINALQKGYSQV------LSQTLAERNTEIESLKNEGENLKRDQAITSGMV---------- 344
Cdd:pfam05667 324 ETEEELQQQREEELEELQEQLEDLESSIQELekeikkLESSIKQVEEELEELKEQNEELEKQYKVKKKTLdllpdaeeni 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 345 TSLQKDVSARNEQVQQLQEEVNQLRIQNKEKeyqLEALTSRCSKlkedlRKEEAQKerreaQEKELKLCRSQMQDMEKEV 424
Cdd:pfam05667 404 AKLQALVDASAQRLVELAGQWEKHRVPLIEE---YRALKEAKSN-----KEDESQR-----KLEEIKELREKIKEVAEEA 470
|
170
....*....|
gi 1958778178 425 KKlREELKKN 434
Cdd:pfam05667 471 KQ-KEELYKQ 479
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
15-85 |
1.39e-03 |
|
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is a telomere-associated E3 ubiquitin-protein ligase that plays an important role in DNA double-strand break (DSB) repair via histone ubiquitination. It is localized in the nucleus and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3), but not with other E2s (UbcH5, UbcH7, UbcH10, hCdc34, and hBendless). It recruits UBC13 for lysine 63-based self polyubiquitylation. Its deficiency causes neuronal pathology and cognitive decline, and its loss results in neuron degeneration. RNF8, together with RNF168, catalyzes a series of ubiquitylation events on substrates such as H2A and H2AX, with the H2AK13/15 ubiquitylation being particularly important for recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of DSBs. Specially, RNF8 mediates the ubiquitination of gammaH2AX, and recruits 53BP1 and BRCA1 to DNA damage sites which promotes DNA damage response (DDR) and inhibits chromosomal instability. Moreover, RNF8 interacts with retinoid X receptor alpha (RXR alpha) and enhances its transcription-stimulating activity. It also regulates the rate of exit from mitosis and cytokinesis. RNF8 contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438715 [Multi-domain] Cd Length: 110 Bit Score: 39.65 E-value: 1.39e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958778178 15 KKSTTIGKHEDSDLVLQSSD---IDNHHALIEFNeAEGTFVLQDFNTRNGTFVNECHIQ-NVAVKLIPGDILRFG 85
Cdd:cd22663 20 GKEVTVGRGLGVTYQLVSTCplmISRNHCVLKKN-DEGQWTIKDNKSLNGVWVNGERIEpLKPYPLNEGDLIQLG 93
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
849-1064 |
1.44e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 849 KLKETLAELEITKAKMIMAEDRLKLQQQSMKALQDERESQkhgfEEEITEYKEQIKQHSQTIVNLEERLSQVTQyyrkie 928
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRALEQELAALEAELAELEK------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 929 gEIATLKDSDSAQKEEVPQ------------EFTIVPSLDSSAKEIACDHLIDDLLMAQKEIL----SQQEIIMKLRTDL 992
Cdd:COG4942 91 -EIAELRAELEAQKEELAEllralyrlgrqpPLALLLSPEDFLDAVRRLQYLKYLAPARREQAeelrADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958778178 993 GEAHTRMSDLRGELsEKQKTELERQVALVRQQNSELSILKAKVVQTTGLVEKKDRELKVLREALRASQEKPR 1064
Cdd:COG4942 170 EAERAELEALLAEL-EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
11-85 |
1.48e-03 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 (FKH1), 2 (FKH2) and similar proteins; This family includes FKH1 and FKH2, as well as pre-rRNA-processing protein FHL1. FKH1 and FKH2 are forkhead transcription factors that regulate the expression of the CLB2 cluster of genes during the G2/M phase of the mitotic cell cycle. The CLB2 cluster of genes includes mitotic regulators such as CLB1, CLB2, CDC5 and CDC20, as well as SWI5 and ACE2. FKH1 and FKH2 are involved in HMRa silencing. They associate with the coding regions of active genes and influence, in opposing ways, transcriptional elongation and termination, and coordinate early transcription elongation and pre-mRNA processing. Both FKH1 and FKH2 play a role as regulators of lifespan in collaboration with the anaphase-promoting complex (APC), likely through combined regulation of stress response, genomic stability, and cell cycle regulation. They also function in controlling yeast cell morphology by preventing pseudohyphal growth and act as rate-limiting replication origin activators via their interaction with the origin recognition complex (ORC). FHL1 is a forkhead protein that controls the pre-rRNA processing machinery in conjunction with IFH1. It might act as a transcriptional regulator of genes specifically involved in that process. IFH1 convert FHL1 from a repressor to an activator. This family also includes AtFHA1 and AtFHA2, which may play a role in the control of plant organ development. AtFHA2 is specifically involved in the regulation of stamen development. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438753 [Multi-domain] Cd Length: 106 Bit Score: 39.53 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 11 FFVLKKSTTIGK---------HEDSDLVLQSSD-IDNHHALIEFNEAEGTFVLQDFNtRNGTFVNE--CHIQNVAVKLIP 78
Cdd:cd22701 12 YYVQKLEVVLGRnsknssstaADSVDIDLGPSKkISRRHARIFYDFTTQCFELSVLG-RNGVKVDGilVKPGSPPVPLRS 90
|
....*..
gi 1958778178 79 GDILRFG 85
Cdd:cd22701 91 GSLIQIG 97
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
257-807 |
1.53e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 42.82 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 257 SQRLSEMAAVVAAARQS-NRCDPRFQDLDEGDDHRQKEIESMKSQINALqkgysqvlsqTLAERNTEIESlknegENLKR 335
Cdd:pfam07111 58 SQALSQQAELISRQLQElRRLEEEVRLLRETSLQQKMRLEAQAMELDAL----------AVAEKAGQAEA-----EGLRA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 336 DQAITSGMVTSLQKDVSARNEQVQQLQEEvnQLRIQNKEKEYQLEALTSRCSKLKEDLRKEEAqkeRREAQEKELKLCRS 415
Cdd:pfam07111 123 ALAGAEMVRKNLEEGSQRELEEIQRLHQE--QLSSLTQAHEEALSSLTSKAEGLEKSLNSLET---KRAGEAKQLAEAQK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 416 QMQDMEKEVKKLREELK---------KNYTGQNVISKTLREKNKVEEK--------LQED-----SRRKLLQ--LQEMGN 471
Cdd:pfam07111 198 EAELLRKQLSKTQEELEaqvtlveslRKYVGEQVPPEVHSQTWELERQelldtmqhLQEDradlqATVELLQvrVQSLTH 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 472 RENLIKMNLERAVGQLENFRSQVIKATFGKTKPFRDKPV---------------TDQQLIERIVQVTEDNLSFQQRKWTL 536
Cdd:pfam07111 278 MLALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREKVFalmvqlkaqdlehrdSVKQLRGQVAELQEQVTSQSQEQAIL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 537 QRETHLHSKQEEVVH-NVEKLRVLLDKCQACMRDSCNSMDLKKEvellqHLQLsppVLGLQKAVLNILRVSLSWLEETEQ 615
Cdd:pfam07111 358 QRALQDKAAEVEVERmSAKGLQMELSRAQEARRRQQQQTASAEE-----QLKF---VVNAMSSTQIWLETTMTRVEQAVA 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 616 LLGDLNIELSdsdkgFSLCLIYLLEHYKKIMIQSEELRAQVNASLETQQSLQEENLAEKEKLTE---KLEQEEKLKARIQ 692
Cdd:pfam07111 430 RIPSLSNRLS-----YAVRKVHTIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREernRLDAELQLSAHLI 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 693 QltEEKAALEESVAEEKNKLqgdLEMTQarvhELENDLACQKEVLeSSVTQEKRKMREVLEAERRKAQDLENQLTQQKEI 772
Cdd:pfam07111 505 Q--QEVGRAREQGEAERQQL---SEVAQ----QLEQELQRAQESL-ASVGQQLEVARQGQQESTEEAASLRQELTQQQEI 574
|
570 580 590
....*....|....*....|....*....|....*
gi 1958778178 773 SESNTYEKLKMRDTLEKEKrrIQDLENRLTKQREE 807
Cdd:pfam07111 575 YGQALQEKVAEVETRLREQ--LSDTKRRLNEARRE 607
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
639-807 |
1.61e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.80 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 639 LEHYKKIMIQSEElraqvnasletQQSLQEENLAEKEKLteKLEQEEKLKARIQQLTEEKAALEESVAEEKNKLQGDLEm 718
Cdd:pfam17380 398 LEAARKVKILEEE-----------RQRKIQQQKVEMEQI--RAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVE- 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 719 tqaRVHELENDLACQKEVLEssvtQEKRKMREVlEAERRKAQDLENQLTQQKEISESNTYEKL------KMRDTLEKEKR 792
Cdd:pfam17380 464 ---RLRQQEEERKRKKLELE----KEKRDRKRA-EEQRRKILEKELEERKQAMIEEERKRKLLekemeeRQKAIYEEERR 535
|
170
....*....|....*
gi 1958778178 793 RIQDLENRLTKQREE 807
Cdd:pfam17380 536 REAEEERRKQQEMEE 550
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
250-433 |
1.64e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 250 QAEIADLSQRLSEMAAVVAAARQSNRCDPRFQDLDEGDDHRQKEIESMKSQINALQKGYSQVLSQTLAERNTEIESLKNE 329
Cdd:COG4913 267 ARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLERE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 330 GENLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEVNQLRIQNKEKEYQLEALTSRCSKLKEDLRKEEAQKERREAQ-EK 408
Cdd:COG4913 347 IERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRElEA 426
|
170 180
....*....|....*....|....*
gi 1958778178 409 ELKLCRSQMQDMEKEVKKLREELKK 433
Cdd:COG4913 427 EIASLERRKSNIPARLLALRDALAE 451
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
660-872 |
1.70e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 660 LETQQSLQEENLAEKE-KLTEKLEQEEKLKARIQQLTEEKAALEESVAEEKNKLqGDLEMTQARvheLENDLA-CQKEV- 736
Cdd:PHA02562 204 IEEQRKKNGENIARKQnKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAL-NKLNTAAAK---IKSKIEqFQKVIk 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 737 -LES-----SVTQEKRKMREVLEAERRKAQDLENQLTQQKEisesnTYEKLKMR-DTLEKEKRRIQDLENRLTKQREEIE 809
Cdd:PHA02562 280 mYEKggvcpTCTQQISEGPDRITKIKDKLKELQHSLEKLDT-----AIDELEEImDEFNEQSKKLLELKNKISTNKQSLI 354
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958778178 810 LkgqkediLNNKLKDALLLVEDAQQMRTAESTRAEKLS---LKLKETLAELEITKAKMIMAEDRLK 872
Cdd:PHA02562 355 T-------LVDKAKKVKAAIEELQAEFVDNAEELAKLQdelDKIVKTKSELVKEKYHRGIVTDLLK 413
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
249-406 |
1.78e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 249 LQAEIADLSQRLSEMAAVVAAARQSNRCDPRFQDLDEGddhrQKEIESMKSQINALQKGYSQV--LSQTLAERNTEIESL 326
Cdd:COG4717 100 LEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL----EAELAELPERLEELEERLEELreLEEELEELEAELAEL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 327 KNEGENLKRDQAITSgmvtslQKDVSARNEQVQQLQEEVNQLRIQNKEKEYQLEALTSRCSKLKEDLRKEEAQKERREAQ 406
Cdd:COG4717 176 QEELEELLEQLSLAT------EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEAR 249
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
230-383 |
1.81e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 230 NRLSDFEMESKykdavIMNLQAEIADLSQRLSEMAAVVAAAR-QSNRCDPRFQDLDE---------GDDHRQKEIESMKS 299
Cdd:COG3206 196 AALEEFRQKNG-----LVDLSEEAKLLLQQLSELESQLAEARaELAEAEARLAALRAqlgsgpdalPELLQSPVIQQLRA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 300 QINALQKGYSQvLSQTLAERNTEIESLKNEGENLKRD-QAITSGMVTSLQKDVSARNEQVQQLQEEVNQLRIQNK---EK 375
Cdd:COG3206 271 QLAELEAELAE-LSARYTPNHPDVIALRAQIAALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAelpEL 349
|
....*...
gi 1958778178 376 EYQLEALT 383
Cdd:COG3206 350 EAELRRLE 357
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
345-432 |
2.32e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 345 TSLQKDVSARNEQVQQLQEEVNQLRIQNKEKEyqLEALTSRCSKLKEDLRkeeAQKERREAQEKELKLCRSQMQDMEKEV 424
Cdd:PRK04863 1023 ASLKSSYDAKRQMLQELKQELQDLGVPADSGA--EERARARRDELHARLS---ANRSRRNQLEKQLTFCEAEMDNLTKKL 1097
|
....*...
gi 1958778178 425 KKLREELK 432
Cdd:PRK04863 1098 RKLERDYH 1105
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
654-1162 |
2.39e-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: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 654 AQVNASLETQQSLQEENLAEKEKLTEKLEQE--EKLKARIQQLTEEKAALEESVAEEKNKLQGDlemtqarvhELENDLA 731
Cdd:pfam12128 393 AGIKDKLAKIREARDRQLAVAEDDLQALESElrEQLEAGKLEFNEEEYRLKSRLGELKLRLNQA---------TATPELL 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 732 CQKEVLESSVtqekRKMREVLEAERRKAQDLENQLTQQKEISEsntyeklKMRDTLEKEKRRIQDLENRLTKQREEIELK 811
Cdd:pfam12128 464 LQLENFDERI----ERAREEQEAANAEVERLQSELRQARKRRD-------QASEALRQASRRLEERQSALDELELQLFPQ 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 812 -GQKEDILNNKLKD-----------ALLLVEDAQQMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDRLKLQQQSmK 879
Cdd:pfam12128 533 aGTLLHFLRKEAPDweqsigkvispELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAE-E 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 880 ALQDERESQKHGFEE------EITEYKEQIKQHSQTIVNLEERLSQVTqyyrkieGEIATLKDS-DSAQKEEVPQEFTIV 952
Cdd:pfam12128 612 ALQSAREKQAAAEEQlvqangELEKASREETFARTALKNARLDLRRLF-------DEKQSEKDKkNKALAERKDSANERL 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 953 PSLDSSAKEiacdhliddLLMAQKEILSQQeiimklRTDLGEAHTRMSDLRGELSEKQKTELERqvaLVRQQNSELSILK 1032
Cdd:pfam12128 685 NSLEAQLKQ---------LDKKHQAWLEEQ------KEQKREARTEKQAYWQVVEGALDAQLAL---LKAAIAARRSGAK 746
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 1033 AkvvQTTGLVEKKDRELKVLrealrasQEKPRPYLSTEQKPRNLSQKCDislQIEPAHPD--SFSSFQEEQFFSD---LG 1107
Cdd:pfam12128 747 A---ELKALETWYKRDLASL-------GVDPDVIAKLKREIRTLERKIE---RIAVRRQEvlRYFDWYQETWLQRrprLA 813
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958778178 1108 AKCKGSRHE--EVIQRQKKALSELRTRIKELEKANSSNHK--DHVNESFLELKtLRMEK 1162
Cdd:pfam12128 814 TQLSNIERAisELQQQLARLIADTKLRRAKLEMERKASEKqqVRLSENLRGLR-CEMSK 871
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
264-486 |
2.39e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 264 AAVVAAARQSNR--CDpRFQ-----DL-DEGDDHRQKEIESMKSQINALQKgysqvlsqtlaerntEIESLKNEGENLKR 335
Cdd:COG0542 369 EALVAAVRLSDRyiTD-RFLpdkaiDLiDEAAARVRMEIDSKPEELDELER---------------RLEQLEIEKEALKK 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 336 DQAITSGmvtslqkdvsarnEQVQQLQEEVNQLRIQnkekeyqLEALTSRCSKLKEDLRKEEAQKERREAQEKELKLCRS 415
Cdd:COG0542 433 EQDEASF-------------ERLAELRDELAELEEE-------LEALKARWEAEKELIEEIQELKEELEQRYGKIPELEK 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 416 QMQDMEKEVKKLREELKKNYTGQN---VISK------TlreknkveeKLQEDSRRKLLQLqemgnrENLIKmnlERAVGQ 486
Cdd:COG0542 493 ELAELEEELAELAPLLREEVTEEDiaeVVSRwtgipvG---------KLLEGEREKLLNL------EEELH---ERVIGQ 554
|
|
| FHA_PML1-like |
cd22681 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ... |
5-95 |
2.57e-03 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 (PML1) and similar proteins; PML1 is an FHA domain-containing protein required for efficient splicing and pre-mRNA nuclear retention. It is a component of the pre-mRNA retention and splicing (RES) complex composed of at least BUD13, IST3, and PML1. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438733 [Multi-domain] Cd Length: 129 Bit Score: 39.34 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 5 LKSPDGFFVLKKSTTIGKHEDSDLVLQSSDIDNHHALIEFNEAEGTFV--LQDFNTRNGTFVNECHI-QNVAVKLIPGDI 81
Cdd:cd22681 36 LNSPSCYLIGREKGESTEIVVADIGIPEETCSKQHCVIQFRNVKGILKpyIMDLDSSNGTCLNDNVIpSSRYVELRSGDV 115
|
90
....*....|....
gi 1958778178 82 LRFgSSGPTYELVI 95
Cdd:cd22681 116 ITF-SKSNDYELVF 128
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
215-465 |
2.64e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.20 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 215 QQDKDDIILLLGREINRLSDFEMESKYKDAvimnLQAEIADLSQRLSEMAAVVAAARQSNrcdprfQDLDEGDDHRQKEI 294
Cdd:PLN02939 138 QNAEKNILLLNQARLQALEDLEKILTEKEA----LQGKINILEMRLSETDARIKLAAQEK------IHVEILEEQLEKLR 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 295 ESMKSQInALQKGYSQVLSQTLAERNTEIESLKNEGENLKR---DQAITSGMVTSLQKDVSARNEQVQQL-------QEE 364
Cdd:PLN02939 208 NELLIRG-ATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAeliEVAETEERVFKLEKERSLLDASLRELeskfivaQED 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 365 VNQLRIQNK----EKEYQLEALTSRCSKLKE----------DLRKEEAQKERREAQEKELKLCRSQMQDMEKEVKKLREE 430
Cdd:PLN02939 287 VSKLSPLQYdcwwEKVENLQDLLDRATNQVEkaalvldqnqDLRDKVDKLEASLKEANVSKFSSYKVELLQQKLKLLEER 366
|
250 260 270
....*....|....*....|....*....|....*....
gi 1958778178 431 LKKN----YTGQNVISKTLREKNKVEEKLQEDSRRKLLQ 465
Cdd:PLN02939 367 LQASdheiHSYIQLYQESIKEFQDTLSKLKEESKKRSLE 405
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
610-902 |
2.69e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 41.59 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 610 LEETEQLLGDLNIELSDSDKGFSLCLIYLLEHYKKImiqsEELRAQVNASLETQQSLQEEN------LAEKEKLTEKLEQ 683
Cdd:pfam19220 85 LEELVARLAKLEAALREAEAAKEELRIELRDKTAQA----EALERQLAAETEQNRALEEENkalreeAQAAEKALQRAEG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 684 E-----------EKLKARIQQLTEEKAALEESVAEEKNKLQGDLEMTQARVHELENDLACQKEVLESSVTQ--------- 743
Cdd:pfam19220 161 ElatarerlallEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQleeaveahr 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 744 -EKRKMREVLEAERRKAQDLENQLTQQKE----------ISESNTYEKLKMRDTLEkekRRIQDLENRLTKQREEielkg 812
Cdd:pfam19220 241 aERASLRMKLEALTARAAATEQLLAEARNqlrdrdeairAAERRLKEASIERDTLE---RRLAGLEADLERRTQQ----- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 813 qkedilnnklkdalllVEDAQQMRTAESTRAEKLSLKLKETLAELEitkakmiMAEDRLKLQQQSMKALQDERESQKHGF 892
Cdd:pfam19220 313 ----------------FQEMQRARAELEERAEMLTKALAAKDAALE-------RAEERIASLSDRIAELTKRFEVERAAL 369
|
330
....*....|
gi 1958778178 893 EEEITEYKEQ 902
Cdd:pfam19220 370 EQANRRLKEE 379
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
666-937 |
2.73e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 666 LQEENLAEKEKLTEKLEQEEKLKARIQQLTEEKAALEEsvAEEKNKLQGDLEMTQARVHELENDLAcqkEVLESSvtQEK 745
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQR--LAEYSWDEIDVASAEREIAELEAELE---RLDASS--DDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 746 RKMREVLEAERRKAQDLENQLTQQKEIsesntyeklkmRDTLEKEKRRIQDLENRLTKQREEIELKGQKEDI--LNNKLK 823
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGE-----------IGRLEKELEQAEEELDELQDRLEAAEDLARLELRalLEERFA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 824 DALL------LVEDAQQMRTAESTRAEKLSLKLKETLAELeitKAKMIMAEDRLKLQQQSMKALQDERESQKhgfEEEIT 897
Cdd:COG4913 757 AALGdavereLRENLEERIDALRARLNRAEEELERAMRAF---NREWPAETADLDADLESLPEYLALLDRLE---EDGLP 830
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958778178 898 EYKEQIKQ--HSQTIVNLEERLSQVTQYYRKIEGEIATLKDS 937
Cdd:COG4913 831 EYEERFKEllNENSIEFVADLLSKLRRAIREIKERIDPLNDS 872
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
743-910 |
3.17e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 743 QEKRKMREVLEAERRKAQDLENQLTQQKEisesntyeklKMRDTLEKEKRRIQDLENRLTKQREEIE-LKGQKEDILNNK 821
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLE----------AAKTELEDLEKEIKRLELEIEEVEARIKkYEEQLGNVRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 822 LKDALLLVEDAQQMRTAEstrAEKLSLKLKETLAELEITKAKmimAEDRLKLQQQSMKALQDERESQKHGFEEEITEYKE 901
Cdd:COG1579 90 EYEALQKEIESLKRRISD---LEDEILELMERIEELEEELAE---LEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
....*....
gi 1958778178 902 QIKQHSQTI 910
Cdd:COG1579 164 EREELAAKI 172
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
797-994 |
3.20e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 797 LENRLTKQREEIELKGQKEDILNNKLKDALllvedAQQMRTAESTRAE--KLSLKLKETLAELEITKAKMIMAEDRLKLQ 874
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKEL-----EEELKEAEEKEEEyaELQEELEELEEELEELEAELEELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 875 QQSMKALQDERESQKHGFE-EEITEYKEQIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKDSDSAQKEEvpqeftivp 953
Cdd:COG4717 122 EKLLQLLPLYQELEALEAElAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE--------- 192
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958778178 954 SLDSSAKEIacDHLIDDLLMAQKEILSQQEIIMKLRTDLGE 994
Cdd:COG4717 193 ELQDLAEEL--EELQQRLAELEEELEEAQEELEELEEELEQ 231
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
664-807 |
3.49e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 664 QSLQEEnLAEKEKLTEKLEQE----EKLKARIQQLTEEKAALEEsvaeEKNKLQGDLEMTQARVHELENDLACQKEVLES 739
Cdd:COG4913 664 ASAERE-IAELEAELERLDASsddlAALEEQLEELEAELEELEE----ELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958778178 740 SVTQEKRKMREVLEAERRKAQDLENQLTQQKEISESntyeklkmrdtLEKEKRRIQDLENRLTKQREE 807
Cdd:COG4913 739 AEDLARLELRALLEERFAAALGDAVERELRENLEER-----------IDALRARLNRAEEELERAMRA 795
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
745-1137 |
3.68e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.64 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 745 KRKMREVLEAERRKAQDLENQLTQQKEISESNTY------------------EKLKMRDTLEKEKRRIQDLENRLTKQRE 806
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFylrqsvidlqtklqemqmERDAMADIRRRESQSQEDLRNQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 807 EIE-LKGQKEDILNnklkDALLLVEDAQQMRTAEstraEKLSLKLKETLAELEITKAKMIMAEDrlklqqqSMKALQdeR 885
Cdd:pfam15921 153 ELEaAKCLKEDMLE----DSNTQIEQLRKMMLSH----EGVLQEIRSILVDFEEASGKKIYEHD-------SMSTMH--F 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 886 ESQKHGFEEEITEYKEQIKQHSQTIVNLEERLSQV-TQYYRKIEGEIATLKDSDSAQKEEVPQEFTIVPSLDSSAKEIAc 964
Cdd:pfam15921 216 RSLGSAISKILRELDTEISYLKGRIFPVEDQLEALkSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQA- 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 965 DHLIDDLLMAQKEILSQQEIIMKLRTDLgeaHTRMSDLRGELSEKQKT------ELERQVALVRQQNSELSILKAKVVQT 1038
Cdd:pfam15921 295 NSIQSQLEIIQEQARNQNSMYMRQLSDL---ESTVSQLRSELREAKRMyedkieELEKQLVLANSELTEARTERDQFSQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 1039 TGLVEkkDRELKVLREALRASQEKPrpyLSTEQKPRNLSQKCDISLQIEPAHPDSFSSFQE----EQFFSDLGAKCKGS- 1113
Cdd:pfam15921 372 SGNLD--DQLQKLLADLHKREKELS---LEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEvqrlEALLKAMKSECQGQm 446
|
410 420
....*....|....*....|....*
gi 1958778178 1114 -RHEEVIQRQKKALSELRTRIKELE 1137
Cdd:pfam15921 447 eRQMAAIQGKNESLEKVSSLTAQLE 471
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
650-1141 |
3.86e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 650 EELRAQVNASLETQQSLQEENLAEKEKLTEKLEQEEKLKARIQQLTEEKAALEESVAEeknkLQGDLEMTQARVHELEND 729
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEE----LEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 730 LACQkevlesSVTQEKRKMREVLEAERRKAQDLENQLTQQKEisesntyeklkMRDTLEKEKRRIQDLENRLTKQREEIE 809
Cdd:COG4717 125 LQLL------PLYQELEALEAELAELPERLEELEERLEELRE-----------LEEELEELEAELAELQEELEELLEQLS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 810 LKGQKEdilnnkLKDALLLVEDAQQMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDRLKLQQQSMKALQderESQK 889
Cdd:COG4717 188 LATEEE------LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLI---AAAL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 890 HGFeeeiteykeqikqhSQTIVNLEERLSQVTQYYRKIEGEIATLKDSDSAQKEEVPQEFtivpsldssaKEIACDHLID 969
Cdd:COG4717 259 LAL--------------LGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA----------EELQALPALE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 970 DLLMAQ-KEILSQQEIIMKL-RTDLGEAHTRMSDLRGELSEKQKTELERQVALVRQQNSELsILKAKVVQTTGLVEK--K 1045
Cdd:COG4717 315 ELEEEElEELLAALGLPPDLsPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL-LAEAGVEDEEELRAAleQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 1046 DRELKVLREALRASQEKPRPYLSTEQKPRNLSQKCDISLQIEpahpdsfsSFQEEQffsdlgakckgSRHEEVIQRQKKA 1125
Cdd:COG4717 394 AEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELE--------ELEEEL-----------EELEEELEELREE 454
|
490
....*....|....*.
gi 1958778178 1126 LSELRTRIKELEKANS 1141
Cdd:COG4717 455 LAELEAELEQLEEDGE 470
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
746-936 |
3.96e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 746 RKMREVLEAERRKAQDL----ENQLTQQKEISESNTYEKLKMRDTLEKEKRRIQDLENRLTKQREEIELKGQKEDILNNK 821
Cdd:COG4913 238 ERAHEALEDAREQIELLepirELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 822 LKDALLLVEDAQQMRTAESTRAEKlslKLKETLAELEITKAKmimAEDRLKLQQQSMKALQDERESQKHGFEEEITEYKE 901
Cdd:COG4913 318 LDALREELDELEAQIRGNGGDRLE---QLEREIERLERELEE---RERRRARLEALLAALGLPLPASAEEFAALRAEAAA 391
|
170 180 190
....*....|....*....|....*....|....*
gi 1958778178 902 QIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKD 936
Cdd:COG4913 392 LLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
298-497 |
4.46e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 298 KSQINALQKGYSQvLSQTLAERNTEIESLKNEGENL--KRDQAITSGMVTSLQKDVSARNEQVQQLQEevnqlriqnkek 375
Cdd:COG4913 609 RAKLAALEAELAE-LEEELAEAEERLEALEAELDALqeRREALQRLAEYSWDEIDVASAEREIAELEA------------ 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 376 eyQLEALTSRCSKLKEDLRKEEAQKERREAQEKELKLCRSQMQDMEKEVKKLREELKKNYTGQNVISKTLRE------KN 449
Cdd:COG4913 676 --ELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLelrallEE 753
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958778178 450 KVEEKLQEDSRRKLlqlqemgnRENLIKmNLERAVGQLENFRSQVIKA 497
Cdd:COG4913 754 RFAAALGDAVEREL--------RENLEE-RIDALRARLNRAEEELERA 792
|
|
| FHA_RAD53-like_rpt1 |
cd22689 |
first forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ... |
13-93 |
4.83e-03 |
|
first forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine/threonine-protein kinase RAD53 and similar proteins; RAD53, also called CHEK2 homolog, or serine-protein kinase 1 (Spk1), is a nuclear protein kinase that phosphorylates proteins on serine, threonine, and tyrosine. It controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints and prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. It may be involved in the phosphorylation of RPH1. RAD53 contains two FHA domains. This model corresponds to the first one. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438741 [Multi-domain] Cd Length: 132 Bit Score: 38.41 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 13 VLKKSTTIGKHEDSDLVLQSSDIDNHHALI---EFNEAEGTFVLQDFNTrNGTFVNEchiQNVAVK----LIPGDILRFG 85
Cdd:cd22689 42 SIKKVWTFGRHPACDYHLGNSRLSNKHFQIllgESDPSDGNVLLNDISS-NGTWLNG---QRLEKNsnqlLSQGDEITIG 117
|
....*...
gi 1958778178 86 SSGPTYEL 93
Cdd:cd22689 118 VGVTGDIL 125
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
346-433 |
4.88e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 346 SLQKDVSARNEQVQQLQEEVNQLRIQNKEKEYQLEALTSRCSKLKEDLRKEEAQkerREAQEKELKLCRSQMQDMEKEVK 425
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE---LAALEAELAELEKEIAELRAELE 100
|
....*...
gi 1958778178 426 KLREELKK 433
Cdd:COG4942 101 AQKEELAE 108
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
351-446 |
4.92e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 351 VSARNEQVQQLQEEVNQLRIQNKEKEYQLEALTSRCSKLKEDLRKEEAQKERREAQ----EKELKLCRSQMQDMEKEVKK 426
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiralEQELAALEAELAELEKEIAE 94
|
90 100
....*....|....*....|
gi 1958778178 427 LREELKKNytgQNVISKTLR 446
Cdd:COG4942 95 LRAELEAQ---KEELAELLR 111
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
648-781 |
4.97e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 40.67 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 648 QSEELRAQVNASLETQQSLQEEnlaekekLTEKLEQEEKLKARIQQLTEEKAALEESVAEEKNKLQGDLEMTQARVHELE 727
Cdd:pfam00038 197 KLEELQQAAARNGDALRSAKEE-------ITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELE 269
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1958778178 728 NDLacqkevlessvtqekRKMREVLEAERRKAQDLEN-QLTQQKEIsesNTYEKL 781
Cdd:pfam00038 270 AEL---------------QETRQEMARQLREYQELLNvKLALDIEI---ATYRKL 306
|
|
| ZapB |
pfam06005 |
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ... |
650-705 |
5.01e-03 |
|
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.
Pssm-ID: 428718 [Multi-domain] Cd Length: 71 Bit Score: 36.86 E-value: 5.01e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958778178 650 EELRAQVNASLETQQSLQEENLAEKEKLTEKLEQEEKLKARIQQLTEEKAALEESV 705
Cdd:pfam06005 7 EQLETKIQAAVDTIALLQMENEELKEENEELKEEANELEEENQQLKQERNQWQERI 62
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
639-1062 |
5.25e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 639 LEHYKKIMIQSEELRAQVNASLETQQSLQEE------------NLAEKEKLTEKLEQE----EKLKARIQQLTE---EKA 699
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREEleklekllqllpLYQELEALEAELAELperlEELEERLEELREleeELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 700 ALEESVAEEKNKLQGDLEMTQARVHELENDLACQKEVLEssvtQEKRKMREVLEAERRKAQDLENQLtqqkeisesntyE 779
Cdd:COG4717 167 ELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ----QRLAELEEELEEAQEELEELEEEL------------E 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 780 KLKMRDTLEKEKRRIQDLENRLTKQREEIELKGQKEDILNNKLKDA--------LLLVEDAQQMRTAESTRAEKLSLKLK 851
Cdd:COG4717 231 QLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAgvlflvlgLLALLFLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 852 ETLAELEITKAKMIMAEDRLKL------------QQQSMKALQDERESQKHgfEEEITEYKEQIKQ--HSQTIVNLEERL 917
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPdlspeellelldRIEELQELLREAEELEE--ELQLEELEQEIAAllAEAGVEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 918 SQVTQY--YRKIEGEIATLKDsdsaqkeevpqeftivpSLDSSAKEIACDHLIDDLLMAQKEILSQQEIIMKLRTDLGEA 995
Cdd:COG4717 389 AALEQAeeYQELKEELEELEE-----------------QLEELLGELEELLEALDEEELEEELEELEEELEELEEELEEL 451
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958778178 996 HTRMSDLRGELSekqktELERQVALVRQQnSELSILKAKVVQttglVEKKDRELKVLREALRASQEK 1062
Cdd:COG4717 452 REELAELEAELE-----QLEEDGELAELL-QELEELKAELRE----LAEEWAALKLALELLEEAREE 508
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
643-905 |
5.53e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 40.60 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 643 KKIMIQSEELRAQVNASLETQQSLQEENLAEKEKLTEKLEQEEklkARIQQLTEEKAALEESVAEEKNKLQGDLEmtqar 722
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQ---ARQKELEQRAAAEKAAKQAEQAAKQAEEK----- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 723 vhelendlacQKEVLESSVTQEK-RKMREVLEAERRKAQDLENQLTQQKeisesntyeKLKMRDTLEKEKRRIQDLENRL 801
Cdd:TIGR02794 118 ----------QKQAEEAKAKQAAeAKAKAEAEAERKAKEEAAKQAEEEA---------KAKAAAEAKKKAEEAKKKAEAE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 802 TKQREEIELKGQKEdilnnklkDALLLVEDAQQMRTAEST-RAEKLSLKLKETLAEleiTKAKMIMAEDRLKLQQQSMKA 880
Cdd:TIGR02794 179 AKAKAEAEAKAKAE--------EAKAKAEAAKAKAAAEAAaKAEAEAAAAAAAEAE---RKADEAELGDIFGLASGSNAE 247
|
250 260
....*....|....*....|....*
gi 1958778178 881 LQDERESQKHGfeEEITEYKEQIKQ 905
Cdd:TIGR02794 248 KQGGARGAAAG--SEVDKYAAIIQQ 270
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
650-755 |
6.19e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 650 EELRAQVNAsLETqqslqEENLAEKEKLTEKLEQEEKLKARIQQLTEEKAALEESVAEEKNKLQGDLEMTQARVHELEND 729
Cdd:COG0542 414 DELERRLEQ-LEI-----EKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKI 487
|
90 100
....*....|....*....|....*...
gi 1958778178 730 LACQKEV--LESSVTQEKRKMREVLEAE 755
Cdd:COG0542 488 PELEKELaeLEEELAELAPLLREEVTEE 515
|
|
| CCDC-167 |
pfam15188 |
Coiled-coil domain-containing protein 167; The function of this family of coiled-coil domains, ... |
379-434 |
6.85e-03 |
|
Coiled-coil domain-containing protein 167; The function of this family of coiled-coil domains, has not, as yet, been determined. Members of this family remain uncharacterized. This family of proteins is found in eukaryotes. Proteins in this family are typically between and 103 amino acids in length.
Pssm-ID: 464553 [Multi-domain] Cd Length: 82 Bit Score: 36.87 E-value: 6.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 379 LEALTSRCSKLKED----LRKEEAQKERREAQEKELKLCRSQMQDMEKEVKKLREELKKN 434
Cdd:pfam15188 8 LEEKIASCRDRLERiekkLRREELSEEDRRSLEKELLLLKKRLEKNEEELKLLRKENRKN 67
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
668-902 |
6.91e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.58 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 668 EENLAEKEKLTEKLEQEEKLKARiqQLTEEKAAL--EESVAEEK-NKLQGDLEMTQARVHELEN---------------- 728
Cdd:pfam10174 442 EEALSEKERIIERLKEQREREDR--ERLEELESLkkENKDLKEKvSALQPELTEKESSLIDLKEhasslassglkkdskl 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 729 ---DLACQKEVLESSVTQEK-RKMREVLEAERRKA------QDLENQLTQQKEISESNTYEKLKMRDTL---EKEK---- 791
Cdd:pfam10174 520 kslEIAVEQKKEECSKLENQlKKAHNAEEAVRTNPeindriRLLEQEVARYKEESGKAQAEVERLLGILrevENEKndkd 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 792 RRIQDLENRLTKQREEIELKG-QKEDILNNKLKDALLLVEDAqqMRTAESTRAEKLSLKLKETLAELEITKAKMIMAEDR 870
Cdd:pfam10174 600 KKIAELESLTLRQMKEQNKKVaNIKHGQQEMKKKGAQLLEEA--RRREDNLADNSQQLQLEELMGALEKTRQELDATKAR 677
|
250 260 270
....*....|....*....|....*....|....*....
gi 1958778178 871 LKLQQQS-------MKALQDERESQKhgfeEEITEYKEQ 902
Cdd:pfam10174 678 LSSTQQSlaekdghLTNLRAERRKQL----EEILEMKQE 712
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
264-419 |
7.09e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.71 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 264 AAVVAAARQSNRCDPRFQDLDEGDDHRQKEIESMKSQINALQKGYSQV---LSQTLAERnteIESLKNEGENLKRDQAIT 340
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQAnllADETLADR---LEELREELDAAQEAQAFI 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 341 S----------GMVTSLQKDvsarNEQVQQLQEEVNQLRIQNKEKEYQLEALT------------------SRCSKLKED 392
Cdd:COG3096 913 QqhgkalaqlePLVAVLQSD----PEQFEQLQADYLQAKEQQRRLKQQIFALSevvqrrphfsyedavgllGENSDLNEK 988
|
170 180
....*....|....*....|....*....
gi 1958778178 393 LRK--EEAQKERREAQEKeLKLCRSQMQD 419
Cdd:COG3096 989 LRArlEQAEEARREAREQ-LRQAQAQYSQ 1016
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
310-457 |
7.26e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 310 QVLSQTLAERNTEIESLKNEGENLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEVNQLRIQNKEKEYQL---------E 380
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnnkeyE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 381 ALTSRCSKLKEDLRKEEAQ----KERREAQEKELKLCRSQMQDMEKEVKKLREELKKnytgqnVISKTLREKNKVEEKLQ 456
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEilelMERIEELEEELAELEAELAELEAELEEKKAELDE------ELAELEAELEELEAERE 166
|
.
gi 1958778178 457 E 457
Cdd:COG1579 167 E 167
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
291-401 |
7.32e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 291 QKEIESMKSQINALQKgYSQVLSQTLAERNTEIESLKNEGENLKRdqaitsgmvtSLQKDVSARNEqVQQLQEEVNQLRI 370
Cdd:COG2433 412 EEEIRRLEEQVERLEA-EVEELEAELEEKDERIERLERELSEARS----------EERREIRKDRE-ISRLDREIERLER 479
|
90 100 110
....*....|....*....|....*....|.
gi 1958778178 371 QNKEKEYQLEALTSRCSKLKEdLRKEEAQKE 401
Cdd:COG2433 480 ELEEERERIEELKRKLERLKE-LWKLEHSGE 509
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
289-695 |
7.36e-03 |
|
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: 40.48 E-value: 7.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 289 HRQKEIESMKSQInalqKGYSQVLSQTLAERNTEIESLKNEGENLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEVNQL 368
Cdd:pfam05483 422 DEKKQFEKIAEEL----KGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKL 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 369 RIQNKEKEYQLEALTSRCSKLKEDLRKEEAQKERREAQEKELKLCRSQMQDmekEVKKLREELKKNytGQNVISKTlrek 448
Cdd:pfam05483 498 LLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRD---ELESVREEFIQK--GDEVKCKL---- 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 449 NKVEEKLQEDSRRKLLQLQEMGNRENLIKmNLERavgQLENfRSQVIKATFGKTKPFRDKPVTD-QQLIERIVQVTEDNL 527
Cdd:pfam05483 569 DKSEENARSIEYEVLKKEKQMKILENKCN-NLKK---QIEN-KNKNIEELHQENKALKKKGSAEnKQLNAYEIKVNKLEL 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 528 SFQQRKWTLQRETHLHSK--------QEEVVHNVEKLRVLLDKcqacmrdscnSMDLKKEVELLQHLQLSPPVLglqkav 599
Cdd:pfam05483 644 ELASAKQKFEEIIDNYQKeiedkkisEEKLLEEVEKAKAIADE----------AVKLQKEIDKRCQHKIAEMVA------ 707
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 600 lnilrvslswLEETEQLLGDLNIELSDSDKGFslcliyllehYKkimiQSEELRAQVNASLETQQS-LQEENLAEKEKLT 678
Cdd:pfam05483 708 ----------LMEKHKHQYDKIIEERDSELGL----------YK----NKEQEQSSAKAALEIELSnIKAELLSLKKQLE 763
|
410
....*....|....*..
gi 1958778178 679 EKLEQEEKLKARIQQLT 695
Cdd:pfam05483 764 IEKEEKEKLKMEAKENT 780
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
868-1061 |
7.97e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 7.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 868 EDRLKLQQQSMKALQDERES--QKHGfeeeITEYKEQIKQHSQTIVNLEERLSQVTQYYRKIEGEIATLKDSDSAQKEEV 945
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEfrQKNG----LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDAL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 946 PqeftivpsldssakEIACDHLIDDLLMAQKEILSQqeiIMKLRTDLGEAHTRMSDLRGELSE----------KQKTELE 1015
Cdd:COG3206 257 P--------------ELLQSPVIQQLRAQLAELEAE---LAELSARYTPNHPDVIALRAQIAAlraqlqqeaqRILASLE 319
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958778178 1016 RQVALVRQQNSELSILKAKVVQTTGLVEKKDRELKVLREALRASQE 1061
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARE 365
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
288-858 |
8.17e-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: 40.54 E-value: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 288 DHRQKEIESmksQINALQKGYSQVLSQTlAERNTEIESLKNEGENLKRDQAITSGMVTSLQKDVSARNEQVQQLQEEVNQ 367
Cdd:pfam01576 404 EHKRKKLEG---QLQELQARLSESERQR-AELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 368 LRIQNKEKEYQLEALTSRCSKLKEDLRKEEaqkERREAQEKELKLCRSQMQDMEKEVK------KLREELKKNYTgQNVI 441
Cdd:pfam01576 480 ETRQKLNLSTRLRQLEDERNSLQEQLEEEE---EAKRNVERQLSTLQAQLSDMKKKLEedagtlEALEEGKKRLQ-RELE 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 442 SKTLREKNKVEEKLQEDSRRKLLQ------LQEMGNRENLIKmNLERAVGQLENFRSQViKATFGKTKPFRDKPVTDQQL 515
Cdd:pfam01576 556 ALTQQLEEKAAAYDKLEKTKNRLQqelddlLVDLDHQRQLVS-NLEKKQKKFDQMLAEE-KAISARYAEERDRAEAEARE 633
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 516 IERIV----------QVTEDNLSFQQRKWTLQRETHLHSKQE--EVVHNVEKLRVLLDKCQACMRDSCNSMDLKKEVELL 583
Cdd:pfam01576 634 KETRAlslaraleeaLEAKEELERTNKQLRAEMEDLVSSKDDvgKNVHELERSKRALEQQVEEMKTQLEELEDELQATED 713
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 584 QHLQLSPPVLGLQKAVLNILRVSLSWLEETEQLLG----DLNIELSDSDKGFSLcliyLLEHYKKIMIQSEELRAQVNAS 659
Cdd:pfam01576 714 AKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVkqvrELEAELEDERKQRAQ----AVAAKKKLELDLKELEAQIDAA 789
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 660 ------------------LETQQSLQEENLAEKEKLTEKLEQEEKLK---ARIQQLTEEKAALE----------ESVAEE 708
Cdd:pfam01576 790 nkgreeavkqlkklqaqmKDLQRELEEARASRDEILAQSKESEKKLKnleAELLQLQEDLAASErarrqaqqerDELADE 869
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 709 -------KNKLQGDLEMTQARVHELENDLACQKEVLESS------VTQEKRKMREVLEAERRKAQDLEN---QLTQQKE- 771
Cdd:pfam01576 870 iasgasgKSALQDEKRRLEARIAQLEEELEEEQSNTELLndrlrkSTLQVEQLTTELAAERSTSQKSESarqQLERQNKe 949
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 772 ----ISESNTYEKLKMRDTLEKEKRRIQDLENRLTKQREEIELKGQKEDILNNKLKDALLLVEDAQQMRTAESTRAEKLS 847
Cdd:pfam01576 950 lkakLQEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGN 1029
|
650
....*....|.
gi 1958778178 848 LKLKETLAELE 858
Cdd:pfam01576 1030 SRMKQLKRQLE 1040
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
290-408 |
8.34e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.95 E-value: 8.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 290 RQKEIESMKSQIN------ALQKGYSQVLSQTLAERNTEIESLKNEGENLKRDQAITSGMVTSLQKDV----SARNEQVQ 359
Cdd:PRK09039 51 KDSALDRLNSQIAeladllSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAgelaQELDSEKQ 130
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1958778178 360 QLQEEVNQLRIQNKekeyQLEALTSRCSKLKEDLrkEEAQKERREAQEK 408
Cdd:PRK09039 131 VSARALAQVELLNQ----QIAALRRQLAALEAAL--DASEKRDRESQAK 173
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
238-457 |
8.71e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 40.13 E-value: 8.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 238 ESKYKDAVIMNLQAEIADLSQRLSEMAAVVAAARQSNRCDPRFQDLDEgdDHRQKEIESMKSQINALQkgysQVLSQTLA 317
Cdd:pfam09731 206 EEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVA--SERIVFQQELVSIFPDII----PVLKEDNL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 318 ERNTEIESLknegenlkrdqaitsgmVTSLQKDVSARNEQVQQLQEEVnQLRIQN--KEKEYQLEALTSRCSKLKEDLRK 395
Cdd:pfam09731 280 LSNDDLNSL-----------------IAHAHREIDQLSKKLAELKKRE-EKHIERalEKQKEELDKLAEELSARLEEVRA 341
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958778178 396 EEAQKERREAQEKELKLCRSQMQDMEKEVKKLRE---------------ELKKNYTgQNVISKTLREKNKVEEKLQE 457
Cdd:pfam09731 342 ADEAQLRLEFEREREEIRESYEEKLRTELERQAEaheehlkdvlveqeiELQREFL-QDIKEKVEEERAGRLLKLNE 417
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
649-877 |
9.37e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.28 E-value: 9.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 649 SEELRAQVNA---SLETQQSLQEENLAEKEKLTEKLE-QEEKLKARIQQLTEEKAALEESVAEEKnklqgdLEMTQARVH 724
Cdd:PRK11281 190 RPSQRVLLQAeqaLLNAQNDLQRKSLEGNTQLQDLLQkQRDYLTARIQRLEHQLQLLQEAINSKR------LTLSEKTVQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 725 ELENDLACQKEVLESSVTQEkrkmrevLEAERR------KAQDLENQLTQQ----KEI------SESNTYEKLK-MRDTL 787
Cdd:PRK11281 264 EAQSQDEAARIQANPLVAQE-------LEINLQlsqrllKATEKLNTLTQQnlrvKNWldrltqSERNIKEQISvLKGSL 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958778178 788 --------EKEK----RRIQDLENR----------LTKQREEIE---------LKGQKEDIlNNKLKDALLLVEDaqqmr 836
Cdd:PRK11281 337 llsrilyqQQQAlpsaDLIEGLADRiadlrleqfeINQQRDALFqpdayidklEAGHKSEV-TDEVRDALLQLLD----- 410
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1958778178 837 taesTRAEKLSLKLKE-----TLA-ELEITKAKMIMAEDRL--KLQQQS 877
Cdd:PRK11281 411 ----ERRELLDQLNKQlnnqlNLAiNLQLNQQQLLSVSDSLqsTLTQQI 455
|
|
| |
