|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
2-97 |
5.19e-51 |
|
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: 174.75 E-value: 5.19e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 2 KAYLKSAEGFFVLN-KSTTIGRHeNSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQNVAVKLIPGD 80
Cdd:cd22700 1 KGYLKSSDGIFQLDpKVTTIGRE-GCDLVLQSPGVEEQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAPGD 79
|
90
....*....|....*..
gi 767902113 81 ILRFGSAGLTYELVIEN 97
Cdd:cd22700 80 VLRFGFGGLPYELVVDN 96
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
18-84 |
1.58e-18 |
|
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 81.08 E-value: 1.58e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767902113 18 TTIGRHENSDLVLQSPDIDNHHALIEYNEaECSFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRF 84
Cdd:pfam00498 1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDG-GGRFYLEDLGSTNGTFVNGQRLGPEPVRLKDGDVIRL 66
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
646-1188 |
8.00e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.00 E-value: 8.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 646 EHYKKLMSQAQELQIKFNSSQ----ETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQER- 720
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKlrelEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYe 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 721 -NRAKETLEEERKRMQELESLLAQQKKALAksitQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEAL 799
Cdd:COG1196 293 lLAELARLEQDIARLEERRRELEERLEELE----EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 800 ESEKRKVQDLENHLTQQKEisESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEE 879
Cdd:COG1196 369 EAEAELAEAEEELEELAEE--LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 880 TQKTKATESLKAESLALKLNETLAELETTKTKMImVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQH----- 954
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALA-ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglaga 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 955 -------------AQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERP----QDPLVAPMTESSAKDMAYEHLID 1017
Cdd:COG1196 526 vavligveaayeaALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPldkiRARAALAAALARGAIGAAVDLVA 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1018 DLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQQS-------KELSVLKEKMAQMSSLV 1090
Cdd:COG1196 606 SDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSltggsrrELLAALLEAEAELEELA 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1091 EKKDRELKALEEALRASQEKHRLQLntEKEQKPRKKTQTCDTSVQIEPVHTEAFSSSQEQQSFSDLGVRCKGSRHEEVIQ 1170
Cdd:COG1196 686 ERLAEEELELEEALLAEEEEERELA--EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE 763
|
570
....*....|....*...
gi 767902113 1171 RQKKALSELRARIKELEK 1188
Cdd:COG1196 764 ELERELERLEREIEALGP 781
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
11-92 |
1.26e-17 |
|
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: 79.24 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 11 FFVLNKSTTIGRHENSDLVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGLT 90
Cdd:cd00060 14 FPLTKGVVTIGRSPDCDIVLDDPSVSRRHARIEVDGGG--VYLEDLGSTNGTFVNGKRITP-PVPLQDGDVIRLGDTTFR 90
|
..
gi 767902113 91 YE 92
Cdd:cd00060 91 FE 92
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
12-93 |
4.80e-17 |
|
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 77.69 E-value: 4.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 12 FVLNKS-TTIGRHENSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGLT 90
Cdd:COG1716 16 FPLDGGpLTIGRAPDNDIVLDDPTVSRRHARIRRDGG--GWVLEDLGSTNGTFVNGQRVTE-PAPLRDGDVIRLGKTELR 92
|
...
gi 767902113 91 YEL 93
Cdd:COG1716 93 FRL 95
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
275-1063 |
3.16e-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: 81.65 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 275 RQNEKEISQkcqvLDEDIDAKQKEIQSLKSQISALQKGYSKVLcQTLSERNSEITSL-KNEGENLKRDNAITSGMVSSLQ 353
Cdd:TIGR02169 233 EALERQKEA----IERQLASLEEELEKLTEEISELEKRLEEIE-QLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 354 KDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRcsvLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLR 433
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE---IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 434 AELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATygrakpfrdk 513
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE---------- 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 514 pvtdqqliEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKE-----VDL 588
Cdd:TIGR02169 455 --------WKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvHGT 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 589 LQHL-QVSPPVSG---------LQKVVLD---VLRHALSWLEE-------------VEQLLRDLGILPSSPNKGFSLYLI 642
Cdd:TIGR02169 527 VAQLgSVGERYATaievaagnrLNNVVVEddaVAKEAIELLKRrkagratflplnkMRDERRDLSILSEDGVIGFAVDLV 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 643 YLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEK---LREHLAEKEKL-----NEERLEQ--EEKLKAKIRQLTEEKAAL 712
Cdd:TIGR02169 607 EFDPKYEPAFKYVFGDTLVVEDIEAARRLMGKYRmvtLEGELFEKSGAmtggsRAPRGGIlfSRSEPAELQRLRERLEGL 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 713 E---EYITQERNRAKETLEEERKRMQELESLLAQQKKALaKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIA 789
Cdd:TIGR02169 687 KrelSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI-EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 790 hEKRKAKEALESEKRKVQDLENHLTQQKeISESNIAYEKrkakeamekEKKKVQDLENRLTKQKEELELKEQKEDVLNNK 869
Cdd:TIGR02169 766 -RIEELEEDLHKLEEALNDLEARLSHSR-IPEIQAELSK---------LEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 870 LSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLIlqqkmvkalqdeqesqrhGFEEEIMEYKE 949
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG------------------DLKKERDELEA 896
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 950 QIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDndpapkEERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQ 1029
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSELKAKLEALEE------ELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
|
810 820 830
....*....|....*....|....*....|....
gi 767902113 1030 QEVIMKLRKDLTEAHSRMSDLRGelnEKQKMELE 1063
Cdd:TIGR02169 971 EPVNMLAIQEYEEVLKRLDELKE---KRAKLEEE 1001
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
291-985 |
3.82e-14 |
|
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: 78.17 E-value: 3.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 291 DIDAKQKEIQSLKSQISALQKGYSKvLCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEV 370
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEE-LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 371 SHLKSQNKDKDHQLEALGSRCSVLKEELKQedahrelreaQEKELKLCKTQIQDMEKEMKKLRAELRKScteqsviSRTL 450
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAE----------LEEKLEELKEELESLEAELEELEAELEEL-------ESRL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 451 REKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATYGRAKPFRDKPVTD-QQLIEKITQVTE 529
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAElEELEEELEELQE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 530 DNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHL--QVSPPVS-------- 599
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsGILGVLSelisvdeg 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 600 -----------GLQKVV---LDVLRHALSWLEEVEQ---------LLRDLGILPSSPN--------KGFSLYLIYLLEHY 648
Cdd:TIGR02168 535 yeaaieaalggRLQAVVvenLNAAKKAIAFLKQNELgrvtflpldSIKGTEIQGNDREilkniegfLGVAKDLVKFDPKL 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 649 KKLMS-------------QAQELQIKFN---------------------SSQETQQSLLQEKlrehlAEKEKLNEERLEQ 694
Cdd:TIGR02168 615 RKALSyllggvlvvddldNALELAKKLRpgyrivtldgdlvrpggvitgGSAKTNSSILERR-----REIEELEEKIEEL 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 695 EEklkaKIRQLTEEKAALEeyitQERNRAKETLEEERKRMQELESLLAQQKKALAKsITQEKNRVKEALEEEQTRVQELE 774
Cdd:TIGR02168 690 EE----KIAELEKALAELR----KELEELEEELEQLRKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELTELE 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 775 ERLARQKEVLESSIAHEKRkAKEALESEKRKVQDLENHLTQQKEISESniayekrkakeamekekkkvqdLENRLTKQKE 854
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAE-AEAEIEELEAQIEQLKEELKALREALDE----------------------LRAELTLLNE 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 855 ELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQE 934
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 767902113 935 SqrhgFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDN 985
Cdd:TIGR02168 898 E----LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
244-953 |
4.52e-14 |
|
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: 77.79 E-value: 4.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 244 EIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQKGYsKVLCQTLSE 323
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL-YALANEISR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 324 RNSEITSLKNEGENLKRDNAITSGMVSSL--QKDILAKD-----EQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKE 396
Cdd:TIGR02168 300 LEQQKQILRERLANLERQLEELEAQLEELesKLDELAEElaeleEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 397 ELKQE----DAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQS-----VISRTLREKSKVEEKLQEDSRRK 467
Cdd:TIGR02168 380 QLETLrskvAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaelkELQAELEELEEELEELQEELERL 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 468 LLQLQEMGNRESVIKINLERAVGQLEHFRSQ--VIKATYGRAKPFRD--KPVTDQQL-IEKITQVTEDNINFQqKKWTLQ 542
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQARldSLERLQENLEGFSEgvKALLKNQSgLSGILGVLSELISVD-EGYEAA 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 543 KETQLSNSKQEETTEN-------IEKLRTSLDSCQACMKISCCSHDlKKEVDLLQHLQVSPPVSG-----------LQKV 604
Cdd:TIGR02168 539 IEAALGGRLQAVVVENlnaakkaIAFLKQNELGRVTFLPLDSIKGT-EIQGNDREILKNIEGFLGvakdlvkfdpkLRKA 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 605 VLDVLRHaLSWLEEVEQLLRDLGILPSSPN----------KGFSLY----------------LIYLLEHYKKLMSQAQEL 658
Cdd:TIGR02168 618 LSYLLGG-VLVVDDLDNALELAKKLRPGYRivtldgdlvrPGGVITggsaktnssilerrreIEELEEKIEELEEKIAEL 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 659 QIKFNSSQETQQSLLQE--KLREHLAEKEKLNEERLEQEEKLKAKIRQLTE-------EKAALEEYITQERNR------A 723
Cdd:TIGR02168 697 EKALAELRKELEELEEEleQLRKELEELSRQISALRKDLARLEAEVEQLEEriaqlskELTELEAEIEELEERleeaeeE 776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 724 KETLEEERkrmQELESLLAQQKKALAKSitqeknrvKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEK 803
Cdd:TIGR02168 777 LAEAEAEI---EELEAQIEQLKEELKAL--------REALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 804 RKVQDLENHLTQQKEISESNIAYEKrkAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKT 883
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEE--LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 884 KATESLKAESLALKLNETLAELettktkmimvEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQ 953
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQERL----------SEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
20-93 |
4.15e-13 |
|
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: 66.57 E-value: 4.15e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767902113 20 IGRhENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHI-QNVAVKLIPGDILRFGSAGLTYEL 93
Cdd:cd22704 21 VGR-EDCDLILQSRSVDKQHAVITYDQIDNEFKIKDLGSLNGTFVNDSRIpEQTYITLKLGDSIRFGYDTNVYRF 94
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
12-92 |
3.65e-12 |
|
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: 63.79 E-value: 3.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 12 FVLNK-STTIGRHENSDLVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHI--QNVAVKLIPGDILRFGSAG 88
Cdd:cd22665 16 FPLYEgENVIGRDPSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNKVRlkPNVRYELIDGDLLLFGDVK 93
|
....
gi 767902113 89 LTYE 92
Cdd:cd22665 94 CQYV 97
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
12-86 |
7.28e-12 |
|
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: 62.71 E-value: 7.28e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767902113 12 FVLNKST-TIGRHENSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIqNVAVKLIPGDILRFGS 86
Cdd:cd22693 13 FPIDKSGiTIGRADDNDLVLSDDFVSSRHARIYLQGS--SWYLEDLGSTNGTFVNGNRV-TQPVVVQPGDTIRIGA 85
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
645-1392 |
1.26e-11 |
|
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: 69.70 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 645 LEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAkirqLTEEKAALEEyitqernrak 724
Cdd:TIGR02168 202 LKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEE----LTAELQELEE---------- 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 725 eTLEEERKRMQELESLLAQQKKALaKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKR 804
Cdd:TIGR02168 268 -KLEELRLEVSELEEEIEELQKEL-YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 805 KVQDLENHLTQQKEISESNIAYEkrkakeameKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTK 884
Cdd:TIGR02168 346 LEELKEELESLEAELEELEAELE---------ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 885 ATESLKAESLALKLNET-LAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEE 963
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 964 KLQK----------VTQHHKKIEGEIATLKDNDPAPKE----------ERPQDPLVApmTESSAKDmAYEHL-------- 1015
Cdd:TIGR02168 497 LQENlegfsegvkaLLKNQSGLSGILGVLSELISVDEGyeaaieaalgGRLQAVVVE--NLNAAKK-AIAFLkqnelgrv 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1016 ---------IDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMS--------------DLRGELNEKQKMELEQNVV----- 1067
Cdd:TIGR02168 574 tflpldsikGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvdDLDNALELAKKLRPGYRIVtldgd 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1068 -----------------LVQQQSKELSVLKEKMAQMSSLVEKKDRELKALEEALRASQEKHRlQLNTEKEQKPRKKTQTc 1130
Cdd:TIGR02168 654 lvrpggvitggsaktnsSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE-QLRKELEELSRQISAL- 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1131 DTSVQIEPVHTEAFSSSQEQQSFSDLGVRCKGSRHEEVIQRQKKALSELRARIKELEkARSPDHKDHQNESFLDLKNLRM 1210
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE-AQIEQLKEELKALREALDELRA 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1211 ENNVQKILLDAKpdlptLSRIEILAPQNGLCNARFGSAMEKSGKM-----DVAEALELSEKLYLDMSKTLGSLMNIKnMS 1285
Cdd:TIGR02168 811 ELTLLNEEAANL-----RERLESLERRIAATERRLEDLEEQIEELsedieSLAAEIEELEELIEELESELEALLNER-AS 884
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1286 GHVSMKYLSRQEREKVNQLRQRDldlvfDKITQLKNQLGRKEELLRGYEKDVEQLrrsKVSIEMYQSQVAKLEDDIYKEA 1365
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELE-----SKRSELRRELEELREKLAQLELRLEGL---EVRIDNLQERLSEEYSLTLEEA 956
|
810 820
....*....|....*....|....*...
gi 767902113 1366 EEKALLKEA-LERMEHQLcqeKRINRAI 1392
Cdd:TIGR02168 957 EALENKIEDdEEEARRRL---KRLENKI 981
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
286-852 |
3.90e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 3.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 286 QVLDEDIDAKQKEIQSLKSQISALQKgyskvlcqTLSERNSEITSLKNEGENLKRDnaitsgmVSSLQKDILAKDEQVQQ 365
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEA--------ELAELEAELEELRLELEELELE-------LEEAQAEEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 366 LKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKlckTQIQDMEKEMKKLRAELRKSCTEQSV 445
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE---EELEEAEAELAEAEEALLEAEAELAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 446 ISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATygrakpfrdkpVTDQQLIEKIT 525
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE-----------EEEEEEEEALE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 526 QVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQAcmkisccSHDLKKEVDLLQHLQVSPP----VSGL 601
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA-------RLLLLLEAEADYEGFLEGVkaalLLAG 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 602 QKVVLDVLRHALSWLEEVEQLLRDLGILPSSPNKGFSL-----YLIYLLEHYKKLMSQAQELQIK-FNSSQETQQSLLQE 675
Cdd:COG1196 519 LRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDevaaaAIEYLKAAKAGRATFLPLDKIRaRAALAAALARGAIG 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 676 KLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQE 755
Cdd:COG1196 599 AAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 756 KNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEAM 835
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
|
570
....*....|....*..
gi 767902113 836 EKEKKKVQDLENRLTKQ 852
Cdd:COG1196 759 PPDLEELERELERLERE 775
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
675-1133 |
5.64e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.86 E-value: 5.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 675 EKLREHLAEKEKLNEERLEQEEKLKA-KIRQLTEEKAALEEyiTQERNRAKETLEEERKRMQELESLLAQQKKALAKSIT 753
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKAEEKKKAdEAKKKAEEAKKADE--AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA 1485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 754 QEknrVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKE 833
Cdd:PTZ00121 1486 DE---AKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEE 1562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 834 AMEKEKKKVQDLENRLTKQKEELELKEQKEdvlnnKLSDALAMVEETQKTKATESLKAESLALKLNETLAELEttktkmi 913
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRKAEEAKKAEEA-----RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE------- 1630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 914 mvEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKieGEIATLKDNDPAPKEER 993
Cdd:PTZ00121 1631 --EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK--AAEALKKEAEEAKKAEE 1706
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 994 PQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQqs 1073
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE-- 1784
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1074 kelsvLKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQTCDTS 1133
Cdd:PTZ00121 1785 -----LDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSK 1839
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
213-968 |
5.99e-11 |
|
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: 67.69 E-value: 5.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 213 AEIYVEEDLAQQDKDEIILLLGKEVSRLSDYEIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDI 292
Cdd:pfam02463 244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEK 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 293 DAKQKEIQSLKSQISALQKGYSKVLCQTLSERNSEITSLKNEGENLKRDNAITSGmVSSLQKDILAKDEQVQQLKEEVSH 372
Cdd:pfam02463 324 KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAK-KKLESERLSSAAKLKEEELELKSE 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 373 LKSQNKDKDHQLEALGSRCSVL-KEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLR 451
Cdd:pfam02463 403 EEKEAQLLLELARQLEDLLKEEkKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKL 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 452 EKSKVE---EKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEH---FRSQVIKATYGRAKPFRDKPVTDQQLIEKIT 525
Cdd:pfam02463 483 QEQLELllsRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHgrlGDLGVAVENYKVAISTAVIVEVSATADEVEE 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 526 QVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHLQVSPPVSGLQKVV 605
Cdd:pfam02463 563 RQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAK 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 606 -----LDVLRHALSWLEEVEQLLRDLGILPSSPNKGFSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREH 680
Cdd:pfam02463 643 akesgLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEEL 722
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 681 LAEKEKLNEERLEQEEKL---KAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKN 757
Cdd:pfam02463 723 LADRVQEAQDKINEELKLlkqKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEE 802
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 758 RvKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLEnHLTQQKEISESNIAYEKRKAKEAMEK 837
Cdd:pfam02463 803 L-RALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEE-ELERLEEEITKEELLQELLLKEEELE 880
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 838 EKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEE 917
Cdd:pfam02463 881 EQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEE 960
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 767902113 918 RLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKV 968
Cdd:pfam02463 961 RNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAI 1011
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
667-970 |
1.11e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 667 ETQQSLlqEKLREHLAEKEKlNEERLEQEEKLKAKIRQLTEEKAALE-EYITQERNRAKETLEEERKRMQELESLLAQQK 745
Cdd:COG1196 183 ATEENL--ERLEDILGELER-QLEPLERQAEKAERYRELKEELKELEaELLLLKLRELEAELEELEAELEELEAELEELE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 746 KALAKsITQEKNRVKEALEEEQTRVQEL---EERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISEs 822
Cdd:COG1196 260 AELAE-LEAELEELRLELEELELELEEAqaeEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE- 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 823 niayEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETL 902
Cdd:COG1196 338 ----ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767902113 903 AELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQ 970
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
237-779 |
1.27e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 237 VSRLSDYEIESKYKDVIIANLQNEVAELSQKVSETTTSRQnekEISQKCQVLDEDIDAKQKEIQSLKSQISALQKGySKV 316
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYELLAELARLEQD-IAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 317 LCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKE 396
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 397 ELKQEDAHRELREAQEKELKL----CKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQ 472
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEaeeaLLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 473 EMGNRESVIKINLERAVGQLEHFRSQ--VIKATYGRAKPFRD--KPVTDQQLIEKITQVTEDNINFQQKKWTLQkETQLS 548
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARllLLLEAEADYEGFLEgvKAALLLAGLRGLAGAVAVLIGVEAAYEAAL-EAALA 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 549 NSKQEETTEN-------IEKLRTSLDSCQACMKIScCSHDLKKEVDLLQHLQVSPPVSGLQkvVLDVLRHALSWLEEVEQ 621
Cdd:COG1196 546 AALQNIVVEDdevaaaaIEYLKAAKAGRATFLPLD-KIRARAALAAALARGAIGAAVDLVA--SDLREADARYYVLGDTL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 622 LLRDLGILPSSPNKGFSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAK 701
Cdd:COG1196 623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767902113 702 IRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAksITQEKNRVKEALEEEQTRVQELEERLAR 779
Cdd:COG1196 703 EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE--EALEELPEPPDLEELERELERLEREIEA 778
|
|
| FHA_DUN1-like |
cd22683 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ... |
17-85 |
1.32e-10 |
|
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: 59.43 E-value: 1.32e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767902113 17 STTIGRHENSDLVLQSPDIDNHHALIEYnEAECSFVLqDFNSRNGTFVNECHIQNVAVKLIPGDILRFG 85
Cdd:cd22683 22 VTTIGRSRSCDLVLSDPSISRFHAELRL-EQNGINVI-DNNSANGTFINGKRIKGKTYILKNGDIIVFG 88
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
233-982 |
1.94e-10 |
|
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: 65.86 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 233 LGKEVSRLSDYEIESKYKDviIANLQNEVAELSQKVSEtttSRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQKG 312
Cdd:TIGR02169 277 LNKKIKDLGEEEQLRVKEK--IGELEAEIASLERSIAE---KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 313 YSKvLCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDI--------------LAKDEQVQQLKEEVSHLKSQNK 378
Cdd:TIGR02169 352 RDK-LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLeklkreinelkrelDRLQEELQRLSEELADLNAAIA 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 379 DKDHQLEALGSRCSVLKEELKQEDAHRE----LREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKS 454
Cdd:TIGR02169 431 GIEAKINELEEEKEDKALEIKKQEWKLEqlaaDLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 455 KVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHF-----------------RSQVIKATYGRAKPFRDKPVTD 517
Cdd:TIGR02169 511 AVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNvvveddavakeaiellkRRKAGRATFLPLNKMRDERRDL 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 518 QQLIEK-ITQVTEDNINFQQK-----KWTLQkETQLsnskqeetTENIEKLRTSLDSCQAcmkisccshdLKKEVDLLQH 591
Cdd:TIGR02169 591 SILSEDgVIGFAVDLVEFDPKyepafKYVFG-DTLV--------VEDIEAARRLMGKYRM----------VTLEGELFEK 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 592 lqvSPPVSGLQKVVLDVLRHALSWLEEVEQLLRDLGILPSSPNKgfslyLIYLLEHYKKLMSQAQELQikfnsSQETQQS 671
Cdd:TIGR02169 652 ---SGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSS-----LQSELRRIENRLDELSQEL-----SDASRKI 718
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 672 LLQEKLREHLAEKEKLNEERLEQ-EEKLKAKIRQLTEEKAALEEYItQERNRAKETLEEERKRMQELESLLAQQKkalAK 750
Cdd:TIGR02169 719 GEIEKEIEQLEQEEEKLKERLEElEEDLSSLEQEIENVKSELKELE-ARIEELEEDLHKLEEALNDLEARLSHSR---IP 794
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 751 SITQEKNRVKEALEEEQTRVQELEERLAR---QKEVLESSIAHEKRKAKEALESEKrkvqdlenhlTQQKEISESNIayE 827
Cdd:TIGR02169 795 EIQAELSKLEEEVSRIEARLREIEQKLNRltlEKEYLEKEIQELQEQRIDLKEQIK----------SIEKEIENLNG--K 862
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 828 KRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESlalkLNETLAELET 907
Cdd:TIGR02169 863 KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA----LEEELSEIED 938
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767902113 908 TKTKMIMVEERLILQQKMVKALQDEQESQRhGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATL 982
Cdd:TIGR02169 939 PKGEDEEIPEEELSLEDVQAELQRVEEEIR-ALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
260-849 |
1.05e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 260 EVAELSQKVSETTTSRQNE------KEISQKCQVLDEDIDAKQKEIQSLKSQISALQKGYSKVLcQTLSERNSEITSLKN 333
Cdd:COG1196 210 EKAERYRELKEELKELEAEllllklRELEAELEELEAELEELEAELEELEAELAELEAELEELR-LELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 334 EGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEK 413
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 414 ELklcKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLE 493
Cdd:COG1196 369 EA---EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 494 HFRSQVIKATygrakpfrdkpvTDQQLIEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDScqacm 573
Cdd:COG1196 446 EAAEEEAELE------------EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE----- 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 574 kisccshDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRHALSWLEEVEQ--LLRDLGILpsspnkgfSLYLIYLLEHYKKL 651
Cdd:COG1196 509 -------GVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQniVVEDDEVA--------AAAIEYLKAAKAGR 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 652 MSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEER 731
Cdd:COG1196 574 ATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEG 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 732 KRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLEN 811
Cdd:COG1196 654 EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733
|
570 580 590
....*....|....*....|....*....|....*...
gi 767902113 812 HLTQQKEISESNIAYEkrKAKEAMEKEKKKVQDLENRL 849
Cdd:COG1196 734 REELLEELLEEEELLE--EEALEELPEPPDLEELEREL 769
|
|
| FHA_PS1-like |
cd22691 |
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) ... |
19-93 |
1.41e-09 |
|
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: 57.04 E-value: 1.41e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767902113 19 TIGRHENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFGSAGLTYEL 93
Cdd:cd22691 32 VVGRHPDCDIVLDHPSISRFHLEIRIIPSRRKITLTDLSSVHGTWVNGQRIEpGVPVELEEGDTVRLGASTRVYRL 107
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
703-1109 |
2.10e-09 |
|
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: 62.39 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 703 RQLTEEKAALEEYiTQERNRAKETLEEERKRMQELESLLAqqkkalaksitqEKNRVKEALEEEQTRVQELEERLARQKE 782
Cdd:TIGR02169 156 RKIIDEIAGVAEF-DRKKEKALEELEEVEENIERLDLIID------------EKRQQLERLRREREKAERYQALLKEKRE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 783 VLESSIAHEKRKAKEALESEKRKVQDLENHLTQ-QKEISESNIAYEKRKAKeamekekkkVQDLENRLTKQKEELELKeq 861
Cdd:TIGR02169 223 YEGYELLKEKEALERQKEAIERQLASLEEELEKlTEEISELEKRLEEIEQL---------LEELNKKIKDLGEEEQLR-- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 862 kedvLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFE 941
Cdd:TIGR02169 292 ----VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 942 EEIMEYKEQIKQHAQT---IVSLEEKLQKVTQHHKKIEGEIatlkdndpapkeerpqdplvapmtessakdmayEHLIDD 1018
Cdd:TIGR02169 368 DLRAELEEVDKEFAETrdeLKDYREKLEKLKREINELKREL---------------------------------DRLQEE 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1019 LLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELnEKQKMELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELK 1098
Cdd:TIGR02169 415 LQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI-KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
|
410
....*....|.
gi 767902113 1099 ALEEALRASQE 1109
Cdd:TIGR02169 494 EAEAQARASEE 504
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
19-85 |
2.39e-09 |
|
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: 56.03 E-value: 2.39e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902113 19 TIGRHENSDLVLQSPDIDNHHALIEYN----EAECSFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFG 85
Cdd:cd22677 25 VFGRLPGCDVVLEHPSISRYHAVLQYRgdadDHDGGFYLYDLGSTHGTFLNKQRIPpKQYYRLRVGHVLKFG 96
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
18-65 |
3.92e-09 |
|
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.
Pssm-ID: 214578 [Multi-domain] Cd Length: 52 Bit Score: 53.72 E-value: 3.92e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 767902113 18 TTIGRHENS-DLVLQSPDIDNHHALIEYNEAECsFVLQDFNSRNGTFVN 65
Cdd:smart00240 1 VTIGRSSEDcDIQLDGPSISRRHAVIVYDGGGR-FYLIDLGSTNGTFVN 48
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
686-1121 |
4.56e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 4.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 686 KLNEERLEQEEKLKAkirqlTEEKAALEEYITQERNRAKETLEEER---KRMQELESLLAQQKKALAKSITQEKNRVKEA 762
Cdd:COG1196 169 KYKERKEEAERKLEA-----TEENLERLEDILGELERQLEPLERQAekaERYRELKEELKELEAELLLLKLRELEAELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 763 LEEEQTRVQELEERLARQKEVLESSIAhEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAkeamekekkkv 842
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELE-ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR----------- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 843 QDLENRLTKQKEELelkeqkedvlnnklsdalamvEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQ 922
Cdd:COG1196 312 RELEERLEELEEEL---------------------AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 923 QKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERpqdplvapm 1002
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE--------- 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1003 tessakdMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQQSKELSVLKEK 1082
Cdd:COG1196 442 -------EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 767902113 1083 MAQMSSLVEKKDREL----KALEEALRASQEKHRLQLNTEKEQ 1121
Cdd:COG1196 515 LLAGLRGLAGAVAVLigveAAYEAALEAALAAALQNIVVEDDE 557
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
675-1116 |
7.40e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.93 E-value: 7.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 675 EKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLE--EERKRMQELESLLAQQKKAL---- 748
Cdd:PTZ00121 1332 DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKAdelk 1411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 749 -----------AKSITQEKNRVKEALE--EEQTRVQELEERLARQKEVLESS-IAHEKRKAKEALE--SEKRKVQDLENH 812
Cdd:PTZ00121 1412 kaaaakkkadeAKKKAEEKKKADEAKKkaEEAKKADEAKKKAEEAKKAEEAKkKAEEAKKADEAKKkaEEAKKADEAKKK 1491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 813 LTQ-QKEISESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVlnnKLSDALAMVEETQKT----KATE 887
Cdd:PTZ00121 1492 AEEaKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK---KKADELKKAEELKKAeekkKAEE 1568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 888 SLKAE---SLALKLNETLAELETTKTKMIMveeRLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEK 964
Cdd:PTZ00121 1569 AKKAEedkNMALRKAEEAKKAEEARIEEVM---KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE 1645
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 965 LQKVTQHHKkiEGEIATLKDNDPAPKEERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKeilsqqevIMKLRKDLTEAH 1044
Cdd:PTZ00121 1646 KKKAEELKK--AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK--------AEELKKKEAEEK 1715
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1045 SRMSDLRG--ELNEKQKMELEQNVVLVQQQSKELSV---LKEKMAQMSSLVEKKDRELKA-----LEEALRASQEKHRLQ 1114
Cdd:PTZ00121 1716 KKAEELKKaeEENKIKAEEAKKEAEEDKKKAEEAKKdeeEKKKIAHLKKEEEKKAEEIRKekeavIEEELDEEDEKRRME 1795
|
..
gi 767902113 1115 LN 1116
Cdd:PTZ00121 1796 VD 1797
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
675-1112 |
8.45e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 8.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 675 EKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKE--TLEEERKRMQELESLLAQQKKALAKsI 752
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkELKEKAEEYIKLSEFYEEYLDELRE-I 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 753 TQEKNRVKEALEEEQTRVQELEERLARQKEVLEssiahEKRKAKEALESEKRKVQDLENHLTQQKEISEsniaYEKRKAK 832
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKEERLEELKK-----KLKELEKRLEELEERHELYEEAKAKKEELER----LKKRLTG 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 833 EAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKA---------TESLKAESLA---LKLNE 900
Cdd:PRK03918 384 LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgrelTEEHRKELLEeytAELKR 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 901 TLAELETTKT-------------KMIMVEERLILQQKMVKALQD-EQESQRHGFEEEIMEYKE----------------- 949
Cdd:PRK03918 464 IEKELKEIEEkerklrkelreleKVLKKESELIKLKELAEQLKElEEKLKKYNLEELEKKAEEyeklkekliklkgeiks 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 950 ------QIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERPQDPLVAPMTESSAKDMAyehliDDLLAAQ 1023
Cdd:PRK03918 544 lkkeleKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAE-----KELEREE 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1024 KEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKM----ELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKA 1099
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK 698
|
490
....*....|...
gi 767902113 1100 LEEALRASQEKHR 1112
Cdd:PRK03918 699 LKEELEEREKAKK 711
|
|
| FHA_Ki67 |
cd22673 |
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ... |
11-92 |
9.55e-09 |
|
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: 54.14 E-value: 9.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 11 FFVLNKSTTIGRHENSDLVLQSPDIDNHHALIEYNEAECsFVLQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGLT 90
Cdd:cd22673 16 FPLTKKSCTFGRDLSCDIRIQLPGVSREHCRIEVDENGK-AYLENLSTTNPTLVNGKAIEK-SAELKDGDVITIGGRSFR 93
|
..
gi 767902113 91 YE 92
Cdd:cd22673 94 FE 95
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
650-1010 |
9.69e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.54 E-value: 9.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 650 KLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKA----KIRQLTEEKAALEEYITQERNRAKE 725
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAdeakKKAEEAKKKADEAKKAAEAKKKADE 1514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 726 TLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQElEERLARQKEVLESSIAHEKRKAKEALESEKRK 805
Cdd:PTZ00121 1515 AKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE-EKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 806 VQDLENHLTQQKEI--SESNIAYEKRKAKEAMEKEKKKVQDLEN--RLTKQKEELELKEQKEDVLNNKLSDALAMVEETQ 881
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMkaEEAKKAEEAKIKAEELKKAEEEKKKVEQlkKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 882 KTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSL 961
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE 1753
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 767902113 962 EEKlQKVTQHHKKIEGEIATLKDNDPAPKEE--RPQDPLVAPMTESSAKDM 1010
Cdd:PTZ00121 1754 EEK-KKIAHLKKEEEKKAEEIRKEKEAVIEEelDEEDEKRRMEVDKKIKDI 1803
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
19-157 |
1.66e-08 |
|
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: 58.62 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 19 TIGRHENSDLVLQSPD--IDNHHALIEYneAECSFVLQDfNSRNGTFVNECHI---QNVAVKLIPGDILRFGSagltYEL 93
Cdd:COG3456 29 TIGRSADCDWVLPDPDrsVSRRHAEIRF--RDGAFCLTD-LSTNGTFLNGSDHplgPGRPVRLRDGDRLRIGD----YEI 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767902113 94 V--IENPPPVSFPWMRGPAPWPGPQPPRATQQPNqAPPPshiPFHQGVQPAPMQRSWSQAFPRPTV 157
Cdd:COG3456 102 RveISGEDEGADDPLAAAPEPAVSSPSNLSDTEA-APDA---ALAFSFSLDPLEALDEAATEAPAT 163
|
|
| FHA_Cep170A |
cd22724 |
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar ... |
20-85 |
2.58e-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: 53.44 E-value: 2.58e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767902113 20 IGRhENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHI-QNVAVKLIPGDILRFG 85
Cdd:cd22724 25 VGR-DDCELMLQSRSVDKQHAVINYDASTDEHKVKDLGSLNGTFVNDVRIpEQTYITLKLDDKLRFG 90
|
|
| FHA_MEK1-like |
cd22670 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ... |
15-92 |
2.70e-08 |
|
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: 53.00 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 15 NKSTTIGRHENSDLVLQSPDIDNHHALIE---YNEAECSFV-LQDfNSRNGTFVNECHI-QNVAVKLIPGDILRF-GSAG 88
Cdd:cd22670 21 NQVITIGRSPSCDIVINDPFVSRTHCRIYsvqFDESSAPLVyVED-LSSNGTYLNGKLIgRNNTVLLSDGDVIEIaHSAT 99
|
....
gi 767902113 89 LTYE 92
Cdd:cd22670 100 FVYV 103
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
682-1229 |
2.97e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 682 AEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEyiTQERNRAKETLEEERKRMQElesllAQQKKALAKSITQEKNRVKE 761
Cdd:PTZ00121 1274 AEEARKADELKKAEEKKKADEAKKAEEKKKADE--AKKKAEEAKKADEAKKKAEE-----AKKKADAAKKKAEEAKKAAE 1346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 762 ALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALE--SEKRKVQDLENHLTQQK----EISESNIAYEKRKAKEAM 835
Cdd:PTZ00121 1347 AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKkkadELKKAAAAKKKADEAKKK 1426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 836 EKEKKKVQDLENRLTKQKEELELKEQKEDvlNNKLSDALAMVEETQKT-----KATESLKAESLALKLNETLAELETTKT 910
Cdd:PTZ00121 1427 AEEKKKADEAKKKAEEAKKADEAKKKAEE--AKKAEEAKKKAEEAKKAdeakkKAEEAKKADEAKKKAEEAKKKADEAKK 1504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 911 KMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQ-----HAQTIVSLEEKlQKVTQHHKKIEGEIATLKDN 985
Cdd:PTZ00121 1505 AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKadelkKAEELKKAEEK-KKAEEAKKAEEDKNMALRKA 1583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 986 DPAPKEERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEvimKLRKDLTEAHSRMSDLRGELNEKQKMELEQN 1065
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE---EEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1066 VVLVQQQSKElsvlKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQTCDTSVQIEPVHTEAFS 1145
Cdd:PTZ00121 1661 IKAAEEAKKA----EEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAK 1736
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1146 SSQEQQSFSDLGVRCKGSRHEEVIQRQKKALSELRARIKELEKA--RSPDHKDHQNESFLDLKNLRMENNVQKILLDAKP 1223
Cdd:PTZ00121 1737 KEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVieEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
|
....*.
gi 767902113 1224 DLPTLS 1229
Cdd:PTZ00121 1817 GNLVIN 1822
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
221-1098 |
3.21e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 58.44 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 221 LAQQDKDEIILLL-GKEVSRLSDYEIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKeisqkcQVLDEDIDAKQKEI 299
Cdd:pfam02463 138 LVQGGKIEIIAMMkPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKL------QELKLKEQAKKALE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 300 QSLKSQISALQKGYSKV-----LCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEvsHLK 374
Cdd:pfam02463 212 YYQLKEKLELEEEYLLYldylkLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEE--ELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 375 SQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRaelRKSCTEQSVISRTLREKS 454
Cdd:pfam02463 290 LLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELE---IKREAEEEEEEELEKLQE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 455 KVEEKLQEDSRRKLLQLQEMGNRESVIKINLE-RAVGQLEHFRSQVIKATYGRAKPFRDKPVTDQQLIEKITQvtEDNIN 533
Cdd:pfam02463 367 KLEQLEEELLAKKKLESERLSSAAKLKEEELElKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESI--ELKQG 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 534 FQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHlqvSPPVSGLQKVVLDVLRHAL 613
Cdd:pfam02463 445 KLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKE---SKARSGLKVLLALIKDGVG 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 614 SWLEEVEQLLRDLGILPSSPNKGFSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEK---EKLNEE 690
Cdd:pfam02463 522 GRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKsiaVLEIDP 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 691 RLEQEEKLKAKIRQLTEEKAAL-----EEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEE 765
Cdd:pfam02463 602 ILNLAQLDKATLEADEDDKRAKvvegiLKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQEL 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 766 EQTRVQELE-----ERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEAMEKEKK 840
Cdd:pfam02463 682 QEKAESELAkeeilRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEE 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 841 KVQDLENRLTKQKEELELKEQKEDVLNN--KLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEER 918
Cdd:pfam02463 762 KEEEKSELSLKEKELAEEREKTEKLKVEeeKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALE 841
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 919 LILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKV--TQHHKKIEGEIATLKDNDPAPKEERpqd 996
Cdd:pfam02463 842 LKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKeeKEKEEKKELEEESQKLNLLEEKENE--- 918
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 997 pLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQQSKEL 1076
Cdd:pfam02463 919 -IEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEK 997
|
890 900
....*....|....*....|..
gi 767902113 1077 SVLKEKMAQMSSLVEKKDRELK 1098
Cdd:pfam02463 998 ERLEEEKKKLIRAIIEETCQRL 1019
|
|
| FHA_Cep170B |
cd22725 |
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) ... |
20-93 |
4.34e-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: 4.34e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767902113 20 IGRhENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQN---VAVKLipGDILRFGSAGLTYEL 93
Cdd:cd22725 25 VGR-EDCELMLQSRSVDKQHAVINYDQDTDEHWVKDLGSLNGTFVNDVRIPDqkyITLKL--NDVIRFGYDSNMYVL 98
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
661-1396 |
4.64e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 661 KFNSSQETQQSLLQEKLREHLAEKeKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESL 740
Cdd:PTZ00121 1099 KAEEAKKTETGKAEEARKAEEAKK-KAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKK 1177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 741 LAQQKKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEAL--ESEKRKVQDLENHLTQQKe 818
Cdd:PTZ00121 1178 AEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKkdAEEAKKAEEERNNEEIRK- 1256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 819 ISESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELElkeqkedvlnnKLSDALAMVEETQKtKATESLKAESLALKL 898
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEA-----------KKAEEKKKADEAKK-KAEEAKKADEAKKKA 1324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 899 NETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEyKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGE 978
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK-KEEAKKKADAAKKKAEEKKKADEAKKKAEED 1403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 979 IATLKDNDPAPKEERPQDPLVAPMTESSAKDMAyehliddllaaqKEILSQQEVIMKLRKDLTEAhSRMSDLRGELNEKQ 1058
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEAKKKAEEKKKADEA------------KKKAEEAKKADEAKKKAEEA-KKAEEAKKKAEEAK 1470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1059 KMELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQTCDTSVQIEP 1138
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADE 1550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1139 VHT-----EAFSSSQEQQSFSDLGVRCKGSRHEEVIQRQKKALSELRARIKELEKARSPDHKDHQNESFLDLKNLRMENN 1213
Cdd:PTZ00121 1551 LKKaeelkKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE 1630
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1214 VQKILLDAKPDLPTlsrieilapqnglcNARFGSAMEKSGKMDVAEALELSEKLYLDMSKTLGSLMNIKNMSGHVSMKYL 1293
Cdd:PTZ00121 1631 EKKKVEQLKKKEAE--------------EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1294 SRQEREKVNQLRQRDLDLVfDKITQLKNQ----LGRKEELLRGYEKDVEQLRRSKVSiEMYQSQVAKLEDDIYKEAEEKA 1369
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAEEK-KKAEELKKAeeenKIKAEEAKKEAEEDKKKAEEAKKD-EEEKKKIAHLKKEEEKKAEEIR 1774
|
730 740
....*....|....*....|....*..
gi 767902113 1370 LLKEALERMEHQLCQEKRINRAIRQQK 1396
Cdd:PTZ00121 1775 KEKEAVIEEELDEEDEKRRMEVDKKIK 1801
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
17-85 |
5.29e-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: 51.94 E-value: 5.29e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767902113 17 STTIGRHENSDLVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHIQnvAVKLIPGDILRFG 85
Cdd:cd22694 17 SVRIGRDPDADVRLDDPRVSRRHALLEFDGDG--WVYTDLGSRNGTYLNGRRVQ--QVKLSDGTRVRLG 81
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
675-1186 |
5.36e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 5.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 675 EKLREHLAEKEKLNEERLEQEEKLKA--KIRQLTEEKAALEEYITQERNRAKETLE--EERKRMQELESLLAQQKKALAK 750
Cdd:PTZ00121 1305 DEAKKKAEEAKKADEAKKKAEEAKKKadAAKKKAEEAKKAAEAAKAEAEAAADEAEaaEEKAEAAEKKKEEAKKKADAAK 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 751 SITQEKNRVKEA---LEEEQTRVQELEERLARQKEVLESSI-AHEKRKAKEALE--SEKRKVQDLENHLTQQKEISESNI 824
Cdd:PTZ00121 1385 KKAEEKKKADEAkkkAEEDKKKADELKKAAAAKKKADEAKKkAEEKKKADEAKKkaEEAKKADEAKKKAEEAKKAEEAKK 1464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 825 AYEkrkakeamekekkkvqdlENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKT-----KATESLKAESlALKLN 899
Cdd:PTZ00121 1465 KAE------------------EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAaeakkKADEAKKAEE-AKKAD 1525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 900 ETLAELETTKTKMIMVEERLILQQKMVKAlqdeqESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQhhKKIEGEI 979
Cdd:PTZ00121 1526 EAKKAEEAKKADEAKKAEEKKKADELKKA-----EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE--ARIEEVM 1598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 980 ATLKDNDPAPKEERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEvimKLRKDLTEAHSRMSDL-RGELNEKQ 1058
Cdd:PTZ00121 1599 KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE---ELKKAEEENKIKAAEEaKKAEEDKK 1675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1059 KMELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQTCDTSVQIEP 1138
Cdd:PTZ00121 1676 KAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 767902113 1139 VHTEAFSSSQEQQSFSDLGVRCKGSRHEEVIQRQKKALSELRARIKEL 1186
Cdd:PTZ00121 1756 KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDI 1803
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
618-1406 |
5.75e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 57.67 E-value: 5.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 618 EVEQLLRDLGILPSSPN-------------------------KGFSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSL 672
Cdd:pfam02463 120 EVAELLESQGISPEAYNflvqggkieiiammkperrleieeeAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 673 LQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSI 752
Cdd:pfam02463 200 LKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEK 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 753 TQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAK 832
Cdd:pfam02463 280 EKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 833 EAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMV-----------------EETQKTKATESLKAESLA 895
Cdd:pfam02463 360 ELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEkeaqlllelarqledllKEEKKEELEILEEEEESI 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 896 LKLNETLAELETTKTKMIMVEERLILQQKMVKALQDE---QESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHH 972
Cdd:pfam02463 440 ELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKEtqlVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDG 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 973 KKIEGEIATLKDNDPAP-KEERPQDPLVAPMTESSAK---DMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMS 1048
Cdd:pfam02463 520 VGGRIISAHGRLGDLGVaVENYKVAISTAVIVEVSATadeVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEI 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1049 DLRGELNEKQKMELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQ 1128
Cdd:pfam02463 600 DPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQ 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1129 TCDTSVQIEpVHTEAFSSSQEQQSFSDLGVRCKGSRHEEVIQRQKKALSELRARIKELEKARSPDHKDHQNESFLDLKNL 1208
Cdd:pfam02463 680 ELQEKAESE-LAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLK 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1209 RMENNVQKILLDAKPDLPTLSRIEILAPQNGLCNARFGSAMEKSGKMDVAEALELSEKLYLDMSKTLGSLMNIKNMSGHV 1288
Cdd:pfam02463 759 KEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEEL 838
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1289 SMKYLSRQEREKVNQLRQRDLDLVFDKITQLKNQLGRKEELLRGYEKDVEQLRRSKVSIE----MYQSQVAKLEDDIYKE 1364
Cdd:pfam02463 839 ALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEkkelEEESQKLNLLEEKENE 918
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 767902113 1365 AEEKALLKEALERMEHQLCQEKRINRAIRQQKMRKLRLRELR 1406
Cdd:pfam02463 919 IEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEE 960
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
13-86 |
6.33e-08 |
|
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: 51.98 E-value: 6.33e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767902113 13 VLNKSTTIGRHENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVN--ECHIQNVAVKLIPGDILRFGS 86
Cdd:cd22678 20 GTRLPLTIGRIQRGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNgeSISPNGRPVVLSSGDVITLGS 95
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
641-956 |
1.37e-07 |
|
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: 56.29 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 641 LIYLLEHYKKLMSQAQelqikfnssQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKA--ALEEYITQ 718
Cdd:pfam17380 274 LLHIVQHQKAVSERQQ---------QEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAiyAEQERMAM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 719 ERNRAKETL-EEERKR----------------MQELESLLA--QQKKALAKSITQEKNRVKEALEEEQTRVQELEERLAR 779
Cdd:pfam17380 345 ERERELERIrQEERKRelerirqeeiameisrMRELERLQMerQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQ 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 780 QKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEAmekekkkvqDLENRLTKQKEELELK 859
Cdd:pfam17380 425 IRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLEL---------EKEKRDRKRAEEQRRK 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 860 EQKEDVLNNKLsdalAMVEETQKTKATE-SLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRH 938
Cdd:pfam17380 496 ILEKELEERKQ----AMIEEERKRKLLEkEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAM 571
|
330
....*....|....*....
gi 767902113 939 GFEEEIM-EYKEQIKQHAQ 956
Cdd:pfam17380 572 EREREMMrQIVESEKARAE 590
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
673-983 |
1.78e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 673 LQEKLREHLAEKEKLNEERLE-------QEEKLKAKIRQLTEEKAALEEYITQERNRAkETLEEERKRMQELESLLAQQK 745
Cdd:TIGR02169 189 LDLIIDEKRQQLERLRREREKaeryqalLKEKREYEGYELLKEKEALERQKEAIERQL-ASLEEELEKLTEEISELEKRL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 746 KALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISES--N 823
Cdd:TIGR02169 268 EEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREieE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 824 IAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLA 903
Cdd:TIGR02169 348 ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 904 ELETTKTKMIMVEERLilqqkmvKALQDEQESQrhgfEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLK 983
Cdd:TIGR02169 428 AIAGIEAKINELEEEK-------EDKALEIKKQ----EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
|
| FHA_AGGF1 |
cd22686 |
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ... |
11-86 |
1.80e-07 |
|
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: 51.51 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 11 FFVLNKSTTIGRHENSDLVLQSPD--IDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQNVAVKLIP-----GDILR 83
Cdd:cd22686 21 FIVTATGATIGREKDHGHTIRIPElgVSKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPyplthGDELK 100
|
...
gi 767902113 84 FGS 86
Cdd:cd22686 101 IGE 103
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
682-1104 |
1.86e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 682 AEKEKLNEErLEQEEKLKAKIRQLTEEKAALEEYITQERNRAkETLEEERKRMQELE-SLLAQQKKALAKSITQEKNRVk 760
Cdd:TIGR02169 170 RKKEKALEE-LEEVEENIERLDLIIDEKRQQLERLRREREKA-ERYQALLKEKREYEgYELLKEKEALERQKEAIERQL- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 761 EALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRkakeamekekk 840
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKER----------- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 841 KVQDLENRLTKQKEELELKEQKEDVLNNKLsdalamvEETQKTKATESLKAESLALKLNETLAELETTKTKMimveerli 920
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREI-------EEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF-------- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 921 lqqkmvKALQDEQESQRhgfeEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERPQDPLva 1000
Cdd:TIGR02169 381 ------AETRDELKDYR----EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL-- 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1001 pmtESSAKDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLrgelnEKQKMELEQNVVLVQQQSKEL-SVL 1079
Cdd:TIGR02169 449 ---EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA-----EAQARASEERVRGGRAVEEVLkASI 520
|
410 420
....*....|....*....|....*
gi 767902113 1080 KEKMAQMSSLVEKKDRELKALEEAL 1104
Cdd:TIGR02169 521 QGVHGTVAQLGSVGERYATAIEVAA 545
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
297-983 |
4.22e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.64 E-value: 4.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 297 KEIQSLKSQISALQKGYsKVLCQTLSERNSEITSLKNEGENLKRDnaitsgmVSSLQKDILAKDEQVQQLKEEVSHLKSQ 376
Cdd:TIGR04523 40 KKLKTIKNELKNKEKEL-KNLDKNLNKDEEKINNSNNKIKILEQQ-------IKDLNDKLKKNKDKINKLNSDLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 377 NKDKDHQLEALGSRCSVLKEELKQEDAH-------------------------RELREAQEKELKLCKTQIQDMEKEMKK 431
Cdd:TIGR04523 112 IKNDKEQKNKLEVELNKLEKQKKENKKNidkflteikkkekeleklnnkyndlKKQKEELENELNLLEKEKLNIQKNIDK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 432 LRAELRKSCTEQSVIsrtlrekskveEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKatygrakpfr 511
Cdd:TIGR04523 192 IKNKLLKLELLLSNL-----------KKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN---------- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 512 dkpvTDQQLIEKITQVTEDNINFQQKkwtlQKETQLSNSKQEETTENIEKLRTSLDscqacmkisccshDLKKEVDllqh 591
Cdd:TIGR04523 251 ----TQTQLNQLKDEQNKIKKQLSEK----QKELEQNNKKIKELEKQLNQLKSEIS-------------DLNNQKE---- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 592 lqvsppvsglqkvvLDVLRHALSWLEEVEQLLRDLGILPSSPNKGFSlyliyllehykKLMSQAQELQIKFNSSQETQQS 671
Cdd:TIGR04523 306 --------------QDWNKELKSELKNQEKKLEEIQNQISQNNKIIS-----------QLNEQISQLKKELTNSESENSE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 672 llqekLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKEtLEEERKRMQELESLLAQQKKALAKS 751
Cdd:TIGR04523 361 -----KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ-KDEQIKKLQQEKELLEKEIERLKET 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 752 ITQEKNRVKEaLEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNiayekrka 831
Cdd:TIGR04523 435 IIKNNSEIKD-LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK-------- 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 832 keamekekkkvQDLENRLTKQKEELELKEQKEDVLNNklsdalamvEETQKTKATESLKAESLALKLNETLAELETTKTK 911
Cdd:TIGR04523 506 -----------KELEEKVKDLTKKISSLKEKIEKLES---------EKKEKESKISDLEDELNKDDFELKKENLEKEIDE 565
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902113 912 MIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLK 983
Cdd:TIGR04523 566 KNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIK 637
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
537-1129 |
4.22e-07 |
|
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: 54.97 E-value: 4.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 537 KKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISccsHDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRHALSWL 616
Cdd:TIGR00618 220 RKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQ---QLLKQLRARIEELRAQEAVLEETQERINRARKAAPLA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 617 EEVE-------QLLRDLGILPSSPNKgfslyLIYLLEHYKKLMSQAQELQIKFNSSQETQQsllQEKLREHLAEKEKLNE 689
Cdd:TIGR00618 297 AHIKavtqieqQAQRIHTELQSKMRS-----RAKLLMKRAAHVKQQSSIEEQRRLLQTLHS---QEIHIRDAHEVATSIR 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 690 ERLEQEEKLKAKIRQLTEEKAALEEyitQERNRAKETLEEERKRMQELESLLA----QQKKALAKS---ITQEKNRVKEA 762
Cdd:TIGR00618 369 EISCQQHTLTQHIHTLQQQKTTLTQ---KLQSLCKELDILQREQATIDTRTSAfrdlQGQLAHAKKqqeLQQRYAELCAA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 763 LEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRK----VQDLENHLTQQKEISESNIAYE-KRKAKEAMEK 837
Cdd:TIGR00618 446 AITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKkavvLARLLELQEEPCPLCGSCIHPNpARQDIDNPGP 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 838 EKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEE 917
Cdd:TIGR00618 526 LTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSE 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 918 ----RLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKI-EGEIATLKDNDPAPKEE 992
Cdd:TIGR00618 606 aedmLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIrVLPKELLASRQLALQKM 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 993 RPQDPLVAPMTESSA-KDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQ 1071
Cdd:TIGR00618 686 QSEKEQLTYWKEMLAqCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFN 765
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767902113 1072 QSKELSVLKEKMAQMSSLV----------EKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQT 1129
Cdd:TIGR00618 766 NNEEVTAALQTGAELSHLAaeiqffnrlrEEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQF 833
|
|
| FHA_SNIP1_DDL-like |
cd22676 |
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA ... |
20-85 |
4.54e-07 |
|
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: 49.99 E-value: 4.54e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767902113 20 IGRHE-NSDLVLQSPDIDNHHALIEY-----------NEAECSFVLqDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFG 85
Cdd:cd22676 25 IGRDRrVADIPLDHPSCSKQHAVIQFrevekrnegdvIENIRPYII-DLGSTNGTFLNGEKIEpRRYYELREKDVLKFG 102
|
|
| VI_FHA |
TIGR03354 |
type VI secretion system FHA domain protein; Members of this protein family are FHA ... |
19-185 |
5.04e-07 |
|
type VI secretion system FHA domain protein; Members of this protein family are FHA (forkhead-associated) domain-containing proteins that are part of type VI secretion loci in a considerable number of bacteria, most of which are known pathogens. Species include Pseudomonas aeruginosa PAO1, Aeromonas hydrophila, Yersinia pestis, Burkholderia mallei, etc. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274537 [Multi-domain] Cd Length: 396 Bit Score: 53.91 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 19 TIGRHENSDLVLQSPD--IDNHHALIEYNEAecSFVLQDFnSRNGTFVNECH---IQNVAVKLIPGDILRFGSagltYEL 93
Cdd:TIGR03354 27 TIGRSEDCDWVLPDPErhVSGRHARIRYRDG--AYLLTDL-STNGVFLNGSGsplGRGNPVRLEQGDRLRLGD----YEI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 94 VIENPPPVSFPWMRGPAPWPGPQPPRATQQPNQAPPPSHIPF----HQGVQPAPMQRSWSQAFPRPTVVLPAsHRRPVSA 169
Cdd:TIGR03354 100 RVSLGDPLVSRQASESRADTSLPTAGGPPTPDPAPLAQLDPLkaldQEPLSAADLDDLSAPLFPPLDARLPA-FAAPIDA 178
|
170
....*....|....*.
gi 767902113 170 NKEMFSFVVDDARKPP 185
Cdd:TIGR03354 179 EPTMVPPFVPLPAPEP 194
|
|
| FHA_GarA_OdhI-like |
cd22684 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium ... |
18-91 |
8.27e-07 |
|
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: 48.53 E-value: 8.27e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767902113 18 TTIGRHENSDLVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHIQnvAVKLIPGDILRFGSAGLTY 91
Cdd:cd22684 23 TTAGRHPESDIFLDDVTVSRRHAEFRRAEGG--FVVRDVGSLNGTYVNRERID--SAVLRNGDEVQIGKFRLVF 92
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
394-786 |
8.94e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 8.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 394 LKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKsCTEQSVISRTLREKSKVEEKLQEDSRRkllqLQE 473
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK-LEKLLQLLPLYQELEALEAELAELPER----LEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 474 MGNRESvikiNLERAVGQLEHFRSQVIKATYGRAKPFRDKPVTDQQLIEKITQVTEDninFQQKKWTLQKETQLSNSKQE 553
Cdd:COG4717 151 LEERLE----ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE---LQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 554 ETTENIEKLRTSLDSCQACMKISCCSHDLK-------KEVDLLQHLQVSPPVSGLQKVVLDVLRHALSWL---------- 616
Cdd:COG4717 224 ELEEELEQLENELEAAALEERLKEARLLLLiaaallaLLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLarekaslgke 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 617 ---------------EEVEQLLRDLGiLPSSPNKGFSLYLIYLLEHYKKLMSQAQELQikfnssQETQQSLLQEKLREHL 681
Cdd:COG4717 304 aeelqalpaleeleeEELEELLAALG-LPPDLSPEELLELLDRIEELQELLREAEELE------EELQLEELEQEIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 682 AEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRA--------KETLEEERKRMQELESLLAQQKKALAKSIT 753
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELeellealdEEELEEELEELEEELEELEEELEELREELA 456
|
410 420 430
....*....|....*....|....*....|...
gi 767902113 754 QEKNRVKEAleEEQTRVQELEERLARQKEVLES 786
Cdd:COG4717 457 ELEAELEQL--EEDGELAELLQELEELKAELRE 487
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
239-822 |
1.53e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 53.30 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 239 RLSDYEIESKYKDVIIANLQNEVAELSQKVSETTtsRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQ---KGYSK 315
Cdd:pfam12128 259 RLSHLHFGYKSDETLIASRQEERQETSAELNQLL--RTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEdqhGAFLD 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 316 VLCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQV-QQLKEEVSHLKS----QNKDKDHQLEA---- 386
Cdd:pfam12128 337 ADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIkEQNNRDIAGIKDklakIREARDRQLAVaedd 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 387 LGSRCSVLKEELKQedAHRELREAQEK------ELKL----------CKTQIQDMEKEMKKLRAELRKSCTEQSVISRTL 450
Cdd:pfam12128 417 LQALESELREQLEA--GKLEFNEEEYRlksrlgELKLrlnqatatpeLLLQLENFDERIERAREEQEAANAEVERLQSEL 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 451 REKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHF-RSQVIKATYGRAKpfrdkpVTDQQLI-------E 522
Cdd:pfam12128 495 RQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFlRKEAPDWEQSIGK------VISPELLhrtdldpE 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 523 KITQVTEDNINFQQKKWTLQK-ETQLSNSKQEETTENIEKLRTSLDSCQACMK-ISCCSHDLKKEVDLLQhLQVSPPVSG 600
Cdd:pfam12128 569 VWDGSVGGELNLYGVKLDLKRiDVPEWAASEEELRERLDKAEEALQSAREKQAaAEEQLVQANGELEKAS-REETFARTA 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 601 LQKVVLDVLRhalsWLEEVEQLLRDLgilpsspNKGfslyliyLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREH 680
Cdd:pfam12128 648 LKNARLDLRR----LFDEKQSEKDKK-------NKA-------LAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQK 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 681 LAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEyitqERNRAKETLEEERKRmqELESL---------LAQQKKALAKS 751
Cdd:pfam12128 710 REARTEKQAYWQVVEGALDAQLALLKAAIAARRS----GAKAELKALETWYKR--DLASLgvdpdviakLKREIRTLERK 783
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767902113 752 ITQEKNRVKEALEEE---QTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHL----TQQKEISES 822
Cdd:pfam12128 784 IERIAVRRQEVLRYFdwyQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERkaseKQQVRLSEN 861
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
235-811 |
1.74e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 235 KEVSRLSDYEIESKykdviiaNLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQKGYS 314
Cdd:PRK03918 152 RQILGLDDYENAYK-------NLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 315 KVlcqtlSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDhQLEALGSRCSVL 394
Cdd:PRK03918 225 KL-----EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 395 KEELKQ-EDAHRELreaqEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQ--EDSRRKLLQL 471
Cdd:PRK03918 299 SEFYEEyLDELREI----EKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHElyEEAKAKKEEL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 472 QEMGNRESVIKI----------------------NLERAVGQLEHFRSQVIKATYGRAKPFRDKPVTDQQLiekitqvTE 529
Cdd:PRK03918 375 ERLKKRLTGLTPeklekeleelekakeeieeeisKITARIGELKKEIKELKKAIEELKKAKGKCPVCGREL-------TE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 530 DNINFQQKKWTLqkETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHLQvsppvSGLQKVVLDVL 609
Cdd:PRK03918 448 EHRKELLEEYTA--ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELE-----EKLKKYNLEEL 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 610 RHALSWLEEVEQLLRDLgilpsspnKGFSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSLLQ----------EKLRE 679
Cdd:PRK03918 521 EKKAEEYEKLKEKLIKL--------KGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKeleelgfesvEELEE 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 680 HLAEKEKLNEERLE---QEEKLKAKIRQLTEEKAALEEyITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEK 756
Cdd:PRK03918 593 RLKELEPFYNEYLElkdAEKELEREEKELKKLEEELDK-AFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLEL 671
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 767902113 757 NRVKEALEEEQTRVQELEERLARQKEVLESSIAhEKRKAKEALESEKRKVQDLEN 811
Cdd:PRK03918 672 SRELAGLRAELEELEKRREEIKKTLEKLKEELE-EREKAKKELEKLEKALERVEE 725
|
|
| FHA_EspA-like |
cd22698 |
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ... |
15-92 |
1.82e-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: 47.41 E-value: 1.82e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767902113 15 NKSTTIGRHENSDLVLQSPDIDNHHALIEYNEAECsfVLQDFNSRNGTFVNECHIQNVAVKliPGDILRFGSAGLTYE 92
Cdd:cd22698 20 QDEFTIGRSSNNDIRLNDHSVSRHHARIVRQGDKC--NLTDLGSTNGTFLNGIRVGTHELK--HGDRIQLGETIFRFI 93
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
653-829 |
1.86e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 653 SQAQELQIKFNSSQEtQQSLLQEKLREHLAEKEKLNEERLEQEEKLKA---KIRQLTEEKAALEEYI---TQERNRAKET 726
Cdd:COG4942 20 DAAAEAEAELEQLQQ-EIAELEKELAALKKEEKALLKQLAALERRIAAlarRIRALEQELAALEAELaelEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 727 LEEERKRMQE-------------LESLLAQQ-------KKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLES 786
Cdd:COG4942 99 LEAQKEELAEllralyrlgrqppLALLLSPEdfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767902113 787 SIAhEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKR 829
Cdd:COG4942 179 LLA-ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
666-824 |
1.92e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 666 QETQQSLLQEKLREHLAEKEKLNEERleqeEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQ----ELESLL 741
Cdd:COG4913 286 AQRRLELLEAELEELRAELARLEAEL----ERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLEreleERERRR 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 742 AQQKKALAkSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSiAHEKRKAKEALESEKRKVQDLENHLTQQKeise 821
Cdd:COG4913 362 ARLEALLA-ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA-LAEAEAALRDLRRELRELEAEIASLERRK---- 435
|
...
gi 767902113 822 SNI 824
Cdd:COG4913 436 SNI 438
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
218-789 |
2.11e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 218 EEDLAQQDKDEIILLLGKEVSRLSDYEIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKEISQKcqvLDEDIDAKQK 297
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE---LEERLEELEE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 298 EIQSLKSQISALQkgyskvlcQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQN 377
Cdd:COG1196 324 ELAELEEELEELE--------EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 378 KDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKlckTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVE 457
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELE---EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 458 EKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATYGR-----AKPFRDKPVTDQQLIEKITQVTEDNI 532
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlagavAVLIGVEAAYEAALEAALAAALQNIV 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 533 NFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRHA 612
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARL 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 613 LSWLEEVEQLLRDL--------GILPSSPNKGFSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEK 684
Cdd:COG1196 633 EAALRRAVTLAGRLrevtlegeGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEA 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 685 EKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQE--------------RNRAKETLEEERKRMQELES--LLAQqkkal 748
Cdd:COG1196 713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELleeealeelpeppdLEELERELERLEREIEALGPvnLLAI----- 787
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 767902113 749 aksitqeknrvkEALEEEQTRVQELEErlarQKEVLESSIA 789
Cdd:COG1196 788 ------------EEYEELEERYDFLSE----QREDLEEARE 812
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
261-973 |
2.30e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 52.53 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 261 VAELSQKVSETTTSRQNEKEIS---------QKCQVLDEDIDAKQKEIQSLKS---QISALQKGYSKVLCQTLSERNSEI 328
Cdd:pfam12128 203 VAILEDDGVVPPKSRLNRQQVEhwirdiqaiAGIMKIRPEFTKLQQEFNTLESaelRLSHLHFGYKSDETLIASRQEERQ 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 329 TSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKdkdhqlEALGSRCSVLKEELKQEDAHRELR 408
Cdd:pfam12128 283 ETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHG------AFLDADIETAAADQEQLPSWQSEL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 409 EAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERA 488
Cdd:pfam12128 357 ENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFN 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 489 VGQLEhfrsqvIKATYGRAKPFRDKPVTDQQLIEKITqvtedniNFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDs 568
Cdd:pfam12128 437 EEEYR------LKSRLGELKLRLNQATATPELLLQLE-------NFDERIERAREEQEAANAEVERLQSELRQARKRRD- 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 569 cQACMKISCCSHDLKKEVDLLQ--HLQVSPPVSGLqkvvLDVLR-HALSWLEEV------EQLLR---DLGILPSSPNKG 636
Cdd:pfam12128 503 -QASEALRQASRRLEERQSALDelELQLFPQAGTL----LHFLRkEAPDWEQSIgkvispELLHRtdlDPEVWDGSVGGE 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 637 FSLYLIyllehykklmsqaqelqikfnssqetqqsllqeklrehlaekeKLNEERLEqeeklkakirqlTEEKAALEEYI 716
Cdd:pfam12128 578 LNLYGV-------------------------------------------KLDLKRID------------VPEWAASEEEL 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 717 TQERNRAKETLEEERKRMQELESLLAQQKKALAKSitqeknrvKEALEEEQTRVQELEERLARQKEVLESsiahEKRKAK 796
Cdd:pfam12128 603 RERLDKAEEALQSAREKQAAAEEQLVQANGELEKA--------SREETFARTALKNARLDLRRLFDEKQS----EKDKKN 670
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 797 EALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEamekekkkvQDLENRLTKQKEELelkeqkedVLNNKLSDALAM 876
Cdd:pfam12128 671 KALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKE---------QKREARTEKQAYWQ--------VVEGALDAQLAL 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 877 VEETqKTKATESLKAESLALK--LNETLAELETTKTKMIMVE-ERLILQQKMVKALQDEQES------QRHGFEEEIMEY 947
Cdd:pfam12128 734 LKAA-IAARRSGAKAELKALEtwYKRDLASLGVDPDVIAKLKrEIRTLERKIERIAVRRQEVlryfdwYQETWLQRRPRL 812
|
730 740
....*....|....*....|....*.
gi 767902113 948 KEQIKQHAQTIVSLEEKLQKVTQHHK 973
Cdd:pfam12128 813 ATQLSNIERAISELQQQLARLIADTK 838
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
254-818 |
2.31e-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: 52.66 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 254 IANLQNEVAELSQKVSETTTSRQNEK--EISQKCQVLDEDIDAKQKEIQSLKSQISALQKGYSKVLCQTLS---ERNSEI 328
Cdd:TIGR00618 269 IEELRAQEAVLEETQERINRARKAAPlaAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSieeQRRLLQ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 329 TSLKNEGENLKRDNAITSgmvsslqkdilaKDEQVQQLKEEVSHLKSQNKDKDH---QLEALGSRCSVLKEELKQEDAHR 405
Cdd:TIGR00618 349 TLHSQEIHIRDAHEVATS------------IREISCQQHTLTQHIHTLQQQKTTltqKLQSLCKELDILQREQATIDTRT 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 406 ELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKS------------------KVEEKLQEDSRRK 467
Cdd:TIGR00618 417 SAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAqslkereqqlqtkeqihlQETRKKAVVLARL 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 468 L-LQLQEMGNRESVIKINLER-AVGQLEHFRSQVIKATYGRAKPFRDKPVTDQQLIEKITQVTEDNINFQQKKWTLQKET 545
Cdd:TIGR00618 497 LeLQEEPCPLCGSCIHPNPARqDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILT 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 546 QLSNskqeETTENIEKLRtsldscqacmkisccshdlkKEVDLLQHLqvsppvsglqkvVLDVLRHALSWLEEVEQLLRD 625
Cdd:TIGR00618 577 QCDN----RSKEDIPNLQ--------------------NITVRLQDL------------TEKLSEAEDMLACEQHALLRK 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 626 LGILpsspnkgfslylIYLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLA----EKEKLNEERLEQEEKLKAK 701
Cdd:TIGR00618 621 LQPE------------QDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALsirvLPKELLASRQLALQKMQSE 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 702 IRQLTEEKAALEEYITQERNRaKETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELEERLAR-- 779
Cdd:TIGR00618 689 KEQLTYWKEMLAQCQTLLREL-ETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNnn 767
|
570 580 590
....*....|....*....|....*....|....*....
gi 767902113 780 QKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKE 818
Cdd:TIGR00618 768 EEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEA 806
|
|
| FHA_NBN |
cd22667 |
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ... |
11-91 |
3.83e-06 |
|
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: 46.94 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 11 FFVLNKSTTIGRHENSDLVLQSPDIDNHHALI--EYNEAECSF-------VLQDFnSRNGTFVNECHIQNVA-VKLIPGD 80
Cdd:cd22667 15 YLLPGGEYTVGRKDCDIIIVDDSSISRKHATLtvLHPEANLSDpdtrpelTLKDL-SKYGTFVNGEKLKGGSeVTLKDGD 93
|
90
....*....|.
gi 767902113 81 ILRFGSAGLTY 91
Cdd:cd22667 94 VITFGVLGSKF 104
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
254-816 |
4.56e-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: 51.56 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 254 IANLQNEVAELSQKVSETTTSRQNEKEisqKCQVLDEDIDAKQKEIQSLKSQISALQKGYSKVlcQTLSERN----SEIT 329
Cdd:TIGR04523 147 IKKKEKELEKLNNKYNDLKKQKEELEN---ELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNL--KKKIQKNksleSQIS 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 330 SLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELRE 409
Cdd:TIGR04523 222 ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLN 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 410 AQEKE--LKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLER 487
Cdd:TIGR04523 302 NQKEQdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQS 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 488 AVGQLEHFRSQVikatygrakpfrdkpvtdQQLIEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLD 567
Cdd:TIGR04523 382 YKQEIKNLESQI------------------NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIK 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 568 scqacmkisccshDLKKEVDLLqhlqvsppvsglqkvvldvlrhalswleevEQLLRDLGILPSSPNKGFSLYLIylleH 647
Cdd:TIGR04523 444 -------------DLTNQDSVK------------------------------ELIIKNLDNTRESLETQLKVLSR----S 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 648 YKKLMSQAQELQIKFNSSQETQQSLLQEK--LREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALE-EYITQERNRAK 724
Cdd:TIGR04523 477 INKIKQNLEQKQKELKSKEKELKKLNEEKkeLEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEdELNKDDFELKK 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 725 ETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELEErlarqKEVLESSIAHEKRKAK---EALES 801
Cdd:TIGR04523 557 ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE-----KEKKISSLEKELEKAKkenEKLSS 631
|
570
....*....|....*
gi 767902113 802 EKRKVQDLENHLTQQ 816
Cdd:TIGR04523 632 IIKNIKSKKNKLKQE 646
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
684-1379 |
5.10e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 684 KEKLNEERLEQ-EEKLKAKIRQLTEEKAALEEYITQERNrAKETLEEERKRMQELESLLaqqkkalaKSITQEKNRVKEA 762
Cdd:PRK03918 152 RQILGLDDYENaYKNLGEVIKEIKRRIERLEKFIKRTEN-IEELIKEKEKELEEVLREI--------NEISSELPELREE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 763 LEEEQTRVQELEER------LARQKEVLESSIAHEKRKAKE---ALESEKRKVQDLENHLTQQKEISESNIAYEKrkAKE 833
Cdd:PRK03918 223 LEKLEKEVKELEELkeeieeLEKELESLEGSKRKLEEKIREleeRIEELKKEIEELEEKVKELKELKEKAEEYIK--LSE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 834 AMEKEKKKVQDLENRLTkqkeelelkeqkedvlnnKLSDALAMVEETQKtkateslKAESLALKLNETLAELETTKTKMI 913
Cdd:PRK03918 301 FYEEYLDELREIEKRLS------------------RLEEEINGIEERIK-------ELEEKEERLEELKKKLKELEKRLE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 914 MVEERLILQQkMVKALQDEQESQRHGFE-EEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEE 992
Cdd:PRK03918 356 ELEERHELYE-EAKAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 993 RPQDPLV-APMTESSAKDMAYEHLIDdllaaqkeilsqqevIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQnvvlvqq 1071
Cdd:PRK03918 435 KGKCPVCgRELTEEHRKELLEEYTAE---------------LKRIEKELKEIEEKERKLRKELRELEKVLKKE------- 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1072 qsKELSVLKEKMAQMSSLVEK-KDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQtcdtsvqiepvhteafsssqeq 1150
Cdd:PRK03918 493 --SELIKLKELAEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKEL---------------------- 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1151 qsfsdlgvrckgsrheEVIQRQKKALSELRARIKELEKARSPDHKDHQNESFLDLKNLRmennvqkilldakpdlptlSR 1230
Cdd:PRK03918 549 ----------------EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELE-------------------ER 593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1231 IEILAPQNGLCNARFGSAMEKSGKMDVAEALELS-EKLYLDMSKTLGSLMNIKNMSGHVSMKYLSRQEREKVNQLRQ--R 1307
Cdd:PRK03918 594 LKELEPFYNEYLELKDAEKELEREEKELKKLEEElDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLElsR 673
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767902113 1308 DLDLVFDKITQLKNQLGRKEELLRGYEKDVEQLRRSKVSIEMYQSQVAKLEDDIYKEAEEKALLKE-ALERME 1379
Cdd:PRK03918 674 ELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKErALSKVG 746
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
225-827 |
5.51e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 51.23 E-value: 5.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 225 DKDEIILLLGKEVSRLSDYEIESKykDVIIANLQNEVAELSQKVSEtttsrqnekeisqkcqvLDEDIdakqKEIQSLKS 304
Cdd:COG5022 843 KAEVLIQKFGRSLKAKKRFSLLKK--ETIYLQSAQRVELAERQLQE-----------------LKIDV----KSISSLKL 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 305 QISALQKGYSKVLCQTLSERNSEITSLKNEGENLKRdnAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQL 384
Cdd:COG5022 900 VNLELESEIIELKKSLSSDLIENLEFKTELIARLKK--LLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLL 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 385 EALGSrcsvLKEELKQEdahRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDS 464
Cdd:COG5022 978 KKSTI----LVREGNKA---NSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILKPLQK 1050
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 465 RRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATYGRAK--PFRDKPVTDQQLIEKITQVteDNINFQQKKWTLQ 542
Cdd:COG5022 1051 LKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKtiNVKDLEVTNRNLVKPANVL--QFIVAQMIKLNLL 1128
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 543 KETQLSNSKQEETTENIEKLRTSLDSCQACMkisccshdlkKEVDLLQHLQVSPPVSGLQKV------VLDVLRHALSwl 616
Cdd:COG5022 1129 QEISKFLSQLVNTLEPVFQKLSVLQLELDGL----------FWEANLEALPSPPPFAALSEKrlyqsaLYDEKSKLSS-- 1196
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 617 EEVEQLLRDLGILPS-----SPNKGFSLYLI---YLLEHYKKLMSQAQELQIKFnssqETQQSLLQEKLREHLAEKEKLN 688
Cdd:COG5022 1197 SEVNDLKNELIALFSkifsgWPRGDKLKKLIsegWVPTEYSTSLKGFNNLNKKF----DTPASMSNEKLLSLLNSIDNLL 1272
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 689 EERLEQEEKLKAKIRQLTEEKAAL--EEYITQERNRAKETLEEERKRMQELESllaqqkkalaKSITQEKNRVKEALEee 766
Cdd:COG5022 1273 SSYKLEEEVLPATINSLLQYINVGlfNALRTKASSLRWKSATEVNYNSEELDD----------WCREFEISDVDEELE-- 1340
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902113 767 qtrvqELEERlARQKEVLESSIAH--EKRKAKEALES-------EKRKVQDLENHLTQQ--KEISESNIAYE 827
Cdd:COG5022 1341 -----ELIQA-VKVLQLLKDDLNKldELLDACYSLNPaeiqnlkSRYDPADKENNLPKEilKKIEALLIKQE 1406
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
679-1409 |
6.19e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 6.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 679 EHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNR 758
Cdd:PTZ00121 1080 DFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARK 1159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 759 VKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEAMEKE 838
Cdd:PTZ00121 1160 AEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDA 1239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 839 KKKVQDLENRLTKQKEELELKEQKEdvlnnklsdalaMVEETQKTKATESLKAEslalklnetlaELETTKTKMIMVEER 918
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMAH------------FARRQAAIKAEEARKAD-----------ELKKAEEKKKADEAK 1296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 919 LILQQKMVKALQDEQESQRHGfeEEIMEYKEQIKQHAqtivsleEKLQKVTQHHKKiegeiatlKDNDPAPKEERPQDPL 998
Cdd:PTZ00121 1297 KAEEKKKADEAKKKAEEAKKA--DEAKKKAEEAKKKA-------DAAKKKAEEAKK--------AAEAAKAEAEAAADEA 1359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 999 VAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEViMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQQSKELSV 1078
Cdd:PTZ00121 1360 EAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA-DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK 1438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1079 lKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQTCDTSVQIEPVHTEAFSSSQEQQSFSDLGV 1158
Cdd:PTZ00121 1439 -KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKK 1517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1159 RCKGSRHEEVIQRQKKALSELRARIKELEKArspdhkdhqnESFLDLKNLRMENNVQKIlldakpdlptlsrieilapqn 1238
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADEAKKAEEKKKA----------DELKKAEELKKAEEKKKA--------------------- 1566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1239 glcnarfgsAMEKSGKMDVAEALELSEKLYLDMSKTLGSLMNIKNMSGHVSMKYLSRQEREKVNQLRQRDLDLVFDKITQ 1318
Cdd:PTZ00121 1567 ---------EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ 1637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1319 LKNQlgRKEEllrgyEKDVEQLRRSKVSIEMYQSQVAKLEDDIYKEAEEKALLKEALERMEHQLCQEKRINRAIRQqkMR 1398
Cdd:PTZ00121 1638 LKKK--EAEE-----KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE--LK 1708
|
730
....*....|.
gi 767902113 1399 KLRLRELRGAQ 1409
Cdd:PTZ00121 1709 KKEAEEKKKAE 1719
|
|
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
13-85 |
6.20e-06 |
|
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: 46.88 E-value: 6.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 13 VLNKSTTIGRHEN------SDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQ-----NVAVKLIPGDI 81
Cdd:cd22679 21 VLDEPVKIGRSVArarpaaNNAIFDCKVLSRNHALLWYDDG--KFYLQDTKSSNGTFVNNQRLSkgseeSEPRELHSGDI 98
|
....
gi 767902113 82 LRFG 85
Cdd:cd22679 99 VQFG 102
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
643-775 |
6.24e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.98 E-value: 6.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 643 YLLEHYKKLMSQAQElqiKFN---SSQETQQSLLQEKLREH---LAEKEKLNEERLEQEEKLKAKIRQLteeKAALEEYI 716
Cdd:PRK00409 502 NIIEEAKKLIGEDKE---KLNeliASLEELERELEQKAEEAealLKEAEKLKEELEEKKEKLQEEEDKL---LEEAEKEA 575
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 767902113 717 TQERNRAKETLEEERKRMQELESLLAQQKKalAKSITQEKNRVKEALEEEQTRVQELEE 775
Cdd:PRK00409 576 QQAIKEAKKEADEIIKELRQLQKGGYASVK--AHELIEARKRLNKANEKKEKKKKKQKE 632
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
213-932 |
6.26e-06 |
|
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: 51.13 E-value: 6.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 213 AEIYVEEDLAQQDKDEIILLLGKEVSRLSDYEIESKyKDVIIANLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDI 292
Cdd:pfam02463 353 AEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSS-AAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEI 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 293 DAKQKEIQSLKSQISALQKGYSKVLCQTLSERNSEitsLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSH 372
Cdd:pfam02463 432 LEEEEESIELKQGKLTEEKEELEKQELKLLKDELE---LKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSG 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 373 LKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEmkKLRAELRKSCTEQSVISRTLRE 452
Cdd:pfam02463 509 LKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQ--KLVRALTELPLGARKLRLLIPK 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 453 KSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATYGRAKPFRDKPVTDQQLIEKITQVTEDNI 532
Cdd:pfam02463 587 LKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKA 666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 533 NFQQKKWTLqKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQhLQVSPPVSGLQKVVLDVLRHA 612
Cdd:pfam02463 667 SLSELTKEL-LEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELL-ADRVQEAQDKINEELKLLKQK 744
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 613 LSWLEEVEQLLRDLGILPSSPNKGFSLYLIYLLEHYKKLMSQAQELQIKfnssqetQQSLLQEKLREHLAEKEKLNEERL 692
Cdd:pfam02463 745 IDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKE-------EKLKAQEEELRALEEELKEEAELL 817
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 693 EQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQE 772
Cdd:pfam02463 818 EEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKE 897
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 773 LEErlarQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQ 852
Cdd:pfam02463 898 EKK----ELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELG 973
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 853 KEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDE 932
Cdd:pfam02463 974 KVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDP 1053
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
425-765 |
7.01e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 50.70 E-value: 7.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 425 MEKEMKKLRAELRKSctEQSVISRTLREKSKVE-----EKLQEDSRRKLLQLQemgnresvikINLERAVGQLEHFRSqv 499
Cdd:PRK05771 2 APVRMKKVLIVTLKS--YKDEVLEALHELGVVHiedlkEELSNERLRKLRSLL----------TKLSEALDKLRSYLP-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 500 ikatYGRAKPFRDKPVTDQQLiEKITQVTEDNINfqqkkwTLQKETqlsnskqEETTENIEKLRTSLDSCQAcmkisccs 579
Cdd:PRK05771 68 ----KLNPLREEKKKVSVKSL-EELIKDVEEELE------KIEKEI-------KELEEEISELENEIKELEQ-------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 580 hdLKKEVDLLQHLqvSPPVSGLQ-----KVVLDVLRHALswLEEVEQLLRDLGILPSSPNKGFSLY-LIYLLEHYKKLMS 653
Cdd:PRK05771 122 --EIERLEPWGNF--DLDLSLLLgfkyvSVFVGTVPEDK--LEELKLESDVENVEYISTDKGYVYVvVVVLKELSDEVEE 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 654 QAQELQIKFNSSQEtqQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAK---ETLEEE 730
Cdd:PRK05771 196 ELKKLGFERLELEE--EGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLEIELERAEalsKFLKTD 273
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 767902113 731 R----------KRMQELESLLaqqKKALAKSITQEKNRVKEALEE 765
Cdd:PRK05771 274 KtfaiegwvpeDRVKKLKELI---DKATGGSAYVEFVEPDEEEEE 315
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
361-983 |
9.54e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 9.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 361 EQVQQLKEEVSHLKSQ---NKDKDHQLEalgsrcsvLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELR 437
Cdd:COG1196 213 ERYRELKEELKELEAElllLKLRELEAE--------LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 438 KscteqsvISRTLREKSKVEEKLQEDSRRKLLQLQEMGNResvikinLERAVGQLEHFRSQVIKATygrakpfrdkpvtd 517
Cdd:COG1196 285 E-------AQAEEYELLAELARLEQDIARLEERRRELEER-------LEELEEELAELEEELEELE-------------- 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 518 QQLIEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTsldscqacmkisccshDLKKEVDLLQHLQVspp 597
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE----------------LAEELLEALRAAAE--- 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 598 vsgLQKVVLDVLRHALSWLEEVEQLLRDLgilpsspnkgfslyliyllehykklmsQAQELQIKFNSSQETQQSLLQEKL 677
Cdd:COG1196 398 ---LAAQLEELEEAEEALLERLERLEEEL---------------------------EELEEALAELEEEEEEEEEALEEA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 678 REHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQE-- 755
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAva 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 756 -----KNRVKEALEEE-----QTRVQELEERLARQKEVLESS-------IAHEKRKAKEALESEKRK-VQDLENHLTQQK 817
Cdd:COG1196 528 vligvEAAYEAALEAAlaaalQNIVVEDDEVAAAAIEYLKAAkagratfLPLDKIRARAALAAALARgAIGAAVDLVASD 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 818 EISESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALK 897
Cdd:COG1196 608 LREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAER 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 898 LNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEG 977
Cdd:COG1196 688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER 767
|
....*.
gi 767902113 978 EIATLK 983
Cdd:COG1196 768 ELERLE 773
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
654-826 |
1.01e-05 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 49.69 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 654 QAQELQIKFnSSQETQQSllqEKLrehLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEeyitQERNRAKETLEEERKR 733
Cdd:PRK11637 138 EHTGLQLIL-SGEESQRG---ERI---LAYFGYLNQARQETIAELKQTREELAAQKAELE----EKQSQQKTLLYEQQAQ 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 734 MQELESLLAQQKKALAKsitqeknrVKEALEEEQTRVQELeerlaRQKEV-LESSIAHEKRKAKEALESEKRKVQDLENh 812
Cdd:PRK11637 207 QQKLEQARNERKKTLTG--------LESSLQKDQQQLSEL-----RANESrLRDSIARAEREAKARAEREAREAARVRD- 272
|
170
....*....|....
gi 767902113 813 ltQQKEISESNIAY 826
Cdd:PRK11637 273 --KQKQAKRKGSTY 284
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
12-85 |
1.54e-05 |
|
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: 45.02 E-value: 1.54e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767902113 12 FVLNKST-TIGRHENSDLVLQSPDIDNHHALIeYNEaECSFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRFG 85
Cdd:cd22680 16 FPFDFSSvSIGRDPENVIVIPDPFVSRNHARI-TVD-SNEIYIEDLGSTNGTFVNDFKRIKGPAKLHPNDIIKLG 88
|
|
| Yop-YscD_cpl |
pfam16697 |
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ... |
19-86 |
1.82e-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: 44.94 E-value: 1.82e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767902113 19 TIGRHENSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRFGS 86
Cdd:pfam16697 20 RIGSDPDCDIVLSDKEVSRVHLKLEVDDE--GWRLDDLGSGNGTLVNGQRVTELGIALRPGDRIELGQ 85
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
667-1127 |
2.03e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 667 ETQQSLLQEKLREHLAEKE------KLNEerLEQEEK-LKAKIRQLTEEKaaleEYITQERNRAKETLEEERKRMQELES 739
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEekdlheRLNG--LESELAeLDEEIERYEEQR----EQARETRDEADEVLEEHEERREELET 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 740 LLAQQKKALAKSITQEKNR--VKEALEEEQTRVQELEERL--ARQKEVLESSIAHEKRKAKEALESEKRKVQD-LENHLT 814
Cdd:PRK02224 256 LEAEIEDLRETIAETEREReeLAEEVRDLRERLEELEEERddLLAEAGLDDADAEAVEARREELEDRDEELRDrLEECRV 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 815 QQKEISESNIAYEKRKAKEAMEKEKKKVQ--DLENRLTKQKEELELKEQKEDVLNNKLSDALAMVE--ETQKTKATESLk 890
Cdd:PRK02224 336 AAQAHNEEAESLREDADDLEERAEELREEaaELESELEEAREAVEDRREEIEELEEEIEELRERFGdaPVDLGNAEDFL- 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 891 aESLALKLNETLAELETTKTKMIMVEERLilqqKMVKALQDE-------QESQRHGFEEEIMEYKEQIKQHAQTIVSLEE 963
Cdd:PRK02224 415 -EELREERDELREREAELEATLRTARERV----EEAEALLEAgkcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 964 KLQKVTQHH------KKIEGEIATLKDNdpapkeerpqdplvapmtessakdmayEHLIDDLLAAQKEIL-SQQEVIMKL 1036
Cdd:PRK02224 490 EVEEVEERLeraedlVEAEDRIERLEER---------------------------REDLEELIAERRETIeEKRERAEEL 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1037 RKDLTEAHSRMSDLRgELNEKQKMELEQNVVLVQQQSKELSVLKE------KMAQMSSLVEKKDRELKALEEALRASQEK 1110
Cdd:PRK02224 543 RERAAELEAEAEEKR-EAAAEAEEEAEEAREEVAELNSKLAELKEriesleRIRTLLAAIADAEDEIERLREKREALAEL 621
|
490
....*....|....*..
gi 767902113 1111 HRLQLNTEKEQKPRKKT 1127
Cdd:PRK02224 622 NDERRERLAEKRERKRE 638
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
15-87 |
2.07e-05 |
|
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: 45.49 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 15 NKSTTIGR--HENSD---LVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHIQ------NVAVKLIPGDILR 83
Cdd:cd22702 31 KQPCIIGSdpHQAISgisVVIPSPQVSELHARITCKNGA--FFLTDLGSEHGTWINDNEGRryrappNFPVRLHPSDVIE 108
|
....
gi 767902113 84 FGSA 87
Cdd:cd22702 109 FGSD 112
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
685-972 |
2.87e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 48.74 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 685 EKLNEERLEQEEKLKAKiRQLTEEKaaLEEYITQERNRAKETLEEERKRMQELESL--LAQQKKALAKSITQEKNRVKEA 762
Cdd:PLN02939 106 EAIAAIDNEQQTNSKDG-EQLSDFQ--LEDLVGMIQNAEKNILLLNQARLQALEDLekILTEKEALQGKINILEMRLSET 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 763 LE------EEQTRVQELEERLAR------QKEVLESSIAHEKRKAKEALESE----KRKVQDLENHLTQQKEISESNIAY 826
Cdd:PLN02939 183 DAriklaaQEKIHVEILEEQLEKlrnellIRGATEGLCVHSLSKELDVLKEEnmllKDDIQFLKAELIEVAETEERVFKL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 827 EKrkakeAMEKEKKKVQDLENRLTKQKEelelkeqkeDVLnnKLS----DAL-AMVEETQKTKATESLKAESLAL----- 896
Cdd:PLN02939 263 EK-----ERSLLDASLRELESKFIVAQE---------DVS--KLSplqyDCWwEKVENLQDLLDRATNQVEKAALvldqn 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 897 --------KLNETLAELETTKTKMIMVEerlILQQKMvKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKV 968
Cdd:PLN02939 327 qdlrdkvdKLEASLKEANVSKFSSYKVE---LLQQKL-KLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEESKKR 402
|
....
gi 767902113 969 TQHH 972
Cdd:PLN02939 403 SLEH 406
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
650-985 |
3.48e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 650 KLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEE 729
Cdd:PTZ00121 1487 EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKA 1566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 730 ERKRMQELESLLAQQKKALAKSItqEKNRVKEALEEEQTRVQELEERLARQKEvlESSIAHEKRKAKEalesEKRKVQDL 809
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAEEAKKA--EEARIEEVMKLYEEEKKMKAEEAKKAEE--AKIKAEELKKAEE----EKKKVEQL 1638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 810 ENHLTQQKEISES-NIAYEKRKAKEAMEKEKkkvQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATES 888
Cdd:PTZ00121 1639 KKKEAEEKKKAEElKKAEEENKIKAAEEAKK---AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEK 1715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 889 LKAESLALKLNETLAELETTKTKmimVEERlilQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKV 968
Cdd:PTZ00121 1716 KKAEELKKAEEENKIKAEEAKKE---AEED---KKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789
|
330
....*....|....*..
gi 767902113 969 TQHHKKIEGEIATLKDN 985
Cdd:PTZ00121 1790 EKRRMEVDKKIKDIFDN 1806
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
641-1109 |
3.66e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 641 LIYLLEHYKKLMSQAQELQIKFNSSQEtQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYiTQER 720
Cdd:TIGR04523 199 LELLLSNLKKKIQKNKSLESQISELKK-QNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK-QKEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 721 NRAKETLEEERKRMQELESLLAQQKKALAKSITQEknrVKEALEEEQTRVQELEERLARQKEVLEssiahekrKAKEALE 800
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKE---LKSELKNQEKKLEEIQNQISQNNKIIS--------QLNEQIS 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 801 SEKRKVQDLEN-HLTQQKEISESNIAYEKrkakeAMEKEKKKVQDLENrLTKQKEELELKEQKEDVLNNKLSDALAMVEE 879
Cdd:TIGR04523 346 QLKKELTNSESeNSEKQRELEEKQNEIEK-----LKKENQSYKQEIKN-LESQINDLESKIQNQEKLNQQKDEQIKKLQQ 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 880 TQKTKATESLKAESLALKLNETLAELETTKTKmimveerLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIV 959
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSV-------KELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELK 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 960 SLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERPQDPLVAPMTESSAKDMAYEHLIDDL----LAAQKEILSQQEVIMK 1035
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFelkkENLEKEIDEKNKEIEE 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1036 LRKDLTEAHSRMSDLRGELNEKQK------MELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKALEEALRASQE 1109
Cdd:TIGR04523 573 LKQTQKSLKKKQEEKQELIDQKEKekkdliKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKE 652
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
674-849 |
3.96e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 674 QEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYItqernrakETLEEERKRMQELESLLAQQKKALAksIT 753
Cdd:COG4717 62 QGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEEL--------EELEAELEELREELEKLEKLLQLLP--LY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 754 QEKNRVKEALEEEQTRVQELEERLARQKEVLEssiahEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKE 833
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEE-----ELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170
....*....|....*.
gi 767902113 834 AMEKEKKKVQDLENRL 849
Cdd:COG4717 207 RLAELEEELEEAQEEL 222
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
254-492 |
4.05e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 254 IANLQNEVAELSQKVSETttsRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQkgyskvlcQTLSERNSEITSLKN 333
Cdd:COG4942 29 LEQLQQEIAELEKELAAL---KKEEKALLKQLAALERRIAALARRIRALEQELAALE--------AELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 334 EgenLKRDNAITSGMVSSLQK-------DILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRE 406
Cdd:COG4942 98 E---LEAQKEELAELLRALYRlgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 407 LREAQEKELKLCKTQIQDMEKEMKKLRAELRKsctEQSVISRTLREKSKVEEKLQEDSRRklLQLQEMGNRESVIKINLE 486
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEK---ELAELAAELAELQQEAEELEALIAR--LEAEAAAAAERTPAAGFA 249
|
....*.
gi 767902113 487 RAVGQL 492
Cdd:COG4942 250 ALKGKL 255
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
641-1128 |
4.14e-05 |
|
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: 48.18 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 641 LIYLLEHYKKLMSQAQElQIKFNSSQETQQSLLQEKLREHLA------EKEKLNEERLEQEEKLKAK-IRQLTEEKAALE 713
Cdd:pfam05483 259 LTFLLEESRDKANQLEE-KTKLQDENLKELIEKKDHLTKELEdikmslQRSMSTQKALEEDLQIATKtICQLTEEKEAQM 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 714 EYITQERNRAKETLEEERKRMQELESLLAQQKKALAKS------ITQEKNRVKEALEEEQTRVQELEERLARQKEVL--E 785
Cdd:pfam05483 338 EELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNedqlkiITMELQKKSSELEEMTKFKNNKEVELEELKKILaeD 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 786 SSIAHEKRKAKEALESEKRKVQDLeNHLTQQKEISESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDV 865
Cdd:pfam05483 418 EKLLDEKKQFEKIAEELKGKEQEL-IFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDK 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 866 L---NNKLS-DALAMVEETQKTKA--TESLKAESLALKLNETLAELETT-KTKMIMVEERLILQQKMVKALQDEQESQRH 938
Cdd:pfam05483 497 LlleNKELTqEASDMTLELKKHQEdiINCKKQEERMLKQIENLEEKEMNlRDELESVREEFIQKGDEVKCKLDKSEENAR 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 939 GFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERPQDPLVAPMTE---SSAKDmAYEHL 1015
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLElelASAKQ-KFEEI 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1016 IDDLlaaQKEILSQQEVIMKLRKDLTEAHSRMSD---LRGELNEKQKMELEQNVVLVQQQSKELSVLKEKMAQMSSLVEK 1092
Cdd:pfam05483 656 IDNY---QKEIEDKKISEEKLLEEVEKAKAIADEavkLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKN 732
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 767902113 1093 KDRELKALEEAL-------RASQEKHRLQLNTEKEQKPRKKTQ 1128
Cdd:pfam05483 733 KEQEQSSAKAALeielsniKAELLSLKKQLEIEKEEKEKLKME 775
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
664-825 |
4.64e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 664 SSQETQQSLLQEKLREHLAEKEKLNEERleqeEKLKAKIRQLTEEKAALEEYIT---QERNRAKETLEEERKRMQE---- 736
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEY----NELQAELEALQAEIDKLQAEIAeaeAEIEERREELGERARALYRsggs 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 737 ----------------------LESLLAQQKKALA--KSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAhEK 792
Cdd:COG3883 102 vsyldvllgsesfsdfldrlsaLSKIADADADLLEelKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA-EQ 180
|
170 180 190
....*....|....*....|....*....|...
gi 767902113 793 RKAKEALESEKRKVQDLENHLTQQKEISESNIA 825
Cdd:COG3883 181 EALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
350-1057 |
7.67e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.66 E-value: 7.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 350 SSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQE-DAHRELREAQEKELKLCKTQIQDMEKE 428
Cdd:TIGR00618 162 SKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMpDTYHERKQVLEKELKHLREALQQTQQS 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 429 MKKLRAE---------LRKSCTEQSVISRTLREKSKVEEKLQE--DSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRS 497
Cdd:TIGR00618 242 HAYLTQKreaqeeqlkKQQLLKQLRARIEELRAQEAVLEETQEriNRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMR 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 498 QVIKATYGRAKPFRDK-PVTDQQLIEKITQVTEDNINFQQKKWTLQKETQlsnSKQEETTENIEKLRTSLDSCQACMKIS 576
Cdd:TIGR00618 322 SRAKLLMKRAAHVKQQsSIEEQRRLLQTLHSQEIHIRDAHEVATSIREIS---CQQHTLTQHIHTLQQQKTTLTQKLQSL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 577 CCSHD------------LKKEVDLLQHLQVSPPVSGLQKVVLDVLRHALSwLEEVEQLLRDLGILPSSPNKGFSLYLIYL 644
Cdd:TIGR00618 399 CKELDilqreqatidtrTSAFRDLQGQLAHAKKQQELQQRYAELCAAAIT-CTAQCEKLEKIHLQESAQSLKEREQQLQT 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 645 LEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQE--EKLKAKIRQLTEEKAALEEYITQERNR 722
Cdd:TIGR00618 478 KEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRrmQRGEQTYAQLETSEEDVYHQLTSERKQ 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 723 AKEtLEEERKRMQELESLLAQQKKALAKSI---TQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIA------HEKR 793
Cdd:TIGR00618 558 RAS-LKEQMQEIQQSFSILTQCDNRSKEDIpnlQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDlqdvrlHLQQ 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 794 KAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDA 873
Cdd:TIGR00618 637 CSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEY 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 874 LAMVEETQKTKATESLKAESLALKLNETLAELEtTKTKMIMVEERLILQQKMVKALQDEQESQRhgFEEEIMEYKEQIKQ 953
Cdd:TIGR00618 717 DREFNEIENASSSLGSDLAAREDALNQSLKELM-HQARTVLKARTEAHFNNNEEVTAALQTGAE--LSHLAAEIQFFNRL 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 954 HAQTIVSLEEKLQKVTQHHKKIEGeIATLKDNDPAPKEERPQDPLvapmtessAKDMAYEHLIDDLLAAQKEILSQQEVI 1033
Cdd:TIGR00618 794 REEDTHLLKTLEAEIGQEIPSDED-ILNLQCETLVQEEEQFLSRL--------EEKSATLGEITHQLLKYEECSKQLAQL 864
|
730 740
....*....|....*....|....
gi 767902113 1034 MKLRKDLTEAHSRMSDLRGELNEK 1057
Cdd:TIGR00618 865 TQEQAKIIQLSDKLNGINQIKIQF 888
|
|
| FHA_FhaA-like |
cd22668 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
17-89 |
8.72e-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: 42.84 E-value: 8.72e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767902113 17 STTIGRHENSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQnVAVKLIPGDILRFGSAGL 89
Cdd:cd22668 19 SNIIGRGSDADFRLPDTGVSRRHAEIRWDGQ--VAHLTDLGSTNGTTVNNAPVT-PEWRLADGDVITLGHSEI 88
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
675-797 |
8.77e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.16 E-value: 8.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 675 EKLREHLAEKEKLNEERLEQEE-----KLKAKIRQLTEEKAALEEYITqernRAKETLEEERKRMQELESLLAQQKKALA 749
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEereltEEEEEIRRLEEQVERLEAEVE----ELEAELEEKDERIERLERELSEARSEER 458
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 767902113 750 KSITQEK---------NRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKE 797
Cdd:COG2433 459 REIRKDReisrldreiERLERELEEERERIEELKRKLERLKELWKLEHSGELVPVKV 515
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
258-813 |
8.84e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.35 E-value: 8.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 258 QNEVAELSQKVSETTTSRQNEKEISQKCQvldEDIDAKQKEIQSLKS---QISALQKGYSKVLCQ-TLSERNSEITSLKN 333
Cdd:TIGR00606 425 QEQADEIRDEKKGLGRTIELKKEILEKKQ---EELKFVIKELQQLEGssdRILELDQELRKAERElSKAEKNSLTETLKK 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 334 EGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVShLKSQNKDKDHQLEALGSRCSvlkEELKQEDAHRELREAQEK 413
Cdd:TIGR00606 502 EVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEM-LTKDKMDKDEQIRKIKSRHS---DELTSLLGYFPNKKQLED 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 414 ELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEdsrrKLLQLQEMGNRESvikinleravgQLE 493
Cdd:TIGR00606 578 WLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYED----KLFDVCGSQDEES-----------DLE 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 494 HFRSQVIKATYGRAkPFRDKPVTDQQLIEKIT-----------QVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKL 562
Cdd:TIGR00606 643 RLKEEIEKSSKQRA-MLAGATAVYSQFITQLTdenqsccpvcqRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKK 721
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 563 RTSLDSCQACMKISCCSHDLK-KEVDLLQH--LQVSPPVSGLQKVVLD---VLRHALSWLEEVEQLLRDLGILpsspnKG 636
Cdd:TIGR00606 722 EKRRDEMLGLAPGRQSIIDLKeKEIPELRNklQKVNRDIQRLKNDIEEqetLLGTIMPEEESAKVCLTDVTIM-----ER 796
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 637 FSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSL-LQEKLREHLAEKE---KLNEERLEQEEKLKAKIRQLTEEKAAL 712
Cdd:TIGR00606 797 FQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQeKQHELDTVVSKIElnrKLIQDQQEQIQHLKSKTNELKSEKLQI 876
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 713 EEYItQERNRAKETLEEERKRMQELESLLAQQKK---ALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIA 789
Cdd:TIGR00606 877 GTNL-QRRQQFEEQLVELSTEVQSLIREIKDAKEqdsPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHG 955
|
570 580
....*....|....*....|....
gi 767902113 790 HEKRKAKEALESEKRKVQDLENHL 813
Cdd:TIGR00606 956 YMKDIENKIQDGKDDYLKQKETEL 979
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
649-821 |
1.07e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.34 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 649 KKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAkirqltEEKAAleeyitQERNRAKETLE 728
Cdd:PRK09510 83 KKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQA------EEAAA------KAAAAAKAKAE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 729 EERKRMQELESLLAQQKKALAKSITQEKN------------RVKEALEEEQTRVQELEER---LARQKEVLESSIAHEKR 793
Cdd:PRK09510 151 AEAKRAAAAAKKAAAEAKKKAEAEAAKKAaaeakkkaeaeaAAKAAAEAKKKAEAEAKKKaaaEAKKKAAAEAKAAAAKA 230
|
170 180
....*....|....*....|....*...
gi 767902113 794 KAKEALESEKRKVQDLENHLTQQKEISE 821
Cdd:PRK09510 231 AAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| FHA_Slr1951-like |
cd22697 |
forkhead associated (FHA) domain found in Synechocystis sp. Slr1951 protein and similar ... |
19-92 |
1.27e-04 |
|
forkhead associated (FHA) domain found in Synechocystis sp. Slr1951 protein and similar proteins; This subfamily corresponds to a group of uncharacterized FHA domain-containing proteins which show high sequence similarity with Synechocystis sp. protein Slr1951 and protein Sll1895. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438749 [Multi-domain] Cd Length: 102 Bit Score: 42.45 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 19 TIGRHENSDLVLQSPDIDNHHALIEY----NEAECSFVLQDF----NSRNGTFVNECHIQNVAvkLIPGDILRFG-SAGL 89
Cdd:cd22697 21 TIGRHPGNDIQIPSQQISRRHATLRRkinpNLDISFWIIDGDlegaESLNGLWVNGERILQHE--LVNGDEIALGpKIVL 98
|
...
gi 767902113 90 TYE 92
Cdd:cd22697 99 RYQ 101
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
666-802 |
1.30e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 666 QETQQSLLQEKLREHLAEKEKLNEERLE----QEEKLKAKIRQLTEEKAALEeyitQERNRAKETLEE-ERKRMQELESL 740
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERE----RRRARLEALLAAlGLPLPASAEEF 382
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 741 LAQQK--KALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLE------SSIAHEKRKAKEALESE 802
Cdd:COG4913 383 AALRAeaAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAslerrkSNIPARLLALRDALAEA 452
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
683-1399 |
1.53e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 683 EKEKLNEERLEQeeklKAKIRQLTEEKAALEE--YITQERNRAKETLEEERKRMQELESLLA-----QQKKALAKSITQE 755
Cdd:PTZ00121 1051 DIDGNHEGKAEA----KAHVGQDEGLKPSYKDfdFDAKEDNRADEATEEAFGKAEEAKKTETgkaeeARKAEEAKKKAED 1126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 756 KNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKvqdlenHLTQQKEISESNIAYEKRKAKEAM 835
Cdd:PTZ00121 1127 ARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAK------KAEAARKAEEVRKAEELRKAEDAR 1200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 836 EKEKKKVQDLENRLTKQKEELELkeqkedvlnnKLSDALAMVEETQKtKATESLKAESLalKLNETLAELETTKTKMIMV 915
Cdd:PTZ00121 1201 KAEAARKAEEERKAEEARKAEDA----------KKAEAVKKAEEAKK-DAEEAKKAEEE--RNNEEIRKFEEARMAHFAR 1267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 916 EERLILQQKMVKALQDEQESQRHGFEE----EIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIE-----GEIATLKDND 986
Cdd:PTZ00121 1268 RQAAIKAEEARKADELKKAEEKKKADEakkaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADaakkkAEEAKKAAEA 1347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 987 PAPKEERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEViMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNV 1066
Cdd:PTZ00121 1348 AKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA-DEAKKKAEEDKKKADELKKAAAAKKKADEAKKK 1426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1067 VLVQQQSKELSVlKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQTCDTSVQIEPVHTEAFSS 1146
Cdd:PTZ00121 1427 AEEKKKADEAKK-KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA 1505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1147 SQEQQSFSDLGVRCKGSRHEEVIQRQKKALSELRARIKELEKArspdhkdhqnESFLDLKNLRMENNVQKilldakpdlp 1226
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA----------DELKKAEELKKAEEKKK---------- 1565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1227 tlsrieilAPQNGLCNARFGSAMEKSGKMDVAEALELSEklyldmsktlgslmniknmsghvSMKYLSRQEREKVNQLRQ 1306
Cdd:PTZ00121 1566 --------AEEAKKAEEDKNMALRKAEEAKKAEEARIEE-----------------------VMKLYEEEKKMKAEEAKK 1614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1307 RDLDlvfdkitQLKNQLGRKEELLRgyeKDVEQLRRSKVSIEMYQSQVAKLEDDIYKEAEEKALLKEALERMEHQLCQEK 1386
Cdd:PTZ00121 1615 AEEA-------KIKAEELKKAEEEK---KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684
|
730
....*....|...
gi 767902113 1387 RINRAIRQQKMRK 1399
Cdd:PTZ00121 1685 EDEKKAAEALKKE 1697
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
709-821 |
1.62e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 709 KAALEEYITQERNRAKETLEEERKRMQEL--ESLLAQQKKALaksitQEKNRVKEALEEEQTRVQELEERLARQKEVLEs 786
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIkkEALLEAKEEIH-----KLRNEFEKELRERRNELQKLEKRLLQKEENLD- 99
|
90 100 110
....*....|....*....|....*....|....*
gi 767902113 787 siahekrKAKEALESEKRKVQDLENHLTQQKEISE 821
Cdd:PRK12704 100 -------RKLELLEKREEELEKKEKELEQKQQELE 127
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
673-779 |
2.84e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.46 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 673 LQEKLREHLAEKEKLNEErleQEEKLKAKIRQLTEEKAALEEYITQERNR-------------AKETLEEERKRMQELES 739
Cdd:COG0542 416 LERRLEQLEIEKEALKKE---QDEASFERLAELRDELAELEEELEALKARweaekelieeiqeLKEELEQRYGKIPELEK 492
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 767902113 740 LLAQQKKALAKSITQEKNRVKEA-----------------LEEEQTRVQELEERLAR 779
Cdd:COG0542 493 ELAELEEELAELAPLLREEVTEEdiaevvsrwtgipvgklLEGEREKLLNLEEELHE 549
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
685-798 |
3.17e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 685 EKLNEERLEQEEKLKAKIRQLTEEKAALEEyITQERNRAKETLEEERKRMQELEsllaQQKKALAKSITQEKNRVKEALE 764
Cdd:COG4942 142 KYLAPARREQAEELRADLAELAALRAELEA-ERAELEALLAELEEERAALEALK----AERQKLLARLEKELAELAAELA 216
|
90 100 110
....*....|....*....|....*....|....
gi 767902113 765 EEQTRVQELEERLARqkevLESSIAHEKRKAKEA 798
Cdd:COG4942 217 ELQQEAEELEALIAR----LEAEAAAAAERTPAA 246
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
287-425 |
3.36e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.57 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 287 VLDEDIDAKQKEIQSLKSQIS------ALQKGYSKVLCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKdilakd 360
Cdd:PRK09039 43 FLSREISGKDSALDRLNSQIAeladllSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEG------ 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767902113 361 eQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKqedAHRELREAQEKELKLCKTQIQDM 425
Cdd:PRK09039 117 -RAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLA---ALEAALDASEKRDRESQAKIADL 177
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
11-93 |
3.67e-04 |
|
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: 41.46 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 11 FFVLNKSTTIGR---------HENSDLVLQSPD-IDNHHALIEYNEAECSFVLQDFnSRNGTFVNE--CHIQNVAVKLIP 78
Cdd:cd22701 12 YYVQKLEVVLGRnsknssstaADSVDIDLGPSKkISRRHARIFYDFTTQCFELSVL-GRNGVKVDGilVKPGSPPVPLRS 90
|
90
....*....|....*
gi 767902113 79 GDILRFGSAGLTYEL 93
Cdd:cd22701 91 GSLIQIGGVLFYFLL 105
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
268-516 |
3.68e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 268 VSETTTSRQNEKEISQkcqvLDEDIDAKQKEIQSLKSQISALQKgyskvlcqTLSERNSEITSLKNEGENLKRDNAITSG 347
Cdd:COG4942 16 AAQADAAAEAEAELEQ----LQQEIAELEKELAALKKEEKALLK--------QLAALERRIAALARRIRALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 348 MVSSLQKDILAKDEQVQQLKEEVSHL--KSQNKDKDHQLEALGSRCSVLKEELKQE------DAHRELREAQEKELKLCK 419
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPEDFLDAVRRLQylkylaPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 420 TQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQV 499
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
250
....*....|....*..
gi 767902113 500 IKATYGRAKPFRDKPVT 516
Cdd:COG4942 244 PAAGFAALKGKLPWPVS 260
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
680-1030 |
4.63e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.94 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 680 HLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEyitqernraketLEEERKRMQELESLLAQQKKA----LAKsiTQE 755
Cdd:COG3096 276 HANERRELSERALELRRELFGARRQLAEEQYRLVE------------MARELEELSARESDLEQDYQAasdhLNL--VQT 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 756 KNRVKEALEEEQTRVQELEERLARQKEVLESsiAHEKR-KAKEALESEKRKVQDLENHLT--QQ--KEISESNIAYE--- 827
Cdd:COG3096 342 ALRQQEKIERYQEDLEELTERLEEQEEVVEE--AAEQLaEAEARLEAAEEEVDSLKSQLAdyQQalDVQQTRAIQYQqav 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 828 --KRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQK--------TKATESLKAESLALK 897
Cdd:COG3096 420 qaLEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKayelvckiAGEVERSQAWQTARE 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 898 LNETLAEL-------ETTKTKMIMVEERLILQQKMVKALQD------EQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEK 964
Cdd:COG3096 500 LLRRYRSQqalaqrlQQLRAQLAELEQRLRQQQNAERLLEEfcqrigQQLDAAEELEELLAELEAQLEELEEQAAEAVEQ 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 965 LQKVTQHHKKIEGEIATLKDNDPA-----PKEERPQDPLVAPMTESSAKDMAYEHLID---------DLLAAQKEILSQQ 1030
Cdd:COG3096 580 RSELRQQLEQLRARIKELAARAPAwlaaqDALERLREQSGEALADSQEVTAAMQQLLErereatverDELAARKQALESQ 659
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
254-744 |
5.20e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 254 IANLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAKQ---KEIQSLKSQISALQKGYSKvlcqtLSERNSEITS 330
Cdd:PRK03918 268 IEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELReieKRLSRLEEEINGIEERIKE-----LEEKEERLEE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 331 LKNEGENLKRDNAITSGMVSSLQkDILAKDEQVQQLKEEvshLKSQNKDKdhqlealgsrcsvLKEELKQEDAHRELREA 410
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKR---LTGLTPEK-------------LEKELEELEKAKEEIEE 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 411 QEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVE--EKLQEDSRRKLLQLQEMGNRESVIKINLERA 488
Cdd:PRK03918 406 EISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKEllEEYTAELKRIEKELKEIEEKERKLRKELREL 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 489 VGQLEHFRS-QVIKATYGRAKPFRDKpvTDQQLIEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLD 567
Cdd:PRK03918 486 EKVLKKESElIKLKELAEQLKELEEK--LKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 568 SCQACMKISCCSHDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRhALSWLEEVEQLLRDLGILPSSPNKGFSlYLIYLLEH 647
Cdd:PRK03918 564 KLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLE-LKDAEKELEREEKELKKLEEELDKAFE-ELAETEKR 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 648 YKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQER--NRAKE 725
Cdd:PRK03918 642 LEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEklEKALE 721
|
490
....*....|....*....
gi 767902113 726 TLEEERKRMQELESLLAQQ 744
Cdd:PRK03918 722 RVEELREKVKKYKALLKER 740
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
244-824 |
5.32e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.04 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 244 EIESKYKDVIiANLQNEVAELsQKVSETTTSRQNEKEISQKCQVLDEDIDAKQ---KEIQSLKSQISALQKGYSkvlcqT 320
Cdd:TIGR01612 1136 EIKKKSENYI-DEIKAQINDL-EDVADKAISNDDPEEIEKKIENIVTKIDKKKniyDEIKKLLNEIAEIEKDKT-----S 1208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 321 LSE-RNSEITSLKNEG----ENLKRDNAITSGMVSSLQKDILAKDEqVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLK 395
Cdd:TIGR01612 1209 LEEvKGINLSYGKNLGklflEKIDEEKKKSEHMIKAMEAYIEDLDE-IKEKSPEIENEMGIEMDIKAEMETFNISHDDDK 1287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 396 EELKQEDAHRE-LREAQEKELKLC-----KTQIQDMEKEMKKLRAELRKSCTEQSvisrtlrekskveeklqedsrrklL 469
Cdd:TIGR01612 1288 DHHIISKKHDEnISDIREKSLKIIedfseESDINDIKKELQKNLLDAQKHNSDIN------------------------L 1343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 470 QLQEMGNRESVIKIN-LERAVGQLEHFRSQVIKATygraKPFRDKPVTDQQLIEKItqvtEDNINFQQKKWTLqkETQLS 548
Cdd:TIGR01612 1344 YLNEIANIYNILKLNkIKKIIDEVKEYTKEIEENN----KNIKDELDKSEKLIKKI----KDDINLEECKSKI--ESTLD 1413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 549 NSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRHALSWL-----EEVEQLL 623
Cdd:TIGR01612 1414 DKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATNDHdfninELKEHID 1493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 624 RDLGI-LPSSPNKGFSLYLIYLLEHYKK----LMSQAQELQIKFNSSQETQQSllqeklREHLAEKEKLNEERLEQEEKL 698
Cdd:TIGR01612 1494 KSKGCkDEADKNAKAIEKNKELFEQYKKdvteLLNKYSALAIKNKFAKTKKDS------EIIIKEIKDAHKKFILEAEKS 1567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 699 KAKIRQLTEEKAALEEYITQ--ERNRA----KETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQE 772
Cdd:TIGR01612 1568 EQKIKEIKKEKFRIEDDAAKndKSNKAaidiQLSLENFENKFLKISDIKKKINDCLKETESIEKKISSFSIDSQDTELKE 1647
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 767902113 773 LEERLARQKEVLESSIAHEK--RKAKEALESEKRKVQDLENHLTQQKEISESNI 824
Cdd:TIGR01612 1648 NGDNLNSLQEFLESLKDQKKniEDKKKELDELDSEIEKIEIDVDQHKKNYEIGI 1701
|
|
| FHA_Par42-like |
cd22675 |
forkhead associated (FHA) domain found in Trypanosoma brucei Parvulin 42 (TbPar42) and similar ... |
20-100 |
5.32e-04 |
|
forkhead associated (FHA) domain found in Trypanosoma brucei Parvulin 42 (TbPar42) and similar proteins; TbPar42 is a nuclear protein that plays a key role in parasite cell proliferation. It exhibits an N-terminal forkhead associated (FHA)-domain and a peptidyl-prolyl-cis/trans-isomerase (PPIase) domain, both connected by a linker. Its PPIase domain adopts a parvulin fold and reflects structural elements of Pin1-type proteins but is catalytically inactive. Its FHA domain may be involved in the binding of phosphorylated target proteins. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438727 [Multi-domain] Cd Length: 113 Bit Score: 41.00 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 20 IGRHENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQnvAVKLIP---GDILRFGSAGLTYElVIE 96
Cdd:cd22675 33 FGRSPVCDYVLEHPSISSVHAVLVFHGEQKCFVLMDLGSTNGVKLNGKRIE--KGRPLPlpvGSVIQFGFSARKYK-VRK 109
|
....
gi 767902113 97 NPPP 100
Cdd:cd22675 110 GPPS 113
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
354-828 |
5.71e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 5.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 354 KDILAKDEQVQQL----KEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKLcktqiqdMEKEM 429
Cdd:PRK03918 182 EKFIKRTENIEELikekEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELES-------LEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 430 KKLRA---ELRKSCTEQSVISRTLREKSKVEEKLQEDSrRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKatygR 506
Cdd:PRK03918 255 RKLEEkirELEERIEELKKEIEELEEKVKELKELKEKA-EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE----R 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 507 AKPFRDKPVTDQQLIEKITQVTEDNINFQQKKWTLQ----KETQLSNSKQEETTENIEKLRTSLDSCQAcmkisccshdl 582
Cdd:PRK03918 330 IKELEEKEERLEELKKKLKELEKRLEELEERHELYEeakaKKEELERLKKRLTGLTPEKLEKELEELEK----------- 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 583 KKEVDLLQHLQVSPPVSGLQKVVLDvLRHALSWLEEVEqllrdlGILPSSPNKgfslyliyLLEHYKKLMSQAQELQIKf 662
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKE-LKKAIEELKKAK------GKCPVCGRE--------LTEEHRKELLEEYTAELK- 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 663 NSSQETQQslLQEKLREHLAEKEKLNEERLEQEE--KLKAKIRQLTEEKAALEEYITQERNRAKE--------------- 725
Cdd:PRK03918 463 RIEKELKE--IEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEELEKKAEeyeklkekliklkge 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 726 --TLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIahEKRKAKEALESEK 803
Cdd:PRK03918 541 ikSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYL--ELKDAEKELEREE 618
|
490 500
....*....|....*....|....*.
gi 767902113 804 RKVQDLENHLTQ-QKEISESNIAYEK 828
Cdd:PRK03918 619 KELKKLEEELDKaFEELAETEKRLEE 644
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
654-798 |
6.13e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 6.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 654 QAQELQIKFNSSQETQQSLLQEKLREHLAE--------------KEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQE 719
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAEllralyrlgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 720 RNR---AKETLEEERKRMQELESLLAQQKKALAKSItQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAK 796
Cdd:COG4942 159 LAElaaLRAELEAERAELEALLAELEEERAALEALK-AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
..
gi 767902113 797 EA 798
Cdd:COG4942 238 AA 239
|
|
| FHA_DgcB-like |
cd22682 |
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ... |
11-86 |
6.20e-04 |
|
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB and similar proteins; DgcB is a GGDEF enzyme that produces cyclic-di-GMP in response to an unknown stimulus. It appends the C-terminal GGDEF enzymatic domain with an N-terminal forkhead-associated (FHA) domain that acts as a consensus phosphopeptide sensor. The GGDEF and sensory FHA domains form an asymmetrical dimer.
Pssm-ID: 438734 [Multi-domain] Cd Length: 96 Bit Score: 40.59 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 11 FFVLNKSTTIGRHENSDLVLQSPDIDNHHALIEYNEAECSfvLQDFNSRNGTFVN--------ECHIQNvavklipGDIL 82
Cdd:cd22682 15 FPITESTIVIGRSVESQVQIDDDSVSRYHAKLAVNPSAVS--IIDLGSTNGTIVNgkkipklaSCDLQN-------GDQI 85
|
....
gi 767902113 83 RFGS 86
Cdd:cd22682 86 KIGN 89
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
888-1126 |
6.29e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 888 SLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQrhgfEEEIMEYKEQIKQHAQTIVSLEEKLQK 967
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 968 VTQHHKKIEGEIATLKDN-----DPAPKEERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEIlsqqevIMKLRKDLTE 1042
Cdd:COG4942 88 LEKEIAELRAELEAQKEElaellRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQ------AEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1043 AHSRMSDLRGELNEKQKMELEQnvvlvQQQSKELSVLK-EKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQ 1121
Cdd:COG4942 162 LAALRAELEAERAELEALLAEL-----EEERAALEALKaERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
....*
gi 767902113 1122 KPRKK 1126
Cdd:COG4942 237 AAAAE 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
667-818 |
6.30e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 667 ETQQSLLQEKLREHLAEKEKLNEERLEQEEK-------------------LKAKIRQLTEEKAALEeyitqERNRAKETL 727
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQERrealqrlaeyswdeidvasAEREIAELEAELERLD-----ASSDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 728 EEERKRMQELESLLAQQKKALAKSITQEKNRVkEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQ 807
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKEL-EQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE 769
|
170
....*....|.
gi 767902113 808 DLENHLTQQKE 818
Cdd:COG4913 770 NLEERIDALRA 780
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
645-1061 |
8.45e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 645 LEHYKKLMSQAQELQiKFNSSQETQQSLLQE--KLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNR 722
Cdd:PRK01156 321 INKYHAIIKKLSVLQ-KDYNDYIKKKSRYDDlnNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKI 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 723 AKETLEEERKRMQELESLLAQQKKALAkSITQEKNRVKEALEEEQTRVQELEER---------LARQK-EVLESSIAHEK 792
Cdd:PRK01156 400 QEIDPDAIKKELNEINVKLQDISSKVS-SLNQRIRALRENLDELSRNMEMLNGQsvcpvcgttLGEEKsNHIINHYNEKK 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 793 RKAKEALESEKRKVQDLENHLTQQKEISEsniaYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSD 872
Cdd:PRK01156 479 SRLEEKIREIEIEVKDIDEKIVDLKKRKE----YLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNR 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 873 ALAMVEETQKTKATESLKAESL--ALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQ 950
Cdd:PRK01156 555 YKSLKLEDLDSKRTSWLNALAVisLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNK 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 951 IKQhAQTIVSLEEKLQKVTQHHKKiegEIATLKDNDPAPKEerpqdpLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQ 1030
Cdd:PRK01156 635 YNE-IQENKILIEKLRGKIDNYKK---QIAEIDSIIPDLKE------ITSRINDIEDNLKKSRKALDDAKANRARLESTI 704
|
410 420 430
....*....|....*....|....*....|.
gi 767902113 1031 EVimkLRKDLTEAHSRMSDLRGELNEKQKME 1061
Cdd:PRK01156 705 EI---LRTRINELSDRINDINETLESMKKIK 732
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
419-789 |
9.22e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 9.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 419 KTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNResviKINLERAVGQLEHFRSQ 498
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD----LARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 499 VIKatygrakpfrdkpvTDQQLIEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDScqacmkiscc 578
Cdd:TIGR02168 752 LSK--------------ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE---------- 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 579 shdLKKEVDLLQ--HLQVSPPVSGLQKVVLDVLRHALSWLEEVEQLLRDLGILPSSPNKgfslyliyLLEHYKKLMSQAQ 656
Cdd:TIGR02168 808 ---LRAELTLLNeeAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE--------LEELIEELESELE 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 657 ELQIKFNSSQE------TQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEE 730
Cdd:TIGR02168 877 ALLNERASLEEalallrSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEA 956
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767902113 731 RKRMQELESLLAQQKKALaKSITQEKNRVK----EALEEeqtrVQELEER---LARQKEVLESSIA 789
Cdd:TIGR02168 957 EALENKIEDDEEEARRRL-KRLENKIKELGpvnlAAIEE----YEELKERydfLTAQKEDLTEAKE 1017
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
297-473 |
9.41e-04 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 42.42 E-value: 9.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 297 KEIQSLKSQISALQKGYS--KVLCQTLSERNS-----------EITSLKNEGENLkrdnaitSGMVSSLQKDILAKDEQV 363
Cdd:pfam17078 3 KVIESLHDQIDALTKTNLqlTVQSQNLLSKLEiaqqkeskfleNLASLKHENDNL-------SSMLNRKERRLKDLEDQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 364 QQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQE--------DAHRELREAQEKELKLCKTQIQDMEKEMKKLRAE 435
Cdd:pfam17078 76 SELKNSYEELTESNKQLKKRLENSSASETTLEAELERLqiqydalvDSQNEYKDHYQQEINTLQESLEDLKLENEKQLEN 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 767902113 436 LrkscteqsvISRTLREKSKVEEKLQE-DSRRKLLQLQE 473
Cdd:pfam17078 156 Y---------QQRISSNDKDIDTKLDSyNNKFKNLDNIY 185
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
690-818 |
9.94e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 9.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 690 ERLEQE-EKLKAKIRQLTEEKAALEEYItqernRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQT 768
Cdd:COG4913 238 ERAHEAlEDAREQIELLEPIRELAERYA-----AARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELE 312
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 767902113 769 RVQELEERLARQKEVLESSIAHEKRKAKEALESE----KRKVQDLENHLTQQKE 818
Cdd:COG4913 313 RLEARLDALREELDELEAQIRGNGGDRLEQLEREierlERELEERERRRARLEA 366
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
667-895 |
1.05e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 667 ETQQSLLQEKLREHLAEKEKLNEE--RLEQE-EKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQ 743
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAEldALQAElEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 744 QKKA-----------LAKSITQEKNRVkEALEEEQTRVQELEERLARQKEVLEssiahekrKAKEALESEKRKVQDLENH 812
Cdd:COG3883 95 LYRSggsvsyldvllGSESFSDFLDRL-SALSKIADADADLLEELKADKAELE--------AKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 813 LTQQKEISESNIAyEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAE 892
Cdd:COG3883 166 LEAAKAELEAQQA-EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
...
gi 767902113 893 SLA 895
Cdd:COG3883 245 SAA 247
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
244-747 |
1.11e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.80 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 244 EIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKEISQKCQVLdEDIDAKQKEIQSLKSQISALQKGYSKVLCQTLSE 323
Cdd:TIGR00618 434 ELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTK-EQIHLQETRKKAVVLARLLELQEEPCPLCGSCIH 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 324 RNSEITSLKNEGENLKRDNAITSGmVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELkqeda 403
Cdd:TIGR00618 513 PNPARQDIDNPGPLTRRMQRGEQT-YAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDI----- 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 404 hrelrEAQEKELKLCKTQIQDMEKEMKKLRAELRkscteqsvisrtlREKSKVEEKLqeDSRRKLLQLQEMGNRESVIKI 483
Cdd:TIGR00618 587 -----PNLQNITVRLQDLTEKLSEAEDMLACEQH-------------ALLRKLQPEQ--DLQDVRLHLQQCSQELALKLT 646
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 484 NLERavgQLEHFRSQVIKATYGRAKPFRDKPVTDQQLIEKITQvtedniNFQQKKWTLQKETQLSNSKQEETTENIEKLR 563
Cdd:TIGR00618 647 ALHA---LQLTLTQERVREHALSIRVLPKELLASRQLALQKMQ------SEKEQLTYWKEMLAQCQTLLRELETHIEEYD 717
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 564 TSLDscQACMKISCCSHDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRHALSWLEEVEQLLRDlgilpsspnkgfslyliy 643
Cdd:TIGR00618 718 REFN--EIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTG------------------ 777
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 644 llehyKKLMSQAQELQIKFNSSQETQQSL--LQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERN 721
Cdd:TIGR00618 778 -----AELSHLAAEIQFFNRLREEDTHLLktLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLL 852
|
490 500
....*....|....*....|....*.
gi 767902113 722 RAKETLEEERKRMQELESLLAQQKKA 747
Cdd:TIGR00618 853 KYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
348-491 |
1.11e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 348 MVSSLQKDILAKDEQVQQLKEEVSHL-KSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQIQDME 426
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALkKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRY 484
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767902113 427 KEMKKLRAELRKSCTEQSVISRTLREKSKVEE--------------KLQEDSRRKLLQLqemgnrESVIKinlERAVGQ 491
Cdd:COG0542 485 GKIPELEKELAELEEELAELAPLLREEVTEEDiaevvsrwtgipvgKLLEGEREKLLNL------EEELH---ERVIGQ 554
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
283-493 |
1.47e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 283 QKCQVLDEDIDAKQKEIQSLKSQISALQKgyskvLCQTLSERNSEITSLKNegenlkrdnaitsgmVSSLQKDILAKDEQ 362
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEA-----ELDALQERREALQRLAE---------------YSWDEIDVASAERE 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 363 VQQLKEEVSHLKSQNKDkdhqLEALGSRCSVLKEELkqeDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTE 442
Cdd:COG4913 670 IAELEAELERLDASSDD----LAALEEQLEELEAEL---EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767902113 443 QSVISRTLREKsKVEEKLQEDSRRKLlqLQEMGNRESVIKINLERAVGQLE 493
Cdd:COG4913 743 ARLELRALLEE-RFAAALGDAVEREL--RENLEERIDALRARLNRAEEELE 790
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
646-799 |
1.60e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 646 EHYKKLMSQA-QELQIKFNSSQETQQSLLQ--EKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYItqernr 722
Cdd:PRK12704 64 EEIHKLRNEFeKELRERRNELQKLEKRLLQkeENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELI------ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 723 aketlEEERKRMQELESLLAQQkkalAKSITQEKnrVKEALEEEQTR-VQELEERlarqkevlessiAHE--KRKAKEAL 799
Cdd:PRK12704 138 -----EEQLQELERISGLTAEE----AKEILLEK--VEEEARHEAAVlIKEIEEE------------AKEeaDKKAKEIL 194
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
677-816 |
1.65e-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: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 677 LREHLAEKEklneERLEQEEKLKAKIRQLTEEKAALEEyitqernrAKETLEEERKRMQELESLLAQQKKALAKSITQEK 756
Cdd:COG4913 666 AEREIAELE----AELERLDASSDDLAALEEQLEELEA--------ELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767902113 757 NRVKEALE-EEQTRVQELEERLARqkEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQ 816
Cdd:COG4913 734 DRLEAAEDlARLELRALLEERFAA--ALGDAVERELRENLEERIDALRARLNRAEEELERA 792
|
|
| FHA_PPP1R8 |
cd22674 |
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ... |
16-93 |
1.70e-03 |
|
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 (PPP1R8) and similar proteins; PPP1R8, also called nuclear inhibitor of protein phosphatase 1 (NIPP-1), is an inhibitor subunit of the major nuclear protein phosphatase-1 (PP-1). It has RNA-binding activity but does not cleave RNA and may target PP-1 to RNA-associated substrates. It may also be involved in pre-mRNA splicing and binds DNA and might act as a transcriptional repressor. PPP1R8 seems to be required for cell proliferation. PPP1R8 contains an FHA domain that mediates interactions with threonine-phosphorylated maternal embryonic leucine zipper kinase (MELK). The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438726 [Multi-domain] Cd Length: 108 Bit Score: 39.56 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 16 KSTTIGR-HENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFGSAGLTYEL 93
Cdd:cd22674 27 KYYLFGRnSDVCDFVLDHPSCSRVHAALVYHKHLNRVFLIDLGSTHGTFVGGIRLEpHKPQQLPIDSTLRFGASTRRYIL 106
|
|
| FHA_EmbR-like |
cd22669 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis transcriptional ... |
5-92 |
1.81e-03 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis transcriptional regulatory protein EmbR and similar proteins; EmbR is a transcriptional regulator of the embCAB operon encoding cell wall arabinosyltransferases (EmbC, -A, and -B), and is phosphorylated by the cognate mycobacterial serine/threonine protein kinase PknH. It interacts with RNA polymerase and possesses a phosphorylation-dependent ATPase activity. EmbR contains a regulatory C-terminal forkhead-associated (FHA) domain, which mediates binding to a threonine-phosphorylated site in PknH. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438721 [Multi-domain] Cd Length: 89 Bit Score: 38.94 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 5 LKSAEGFFVLNKSTTIGRHENSDLVLQSPDIDNHHALIEYNEAECSfvLQDFNSRNGTFVNECHIQNVAVkLIPGDILRF 84
Cdd:cd22669 5 IASGRGYPLQAAATRIGRLHDNDIVLDSANVSRHHAVIVDTGTNYV--INDLRSSNGVHVQHERIRSAVT-LNDGDHIRI 81
|
....*...
gi 767902113 85 GSAGLTYE 92
Cdd:cd22669 82 CDHEFTFQ 89
|
|
| FHA_Ct664-like |
cd22696 |
forkhead associated (FHA) domain found in Chlamydia trachomatis Ct664 protein and similar ... |
8-86 |
1.88e-03 |
|
forkhead associated (FHA) domain found in Chlamydia trachomatis Ct664 protein and similar proteins; This subfamily corresponds to a group of uncharacterized FHA domain-containing proteins which show high sequence similarity with Chlamydia trachomatis Ct664 protein. Ct664 situates within the type III secretion system cluster that also encodes an STPK (CT673 in C. trachomatis), suggesting a role of CT664 in the chlamydial type III secretion system by mediating phosphorylation-dependent protein-protein interactions. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438748 [Multi-domain] Cd Length: 97 Bit Score: 39.01 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 8 AEGFFVLNKSTTIGRHEN-SDLVLQSPDIDNHHALIEYNEAECSFVlQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGS 86
Cdd:cd22696 13 AEFFLESGKTYFIGKDPTvCDIVLQDPSISRQHARLSIDQDNRVFI-EDLSSKNGVLVNGKPIEG-KEEISGSDVISLGT 90
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
270-492 |
1.92e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 42.05 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 270 ETTTSRQNEKEISQKCQVLdedIDAKQKEIQSLKSQISA----LQKGYSKVLCQTLSERN---SEITSLKNEGENLKRDN 342
Cdd:pfam09787 1 NLESAKQELADYKQKAARI---LQSKEKLIASLKEGSGVegldSSTALTLELEELRQERDllrEEIQKLRGQIQQLRTEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 343 AitsGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRelreaqekelklcKTQI 422
Cdd:pfam09787 78 Q---ELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATL-------------QSRI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767902113 423 QDMEKEMKKLRAELR---KSCTEQSVISRTLREkskveekLQEDSRRKLLQLQEMGNRESVIKINLERAVGQL 492
Cdd:pfam09787 142 KDREAEIEKLRNQLTsksQSSSSQSELENRLHQ-------LTETLIQKQTMLEALSTEKNSLVLQLERMEQQI 207
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
646-888 |
2.13e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 646 EHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKE 725
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 726 TLEEERKRMQEL---ESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELE-----ERLARQKEVLESSIAHEKRKAKE 797
Cdd:PTZ00121 1641 KEAEEKKKAEELkkaEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEalkkeAEEAKKAEELKKKEAEEKKKAEE 1720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 798 ALESEKRKVQDLENHLTQQKEisesniayEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKL--SDALA 875
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEE--------DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELdeEDEKR 1792
|
250
....*....|...
gi 767902113 876 MVEETQKTKATES 888
Cdd:PTZ00121 1793 RMEVDKKIKDIFD 1805
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
649-819 |
2.14e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 649 KKLMSQAQELQIKFNSSQETQQSLLQE------------------------------KLREHLAEKEKLNEERLEQEEKL 698
Cdd:pfam01576 408 KKLEGQLQELQARLSESERQRAELAEKlsklqselesvssllneaegkniklskdvsSLESQLQDTQELLQEETRQKLNL 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 699 KAKIRQLTEEKAALEEYItQERNRAKETLEeerKRMQELESLLAQQKKALaksitQEKNRVKEALEEEQTRVQELEERLA 778
Cdd:pfam01576 488 STRLRQLEDERNSLQEQL-EEEEEAKRNVE---RQLSTLQAQLSDMKKKL-----EEDAGTLEALEEGKKRLQRELEALT 558
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767902113 779 RQKEvlessiahEKRKAKEALESEKRKVQ----DLENHLTQQKEI 819
Cdd:pfam01576 559 QQLE--------EKAAAYDKLEKTKNRLQqeldDLLVDLDHQRQL 595
|
|
| FHA_Rv1747-like_rpt2 |
cd22737 |
second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
20-92 |
2.21e-03 |
|
second 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 second FHA domain, which has a circularly permuted FHA domain fold with a conserved pThr-binding interface.
Pssm-ID: 439356 [Multi-domain] Cd Length: 93 Bit Score: 39.01 E-value: 2.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767902113 20 IGRHENSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQnvAVKLIPGDILRFGSAGLTYE 92
Cdd:cd22737 25 IGRASDNDIVIPEGSVSRHHATLVPTPG--GTQIRDLRSTNGTFVNGLRVD--AALLHDGDVVTIGDIDFVFE 93
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
244-829 |
2.25e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 244 EIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQkgyskvlcQTLSE 323
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLR--------ETIAE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 324 RNSEITSLKNEgenlkrdnaitsgmvsslqkdILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRcsvlKEELKQEDA 403
Cdd:PRK02224 270 TEREREELAEE---------------------VRDLRERLEELEEERDDLLAEAGLDDADAEAVEAR----REELEDRDE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 404 hrELREaqekELKLCKTQIQDMEKEMKKLRAELRKSCTEqsviSRTLREKSKVEEKLQEDSRRKllqlqemgnresviki 483
Cdd:PRK02224 325 --ELRD----RLEECRVAAQAHNEEAESLREDADDLEER----AEELREEAAELESELEEAREA---------------- 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 484 nLERAVGQLEHFRSQVIKAtygrAKPFRDKPVTDQQLIEKITQVTEDninfqqKKWTLQKETQLSNSKQEEtTENIEKLR 563
Cdd:PRK02224 379 -VEDRREEIEELEEEIEEL----RERFGDAPVDLGNAEDFLEELREE------RDELREREAELEATLRTA-RERVEEAE 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 564 TSLDS--CQACMkisccshdlkkevdllQHLQVSPPVsglqkvvlDVLRHALSWLEEVEQLLRDLGILPSSPNKGfslyl 641
Cdd:PRK02224 447 ALLEAgkCPECG----------------QPVEGSPHV--------ETIEEDRERVEELEAELEDLEEEVEEVEER----- 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 642 IYLLEHYKKLMSQAQELQIKfnssQETQQSLLQEKlREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQER- 720
Cdd:PRK02224 498 LERAEDLVEAEDRIERLEER----REDLEELIAER-RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEARe 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 721 -----NRAKETLEEERKRMQELESLLA-------------QQKKALAKSITQEKNRVKE------ALEEE--QTRVQELE 774
Cdd:PRK02224 573 evaelNSKLAELKERIESLERIRTLLAaiadaedeierlrEKREALAELNDERRERLAEkrerkrELEAEfdEARIEEAR 652
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 767902113 775 ERLARQKEVLE--SSIAHEKRKAKEALESEkrkVQDLENHLTQQKEISESNIAYEKR 829
Cdd:PRK02224 653 EDKERAEEYLEqvEEKLDELREERDDLQAE---IGAVENELEELEELRERREALENR 706
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
720-802 |
2.39e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 40.16 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 720 RNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQE----LEERLARQKEVLESSIAHEKRKA 795
Cdd:COG0711 33 QEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEEakaeAEAEAERIIAQAEAEIEQERAKA 112
|
....*..
gi 767902113 796 KEALESE 802
Cdd:COG0711 113 LAELRAE 119
|
|
| FHA_GarA-like |
cd22720 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis glycogen accumulation ... |
12-91 |
2.68e-03 |
|
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: 38.83 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 12 FVLNKSTT-IGRHENSDLVLQSPDIDNHHAliEYNEAECSFVLQDFNSRNGTFVNECHIqNVAVkLIPGDILRFGSAGLT 90
Cdd:cd22720 19 FLLDQAITsAGRHPDSDIFLDDVTVSRRHA--EFRLENNEFNVVDVGSLNGTYVNREPV-DSAV-LANGDEVQIGKFRLV 94
|
.
gi 767902113 91 Y 91
Cdd:cd22720 95 F 95
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
644-802 |
2.72e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 644 LLEHYKKLMSQAQELQIKFNSSQEtQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQL------------------ 705
Cdd:COG3883 35 AQAELDALQAELEELNEEYNELQA-ELEALQAEIDKLQAEIAEAEAEIEERREELGERARALyrsggsvsyldvllgses 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 706 ---------------TEEKAALEEYITQER--NRAKETLEEERKRMQELESLLAQQKKALAKSITqEKNRVKEALEEEQT 768
Cdd:COG3883 114 fsdfldrlsalskiaDADADLLEELKADKAelEAKKAELEAKLAELEALKAELEAAKAELEAQQA-EQEALLAQLSAEEA 192
|
170 180 190
....*....|....*....|....*....|....
gi 767902113 769 RVQELEERLARQKEVLESSIAHEKRKAKEALESE 802
Cdd:COG3883 193 AAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
675-822 |
2.91e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 675 EKLREHL-AEKEKLNE--ERLEQEEK-LKAKIRQLTEEKaaleeyitQERNRAKETLEEERKRMQE-LESLLAQQKKALA 749
Cdd:PRK00409 505 EEAKKLIgEDKEKLNEliASLEELEReLEQKAEEAEALL--------KEAEKLKEELEEKKEKLQEeEDKLLEEAEKEAQ 576
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767902113 750 KsitqeknRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKA-KEALESekrkvqdLENHLTQQKEISES 822
Cdd:PRK00409 577 Q-------AIKEAKKEADEIIKELRQLQKGGYASVKAHELIEARKRlNKANEK-------KEKKKKKQKEKQEE 636
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
245-985 |
3.44e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.35 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 245 IESKYKDVIIANLQNEVAELSQKVSETTTS--RQNEKEISQ------------KCQVLDEDIDAKQKEIQSLKSQISALQ 310
Cdd:TIGR01612 960 IEKSYKDKFDNTLIDKINELDKAFKDASLNdyEAKNNELIKyfndlkanlgknKENMLYHQFDEKEKATNDIEQKIEDAN 1039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 311 KGYSKVLCQTlserNSEITSLKNEGENLKRDNaitsgmVSSLQKDILAKDE----QVQQLKEEVSHLKSQNKDKDHQLEa 386
Cdd:TIGR01612 1040 KNIPNIEIAI----HTSIYNIIDEIEKEIGKN------IELLNKEILEEAEinitNFNEIKEKLKHYNFDDFGKEENIK- 1108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 387 LGSRCSVLKEELK----QEDAH----RELREAQEKELKLCKTQIQDMEKemkklraelrksCTEQSVISRTLREKSKVEE 458
Cdd:TIGR01612 1109 YADEINKIKDDIKnldqKIDHHikalEEIKKKSENYIDEIKAQINDLED------------VADKAISNDDPEEIEKKIE 1176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 459 KLQEDSRRKLLQLQEMGNRESVIKiNLERAVGQLEHFRSqvIKATYGRA--KPFRDKPVTDQQLIEKITQVTE------D 530
Cdd:TIGR01612 1177 NIVTKIDKKKNIYDEIKKLLNEIA-EIEKDKTSLEEVKG--INLSYGKNlgKLFLEKIDEEKKKSEHMIKAMEayiedlD 1253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 531 NINFQQKKWTLQKETQLSNSKQEET------------------TENIEKLRT-SLDSCQACMKISCCShDLKKEvdllqh 591
Cdd:TIGR01612 1254 EIKEKSPEIENEMGIEMDIKAEMETfnishdddkdhhiiskkhDENISDIREkSLKIIEDFSEESDIN-DIKKE------ 1326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 592 lqvsppvsgLQKVVLDVLRHAlswlEEVEQLLrdlgilpsspNKGFSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQS 671
Cdd:TIGR01612 1327 ---------LQKNLLDAQKHN----SDINLYL----------NEIANIYNILKLNKIKKIIDEVKEYTKEIEENNKNIKD 1383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 672 LL--QEKLREHLAEKEKLNEERLEQEEKLKAK-IRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKAL 748
Cdd:TIGR01612 1384 ELdkSEKLIKKIKDDINLEECKSKIESTLDDKdIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMAD 1463
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 749 AKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKR--KAKEALESEKRKVQDLENHLTQQKeiSESNIAY 826
Cdd:TIGR01612 1464 NKSQHILKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAieKNKELFEQYKKDVTELLNKYSALA--IKNKFAK 1541
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 827 EKRKAKEAMEKekkkVQDLENRLTKQKEELELKEQK---------EDVLNNKLSDALAM-VEETQKTKATESLKAESLAL 896
Cdd:TIGR01612 1542 TKKDSEIIIKE----IKDAHKKFILEAEKSEQKIKEikkekfrieDDAAKNDKSNKAAIdIQLSLENFENKFLKISDIKK 1617
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 897 KLNETLAELETTKTKMimveerlilqQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIE 976
Cdd:TIGR01612 1618 KINDCLKETESIEKKI----------SSFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIE 1687
|
....*....
gi 767902113 977 GEIATLKDN 985
Cdd:TIGR01612 1688 IDVDQHKKN 1696
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
257-464 |
3.50e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 257 LQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQKgyskvlcqTLSERNSEITSLKNEGE 336
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA--------EIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 337 NLKRDNAITSGMVSSLQKDILAKD--EQVQQLkEEVSHLKSQNKDKDHQLEALGSRCSVLKEEL-KQEDAHRELREAQEK 413
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLLGSESfsDFLDRL-SALSKIADADADLLEELKADKAELEAKKAELeAKLAELEALKAELEA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767902113 414 ELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDS 464
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
645-799 |
3.55e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 645 LEHYKKLMSQAQELQIKFNSSQETQQSLLQE--------KLREHLAEKEKLNEE------RLEQEEKLKAKIRQLTEEKA 710
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREEleklekllQLLPLYQELEALEAElaelpeRLEELEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 711 ALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAksitQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAH 790
Cdd:COG4717 167 ELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ----QRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
....*....
gi 767902113 791 EKRKAKEAL 799
Cdd:COG4717 243 ERLKEARLL 251
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
666-1189 |
3.56e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 666 QETQQSLLQEKLREHLAEKEKLNEERLEQE---EKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQE-LESLL 741
Cdd:TIGR02169 221 REYEGYELLKEKEALERQKEAIERQLASLEeelEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEkIGELE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 742 AQQkkALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAhEKRKAKEALESEKRKVQDLENHLTQQ-KEIS 820
Cdd:TIGR02169 301 AEI--ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIE-EERKRRDKLTEEYAELKEELEDLRAElEEVD 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 821 ESNIAY--EKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKL 898
Cdd:TIGR02169 378 KEFAETrdELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 899 NETLAELETTKTKMIMVEERLILQQKMVKALQ---DEQESQRHGFEEEIMEYK---EQIKQHAQTIVSLEEKLQKV-TQH 971
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKELSKLQrelAEAEAQARASEERVRGGRaveEVLKASIQGVHGTVAQLGSVgERY 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 972 HKKIEGE-------------------IATLKDNDPAP------KEERPQDPLVAPMTESSAKDMAY-------------- 1012
Cdd:TIGR02169 538 ATAIEVAagnrlnnvvveddavakeaIELLKRRKAGRatflplNKMRDERRDLSILSEDGVIGFAVdlvefdpkyepafk 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1013 ------------------------------------------------------------------EHLIDDLLAAQKEI 1026
Cdd:TIGR02169 618 yvfgdtlvvedieaarrlmgkyrmvtlegelfeksgamtggsraprggilfsrsepaelqrlrerlEGLKRELSSLQSEL 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1027 LSQQEVIMKLRKDLTEAHSRMSDLRGELN------EKQKMELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKAL 1100
Cdd:TIGR02169 698 RRIENRLDELSQELSDASRKIGEIEKEIEqleqeeEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKL 777
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 1101 EEAL---RASQEKHRLQ-----LNTEKEQKPRKKTQTCDTSVQIEPVHTEAFSSSQEQQSFSDLGVRCKgSRHEEVIQRQ 1172
Cdd:TIGR02169 778 EEALndlEARLSHSRIPeiqaeLSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK-EQIKSIEKEI 856
|
650 660
....*....|....*....|
gi 767902113 1173 ---KKALSELRARIKELEKA 1189
Cdd:TIGR02169 857 enlNGKKEELEEELEELEAA 876
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
666-810 |
3.70e-03 |
|
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: 41.86 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 666 QETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEE-------YITQERNRAKETLEEERKRMQELE 738
Cdd:pfam15709 357 QEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEeerkqrlQLQAAQERARQQQEEFRRKLQELQ 436
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902113 739 SLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELEErlarqKEVLESSIAHEKRKAKEALESEKRKVQDLE 810
Cdd:pfam15709 437 RKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAE-----EERLEYQRQKQEAEEKARLEAEERRQKEEE 503
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
226-484 |
4.23e-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: 41.73 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 226 KDEIILLLGKEVSRLSDyeiESKYKDVIIANLQNEVAELSQKVSETTTSrqnekeisqkCQVLDEDIDAKQKEIQSLKSQ 305
Cdd:pfam10174 392 KERKINVLQKKIENLQE---QLRDKDKQLAGLKERVKSLQTDSSNTDTA----------LTTLEEALSEKERIIERLKEQ 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 306 ISALQKgyskvlcqtlsERNSEITSLKNEGENLKRDnaitsgmVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLE 385
Cdd:pfam10174 459 REREDR-----------ERLEELESLKKENKDLKEK-------VSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLK 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 386 ALGSRCSVLKEE-LKQEDAHRELREAQEKELKLCK--TQIQDMEKEMKKLRAELRKSCTEQSVISRTLR----EKSKVEE 458
Cdd:pfam10174 521 SLEIAVEQKKEEcSKLENQLKKAHNAEEAVRTNPEinDRIRLLEQEVARYKEESGKAQAEVERLLGILRevenEKNDKDK 600
|
250 260
....*....|....*....|....*.
gi 767902113 459 KLQEDSRRKLLQLQEMGNRESVIKIN 484
Cdd:pfam10174 601 KIAELESLTLRQMKEQNKKVANIKHG 626
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
670-829 |
4.37e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.90 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 670 QSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEyitqERNRAKETLEEERKRMQELESllaqQKKALA 749
Cdd:pfam09787 17 ARILQSKEKLIASLKEGSGVEGLDSSTALTLELEELRQERDLLRE----EIQKLRGQIQQLRTELQELEA----QQQEEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 750 KSITQEKNRVKEALEEEQTRVQELEERLARQKEVLeSSIAHEKRKAKEALESEKRK----VQDLENHLTQQKEISESNIA 825
Cdd:pfam09787 89 ESSREQLQELEEQLATERSARREAEAELERLQEEL-RYLEEELRRSKATLQSRIKDreaeIEKLRNQLTSKSQSSSSQSE 167
|
....
gi 767902113 826 YEKR 829
Cdd:pfam09787 168 LENR 171
|
|
| FlgN |
pfam05130 |
FlgN protein; This family includes the FlgN protein and export chaperone involved in flagellar ... |
724-819 |
4.51e-03 |
|
FlgN protein; This family includes the FlgN protein and export chaperone involved in flagellar synthesis.
Pssm-ID: 428323 [Multi-domain] Cd Length: 140 Bit Score: 39.27 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 724 KETLEEERKRMQELESLLAQQKKALAK-------SITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAK 796
Cdd:pfam05130 4 IELLEEELELLEELLELLEEEQEALKAgdiealeELTEEKQELLQKLAQLEKERRELLAELGLSPEEATLSELLAKEEED 83
|
90 100
....*....|....*....|...
gi 767902113 797 EALESEKRKVQDLENHLTQQKEI 819
Cdd:pfam05130 84 PELRELWQELLELLERLKELNEL 106
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
244-439 |
4.74e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 244 EIESKYKDviIANLQNEVAELSQKVSETTtsrQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQKGYSKVLCQT-LS 322
Cdd:TIGR04523 490 ELKSKEKE--LKKLNEEKKELEEKVKDLT---KKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKeID 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 323 ERNSEITSLKNEGENLKRDN-------AITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLK 395
Cdd:TIGR04523 565 EKNKEIEELKQTQKSLKKKQeekqeliDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLK 644
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767902113 396 EELKQ----EDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKS 439
Cdd:TIGR04523 645 QEVKQiketIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLH 692
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
257-480 |
4.83e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 257 LQNEVAELSQKVSETTTS----RQNEKEISqkcqvLDEDIDAKQKEIQSLKSQISALQkgyskvlcqtlsernSEITSLK 332
Cdd:COG3206 180 LEEQLPELRKELEEAEAAleefRQKNGLVD-----LSEEAKLLLQQLSELESQLAEAR---------------AELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 333 NEGENLKRDNAITSGMVSSLQKD--ILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDahRELREA 410
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEA--QRILAS 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767902113 411 QEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQE-DSRRKLLQLQEMGNRESV 480
Cdd:COG3206 318 LEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESlLQRLEEARLAEALTVGNV 388
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
673-797 |
4.88e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.77 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 673 LQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKEtleeerkrMQEL-ESLLAQQKKALAKS 751
Cdd:smart00787 145 LKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDE--------LEDCdPTELDRAKEKLKKL 216
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 767902113 752 ITQEKNRVKEaLEEEQTRVQELE---ERLARQKEVLESSIAHEKRKAKE 797
Cdd:smart00787 217 LQEIMIKVKK-LEELEEELQELEskiEDLTNKKSELNTEIAEAEKKLEQ 264
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
667-770 |
5.28e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.48 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 667 ETQQSLLQEKLREHLAEKEKLNEERLEQEEkLKAKIRQLTEEKAALEEYitqernrAKETLEEERKRMQELESLLAQQKK 746
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQ-SQALAEAQQQELVALEGL-------AAELEEKQQELEAQLEQLQEKAAE 209
|
90 100
....*....|....*....|....*....
gi 767902113 747 ALAKSITQEKNRVKEA-----LEEEQTRV 770
Cdd:PRK11448 210 TSQERKQKRKEITDQAakrleLSEEETRI 238
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
290-726 |
5.29e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 290 EDIDAKQKEIQSLKSQISALQKgyskvLCQTLSERNSEITSLKNEGENLKRDnaitsgmvsslqKDILAKDEQVQQLKEE 369
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAE-----LQEELEELEEELEELEAELEELREE------------LEKLEKLLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 370 VSHLKSQNKDKDHQLEALGSRCSVLKEELKQ----EDAHRELREAQEKELKLC----KTQIQDMEKEMKKLRAELRKSCT 441
Cdd:COG4717 134 LEALEAELAELPERLEELEERLEELRELEEEleelEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 442 EQSVISRTLREKSKVEEKLQEDSR-----RKLLQLQEMGNRESVIkINLERAVGQLEHFRSQVIKA--------TYGRAK 508
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELEaaaleERLKEARLLLLIAAAL-LALLGLGGSLLSLILTIAGVlflvlgllALLFLL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 509 PFRDKPVTDQQLIEKITQVTEDNInfQQKKWT-----LQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLK 583
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEEL--EEEELEellaaLGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 584 KEVDLLQHLQVSPpvsglqkvvLDVLRHALSWLEEVEQLLRDLGILPSSPNKGFSLYLIYLLEHYKK-LMSQAQELQIKF 662
Cdd:COG4717 371 EIAALLAEAGVED---------EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEeLEEELEELEEEL 441
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767902113 663 NSSQETQQSLLQEKLR-----EHLAEKEKLnEERLEQEEKLKAKIRQLTEEKAAL---EEYITQERNRAKET 726
Cdd:COG4717 442 EELEEELEELREELAEleaelEQLEEDGEL-AELLQELEELKAELRELAEEWAALklaLELLEEAREEYREE 512
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
19-85 |
5.32e-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: 38.11 E-value: 5.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767902113 19 TIGRHENS--DLVLQ-SPDIDNHHALIEYNeAECSFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFG 85
Cdd:cd22663 24 TVGRGLGVtyQLVSTcPLMISRNHCVLKKN-DEGQWTIKDNKSLNGVWVNGERIEpLKPYPLNEGDLIQLG 93
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
219-442 |
5.55e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 219 EDLAQQDKDEIILLLGK---EVSRLSDY-EIESKYKDVIIANLQnevaelSQKVSETTTSRQNEKEISQKcqvLDEDIDA 294
Cdd:PRK05771 34 EDLKEELSNERLRKLRSlltKLSEALDKlRSYLPKLNPLREEKK------KVSVKSLEELIKDVEEELEK---IEKEIKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 295 KQKEIQSLKSQISALQKgyskvlcqtlseRNSEITSLKNEGENLK--RDNAITSGMVSSLQKDIlaKDEQVQQLKEEVSH 372
Cdd:PRK05771 105 LEEEISELENEIKELEQ------------EIERLEPWGNFDLDLSllLGFKYVSVFVGTVPEDK--LEELKLESDVENVE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 373 LKSQNKDKDhqlealgsRCSVLKEELKQEDAHRELREAQEKELKL------------CKTQIQDMEKEMKKLRAELRKSC 440
Cdd:PRK05771 171 YISTDKGYV--------YVVVVVLKELSDEVEEELKKLGFERLELeeegtpselireIKEELEEIEKERESLLEELKELA 242
|
..
gi 767902113 441 TE 442
Cdd:PRK05771 243 KK 244
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
654-766 |
5.58e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 40.73 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 654 QAQELQIKFNSSQE-TQQSLLQekLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERK 732
Cdd:pfam02841 173 KAEEVLQEFLQSKEaVEEAILQ--TDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIE 250
|
90 100 110
....*....|....*....|....*....|....*
gi 767902113 733 RM-QELESLLAQQKKALAKSITQEKNRVKEALEEE 766
Cdd:pfam02841 251 KMeAEREQLLAEQERMLEHKLQEQEELLKEGFKTE 285
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
217-1108 |
5.62e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.57 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 217 VEEDLAQQDKDEIILLLGKEVSRLSDYEIESKykdvIIANLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAKQ 296
Cdd:TIGR00606 207 MELKYLKQYKEKACEIRDQITSKEAQLESSRE----IVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQME 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 297 KEIQSLKSQISALQKGYSKVLCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSL--QKDILAKDEQVQQLKEEVSHLK 374
Cdd:TIGR00606 283 KDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLnqEKTELLVEQGRLQLQADRHQEH 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 375 SQNKDKDHQLEALGSRCSVLKE----ELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTL 450
Cdd:TIGR00606 363 IRARDSLIQSLATRLELDGFERgpfsERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTI 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 451 REKSKVEEKLQEDSRRKLLQLQEMGN------------RESVIKINLERAVGQLEHFRSQVIKATYGRAKPFRDKPVTDQ 518
Cdd:TIGR00606 443 ELKKEILEKKQEELKFVIKELQQLEGssdrileldqelRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQ 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 519 QLIEK---------ITQVTEDNINFQQK-------------------KWTLQKETQLSNSKQE--ETTENIEKLRTSLDS 568
Cdd:TIGR00606 523 EMEQLnhhtttrtqMEMLTKDKMDKDEQirkiksrhsdeltsllgyfPNKKQLEDWLHSKSKEinQTRDRLAKLNKELAS 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 569 CQAcMKISCCSHDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRHAlswlEEVEQLLRDLGILPSSPNkgfsLYLIYLLEHY 648
Cdd:TIGR00606 603 LEQ-NKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLK----EEIEKSSKQRAMLAGATA----VYSQFITQLT 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 649 KKLMSQAQELQIKFNSSQETQQ--SLLQEKLREHLAEKEKLnEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKET 726
Cdd:TIGR00606 674 DENQSCCPVCQRVFQTEAELQEfiSDLQSKLRLAPDKLKST-ESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNK 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 727 LEEERKRMQELESLLAQQKKALAKSITQEknrvkEALEEEQTRVQELEERLARQKEVlessiahEKRKAKEALESEKRKV 806
Cdd:TIGR00606 753 LQKVNRDIQRLKNDIEEQETLLGTIMPEE-----ESAKVCLTDVTIMERFQMELKDV-------ERKIAQQAAKLQGSDL 820
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 807 QDLENHLTQQKEISEsniaYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQkTKAT 886
Cdd:TIGR00606 821 DRTVQQVNQEKQEKQ----HELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLV-ELST 895
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 887 ESLKAESLALKLNETLAELETTKTKMIMVEERLIlqqkmvkalqDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQ 966
Cdd:TIGR00606 896 EVQSLIREIKDAKEQDSPLETFLEKDQQEKEELI----------SSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQ 965
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 967 KVTQHHKK-IEGEIATLKdndpAPKEERPQDplvapmTESSAKDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHS 1045
Cdd:TIGR00606 966 DGKDDYLKqKETELNTVN----AQLEECEKH------QEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEE 1035
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767902113 1046 RMSDLRGELNEKQKMELEQNvvlVQQQSKELSVLKEKMAQMSSLVEKKDRELKALEEALRASQ 1108
Cdd:TIGR00606 1036 ELKQHLKEMGQMQVLQMKQE---HQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
667-782 |
5.72e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 667 ETQQSLLQEKLREHLAEKEKLnEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAK--ETLEEERKRMQELESLLAQQ 744
Cdd:COG3206 225 ESQLAEARAELAEAEARLAAL-RAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAElsARYTPNHPDVIALRAQIAAL 303
|
90 100 110
....*....|....*....|....*....|....*...
gi 767902113 745 KKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKE 782
Cdd:COG3206 304 RAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEA 341
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
672-737 |
5.77e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 41.39 E-value: 5.77e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767902113 672 LLQEKLREhlaeKEKLNEERLEQEeKLKAKIRQLTEEKAALEeyitQERNRAKETLEEERKRMQEL 737
Cdd:PLN02316 250 LLEEKRRE----LEKLAKEEAERE-RQAEEQRRREEEKAAME----ADRAQAKAEVEKRREKLQNL 306
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
656-786 |
5.92e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 656 QELQIKFNSSQETQQSLLQEKLREHLAEkekLNEERLEQEEKLKAK---IRQLTEEKAALEEYITQERNRAKETLEEE-- 730
Cdd:COG3206 247 AQLGSGPDALPELLQSPVIQQLRAQLAE---LEAELAELSARYTPNhpdVIALRAQIAALRAQLQQEAQRILASLEAEle 323
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 767902113 731 --RKRMQELESLLAQQKKALAKsitqeknrvkeaLEEEQTRVQELEERLARQKEVLES 786
Cdd:COG3206 324 alQAREASLQAQLAQLEARLAE------------LPELEAELRRLEREVEVARELYES 369
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
219-472 |
6.78e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.04 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 219 EDLAQ--QDKDEIILLLGK-EVSRLSDYEIESKYKDviiaNLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAK 295
Cdd:PLN02939 131 EDLVGmiQNAEKNILLLNQaRLQALEDLEKILTEKE----ALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 296 QKEIqslkSQISALQKGYSKVLCQTLSERNSEITSLKNEGENLKrdnaitsGMVSSLQKdilaKDEQVQQLKEEVSHLKS 375
Cdd:PLN02939 207 RNEL----LIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLK-------AELIEVAE----TEERVFKLEKERSLLDA 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 376 QNKDKDHQLeaLGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQI----------QDMEKEMKKLRAELRKSCT--EQ 443
Cdd:PLN02939 272 SLRELESKF--IVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVekaalvldqnQDLRDKVDKLEASLKEANVskFS 349
|
250 260 270
....*....|....*....|....*....|
gi 767902113 444 SVISRTLREKSK-VEEKLQEDSRRKLLQLQ 472
Cdd:PLN02939 350 SYKVELLQQKLKlLEERLQASDHEIHSYIQ 379
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
285-397 |
7.01e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 7.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 285 CQVLDEDIDAKQKEIQSLKSQISALQKGYSKVLC--QTLSERNSEITSLKNEGENLKRDnaitsgmVSSLQKDILAKDEQ 362
Cdd:PHA02562 287 CPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTaiDELEEIMDEFNEQSKKLLELKNK-------ISTNKQSLITLVDK 359
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 767902113 363 VQQLKEEVSHLKSQNKDKD-------HQLEALGSRCSVLKEE 397
Cdd:PHA02562 360 AKKVKAAIEELQAEFVDNAeelaklqDELDKIVKTKSELVKE 401
|
|
| FHA_CHK2 |
cd22666 |
forkhead associated (FHA) domain found in checkpoint kinase 2 (Chk2) and similar proteins; ... |
10-65 |
7.09e-03 |
|
forkhead associated (FHA) domain found in checkpoint kinase 2 (Chk2) and similar proteins; Chk2, also called Hucds1, Cds1 homolog, or serine/threonine-protein kinase Chk2, plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438718 [Multi-domain] Cd Length: 112 Bit Score: 37.99 E-value: 7.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767902113 10 GFFVL---NKSTTIGRHENSDLVLQSPDIDNH---------HALI--EYNEAECSFV-LQDFnSRNGTFVN 65
Cdd:cd22666 10 GFSSLdlvKDEYTFGRDKSCDYCFDSPALKKTsyyrtyskkHFRIfrEKGSKNTYPVfLEDH-SSNGTFVN 79
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
674-829 |
7.24e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 674 QEKLREHLAEKEKLNEERLEQEE---KLKAKIRQLTEEKAA---LEEYITQERN-----RAKETLEEERKRM-------Q 735
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEErleALEAELDALQERREAlqrLAEYSWDEIDvasaeREIAELEAELERLdassddlA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 736 ELESLLAQQKKALaKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQ 815
Cdd:COG4913 689 ALEEQLEELEAEL-EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767
|
170
....*....|....
gi 767902113 816 QKEISESNIAYEKR 829
Cdd:COG4913 768 RENLEERIDALRAR 781
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
359-438 |
8.18e-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: 8.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 359 KDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRK 438
Cdd:COG2433 411 EEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREIERLERELEEERERIEE 490
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
654-850 |
8.68e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 654 QAQELQIKFNSSQETQQSLLQE--KLREHLAEKEKlneeRLeQEEKLKAKIRQLTEEKAALEEYIT---QERNRAKETLE 728
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQlpELRKELEEAEA----AL-EEFRQKNGLVDLSEEAKLLLQQLSeleSQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 729 EERKRMQELESLLAQQKKALAK-SITQEKNRVKEALEEEQTRVQELEER----------LARQKEVLESSIAHEKRKAKE 797
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPElLQSPVIQQLRAQLAELEAELAELSARytpnhpdviaLRAQIAALRAQLQQEAQRILA 316
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767902113 798 ALESEKRKVQDLENHLTQQKEISESNIAyekrkakeamekekkKVQDLENRLT 850
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLA---------------ELPELEAELR 354
|
|
| FHA_RAD53-like_rpt1 |
cd22689 |
first forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ... |
13-65 |
8.92e-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: 38.03 E-value: 8.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 767902113 13 VLNKSTTIGRHENSDLVLQSPDIDNHHALI---EYNEAECSFVLQDFNSrNGTFVN 65
Cdd:cd22689 42 SIKKVWTFGRHPACDYHLGNSRLSNKHFQIllgESDPSDGNVLLNDISS-NGTWLN 96
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
254-544 |
9.57e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 40.61 E-value: 9.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 254 IANLQNEVAELSQKVSET--TTSRQNEKEISQKCQVLDEDIDAKQKEI---QSLKSQISALQKGYSKVLCQ------TLS 322
Cdd:PLN03229 431 VRELEGEVEKLKEQILKAkeSSSKPSELALNEMIEKLKKEIDLEYTEAviaMGLQERLENLREEFSKANSQdqlmhpVLM 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 323 ERnseITSLKNE-GENLKRDNAITS-----GMVS--SLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALgsrcSVL 394
Cdd:PLN03229 511 EK---IEKLKDEfNKRLSRAPNYLSlkyklDMLNefSRAKALSEKKSKAEKLKAEINKKFKEVMDRPEIKEKM----EAL 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 395 KEELKQEDAHRElrEAQEKELKlckTQIQDMEKEMKKLRAELRKSCTEQsVISRTLREKSKVEEKLQEDSRRKLLQLQEM 474
Cdd:PLN03229 584 KAEVASSGASSG--DELDDDLK---EKVEKMKKEIELELAGVLKSMGLE-VIGVTKKNKDTAEQTPPPNLQEKIESLNEE 657
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767902113 475 GNRESVIKINLERAVGQLEHFRSQVIKATYGRAKPFRDKPVT-DQQLIEKITQVTeDNINFQQKKWTLQKE 544
Cdd:PLN03229 658 INKKIERVIRSSDLKSKIELLKLEVAKASKTPDVTEKEKIEAlEQQIKQKIAEAL-NSSELKEKFEELEAE 727
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
253-373 |
9.69e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 9.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902113 253 IIANLQNEVAELSQKVSETTTSRQNEKEIsqkcqvLDEdIDAKQKEIQSLKSQISALQkgyskvlcQTLSERNSEITSLK 332
Cdd:PHA02562 300 RITKIKDKLKELQHSLEKLDTAIDELEEI------MDE-FNEQSKKLLELKNKISTNK--------QSLITLVDKAKKVK 364
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 767902113 333 NEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHL 373
Cdd:PHA02562 365 AAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR 405
|
|
| |
