|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
2-97 |
5.06e-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: 5.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 2 KAYLKSAEGFFVLN-KSTTIGRHeNSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQNVAVKLIPGD 80
Cdd:cd22700 1 KGYLKSSDGIFQLDpKVTTIGRE-GCDLVLQSPGVEEQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAPGD 79
|
90
....*....|....*..
gi 1959220873 81 ILRFGSAGLTYELVIEN 97
Cdd:cd22700 80 VLRFGFGGLPYELVVDN 96
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
18-84 |
1.54e-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: 1.54e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1959220873 18 TTIGRHENSDLVLQSPDIDNHHALIEYNEaECSFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRF 84
Cdd:pfam00498 1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDG-GGRFYLEDLGSTNGTFVNGQRLGPEPVRLKDGDVIRL 66
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
646-1188 |
7.75e-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: 7.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 646 EHYKKLMSQAQELQIKFNSSQ----ETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQER- 720
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKlrelEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYe 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 721 -NRAKETLEEERKRMQELESLLAQQKKALAksitQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEAL 799
Cdd:COG1196 293 lLAELARLEQDIARLEERRRELEERLEELE----EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 800 ESEKRKVQDLENHLTQQKEisESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEE 879
Cdd:COG1196 369 EAEAELAEAEEELEELAEE--LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 880 TQKTKATESLKAESLALKLNETLAELETTKTKMImVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQH----- 954
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALA-ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglaga 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 955 -------------AQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERP----QDPLVAPMTESSAKDMAYEHLID 1017
Cdd:COG1196 526 vavligveaayeaALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPldkiRARAALAAALARGAIGAAVDLVA 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1018 DLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQQS-------KELSVLKEKMAQMSSLV 1090
Cdd:COG1196 606 SDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSltggsrrELLAALLEAEAELEELA 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1091 EKKDRELKALEEALRASQEKHRLQLntEKEQKPRKKTQTCDTSVQIEPVHTEAFSSSQEQQSFSDLGVRCKGSRHEEVIQ 1170
Cdd:COG1196 686 ERLAEEELELEEALLAEEEEERELA--EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE 763
|
570
....*....|....*...
gi 1959220873 1171 RQKKALSELRARIKELEK 1188
Cdd:COG1196 764 ELERELERLEREIEALGP 781
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
11-92 |
1.23e-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: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 11 FFVLNKSTTIGRHENSDLVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGLT 90
Cdd:cd00060 14 FPLTKGVVTIGRSPDCDIVLDDPSVSRRHARIEVDGGG--VYLEDLGSTNGTFVNGKRITP-PVPLQDGDVIRLGDTTFR 90
|
..
gi 1959220873 91 YE 92
Cdd:cd00060 91 FE 92
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
12-93 |
4.69e-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: 4.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 12 FVLNKS-TTIGRHENSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGLT 90
Cdd:COG1716 16 FPLDGGpLTIGRAPDNDIVLDDPTVSRRHARIRRDGG--GWVLEDLGSTNGTFVNGQRVTE-PAPLRDGDVIRLGKTELR 92
|
...
gi 1959220873 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 |
9.68e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 80.11 E-value: 9.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 275 RQNEKEISQkcqvLDEDIDAKQKEIQSLKSQISALQKGYSKVLcQTLSERNSEITSL-KNEGENLKRDNAITSGMVSSLQ 353
Cdd:TIGR02169 233 EALERQKEA----IERQLASLEEELEKLTEEISELEKRLEEIE-QLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 354 KDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRcsvLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLR 433
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE---IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 434 AELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATygrakpfrdk 513
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE---------- 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 514 pvtdqqliEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKE-----VDL 588
Cdd:TIGR02169 455 --------WKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvHGT 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 589 LQHL-QVSPPVSG---------LQKVVLD---VLRHALSWLEE-------------VEQLLRDLGILPSSPNKGFSLYLI 642
Cdd:TIGR02169 527 VAQLgSVGERYATaievaagnrLNNVVVEddaVAKEAIELLKRrkagratflplnkMRDERRDLSILSEDGVIGFAVDLV 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 643 YLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEK---LREHLAEKEKL-------NEERLEQEEKLKAKIRQLTEEKAAL 712
Cdd:TIGR02169 607 EFDPKYEPAFKYVFGDTLVVEDIEAARRLMGKYRmvtLEGELFEKSGAmtggsraPRGGILFSRSEPAELQRLRERLEGL 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 713 E---EYITQERNRAKETLEEERKRMQELESLLAQQKKALaKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIA 789
Cdd:TIGR02169 687 KrelSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI-EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 790 hEKRKAKEALESEKRKVQDLENHLTQQKeISESNIAYEKrkakeamekEKKKVQDLENRLTKQKEELELKEQKEDVLNNK 869
Cdd:TIGR02169 766 -RIEELEEDLHKLEEALNDLEARLSHSR-IPEIQAELSK---------LEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 870 LSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLIlqqkmvkalqdeqesqrhGFEEEIMEYKE 949
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG------------------DLKKERDELEA 896
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 950 QIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDndpapkEERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQ 1029
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSELKAKLEALEE------ELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
|
810 820 830
....*....|....*....|....*....|....
gi 1959220873 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 |
1.09e-13 |
|
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: 76.63 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 291 DIDAKQKEIQSLKSQISALQKGYSKvLCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEV 370
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEE-LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 371 SHLKSQNKDKDHQLEALGSRCSVLKEELKQedahrelreaQEKELKLCKTQIQDMEKEMKKLRAELRKScteqsviSRTL 450
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAE----------LEEKLEELKEELESLEAELEELEAELEEL-------ESRL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 451 REKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATYGRAKPFRDKPVTD-QQLIEKITQVTE 529
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAElEELEEELEELQE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 530 DNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHL--QVSPPVS-------- 599
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsGILGVLSelisvdeg 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 600 -----------GLQKVV---LDVLRHALSWLEEVEQ---------LLRDLGILPSSPN--------KGFSLYLIYLLEHY 648
Cdd:TIGR02168 535 yeaaieaalggRLQAVVvenLNAAKKAIAFLKQNELgrvtflpldSIKGTEIQGNDREilkniegfLGVAKDLVKFDPKL 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 649 KKLMS-------------QAQELQIKFN---------------------SSQETQQSLLQEKlrehlAEKEKLNEERLEQ 694
Cdd:TIGR02168 615 RKALSyllggvlvvddldNALELAKKLRpgyrivtldgdlvrpggvitgGSAKTNSSILERR-----REIEELEEKIEEL 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 695 EEklkaKIRQLTEEKAALEeyitQERNRAKETLEEERKRMQELESLLAQQKKALAKsITQEKNRVKEALEEEQTRVQELE 774
Cdd:TIGR02168 690 EE----KIAELEKALAELR----KELEELEEELEQLRKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELTELE 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 775 ERLARQKEVLESSIAHEKRkAKEALESEKRKVQDLENHLTQQKEISESniayekrkakeamekekkkvqdLENRLTKQKE 854
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAE-AEAEIEELEAQIEQLKEELKALREALDE----------------------LRAELTLLNE 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 855 ELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQE 934
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1959220873 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 |
1.28e-13 |
|
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: 76.25 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 244 EIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQKGYsKVLCQTLSE 323
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL-YALANEISR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 324 RNSEITSLKNEGENLKRDNAITSGMVSSL--QKDILAKD-----EQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKE 396
Cdd:TIGR02168 300 LEQQKQILRERLANLERQLEELEAQLEELesKLDELAEElaeleEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 397 ELKQE----DAHRELREAQEKELKLCKTQIQDMEKEMKKLRAEL-----RKSCTEQSVISRTLREKSKVEEKLQEDSRRK 467
Cdd:TIGR02168 380 QLETLrskvAQLELQIASLNNEIERLEARLERLEDRRERLQQEIeellkKLEEAELKELQAELEELEEELEELQEELERL 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 468 LLQLQEMGNRESVIKINLERAVGQLEHFRSQV--IKATYGRAKPFRD--KPVTDQQL-IEKITQVTEDNINFQqKKWTLQ 542
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQARLdsLERLQENLEGFSEgvKALLKNQSgLSGILGVLSELISVD-EGYEAA 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 543 KETQLSNSKQEETTEN-------IEKLRTSLDSCQACMKISCCSHDlKKEVDLLQHLQVSPPVSG-----------LQKV 604
Cdd:TIGR02168 539 IEAALGGRLQAVVVENlnaakkaIAFLKQNELGRVTFLPLDSIKGT-EIQGNDREILKNIEGFLGvakdlvkfdpkLRKA 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 605 VLDVLRHaLSWLEEVEQLLRDLGILPSSPN----------KGFSLY----------------LIYLLEHYKKLMSQAQEL 658
Cdd:TIGR02168 618 LSYLLGG-VLVVDDLDNALELAKKLRPGYRivtldgdlvrPGGVITggsaktnssilerrreIEELEEKIEELEEKIAEL 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 659 QIKFNSSQETQQSLLQE--KLREHLAEKEKLNEERLEQEEKLKAKIRQLTE-------EKAALEEYITQERNR------A 723
Cdd:TIGR02168 697 EKALAELRKELEELEEEleQLRKELEELSRQISALRKDLARLEAEVEQLEEriaqlskELTELEAEIEELEERleeaeeE 776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 724 KETLEEERkrmQELESLLAQQKKALAKSitqeknrvKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEK 803
Cdd:TIGR02168 777 LAEAEAEI---EELEAQIEQLKEELKAL--------REALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 804 RKVQDLENHLTQQKEISESNIAYEKrkAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKT 883
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEE--LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 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 |
4.88e-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: 4.88e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1959220873 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 |
3.56e-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: 3.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 12 FVLNK-STTIGRHENSDLVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHI--QNVAVKLIPGDILRFGSAG 88
Cdd:cd22665 16 FPLYEgENVIGRDPSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNKVRlkPNVRYELIDGDLLLFGDVK 93
|
....
gi 1959220873 89 LTYE 92
Cdd:cd22665 94 CQYV 97
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
662-1462 |
3.95e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 71.71 E-value: 3.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 662 FNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLL 741
Cdd:PTZ00121 1081 FDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKA 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 742 AQQKKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEK-RKVQDLENHLTQQKEIS 820
Cdd:PTZ00121 1161 EDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDaKKAEAVKKAEEAKKDAE 1240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 821 ESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQK-EDVLNNKLSDALAMVEETQKT-----KATESLKAESL 894
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADElKKAEEKKKADEAKKAEEKKKAdeakkKAEEAKKADEA 1320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 895 ALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEyKEQIKQHAQTIVSLEEKLQKVTQHHKK 974
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK-KEEAKKKADAAKKKAEEKKKADEAKKK 1399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 975 IEGEIATLKDNDPAPKEERPQDPLVAPMTESSAKDMAyehliddllaaqKEILSQQEVIMKLRKDLTEAHsRMSDLRGEL 1054
Cdd:PTZ00121 1400 AEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEA------------KKKAEEAKKADEAKKKAEEAK-KAEEAKKKA 1466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1055 NEKQKMELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQTCDTSV 1134
Cdd:PTZ00121 1467 EEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK 1546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1135 QIEPVHT-----EAFSSSQEQQSFSDLGVRCKGSRHEEVIQRQKKALSELRARIKELEKARSPDHKDHQNESFLDLKNLR 1209
Cdd:PTZ00121 1547 KADELKKaeelkKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK 1626
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1210 MENNVQKILLDAKPDLPTlsrieilapqnglcNARFGSAMEKSGKMDVAEALELSEKLYLDMSKTlgslmniknmsghVS 1289
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAE--------------EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA-------------EE 1679
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1290 MKYLSRQEREKVNQLRQrdldlvfdkitqlKNQLGRKEELLRGYE----KDVEQLRRSKVSIEMYQSQVAKLEDDIYKEA 1365
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKK-------------EAEEAKKAEELKKKEaeekKKAEELKKAEEENKIKAEEAKKEAEEDKKKA 1746
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1366 EEKALLKEALERMEHQLCQEKRINRAIRQQKESVEEHELrnakestpcncafKEKDRQRRVFVE-MVKNRMQNS-NSQVG 1443
Cdd:PTZ00121 1747 EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL-------------DEEDEKRRMEVDkKIKDIFDNFaNIIEG 1813
|
810
....*....|....*....
gi 1959220873 1444 TRKASLKMDQEREMLRKET 1462
Cdd:PTZ00121 1814 GKEGNLVINDSKEMEDSAI 1832
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
12-86 |
7.10e-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: 7.10e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1959220873 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 ... |
673-1392 |
3.82e-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: 68.16 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 673 LQEKLREH-----LAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQernraketLEEERKRMQELESLLAQQKKA 747
Cdd:TIGR02168 218 LKAELRELelallVLRLEELREELEELQEELKEAEEELEELTAELQELEEK--------LEELRLEVSELEEEIEELQKE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 748 LaKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYE 827
Cdd:TIGR02168 290 L-YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 828 krkakeameKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNET-LAELE 906
Cdd:TIGR02168 369 ---------ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAeLKELQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 907 TTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQK----------VTQHHKKIE 976
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENlegfsegvkaLLKNQSGLS 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 977 GEIATLKDNDPAPKE----------ERPQDPLVApmTESSAKDmAYEHL-----------------IDDLLAAQKEILSQ 1029
Cdd:TIGR02168 520 GILGVLSELISVDEGyeaaieaalgGRLQAVVVE--NLNAAKK-AIAFLkqnelgrvtflpldsikGTEIQGNDREILKN 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1030 QEVIMKLRKDLTEAHSRMS--------------DLRGELNEKQKMELEQNVV----------------------LVQQQS 1073
Cdd:TIGR02168 597 IEGFLGVAKDLVKFDPKLRkalsyllggvlvvdDLDNALELAKKLRPGYRIVtldgdlvrpggvitggsaktnsSILERR 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1074 KELSVLKEKMAQMSSLVEKKDRELKALEEALRASQEKHRlQLNTEKEQKPRKKTQTcDTSVQIEPVHTEAFSSSQEQQSF 1153
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELE-QLRKELEELSRQISAL-RKDLARLEAEVEQLEERIAQLSK 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1154 SDLGVRCKGSRHEEVIQRQKKALSELRARIKELEkARSPDHKDHQNESFLDLKNLRMENNVQKILLDAKpdlptLSRIEI 1233
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELE-AQIEQLKEELKALREALDELRAELTLLNEEAANL-----RERLES 828
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1234 LAPQNGLCNARFGSAMEKSGKM-----DVAEALELSEKLYLDMSKTLGSLMNIKnMSGHVSMKYLSRQEREKVNQLRQRD 1308
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELsedieSLAAEIEELEELIEELESELEALLNER-ASLEEALALLRSELEELSEELRELE 907
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1309 ldlvfDKITQLKNQLGRKEELLRGYEKDVEQLrrsKVSIEMYQSQVAKLEDDIYKEAEEKALLKEA-LERMEHQLcqeKR 1387
Cdd:TIGR02168 908 -----SKRSELRRELEELREKLAQLELRLEGL---EVRIDNLQERLSEEYSLTLEEAEALENKIEDdEEEARRRL---KR 976
|
....*
gi 1959220873 1388 INRAI 1392
Cdd:TIGR02168 977 LENKI 981
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
286-852 |
4.49e-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: 4.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 286 QVLDEDIDAKQKEIQSLKSQISALQKgyskvlcqTLSERNSEITSLKNEGENLKRDnaitsgmVSSLQKDILAKDEQVQQ 365
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEA--------ELAELEAELEELRLELEELELE-------LEEAQAEEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 366 LKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKlckTQIQDMEKEMKKLRAELRKSCTEQSV 445
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE---EELEEAEAELAEAEEALLEAEAELAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 446 ISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATygrakpfrdkpVTDQQLIEKIT 525
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE-----------EEEEEEEEALE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 526 QVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQAcmkisccSHDLKKEVDLLQHLQVSPP----VSGL 601
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA-------RLLLLLEAEADYEGFLEGVkaalLLAG 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 602 QKVVLDVLRHALSWLEEVEQLLRDLGILPSSPNKGFSL-----YLIYLLEHYKKLMSQAQELQIK-FNSSQETQQSLLQE 675
Cdd:COG1196 519 LRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDevaaaAIEYLKAAKAGRATFLPLDKIRaRAALAAALARGAIG 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 676 KLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQE 755
Cdd:COG1196 599 AAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 756 KNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEAM 835
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
|
570
....*....|....*..
gi 1959220873 836 EKEKKKVQDLENRLTKQ 852
Cdd:COG1196 759 PPDLEELERELERLERE 775
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
667-970 |
1.04e-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: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 667 ETQQSLlqEKLREHLAEKEKlNEERLEQEEKLKAKIRQLTEEKAALE-EYITQERNRAKETLEEERKRMQELESLLAQQK 745
Cdd:COG1196 183 ATEENL--ERLEDILGELER-QLEPLERQAEKAERYRELKEELKELEaELLLLKLRELEAELEELEAELEELEAELEELE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 746 KALAKsITQEKNRVKEALEEEQTRVQEL---EERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISEs 822
Cdd:COG1196 260 AELAE-LEAELEELRLELEELELELEEAqaeEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE- 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 823 niayEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETL 902
Cdd:COG1196 338 ----ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1959220873 903 AELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQ 970
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| FHA_DUN1-like |
cd22683 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ... |
17-85 |
1.29e-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: 1.29e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1959220873 17 STTIGRHENSDLVLQSPDIDNHHALIEYnEAECSFVLqDFNSRNGTFVNECHIQNVAVKLIPGDILRFG 85
Cdd:cd22683 22 VTTIGRSRSCDLVLSDPSISRFHAELRL-EQNGINVI-DNNSANGTFINGKRIKGKTYILKNGDIIVFG 88
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
237-779 |
1.42e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 237 VSRLSDYEIESKYKDVIIANLQNEVAELSQKVSETTTSRQnekEISQKCQVLDEDIDAKQKEIQSLKSQISALQKGySKV 316
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYELLAELARLEQD-IAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 317 LCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKE 396
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 397 ELKQEDAHRELREAQEKELKL----CKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQ 472
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEaeeaLLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 473 EMGNRESVIKINLERAVGQLEHFRSQ--VIKATYGRAKPFRD--KPVTDQQLIEKITQVTEDNINFQQKKWTLQkETQLS 548
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARllLLLEAEADYEGFLEgvKAALLLAGLRGLAGAVAVLIGVEAAYEAAL-EAALA 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 549 NSKQEETTEN-------IEKLRTSLDSCQACMKIScCSHDLKKEVDLLQHLQVSPPVSGLQkvVLDVLRHALSWLEEVEQ 621
Cdd:COG1196 546 AALQNIVVEDdevaaaaIEYLKAAKAGRATFLPLD-KIRARAALAAALARGAIGAAVDLVA--SDLREADARYYVLGDTL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 622 LLRDLGILPSSPNKGFSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAK 701
Cdd:COG1196 623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1959220873 702 IRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAksITQEKNRVKEALEEEQTRVQELEERLAR 779
Cdd:COG1196 703 EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE--EALEELPEPPDLEELERELERLEREIEA 778
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
675-1133 |
1.47e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.32 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 675 EKLREHLAEKEKLNEERLEQEEKLKA-KIRQLTEEKAALEEyiTQERNRAKETLEEERKRMQELESLLAQQKKALAKSIT 753
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKAEEKKKAdEAKKKAEEAKKADE--AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA 1485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 754 QEknrVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKE 833
Cdd:PTZ00121 1486 DE---AKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEE 1562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 834 AMEKEKKKVQDLENRLTKQKEELELKEQKEdvlnnKLSDALAMVEETQKTKATESLKAESLALKLNETLAELEttktkmi 913
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRKAEEAKKAEEA-----RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE------- 1630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 914 mvEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKieGEIATLKDNDPAPKEER 993
Cdd:PTZ00121 1631 --EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK--AAEALKKEAEEAKKAEE 1706
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 994 PQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQqs 1073
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE-- 1784
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 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 |
3.68e-10 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 64.99 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 213 AEIYVEEDLAQQDKDEIILLLGKEVSRLSDYEIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDI 292
Cdd:pfam02463 244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEK 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 293 DAKQKEIQSLKSQISALQKGYSKVLCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSH 372
Cdd:pfam02463 324 KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 373 LKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLRE 452
Cdd:pfam02463 404 EKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQ 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 453 KSKVE---EKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEH---FRSQVIKATYGRAKPFRDKPVTDQQLIEKITQ 526
Cdd:pfam02463 484 EQLELllsRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHgrlGDLGVAVENYKVAISTAVIVEVSATADEVEER 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 527 VTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHLQVSPPVSGLQKVV- 605
Cdd:pfam02463 564 QKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKa 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 606 ----LDVLRHALSWLEEVEQLLRDLGILPSSPNKGFSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHL 681
Cdd:pfam02463 644 kesgLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELL 723
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 682 AEKEKLNEERLEQEEKL---KAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNR 758
Cdd:pfam02463 724 ADRVQEAQDKINEELKLlkqKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL 803
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 759 vKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLEnHLTQQKEISESNIAYEKRKAKEAMEKE 838
Cdd:pfam02463 804 -RALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEE-ELERLEEEITKEELLQELLLKEEELEE 881
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 839 KKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEER 918
Cdd:pfam02463 882 QKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEER 961
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1959220873 919 LILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKV 968
Cdd:pfam02463 962 NKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAI 1011
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
233-982 |
6.00e-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: 64.32 E-value: 6.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 233 LGKEVSRLSDYEIESKYKDviIANLQNEVAELSQKVSEtttSRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQKG 312
Cdd:TIGR02169 277 LNKKIKDLGEEEQLRVKEK--IGELEAEIASLERSIAE---KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 313 YSKvLCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDI--------------LAKDEQVQQLKEEVSHLKSQNK 378
Cdd:TIGR02169 352 RDK-LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLeklkreinelkrelDRLQEELQRLSEELADLNAAIA 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 379 DKDHQLEALGSRCSVLKEELKQEDAHRE----LREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKS 454
Cdd:TIGR02169 431 GIEAKINELEEEKEDKALEIKKQEWKLEqlaaDLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 455 KVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHF-----------------RSQVIKATYGRAKPFRDKPVTD 517
Cdd:TIGR02169 511 AVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNvvveddavakeaiellkRRKAGRATFLPLNKMRDERRDL 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 518 QQLIEK-ITQVTEDNINFQQK-----KWTLQkETQLsnskqeetTENIEKLRTSLDSCQAcmkisccshdLKKEVDLLQH 591
Cdd:TIGR02169 591 SILSEDgVIGFAVDLVEFDPKyepafKYVFG-DTLV--------VEDIEAARRLMGKYRM----------VTLEGELFEK 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 592 lqvSPPVSGLQKVVLDVLRHALSWLEEVEQLLRDLGILPSSPNKgfslyLIYLLEHYKKLMSQAQELQikfnsSQETQQS 671
Cdd:TIGR02169 652 ---SGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSS-----LQSELRRIENRLDELSQEL-----SDASRKI 718
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 672 LLQEKLREHLAEKEKLNEERLEQ-EEKLKAKIRQLTEEKAALEEYItQERNRAKETLEEERKRMQELESLLAQQKkalAK 750
Cdd:TIGR02169 719 GEIEKEIEQLEQEEEKLKERLEElEEDLSSLEQEIENVKSELKELE-ARIEELEEDLHKLEEALNDLEARLSHSR---IP 794
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 751 SITQEKNRVKEALEEEQTRVQELEERLAR---QKEVLESSIAHEKRKAKEALESEKrkvqdlenhlTQQKEISESNIayE 827
Cdd:TIGR02169 795 EIQAELSKLEEEVSRIEARLREIEQKLNRltlEKEYLEKEIQELQEQRIDLKEQIK----------SIEKEIENLNG--K 862
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 828 KRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESlalkLNETLAELET 907
Cdd:TIGR02169 863 KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA----LEEELSEIED 938
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1959220873 908 TKTKMIMVEERLILQQKMVKALQDEQESQRhGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATL 982
Cdd:TIGR02169 939 PKGEDEEIPEEELSLEDVQAELQRVEEEIR-ALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
260-849 |
1.15e-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: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 260 EVAELSQKVSETTTSRQNE------KEISQKCQVLDEDIDAKQKEIQSLKSQISALQKGYSKVLcQTLSERNSEITSLKN 333
Cdd:COG1196 210 EKAERYRELKEELKELEAEllllklRELEAELEELEAELEELEAELEELEAELAELEAELEELR-LELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 334 EGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEK 413
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 414 ELklcKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLE 493
Cdd:COG1196 369 EA---EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 494 HFRSQVIKATygrakpfrdkpvTDQQLIEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDScqacm 573
Cdd:COG1196 446 EAAEEEAELE------------EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE----- 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 574 kisccshDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRHALSWLEEVEQ--LLRDLGILpsspnkgfSLYLIYLLEHYKKL 651
Cdd:COG1196 509 -------GVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQniVVEDDEVA--------AAAIEYLKAAKAGR 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 652 MSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEER 731
Cdd:COG1196 574 ATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEG 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 732 KRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLEN 811
Cdd:COG1196 654 EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733
|
570 580 590
....*....|....*....|....*....|....*...
gi 1959220873 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 |
1.38e-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: 1.38e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1959220873 19 TIGRHENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFGSAGLTYEL 93
Cdd:cd22691 32 VVGRHPDCDIVLDHPSISRFHLEIRIIPSRRKITLTDLSSVHGTWVNGQRIEpGVPVELEEGDTVRLGASTRVYRL 107
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
19-85 |
2.33e-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: 2.33e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1959220873 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 |
3.83e-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: 3.83e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1959220873 18 TTIGRHENS-DLVLQSPDIDNHHALIEYNEAECsFVLQDFNSRNGTFVN 65
Cdd:smart00240 1 VTIGRSSEDcDIQLDGPSISRRHAVIVYDGGGR-FYLIDLGSTNGTFVN 48
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
703-1112 |
3.99e-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: 61.62 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 703 RQLTEEKAALEEYiTQERNRAKETLEEERKRMQELESLLAqqkkalaksitqEKNRVKEALEEEQTRVQELEERLARQKE 782
Cdd:TIGR02169 156 RKIIDEIAGVAEF-DRKKEKALEELEEVEENIERLDLIID------------EKRQQLERLRREREKAERYQALLKEKRE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 783 VLESSIAHEKRKAKEALESEKRKVQDLENHLTQ-QKEISESNIAYEKRKAKeamekekkkVQDLENRLTKQKEELELKeq 861
Cdd:TIGR02169 223 YEGYELLKEKEALERQKEAIERQLASLEEELEKlTEEISELEKRLEEIEQL---------LEELNKKIKDLGEEEQLR-- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 862 kedvLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFE 941
Cdd:TIGR02169 292 ----VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 942 EEIMEYKEQIKQHAQT---IVSLEEKLQKVTQHHKKIEGEIatlkdndpapkeerpqdplvapmtessakdmayEHLIDD 1018
Cdd:TIGR02169 368 DLRAELEEVDKEFAETrdeLKDYREKLEKLKREINELKREL---------------------------------DRLQEE 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1019 LLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELnEKQKMELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELK 1098
Cdd:TIGR02169 415 LQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI-KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
|
410
....*....|....
gi 1959220873 1099 ALEEALRASQEKHR 1112
Cdd:TIGR02169 494 EAEAQARASEERVR 507
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
686-1121 |
4.83e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 4.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 686 KLNEERLEQEEKLKAkirqlTEEKAALEEYITQERNRAKETLEEER---KRMQELESLLAQQKKALAKSITQEKNRVKEA 762
Cdd:COG1196 169 KYKERKEEAERKLEA-----TEENLERLEDILGELERQLEPLERQAekaERYRELKEELKELEAELLLLKLRELEAELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 763 LEEEQTRVQELEERLARQKEVLESSIAhEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAkeamekekkkv 842
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELE-ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR----------- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 843 QDLENRLTKQKEELelkeqkedvlnnklsdalamvEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQ 922
Cdd:COG1196 312 RELEERLEELEEEL---------------------AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 923 QKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERpqdplvapm 1002
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE--------- 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1003 tessakdMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQQSKELSVLKEK 1082
Cdd:COG1196 442 -------EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1959220873 1083 MAQMSSLVEKKDREL----KALEEALRASQEKHRLQLNTEKEQ 1121
Cdd:COG1196 515 LLAGLRGLAGAVAVLigveAAYEAALEAALAAALQNIVVEDDE 557
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
618-1461 |
6.53e-09 |
|
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: 60.76 E-value: 6.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 618 EVEQLLRDLGILPSSPN-------------------------KGFSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSL 672
Cdd:pfam02463 120 EVAELLESQGISPEAYNflvqggkieiiammkperrleieeeAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 673 LQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSI 752
Cdd:pfam02463 200 LKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEK 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 753 TQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAK 832
Cdd:pfam02463 280 EKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 833 EAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTktkm 912
Cdd:pfam02463 360 ELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE---- 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 913 imvEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQT-IVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKE 991
Cdd:pfam02463 436 ---EESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETqLVKLQEQLELLLSRQKLEERSQKESKARSGLKVL 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 992 ERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQ 1071
Cdd:pfam02463 513 LALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLK 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1072 QSKELSVLKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQTCDTSVQIEPVHTEAFSSSQEQQ 1151
Cdd:pfam02463 593 SIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELT 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1152 SFSDLGVRCKGSRHEEVIQRQKKALSELRARIKELEKARSPDHKDHQNESFLDLKNLRMENNVQKILLDAKPDLPTLSRI 1231
Cdd:pfam02463 673 KELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEE 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1232 EILAPQNGLCNARFGSAMEKSGKMDV----AEALELSEKLYLDMSKTLGSLMNIKNMSGHVSMKYLSRQEREKVNQLRQ- 1306
Cdd:pfam02463 753 EKSRLKKEEKEEEKSELSLKEKELAEerekTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKe 832
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1307 --RDLDLVFDKITQLKNQLGRKEELLRGYEKDVEQLRRSKVSIEMYQSQVAKLEDDIYKEAEEKALLKEALERMEHQLCQ 1384
Cdd:pfam02463 833 eeLEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLL 912
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1959220873 1385 EKRINRAIRQQKESVEEHELRNAKESTPCNCAFKEKDRQR--RVFVEMVKNRMQNSNSQVGTRKASLKMDQEREMLRKE 1461
Cdd:pfam02463 913 EEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEEnnKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYN 991
|
|
| FHA_Ki67 |
cd22673 |
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ... |
11-92 |
9.32e-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: 9.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 11 FFVLNKSTTIGRHENSDLVLQSPDIDNHHALIEYNEAECsFVLQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGLT 90
Cdd:cd22673 16 FPLTKKSCTFGRDLSCDIRIQLPGVSREHCRIEVDENGK-AYLENLSTTNPTLVNGKAIEK-SAELKDGDVITIGGRSFR 93
|
..
gi 1959220873 91 YE 92
Cdd:cd22673 94 FE 95
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
19-157 |
1.04e-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: 59.39 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 19 TIGRHENSDLVLQSPD--IDNHHALIEYneAECSFVLQDfNSRNGTFVNECHI---QNVAVKLIPGDILRFGSagltYEL 93
Cdd:COG3456 29 TIGRSADCDWVLPDPDrsVSRRHAEIRF--RDGAFCLTD-LSTNGTFLNGSDHplgPGRPVRLRDGDRLRIGD----YEI 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1959220873 94 V--IENPPPVSFPWMRGPAPWPGPQPPRATQQPNqAPPPshiPFHQGVQPAPMQRSWSQAFPRPTV 157
Cdd:COG3456 102 RveISGEDEGADDPLAAAPEPAVSSPSNLSDTEA-APDA---ALAFSFSLDPLEALDEAATEAPAT 163
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
683-1468 |
2.26e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.38 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 683 EKEKLNEERLEQeeklKAKIRQLTEEKAALEE--YITQERNRAKETLEEERKRMQELESLLA-----QQKKALAKSITQE 755
Cdd:PTZ00121 1051 DIDGNHEGKAEA----KAHVGQDEGLKPSYKDfdFDAKEDNRADEATEEAFGKAEEAKKTETgkaeeARKAEEAKKKAED 1126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 756 KNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKvqdlenHLTQQKEISESNIAYEKRKAKEAM 835
Cdd:PTZ00121 1127 ARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAK------KAEAARKAEEVRKAEELRKAEDAR 1200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 836 EKEKKKVQDLENRLTKQKEELELkeqkedvlnnKLSDALAMVEETQKtKATESLKAESLalKLNETLAELETTKTKMIMV 915
Cdd:PTZ00121 1201 KAEAARKAEEERKAEEARKAEDA----------KKAEAVKKAEEAKK-DAEEAKKAEEE--RNNEEIRKFEEARMAHFAR 1267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 916 EERLILQQKMVKALQDEQESQRHGFEE----EIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIE-----GEIATLKDND 986
Cdd:PTZ00121 1268 RQAAIKAEEARKADELKKAEEKKKADEakkaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADaakkkAEEAKKAAEA 1347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 987 PAPKEERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEViMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNV 1066
Cdd:PTZ00121 1348 AKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA-DEAKKKAEEDKKKADELKKAAAAKKKADEAKKK 1426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1067 VLVQQQSKELSVlKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQTCDTSVQIEPVHTEAFSS 1146
Cdd:PTZ00121 1427 AEEKKKADEAKK-KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA 1505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1147 SQEQQSFSDLGVRCKGSRHEEVIQRQKKALSELRARIKELEKArspdhkdhqnESFLDLKNLRMENNVQKIlldakpdlp 1226
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA----------DELKKAEELKKAEEKKKA--------- 1566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1227 tlsrieilapqnglcnarfgsAMEKSGKMDVAEALELSEKLYLDMSKTLGSLMNIKNMSGHVSMKYLSRQEREKVNQLRQ 1306
Cdd:PTZ00121 1567 ---------------------EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1307 RDLDLVFDKITQLKNQlgRKEELlrgyeKDVEQLRRSKVSIEMYQSQVAKLEDDIYKEAEEKALLKEALERMEHQLCQEK 1386
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKK--EAEEK-----KKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA 1698
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1387 RINRAIRQQKESVEEhELRNAKEstpcncaFKEKDRQRRVFVEMVKNRMQNSNSQVGTRKASLKMDQEREMLRKETSSKS 1466
Cdd:PTZ00121 1699 EEAKKAEELKKKEAE-EKKKAEE-------LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKA 1770
|
..
gi 1959220873 1467 SQ 1468
Cdd:PTZ00121 1771 EE 1772
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
650-1010 |
2.28e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.38 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 650 KLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKA----KIRQLTEEKAALEEYITQERNRAKE 725
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAdeakKKAEEAKKKADEAKKAAEAKKKADE 1514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 726 TLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQElEERLARQKEVLESSIAHEKRKAKEALESEKRK 805
Cdd:PTZ00121 1515 AKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE-EKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 806 VQDLENHLTQQKEI--SESNIAYEKRKAKEAMEKEKKKVQDLEN--RLTKQKEELELKEQKEDVLNNKLSDALAMVEETQ 881
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMkaEEAKKAEEAKIKAEELKKAEEEKKKVEQlkKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 882 KTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSL 961
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE 1753
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1959220873 962 EEKlQKVTQHHKKIEGEIATLKDNDPAPKEE--RPQDPLVAPMTESSAKDM 1010
Cdd:PTZ00121 1754 EEK-KKIAHLKKEEEKKAEEIRKEKEAVIEEelDEEDEKRRMEVDKKIKDI 1803
|
|
| FHA_MEK1-like |
cd22670 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ... |
15-92 |
2.63e-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: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 15 NKSTTIGRHENSDLVLQSPDIDNHHALIE---YNEAECSFV-LQDfNSRNGTFVNECHI-QNVAVKLIPGDILRF-GSAG 88
Cdd:cd22670 21 NQVITIGRSPSCDIVINDPFVSRTHCRIYsvqFDESSAPLVyVED-LSSNGTYLNGKLIgRNNTVLLSDGDVIEIaHSAT 99
|
....
gi 1959220873 89 LTYE 92
Cdd:cd22670 100 FVYV 103
|
|
| FHA_Cep170A |
cd22724 |
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar ... |
20-85 |
2.75e-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: 53.05 E-value: 2.75e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1959220873 20 IGRhENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHI-QNVAVKLIPGDILRFG 85
Cdd:cd22724 25 VGR-DDCELMLQSRSVDKQHAVINYDASTDEHKVKDLGSLNGTFVNDVRIpEQTYITLKLDDKLRFG 90
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
675-1112 |
3.36e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 675 EKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKE--TLEEERKRMQELESLLAQQKKALAKsI 752
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkELKEKAEEYIKLSEFYEEYLDELRE-I 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 753 TQEKNRVKEALEEEQTRVQELEERLARQKEVLEssiahEKRKAKEALESEKRKVQDLENHLTQQKEISEsniaYEKRKAK 832
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKEERLEELKK-----KLKELEKRLEELEERHELYEEAKAKKEELER----LKKRLTG 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 833 EAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKA---------TESLKAESLA---LKLNE 900
Cdd:PRK03918 384 LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgrelTEEHRKELLEeytAELKR 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 901 TLAELETTKT-------------KMIMVEERLILQQKMVKALQD-EQESQRHGFEEEIMEYKE----------------- 949
Cdd:PRK03918 464 IEKELKEIEEkerklrkelreleKVLKKESELIKLKELAEQLKElEEKLKKYNLEELEKKAEEyeklkekliklkgeiks 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 950 ------QIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERPQDPLVAPMTESSAKDMAyehliDDLLAAQ 1023
Cdd:PRK03918 544 lkkeleKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAE-----KELEREE 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1024 KEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKM----ELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKA 1099
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK 698
|
490
....*....|...
gi 1959220873 1100 LEEALRASQEKHR 1112
Cdd:PRK03918 699 LKEELEEREKAKK 711
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
17-85 |
5.16e-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: 5.16e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1959220873 17 STTIGRHENSDLVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHIQnvAVKLIPGDILRFG 85
Cdd:cd22694 17 SVRIGRDPDADVRLDDPRVSRRHALLEFDGDG--WVYTDLGSRNGTYLNGRRVQ--QVKLSDGTRVRLG 81
|
|
| FHA_Cep170B |
cd22725 |
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) ... |
20-93 |
5.50e-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: 52.24 E-value: 5.50e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1959220873 20 IGRhENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQN---VAVKLipGDILRFGSAGLTYEL 93
Cdd:cd22725 25 VGR-EDCELMLQSRSVDKQHAVINYDQDTDEHWVKDLGSLNGTFVNDVRIPDqkyITLKL--NDVIRFGYDSNMYVL 98
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
13-86 |
6.18e-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: 6.18e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1959220873 13 VLNKSTTIGRHENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVN--ECHIQNVAVKLIPGDILRFGS 86
Cdd:cd22678 20 GTRLPLTIGRIQRGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNgeSISPNGRPVVLSSGDVITLGS 95
|
|
| FHA_AGGF1 |
cd22686 |
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ... |
11-86 |
1.76e-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: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 11 FFVLNKSTTIGRHENSDLVLQSPD--IDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQNVAVKLIP-----GDILR 83
Cdd:cd22686 21 FIVTATGATIGREKDHGHTIRIPElgVSKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPyplthGDELK 100
|
...
gi 1959220873 84 FGS 86
Cdd:cd22686 101 IGE 103
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
641-956 |
2.30e-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: 55.51 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 641 LIYLLEHYKKLMSQAQelqikfnssQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKA--ALEEYITQ 718
Cdd:pfam17380 274 LLHIVQHQKAVSERQQ---------QEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAiyAEQERMAM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 719 ERNRAKETL-EEERKR----------------MQELESLLA--QQKKALAKSITQEKNRVKEALEEEQTRVQELEERLAR 779
Cdd:pfam17380 345 ERERELERIrQEERKRelerirqeeiameisrMRELERLQMerQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQ 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 780 QKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEAmekekkkvqDLENRLTKQKEELELK 859
Cdd:pfam17380 425 IRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLEL---------EKEKRDRKRAEEQRRK 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 860 EQKEDVLNNKLsdalAMVEETQKTKATE-SLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRH 938
Cdd:pfam17380 496 ILEKELEERKQ----AMIEEERKRKLLEkEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAM 571
|
330
....*....|....*....
gi 1959220873 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 |
2.43e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.84 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 673 LQEKLREHLAEKEKLNEERLE-------QEEKLKAKIRQLTEEKAALEEYITQERNRAkETLEEERKRMQELESLLAQQK 745
Cdd:TIGR02169 189 LDLIIDEKRQQLERLRREREKaeryqalLKEKREYEGYELLKEKEALERQKEAIERQL-ASLEEELEKLTEEISELEKRL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 746 KALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISES--N 823
Cdd:TIGR02169 268 EEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREieE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 824 IAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLA 903
Cdd:TIGR02169 348 ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 904 ELETTKTKMIMVEERLilqqkmvKALQDEQESQrhgfEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLK 983
Cdd:TIGR02169 428 AIAGIEAKINELEEEK-------EDKALEIKKQ----EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
|
| VI_FHA |
TIGR03354 |
type VI secretion system FHA domain protein; Members of this protein family are FHA ... |
19-185 |
3.38e-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: 54.30 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 19 TIGRHENSDLVLQSPD--IDNHHALIEYNEAecSFVLQDFnSRNGTFVNECH---IQNVAVKLIPGDILRFGSagltYEL 93
Cdd:TIGR03354 27 TIGRSEDCDWVLPDPErhVSGRHARIRYRDG--AYLLTDL-STNGVFLNGSGsplGRGNPVRLEQGDRLRLGD----YEI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 94 VIENPPPVSFPWMRGPAPWPGPQPPRATQQPNQAPPPSHIPF----HQGVQPAPMQRSWSQAFPRPTVVLPAsHRRPVSA 169
Cdd:TIGR03354 100 RVSLGDPLVSRQASESRADTSLPTAGGPPTPDPAPLAQLDPLkaldQEPLSAADLDDLSAPLFPPLDARLPA-FAAPIDA 178
|
170
....*....|....*.
gi 1959220873 170 NKEMFSFVVDDARKPP 185
Cdd:TIGR03354 179 EPTMVPPFVPLPAPEP 194
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
682-1050 |
3.46e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 682 AEKEKLNEErLEQEEKLKAKIRQLTEEKAALEEYITQERNRAkETLEEERKRMQELE-SLLAQQKKALAKSITQEKNRVk 760
Cdd:TIGR02169 170 RKKEKALEE-LEEVEENIERLDLIIDEKRQQLERLRREREKA-ERYQALLKEKREYEgYELLKEKEALERQKEAIERQL- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 761 EALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRkakeamekekk 840
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKER----------- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 841 KVQDLENRLTKQKEELELKEQKEDVLNNKLsdalamvEETQKTKATESLKAESLALKLNETLAELETTKTKMimveerli 920
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREI-------EEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF-------- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 921 lqqkmvKALQDEQESQRhgfeEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERPQDPLva 1000
Cdd:TIGR02169 381 ------AETRDELKDYR----EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL-- 448
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1001 pmtESSAKDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDL 1050
Cdd:TIGR02169 449 ---EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA 495
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
221-1098 |
3.74e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 54.98 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 221 LAQQDKDEIILLL-GKEVSRLSDYEIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKeisqkcQVLDEDIDAKQKEI 299
Cdd:pfam02463 138 LVQGGKIEIIAMMkPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKL------QELKLKEQAKKALE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 300 QSLKSQISALQKGYSKV-----LCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEvsHLK 374
Cdd:pfam02463 212 YYQLKEKLELEEEYLLYldylkLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEE--ELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 375 SQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRaelRKSCTEQSVISRTLREKS 454
Cdd:pfam02463 290 LLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELE---IKREAEEEEEEELEKLQE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 455 KVEEKLQEDSRRKLLQLQEMGNRESVIKINLE-RAVGQLEHFRSQVIKATYGRAKPFRDKPVTDQQLIEKITQvtEDNIN 533
Cdd:pfam02463 367 KLEQLEEELLAKKKLESERLSSAAKLKEEELElKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESI--ELKQG 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 534 FQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHlqvSPPVSGLQKVVLDVLRHAL 613
Cdd:pfam02463 445 KLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKE---SKARSGLKVLLALIKDGVG 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 614 SWLEEVEQLLRDLGILPSSPNKGFSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEK---EKLNEE 690
Cdd:pfam02463 522 GRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKsiaVLEIDP 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 691 RLEQEEKLKAKIRQLTEEKAAL-------EEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEAL 763
Cdd:pfam02463 602 ILNLAQLDKATLEADEDDKRAKvvegilkDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQEL 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 764 EEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEAMEKEKKKVQ 843
Cdd:pfam02463 682 QEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEE 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 844 DLENRLTKQKEELELKEQKEDVLNNKL-----SDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEER 918
Cdd:pfam02463 762 KEEEKSELSLKEKELAEEREKTEKLKVeeekeEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALE 841
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 919 LILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKV--TQHHKKIEGEIATLKDNDPAPKEERpqd 996
Cdd:pfam02463 842 LKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKeeKEKEEKKELEEESQKLNLLEEKENE--- 918
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 997 pLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQQSKEL 1076
Cdd:pfam02463 919 -IEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEK 997
|
890 900
....*....|....*....|..
gi 1959220873 1077 SVLKEKMAQMSSLVEKKDRELK 1098
Cdd:pfam02463 998 ERLEEEKKKLIRAIIEETCQRL 1019
|
|
| FHA_SNIP1_DDL-like |
cd22676 |
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA ... |
20-85 |
5.18e-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: 49.60 E-value: 5.18e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1959220873 20 IGRHE-NSDLVLQSPDIDNHHALIEY-----------NEAECSFVLqDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFG 85
Cdd:cd22676 25 IGRDRrVADIPLDHPSCSKQHAVIQFrevekrnegdvIENIRPYII-DLGSTNGTFLNGEKIEpRRYYELREKDVLKFG 102
|
|
| FHA_GarA_OdhI-like |
cd22684 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium ... |
18-91 |
8.07e-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: 8.07e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1959220873 18 TTIGRHENSDLVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHIQnvAVKLIPGDILRFGSAGLTY 91
Cdd:cd22684 23 TTAGRHPESDIFLDDVTVSRRHAEFRRAEGG--FVVRDVGSLNGTYVNRERID--SAVLRNGDEVQIGKFRLVF 92
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
537-1129 |
1.12e-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: 53.43 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 537 KKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISccsHDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRHALSWL 616
Cdd:TIGR00618 220 RKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQ---QLLKQLRARIEELRAQEAVLEETQERINRARKAAPLA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 617 EEVE-------QLLRDLGILPSSPNKgfslyLIYLLEHYKKLMSQAQELQIKFNSSQETQQsllQEKLREHLAEKEKLNE 689
Cdd:TIGR00618 297 AHIKavtqieqQAQRIHTELQSKMRS-----RAKLLMKRAAHVKQQSSIEEQRRLLQTLHS---QEIHIRDAHEVATSIR 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 690 ERLEQEEKLKAKIRQLTEEKAALEEyitQERNRAKETLEEERKRMQELESLLA----QQKKALAKS---ITQEKNRVKEA 762
Cdd:TIGR00618 369 EISCQQHTLTQHIHTLQQQKTTLTQ---KLQSLCKELDILQREQATIDTRTSAfrdlQGQLAHAKKqqeLQQRYAELCAA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 763 LEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRK----VQDLENHLTQQKEISESNIAYE-KRKAKEAMEK 837
Cdd:TIGR00618 446 AITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKkavvLARLLELQEEPCPLCGSCIHPNpARQDIDNPGP 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 838 EKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEE 917
Cdd:TIGR00618 526 LTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSE 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 918 ----RLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKI-EGEIATLKDNDPAPKEE 992
Cdd:TIGR00618 606 aedmLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIrVLPKELLASRQLALQKM 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 993 RPQDPLVAPMTESSA-KDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQ 1071
Cdd:TIGR00618 686 QSEKEQLTYWKEMLAqCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFN 765
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1959220873 1072 QSKELSVLKEKMAQMSSLV----------EKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQT 1129
Cdd:TIGR00618 766 NNEEVTAALQTGAELSHLAaeiqffnrlrEEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQF 833
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
394-786 |
1.19e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 394 LKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKsCTEQSVISRTLREKSKVEEKLQEDSRRkllqLQE 473
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK-LEKLLQLLPLYQELEALEAELAELPER----LEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 474 MGNRESvikiNLERAVGQLEHFRSQVIKATYGRAKPFRDKPVTDQQLIEKITQVTEDninFQQKKWTLQKETQLSNSKQE 553
Cdd:COG4717 151 LEERLE----ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE---LQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 554 ETTENIEKLRTSLDSCQACMKISCCSHDLK-------KEVDLLQHLQVSPPVSGLQKVVLDVLRHALSWL---------- 616
Cdd:COG4717 224 ELEEELEQLENELEAAALEERLKEARLLLLiaaallaLLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLarekaslgke 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 617 ---------------EEVEQLLRDLGiLPSSPNKGFSLYLIYLLEHYKKLMSQAQELQikfnssQETQQSLLQEKLREHL 681
Cdd:COG4717 304 aeelqalpaleeleeEELEELLAALG-LPPDLSPEELLELLDRIEELQELLREAEELE------EELQLEELEQEIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 682 AEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRA--------KETLEEERKRMQELESLLAQQKKALAKSIT 753
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELeellealdEEELEEELEELEEELEELEEELEELREELA 456
|
410 420 430
....*....|....*....|....*....|...
gi 1959220873 754 QEKNRVKEAleEEQTRVQELEERLARQKEVLES 786
Cdd:COG4717 457 ELEAELEQL--EEDGELAELLQELEELKAELRE 487
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
666-824 |
1.48e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 666 QETQQSLLQEKLREHLAEKEKLNEERleqeEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQ----ELESLL 741
Cdd:COG4913 286 AQRRLELLEAELEELRAELARLEAEL----ERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLEreleERERRR 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 742 AQQKKALAkSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSiAHEKRKAKEALESEKRKVQDLENHLTQQKeise 821
Cdd:COG4913 362 ARLEALLA-ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA-LAEAEAALRDLRRELRELEAEIASLERRK---- 435
|
...
gi 1959220873 822 SNI 824
Cdd:COG4913 436 SNI 438
|
|
| FHA_EspA-like |
cd22698 |
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ... |
15-92 |
1.78e-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: 1.78e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1959220873 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 |
2.13e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.69 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 653 SQAQELQIKFNSSQEtQQSLLQEKLREHLAEKEKLNEERLEQEEKLKA---KIRQLTEEKAALEEYI---TQERNRAKET 726
Cdd:COG4942 20 DAAAEAEAELEQLQQ-EIAELEKELAALKKEEKALLKQLAALERRIAAlarRIRALEQELAALEAELaelEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 727 LEEERKRMQE-------------LESLLAQQ-------KKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLES 786
Cdd:COG4942 99 LEAQKEELAEllralyrlgrqppLALLLSPEdfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1959220873 787 SIAhEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKR 829
Cdd:COG4942 179 LLA-ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
218-789 |
2.28e-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: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 218 EEDLAQQDKDEIILLLGKEVSRLSDYEIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKEISQKcqvLDEDIDAKQK 297
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE---LEERLEELEE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 298 EIQSLKSQISALQkgyskvlcQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQN 377
Cdd:COG1196 324 ELAELEEELEELE--------EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 378 KDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKlckTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVE 457
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELE---EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 458 EKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATYGR-----AKPFRDKPVTDQQLIEKITQVTEDNI 532
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlagavAVLIGVEAAYEAALEAALAAALQNIV 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 533 NFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRHA 612
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARL 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 613 LSWLEEVEQLLRDL--------GILPSSPNKGFSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEK 684
Cdd:COG1196 633 EAALRRAVTLAGRLrevtlegeGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEA 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 685 EKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQE--------------RNRAKETLEEERKRMQELES--LLAQqkkal 748
Cdd:COG1196 713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELleeealeelpeppdLEELERELERLEREIEALGPvnLLAI----- 787
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1959220873 749 aksitqeknrvkEALEEEQTRVQELEErlarQKEVLESSIA 789
Cdd:COG1196 788 ------------EEYEELEERYDFLSE----QREDLEEARE 812
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
239-822 |
2.32e-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: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 239 RLSDYEIESKYKDVIIANLQNEVAELSQKVSETTtsRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQ---KGYSK 315
Cdd:pfam12128 259 RLSHLHFGYKSDETLIASRQEERQETSAELNQLL--RTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEdqhGAFLD 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 316 VLCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQV-QQLKEEVSHLKS----QNKDKDHQLEA---- 386
Cdd:pfam12128 337 ADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIkEQNNRDIAGIKDklakIREARDRQLAVaedd 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 387 LGSRCSVLKEELKQedAHRELREAQEK------ELKL----------CKTQIQDMEKEMKKLRAELRKSCTEQSVISRTL 450
Cdd:pfam12128 417 LQALESELREQLEA--GKLEFNEEEYRlksrlgELKLrlnqatatpeLLLQLENFDERIERAREEQEAANAEVERLQSEL 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 451 REKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHF-RSQVIKATYGRAKpfrdkpVTDQQLI-------E 522
Cdd:pfam12128 495 RQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFlRKEAPDWEQSIGK------VISPELLhrtdldpE 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 523 KITQVTEDNINFQQKKWTLQK-ETQLSNSKQEETTENIEKLRTSLDSCQACMK-ISCCSHDLKKEVDLLQhLQVSPPVSG 600
Cdd:pfam12128 569 VWDGSVGGELNLYGVKLDLKRiDVPEWAASEEELRERLDKAEEALQSAREKQAaAEEQLVQANGELEKAS-REETFARTA 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 601 LQKVVLDVLRhalsWLEEVEQLLRDLgilpsspNKGfslyliyLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREH 680
Cdd:pfam12128 648 LKNARLDLRR----LFDEKQSEKDKK-------NKA-------LAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQK 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 681 LAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEyitqERNRAKETLEEERKRmqELESL---------LAQQKKALAKS 751
Cdd:pfam12128 710 REARTEKQAYWQVVEGALDAQLALLKAAIAARRS----GAKAELKALETWYKR--DLASLgvdpdviakLKREIRTLERK 783
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1959220873 752 ITQEKNRVKEALEEE---QTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHL----TQQKEISES 822
Cdd:pfam12128 784 IERIAVRRQEVLRYFdwyQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERkaseKQQVRLSEN 861
|
|
| FHA_NBN |
cd22667 |
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ... |
11-91 |
3.74e-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: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 11 FFVLNKSTTIGRHENSDLVLQSPDIDNHHALI--EYNEAECSF-------VLQDFnSRNGTFVNECHIQNVA-VKLIPGD 80
Cdd:cd22667 15 YLLPGGEYTVGRKDCDIIIVDDSSISRKHATLtvLHPEANLSDpdtrpelTLKDL-SKYGTFVNGEKLKGGSeVTLKDGD 93
|
90
....*....|.
gi 1959220873 81 ILRFGSAGLTY 91
Cdd:cd22667 94 VITFGVLGSKF 104
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
261-973 |
3.98e-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: 51.76 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 261 VAELSQKVSETTTSRQNEKEIS---------QKCQVLDEDIDAKQKEIQSLKS---QISALQKGYSKVLCQTLSERNSEI 328
Cdd:pfam12128 203 VAILEDDGVVPPKSRLNRQQVEhwirdiqaiAGIMKIRPEFTKLQQEFNTLESaelRLSHLHFGYKSDETLIASRQEERQ 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 329 TSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKdkdhqlEALGSRCSVLKEELKQEDAHRELR 408
Cdd:pfam12128 283 ETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHG------AFLDADIETAAADQEQLPSWQSEL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 409 EAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERA 488
Cdd:pfam12128 357 ENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFN 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 489 VGQLEhfrsqvIKATYGRAKPFRDKPVTDQQLIEKITqvtedniNFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDs 568
Cdd:pfam12128 437 EEEYR------LKSRLGELKLRLNQATATPELLLQLE-------NFDERIERAREEQEAANAEVERLQSELRQARKRRD- 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 569 cQACMKISCCSHDLKKEVDLLQ--HLQVSPPVSGLqkvvLDVLR-HALSWLEEV------EQLLR---DLGILPSSPNKG 636
Cdd:pfam12128 503 -QASEALRQASRRLEERQSALDelELQLFPQAGTL----LHFLRkEAPDWEQSIgkvispELLHRtdlDPEVWDGSVGGE 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 637 FSLYLIyllehykklmsqaqelqikfnssqetqqsllqeklrehlaekeKLNEERLEqeeklkakirqlTEEKAALEEYI 716
Cdd:pfam12128 578 LNLYGV-------------------------------------------KLDLKRID------------VPEWAASEEEL 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 717 TQERNRAKETLEEERKRMQELESLLAQQKKALAKSitqeknrvKEALEEEQTRVQELEERLARQKEVLESsiahEKRKAK 796
Cdd:pfam12128 603 RERLDKAEEALQSAREKQAAAEEQLVQANGELEKA--------SREETFARTALKNARLDLRRLFDEKQS----EKDKKN 670
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 797 EALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEamekekkkvQDLENRLTKQKEELelkeqkedVLNNKLSDALAM 876
Cdd:pfam12128 671 KALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKE---------QKREARTEKQAYWQ--------VVEGALDAQLAL 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 877 VEETqKTKATESLKAESLALK--LNETLAELETTKTKMIMVE-ERLILQQKMVKALQDEQES------QRHGFEEEIMEY 947
Cdd:pfam12128 734 LKAA-IAARRSGAKAELKALEtwYKRDLASLGVDPDVIAKLKrEIRTLERKIERIAVRRQEVlryfdwYQETWLQRRPRL 812
|
730 740
....*....|....*....|....*.
gi 1959220873 948 KEQIKQHAQTIVSLEEKLQKVTQHHK 973
Cdd:pfam12128 813 ATQLSNIERAISELQQQLARLIADTK 838
|
|
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
13-85 |
7.13e-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: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 13 VLNKSTTIGRHEN------SDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQ-----NVAVKLIPGDI 81
Cdd:cd22679 21 VLDEPVKIGRSVArarpaaNNAIFDCKVLSRNHALLWYDDG--KFYLQDTKSSNGTFVNNQRLSkgseeSEPRELHSGDI 98
|
....
gi 1959220873 82 LRFG 85
Cdd:cd22679 99 VQFG 102
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
257-818 |
7.88e-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: 50.74 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 257 LQNEVAELSQKVSETTTSRQNEK--EISQKCQVLDEDIDAKQKEIQSLKSQISALQKGYSKVLCQTLS---ERNSEITSL 331
Cdd:TIGR00618 272 LRAQEAVLEETQERINRARKAAPlaAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSieeQRRLLQTLH 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 332 KNEGENLKRDNAITSgmvsslqkdilaKDEQVQQLKEEVSHLKSQNKDKDH---QLEALGSRCSVLKEELKQEDAHRELR 408
Cdd:TIGR00618 352 SQEIHIRDAHEVATS------------IREISCQQHTLTQHIHTLQQQKTTltqKLQSLCKELDILQREQATIDTRTSAF 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 409 EAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKS------------------KVEEKLQEDSRRKL-L 469
Cdd:TIGR00618 420 RDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAqslkereqqlqtkeqihlQETRKKAVVLARLLeL 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 470 QLQEMGNRESVIKINLER-AVGQLEHFRSQVIKATYGRAKPFRDKPVTDQQLIEKITQVTEDNINFQQKKWTLQKETQLS 548
Cdd:TIGR00618 500 QEEPCPLCGSCIHPNPARqDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCD 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 549 NskqeETTENIEKLRtsldscqacmkisccshdlkKEVDLLQHLqvsppvsglqkvVLDVLRHALSWLEEVEQLLRDLGI 628
Cdd:TIGR00618 580 N----RSKEDIPNLQ--------------------NITVRLQDL------------TEKLSEAEDMLACEQHALLRKLQP 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 629 LpsspnkgfslylIYLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLA----EKEKLNEERLEQEEKLKAKIRQ 704
Cdd:TIGR00618 624 E------------QDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALsirvLPKELLASRQLALQKMQSEKEQ 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 705 LTEEKAALEEYITQERNRaKETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELEERLAR--QKE 782
Cdd:TIGR00618 692 LTYWKEMLAQCQTLLREL-ETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNnnEEV 770
|
570 580 590
....*....|....*....|....*....|....*.
gi 1959220873 783 VLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKE 818
Cdd:TIGR00618 771 TAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEA 806
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
643-775 |
8.38e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.60 E-value: 8.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 643 YLLEHYKKLMSQAQElqiKFN---SSQETQQSLLQEKLREH---LAEKEKLNEERLEQEEKLKAKIRQLteeKAALEEYI 716
Cdd:PRK00409 502 NIIEEAKKLIGEDKE---KLNeliASLEELERELEQKAEEAealLKEAEKLKEELEEKKEKLQEEEDKL---LEEAEKEA 575
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1959220873 717 TQERNRAKETLEEERKRMQELESLLAQQKKalAKSITQEKNRVKEALEEEQTRVQELEE 775
Cdd:PRK00409 576 QQAIKEAKKEADEIIKELRQLQKGGYASVK--AHELIEARKRLNKANEKKEKKKKKQKE 632
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
235-811 |
9.13e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 9.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 235 KEVSRLSDYEIESKykdviiaNLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQKGYS 314
Cdd:PRK03918 152 RQILGLDDYENAYK-------NLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 315 KVlcqtlSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDhQLEALGSRCSVL 394
Cdd:PRK03918 225 KL-----EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 395 KEELKQ-EDAHRELreaqEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQ--EDSRRKLLQL 471
Cdd:PRK03918 299 SEFYEEyLDELREI----EKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHElyEEAKAKKEEL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 472 QEMGNRESVIKI----------------------NLERAVGQLEHFRSQVIKATYGRAKPFRDKPVTDQQLiekitqvTE 529
Cdd:PRK03918 375 ERLKKRLTGLTPeklekeleelekakeeieeeisKITARIGELKKEIKELKKAIEELKKAKGKCPVCGREL-------TE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 530 DNINFQQKKWTLqkETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHLQvsppvSGLQKVVLDVL 609
Cdd:PRK03918 448 EHRKELLEEYTA--ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELE-----EKLKKYNLEEL 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 610 RHALSWLEEVEQLLRDLgilpsspnKGFSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSLLQ----------EKLRE 679
Cdd:PRK03918 521 EKKAEEYEKLKEKLIKL--------KGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKeleelgfesvEELEE 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 680 HLAEKEKLNEERLE---QEEKLKAKIRQLTEEKAALEEyITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEK 756
Cdd:PRK03918 593 RLKELEPFYNEYLElkdAEKELEREEKELKKLEEELDK-AFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLEL 671
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1959220873 757 NRVKEALEEEQTRVQELEERLARQKEVLESSIAhEKRKAKEALESEKRKVQDLEN 811
Cdd:PRK03918 672 SRELAGLRAELEELEKRREEIKKTLEKLKEELE-EREKAKKELEKLEKALERVEE 725
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
654-826 |
1.07e-05 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 49.69 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 654 QAQELQIKFnSSQETQQSllqEKLrehLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEeyitQERNRAKETLEEERKR 733
Cdd:PRK11637 138 EHTGLQLIL-SGEESQRG---ERI---LAYFGYLNQARQETIAELKQTREELAAQKAELE----EKQSQQKTLLYEQQAQ 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 734 MQELESLLAQQKKALAKsitqeknrVKEALEEEQTRVQELeerlaRQKEV-LESSIAHEKRKAKEALESEKRKVQDLENh 812
Cdd:PRK11637 207 QQKLEQARNERKKTLTG--------LESSLQKDQQQLSEL-----RANESrLRDSIARAEREAKARAEREAREAARVRD- 272
|
170
....*....|....
gi 1959220873 813 ltQQKEISESNIAY 826
Cdd:PRK11637 273 --KQKQAKRKGSTY 284
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
361-983 |
1.10e-05 |
|
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: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 361 EQVQQLKEEVSHLKSQ---NKDKDHQLEalgsrcsvLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELR 437
Cdd:COG1196 213 ERYRELKEELKELEAElllLKLRELEAE--------LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 438 KscteqsvISRTLREKSKVEEKLQEDSRRKLLQLQEMGNResvikinLERAVGQLEHFRSQVIKATygrakpfrdkpvtd 517
Cdd:COG1196 285 E-------AQAEEYELLAELARLEQDIARLEERRRELEER-------LEELEEELAELEEELEELE-------------- 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 518 QQLIEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTsldscqacmkisccshDLKKEVDLLQHLQVspp 597
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE----------------LAEELLEALRAAAE--- 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 598 vsgLQKVVLDVLRHALSWLEEVEQLLRDLgilpsspnkgfslyliyllehykklmsQAQELQIKFNSSQETQQSLLQEKL 677
Cdd:COG1196 398 ---LAAQLEELEEAEEALLERLERLEEEL---------------------------EELEEALAELEEEEEEEEEALEEA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 678 REHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQE-- 755
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAva 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 756 -----KNRVKEALEEE-----QTRVQELEERLARQKEVLESS-------IAHEKRKAKEALESEKRK-VQDLENHLTQQK 817
Cdd:COG1196 528 vligvEAAYEAALEAAlaaalQNIVVEDDEVAAAAIEYLKAAkagratfLPLDKIRARAALAAALARgAIGAAVDLVASD 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 818 EISESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALK 897
Cdd:COG1196 608 LREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAER 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 898 LNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEG 977
Cdd:COG1196 688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER 767
|
....*.
gi 1959220873 978 EIATLK 983
Cdd:COG1196 768 ELERLE 773
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
425-765 |
1.29e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 49.93 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 425 MEKEMKKLRAELRKSctEQSVISRTLREKSKVE-----EKLQEDSRRKLLQLQemgnresvikINLERAVGQLEHFRSqv 499
Cdd:PRK05771 2 APVRMKKVLIVTLKS--YKDEVLEALHELGVVHiedlkEELSNERLRKLRSLL----------TKLSEALDKLRSYLP-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 500 ikatYGRAKPFRDKPVTDQQLiEKITQVTEDNINfqqkkwTLQKETqlsnskqEETTENIEKLRTSLDSCQAcmkisccs 579
Cdd:PRK05771 68 ----KLNPLREEKKKVSVKSL-EELIKDVEEELE------KIEKEI-------KELEEEISELENEIKELEQ-------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 580 hdLKKEVDLLQHLqvSPPVSGLQ-----KVVLDVLRHALswLEEVEQLLRDLGILPSSPNKGFSLY-LIYLLEHYKKLMS 653
Cdd:PRK05771 122 --EIERLEPWGNF--DLDLSLLLgfkyvSVFVGTVPEDK--LEELKLESDVENVEYISTDKGYVYVvVVVLKELSDEVEE 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 654 QAQELQIKFNSSQEtqQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAK---ETLEEE 730
Cdd:PRK05771 196 ELKKLGFERLELEE--EGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLEIELERAEalsKFLKTD 273
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1959220873 731 R----------KRMQELESLLaqqKKALAKSITQEKNRVKEALEE 765
Cdd:PRK05771 274 KtfaiegwvpeDRVKKLKELI---DKATGGSAYVEFVEPDEEEEE 315
|
|
| Yop-YscD_cpl |
pfam16697 |
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ... |
19-86 |
1.40e-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: 1.40e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1959220873 19 TIGRHENSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRFGS 86
Cdd:pfam16697 20 RIGSDPDCDIVLSDKEVSRVHLKLEVDDE--GWRLDDLGSGNGTLVNGQRVTELGIALRPGDRIELGQ 85
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
15-87 |
2.02e-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: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 15 NKSTTIGR--HENSD---LVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHIQ------NVAVKLIPGDILR 83
Cdd:cd22702 31 KQPCIIGSdpHQAISgisVVIPSPQVSELHARITCKNGA--FFLTDLGSEHGTWINDNEGRryrappNFPVRLHPSDVIE 108
|
....
gi 1959220873 84 FGSA 87
Cdd:cd22702 109 FGSD 112
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
12-85 |
2.14e-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: 44.64 E-value: 2.14e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1959220873 12 FVLNKST-TIGRHENSDLVLQSPDIDNHHALIeYNEaECSFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRFG 85
Cdd:cd22680 16 FPFDFSSvSIGRDPENVIVIPDPFVSRNHARI-TVD-SNEIYIEDLGSTNGTFVNDFKRIKGPAKLHPNDIIKLG 88
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
684-1409 |
2.19e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 684 KEKLNEERLEQ-EEKLKAKIRQLTEEKAALEEYITQERNrAKETLEEERKRMQELESLLaqqkkalaKSITQEKNRVKEA 762
Cdd:PRK03918 152 RQILGLDDYENaYKNLGEVIKEIKRRIERLEKFIKRTEN-IEELIKEKEKELEEVLREI--------NEISSELPELREE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 763 LEEEQTRVQELEER------LARQKEVLESSIAHEKRKAKE---ALESEKRKVQDLENHLTQQKEISESNIAYEKrkAKE 833
Cdd:PRK03918 223 LEKLEKEVKELEELkeeieeLEKELESLEGSKRKLEEKIREleeRIEELKKEIEELEEKVKELKELKEKAEEYIK--LSE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 834 AMEKEKKKVQDLENRLTkqkeelelkeqkedvlnnKLSDALAMVEETQKtkateslKAESLALKLNETLAELETTKTKMI 913
Cdd:PRK03918 301 FYEEYLDELREIEKRLS------------------RLEEEINGIEERIK-------ELEEKEERLEELKKKLKELEKRLE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 914 MVEERLILQQkMVKALQDEQESQRHGFE-EEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEE 992
Cdd:PRK03918 356 ELEERHELYE-EAKAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 993 RPQDPLV-APMTESSAKDMAYEHLIDdllaaqkeilsqqevIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQnvvlvqq 1071
Cdd:PRK03918 435 KGKCPVCgRELTEEHRKELLEEYTAE---------------LKRIEKELKEIEEKERKLRKELRELEKVLKKE------- 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1072 qsKELSVLKEKMAQMSSLVEK-KDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQtcdtsvqiepvhteafsssqeq 1150
Cdd:PRK03918 493 --SELIKLKELAEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKEL---------------------- 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1151 qsfsdlgvrckgsrheEVIQRQKKALSELRARIKELEKARSPDHKDHQNESFLDLKNLRmennvqkilldakpdlptlSR 1230
Cdd:PRK03918 549 ----------------EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELE-------------------ER 593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1231 IEILAPQNGLCNARFGSAMEKSGKMDVAEALELS-EKLYLDMSKTLGSLMNIKNMSGHVSMKYLSRQEREKVNQLRQ--R 1307
Cdd:PRK03918 594 LKELEPFYNEYLELKDAEKELEREEKELKKLEEElDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLElsR 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1308 DLDLVFDKITQLKNQLGRKEELLRGYEKDVEQLRRSKVSIEMYQSQVAKLEDDIYKEAEEKALLKE-ALERMEH------ 1380
Cdd:PRK03918 674 ELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKErALSKVGEiaseif 753
|
730 740 750
....*....|....*....|....*....|
gi 1959220873 1381 -QLCQEKRINRAIRQQKESVEEHELRNAKE 1409
Cdd:PRK03918 754 eELTEGKYSGVRVKAEENKVKLFVVYQGKE 783
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
667-1127 |
2.22e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 667 ETQQSLLQEKLREHLAEKE------KLNEerLEQEEK-LKAKIRQLTEEKaaleEYITQERNRAKETLEEERKRMQELES 739
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEekdlheRLNG--LESELAeLDEEIERYEEQR----EQARETRDEADEVLEEHEERREELET 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 740 LLAQQKKALAKSITQEKNR--VKEALEEEQTRVQELEERL--ARQKEVLESSIAHEKRKAKEALESEKRKVQD-LENHLT 814
Cdd:PRK02224 256 LEAEIEDLRETIAETEREReeLAEEVRDLRERLEELEEERddLLAEAGLDDADAEAVEARREELEDRDEELRDrLEECRV 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 815 QQKEISESNIAYEKRKAKEAM--EKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVE--ETQKTKATESLk 890
Cdd:PRK02224 336 AAQAHNEEAESLREDADDLEEraEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGdaPVDLGNAEDFL- 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 891 aESLALKLNETLAELETTKTKMIMVEERLilqqKMVKALQDE-------QESQRHGFEEEIMEYKEQIKQHAQTIVSLEE 963
Cdd:PRK02224 415 -EELREERDELREREAELEATLRTARERV----EEAEALLEAgkcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 964 KLQKVTQHH------KKIEGEIATLKDNdpapkeerpqdplvapmtessakdmayEHLIDDLLAAQKEIL-SQQEVIMKL 1036
Cdd:PRK02224 490 EVEEVEERLeraedlVEAEDRIERLEER---------------------------REDLEELIAERRETIeEKRERAEEL 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1037 RKDLTEAHSRMSDLRgELNEKQKMELEQNVVLVQQQSKELSVLKE------KMAQMSSLVEKKDRELKALEEALRASQEK 1110
Cdd:PRK02224 543 RERAAELEAEAEEKR-EAAAEAEEEAEEAREEVAELNSKLAELKEriesleRIRTLLAAIADAEDEIERLREKREALAEL 621
|
490
....*....|....*..
gi 1959220873 1111 HRLQLNTEKEQKPRKKT 1127
Cdd:PRK02224 622 NDERRERLAEKRERKRE 638
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
297-983 |
2.31e-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: 48.86 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 297 KEIQSLKSQISALQKGYsKVLCQTLSERNSEITSLKNEGENLKRDnaitsgmVSSLQKDILAKDEQVQQLKEEVSHLKSQ 376
Cdd:TIGR04523 40 KKLKTIKNELKNKEKEL-KNLDKNLNKDEEKINNSNNKIKILEQQ-------IKDLNDKLKKNKDKINKLNSDLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 377 NKDKDHQLEALGSRCSVLKEELKQEDAH-------------------------RELREAQEKELKLCKTQIQDMEKEMKK 431
Cdd:TIGR04523 112 IKNDKEQKNKLEVELNKLEKQKKENKKNidkflteikkkekeleklnnkyndlKKQKEELENELNLLEKEKLNIQKNIDK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 432 LRAELRKSCTEQSVIsrtlrekskveEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKatygrakpfr 511
Cdd:TIGR04523 192 IKNKLLKLELLLSNL-----------KKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN---------- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 512 dkpvTDQQLIEKITQVTEDNINFQQKkwtlQKETQLSNSKQEETTENIEKLRTSLDscqacmkisccshDLKKEVDllqh 591
Cdd:TIGR04523 251 ----TQTQLNQLKDEQNKIKKQLSEK----QKELEQNNKKIKELEKQLNQLKSEIS-------------DLNNQKE---- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 592 lqvsppvsglqkvvLDVLRHALSWLEEVEQLLRDLGILPSSPNKGFSlyliyllehykKLMSQAQELQIKFNSSQETQQS 671
Cdd:TIGR04523 306 --------------QDWNKELKSELKNQEKKLEEIQNQISQNNKIIS-----------QLNEQISQLKKELTNSESENSE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 672 llqekLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKEtLEEERKRMQELESLLAQQKKALAKS 751
Cdd:TIGR04523 361 -----KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ-KDEQIKKLQQEKELLEKEIERLKET 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 752 ITQEKNRVKEaLEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNiayekrka 831
Cdd:TIGR04523 435 IIKNNSEIKD-LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK-------- 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 832 keamekekkkvQDLENRLTKQKEELELKEQKEDVLNNklsdalamvEETQKTKATESLKAESLALKLNETLAELETTKTK 911
Cdd:TIGR04523 506 -----------KELEEKVKDLTKKISSLKEKIEKLES---------EKKEKESKISDLEDELNKDDFELKKENLEKEIDE 565
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1959220873 912 MIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLK 983
Cdd:TIGR04523 566 KNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIK 637
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
225-827 |
2.80e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 48.92 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 225 DKDEIILLLGKEVSRLSDYEIESKykDVIIANLQNEVAELSQKVSEtttsrqnekeisqkcqvLDEDIdakqKEIQSLKS 304
Cdd:COG5022 843 KAEVLIQKFGRSLKAKKRFSLLKK--ETIYLQSAQRVELAERQLQE-----------------LKIDV----KSISSLKL 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 305 QISALQKGYSKVLCQTLSERNSEITSLKNEGENLKRdnAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQL 384
Cdd:COG5022 900 VNLELESEIIELKKSLSSDLIENLEFKTELIARLKK--LLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLL 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 385 EALGSrcsvLKEELKQEdahRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDS 464
Cdd:COG5022 978 KKSTI----LVREGNKA---NSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILKPLQK 1050
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 465 RRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATYGRAK--PFRDKPVTDQQLIEKITQVteDNINFQQKKWTLQ 542
Cdd:COG5022 1051 LKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKtiNVKDLEVTNRNLVKPANVL--QFIVAQMIKLNLL 1128
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 543 KETQLSNSKQEETTENIEKLRTSLDSCQACMkisccshdlkKEVDLLQHLQVSPPVSGLQKV------VLDVLRHALSwl 616
Cdd:COG5022 1129 QEISKFLSQLVNTLEPVFQKLSVLQLELDGL----------FWEANLEALPSPPPFAALSEKrlyqsaLYDEKSKLSS-- 1196
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 617 EEVEQLLRDLGILPS-----SPNKGFSLYLI---YLLEHYKKLMSQAQELQIKFnssqETQQSLLQEKLREHLAEKEKLN 688
Cdd:COG5022 1197 SEVNDLKNELIALFSkifsgWPRGDKLKKLIsegWVPTEYSTSLKGFNNLNKKF----DTPASMSNEKLLSLLNSIDNLL 1272
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 689 EERLEQEEKLKAKIRQLTEEKAAL--EEYITQERNRAKETLEEERKRMQELESllaqqkkalaKSITQEKNRVKEALEee 766
Cdd:COG5022 1273 SSYKLEEEVLPATINSLLQYINVGlfNALRTKASSLRWKSATEVNYNSEELDD----------WCREFEISDVDEELE-- 1340
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1959220873 767 qtrvqELEERlARQKEVLESSIAH--EKRKAKEALES-------EKRKVQDLENHLTQQ--KEISESNIAYE 827
Cdd:COG5022 1341 -----ELIQA-VKVLQLLKDDLNKldELLDACYSLNPaeiqnlkSRYDPADKENNLPKEilKKIEALLIKQE 1406
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
213-932 |
3.06e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.81 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 213 AEIYVEEDLAQQDKDEIILLLGKEVSRLSDYEIESKyKDVIIANLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDI 292
Cdd:pfam02463 353 AEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSS-AAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEI 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 293 DAKQKEIQSLKSQISALQKGYSKVLCQTLSERNSEitsLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSH 372
Cdd:pfam02463 432 LEEEEESIELKQGKLTEEKEELEKQELKLLKDELE---LKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSG 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 373 LKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEmkKLRAELRKSCTEQSVISRTLRE 452
Cdd:pfam02463 509 LKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQ--KLVRALTELPLGARKLRLLIPK 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 453 KSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATYGRAKPFRDKPVTDQQLIEKITQVTEDNI 532
Cdd:pfam02463 587 LKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKA 666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 533 NFQQKKWTLqKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQhLQVSPPVSGLQKVVLDVLRHA 612
Cdd:pfam02463 667 SLSELTKEL-LEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELL-ADRVQEAQDKINEELKLLKQK 744
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 613 LSWLEEVEQLLRDLGILPSSPNKGFSLYLIYLLEHYKKLMSQAQELQIKfnssqetQQSLLQEKLREHLAEKEKLNEERL 692
Cdd:pfam02463 745 IDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKE-------EKLKAQEEELRALEEELKEEAELL 817
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 693 EQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQE 772
Cdd:pfam02463 818 EEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKE 897
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 773 LEErlarQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQ 852
Cdd:pfam02463 898 EKK----ELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELG 973
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 853 KEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDE 932
Cdd:pfam02463 974 KVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDP 1053
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
685-972 |
3.66e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 48.36 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 685 EKLNEERLEQEEKLKAKiRQLTEEKaaLEEYITQERNRAKETLEEERKRMQELESL--LAQQKKALAKSITQEKNRVKEA 762
Cdd:PLN02939 106 EAIAAIDNEQQTNSKDG-EQLSDFQ--LEDLVGMIQNAEKNILLLNQARLQALEDLekILTEKEALQGKINILEMRLSET 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 763 LE------EEQTRVQELEERLAR------QKEVLESSIAHEKRKAKEALESE----KRKVQDLENHLTQQKEISESNIAY 826
Cdd:PLN02939 183 DAriklaaQEKIHVEILEEQLEKlrnellIRGATEGLCVHSLSKELDVLKEEnmllKDDIQFLKAELIEVAETEERVFKL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 827 EKrkakeAMEKEKKKVQDLENRLTKQKE-ELELKEQKEDVLNNKLSDALAMVEETQKtkateslKAESLAL--------- 896
Cdd:PLN02939 263 EK-----ERSLLDASLRELESKFIVAQEdVSKLSPLQYDCWWEKVENLQDLLDRATN-------QVEKAALvldqnqdlr 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 897 ----KLNETLAELETTKTKMIMVEerlILQQKMvKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHH 972
Cdd:PLN02939 331 dkvdKLEASLKEANVSKFSSYKVE---LLQQKL-KLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEESKKRSLEH 406
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
254-492 |
4.16e-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: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 254 IANLQNEVAELSQKVSETttsRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQkgyskvlcQTLSERNSEITSLKN 333
Cdd:COG4942 29 LEQLQQEIAELEKELAAL---KKEEKALLKQLAALERRIAALARRIRALEQELAALE--------AELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 334 EgenLKRDNAITSGMVSSLQK-------DILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRE 406
Cdd:COG4942 98 E---LEAQKEELAELLRALYRlgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 407 LREAQEKELKLCKTQIQDMEKEMKKLRAELRKsctEQSVISRTLREKSKVEEKLQEDSRRklLQLQEMGNRESVIKINLE 486
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEK---ELAELAAELAELQQEAEELEALIAR--LEAEAAAAAERTPAAGFA 249
|
....*.
gi 1959220873 487 RAVGQL 492
Cdd:COG4942 250 ALKGKL 255
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
674-849 |
4.17e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 674 QEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYItqernrakETLEEERKRMQELESLLAQQKKALAksIT 753
Cdd:COG4717 62 QGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEEL--------EELEAELEELREELEKLEKLLQLLP--LY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 754 QEKNRVKEALEEEQTRVQELEERLARQKEVLEssiahEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKE 833
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEE-----ELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170
....*....|....*.
gi 1959220873 834 AMEKEKKKVQDLENRL 849
Cdd:COG4717 207 RLAELEEELEEAQEEL 222
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
645-1189 |
4.67e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 4.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 645 LEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITqERNRAK 724
Cdd:TIGR02168 202 LKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL-EVSELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 725 ETLEEERKRMQELESLLA---QQKKALAKSITQ---EKNRVKEALEEEQTRVQELEERLARQKEVLESsIAHEKRKAKEA 798
Cdd:TIGR02168 281 EEIEELQKELYALANEISrleQQKQILRERLANlerQLEELEAQLEELESKLDELAEELAELEEKLEE-LKEELESLEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 799 LESEKRKVQDLENHLTQQKEISE---SNIAYEKRKAKEAM---EKEKKKVQDLENRLTKQKEELELKEQKEDvlNNKLSD 872
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLEtlrSKVAQLELQIASLNneiERLEARLERLEDRRERLQQEIEELLKKLE--EAELKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 873 ALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEE--EIMEYKEQ 950
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGvkALLKNQSG 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 951 IKQH---AQTIVSLEEKLQK-------------VTQHHKKIEGEIATLKDN--------------DPAPKEERPQDPLVA 1000
Cdd:TIGR02168 518 LSGIlgvLSELISVDEGYEAaieaalggrlqavVVENLNAAKKAIAFLKQNelgrvtflpldsikGTEIQGNDREILKNI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1001 PMTESSAKDM-----AYEHLIDDLLA------------------------------------------------------ 1021
Cdd:TIGR02168 598 EGFLGVAKDLvkfdpKLRKALSYLLGgvlvvddldnalelakklrpgyrivtldgdlvrpggvitggsaktnssilerrr 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1022 -----------AQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKM-------------ELEQNVVLVQQQSKELS 1077
Cdd:TIGR02168 678 eieeleekieeLEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQisalrkdlarleaEVEQLEERIAQLSKELT 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1078 VLKEKMAQMSSLVEKKDRELKALE---EALRASQEKHRLQLNTEKEQKPRKKTQTCDTSVQIEPVHTEAFSSSQEQQSFS 1154
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEaeiEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837
|
650 660 670
....*....|....*....|....*....|....*..
gi 1959220873 1155 DLGVRCKGS--RHEEVIQRQKKALSELRARIKELEKA 1189
Cdd:TIGR02168 838 RRLEDLEEQieELSEDIESLAAEIEELEELIEELESE 874
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
650-985 |
7.34e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 7.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 650 KLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEE 729
Cdd:PTZ00121 1487 EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKA 1566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 730 ERKRMQELESLLAQQKKALAKSItqEKNRVKEALEEEQTRVQELEERLARQKEvlESSIAHEKRKAKEalesEKRKVQDL 809
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAEEAKKA--EEARIEEVMKLYEEEKKMKAEEAKKAEE--AKIKAEELKKAEE----EKKKVEQL 1638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 810 ENHLTQQKEISES-NIAYEKRKAKEAMEKEKkkvQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATES 888
Cdd:PTZ00121 1639 KKKEAEEKKKAEElKKAEEENKIKAAEEAKK---AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEK 1715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 889 LKAESLALKLNETLAELETTKTKmimVEERlilQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKV 968
Cdd:PTZ00121 1716 KKAEELKKAEEENKIKAEEAKKE---AEED---KKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789
|
330
....*....|....*..
gi 1959220873 969 TQHHKKIEGEIATLKDN 985
Cdd:PTZ00121 1790 EKRRMEVDKKIKDIFDN 1806
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
664-825 |
7.67e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 7.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 664 SSQETQQSLLQEKLREHLAEKEKLNEERleqeEKLKAKIRQLTEEKAALEEYIT---QERNRAKETLEEERKRMQE---- 736
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEY----NELQAELEALQAEIDKLQAEIAeaeAEIEERREELGERARALYRsggs 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 737 ----------------------LESLLAQQKKALA--KSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAhEK 792
Cdd:COG3883 102 vsyldvllgsesfsdfldrlsaLSKIADADADLLEelKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA-EQ 180
|
170 180 190
....*....|....*....|....*....|...
gi 1959220873 793 RKAKEALESEKRKVQDLENHLTQQKEISESNIA 825
Cdd:COG3883 181 EALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| FHA_FhaA-like |
cd22668 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
17-89 |
8.51e-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: 8.51e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1959220873 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 |
8.61e-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: 8.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 675 EKLREHLAEKEKLNEERLEQEE-----KLKAKIRQLTEEKAALEEYITqernRAKETLEEERKRMQELESLLAQQKKALA 749
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEereltEEEEEIRRLEEQVERLEAEVE----ELEAELEEKDERIERLERELSEARSEER 458
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1959220873 750 KSITQEK---------NRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKE 797
Cdd:COG2433 459 REIRKDReisrldreiERLERELEEERERIEELKRKLERLKELWKLEHSGELVPVKV 515
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
649-821 |
1.08e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.34 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 649 KKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAkirqltEEKAAleeyitQERNRAKETLE 728
Cdd:PRK09510 83 KKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQA------EEAAA------KAAAAAKAKAE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 729 EERKRMQELESLLAQQKKALAKSITQEKN------------RVKEALEEEQTRVQELEER---LARQKEVLESSIAHEKR 793
Cdd:PRK09510 151 AEAKRAAAAAKKAAAEAKKKAEAEAAKKAaaeakkkaeaeaAAKAAAEAKKKAEAEAKKKaaaEAKKKAAAEAKAAAAKA 230
|
170 180
....*....|....*....|....*...
gi 1959220873 794 KAKEALESEKRKVQDLENHLTQQKEISE 821
Cdd:PRK09510 231 AAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
666-802 |
1.09e-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: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 666 QETQQSLLQEKLREHLAEKEKLNEERLE----QEEKLKAKIRQLTEEKAALEeyitQERNRAKETLEE-ERKRMQELESL 740
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERE----RRRARLEALLAAlGLPLPASAEEF 382
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 741 LAQQK--KALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLE------SSIAHEKRKAKEALESE 802
Cdd:COG4913 383 AALRAeaAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAslerrkSNIPARLLALRDALAEA 452
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
254-816 |
1.12e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 254 IANLQNEVAELSQKVSETTTSRQNEKEisqKCQVLDEDIDAKQKEIQSLKSQISALQKGYSKVlcQTLSERN----SEIT 329
Cdd:TIGR04523 147 IKKKEKELEKLNNKYNDLKKQKEELEN---ELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNL--KKKIQKNksleSQIS 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 330 SLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELRE 409
Cdd:TIGR04523 222 ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLN 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 410 AQEKE--LKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLER 487
Cdd:TIGR04523 302 NQKEQdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQS 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 488 AVGQLEHFRSQVikatygrakpfrdkpvtdQQLIEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLD 567
Cdd:TIGR04523 382 YKQEIKNLESQI------------------NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIK 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 568 scqacmkisccshDLKKEVDLLqhlqvsppvsglqkvvldvlrhalswleevEQLLRDLGILPSSPNKGFSLYLIylleH 647
Cdd:TIGR04523 444 -------------DLTNQDSVK------------------------------ELIIKNLDNTRESLETQLKVLSR----S 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 648 YKKLMSQAQELQIKFNSSQETQQSLLQEK--LREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALE-EYITQERNRAK 724
Cdd:TIGR04523 477 INKIKQNLEQKQKELKSKEKELKKLNEEKkeLEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEdELNKDDFELKK 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 725 ETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELEErlarqKEVLESSIAHEKRKAK---EALES 801
Cdd:TIGR04523 557 ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE-----KEKKISSLEKELEKAKkenEKLSS 631
|
570
....*....|....*
gi 1959220873 802 EKRKVQDLENHLTQQ 816
Cdd:TIGR04523 632 IIKNIKSKKNKLKQE 646
|
|
| FHA_Slr1951-like |
cd22697 |
forkhead associated (FHA) domain found in Synechocystis sp. Slr1951 protein and similar ... |
19-92 |
1.28e-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: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 19 TIGRHENSDLVLQSPDIDNHHALIEY----NEAECSFVLQDF----NSRNGTFVNECHIQNVAvkLIPGDILRFG-SAGL 89
Cdd:cd22697 21 TIGRHPGNDIQIPSQQISRRHATLRRkinpNLDISFWIIDGDlegaESLNGLWVNGERILQHE--LVNGDEIALGpKIVL 98
|
...
gi 1959220873 90 TYE 92
Cdd:cd22697 99 RYQ 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
703-1402 |
1.30e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 703 RQLTEEKAALE--EYITQERNRAKETLEEERK---RMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELEERL 777
Cdd:TIGR02168 179 RKLERTRENLDrlEDILNELERQLKSLERQAEkaeRYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 778 ARQKEVLESSIAhEKRKAKEALESEKRKVQDLENHLTQQkeisesniayekrkakeamekekkkVQDLENRLTKQKEELE 857
Cdd:TIGR02168 259 TAELQELEEKLE-ELRLEVSELEEEIEELQKELYALANE-------------------------ISRLEQQKQILRERLA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 858 LKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLilqqkmvkalqDEQESQR 937
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL-----------EELEEQL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 938 HGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERPQdplvapmTESSAKDMAYEHLID 1017
Cdd:TIGR02168 382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ-------AELEELEEELEELQE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1018 DLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKM--ELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDR 1095
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLqeNLEGFSEGVKALLKNQSGLSGILGVLSELISVDEG 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1096 ELKALEEALRAsqekHRLQLNTEKEQKPRKktqtcdtsvqiepvhteafsssqeqqsfsdlgvrckgsrheeVIQRQKKA 1175
Cdd:TIGR02168 535 YEAAIEAALGG----RLQAVVVENLNAAKK------------------------------------------AIAFLKQN 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1176 LSElRARIKELekaRSPDHKDHQNESFLDLKNLRMENNVQKILLDAKPDLPT-----LSRIEILApqnglcnarfgsame 1250
Cdd:TIGR02168 569 ELG-RVTFLPL---DSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKalsylLGGVLVVD--------------- 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1251 ksgkmDVAEALELSEKLYLDMSK-TL-GSLMNIKNM----SGHVSMKYLSR-QEREKVNQlrqrDLDLVFDKITQLKNQL 1323
Cdd:TIGR02168 630 -----DLDNALELAKKLRPGYRIvTLdGDLVRPGGVitggSAKTNSSILERrREIEELEE----KIEELEEKIAELEKAL 700
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1324 GRKEELLRGYEKDVEQLRRSKVSIEMYQS----QVAKLEDDIYKEAEEKALLKEALERMEHQLCQEKRINRAIRQQKESV 1399
Cdd:TIGR02168 701 AELRKELEELEEELEQLRKELEELSRQISalrkDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA 780
|
...
gi 1959220873 1400 EEH 1402
Cdd:TIGR02168 781 EAE 783
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
709-821 |
2.13e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 709 KAALEEYITQERNRAKETLEEERKRMQEL--ESLLAQQKKALaksitQEKNRVKEALEEEQTRVQELEERLARQKEVLEs 786
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIkkEALLEAKEEIH-----KLRNEFEKELRERRNELQKLEKRLLQKEENLD- 99
|
90 100 110
....*....|....*....|....*....|....*
gi 1959220873 787 siahekrKAKEALESEKRKVQDLENHLTQQKEISE 821
Cdd:PRK12704 100 -------RKLELLEKREEELEKKEKELEQKQQELE 127
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
350-1042 |
2.38e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.73 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 350 SSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQE-DAHRELREAQEKELKLCKTQIQDMEKE 428
Cdd:TIGR00618 162 SKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMpDTYHERKQVLEKELKHLREALQQTQQS 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 429 MKKLRAE---------LRKSCTEQSVISRTLREKSKVEEKLQE--DSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRS 497
Cdd:TIGR00618 242 HAYLTQKreaqeeqlkKQQLLKQLRARIEELRAQEAVLEETQEriNRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMR 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 498 QVIKATYGRAKPFRDK-PVTDQQLIEKITQVTEDNINFQQKKWTLQKETQlsnSKQEETTENIEKLRTSLDSCQACMKIS 576
Cdd:TIGR00618 322 SRAKLLMKRAAHVKQQsSIEEQRRLLQTLHSQEIHIRDAHEVATSIREIS---CQQHTLTQHIHTLQQQKTTLTQKLQSL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 577 CCSHD------------LKKEVDLLQHLQVSPPVSGLQKVVLDVLRHALSwLEEVEQLLRDLGILPSSPNKGFSLYLIYL 644
Cdd:TIGR00618 399 CKELDilqreqatidtrTSAFRDLQGQLAHAKKQQELQQRYAELCAAAIT-CTAQCEKLEKIHLQESAQSLKEREQQLQT 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 645 LEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQE--EKLKAKIRQLTEEKAALEEYITQERNR 722
Cdd:TIGR00618 478 KEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRrmQRGEQTYAQLETSEEDVYHQLTSERKQ 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 723 AKEtLEEERKRMQELESLLAQQKKALAKSI---TQEKNRVKEALEEEQTRVQELEERLARQKEVLESSI------AHEKR 793
Cdd:TIGR00618 558 RAS-LKEQMQEIQQSFSILTQCDNRSKEDIpnlQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQdlqdvrLHLQQ 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 794 KAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDA 873
Cdd:TIGR00618 637 CSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEY 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 874 LAMVEETQKTKATESLKAESLALKLNETLAELEtTKTKMIMVEERLILQQKMVKALQDEQESQRhgFEEEIMEYKEQIKQ 953
Cdd:TIGR00618 717 DREFNEIENASSSLGSDLAAREDALNQSLKELM-HQARTVLKARTEAHFNNNEEVTAALQTGAE--LSHLAAEIQFFNRL 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 954 HAQTIVSLEEKLQKVTQHHKKIEGeIATLKDNDPAPKEERPQDPLvapmtessAKDMAYEHLIDDLLAAQKEILSQQEVI 1033
Cdd:TIGR00618 794 REEDTHLLKTLEAEIGQEIPSDED-ILNLQCETLVQEEEQFLSRL--------EEKSATLGEITHQLLKYEECSKQLAQL 864
|
....*....
gi 1959220873 1034 MKLRKDLTE 1042
Cdd:TIGR00618 865 TQEQAKIIQ 873
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
673-779 |
2.65e-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: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 673 LQEKLREHLAEKEKLNEErleQEEKLKAKIRQLTEEKAALEEYITQERNR-------------AKETLEEERKRMQELES 739
Cdd:COG0542 416 LERRLEQLEIEKEALKKE---QDEASFERLAELRDELAELEEELEALKARweaekelieeiqeLKEELEQRYGKIPELEK 492
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1959220873 740 LLAQQKKALAKSITQEKNRVKEA-----------------LEEEQTRVQELEERLAR 779
Cdd:COG0542 493 ELAELEEELAELAPLLREEVTEEdiaevvsrwtgipvgklLEGEREKLLNLEEELHE 549
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
287-425 |
2.77e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.96 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 287 VLDEDIDAKQKEIQSLKSQIS------ALQKGYSKVLCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKdilakd 360
Cdd:PRK09039 43 FLSREISGKDSALDRLNSQIAeladllSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEG------ 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1959220873 361 eQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKqedAHRELREAQEKELKLCKTQIQDM 425
Cdd:PRK09039 117 -RAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLA---ALEAALDASEKRDRESQAKIADL 177
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
685-798 |
3.40e-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: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 685 EKLNEERLEQEEKLKAKIRQLTEEKAALEEyITQERNRAKETLEEERKRMQELEsllaQQKKALAKSITQEKNRVKEALE 764
Cdd:COG4942 142 KYLAPARREQAEELRADLAELAALRAELEA-ERAELEALLAELEEERAALEALK----AERQKLLARLEKELAELAAELA 216
|
90 100 110
....*....|....*....|....*....|....
gi 1959220873 765 EEQTRVQELEERLARqkevLESSIAHEKRKAKEA 798
Cdd:COG4942 217 ELQQEAEELEALIAR----LEAEAAAAAERTPAA 246
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
641-1128 |
3.45e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.10 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 641 LIYLLEHYKKLMSQAQElQIKFNSSQETQQSLLQEKLREHLA------EKEKLNEERLEQEEKLKAK-IRQLTEEKAALE 713
Cdd:pfam05483 259 LTFLLEESRDKANQLEE-KTKLQDENLKELIEKKDHLTKELEdikmslQRSMSTQKALEEDLQIATKtICQLTEEKEAQM 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 714 EYITQERNRAKETLEEERKRMQELESLLAQQKKALAKS------ITQEKNRVKEALEEEQTRVQELEERLARQKEVL--E 785
Cdd:pfam05483 338 EELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNedqlkiITMELQKKSSELEEMTKFKNNKEVELEELKKILaeD 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 786 SSIAHEKRKAKEALESEKRKVQDLeNHLTQQKEISESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDV 865
Cdd:pfam05483 418 EKLLDEKKQFEKIAEELKGKEQEL-IFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDK 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 866 L---NNKLS-DALAMVEETQKTKA--TESLKAESLALKLNETLAELETT-KTKMIMVEERLILQQKMVKALQDEQESQRH 938
Cdd:pfam05483 497 LlleNKELTqEASDMTLELKKHQEdiINCKKQEERMLKQIENLEEKEMNlRDELESVREEFIQKGDEVKCKLDKSEENAR 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 939 GFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERP--QDPLVAPMTESSAKDMAYEHLI 1016
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNayEIKVNKLELELASAKQKFEEII 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1017 DDLlaaQKEILSQQEVIMKLRKDLTEAHSRMSD---LRGELNEKQKMELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKK 1093
Cdd:pfam05483 657 DNY---QKEIEDKKISEEKLLEEVEKAKAIADEavkLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNK 733
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1959220873 1094 DRELKALEEAL-------RASQEKHRLQLNTEKEQKPRKKTQ 1128
Cdd:pfam05483 734 EQEQSSAKAALeielsniKAELLSLKKQLEIEKEEKEKLKME 775
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
11-93 |
3.58e-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: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 11 FFVLNKSTTIGR---------HENSDLVLQSPD-IDNHHALIEYNEAECSFVLQDFnSRNGTFVNE--CHIQNVAVKLIP 78
Cdd:cd22701 12 YYVQKLEVVLGRnsknssstaADSVDIDLGPSKkISRRHARIFYDFTTQCFELSVL-GRNGVKVDGilVKPGSPPVPLRS 90
|
90
....*....|....*
gi 1959220873 79 GDILRFGSAGLTYEL 93
Cdd:cd22701 91 GSLIQIGGVLFYFLL 105
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
641-1109 |
3.81e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 641 LIYLLEHYKKLMSQAQELQIKFNSSQEtQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYiTQER 720
Cdd:TIGR04523 199 LELLLSNLKKKIQKNKSLESQISELKK-QNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK-QKEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 721 NRAKETLEEERKRMQELESLLAQQKKALAKSITQEknrVKEALEEEQTRVQELEERLARQKEVLEssiahekrKAKEALE 800
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKE---LKSELKNQEKKLEEIQNQISQNNKIIS--------QLNEQIS 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 801 SEKRKVQDLEN-HLTQQKEISESNIAYEKrkakeAMEKEKKKVQDLENrLTKQKEELELKEQKEDVLNNKLSDALAMVEE 879
Cdd:TIGR04523 346 QLKKELTNSESeNSEKQRELEEKQNEIEK-----LKKENQSYKQEIKN-LESQINDLESKIQNQEKLNQQKDEQIKKLQQ 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 880 TQKTKATESLKAESLALKLNETLAELETTKTKmimveerLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIV 959
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSV-------KELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELK 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 960 SLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERPQDPLVAPMTESSAKDMAYEHLIDDL----LAAQKEILSQQEVIMK 1035
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFelkkENLEKEIDEKNKEIEE 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1036 LRKDLTEAHSRMSDLRGELNEKQK------MELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKALEEALRASQE 1109
Cdd:TIGR04523 573 LKQTQKSLKKKQEEKQELIDQKEKekkdliKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKE 652
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
268-516 |
3.97e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 268 VSETTTSRQNEKEISQkcqvLDEDIDAKQKEIQSLKSQISALQKgyskvlcqTLSERNSEITSLKNEGENLKRDNAITSG 347
Cdd:COG4942 16 AAQADAAAEAEAELEQ----LQQEIAELEKELAALKKEEKALLK--------QLAALERRIAALARRIRALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 348 MVSSLQKDILAKDEQVQQLKEEVSHL--KSQNKDKDHQLEALGSRCSVLKEELKQE------DAHRELREAQEKELKLCK 419
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPEDFLDAVRRLQylkylaPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 420 TQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQV 499
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
250
....*....|....*..
gi 1959220873 500 IKATYGRAKPFRDKPVT 516
Cdd:COG4942 244 PAAGFAALKGKLPWPVS 260
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
258-813 |
4.07e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.04 E-value: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 258 QNEVAELSQKVSETTTSRQNEKEISQKCQvldEDIDAKQKEIQSLKS---QISALQKGYSKVLCQ-TLSERNSEITSLKN 333
Cdd:TIGR00606 425 QEQADEIRDEKKGLGRTIELKKEILEKKQ---EELKFVIKELQQLEGssdRILELDQELRKAERElSKAEKNSLTETLKK 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 334 EGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVShLKSQNKDKDHQLEALGSRCSvlkEELKQEDAHRELREAQEK 413
Cdd:TIGR00606 502 EVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEM-LTKDKMDKDEQIRKIKSRHS---DELTSLLGYFPNKKQLED 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 414 ELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEdsrrKLLQLQEMGNRESvikinleravgQLE 493
Cdd:TIGR00606 578 WLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYED----KLFDVCGSQDEES-----------DLE 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 494 HFRSQVIKATYGRAkPFRDKPVTDQQLIEKIT-----------QVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKL 562
Cdd:TIGR00606 643 RLKEEIEKSSKQRA-MLAGATAVYSQFITQLTdenqsccpvcqRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKK 721
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 563 RTSLDSCQACMKISCCSHDLK-KEVDLLQH--LQVSPPVSGLQKVVLD---VLRHALSWLEEVEQLLRDLGILpsspnKG 636
Cdd:TIGR00606 722 EKRRDEMLGLAPGRQSIIDLKeKEIPELRNklQKVNRDIQRLKNDIEEqetLLGTIMPEEESAKVCLTDVTIM-----ER 796
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 637 FSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSL-LQEKLREHLAEKE---KLNEERLEQEEKLKAKIRQLTEEKAAL 712
Cdd:TIGR00606 797 FQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQeKQHELDTVVSKIElnrKLIQDQQEQIQHLKSKTNELKSEKLQI 876
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 713 EEYItQERNRAKETLEEERKRMQELESLLAQQKK---ALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIA 789
Cdd:TIGR00606 877 GTNL-QRRQQFEEQLVELSTEVQSLIREIKDAKEqdsPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHG 955
|
570 580
....*....|....*....|....
gi 1959220873 790 HEKRKAKEALESEKRKVQDLENHL 813
Cdd:TIGR00606 956 YMKDIENKIQDGKDDYLKQKETEL 979
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
680-1030 |
4.18e-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: 45.33 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 680 HLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEyitqernraketLEEERKRMQELESLLAQQKKA----LAKsiTQE 755
Cdd:COG3096 276 HANERRELSERALELRRELFGARRQLAEEQYRLVE------------MARELEELSARESDLEQDYQAasdhLNL--VQT 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 756 KNRVKEALEEEQTRVQELEERLARQKEVLESsiAHEKR-KAKEALESEKRKVQDLENHLT--QQ--KEISESNIAYE--- 827
Cdd:COG3096 342 ALRQQEKIERYQEDLEELTERLEEQEEVVEE--AAEQLaEAEARLEAAEEEVDSLKSQLAdyQQalDVQQTRAIQYQqav 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 828 --KRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQK--------TKATESLKAESLALK 897
Cdd:COG3096 420 qaLEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKayelvckiAGEVERSQAWQTARE 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 898 LNETLAEL-------ETTKTKMIMVEERLILQQKMVKALqdEQESQRHG--------FEEEIMEYKEQIKQHAQTIVSLE 962
Cdd:COG3096 500 LLRRYRSQqalaqrlQQLRAQLAELEQRLRQQQNAERLL--EEFCQRIGqqldaaeeLEELLAELEAQLEELEEQAAEAV 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 963 EKLQKVTQHHKKIEGEIATLKDNDPA-----PKEERPQDPLVAPMTESSAKDMAYEHLID---------DLLAAQKEILS 1028
Cdd:COG3096 578 EQRSELRQQLEQLRARIKELAARAPAwlaaqDALERLREQSGEALADSQEVTAAMQQLLErereatverDELAARKQALE 657
|
..
gi 1959220873 1029 QQ 1030
Cdd:COG3096 658 SQ 659
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
667-818 |
5.09e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 667 ETQQSLLQEKLREHLAEKEKLNEERLEQEEK-------------------LKAKIRQLTEEKAALEeyitqERNRAKETL 727
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQERrealqrlaeyswdeidvasAEREIAELEAELERLD-----ASSDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 728 EEERKRMQELESLLAQQKKALAKSITQEKNRVkEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQ 807
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKEL-EQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE 769
|
170
....*....|.
gi 1959220873 808 DLENHLTQQKE 818
Cdd:COG4913 770 NLEERIDALRA 780
|
|
| FHA_Par42-like |
cd22675 |
forkhead associated (FHA) domain found in Trypanosoma brucei Parvulin 42 (TbPar42) and similar ... |
20-100 |
5.19e-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: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 20 IGRHENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQnvAVKLIP---GDILRFGSAGLTYElVIE 96
Cdd:cd22675 33 FGRSPVCDYVLEHPSISSVHAVLVFHGEQKCFVLMDLGSTNGVKLNGKRIE--KGRPLPlpvGSVIQFGFSARKYK-VRK 109
|
....
gi 1959220873 97 NPPP 100
Cdd:cd22675 110 GPPS 113
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
654-798 |
6.35e-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: 6.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 654 QAQELQIKFNSSQETQQSLLQEKLREHLAE--------------KEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQE 719
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAEllralyrlgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 720 RNR---AKETLEEERKRMQELESLLAQQKKALAKSItQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAK 796
Cdd:COG4942 159 LAElaaLRAELEAERAELEALLAELEEERAALEALK-AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
..
gi 1959220873 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 |
7.14e-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: 40.20 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 11 FFVLNKSTTIGRHENSDLVLQSPDIDNHHALIEYNEAECSfvLQDFNSRNGTFVN--------ECHIQNvavklipGDIL 82
Cdd:cd22682 15 FPITESTIVIGRSVESQVQIDDDSVSRYHAKLAVNPSAVS--IIDLGSTNGTIVNgkkipklaSCDLQN-------GDQI 85
|
....
gi 1959220873 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 |
7.48e-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: 43.60 E-value: 7.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 888 SLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQrhgfEEEIMEYKEQIKQHAQTIVSLEEKLQK 967
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 968 VTQHHKKIEGEIATLKDN-----DPAPKEERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEIlsqqevIMKLRKDLTE 1042
Cdd:COG4942 88 LEKEIAELRAELEAQKEElaellRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQ------AEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1043 AHSRMSDLRGELNEKQKMELEQnvvlvQQQSKELSVLK-EKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQ 1121
Cdd:COG4942 162 LAALRAELEAERAELEALLAEL-----EEERAALEALKaERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
....*
gi 1959220873 1122 KPRKK 1126
Cdd:COG4942 237 AAAAE 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
690-818 |
8.46e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 690 ERLEQE-EKLKAKIRQLTEEKAALEEYItqernRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQT 768
Cdd:COG4913 238 ERAHEAlEDAREQIELLEPIRELAERYA-----AARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELE 312
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1959220873 769 RVQELEERLARQKEVLESSIAHEKRKAKEALESE----KRKVQDLENHLTQQKE 818
Cdd:COG4913 313 RLEARLDALREELDELEAQIRGNGGDRLEQLEREierlERELEERERRRARLEA 366
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
348-491 |
1.07e-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: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 348 MVSSLQKDILAKDEQVQQLKEEVSHL-KSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQIQDME 426
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALkKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRY 484
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1959220873 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 |
1.24e-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: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 283 QKCQVLDEDIDAKQKEIQSLKSQISALQKgyskvLCQTLSERNSEITSLKNegenlkrdnaitsgmVSSLQKDILAKDEQ 362
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEA-----ELDALQERREALQRLAE---------------YSWDEIDVASAERE 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 363 VQQLKEEVSHLKSQNKDkdhqLEALGSRCSVLKEELkqeDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTE 442
Cdd:COG4913 670 IAELEAELERLDASSDD----LAALEEQLEELEAEL---EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1959220873 443 QSVISRTLREKsKVEEKLQEDSRRKLlqLQEMGNRESVIKINLERAVGQLE 493
Cdd:COG4913 743 ARLELRALLEE-RFAAALGDAVEREL--RENLEERIDALRARLNRAEEELE 790
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
677-816 |
1.45e-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: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 677 LREHLAEKEklneERLEQEEKLKAKIRQLTEEKAALEEyitqernrAKETLEEERKRMQELESLLAQQKKALAKSITQEK 756
Cdd:COG4913 666 AEREIAELE----AELERLDASSDDLAALEEQLEELEA--------ELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1959220873 757 NRVKEALE-EEQTRVQELEERLARqkEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQ 816
Cdd:COG4913 734 DRLEAAEDlARLELRALLEERFAA--ALGDAVERELRENLEERIDALRARLNRAEEELERA 792
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
419-789 |
1.64e-03 |
|
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: 43.12 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 419 KTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNResviKINLERAVGQLEHFRSQ 498
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD----LARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 499 VIKatygrakpfrdkpvTDQQLIEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDScqacmkiscc 578
Cdd:TIGR02168 752 LSK--------------ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE---------- 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 579 shdLKKEVDLLQ--HLQVSPPVSGLQKVVLDVLRHALSWLEEVEQLLRDLGILPSSPNKgfslyliyLLEHYKKLMSQAQ 656
Cdd:TIGR02168 808 ---LRAELTLLNeeAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE--------LEELIEELESELE 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 657 ELQIKFNSSQE------TQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEE 730
Cdd:TIGR02168 877 ALLNERASLEEalallrSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEA 956
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1959220873 731 RKRMQELESLLAQQKKALaKSITQEKNRVK----EALEEeqtrVQELEER---LARQKEVLESSIA 789
Cdd:TIGR02168 957 EALENKIEDDEEEARRRL-KRLENKIKELGpvnlAAIEE----YEELKERydfLTAQKEDLTEAKE 1017
|
|
| FHA_PPP1R8 |
cd22674 |
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ... |
16-93 |
1.66e-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: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 16 KSTTIGR-HENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFGSAGLTYEL 93
Cdd:cd22674 27 KYYLFGRnSDVCDFVLDHPSCSRVHAALVYHKHLNRVFLIDLGSTHGTFVGGIRLEpHKPQQLPIDSTLRFGASTRRYIL 106
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
667-895 |
1.66e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 667 ETQQSLLQEKLREHLAEKEKLNEE--RLEQE-EKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQ 743
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAEldALQAElEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 744 QKKA-----------LAKSITQEKNRVkEALEEEQTRVQELEERLARQKEVLEssiahekrKAKEALESEKRKVQDLENH 812
Cdd:COG3883 95 LYRSggsvsyldvllGSESFSDFLDRL-SALSKIADADADLLEELKADKAELE--------AKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 813 LTQQKEISESNIAyEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAE 892
Cdd:COG3883 166 LEAAKAELEAQQA-EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
...
gi 1959220873 893 SLA 895
Cdd:COG3883 245 SAA 247
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
254-744 |
1.73e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 254 IANLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAKQ---KEIQSLKSQISALQKGYSKvlcqtLSERNSEITS 330
Cdd:PRK03918 268 IEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELReieKRLSRLEEEINGIEERIKE-----LEEKEERLEE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 331 LKNEGENLKRDNAITSGMVSSLQkDILAKDEQVQQLKEEvshLKSQNKDKdhqlealgsrcsvLKEELKQEDAHRELREA 410
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKR---LTGLTPEK-------------LEKELEELEKAKEEIEE 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 411 QEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVE--EKLQEDSRRKLLQLQEMGNRESVIKINLERA 488
Cdd:PRK03918 406 EISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKEllEEYTAELKRIEKELKEIEEKERKLRKELREL 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 489 VGQLEHFRS-QVIKATYGRAKPFRDKpvTDQQLIEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLD 567
Cdd:PRK03918 486 EKVLKKESElIKLKELAEQLKELEEK--LKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 568 SCQACMKISCCSHDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRhALSWLEEVEQLLRDLGILPSSPNKGFSlYLIYLLEH 647
Cdd:PRK03918 564 KLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLE-LKDAEKELEREEKELKKLEEELDKAFE-ELAETEKR 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 648 YKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQER--NRAKE 725
Cdd:PRK03918 642 LEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEklEKALE 721
|
490
....*....|....*....
gi 1959220873 726 TLEEERKRMQELESLLAQQ 744
Cdd:PRK03918 722 RVEELREKVKKYKALLKER 740
|
|
| FHA_Ct664-like |
cd22696 |
forkhead associated (FHA) domain found in Chlamydia trachomatis Ct664 protein and similar ... |
8-86 |
1.84e-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: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 8 AEGFFVLNKSTTIGRHEN-SDLVLQSPDIDNHHALIEYNEAECSFVlQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGS 86
Cdd:cd22696 13 AEFFLESGKTYFIGKDPTvCDIVLQDPSISRQHARLSIDQDNRVFI-EDLSSKNGVLVNGKPIEG-KEEISGSDVISLGT 90
|
|
| FHA_Rv1747-like_rpt2 |
cd22737 |
second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
20-92 |
2.16e-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: 2.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1959220873 20 IGRHENSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQnvAVKLIPGDILRFGSAGLTYE 92
Cdd:cd22737 25 IGRASDNDIVIPEGSVSRHHATLVPTPG--GTQIRDLRSTNGTFVNGLRVD--AALLHDGDVVTIGDIDFVFE 93
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
646-799 |
2.18e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 646 EHYKKLMSQA-QELQIKFNSSQETQQSLLQ--EKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYItqernr 722
Cdd:PRK12704 64 EEIHKLRNEFeKELRERRNELQKLEKRLLQkeENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELI------ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 723 aketlEEERKRMQELESLLAQQkkalAKSITQEKnrVKEALEEEQTR-VQELEERlarqkevlessiAHE--KRKAKEAL 799
Cdd:PRK12704 138 -----EEQLQELERISGLTAEE----AKEILLEK--VEEEARHEAAVlIKEIEEE------------AKEeaDKKAKEIL 194
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
645-1061 |
2.25e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 645 LEHYKKLMSQAQELQiKFNSSQETQQSLLQE--KLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNR 722
Cdd:PRK01156 321 INKYHAIIKKLSVLQ-KDYNDYIKKKSRYDDlnNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKI 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 723 AKETLEEERKRMQELESLLAQQKKALAkSITQEKNRVKEALEEEQTRVQELEER---------LARQK-EVLESSIAHEK 792
Cdd:PRK01156 400 QEIDPDAIKKELNEINVKLQDISSKVS-SLNQRIRALRENLDELSRNMEMLNGQsvcpvcgttLGEEKsNHIINHYNEKK 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 793 RKAKEALESEKRKVQDLENHLTQQKEISEsniaYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSD 872
Cdd:PRK01156 479 SRLEEKIREIEIEVKDIDEKIVDLKKRKE----YLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNR 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 873 ALAMVEETQKTKATESLKAESL--ALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQ 950
Cdd:PRK01156 555 YKSLKLEDLDSKRTSWLNALAVisLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNK 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 951 IKQhAQTIVSLEEKLQKVTQHHKKiegEIATLKDNDPAPKEerpqdpLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQ 1030
Cdd:PRK01156 635 YNE-IQENKILIEKLRGKIDNYKK---QIAEIDSIIPDLKE------ITSRINDIEDNLKKSRKALDDAKANRARLESTI 704
|
410 420 430
....*....|....*....|....*....|.
gi 1959220873 1031 EVimkLRKDLTEAHSRMSDLRGELNEKQKME 1061
Cdd:PRK01156 705 EI---LRTRINELSDRINDINETLESMKKIK 732
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
244-829 |
2.41e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 244 EIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQkgyskvlcQTLSE 323
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLR--------ETIAE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 324 RNSEITSLKNEgenlkrdnaitsgmvsslqkdILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRcsvlKEELKQEDA 403
Cdd:PRK02224 270 TEREREELAEE---------------------VRDLRERLEELEEERDDLLAEAGLDDADAEAVEAR----REELEDRDE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 404 hrELREaqekELKLCKTQIQDMEKEMKKLRAELRKSCTEqsviSRTLREKSKVEEKLQEDSRRKllqlqemgnresviki 483
Cdd:PRK02224 325 --ELRD----RLEECRVAAQAHNEEAESLREDADDLEER----AEELREEAAELESELEEAREA---------------- 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 484 nLERAVGQLEHFRSQVIKAtygrAKPFRDKPVTDQQLIEKITQVTEDninfqqKKWTLQKETQLSNSKQEEtTENIEKLR 563
Cdd:PRK02224 379 -VEDRREEIEELEEEIEEL----RERFGDAPVDLGNAEDFLEELREE------RDELREREAELEATLRTA-RERVEEAE 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 564 TSLDS--CQACMkisccshdlkkevdllQHLQVSPPVsglqkvvlDVLRHALSWLEEVEQLLRDLGILPSSPNKGfslyl 641
Cdd:PRK02224 447 ALLEAgkCPECG----------------QPVEGSPHV--------ETIEEDRERVEELEAELEDLEEEVEEVEER----- 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 642 IYLLEHYKKLMSQAQELQIKfnssQETQQSLLQEKlREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQER- 720
Cdd:PRK02224 498 LERAEDLVEAEDRIERLEER----REDLEELIAER-RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEARe 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 721 -----NRAKETLEEERKRMQELESLLA-------------QQKKALAKSITQEKNRVKE------ALEEE--QTRVQELE 774
Cdd:PRK02224 573 evaelNSKLAELKERIESLERIRTLLAaiadaedeierlrEKREALAELNDERRERLAEkrerkrELEAEfdEARIEEAR 652
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1959220873 775 ERLARQKEVLE--SSIAHEKRKAKEALESEkrkVQDLENHLTQQKEISESNIAYEKR 829
Cdd:PRK02224 653 EDKERAEEYLEqvEEKLDELREERDDLQAE---IGAVENELEELEELRERREALENR 706
|
|
| FHA_GarA-like |
cd22720 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis glycogen accumulation ... |
12-91 |
2.62e-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: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 12 FVLNKSTT-IGRHENSDLVLQSPDIDNHHAliEYNEAECSFVLQDFNSRNGTFVNECHIqNVAVkLIPGDILRFGSAGLT 90
Cdd:cd22720 19 FLLDQAITsAGRHPDSDIFLDDVTVSRRHA--EFRLENNEFNVVDVGSLNGTYVNREPV-DSAV-LANGDEVQIGKFRLV 94
|
.
gi 1959220873 91 Y 91
Cdd:cd22720 95 F 95
|
|
| FHA_EmbR-like |
cd22669 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis transcriptional ... |
5-92 |
2.64e-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: 38.55 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 5 LKSAEGFFVLNKSTTIGRHENSDLVLQSPDIDNHHALIEYNEAECSfvLQDFNSRNGTFVNECHIQNVAVkLIPGDILRF 84
Cdd:cd22669 5 IASGRGYPLQAAATRIGRLHDNDIVLDSANVSRHHAVIVDTGTNYV--INDLRSSNGVHVQHERIRSAVT-LNDGDHIRI 81
|
....*...
gi 1959220873 85 GSAGLTYE 92
Cdd:cd22669 82 CDHEFTFQ 89
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
720-802 |
2.80e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 39.77 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 720 RNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQE----LEERLARQKEVLESSIAHEKRKA 795
Cdd:COG0711 33 QEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEEakaeAEAEAERIIAQAEAEIEQERAKA 112
|
....*..
gi 1959220873 796 KEALESE 802
Cdd:COG0711 113 LAELRAE 119
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
244-747 |
2.86e-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: 42.26 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 244 EIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKEISQKCQVLdEDIDAKQKEIQSLKSQISALQKGYSKVLCQTLSE 323
Cdd:TIGR00618 434 ELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTK-EQIHLQETRKKAVVLARLLELQEEPCPLCGSCIH 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 324 RNSEITSLKNEGENLKRDNAITSGmVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELkqeda 403
Cdd:TIGR00618 513 PNPARQDIDNPGPLTRRMQRGEQT-YAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDI----- 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 404 hrelrEAQEKELKLCKTQIQDMEKEMKKLRAELRkscteqsvisrtlREKSKVEEKLqeDSRRKLLQLQEMGNRESVIKI 483
Cdd:TIGR00618 587 -----PNLQNITVRLQDLTEKLSEAEDMLACEQH-------------ALLRKLQPEQ--DLQDVRLHLQQCSQELALKLT 646
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 484 NLERavgQLEHFRSQVIKATYGRAKPFRDKPVTDQQLIEKITQvtedniNFQQKKWTLQKETQLSNSKQEETTENIEKLR 563
Cdd:TIGR00618 647 ALHA---LQLTLTQERVREHALSIRVLPKELLASRQLALQKMQ------SEKEQLTYWKEMLAQCQTLLRELETHIEEYD 717
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 564 TSLDscQACMKISCCSHDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRHALSWLEEVEQLLRDlgilpsspnkgfslyliy 643
Cdd:TIGR00618 718 REFN--EIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTG------------------ 777
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 644 llehyKKLMSQAQELQIKFNSSQETQQSL--LQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERN 721
Cdd:TIGR00618 778 -----AELSHLAAEIQFFNRLREEDTHLLktLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLL 852
|
490 500
....*....|....*....|....*.
gi 1959220873 722 RAKETLEEERKRMQELESLLAQQKKA 747
Cdd:TIGR00618 853 KYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
297-444 |
2.90e-03 |
|
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: 40.88 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 297 KEIQSLKSQISALQKG------YSKVLCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEV 370
Cdd:pfam17078 3 KVIESLHDQIDALTKTnlqltvQSQNLLSKLEIAQQKESKFLENLASLKHENDNLSSMLNRKERRLKDLEDQLSELKNSY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 371 SHLKSQNKDKDHQLEALGSRCSVLKEELKQE--------DAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTE 442
Cdd:pfam17078 83 EELTESNKQLKKRLENSSASETTLEAELERLqiqydalvDSQNEYKDHYQQEINTLQESLEDLKLENEKQLENYQQRISS 162
|
..
gi 1959220873 443 QS 444
Cdd:pfam17078 163 ND 164
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
646-888 |
3.81e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 646 EHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKE 725
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 726 TLEEERKRMQEL---ESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELE-----ERLARQKEVLESSIAHEKRKAKE 797
Cdd:PTZ00121 1641 KEAEEKKKAEELkkaEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEalkkeAEEAKKAEELKKKEAEEKKKAEE 1720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 798 ALESEKRKVQDLENHLTQQKEisesniayEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKL--SDALA 875
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEE--------DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELdeEDEKR 1792
|
250
....*....|...
gi 1959220873 876 MVEETQKTKATES 888
Cdd:PTZ00121 1793 RMEVDKKIKDIFD 1805
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
270-492 |
3.87e-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: 41.28 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 270 ETTTSRQNEKEISQKCQVLdedIDAKQKEIQSLKSQISA----LQKGYSKVLCQTLSERN---SEITSLKNEGENLKRDN 342
Cdd:pfam09787 1 NLESAKQELADYKQKAARI---LQSKEKLIASLKEGSGVegldSSTALTLELEELRQERDllrEEIQKLRGQIQQLRTEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 343 AitsGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRelreaqekelklcKTQI 422
Cdd:pfam09787 78 Q---ELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATL-------------QSRI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1959220873 423 QDMEKEMKKLRAELR---KSCTEQSVISRTLREkskveekLQEDSRRKLLQLQEMGNRESVIKINLERAVGQL 492
Cdd:pfam09787 142 KDREAEIEKLRNQLTsksQSSSSQSELENRLHQ-------LTETLIQKQTMLEALSTEKNSLVLQLERMEQQI 207
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
675-822 |
4.04e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 675 EKLREHL-AEKEKLNE--ERLEQEEK-LKAKIRQLTEEKaaleeyitQERNRAKETLEEERKRMQE-LESLLAQQKKALA 749
Cdd:PRK00409 505 EEAKKLIgEDKEKLNEliASLEELEReLEQKAEEAEALL--------KEAEKLKEELEEKKEKLQEeEDKLLEEAEKEAQ 576
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1959220873 750 KsitqeknRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKA-KEALESekrkvqdLENHLTQQKEISES 822
Cdd:PRK00409 577 Q-------AIKEAKKEADEIIKELRQLQKGGYASVKAHELIEARKRlNKANEK-------KEKKKKKQKEKQEE 636
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
644-802 |
4.06e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 644 LLEHYKKLMSQAQELQIKFNSSQEtQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQL------------------ 705
Cdd:COG3883 35 AQAELDALQAELEELNEEYNELQA-ELEALQAEIDKLQAEIAEAEAEIEERREELGERARALyrsggsvsyldvllgses 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 706 ---------------TEEKAALEEYITQER--NRAKETLEEERKRMQELESLLAQQKKALAKSITqEKNRVKEALEEEQT 768
Cdd:COG3883 114 fsdfldrlsalskiaDADADLLEELKADKAelEAKKAELEAKLAELEALKAELEAAKAELEAQQA-EQEALLAQLSAEEA 192
|
170 180 190
....*....|....*....|....*....|....
gi 1959220873 769 RVQELEERLARQKEVLESSIAHEKRKAKEALESE 802
Cdd:COG3883 193 AAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
645-799 |
4.17e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 645 LEHYKKLMSQAQELQIKFNSSQETQQSLLQE--------KLREHLAEKEKLNEE------RLEQEEKLKAKIRQLTEEKA 710
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREEleklekllQLLPLYQELEALEAElaelpeRLEELEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 711 ALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAksitQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAH 790
Cdd:COG4717 167 ELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ----QRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
....*....
gi 1959220873 791 EKRKAKEAL 799
Cdd:COG4717 243 ERLKEARLL 251
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
649-819 |
4.57e-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: 41.70 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 649 KKLMSQAQELQIKFNSSQETQQSLLQE------------------------------KLREHLAEKEKLNEERLEQEEKL 698
Cdd:pfam01576 408 KKLEGQLQELQARLSESERQRAELAEKlsklqselesvssllneaegkniklskdvsSLESQLQDTQELLQEETRQKLNL 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 699 KAKIRQLTEEKAALEEYItQERNRAKETLEeerKRMQELESLLAQQKKALaksitQEKNRVKEALEEEQTRVQELEERLA 778
Cdd:pfam01576 488 STRLRQLEDERNSLQEQL-EEEEEAKRNVE---RQLSTLQAQLSDMKKKL-----EEDAGTLEALEEGKKRLQRELEALT 558
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1959220873 779 RQKEvlessiahEKRKAKEALESEKRKVQ----DLENHLTQQKEI 819
Cdd:pfam01576 559 QQLE--------EKAAAYDKLEKTKNRLQqeldDLLVDLDHQRQL 595
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
667-770 |
4.69e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.48 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 667 ETQQSLLQEKLREHLAEKEKLNEERLEQEEkLKAKIRQLTEEKAALEEYitqernrAKETLEEERKRMQELESLLAQQKK 746
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQ-SQALAEAQQQELVALEGL-------AAELEEKQQELEAQLEQLQEKAAE 209
|
90 100
....*....|....*....|....*....
gi 1959220873 747 ALAKSITQEKNRVKEA-----LEEEQTRV 770
Cdd:PRK11448 210 TSQERKQKRKEITDQAakrleLSEEETRI 238
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
666-810 |
4.74e-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: 41.48 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 666 QETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEE-------YITQERNRAKETLEEERKRMQELE 738
Cdd:pfam15709 357 QEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEeerkqrlQLQAAQERARQQQEEFRRKLQELQ 436
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1959220873 739 SLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELEErlarqKEVLESSIAHEKRKAKEALESEKRKVQDLE 810
Cdd:pfam15709 437 RKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAE-----EERLEYQRQKQEAEEKARLEAEERRQKEEE 503
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
257-464 |
4.99e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 257 LQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQKgyskvlcqTLSERNSEITSLKNEGE 336
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA--------EIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 337 NLKRDNAITSGMVSSLQKDILAKD--EQVQQLkEEVSHLKSQNKDKDHQLEALGSRCSVLKEEL-KQEDAHRELREAQEK 413
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLLGSESfsDFLDRL-SALSKIADADADLLEELKADKAELEAKKAELeAKLAELEALKAELEA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1959220873 414 ELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDS 464
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
19-85 |
5.24e-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: 5.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1959220873 19 TIGRHENS--DLVLQ-SPDIDNHHALIEYNeAECSFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFG 85
Cdd:cd22663 24 TVGRGLGVtyQLVSTcPLMISRNHCVLKKN-DEGQWTIKDNKSLNGVWVNGERIEpLKPYPLNEGDLIQLG 93
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
244-824 |
5.37e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.58 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 244 EIESKYKDVIiANLQNEVAELsQKVSETTTSRQNEKEISQKCQVLDEDIDAKQ---KEIQSLKSQISALQKGYSkvlcqT 320
Cdd:TIGR01612 1136 EIKKKSENYI-DEIKAQINDL-EDVADKAISNDDPEEIEKKIENIVTKIDKKKniyDEIKKLLNEIAEIEKDKT-----S 1208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 321 LSE-RNSEITSLKNEG----ENLKRDNAITSGMVSSLQKDILAKDEqVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLK 395
Cdd:TIGR01612 1209 LEEvKGINLSYGKNLGklflEKIDEEKKKSEHMIKAMEAYIEDLDE-IKEKSPEIENEMGIEMDIKAEMETFNISHDDDK 1287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 396 EELKQEDAHRE-LREAQEKELKLC-----KTQIQDMEKEMKKLRAELRKSCTEQSvisrtlrekskveeklqedsrrklL 469
Cdd:TIGR01612 1288 DHHIISKKHDEnISDIREKSLKIIedfseESDINDIKKELQKNLLDAQKHNSDIN------------------------L 1343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 470 QLQEMGNRESVIKIN-LERAVGQLEHFRSQVIKATygraKPFRDKPVTDQQLIEKItqvtEDNINFQQKKWTLqkETQLS 548
Cdd:TIGR01612 1344 YLNEIANIYNILKLNkIKKIIDEVKEYTKEIEENN----KNIKDELDKSEKLIKKI----KDDINLEECKSKI--ESTLD 1413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 549 NSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRHALSWL-----EEVEQLL 623
Cdd:TIGR01612 1414 DKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATNDHdfninELKEHID 1493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 624 RDLGI-LPSSPNKGFSLYLIYLLEHYKK----LMSQAQELQIKFNSSQETQQSllqeklREHLAEKEKLNEERLEQEEKL 698
Cdd:TIGR01612 1494 KSKGCkDEADKNAKAIEKNKELFEQYKKdvteLLNKYSALAIKNKFAKTKKDS------EIIIKEIKDAHKKFILEAEKS 1567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 699 KAKIRQLTEEKAALEEYITQ--ERNRA----KETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQE 772
Cdd:TIGR01612 1568 EQKIKEIKKEKFRIEDDAAKndKSNKAaidiQLSLENFENKFLKISDIKKKINDCLKETESIEKKISSFSIDSQDTELKE 1647
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1959220873 773 LEERLARQKEVLESSIAHEK--RKAKEALESEKRKVQDLENHLTQQKEISESNI 824
Cdd:TIGR01612 1648 NGDNLNSLQEFLESLKDQKKniEDKKKELDELDSEIEKIEIDVDQHKKNYEIGI 1701
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
257-480 |
5.39e-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: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 257 LQNEVAELSQKVSETTTS----RQNEKEISqkcqvLDEDIDAKQKEIQSLKSQISALQkgyskvlcqtlsernSEITSLK 332
Cdd:COG3206 180 LEEQLPELRKELEEAEAAleefRQKNGLVD-----LSEEAKLLLQQLSELESQLAEAR---------------AELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 333 NEGENLKRDNAITSGMVSSLQKD--ILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDahRELREA 410
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEA--QRILAS 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1959220873 411 QEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQE-DSRRKLLQLQEMGNRESV 480
Cdd:COG3206 318 LEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESlLQRLEEARLAEALTVGNV 388
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
672-737 |
5.67e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 41.39 E-value: 5.67e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1959220873 672 LLQEKLREhlaeKEKLNEERLEQEeKLKAKIRQLTEEKAALEeyitQERNRAKETLEEERKRMQEL 737
Cdd:PLN02316 250 LLEEKRRE----LEKLAKEEAERE-RQAEEQRRREEEKAAME----ADRAQAKAEVEKRREKLQNL 306
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
667-782 |
6.07e-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: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 667 ETQQSLLQEKLREHLAEKEKLnEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAK--ETLEEERKRMQELESLLAQQ 744
Cdd:COG3206 225 ESQLAEARAELAEAEARLAAL-RAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAElsARYTPNHPDVIALRAQIAAL 303
|
90 100 110
....*....|....*....|....*....|....*...
gi 1959220873 745 KKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKE 782
Cdd:COG3206 304 RAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEA 341
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
674-829 |
6.27e-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: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 674 QEKLREHLAEKEKLNEERLEQEE---KLKAKIRQLTEEKAA---LEEYITQERN-----RAKETLEEERKRM-------Q 735
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEErleALEAELDALQERREAlqrLAEYSWDEIDvasaeREIAELEAELERLdassddlA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 736 ELESLLAQQKKALaKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQ 815
Cdd:COG4913 689 ALEEQLEELEAEL-EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767
|
170
....*....|....
gi 1959220873 816 QKEISESNIAYEKR 829
Cdd:COG4913 768 RENLEERIDALRAR 781
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
656-786 |
6.39e-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: 6.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 656 QELQIKFNSSQETQQSLLQEKLREHLAEkekLNEERLEQEEKLKAK---IRQLTEEKAALEEYITQERNRAKETLEEE-- 730
Cdd:COG3206 247 AQLGSGPDALPELLQSPVIQQLRAQLAE---LEAELAELSARYTPNhpdVIALRAQIAALRAQLQQEAQRILASLEAEle 323
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1959220873 731 --RKRMQELESLLAQQKKALAKsitqeknrvkeaLEEEQTRVQELEERLARQKEVLES 786
Cdd:COG3206 324 alQAREASLQAQLAQLEARLAE------------LPELEAELRRLEREVEVARELYES 369
|
|
| FlgN |
pfam05130 |
FlgN protein; This family includes the FlgN protein and export chaperone involved in flagellar ... |
724-819 |
6.64e-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: 38.50 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 724 KETLEEERKRMQELESLLAQQKKALAK-------SITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAK 796
Cdd:pfam05130 4 IELLEEELELLEELLELLEEEQEALKAgdiealeELTEEKQELLQKLAQLEKERRELLAELGLSPEEATLSELLAKEEED 83
|
90 100
....*....|....*....|...
gi 1959220873 797 EALESEKRKVQDLENHLTQQKEI 819
Cdd:pfam05130 84 PELRELWQELLELLERLKELNEL 106
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
666-1189 |
6.69e-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: 41.21 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 666 QETQQSLLQEKLREHLAEKEKLNEERLEQE---EKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQE-LESLL 741
Cdd:TIGR02169 221 REYEGYELLKEKEALERQKEAIERQLASLEeelEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEkIGELE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 742 AQQkkALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAhEKRKAKEALESEKRKVQDLENHLTQQ-KEIS 820
Cdd:TIGR02169 301 AEI--ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIE-EERKRRDKLTEEYAELKEELEDLRAElEEVD 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 821 ESNIAY--EKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKL 898
Cdd:TIGR02169 378 KEFAETrdELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 899 NETLAELETTKTKMIMVEERLILQQKMVKALQ---DEQESQRHGFEEEIMEYK---EQIKQHAQTIVSLEEKLQKV-TQH 971
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKELSKLQrelAEAEAQARASEERVRGGRaveEVLKASIQGVHGTVAQLGSVgERY 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 972 HKKIEGE-------------------IATLKDNDPAP------KEERPQDPLVAPMTESSAKDMAY-------------- 1012
Cdd:TIGR02169 538 ATAIEVAagnrlnnvvveddavakeaIELLKRRKAGRatflplNKMRDERRDLSILSEDGVIGFAVdlvefdpkyepafk 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1013 ------------------------------------------------------------------EHLIDDLLAAQKEI 1026
Cdd:TIGR02169 618 yvfgdtlvvedieaarrlmgkyrmvtlegelfeksgamtggsraprggilfsrsepaelqrlrerlEGLKRELSSLQSEL 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1027 LSQQEVIMKLRKDLTEAHSRMSDLRGELN------EKQKMELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKAL 1100
Cdd:TIGR02169 698 RRIENRLDELSQELSDASRKIGEIEKEIEqleqeeEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKL 777
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 1101 EEAL---RASQEKHRLQ-----LNTEKEQKPRKKTQTCDTSVQIEPVHTEAFSSSQEQQSFSDLGVRCKGSRHE--EVIQ 1170
Cdd:TIGR02169 778 EEALndlEARLSHSRIPeiqaeLSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSieKEIE 857
|
650
....*....|....*....
gi 1959220873 1171 RQKKALSELRARIKELEKA 1189
Cdd:TIGR02169 858 NLNGKKEELEEELEELEAA 876
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
670-829 |
6.91e-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: 40.51 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 670 QSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEyitqERNRAKETLEEERKRMQELESllaqQKKALA 749
Cdd:pfam09787 17 ARILQSKEKLIASLKEGSGVEGLDSSTALTLELEELRQERDLLRE----EIQKLRGQIQQLRTELQELEA----QQQEEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 750 KSITQEKNRVKEALEEEQTRVQELEERLARQKEVLeSSIAHEKRKAKEALESEKRK----VQDLENHLTQQKEISESNIA 825
Cdd:pfam09787 89 ESSREQLQELEEQLATERSARREAEAELERLQEEL-RYLEEELRRSKATLQSRIKDreaeIEKLRNQLTSKSQSSSSQSE 167
|
....
gi 1959220873 826 YEKR 829
Cdd:pfam09787 168 LENR 171
|
|
| FHA_CHK2 |
cd22666 |
forkhead associated (FHA) domain found in checkpoint kinase 2 (Chk2) and similar proteins; ... |
10-65 |
6.92e-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: 6.92e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1959220873 10 GFFVL---NKSTTIGRHENSDLVLQSPDIDNH---------HALI--EYNEAECSFV-LQDFnSRNGTFVN 65
Cdd:cd22666 10 GFSSLdlvKDEYTFGRDKSCDYCFDSPALKKTsyyrtyskkHFRIfrEKGSKNTYPVfLEDH-SSNGTFVN 79
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
290-726 |
7.89e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 7.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 290 EDIDAKQKEIQSLKSQISALQKgyskvLCQTLSERNSEITSLKNEGENLKRDnaitsgmvsslqKDILAKDEQVQQLKEE 369
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAE-----LQEELEELEEELEELEAELEELREE------------LEKLEKLLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 370 VSHLKSQNKDKDHQLEALGSRCSVLKEELKQ----EDAHRELREAQEKELKLC----KTQIQDMEKEMKKLRAELRKSCT 441
Cdd:COG4717 134 LEALEAELAELPERLEELEERLEELRELEEEleelEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 442 EQSVISRTLREKSKVEEKLQEDSR-----RKLLQLQEMGNRESVIkINLERAVGQLEHFRSQVIKA--------TYGRAK 508
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELEaaaleERLKEARLLLLIAAAL-LALLGLGGSLLSLILTIAGVlflvlgllALLFLL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 509 PFRDKPVTDQQLIEKITQVTEDNInfQQKKWT-----LQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLK 583
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEEL--EEEELEellaaLGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 584 KEVDLLQHLQVSPpvsglqkvvLDVLRHALSWLEEVEQLLRDLGILPSSPNKGFSLYLIYLLEHYKK-LMSQAQELQIKF 662
Cdd:COG4717 371 EIAALLAEAGVED---------EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEeLEEELEELEEEL 441
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1959220873 663 NSSQETQQSLLQEKLR-----EHLAEKEKLnEERLEQEEKLKAKIRQLTEEKAAL---EEYITQERNRAKET 726
Cdd:COG4717 442 EELEEELEELREELAEleaelEQLEEDGEL-AELLQELEELKAELRELAEEWAALklaLELLEEAREEYREE 512
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
359-438 |
8.04e-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: 8.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 359 KDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRK 438
Cdd:COG2433 411 EEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREIERLERELEEERERIEE 490
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
219-442 |
8.21e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.68 E-value: 8.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 219 EDLAQQDKDEIILLLGK---EVSRLSDY-EIESKYKDVIIANLQnevaelSQKVSETTTSRQNEKEISQKcqvLDEDIDA 294
Cdd:PRK05771 34 EDLKEELSNERLRKLRSlltKLSEALDKlRSYLPKLNPLREEKK------KVSVKSLEELIKDVEEELEK---IEKEIKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 295 KQKEIQSLKSQISALQKgySKVLCQTLSERNSEItSLKNEGENLKrdnaITSGMVSSLQKDILAKDEQVQQLKEEvshlk 374
Cdd:PRK05771 105 LEEEISELENEIKELEQ--EIERLEPWGNFDLDL-SLLLGFKYVS----VFVGTVPEDKLEELKLESDVENVEYI----- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 375 SQNKDKDhqlealgsRCSVLKEELKQEDAHRELREAQEKELKL------------CKTQIQDMEKEMKKLRAELRKSCTE 442
Cdd:PRK05771 173 STDKGYV--------YVVVVVLKELSDEVEEELKKLGFERLELeeegtpselireIKEELEEIEKERESLLEELKELAKK 244
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
673-797 |
9.01e-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: 40.00 E-value: 9.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 673 LQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEErkrmqelESLLAQQKKALAKSI 752
Cdd:smart00787 145 LKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCD-------PTELDRAKEKLKKLL 217
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1959220873 753 TQEKNRVKEaLEEEQTRVQELE---ERLARQKEVLESSIAHEKRKAKE 797
Cdd:smart00787 218 QEIMIKVKK-LEELEEELQELEskiEDLTNKKSELNTEIAEAEKKLEQ 264
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
654-766 |
9.38e-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: 39.96 E-value: 9.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 654 QAQELQIKFNSSQE-TQQSLLQekLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERK 732
Cdd:pfam02841 173 KAEEVLQEFLQSKEaVEEAILQ--TDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIE 250
|
90 100 110
....*....|....*....|....*....|....*
gi 1959220873 733 RM-QELESLLAQQKKALAKSITQEKNRVKEALEEE 766
Cdd:pfam02841 251 KMeAEREQLLAEQERMLEHKLQEQEELLKEGFKTE 285
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
219-472 |
9.51e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.66 E-value: 9.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 219 EDLAQ--QDKDEIILLLGK-EVSRLSDYEIESKYKDviiaNLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAK 295
Cdd:PLN02939 131 EDLVGmiQNAEKNILLLNQaRLQALEDLEKILTEKE----ALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 296 QKEIqslkSQISALQKGYSKVLCQTLSERNSEITSLKNEGENLKrdnaitsGMVSSLQKdilaKDEQVQQLKEEVSHLKS 375
Cdd:PLN02939 207 RNEL----LIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLK-------AELIEVAE----TEERVFKLEKERSLLDA 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 376 QNKDKDHQLeaLGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQI----------QDMEKEMKKLRAELRKSCT--EQ 443
Cdd:PLN02939 272 SLRELESKF--IVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVekaalvldqnQDLRDKVDKLEASLKEANVskFS 349
|
250 260 270
....*....|....*....|....*....|
gi 1959220873 444 SVISRTLREKSK-VEEKLQEDSRRKLLQLQ 472
Cdd:PLN02939 350 SYKVELLQQKLKlLEERLQASDHEIHSYIQ 379
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
654-850 |
9.60e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 9.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 654 QAQELQIKFNSSQETQQSLLQE--KLREHLAEKEKlneeRLeQEEKLKAKIRQLTEEKAALEEYIT---QERNRAKETLE 728
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQlpELRKELEEAEA----AL-EEFRQKNGLVDLSEEAKLLLQQLSeleSQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959220873 729 EERKRMQELESLLAQQKKALAK-SITQEKNRVKEALEEEQTRVQELEER----------LARQKEVLESSIAHEKRKAKE 797
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPElLQSPVIQQLRAQLAELEAELAELSARytpnhpdviaLRAQIAALRAQLQQEAQRILA 316
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1959220873 798 ALESEKRKVQDLENHLTQQKEISESNIAyekrkakeamekekkKVQDLENRLT 850
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLA---------------ELPELEAELR 354
|
|
| |
