|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
19-114 |
5.03e-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: 5.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 19 KAYLKSAEGFFVLN-KSTTIGRHeNSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQNVAVKLIPGD 97
Cdd:cd22700 1 KGYLKSSDGIFQLDpKVTTIGRE-GCDLVLQSPGVEEQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAPGD 79
|
90
....*....|....*..
gi 1370451798 98 ILRFGSAGLTYELVIEN 114
Cdd:cd22700 80 VLRFGFGGLPYELVVDN 96
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
35-101 |
1.53e-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: 1.53e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370451798 35 TTIGRHENSDLVLQSPDIDNHHALIEYNEaECSFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRF 101
Cdd:pfam00498 1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDG-GGRFYLEDLGSTNGTFVNGQRLGPEPVRLKDGDVIRL 66
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
663-1205 |
5.71e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.38 E-value: 5.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 663 EHYKKLMSQAQELQIKFNSSQ----ETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQER- 737
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKlrelEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYe 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 738 -NRAKETLEEERKRMQELESLLAQQKKALAksitQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEAL 816
Cdd:COG1196 293 lLAELARLEQDIARLEERRRELEERLEELE----EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 817 ESEKRKVQDLENHLTQQKEisESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEE 896
Cdd:COG1196 369 EAEAELAEAEEELEELAEE--LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 897 TQKTKATESLKAESLALKLNETLAELETTKTKMImVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQH----- 971
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALA-ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglaga 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 972 -------------AQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERP----QDPLVAPMTESSAKDMAYEHLID 1034
Cdd:COG1196 526 vavligveaayeaALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPldkiRARAALAAALARGAIGAAVDLVA 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1035 DLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQQS-------KELSVLKEKMAQMSSLV 1107
Cdd:COG1196 606 SDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSltggsrrELLAALLEAEAELEELA 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1108 EKKDRELKALEEALRASQEKHRLQLntEKEQKPRKKTQTCDTSVQIEPVHTEAFSSSQEQQSFSDLGVRCKGSRHEEVIQ 1187
Cdd:COG1196 686 ERLAEEELELEEALLAEEEEERELA--EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE 763
|
570
....*....|....*...
gi 1370451798 1188 RQKKALSELRARIKELEK 1205
Cdd:COG1196 764 ELERELERLEREIEALGP 781
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
28-109 |
1.22e-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: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 28 FFVLNKSTTIGRHENSDLVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGLT 107
Cdd:cd00060 14 FPLTKGVVTIGRSPDCDIVLDDPSVSRRHARIEVDGGG--VYLEDLGSTNGTFVNGKRITP-PVPLQDGDVIRLGDTTFR 90
|
..
gi 1370451798 108 YE 109
Cdd:cd00060 91 FE 92
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
29-110 |
4.65e-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: 4.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 29 FVLNKS-TTIGRHENSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGLT 107
Cdd:COG1716 16 FPLDGGpLTIGRAPDNDIVLDDPTVSRRHARIRRDGG--GWVLEDLGSTNGTFVNGQRVTE-PAPLRDGDVIRLGKTELR 92
|
...
gi 1370451798 108 YEL 110
Cdd:COG1716 93 FRL 95
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
292-1080 |
7.08e-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: 80.50 E-value: 7.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 292 RQNEKEISQkcqvLDEDIDAKQKEIQSLKSQISALQKGYSKVLcQTLSERNSEITSL-KNEGENLKRDNAITSGMVSSLQ 370
Cdd:TIGR02169 233 EALERQKEA----IERQLASLEEELEKLTEEISELEKRLEEIE-QLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 371 KDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRcsvLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLR 450
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE---IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 451 AELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATygrakpfrdk 530
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE---------- 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 531 pvtdqqliEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKE-----VDL 605
Cdd:TIGR02169 455 --------WKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvHGT 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 606 LQHL-QVSPPVSG---------LQKVVLD---VLRHALSWLEE-------------VEQLLRDLGILPSSPNKGFSLYLI 659
Cdd:TIGR02169 527 VAQLgSVGERYATaievaagnrLNNVVVEddaVAKEAIELLKRrkagratflplnkMRDERRDLSILSEDGVIGFAVDLV 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 660 YLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEK---LREHLAEKEKL-------NEERLEQEEKLKAKIRQLTEEKAAL 729
Cdd:TIGR02169 607 EFDPKYEPAFKYVFGDTLVVEDIEAARRLMGKYRmvtLEGELFEKSGAmtggsraPRGGILFSRSEPAELQRLRERLEGL 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 730 E---EYITQERNRAKETLEEERKRMQELESLLAQQKKALaKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIA 806
Cdd:TIGR02169 687 KrelSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI-EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 807 hEKRKAKEALESEKRKVQDLENHLTQQKeISESNIAYEKrkakeamekEKKKVQDLENRLTKQKEELELKEQKEDVLNNK 886
Cdd:TIGR02169 766 -RIEELEEDLHKLEEALNDLEARLSHSR-IPEIQAELSK---------LEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 887 LSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLIlqqkmvkalqdeqesqrhGFEEEIMEYKE 966
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG------------------DLKKERDELEA 896
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 967 QIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDndpapkEERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQ 1046
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSELKAKLEALEE------ELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
|
810 820 830
....*....|....*....|....*....|....
gi 1370451798 1047 QEVIMKLRKDLTEAHSRMSDLRGelnEKQKMELE 1080
Cdd:TIGR02169 971 EPVNMLAIQEYEEVLKRLDELKE---KRAKLEEE 1001
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
261-970 |
7.11e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.02 E-value: 7.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 261 EIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQKGYsKVLCQTLSE 340
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL-YALANEISR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 341 RNSEITSLKNEGENLKRDNAITSGMVSSL--QKDILAKD-----EQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKE 413
Cdd:TIGR02168 300 LEQQKQILRERLANLERQLEELEAQLEELesKLDELAEElaeleEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 414 ELKQE----DAHRELREAQEKELKLCKTQIQDMEKEMKKLRAEL-----RKSCTEQSVISRTLREKSKVEEKLQEDSRRK 484
Cdd:TIGR02168 380 QLETLrskvAQLELQIASLNNEIERLEARLERLEDRRERLQQEIeellkKLEEAELKELQAELEELEEELEELQEELERL 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 485 LLQLQEMGNRESVIKINLERAVGQLEHFRSQV--IKATYGRAKPFRD--KPVTDQQL-IEKITQVTEDNINFQqKKWTLQ 559
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQARLdsLERLQENLEGFSEgvKALLKNQSgLSGILGVLSELISVD-EGYEAA 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 560 KETQLSNSKQEETTEN-------IEKLRTSLDSCQACMKISCCSHDlKKEVDLLQHLQVSPPVSG-----------LQKV 621
Cdd:TIGR02168 539 IEAALGGRLQAVVVENlnaakkaIAFLKQNELGRVTFLPLDSIKGT-EIQGNDREILKNIEGFLGvakdlvkfdpkLRKA 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 622 VLDVLRHaLSWLEEVEQLLRDLGILPSSPN----------KGFSLY----------------LIYLLEHYKKLMSQAQEL 675
Cdd:TIGR02168 618 LSYLLGG-VLVVDDLDNALELAKKLRPGYRivtldgdlvrPGGVITggsaktnssilerrreIEELEEKIEELEEKIAEL 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 676 QIKFNSSQETQQSLLQE--KLREHLAEKEKLNEERLEQEEKLKAKIRQLTE-------EKAALEEYITQERNR------A 740
Cdd:TIGR02168 697 EKALAELRKELEELEEEleQLRKELEELSRQISALRKDLARLEAEVEQLEEriaqlskELTELEAEIEELEERleeaeeE 776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 741 KETLEEERkrmQELESLLAQQKKALAKSitqeknrvKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEK 820
Cdd:TIGR02168 777 LAEAEAEI---EELEAQIEQLKEELKAL--------REALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 821 RKVQDLENHLTQQKEISESNIAYEKrkAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKT 900
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEE--LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 901 KATESLKAESLALKLNETLAELettktkmimvEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQ 970
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQERL----------SEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
308-1002 |
7.29e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.02 E-value: 7.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 308 DIDAKQKEIQSLKSQISALQKGYSKvLCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEV 387
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEE-LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 388 SHLKSQNKDKDHQLEALGSRCSVLKEELKQedahrelreaQEKELKLCKTQIQDMEKEMKKLRAELRKScteqsviSRTL 467
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAE----------LEEKLEELKEELESLEAELEELEAELEEL-------ESRL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 468 REKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATYGRAKPFRDKPVTD-QQLIEKITQVTE 546
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAElEELEEELEELQE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 547 DNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHL--QVSPPVS-------- 616
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsGILGVLSelisvdeg 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 617 -----------GLQKVV---LDVLRHALSWLEEVEQ---------LLRDLGILPSSPN--------KGFSLYLIYLLEHY 665
Cdd:TIGR02168 535 yeaaieaalggRLQAVVvenLNAAKKAIAFLKQNELgrvtflpldSIKGTEIQGNDREilkniegfLGVAKDLVKFDPKL 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 666 KKLMS-------------QAQELQIKFN---------------------SSQETQQSLLQEKlrehlAEKEKLNEERLEQ 711
Cdd:TIGR02168 615 RKALSyllggvlvvddldNALELAKKLRpgyrivtldgdlvrpggvitgGSAKTNSSILERR-----REIEELEEKIEEL 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 712 EEklkaKIRQLTEEKAALEeyitQERNRAKETLEEERKRMQELESLLAQQKKALAKsITQEKNRVKEALEEEQTRVQELE 791
Cdd:TIGR02168 690 EE----KIAELEKALAELR----KELEELEEELEQLRKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELTELE 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 792 ERLARQKEVLESSIAHEKRkAKEALESEKRKVQDLENHLTQQKEISESniayekrkakeamekekkkvqdLENRLTKQKE 871
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAE-AEAEIEELEAQIEQLKEELKALREALDE----------------------LRAELTLLNE 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 872 ELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQE 951
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1370451798 952 SqrhgFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDN 1002
Cdd:TIGR02168 898 E----LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
37-110 |
4.80e-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: 4.80e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370451798 37 IGRhENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHI-QNVAVKLIPGDILRFGSAGLTYEL 110
Cdd:cd22704 21 VGR-EDCDLILQSRSVDKQHAVITYDQIDNEFKIKDLGSLNGTFVNDSRIpEQTYITLKLGDSIRFGYDTNVYRF 94
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
29-109 |
3.54e-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: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 29 FVLNK-STTIGRHENSDLVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHI--QNVAVKLIPGDILRFGSAG 105
Cdd:cd22665 16 FPLYEgENVIGRDPSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNKVRlkPNVRYELIDGDLLLFGDVK 93
|
....
gi 1370451798 106 LTYE 109
Cdd:cd22665 94 CQYV 97
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
29-103 |
7.05e-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: 7.05e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370451798 29 FVLNKST-TIGRHENSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIqNVAVKLIPGDILRFGS 103
Cdd:cd22693 13 FPIDKSGiTIGRADDNDLVLSDDFVSSRHARIYLQGS--SWYLEDLGSTNGTFVNGNRV-TQPVVVQPGDTIRIGA 85
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
690-1409 |
2.08e-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: 68.93 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 690 LQEKLREH-----LAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQernraketLEEERKRMQELESLLAQQKKA 764
Cdd:TIGR02168 218 LKAELRELelallVLRLEELREELEELQEELKEAEEELEELTAELQELEEK--------LEELRLEVSELEEEIEELQKE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 765 LaKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYE 844
Cdd:TIGR02168 290 L-YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 845 krkakeameKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNET-LAELE 923
Cdd:TIGR02168 369 ---------ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAeLKELQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 924 TTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQK----------VTQHHKKIE 993
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENlegfsegvkaLLKNQSGLS 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 994 GEIATLKDNDPAPKE----------ERPQDPLVApmTESSAKDmAYEHL-----------------IDDLLAAQKEILSQ 1046
Cdd:TIGR02168 520 GILGVLSELISVDEGyeaaieaalgGRLQAVVVE--NLNAAKK-AIAFLkqnelgrvtflpldsikGTEIQGNDREILKN 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1047 QEVIMKLRKDLTEAHSRMS--------------DLRGELNEKQKMELEQNVV----------------------LVQQQS 1090
Cdd:TIGR02168 597 IEGFLGVAKDLVKFDPKLRkalsyllggvlvvdDLDNALELAKKLRPGYRIVtldgdlvrpggvitggsaktnsSILERR 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1091 KELSVLKEKMAQMSSLVEKKDRELKALEEALRASQEKHRlQLNTEKEQKPRKKTQTcDTSVQIEPVHTEAFSSSQEQQSF 1170
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELE-QLRKELEELSRQISAL-RKDLARLEAEVEQLEERIAQLSK 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1171 SDLGVRCKGSRHEEVIQRQKKALSELRARIKELEkARSPDHKDHQNESFLDLKNLRMENNVQKILLDAKpdlptLSRIEI 1250
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELE-AQIEQLKEELKALREALDELRAELTLLNEEAANL-----RERLES 828
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1251 LAPQNGLCNARFGSAMEKSGKM-----DVAEALELSEKLYLDMSKTLGSLMNIKnMSGHVSMKYLSRQEREKVNQLRQRD 1325
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELsedieSLAAEIEELEELIEELESELEALLNER-ASLEEALALLRSELEELSEELRELE 907
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1326 ldlvfDKITQLKNQLGRKEELLRGYEKDVEQLrrsKVSIEMYQSQVAKLEDDIYKEAEEKALLKEA-LERMEHQLcqeKR 1404
Cdd:TIGR02168 908 -----SKRSELRRELEELREKLAQLELRLEGL---EVRIDNLQERLSEEYSLTLEEAEALENKIEDdEEEARRRL---KR 976
|
....*
gi 1370451798 1405 INRAI 1409
Cdd:TIGR02168 977 LENKI 981
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
303-869 |
3.39e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 303 QVLDEDIDAKQKEIQSLKSQISALQKgyskvlcqTLSERNSEITSLKNEGENLKRDnaitsgmVSSLQKDILAKDEQVQQ 382
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEA--------ELAELEAELEELRLELEELELE-------LEEAQAEEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 383 LKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKlckTQIQDMEKEMKKLRAELRKSCTEQSV 462
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE---EELEEAEAELAEAEEALLEAEAELAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 463 ISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATygrakpfrdkpVTDQQLIEKIT 542
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE-----------EEEEEEEEALE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 543 QVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQAcmkisccSHDLKKEVDLLQHLQVSPP----VSGL 618
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA-------RLLLLLEAEADYEGFLEGVkaalLLAG 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 619 QKVVLDVLRHALSWLEEVEQLLRDLGILPSSPNKGFSL-----YLIYLLEHYKKLMSQAQELQIK-FNSSQETQQSLLQE 692
Cdd:COG1196 519 LRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDevaaaAIEYLKAAKAGRATFLPLDKIRaRAALAAALARGAIG 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 693 KLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQE 772
Cdd:COG1196 599 AAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 773 KNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEAM 852
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
|
570
....*....|....*..
gi 1370451798 853 EKEKKKVQDLENRLTKQ 869
Cdd:COG1196 759 PPDLEELERELERLERE 775
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
692-1150 |
8.00e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.47 E-value: 8.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 692 EKLREHLAEKEKLNEERLEQEEKLKA-KIRQLTEEKAALEEyiTQERNRAKETLEEERKRMQELESLLAQQKKALAKSIT 770
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKAEEKKKAdEAKKKAEEAKKADE--AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA 1485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 771 QEknrVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKE 850
Cdd:PTZ00121 1486 DE---AKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEE 1562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 851 AMEKEKKKVQDLENRLTKQKEELELKEQKEdvlnnKLSDALAMVEETQKTKATESLKAESLALKLNETLAELEttktkmi 930
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRKAEEAKKAEEA-----RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE------- 1630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 931 mvEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKieGEIATLKDNDPAPKEER 1010
Cdd:PTZ00121 1631 --EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK--AAEALKKEAEEAKKAEE 1706
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1011 PQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQqs 1090
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE-- 1784
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1091 kelsvLKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQTCDTS 1150
Cdd:PTZ00121 1785 -----LDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSK 1839
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
684-987 |
9.15e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 9.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 684 ETQQSLlqEKLREHLAEKEKlNEERLEQEEKLKAKIRQLTEEKAALE-EYITQERNRAKETLEEERKRMQELESLLAQQK 762
Cdd:COG1196 183 ATEENL--ERLEDILGELER-QLEPLERQAEKAERYRELKEELKELEaELLLLKLRELEAELEELEAELEELEAELEELE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 763 KALAKsITQEKNRVKEALEEEQTRVQEL---EERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISEs 839
Cdd:COG1196 260 AELAE-LEAELEELRLELEELELELEEAqaeEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE- 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 840 niayEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETL 919
Cdd:COG1196 338 ----ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370451798 920 AELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQ 987
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
254-796 |
1.15e-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: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 254 VSRLSDYEIESKYKDVIIANLQNEVAELSQKVSETTTSRQnekEISQKCQVLDEDIDAKQKEIQSLKSQISALQKGySKV 333
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYELLAELARLEQD-IAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 334 LCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKE 413
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 414 ELKQEDAHRELREAQEKELKL----CKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQ 489
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEaeeaLLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 490 EMGNRESVIKINLERAVGQLEHFRSQ--VIKATYGRAKPFRD--KPVTDQQLIEKITQVTEDNINFQQKKWTLQkETQLS 565
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARllLLLEAEADYEGFLEgvKAALLLAGLRGLAGAVAVLIGVEAAYEAAL-EAALA 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 566 NSKQEETTEN-------IEKLRTSLDSCQACMKIScCSHDLKKEVDLLQHLQVSPPVSGLQkvVLDVLRHALSWLEEVEQ 638
Cdd:COG1196 546 AALQNIVVEDdevaaaaIEYLKAAKAGRATFLPLD-KIRARAALAAALARGAIGAAVDLVA--SDLREADARYYVLGDTL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 639 LLRDLGILPSSPNKGFSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAK 718
Cdd:COG1196 623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370451798 719 IRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAksITQEKNRVKEALEEEQTRVQELEERLAR 796
Cdd:COG1196 703 EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE--EALEELPEPPDLEELERELERLEREIEA 778
|
|
| FHA_DUN1-like |
cd22683 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ... |
34-102 |
1.28e-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: 1.28e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370451798 34 STTIGRHENSDLVLQSPDIDNHHALIEYnEAECSFVLqDFNSRNGTFVNECHIQNVAVKLIPGDILRFG 102
Cdd:cd22683 22 VTTIGRSRSCDLVLSDPSISRFHAELRL-EQNGINVI-DNNSANGTFINGKRIKGKTYILKNGDIIVFG 88
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
230-985 |
2.43e-10 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 65.38 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 230 AEIYVEEDLAQQDKDEIILLLGKEVSRLSDYEIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDI 309
Cdd:pfam02463 244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEK 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 310 DAKQKEIQSLKSQISALQKGYSKVLCQTLSERNSEITSLKNEGENLKRDNAITSGmVSSLQKDILAKDEQVQQLKEEVSH 389
Cdd:pfam02463 324 KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAK-KKLESERLSSAAKLKEEELELKSE 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 390 LKSQNKDKDHQLEALGSRCSVL-KEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLR 468
Cdd:pfam02463 403 EEKEAQLLLELARQLEDLLKEEkKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKL 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 469 EKSKVE---EKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEH---FRSQVIKATYGRAKPFRDKPVTDQQLIEKIT 542
Cdd:pfam02463 483 QEQLELllsRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHgrlGDLGVAVENYKVAISTAVIVEVSATADEVEE 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 543 QVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHLQVSPPVSGLQKVV 622
Cdd:pfam02463 563 RQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAK 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 623 -----LDVLRHALSWLEEVEQLLRDLGILPSSPNKGFSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREH 697
Cdd:pfam02463 643 akesgLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEEL 722
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 698 LAEKEKLNEERLEQEEKL---KAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKN 774
Cdd:pfam02463 723 LADRVQEAQDKINEELKLlkqKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEE 802
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 775 RvKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLEnHLTQQKEISESNIAYEKRKAKEAMEK 854
Cdd:pfam02463 803 L-RALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEE-ELERLEEEITKEELLQELLLKEEELE 880
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 855 EKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEE 934
Cdd:pfam02463 881 EQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEE 960
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1370451798 935 RLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKV 985
Cdd:pfam02463 961 RNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAI 1011
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
250-999 |
3.83e-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: 64.70 E-value: 3.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 250 LGKEVSRLSDYEIESKYKDviIANLQNEVAELSQKVSEtttSRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQKG 329
Cdd:TIGR02169 277 LNKKIKDLGEEEQLRVKEK--IGELEAEIASLERSIAE---KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 330 YSKvLCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDI--------------LAKDEQVQQLKEEVSHLKSQNK 395
Cdd:TIGR02169 352 RDK-LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLeklkreinelkrelDRLQEELQRLSEELADLNAAIA 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 396 DKDHQLEALGSRCSVLKEELKQEDAHRE----LREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKS 471
Cdd:TIGR02169 431 GIEAKINELEEEKEDKALEIKKQEWKLEqlaaDLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 472 KVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHF-----------------RSQVIKATYGRAKPFRDKPVTD 534
Cdd:TIGR02169 511 AVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNvvveddavakeaiellkRRKAGRATFLPLNKMRDERRDL 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 535 QQLIEK-ITQVTEDNINFQQK-----KWTLQkETQLsnskqeetTENIEKLRTSLDSCQAcmkisccshdLKKEVDLLQH 608
Cdd:TIGR02169 591 SILSEDgVIGFAVDLVEFDPKyepafKYVFG-DTLV--------VEDIEAARRLMGKYRM----------VTLEGELFEK 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 609 lqvSPPVSGLQKVVLDVLRHALSWLEEVEQLLRDLGILPSSPNKgfslyLIYLLEHYKKLMSQAQELQikfnsSQETQQS 688
Cdd:TIGR02169 652 ---SGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSS-----LQSELRRIENRLDELSQEL-----SDASRKI 718
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 689 LLQEKLREHLAEKEKLNEERLEQ-EEKLKAKIRQLTEEKAALEEYItQERNRAKETLEEERKRMQELESLLAQQKkalAK 767
Cdd:TIGR02169 719 GEIEKEIEQLEQEEEKLKERLEElEEDLSSLEQEIENVKSELKELE-ARIEELEEDLHKLEEALNDLEARLSHSR---IP 794
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 768 SITQEKNRVKEALEEEQTRVQELEERLAR---QKEVLESSIAHEKRKAKEALESEKrkvqdlenhlTQQKEISESNIayE 844
Cdd:TIGR02169 795 EIQAELSKLEEEVSRIEARLREIEQKLNRltlEKEYLEKEIQELQEQRIDLKEQIK----------SIEKEIENLNG--K 862
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 845 KRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESlalkLNETLAELET 924
Cdd:TIGR02169 863 KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA----LEEELSEIED 938
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370451798 925 TKTKMIMVEERLILQQKMVKALQDEQESQRhGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATL 999
Cdd:TIGR02169 939 PKGEDEEIPEEELSLEDVQAELQRVEEEIR-ALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
277-866 |
8.80e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 8.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 277 EVAELSQKVSETTTSRQNE------KEISQKCQVLDEDIDAKQKEIQSLKSQISALQKGYSKVLcQTLSERNSEITSLKN 350
Cdd:COG1196 210 EKAERYRELKEELKELEAEllllklRELEAELEELEAELEELEAELEELEAELAELEAELEELR-LELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 351 EGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEK 430
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 431 ELklcKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLE 510
Cdd:COG1196 369 EA---EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 511 HFRSQVIKATygrakpfrdkpvTDQQLIEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDScqacm 590
Cdd:COG1196 446 EAAEEEAELE------------EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE----- 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 591 kisccshDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRHALSWLEEVEQ--LLRDLGILpsspnkgfSLYLIYLLEHYKKL 668
Cdd:COG1196 509 -------GVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQniVVEDDEVA--------AAAIEYLKAAKAGR 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 669 MSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEER 748
Cdd:COG1196 574 ATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEG 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 749 KRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLEN 828
Cdd:COG1196 654 EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733
|
570 580 590
....*....|....*....|....*....|....*...
gi 1370451798 829 HLTQQKEISESNIAYEkrKAKEAMEKEKKKVQDLENRL 866
Cdd:COG1196 734 REELLEELLEEEELLE--EEALEELPEPPDLEELEREL 769
|
|
| FHA_PS1-like |
cd22691 |
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) ... |
36-110 |
1.37e-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: 1.37e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370451798 36 TIGRHENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFGSAGLTYEL 110
Cdd:cd22691 32 VVGRHPDCDIVLDHPSISRFHLEIRIIPSRRKITLTDLSSVHGTWVNGQRIEpGVPVELEEGDTVRLGASTRVYRL 107
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
36-102 |
2.31e-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: 2.31e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370451798 36 TIGRHENSDLVLQSPDIDNHHALIEYN----EAECSFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFG 102
Cdd:cd22677 25 VFGRLPGCDVVLEHPSISRYHAVLQYRgdadDHDGGFYLYDLGSTHGTFLNKQRIPpKQYYRLRVGHVLKFG 96
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
720-1129 |
2.82e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.01 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 720 RQLTEEKAALEEYiTQERNRAKETLEEERKRMQELESLLAqqkkalaksitqEKNRVKEALEEEQTRVQELEERLARQKE 799
Cdd:TIGR02169 156 RKIIDEIAGVAEF-DRKKEKALEELEEVEENIERLDLIID------------EKRQQLERLRREREKAERYQALLKEKRE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 800 VLESSIAHEKRKAKEALESEKRKVQDLENHLTQ-QKEISESNIAYEKRKAKeamekekkkVQDLENRLTKQKEELELKeq 878
Cdd:TIGR02169 223 YEGYELLKEKEALERQKEAIERQLASLEEELEKlTEEISELEKRLEEIEQL---------LEELNKKIKDLGEEEQLR-- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 879 kedvLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFE 958
Cdd:TIGR02169 292 ----VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 959 EEIMEYKEQIKQHAQT---IVSLEEKLQKVTQHHKKIEGEIatlkdndpapkeerpqdplvapmtessakdmayEHLIDD 1035
Cdd:TIGR02169 368 DLRAELEEVDKEFAETrdeLKDYREKLEKLKREINELKREL---------------------------------DRLQEE 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1036 LLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELnEKQKMELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELK 1115
Cdd:TIGR02169 415 LQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI-KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
|
410
....*....|....
gi 1370451798 1116 ALEEALRASQEKHR 1129
Cdd:TIGR02169 494 EAEAQARASEERVR 507
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
703-1138 |
3.68e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 703 KLNEERLEQEEKLKAkirqlTEEKAALEEYITQERNRAKETLEEER---KRMQELESLLAQQKKALAKSITQEKNRVKEA 779
Cdd:COG1196 169 KYKERKEEAERKLEA-----TEENLERLEDILGELERQLEPLERQAekaERYRELKEELKELEAELLLLKLRELEAELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 780 LEEEQTRVQELEERLARQKEVLESSIAhEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAkeamekekkkv 859
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELE-ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR----------- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 860 QDLENRLTKQKEELelkeqkedvlnnklsdalamvEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQ 939
Cdd:COG1196 312 RELEERLEELEEEL---------------------AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 940 QKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERpqdplvapm 1019
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE--------- 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1020 tessakdMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQQSKELSVLKEK 1099
Cdd:COG1196 442 -------EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1370451798 1100 MAQMSSLVEKKDREL----KALEEALRASQEKHRLQLNTEKEQ 1138
Cdd:COG1196 515 LLAGLRGLAGAVAVLigveAAYEAALEAALAAALQNIVVEDDE 557
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
35-82 |
3.80e-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: 3.80e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1370451798 35 TTIGRHENS-DLVLQSPDIDNHHALIEYNEAECsFVLQDFNSRNGTFVN 82
Cdd:smart00240 1 VTIGRSSEDcDIQLDGPSISRRHAVIVYDGGGR-FYLIDLGSTNGTFVN 48
|
|
| FHA_Ki67 |
cd22673 |
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ... |
28-109 |
9.26e-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: 9.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 28 FFVLNKSTTIGRHENSDLVLQSPDIDNHHALIEYNEAECsFVLQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGLT 107
Cdd:cd22673 16 FPLTKKSCTFGRDLSCDIRIQLPGVSREHCRIEVDENGK-AYLENLSTTNPTLVNGKAIEK-SAELKDGDVITIGGRSFR 93
|
..
gi 1370451798 108 YE 109
Cdd:cd22673 94 FE 95
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
36-174 |
1.02e-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: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 36 TIGRHENSDLVLQSPD--IDNHHALIEYneAECSFVLQDfNSRNGTFVNECHI---QNVAVKLIPGDILRFGSagltYEL 110
Cdd:COG3456 29 TIGRSADCDWVLPDPDrsVSRRHAEIRF--RDGAFCLTD-LSTNGTFLNGSDHplgPGRPVRLRDGDRLRIGD----YEI 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370451798 111 V--IENPPPVSFPWMRGPAPWPGPQPPRATQQPNqAPPPshiPFHQGVQPAPMQRSWSQAFPRPTV 174
Cdd:COG3456 102 RveISGEDEGADDPLAAAPEPAVSSPSNLSDTEA-APDA---ALAFSFSLDPLEALDEAATEAPAT 163
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
692-1133 |
1.26e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 692 EKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLE--EERKRMQELESLLAQQKKAL---- 765
Cdd:PTZ00121 1332 DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKAdelk 1411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 766 -----------AKSITQEKNRVKEALE--EEQTRVQELEERLARQKEVLESS-IAHEKRKAKEALE--SEKRKVQDLENH 829
Cdd:PTZ00121 1412 kaaaakkkadeAKKKAEEKKKADEAKKkaEEAKKADEAKKKAEEAKKAEEAKkKAEEAKKADEAKKkaEEAKKADEAKKK 1491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 830 LTQ-QKEISESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVlnnKLSDALAMVEETQKT----KATE 904
Cdd:PTZ00121 1492 AEEaKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK---KKADELKKAEELKKAeekkKAEE 1568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 905 SLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQK 984
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 985 VTQHHKkiEGEIATLKDNDPAPKEERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKeilsqqevIMKLRKDLTEAHSRM 1064
Cdd:PTZ00121 1649 AEELKK--AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK--------AEELKKKEAEEKKKA 1718
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370451798 1065 SDLRG--ELNEKQKMELEQNVVLVQQQSKELSV---LKEKMAQMSSLVEKKDRELKA-----LEEALRASQEKHRLQLN 1133
Cdd:PTZ00121 1719 EELKKaeEENKIKAEEAKKEAEEDKKKAEEAKKdeeEKKKIAHLKKEEEKKAEEIRKekeavIEEELDEEDEKRRMEVD 1797
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
667-1027 |
1.31e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 667 KLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKA----KIRQLTEEKAALEEYITQERNRAKE 742
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAdeakKKAEEAKKKADEAKKAAEAKKKADE 1514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 743 TLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQElEERLARQKEVLESSIAHEKRKAKEALESEKRK 822
Cdd:PTZ00121 1515 AKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE-EKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 823 VQDLENHLTQQKEI--SESNIAYEKRKAKEAMEKEKKKVQDLEN--RLTKQKEELELKEQKEDVLNNKLSDALAMVEETQ 898
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMkaEEAKKAEEAKIKAEELKKAEEEKKKVEQlkKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 899 KTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSL 978
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE 1753
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1370451798 979 EEKlQKVTQHHKKIEGEIATLKDNDPAPKEE--RPQDPLVAPMTESSAKDM 1027
Cdd:PTZ00121 1754 EEK-KKIAHLKKEEEKKAEEIRKEKEAVIEEelDEEDEKRRMEVDKKIKDI 1803
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
692-1129 |
1.86e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 692 EKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKE--TLEEERKRMQELESLLAQQKKALAKsI 769
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkELKEKAEEYIKLSEFYEEYLDELRE-I 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 770 TQEKNRVKEALEEEQTRVQELEERLARQKEVLEssiahEKRKAKEALESEKRKVQDLENHLTQQKEISEsniaYEKRKAK 849
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKEERLEELKK-----KLKELEKRLEELEERHELYEEAKAKKEELER----LKKRLTG 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 850 EAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKA---------TESLKAESLA---LKLNE 917
Cdd:PRK03918 384 LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgrelTEEHRKELLEeytAELKR 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 918 TLAELETTKT-------------KMIMVEERLILQQKMVKALQD-EQESQRHGFEEEIMEYKE----------------- 966
Cdd:PRK03918 464 IEKELKEIEEkerklrkelreleKVLKKESELIKLKELAEQLKElEEKLKKYNLEELEKKAEEyeklkekliklkgeiks 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 967 ------QIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERPQDPLVAPMTESSAKDMAyehliDDLLAAQ 1040
Cdd:PRK03918 544 lkkeleKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAE-----KELEREE 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1041 KEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKM----ELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKA 1116
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK 698
|
490
....*....|...
gi 1370451798 1117 LEEALRASQEKHR 1129
Cdd:PRK03918 699 LKEELEEREKAKK 711
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
678-1452 |
1.90e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.38 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 678 KFNSSQETQQSLLQEKLREHLAEKeKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESL 757
Cdd:PTZ00121 1099 KAEEAKKTETGKAEEARKAEEAKK-KAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKK 1177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 758 LAQQKKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEAL--ESEKRKVQDLENHLTQQKe 835
Cdd:PTZ00121 1178 AEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKkdAEEAKKAEEERNNEEIRK- 1256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 836 ISESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELElkeqkedvlnnKLSDALAMVEETQKtKATESLKAESLALKL 915
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEA-----------KKAEEKKKADEAKK-KAEEAKKADEAKKKA 1324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 916 NETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEyKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGE 995
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK-KEEAKKKADAAKKKAEEKKKADEAKKKAEED 1403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 996 IATLKDNDPAPKEERPQDPLVAPMTESSAKDMAyehliddllaaqKEILSQQEVIMKLRKDLTEAhSRMSDLRGELNEKQ 1075
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEAKKKAEEKKKADEA------------KKKAEEAKKADEAKKKAEEA-KKAEEAKKKAEEAK 1470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1076 KMELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQTCDTSVQIEP 1155
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADE 1550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1156 VHT-----EAFSSSQEQQSFSDLGVRCKGSRHEEVIQRQKKALSELRARIKELEKARSPDHKDHQNESFLDLKNLRMENN 1230
Cdd:PTZ00121 1551 LKKaeelkKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE 1630
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1231 VQKILLDAKPDLPTlsrieilapqnglcNARFGSAMEKSGKMDVAEALELSEKLYLDMSKTLGSLMNIKNMSGHVSMKYL 1310
Cdd:PTZ00121 1631 EKKKVEQLKKKEAE--------------EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1311 SRQEREKVNQLRQRDLDLVfDKITQLKNQ----LGRKEELLRGYEKDVEQLRRSKVSiEMYQSQVAKLEDDIYKEAEEKA 1386
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAEEK-KKAEELKKAeeenKIKAEEAKKEAEEDKKKAEEAKKD-EEEKKKIAHLKKEEEKKAEEIR 1774
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370451798 1387 LLKEALerMEHQLCQEKRINRAIRQQKrrvfvemVKNRMQNS-NSQVGTRKASLKMDQEREMLRKET 1452
Cdd:PTZ00121 1775 KEKEAV--IEEELDEEDEKRRMEVDKK-------IKDIFDNFaNIIEGGKEGNLVINDSKEMEDSAI 1832
|
|
| FHA_MEK1-like |
cd22670 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ... |
32-109 |
2.61e-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: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 32 NKSTTIGRHENSDLVLQSPDIDNHHALIE---YNEAECSFV-LQDfNSRNGTFVNECHI-QNVAVKLIPGDILRF-GSAG 105
Cdd:cd22670 21 NQVITIGRSPSCDIVINDPFVSRTHCRIYsvqFDESSAPLVyVED-LSSNGTYLNGKLIgRNNTVLLSDGDVIEIaHSAT 99
|
....
gi 1370451798 106 LTYE 109
Cdd:cd22670 100 FVYV 103
|
|
| FHA_Cep170A |
cd22724 |
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar ... |
37-102 |
2.84e-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: 2.84e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370451798 37 IGRhENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHI-QNVAVKLIPGDILRFG 102
Cdd:cd22724 25 VGR-DDCELMLQSRSVDKQHAVINYDASTDEHKVKDLGSLNGTFVNDVRIpEQTYITLKLDDKLRFG 90
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
34-102 |
5.12e-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: 5.12e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370451798 34 STTIGRHENSDLVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHIQnvAVKLIPGDILRFG 102
Cdd:cd22694 17 SVRIGRDPDADVRLDDPRVSRRHALLEFDGDG--WVYTDLGSRNGTYLNGRRVQ--QVKLSDGTRVRLG 81
|
|
| FHA_Cep170B |
cd22725 |
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) ... |
37-110 |
5.46e-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: 5.46e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370451798 37 IGRhENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQN---VAVKLipGDILRFGSAGLTYEL 110
Cdd:cd22725 25 VGR-EDCELMLQSRSVDKQHAVINYDQDTDEHWVKDLGSLNGTFVNDVRIPDqkyITLKL--NDVIRFGYDSNMYVL 98
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
30-103 |
6.14e-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: 6.14e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370451798 30 VLNKSTTIGRHENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVN--ECHIQNVAVKLIPGDILRFGS 103
Cdd:cd22678 20 GTRLPLTIGRIQRGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNgeSISPNGRPVVLSSGDVITLGS 95
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
658-973 |
1.38e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 56.29 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 658 LIYLLEHYKKLMSQAQelqikfnssQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKA--ALEEYITQ 735
Cdd:pfam17380 274 LLHIVQHQKAVSERQQ---------QEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAiyAEQERMAM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 736 ERNRAKETL-EEERKR----------------MQELESLLA--QQKKALAKSITQEKNRVKEALEEEQTRVQELEERLAR 796
Cdd:pfam17380 345 ERERELERIrQEERKRelerirqeeiameisrMRELERLQMerQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQ 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 797 QKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEAmekekkkvqDLENRLTKQKEELELK 876
Cdd:pfam17380 425 IRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLEL---------EKEKRDRKRAEEQRRK 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 877 EQKEDVLNNKLsdalAMVEETQKTKATE-SLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRH 955
Cdd:pfam17380 496 ILEKELEERKQ----AMIEEERKRKLLEkEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAM 571
|
330
....*....|....*....
gi 1370451798 956 GFEEEIM-EYKEQIKQHAQ 973
Cdd:pfam17380 572 EREREMMrQIVESEKARAE 590
|
|
| FHA_AGGF1 |
cd22686 |
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ... |
6-103 |
1.52e-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: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 6 PCRLFIYGKTERMKAylksaeG--FFVLNKSTTIGRHENSDLVLQSPD--IDNHHALIEYNEAECSFVLQDFNSRNGTFV 81
Cdd:cd22686 3 PCIRVIVVESPSLQV------GslFIVTATGATIGREKDHGHTIRIPElgVSKFHAEIYYDDDEQSYTIVDLGSQNGTYL 76
|
90 100
....*....|....*....|....*..
gi 1370451798 82 NECHIQNVAVKLIP-----GDILRFGS 103
Cdd:cd22686 77 NGVRISQPKEKSDPyplthGDELKIGE 103
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
635-1424 |
1.72e-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: 56.13 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 635 EVEQLLRDLGILPSSPN-------------------------KGFSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSL 689
Cdd:pfam02463 120 EVAELLESQGISPEAYNflvqggkieiiammkperrleieeeAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 690 LQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSI 769
Cdd:pfam02463 200 LKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEK 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 770 TQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAK 849
Cdd:pfam02463 280 EKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 850 EAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTktkm 929
Cdd:pfam02463 360 ELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE---- 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 930 imvEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQT-IVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKE 1008
Cdd:pfam02463 436 ---EESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETqLVKLQEQLELLLSRQKLEERSQKESKARSGLKVL 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1009 ERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQ 1088
Cdd:pfam02463 513 LALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLK 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1089 QSKELSVLKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQTCDTSVQIEPVHTEAFSSSQEQQ 1168
Cdd:pfam02463 593 SIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELT 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1169 SFSDLGVRCKGSRHEEVIQRQKKALSELRARIKELEKARSPDHKDHQNESFLDLKNLRMENNVQKILLDAKPDLPTLSRI 1248
Cdd:pfam02463 673 KELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEE 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1249 EILAPQNGLCNARFGSAMEKSGKMDVAEALELSEKLYLDMSKTLGSLMNIKNMsghvsMKYLSRQEREKVNQLRQRDLDL 1328
Cdd:pfam02463 753 EKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRA-----LEEELKEEAELLEEEQLLIEQE 827
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1329 VFDKITQLKNQLGRKEELLRGYEKDVEQLRRSKVSI---EMYQSQVAKLEDDIYKEAEEKALLKEALERME-HQLCQEKR 1404
Cdd:pfam02463 828 EKIKEEELEELALELKEEQKLEKLAEEELERLEEEItkeELLQELLLKEEELEEQKLKDELESKEEKEKEEkKELEEESQ 907
|
810 820
....*....|....*....|
gi 1370451798 1405 INRAIRQQKRRVFVEMVKNR 1424
Cdd:pfam02463 908 KLNLLEEKENEIEERIKEEA 927
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
690-1000 |
1.92e-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: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 690 LQEKLREHLAEKEKLNEERLE-------QEEKLKAKIRQLTEEKAALEEYITQERNRAkETLEEERKRMQELESLLAQQK 762
Cdd:TIGR02169 189 LDLIIDEKRQQLERLRREREKaeryqalLKEKREYEGYELLKEKEALERQKEAIERQL-ASLEEELEKLTEEISELEKRL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 763 KALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISES--N 840
Cdd:TIGR02169 268 EEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREieE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 841 IAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLA 920
Cdd:TIGR02169 348 ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 921 ELETTKTKMIMVEERLilqqkmvKALQDEQESQrhgfEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLK 1000
Cdd:TIGR02169 428 AIAGIEAKINELEEEK-------EDKALEIKKQ----EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
238-1115 |
2.16e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 55.75 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 238 LAQQDKDEIILLL-GKEVSRLSDYEIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKeisqkcQVLDEDIDAKQKEI 316
Cdd:pfam02463 138 LVQGGKIEIIAMMkPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKL------QELKLKEQAKKALE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 317 QSLKSQISALQKGYSKV-----LCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEvsHLK 391
Cdd:pfam02463 212 YYQLKEKLELEEEYLLYldylkLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEE--ELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 392 SQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRaelRKSCTEQSVISRTLREKS 471
Cdd:pfam02463 290 LLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELE---IKREAEEEEEEELEKLQE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 472 KVEEKLQEDSRRKLLQLQEMGNRESVIKINLE-RAVGQLEHFRSQVIKATYGRAKPFRDKPVTDQQLIEKITQvtEDNIN 550
Cdd:pfam02463 367 KLEQLEEELLAKKKLESERLSSAAKLKEEELElKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESI--ELKQG 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 551 FQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHlqvSPPVSGLQKVVLDVLRHAL 630
Cdd:pfam02463 445 KLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKE---SKARSGLKVLLALIKDGVG 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 631 SWLEEVEQLLRDLGILPSSPNKGFSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEK---EKLNEE 707
Cdd:pfam02463 522 GRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKsiaVLEIDP 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 708 RLEQEEKLKAKIRQLTEEKAAL-------EEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEAL 780
Cdd:pfam02463 602 ILNLAQLDKATLEADEDDKRAKvvegilkDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQEL 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 781 EEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEAMEKEKKKVQ 860
Cdd:pfam02463 682 QEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEE 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 861 DLENRLTKQKEELELKEQKEDVLNNKL-----SDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEER 935
Cdd:pfam02463 762 KEEEKSELSLKEKELAEEREKTEKLKVeeekeEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALE 841
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 936 LILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKV--TQHHKKIEGEIATLKDNDPAPKEERpqd 1013
Cdd:pfam02463 842 LKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKeeKEKEEKKELEEESQKLNLLEEKENE--- 918
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1014 pLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQQSKEL 1093
Cdd:pfam02463 919 -IEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEK 997
|
890 900
....*....|....*....|..
gi 1370451798 1094 SVLKEKMAQMSSLVEKKDRELK 1115
Cdd:pfam02463 998 ERLEEEKKKLIRAIIEETCQRL 1019
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
699-1067 |
2.53e-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: 55.46 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 699 AEKEKLNEErLEQEEKLKAKIRQLTEEKAALEEYITQERNRAkETLEEERKRMQELE-SLLAQQKKALAKSITQEKNRVk 777
Cdd:TIGR02169 170 RKKEKALEE-LEEVEENIERLDLIIDEKRQQLERLRREREKA-ERYQALLKEKREYEgYELLKEKEALERQKEAIERQL- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 778 EALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRkakeamekekk 857
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKER----------- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 858 KVQDLENRLTKQKEELELKEQKEDVLNNKLsdalamvEETQKTKATESLKAESLALKLNETLAELETTKTKMimveerli 937
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREI-------EEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF-------- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 938 lqqkmvKALQDEQESQRhgfeEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERPQDPLva 1017
Cdd:TIGR02169 381 ------AETRDELKDYR----EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL-- 448
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1018 pmtESSAKDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDL 1067
Cdd:TIGR02169 449 ---EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA 495
|
|
| VI_FHA |
TIGR03354 |
type VI secretion system FHA domain protein; Members of this protein family are FHA ... |
36-202 |
3.12e-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: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 36 TIGRHENSDLVLQSPD--IDNHHALIEYNEAecSFVLQDFnSRNGTFVNECH---IQNVAVKLIPGDILRFGSagltYEL 110
Cdd:TIGR03354 27 TIGRSEDCDWVLPDPErhVSGRHARIRYRDG--AYLLTDL-STNGVFLNGSGsplGRGNPVRLEQGDRLRLGD----YEI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 111 VIENPPPVSFPWMRGPAPWPGPQPPRATQQPNQAPPPSHIPF----HQGVQPAPMQRSWSQAFPRPTVVLPAsHRRPVSA 186
Cdd:TIGR03354 100 RVSLGDPLVSRQASESRADTSLPTAGGPPTPDPAPLAQLDPLkaldQEPLSAADLDDLSAPLFPPLDARLPA-FAAPIDA 178
|
170
....*....|....*.
gi 1370451798 187 NKEMFSFVVDDARKPP 202
Cdd:TIGR03354 179 EPTMVPPFVPLPAPEP 194
|
|
| FHA_SNIP1_DDL-like |
cd22676 |
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA ... |
37-102 |
5.19e-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: 5.19e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370451798 37 IGRHE-NSDLVLQSPDIDNHHALIEY-----------NEAECSFVLqDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFG 102
Cdd:cd22676 25 IGRDRrVADIPLDHPSCSKQHAVIQFrevekrnegdvIENIRPYII-DLGSTNGTFLNGEKIEpRRYYELREKDVLKFG 102
|
|
| FHA_EspA-like |
cd22698 |
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ... |
8-109 |
7.42e-07 |
|
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: 48.56 E-value: 7.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 8 RLFIYGKTERMKAYLKSAEgffvlnksTTIGRHENSDLVLQSPDIDNHHALIEYNEAECsfVLQDFNSRNGTFVNECHIQ 87
Cdd:cd22698 4 LIEQKGSEEGKDYELDQDE--------FTIGRSSNNDIRLNDHSVSRHHARIVRQGDKC--NLTDLGSTNGTFLNGIRVG 73
|
90 100
....*....|....*....|..
gi 1370451798 88 NVAVKliPGDILRFGSAGLTYE 109
Cdd:cd22698 74 THELK--HGDRIQLGETIFRFI 93
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
554-1146 |
7.69e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.20 E-value: 7.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 554 KKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISccsHDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRHALSWL 633
Cdd:TIGR00618 220 RKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQ---QLLKQLRARIEELRAQEAVLEETQERINRARKAAPLA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 634 EEVE-------QLLRDLGILPSSPNKgfslyLIYLLEHYKKLMSQAQELQIKFNSSQETQQsllQEKLREHLAEKEKLNE 706
Cdd:TIGR00618 297 AHIKavtqieqQAQRIHTELQSKMRS-----RAKLLMKRAAHVKQQSSIEEQRRLLQTLHS---QEIHIRDAHEVATSIR 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 707 ERLEQEEKLKAKIRQLTEEKAALEEyitQERNRAKETLEEERKRMQELESLLA----QQKKALAKS---ITQEKNRVKEA 779
Cdd:TIGR00618 369 EISCQQHTLTQHIHTLQQQKTTLTQ---KLQSLCKELDILQREQATIDTRTSAfrdlQGQLAHAKKqqeLQQRYAELCAA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 780 LEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRK----VQDLENHLTQQKEISESNIAYE-KRKAKEAMEK 854
Cdd:TIGR00618 446 AITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKkavvLARLLELQEEPCPLCGSCIHPNpARQDIDNPGP 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 855 EKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEE 934
Cdd:TIGR00618 526 LTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSE 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 935 ----RLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKI-EGEIATLKDNDPAPKEE 1009
Cdd:TIGR00618 606 aedmLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIrVLPKELLASRQLALQKM 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1010 RPQDPLVAPMTESSA-KDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQ 1088
Cdd:TIGR00618 686 QSEKEQLTYWKEMLAqCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFN 765
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370451798 1089 QSKELSVLKEKMAQMSSLV----------EKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQT 1146
Cdd:TIGR00618 766 NNEEVTAALQTGAELSHLAaeiqffnrlrEEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQF 833
|
|
| FHA_GarA_OdhI-like |
cd22684 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium ... |
35-108 |
8.01e-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: 8.01e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370451798 35 TTIGRHENSDLVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHIQnvAVKLIPGDILRFGSAGLTY 108
Cdd:cd22684 23 TTAGRHPESDIFLDDVTVSRRHAEFRRAEGG--FVVRDVGSLNGTYVNRERID--SAVLRNGDEVQIGKFRLVF 92
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
411-803 |
9.72e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 9.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 411 LKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKsCTEQSVISRTLREKSKVEEKLQEDSRRkllqLQE 490
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK-LEKLLQLLPLYQELEALEAELAELPER----LEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 491 MGNRESvikiNLERAVGQLEHFRSQVIKATYGRAKPFRDKPVTDQQLIEKITQVTEDninFQQKKWTLQKETQLSNSKQE 570
Cdd:COG4717 151 LEERLE----ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE---LQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 571 ETTENIEKLRTSLDSCQACMKISCCSHDLK-------KEVDLLQHLQVSPPVSGLQKVVLDVLRHALSWL---------- 633
Cdd:COG4717 224 ELEEELEQLENELEAAALEERLKEARLLLLiaaallaLLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLarekaslgke 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 634 ---------------EEVEQLLRDLGiLPSSPNKGFSLYLIYLLEHYKKLMSQAQELQikfnssQETQQSLLQEKLREHL 698
Cdd:COG4717 304 aeelqalpaleeleeEELEELLAALG-LPPDLSPEELLELLDRIEELQELLREAEELE------EELQLEELEQEIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 699 AEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRA--------KETLEEERKRMQELESLLAQQKKALAKSIT 770
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELeellealdEEELEEELEELEEELEELEEELEELREELA 456
|
410 420 430
....*....|....*....|....*....|...
gi 1370451798 771 QEKNRVKEAleEEQTRVQELEERLARQKEVLES 803
Cdd:COG4717 457 ELEAELEQL--EEDGELAELLQELEELKAELRE 487
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
683-841 |
1.28e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 683 QETQQSLLQEKLREHLAEKEKLNEERleqeEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQ----ELESLL 758
Cdd:COG4913 286 AQRRLELLEAELEELRAELARLEAEL----ERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLEreleERERRR 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 759 AQQKKALAkSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSiAHEKRKAKEALESEKRKVQDLENHLTQQKeise 838
Cdd:COG4913 362 ARLEALLA-ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA-LAEAEAALRDLRRELRELEAEIASLERRK---- 435
|
...
gi 1370451798 839 SNI 841
Cdd:COG4913 436 SNI 438
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
256-839 |
1.58e-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: 52.92 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 256 RLSDYEIESKYKDVIIANLQNEVAELSQKVSETTtsRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQ---KGYSK 332
Cdd:pfam12128 259 RLSHLHFGYKSDETLIASRQEERQETSAELNQLL--RTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEdqhGAFLD 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 333 VLCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQV-QQLKEEVSHLKS----QNKDKDHQLEA---- 403
Cdd:pfam12128 337 ADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIkEQNNRDIAGIKDklakIREARDRQLAVaedd 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 404 LGSRCSVLKEELKQedAHRELREAQEK------ELKL----------CKTQIQDMEKEMKKLRAELRKSCTEQSVISRTL 467
Cdd:pfam12128 417 LQALESELREQLEA--GKLEFNEEEYRlksrlgELKLrlnqatatpeLLLQLENFDERIERAREEQEAANAEVERLQSEL 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 468 REKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHF-RSQVIKATYGRAKpfrdkpVTDQQLI-------E 539
Cdd:pfam12128 495 RQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFlRKEAPDWEQSIGK------VISPELLhrtdldpE 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 540 KITQVTEDNINFQQKKWTLQK-ETQLSNSKQEETTENIEKLRTSLDSCQACMK-ISCCSHDLKKEVDLLQhLQVSPPVSG 617
Cdd:pfam12128 569 VWDGSVGGELNLYGVKLDLKRiDVPEWAASEEELRERLDKAEEALQSAREKQAaAEEQLVQANGELEKAS-REETFARTA 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 618 LQKVVLDVLRhalsWLEEVEQLLRDLgilpsspNKGfslyliyLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREH 697
Cdd:pfam12128 648 LKNARLDLRR----LFDEKQSEKDKK-------NKA-------LAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQK 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 698 LAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEyitqERNRAKETLEEERKRmqELESL---------LAQQKKALAKS 768
Cdd:pfam12128 710 REARTEKQAYWQVVEGALDAQLALLKAAIAARRS----GAKAELKALETWYKR--DLASLgvdpdviakLKREIRTLERK 783
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370451798 769 ITQEKNRVKEALEEE---QTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHL----TQQKEISES 839
Cdd:pfam12128 784 IERIAVRRQEVLRYFdwyQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERkaseKQQVRLSEN 861
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
235-806 |
1.86e-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: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 235 EEDLAQQDKDEIILLLGKEVSRLSDYEIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKEISQKcqvLDEDIDAKQK 314
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE---LEERLEELEE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 315 EIQSLKSQISALQkgyskvlcQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQN 394
Cdd:COG1196 324 ELAELEEELEELE--------EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 395 KDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKlckTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVE 474
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELE---EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 475 EKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATYGR-----AKPFRDKPVTDQQLIEKITQVTEDNI 549
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlagavAVLIGVEAAYEAALEAALAAALQNIV 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 550 NFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRHA 629
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARL 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 630 LSWLEEVEQLLRDL--------GILPSSPNKGFSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEK 701
Cdd:COG1196 633 EAALRRAVTLAGRLrevtlegeGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEA 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 702 EKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQE--------------RNRAKETLEEERKRMQELES--LLAQqkkal 765
Cdd:COG1196 713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELleeealeelpeppdLEELERELERLEREIEALGPvnLLAI----- 787
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1370451798 766 aksitqeknrvkEALEEEQTRVQELEErlarQKEVLESSIA 806
Cdd:COG1196 788 ------------EEYEELEERYDFLSE----QREDLEEARE 812
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
670-846 |
1.99e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.69 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 670 SQAQELQIKFNSSQEtQQSLLQEKLREHLAEKEKLNEERLEQEEKLKA---KIRQLTEEKAALEEYI---TQERNRAKET 743
Cdd:COG4942 20 DAAAEAEAELEQLQQ-EIAELEKELAALKKEEKALLKQLAALERRIAAlarRIRALEQELAALEAELaelEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 744 LEEERKRMQE-------------LESLLAQQ-------KKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLES 803
Cdd:COG4942 99 LEAQKEELAEllralyrlgrqppLALLLSPEdfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1370451798 804 SIAhEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKR 846
Cdd:COG4942 179 LLA-ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
696-1455 |
2.23e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 696 EHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNR 775
Cdd:PTZ00121 1080 DFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARK 1159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 776 VKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEAMEKE 855
Cdd:PTZ00121 1160 AEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDA 1239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 856 KKKVQDLENRLTKQKEELELKEQKEdvlnnklsdalaMVEETQKTKATESLKAEslalklnetlaELETTKTKMIMVEER 935
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMAH------------FARRQAAIKAEEARKAD-----------ELKKAEEKKKADEAK 1296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 936 LILQQKMVKALQDEQESQRHGfeEEIMEYKEQIKQHAqtivsleEKLQKVTQHHKKiegeiatlKDNDPAPKEERPQDPL 1015
Cdd:PTZ00121 1297 KAEEKKKADEAKKKAEEAKKA--DEAKKKAEEAKKKA-------DAAKKKAEEAKK--------AAEAAKAEAEAAADEA 1359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1016 VAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEViMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQQSKELSV 1095
Cdd:PTZ00121 1360 EAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA-DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK 1438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1096 lKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQTCDTSVQIEPVHTEAFSSSQEQQSFSDLGV 1175
Cdd:PTZ00121 1439 -KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKK 1517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1176 RCKGSRHEEVIQRQKKALSELRARIKELEKArspdhkdhqnESFLDLKNLRMENNVQKIlldakpdlptlsrieilapqn 1255
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADEAKKAEEKKKA----------DELKKAEELKKAEEKKKA--------------------- 1566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1256 glcnarfgsAMEKSGKMDVAEALELSEKLYLDMSKTLGSLMNIKNMSGHVSMKYLSRQEREKVNQLRQRDLDLVFDKITQ 1335
Cdd:PTZ00121 1567 ---------EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ 1637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1336 LKNQlgRKEEllrgyEKDVEQLRRSKVSIEMYQSQVAKLEDDIYKEAEEKALLKEALERMEHQLCQEKRINRAIRQQKRR 1415
Cdd:PTZ00121 1638 LKKK--EAEE-----KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1370451798 1416 VFVEMVKNRMQNSNSQVGTRKASLKMDQEREMLRKETSSK 1455
Cdd:PTZ00121 1711 EAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
278-990 |
2.63e-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: 52.15 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 278 VAELSQKVSETTTSRQNEKEIS---------QKCQVLDEDIDAKQKEIQSLKS---QISALQKGYSKVLCQTLSERNSEI 345
Cdd:pfam12128 203 VAILEDDGVVPPKSRLNRQQVEhwirdiqaiAGIMKIRPEFTKLQQEFNTLESaelRLSHLHFGYKSDETLIASRQEERQ 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 346 TSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKdkdhqlEALGSRCSVLKEELKQEDAHRELR 425
Cdd:pfam12128 283 ETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHG------AFLDADIETAAADQEQLPSWQSEL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 426 EAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERA 505
Cdd:pfam12128 357 ENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFN 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 506 VGQLEhfrsqvIKATYGRAKPFRDKPVTDQQLIEKITqvtedniNFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDs 585
Cdd:pfam12128 437 EEEYR------LKSRLGELKLRLNQATATPELLLQLE-------NFDERIERAREEQEAANAEVERLQSELRQARKRRD- 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 586 cQACMKISCCSHDLKKEVDLLQ--HLQVSPPVSGLqkvvLDVLR-HALSWLEEV------EQLLR---DLGILPSSPNKG 653
Cdd:pfam12128 503 -QASEALRQASRRLEERQSALDelELQLFPQAGTL----LHFLRkEAPDWEQSIgkvispELLHRtdlDPEVWDGSVGGE 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 654 FSLYLIyllehykklmsqaqelqikfnssqetqqsllqeklrehlaekeKLNEERLEqeeklkakirqlTEEKAALEEYI 733
Cdd:pfam12128 578 LNLYGV-------------------------------------------KLDLKRID------------VPEWAASEEEL 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 734 TQERNRAKETLEEERKRMQELESLLAQQKKALAKSitqeknrvKEALEEEQTRVQELEERLARQKEVLESsiahEKRKAK 813
Cdd:pfam12128 603 RERLDKAEEALQSAREKQAAAEEQLVQANGELEKA--------SREETFARTALKNARLDLRRLFDEKQS----EKDKKN 670
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 814 EALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEamekekkkvQDLENRLTKQKEELelkeqkedVLNNKLSDALAM 893
Cdd:pfam12128 671 KALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKE---------QKREARTEKQAYWQ--------VVEGALDAQLAL 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 894 VEETqKTKATESLKAESLALK--LNETLAELETTKTKMIMVE-ERLILQQKMVKALQDEQES------QRHGFEEEIMEY 964
Cdd:pfam12128 734 LKAA-IAARRSGAKAELKALEtwYKRDLASLGVDPDVIAKLKrEIRTLERKIERIAVRRQEVlryfdwYQETWLQRRPRL 812
|
730 740
....*....|....*....|....*.
gi 1370451798 965 KEQIKQHAQTIVSLEEKLQKVTQHHK 990
Cdd:pfam12128 813 ATQLSNIERAISELQQQLARLIADTK 838
|
|
| FHA_NBN |
cd22667 |
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ... |
28-108 |
3.71e-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: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 28 FFVLNKSTTIGRHENSDLVLQSPDIDNHHALI--EYNEAECSF-------VLQDFnSRNGTFVNECHIQNVA-VKLIPGD 97
Cdd:cd22667 15 YLLPGGEYTVGRKDCDIIIVDDSSISRKHATLtvLHPEANLSDpdtrpelTLKDL-SKYGTFVNGEKLKGGSeVTLKDGD 93
|
90
....*....|.
gi 1370451798 98 ILRFGSAGLTY 108
Cdd:cd22667 94 VITFGVLGSKF 104
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
252-828 |
4.88e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 252 KEVSRLSDYEIESKykdviiaNLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQKGYS 331
Cdd:PRK03918 152 RQILGLDDYENAYK-------NLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 332 KVlcqtlSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDhQLEALGSRCSVL 411
Cdd:PRK03918 225 KL-----EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 412 KEELKQ-EDAHRELreaqEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQ--EDSRRKLLQL 488
Cdd:PRK03918 299 SEFYEEyLDELREI----EKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHElyEEAKAKKEEL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 489 QEMGNRESVIKI----------------------NLERAVGQLEHFRSQVIKATYGRAKPFRDKPVTDQQLiekitqvTE 546
Cdd:PRK03918 375 ERLKKRLTGLTPeklekeleelekakeeieeeisKITARIGELKKEIKELKKAIEELKKAKGKCPVCGREL-------TE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 547 DNINFQQKKWTLqkETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHLQvsppvSGLQKVVLDVL 626
Cdd:PRK03918 448 EHRKELLEEYTA--ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELE-----EKLKKYNLEEL 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 627 RHALSWLEEVEQLLRDLgilpsspnKGFSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSLLQ----------EKLRE 696
Cdd:PRK03918 521 EKKAEEYEKLKEKLIKL--------KGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKeleelgfesvEELEE 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 697 HLAEKEKLNEERLE---QEEKLKAKIRQLTEEKAALEEyITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEK 773
Cdd:PRK03918 593 RLKELEPFYNEYLElkdAEKELEREEKELKKLEEELDK-AFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLEL 671
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1370451798 774 NRVKEALEEEQTRVQELEERLARQKEVLESSIAhEKRKAKEALESEKRKVQDLEN 828
Cdd:PRK03918 672 SRELAGLRAELEELEKRREEIKKTLEKLKEELE-EREKAKKELEKLEKALERVEE 725
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
274-835 |
4.95e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.51 E-value: 4.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 274 LQNEVAELSQKVSETTTSRQNEK--EISQKCQVLDEDIDAKQKEIQSLKSQISALQKGYSKVLCQTLS---ERNSEITSL 348
Cdd:TIGR00618 272 LRAQEAVLEETQERINRARKAAPlaAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSieeQRRLLQTLH 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 349 KNEGENLKRDNAITSgmvsslqkdilaKDEQVQQLKEEVSHLKSQNKDKDH---QLEALGSRCSVLKEELKQEDAHRELR 425
Cdd:TIGR00618 352 SQEIHIRDAHEVATS------------IREISCQQHTLTQHIHTLQQQKTTltqKLQSLCKELDILQREQATIDTRTSAF 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 426 EAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKS------------------KVEEKLQEDSRRKL-L 486
Cdd:TIGR00618 420 RDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAqslkereqqlqtkeqihlQETRKKAVVLARLLeL 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 487 QLQEMGNRESVIKINLER-AVGQLEHFRSQVIKATYGRAKPFRDKPVTDQQLIEKITQVTEDNINFQQKKWTLQKETQLS 565
Cdd:TIGR00618 500 QEEPCPLCGSCIHPNPARqDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCD 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 566 NskqeETTENIEKLRtsldscqacmkisccshdlkKEVDLLQHLqvsppvsglqkvVLDVLRHALSWLEEVEQLLRDLGI 645
Cdd:TIGR00618 580 N----RSKEDIPNLQ--------------------NITVRLQDL------------TEKLSEAEDMLACEQHALLRKLQP 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 646 LpsspnkgfslylIYLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLA----EKEKLNEERLEQEEKLKAKIRQ 721
Cdd:TIGR00618 624 E------------QDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALsirvLPKELLASRQLALQKMQSEKEQ 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 722 LTEEKAALEEYITQERNRaKETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELEERLAR--QKE 799
Cdd:TIGR00618 692 LTYWKEMLAQCQTLLREL-ETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNnnEEV 770
|
570 580 590
....*....|....*....|....*....|....*.
gi 1370451798 800 VLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKE 835
Cdd:TIGR00618 771 TAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEA 806
|
|
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
30-102 |
6.01e-06 |
|
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and similar proteins; SLMAP, also called sarcolemmal-associated protein (SLAP), is a tail-anchored protein involved in fundamental cellular processes, such as myoblast fusion, cell cycle progression, and chromosomal inheritance. It is a cardiac membrane protein that plays an important role in E-C coupling and the adrenergic response of the heart. Overexpression of the SLMAP gene has been associated with diabetes and endothelial dysfunction of macro- and micro-blood vessels. SLMAP contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438731 [Multi-domain] Cd Length: 126 Bit Score: 46.88 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 30 VLNKSTTIGRHEN------SDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQ-----NVAVKLIPGDI 98
Cdd:cd22679 21 VLDEPVKIGRSVArarpaaNNAIFDCKVLSRNHALLWYDDG--KFYLQDTKSSNGTFVNNQRLSkgseeSEPRELHSGDI 98
|
....
gi 1370451798 99 LRFG 102
Cdd:cd22679 99 VQFG 102
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
660-792 |
7.97e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.60 E-value: 7.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 660 YLLEHYKKLMSQAQElqiKFN---SSQETQQSLLQEKLREH---LAEKEKLNEERLEQEEKLKAKIRQLteeKAALEEYI 733
Cdd:PRK00409 502 NIIEEAKKLIGEDKE---KLNeliASLEELERELEQKAEEAealLKEAEKLKEELEEKKEKLQEEEDKL---LEEAEKEA 575
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370451798 734 TQERNRAKETLEEERKRMQELESLLAQQKKalAKSITQEKNRVKEALEEEQTRVQELEE 792
Cdd:PRK00409 576 QQAIKEAKKEADEIIKELRQLQKGGYASVK--AHELIEARKRLNKANEKKEKKKKKQKE 632
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
378-1000 |
8.54e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 8.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 378 EQVQQLKEEVSHLKSQ---NKDKDHQLEalgsrcsvLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELR 454
Cdd:COG1196 213 ERYRELKEELKELEAElllLKLRELEAE--------LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 455 KscteqsvISRTLREKSKVEEKLQEDSRRKLLQLQEMGNResvikinLERAVGQLEHFRSQVIKATygrakpfrdkpvtd 534
Cdd:COG1196 285 E-------AQAEEYELLAELARLEQDIARLEERRRELEER-------LEELEEELAELEEELEELE-------------- 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 535 QQLIEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTsldscqacmkisccshDLKKEVDLLQHLQVspp 614
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE----------------LAEELLEALRAAAE--- 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 615 vsgLQKVVLDVLRHALSWLEEVEQLLRDLgilpsspnkgfslyliyllehykklmsQAQELQIKFNSSQETQQSLLQEKL 694
Cdd:COG1196 398 ---LAAQLEELEEAEEALLERLERLEEEL---------------------------EELEEALAELEEEEEEEEEALEEA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 695 REHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQE-- 772
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAva 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 773 -----KNRVKEALEEE-----QTRVQELEERLARQKEVLESS-------IAHEKRKAKEALESEKRK-VQDLENHLTQQK 834
Cdd:COG1196 528 vligvEAAYEAALEAAlaaalQNIVVEDDEVAAAAIEYLKAAkagratfLPLDKIRARAALAAALARgAIGAAVDLVASD 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 835 EISESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALK 914
Cdd:COG1196 608 LREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAER 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 915 LNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEG 994
Cdd:COG1196 688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER 767
|
....*.
gi 1370451798 995 EIATLK 1000
Cdd:COG1196 768 ELERLE 773
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
314-1000 |
8.77e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.40 E-value: 8.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 314 KEIQSLKSQISALQKGYsKVLCQTLSERNSEITSLKNEGENLKRDnaitsgmVSSLQKDILAKDEQVQQLKEEVSHLKSQ 393
Cdd:TIGR04523 40 KKLKTIKNELKNKEKEL-KNLDKNLNKDEEKINNSNNKIKILEQQ-------IKDLNDKLKKNKDKINKLNSDLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 394 NKDKDHQLEALGSRCSVLKEELKQEDAH-------------------------RELREAQEKELKLCKTQIQDMEKEMKK 448
Cdd:TIGR04523 112 IKNDKEQKNKLEVELNKLEKQKKENKKNidkflteikkkekeleklnnkyndlKKQKEELENELNLLEKEKLNIQKNIDK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 449 LRAELRKSCTEQSVIsrtlrekskveEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKatygrakpfr 528
Cdd:TIGR04523 192 IKNKLLKLELLLSNL-----------KKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN---------- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 529 dkpvTDQQLIEKITQVTEDNINFQQKkwtlQKETQLSNSKQEETTENIEKLRTSLDscqacmkisccshDLKKEVDllqh 608
Cdd:TIGR04523 251 ----TQTQLNQLKDEQNKIKKQLSEK----QKELEQNNKKIKELEKQLNQLKSEIS-------------DLNNQKE---- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 609 lqvsppvsglqkvvLDVLRHALSWLEEVEQLLRDLGILPSSPNKGFSlyliyllehykKLMSQAQELQIKFNSSQETQQS 688
Cdd:TIGR04523 306 --------------QDWNKELKSELKNQEKKLEEIQNQISQNNKIIS-----------QLNEQISQLKKELTNSESENSE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 689 llqekLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKEtLEEERKRMQELESLLAQQKKALAKS 768
Cdd:TIGR04523 361 -----KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ-KDEQIKKLQQEKELLEKEIERLKET 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 769 ITQEKNRVKEaLEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNiayekrka 848
Cdd:TIGR04523 435 IIKNNSEIKD-LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK-------- 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 849 keamekekkkvQDLENRLTKQKEELELKEQKEDVLNNklsdalamvEETQKTKATESLKAESLALKLNETLAELETTKTK 928
Cdd:TIGR04523 506 -----------KELEEKVKDLTKKISSLKEKIEKLES---------EKKEKESKISDLEDELNKDDFELKKENLEKEIDE 565
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370451798 929 MIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLK 1000
Cdd:TIGR04523 566 KNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIK 637
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
671-843 |
9.95e-06 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 49.69 E-value: 9.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 671 QAQELQIKFnSSQETQQSllqEKLrehLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEeyitQERNRAKETLEEERKR 750
Cdd:PRK11637 138 EHTGLQLIL-SGEESQRG---ERI---LAYFGYLNQARQETIAELKQTREELAAQKAELE----EKQSQQKTLLYEQQAQ 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 751 MQELESLLAQQKKALAKsitqeknrVKEALEEEQTRVQELeerlaRQKEV-LESSIAHEKRKAKEALESEKRKVQDLENh 829
Cdd:PRK11637 207 QQKLEQARNERKKTLTG--------LESSLQKDQQQLSEL-----RANESrLRDSIARAEREAKARAEREAREAARVRD- 272
|
170
....*....|....
gi 1370451798 830 ltQQKEISESNIAY 843
Cdd:PRK11637 273 --KQKQAKRKGSTY 284
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
684-1144 |
1.30e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 684 ETQQSLLQEKLREHLAEKE------KLNEerLEQEEK-LKAKIRQLTEEKaaleEYITQERNRAKETLEEERKRMQELES 756
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEekdlheRLNG--LESELAeLDEEIERYEEQR----EQARETRDEADEVLEEHEERREELET 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 757 LLAQQKKALAKSITQEKNR--VKEALEEEQTRVQELEERL--ARQKEVLESSIAHEKRKAKEALESEKRKVQD-LENHLT 831
Cdd:PRK02224 256 LEAEIEDLRETIAETEREReeLAEEVRDLRERLEELEEERddLLAEAGLDDADAEAVEARREELEDRDEELRDrLEECRV 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 832 QQKEISESNIAYEKRKAKEAM--EKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVE--ETQKTKATESLk 907
Cdd:PRK02224 336 AAQAHNEEAESLREDADDLEEraEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGdaPVDLGNAEDFL- 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 908 aESLALKLNETLAELETTKTKMIMVEERLilqqKMVKALQDE-------QESQRHGFEEEIMEYKEQIKQHAQTIVSLEE 980
Cdd:PRK02224 415 -EELREERDELREREAELEATLRTARERV----EEAEALLEAgkcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 981 KLQKVTQHH------KKIEGEIATLKDNdpapkeerpqdplvapmtessakdmayEHLIDDLLAAQKEIL-SQQEVIMKL 1053
Cdd:PRK02224 490 EVEEVEERLeraedlVEAEDRIERLEER---------------------------REDLEELIAERRETIeEKRERAEEL 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1054 RKDLTEAHSRMSDLRgELNEKQKMELEQNVVLVQQQSKELSVLKE------KMAQMSSLVEKKDRELKALEEALRASQEK 1127
Cdd:PRK02224 543 RERAAELEAEAEEKR-EAAAEAEEEAEEAREEVAELNSKLAELKEriesleRIRTLLAAIADAEDEIERLREKREALAEL 621
|
490
....*....|....*..
gi 1370451798 1128 HRLQLNTEKEQKPRKKT 1144
Cdd:PRK02224 622 NDERRERLAEKRERKRE 638
|
|
| Yop-YscD_cpl |
pfam16697 |
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ... |
36-103 |
1.39e-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: 1.39e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370451798 36 TIGRHENSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRFGS 103
Cdd:pfam16697 20 RIGSDPDCDIVLSDKEVSRVHLKLEVDDE--GWRLDDLGSGNGTLVNGQRVTELGIALRPGDRIELGQ 85
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
442-782 |
1.67e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 49.54 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 442 MEKEMKKLRAELRKSctEQSVISRTLREKSKVE-----EKLQEDSRRKLLQLQemgnresvikINLERAVGQLEHFRSqv 516
Cdd:PRK05771 2 APVRMKKVLIVTLKS--YKDEVLEALHELGVVHiedlkEELSNERLRKLRSLL----------TKLSEALDKLRSYLP-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 517 ikatYGRAKPFRDKPVTDQQLiEKITQVTEDNINfqqkkwTLQKETqlsnskqEETTENIEKLRTSLDSCQAcmkisccs 596
Cdd:PRK05771 68 ----KLNPLREEKKKVSVKSL-EELIKDVEEELE------KIEKEI-------KELEEEISELENEIKELEQ-------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 597 hdLKKEVDLLQHLqvSPPVSGLQ-----KVVLDVLRHALswLEEVEQLLRDLGILPSSPNKGFSLY-LIYLLEHYKKLMS 670
Cdd:PRK05771 122 --EIERLEPWGNF--DLDLSLLLgfkyvSVFVGTVPEDK--LEELKLESDVENVEYISTDKGYVYVvVVVLKELSDEVEE 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 671 QAQELQIKFNSSQEtqQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAK---ETLEEE 747
Cdd:PRK05771 196 ELKKLGFERLELEE--EGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLEIELERAEalsKFLKTD 273
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1370451798 748 R----------KRMQELESLLaqqKKALAKSITQEKNRVKEALEE 782
Cdd:PRK05771 274 KtfaiegwvpeDRVKKLKELI---DKATGGSAYVEFVEPDEEEEE 315
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
701-1396 |
1.86e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 701 KEKLNEERLEQ-EEKLKAKIRQLTEEKAALEEYITQErnraketlEEERKRMQELESLLAQQKKALaKSITQEKNRVKEA 779
Cdd:PRK03918 152 RQILGLDDYENaYKNLGEVIKEIKRRIERLEKFIKRT--------ENIEELIKEKEKELEEVLREI-NEISSELPELREE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 780 LEEEQTRVQELEER------LARQKEVLESSIAHEKRKAKE---ALESEKRKVQDLENHLTQQKEISESNIAYEKrkAKE 850
Cdd:PRK03918 223 LEKLEKEVKELEELkeeieeLEKELESLEGSKRKLEEKIREleeRIEELKKEIEELEEKVKELKELKEKAEEYIK--LSE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 851 AMEKEKKKVQDLENRLTkqkeelelkeqkedvlnnKLSDALAMVEETQKtkateslKAESLALKLNETLAELETTKTKMI 930
Cdd:PRK03918 301 FYEEYLDELREIEKRLS------------------RLEEEINGIEERIK-------ELEEKEERLEELKKKLKELEKRLE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 931 MVEERLILQQkMVKALQDEQESQRHGFE-EEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEE 1009
Cdd:PRK03918 356 ELEERHELYE-EAKAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1010 RPQDPLV-APMTESSAKDMAYEHLIDdllaaqkeilsqqevIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQnvvlvqq 1088
Cdd:PRK03918 435 KGKCPVCgRELTEEHRKELLEEYTAE---------------LKRIEKELKEIEEKERKLRKELRELEKVLKKE------- 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1089 qsKELSVLKEKMAQMSSLVEK-KDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQtcdtsvqiepvhteafsssqeq 1167
Cdd:PRK03918 493 --SELIKLKELAEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKEL---------------------- 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1168 qsfsdlgvrckgsrheEVIQRQKKALSELRARIKELEKARSPDHKDHQNESFLDLKNLRmennvqkilldakpdlptlSR 1247
Cdd:PRK03918 549 ----------------EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELE-------------------ER 593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1248 IEILAPQNGLCNARFGSAMEKSGKMDVAEALELS-EKLYLDMSKTLGSLMNIKNMSGHVSMKYLSRQEREKVNQLRQ--R 1324
Cdd:PRK03918 594 LKELEPFYNEYLELKDAEKELEREEKELKKLEEElDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLElsR 673
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370451798 1325 DLDLVFDKITQLKNQLGRKEELLRGYEKDVEQLRRSKVSIEMYQSQVAKLEDDIYKEAEEKALLKE-ALERME 1396
Cdd:PRK03918 674 ELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKErALSKVG 746
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
230-949 |
1.97e-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: 49.58 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 230 AEIYVEEDLAQQDKDEIILLLGKEVSRLSDYEIESKyKDVIIANLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDI 309
Cdd:pfam02463 353 AEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSS-AAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEI 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 310 DAKQKEIQSLKSQISALQKGYSKVLCQTLSERNSEitsLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSH 389
Cdd:pfam02463 432 LEEEEESIELKQGKLTEEKEELEKQELKLLKDELE---LKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSG 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 390 LKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEmkKLRAELRKSCTEQSVISRTLRE 469
Cdd:pfam02463 509 LKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQ--KLVRALTELPLGARKLRLLIPK 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 470 KSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATYGRAKPFRDKPVTDQQLIEKITQVTEDNI 549
Cdd:pfam02463 587 LKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKA 666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 550 NFQQKKWTLqKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQhLQVSPPVSGLQKVVLDVLRHA 629
Cdd:pfam02463 667 SLSELTKEL-LEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELL-ADRVQEAQDKINEELKLLKQK 744
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 630 LSWLEEVEQLLRDLGILPSSPNKGFSLYLIYLLEHYKKLMSQAQELQIKfnssqetQQSLLQEKLREHLAEKEKLNEERL 709
Cdd:pfam02463 745 IDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKE-------EKLKAQEEELRALEEELKEEAELL 817
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 710 EQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQE 789
Cdd:pfam02463 818 EEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKE 897
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 790 LEErlarQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQ 869
Cdd:pfam02463 898 EKK----ELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELG 973
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 870 KEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDE 949
Cdd:pfam02463 974 KVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDP 1053
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
32-104 |
2.01e-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: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 32 NKSTTIGR--HENSD---LVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHIQ------NVAVKLIPGDILR 100
Cdd:cd22702 31 KQPCIIGSdpHQAISgisVVIPSPQVSELHARITCKNGA--FFLTDLGSEHGTWINDNEGRryrappNFPVRLHPSDVIE 108
|
....
gi 1370451798 101 FGSA 104
Cdd:cd22702 109 FGSD 112
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
29-102 |
2.12e-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: 2.12e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370451798 29 FVLNKST-TIGRHENSDLVLQSPDIDNHHALIeYNEaECSFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRFG 102
Cdd:cd22680 16 FPFDFSSvSIGRDPENVIVIPDPFVSRNHARI-TVD-SNEIYIEDLGSTNGTFVNDFKRIKGPAKLHPNDIIKLG 88
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
242-844 |
2.25e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 49.31 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 242 DKDEIILLLGKEVSRLSDYEIESKykDVIIANLQNEVAELSQKVSEtttsrqnekeisqkcqvLDEDIdakqKEIQSLKS 321
Cdd:COG5022 843 KAEVLIQKFGRSLKAKKRFSLLKK--ETIYLQSAQRVELAERQLQE-----------------LKIDV----KSISSLKL 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 322 QISALQKGYSKVLCQTLSERNSEITSLKNEGENLKRdnAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQL 401
Cdd:COG5022 900 VNLELESEIIELKKSLSSDLIENLEFKTELIARLKK--LLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLL 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 402 EALGSrcsvLKEELKQEdahRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDS 481
Cdd:COG5022 978 KKSTI----LVREGNKA---NSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILKPLQK 1050
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 482 RRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATYGRAK--PFRDKPVTDQQLIEKITQVteDNINFQQKKWTLQ 559
Cdd:COG5022 1051 LKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKtiNVKDLEVTNRNLVKPANVL--QFIVAQMIKLNLL 1128
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 560 KETQLSNSKQEETTENIEKLRTSLDSCQACMkisccshdlkKEVDLLQHLQVSPPVSGLQKV------VLDVLRHALSwl 633
Cdd:COG5022 1129 QEISKFLSQLVNTLEPVFQKLSVLQLELDGL----------FWEANLEALPSPPPFAALSEKrlyqsaLYDEKSKLSS-- 1196
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 634 EEVEQLLRDLGILPS-----SPNKGFSLYLI---YLLEHYKKLMSQAQELQIKFnssqETQQSLLQEKLREHLAEKEKLN 705
Cdd:COG5022 1197 SEVNDLKNELIALFSkifsgWPRGDKLKKLIsegWVPTEYSTSLKGFNNLNKKF----DTPASMSNEKLLSLLNSIDNLL 1272
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 706 EERLEQEEKLKAKIRQLTEEKAAL--EEYITQERNRAKETLEEERKRMQELESllaqqkkalaKSITQEKNRVKEALEee 783
Cdd:COG5022 1273 SSYKLEEEVLPATINSLLQYINVGlfNALRTKASSLRWKSATEVNYNSEELDD----------WCREFEISDVDEELE-- 1340
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370451798 784 qtrvqELEERlARQKEVLESSIAH--EKRKAKEALES-------EKRKVQDLENHLTQQ--KEISESNIAYE 844
Cdd:COG5022 1341 -----ELIQA-VKVLQLLKDDLNKldELLDACYSLNPaeiqnlkSRYDPADKENNLPKEilKKIEALLIKQE 1406
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
702-989 |
3.02e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 48.74 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 702 EKLNEERLEQEEKLKAKiRQLTEEKaaLEEYITQERNRAKETLEEERKRMQELESL--LAQQKKALAKSITQEKNRVKEA 779
Cdd:PLN02939 106 EAIAAIDNEQQTNSKDG-EQLSDFQ--LEDLVGMIQNAEKNILLLNQARLQALEDLekILTEKEALQGKINILEMRLSET 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 780 LE------EEQTRVQELEERLAR------QKEVLESSIAHEKRKAKEALESE----KRKVQDLENHLTQQKEISESNIAY 843
Cdd:PLN02939 183 DAriklaaQEKIHVEILEEQLEKlrnellIRGATEGLCVHSLSKELDVLKEEnmllKDDIQFLKAELIEVAETEERVFKL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 844 EKrkakeAMEKEKKKVQDLENRLTKQKE-ELELKEQKEDVLNNKLSDALAMVEETQKtkateslKAESLAL--------- 913
Cdd:PLN02939 263 EK-----ERSLLDASLRELESKFIVAQEdVSKLSPLQYDCWWEKVENLQDLLDRATN-------QVEKAALvldqnqdlr 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 914 ----KLNETLAELETTKTKMIMVEerlILQQKMvKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHH 989
Cdd:PLN02939 331 dkvdKLEASLKEANVSKFSSYKVE---LLQQKL-KLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEESKKRSLEH 406
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
662-1206 |
3.09e-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: 48.90 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 662 LEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITqERNRAK 741
Cdd:TIGR02168 202 LKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL-EVSELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 742 ETLEEERKRMQELESLLA---QQKKALAKSITQ---EKNRVKEALEEEQTRVQELEERLARQKEVLESsIAHEKRKAKEA 815
Cdd:TIGR02168 281 EEIEELQKELYALANEISrleQQKQILRERLANlerQLEELEAQLEELESKLDELAEELAELEEKLEE-LKEELESLEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 816 LESEKRKVQDLENHLTQQKEISE---SNIAYEKRKAKEAM---EKEKKKVQDLENRLTKQKEELELKEQKEDvlNNKLSD 889
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLEtlrSKVAQLELQIASLNneiERLEARLERLEDRRERLQQEIEELLKKLE--EAELKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 890 ALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEE--EIMEYKEQ 967
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGvkALLKNQSG 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 968 IKQH---AQTIVSLEEKLQK-------------VTQHHKKIEGEIATLKDN--------------DPAPKEERPQDPLVA 1017
Cdd:TIGR02168 518 LSGIlgvLSELISVDEGYEAaieaalggrlqavVVENLNAAKKAIAFLKQNelgrvtflpldsikGTEIQGNDREILKNI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1018 PMTESSAKDM-----AYEHLIDDLLA------------------------------------------------------ 1038
Cdd:TIGR02168 598 EGFLGVAKDLvkfdpKLRKALSYLLGgvlvvddldnalelakklrpgyrivtldgdlvrpggvitggsaktnssilerrr 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1039 -----------AQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKM-------------ELEQNVVLVQQQSKELS 1094
Cdd:TIGR02168 678 eieeleekieeLEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQisalrkdlarleaEVEQLEERIAQLSKELT 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1095 VLKEKMAQMSSLVEKKDRELKALE---EALRASQEKHRLQLNTEKEQKPRKKTQTCDTSVQIEPVHTEAFSSSQEQQSFS 1171
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEaeiEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837
|
650 660 670
....*....|....*....|....*....|....*..
gi 1370451798 1172 DLGVRCKGS--RHEEVIQRQKKALSELRARIKELEKA 1206
Cdd:TIGR02168 838 RRLEDLEEQieELSEDIESLAAEIEELEELIEELESE 874
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
691-866 |
3.86e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 691 QEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYItqernrakETLEEERKRMQELESLLAQQKKALAksIT 770
Cdd:COG4717 62 QGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEEL--------EELEAELEELREELEKLEKLLQLLP--LY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 771 QEKNRVKEALEEEQTRVQELEERLARQKEVLEssiahEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKE 850
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEE-----ELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170
....*....|....*.
gi 1370451798 851 AMEKEKKKVQDLENRL 866
Cdd:COG4717 207 RLAELEEELEEAQEEL 222
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
271-509 |
4.09e-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: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 271 IANLQNEVAELSQKVSETttsRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQkgyskvlcQTLSERNSEITSLKN 350
Cdd:COG4942 29 LEQLQQEIAELEKELAAL---KKEEKALLKQLAALERRIAALARRIRALEQELAALE--------AELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 351 EgenLKRDNAITSGMVSSLQK-------DILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRE 423
Cdd:COG4942 98 E---LEAQKEELAELLRALYRlgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 424 LREAQEKELKLCKTQIQDMEKEMKKLRAELRKsctEQSVISRTLREKSKVEEKLQEDSRRklLQLQEMGNRESVIKINLE 503
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEK---ELAELAAELAELQQEAEELEALIAR--LEAEAAAAAERTPAAGFA 249
|
....*.
gi 1370451798 504 RAVGQL 509
Cdd:COG4942 250 ALKGKL 255
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
667-1002 |
4.40e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 667 KLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEE 746
Cdd:PTZ00121 1487 EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKA 1566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 747 ERKRMQELESLLAQQKKALAKSItqEKNRVKEALEEEQTRVQELEERLARQKEvlESSIAHEKRKAKEalesEKRKVQDL 826
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAEEAKKA--EEARIEEVMKLYEEEKKMKAEEAKKAEE--AKIKAEELKKAEE----EKKKVEQL 1638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 827 ENHLTQQKEISES-NIAYEKRKAKEAMEKEKkkvQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATES 905
Cdd:PTZ00121 1639 KKKEAEEKKKAEElKKAEEENKIKAAEEAKK---AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEK 1715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 906 LKAESLALKLNETLAELETTKTKmimVEERlilQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKV 985
Cdd:PTZ00121 1716 KKAEELKKAEEENKIKAEEAKKE---AEED---KKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789
|
330
....*....|....*..
gi 1370451798 986 TQHHKKIEGEIATLKDN 1002
Cdd:PTZ00121 1790 EKRRMEVDKKIKDIFDN 1806
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
720-1442 |
4.44e-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: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 720 RQLTEEKAALE--EYITQERNRAKETLEEERK---RMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELEERL 794
Cdd:TIGR02168 179 RKLERTRENLDrlEDILNELERQLKSLERQAEkaeRYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 795 ARQKEVLESSIAhEKRKAKEALESEKRKVQDLENHLTQQkeisesniayekrkakeamekekkkVQDLENRLTKQKEELE 874
Cdd:TIGR02168 259 TAELQELEEKLE-ELRLEVSELEEEIEELQKELYALANE-------------------------ISRLEQQKQILRERLA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 875 LKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLilqqkmvkalqDEQESQR 954
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL-----------EELEEQL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 955 HGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERPQdplvapmTESSAKDMAYEHLID 1034
Cdd:TIGR02168 382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ-------AELEELEEELEELQE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1035 DLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKM--ELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDR 1112
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLqeNLEGFSEGVKALLKNQSGLSGILGVLSELISVDEG 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1113 ELKALEEALRAsqekHRLQLNTEKEQKPRKktqtcdtsvqiepvhteafsssqeqqsfsdlgvrckgsrheeVIQRQKKA 1192
Cdd:TIGR02168 535 YEAAIEAALGG----RLQAVVVENLNAAKK------------------------------------------AIAFLKQN 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1193 LSElRARIKELekaRSPDHKDHQNESFLDLKNLRMENNVQKILLDAKPDLPT-----LSRIEILApqnglcnarfgsame 1267
Cdd:TIGR02168 569 ELG-RVTFLPL---DSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKalsylLGGVLVVD--------------- 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1268 ksgkmDVAEALELSEKLYLDMSK-TL-GSLMNIKNM----SGHVSMKYLSR-QEREKVNQlrqrDLDLVFDKITQLKNQL 1340
Cdd:TIGR02168 630 -----DLDNALELAKKLRPGYRIvTLdGDLVRPGGVitggSAKTNSSILERrREIEELEE----KIEELEEKIAELEKAL 700
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1341 GRKEELLRGYEKDVEQLRRSKVSIEMYQS----QVAKLEDDIYKEAEEKALLKEALERMEHQLCQEKRINRAIRQQKRRV 1416
Cdd:TIGR02168 701 AELRKELEELEEELEQLRKELEELSRQISalrkDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA 780
|
730 740 750
....*....|....*....|....*....|.
gi 1370451798 1417 FVEMVK-----NRMQNSNSQVGTRKASLKMD 1442
Cdd:TIGR02168 781 EAEIEEleaqiEQLKEELKALREALDELRAE 811
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
271-833 |
5.49e-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: 47.71 E-value: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 271 IANLQNEVAELSQKVSETTTSRQNEKEisqKCQVLDEDIDAKQKEIQSLKSQISALQKGYSKVlcQTLSERN----SEIT 346
Cdd:TIGR04523 147 IKKKEKELEKLNNKYNDLKKQKEELEN---ELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNL--KKKIQKNksleSQIS 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 347 SLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELRE 426
Cdd:TIGR04523 222 ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLN 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 427 AQEKE--LKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLER 504
Cdd:TIGR04523 302 NQKEQdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQS 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 505 AVGQLEHFRSQVikatygrakpfrdkpvtdQQLIEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLD 584
Cdd:TIGR04523 382 YKQEIKNLESQI------------------NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIK 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 585 scqacmkisccshDLKKEVDLLqhlqvsppvsglqkvvldvlrhalswleevEQLLRDLGILPSSPNKGFSLYLIylleH 664
Cdd:TIGR04523 444 -------------DLTNQDSVK------------------------------ELIIKNLDNTRESLETQLKVLSR----S 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 665 YKKLMSQAQELQIKFNSSQETQQSLLQEK--LREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALE-EYITQERNRAK 741
Cdd:TIGR04523 477 INKIKQNLEQKQKELKSKEKELKKLNEEKkeLEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEdELNKDDFELKK 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 742 ETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELEErlarqKEVLESSIAHEKRKAK---EALES 818
Cdd:TIGR04523 557 ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE-----KEKKISSLEKELEKAKkenEKLSS 631
|
570
....*....|....*
gi 1370451798 819 EKRKVQDLENHLTQQ 833
Cdd:TIGR04523 632 IIKNIKSKKNKLKQE 646
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
681-842 |
5.77e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 5.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 681 SSQETQQSLLQEKLREHLAEKEKLNEERleqeEKLKAKIRQLTEEKAALEEYIT---QERNRAKETLEEERKRMQE---- 753
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEY----NELQAELEALQAEIDKLQAEIAeaeAEIEERREELGERARALYRsggs 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 754 ----------------------LESLLAQQKKALA--KSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAhEK 809
Cdd:COG3883 102 vsyldvllgsesfsdfldrlsaLSKIADADADLLEelKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA-EQ 180
|
170 180 190
....*....|....*....|....*....|...
gi 1370451798 810 RKAKEALESEKRKVQDLENHLTQQKEISESNIA 842
Cdd:COG3883 181 EALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
666-838 |
7.74e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.72 E-value: 7.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 666 KKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAkirqltEEKAAleeyitQERNRAKETLE 745
Cdd:PRK09510 83 KKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQA------EEAAA------KAAAAAKAKAE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 746 EERKRMQELESLLAQQKKALAKSITQEKN------------RVKEALEEEQTRVQELEER---LARQKEVLESSIAHEKR 810
Cdd:PRK09510 151 AEAKRAAAAAKKAAAEAKKKAEAEAAKKAaaeakkkaeaeaAAKAAAEAKKKAEAEAKKKaaaEAKKKAAAEAKAAAAKA 230
|
170 180
....*....|....*....|....*...
gi 1370451798 811 KAKEALESEKRKVQDLENHLTQQKEISE 838
Cdd:PRK09510 231 AAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
692-814 |
7.98e-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: 7.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 692 EKLREHLAEKEKLNEERLEQEE-----KLKAKIRQLTEEKAALEEYITqernRAKETLEEERKRMQELESLLAQQKKALA 766
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEereltEEEEEIRRLEEQVERLEAEVE----ELEAELEEKDERIERLERELSEARSEER 458
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370451798 767 KSITQEK---------NRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKE 814
Cdd:COG2433 459 REIRKDReisrldreiERLERELEEERERIEELKRKLERLKELWKLEHSGELVPVKV 515
|
|
| FHA_FhaA-like |
cd22668 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
34-106 |
8.45e-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: 8.45e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370451798 34 STTIGRHENSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQnVAVKLIPGDILRFGSAGL 106
Cdd:cd22668 19 SNIIGRGSDADFRLPDTGVSRRHAEIRWDGQ--VAHLTDLGSTNGTTVNNAPVT-PEWRLADGDVITLGHSEI 88
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
683-819 |
1.04e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 683 QETQQSLLQEKLREHLAEKEKLNEERLE----QEEKLKAKIRQLTEEKAALEeyitQERNRAKETLEE-ERKRMQELESL 757
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERE----RRRARLEALLAAlGLPLPASAEEF 382
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 758 LAQQK--KALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLE------SSIAHEKRKAKEALESE 819
Cdd:COG4913 383 AALRAeaAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAslerrkSNIPARLLALRDALAEA 452
|
|
| FHA_Slr1951-like |
cd22697 |
forkhead associated (FHA) domain found in Synechocystis sp. Slr1951 protein and similar ... |
36-109 |
1.29e-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: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 36 TIGRHENSDLVLQSPDIDNHHALIEY----NEAECSFVLQDF----NSRNGTFVNECHIQNVAvkLIPGDILRFG-SAGL 106
Cdd:cd22697 21 TIGRHPGNDIQIPSQQISRRHATLRRkinpNLDISFWIIDGDlegaESLNGLWVNGERILQHE--LVNGDEIALGpKIVL 98
|
...
gi 1370451798 107 TYE 109
Cdd:cd22697 99 RYQ 101
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
367-1074 |
1.53e-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: 46.50 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 367 SSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQE-DAHRELREAQEKELKLCKTQIQDMEKE 445
Cdd:TIGR00618 162 SKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMpDTYHERKQVLEKELKHLREALQQTQQS 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 446 MKKLRAE---------LRKSCTEQSVISRTLREKSKVEEKLQE--DSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRS 514
Cdd:TIGR00618 242 HAYLTQKreaqeeqlkKQQLLKQLRARIEELRAQEAVLEETQEriNRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMR 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 515 QVIKATYGRAKPFRDK-PVTDQQLIEKITQVTEDNINFQQKKWTLQKETQlsnSKQEETTENIEKLRTSLDSCQACMKIS 593
Cdd:TIGR00618 322 SRAKLLMKRAAHVKQQsSIEEQRRLLQTLHSQEIHIRDAHEVATSIREIS---CQQHTLTQHIHTLQQQKTTLTQKLQSL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 594 CCSHD------------LKKEVDLLQHLQVSPPVSGLQKVVLDVLRHALSwLEEVEQLLRDLGILPSSPNKGFSLYLIYL 661
Cdd:TIGR00618 399 CKELDilqreqatidtrTSAFRDLQGQLAHAKKQQELQQRYAELCAAAIT-CTAQCEKLEKIHLQESAQSLKEREQQLQT 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 662 LEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQE--EKLKAKIRQLTEEKAALEEYITQERNR 739
Cdd:TIGR00618 478 KEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRrmQRGEQTYAQLETSEEDVYHQLTSERKQ 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 740 AKEtLEEERKRMQELESLLAQQKKALAKSI---TQEKNRVKEALEEEQTRVQELEERLARQKEVLESSI------AHEKR 810
Cdd:TIGR00618 558 RAS-LKEQMQEIQQSFSILTQCDNRSKEDIpnlQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQdlqdvrLHLQQ 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 811 KAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDA 890
Cdd:TIGR00618 637 CSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEY 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 891 LAMVEETQKTKATESLKAESLALKLNETLAELEtTKTKMIMVEERLILQQKMVKALQDEQESQRhgFEEEIMEYKEQIKQ 970
Cdd:TIGR00618 717 DREFNEIENASSSLGSDLAAREDALNQSLKELM-HQARTVLKARTEAHFNNNEEVTAALQTGAE--LSHLAAEIQFFNRL 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 971 HAQTIVSLEEKLQKVTQHHKKIEGeIATLKDNDPAPKEERPQDPLvapmtessAKDMAYEHLIDDLLAAQKEILSQQEVI 1050
Cdd:TIGR00618 794 REEDTHLLKTLEAEIGQEIPSDED-ILNLQCETLVQEEEQFLSRL--------EEKSATLGEITHQLLKYEECSKQLAQL 864
|
730 740
....*....|....*....|....
gi 1370451798 1051 MKLRKDLTEAHSRMSDLRGELNEK 1074
Cdd:TIGR00618 865 TQEQAKIIQLSDKLNGINQIKIQF 888
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
726-838 |
1.78e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 726 KAALEEYITQERNRAKETLEEERKRMQEL--ESLLAQQKKALaksitQEKNRVKEALEEEQTRVQELEERLARQKEVLEs 803
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIkkEALLEAKEEIH-----KLRNEFEKELRERRNELQKLEKRLLQKEENLD- 99
|
90 100 110
....*....|....*....|....*....|....*
gi 1370451798 804 siahekrKAKEALESEKRKVQDLENHLTQQKEISE 838
Cdd:PRK12704 100 -------RKLELLEKREEELEKKEKELEQKQQELE 127
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
658-1145 |
2.13e-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: 45.87 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 658 LIYLLEHYKKLMSQAQElQIKFNSSQETQQSLLQEKLREHLA------EKEKLNEERLEQEEKLKAK-IRQLTEEKAALE 730
Cdd:pfam05483 259 LTFLLEESRDKANQLEE-KTKLQDENLKELIEKKDHLTKELEdikmslQRSMSTQKALEEDLQIATKtICQLTEEKEAQM 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 731 EYITQERNRAKETLEEERKRMQELESLLAQQKKALAKS------ITQEKNRVKEALEEEQTRVQELEERLARQKEVL--E 802
Cdd:pfam05483 338 EELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNedqlkiITMELQKKSSELEEMTKFKNNKEVELEELKKILaeD 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 803 SSIAHEKRKAKEALESEKRKVQDLeNHLTQQKEISESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDV 882
Cdd:pfam05483 418 EKLLDEKKQFEKIAEELKGKEQEL-IFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDK 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 883 L---NNKLS-DALAMVEETQKTKA--TESLKAESLALKLNETLAELETT-KTKMIMVEERLILQQKMVKALQDEQESQRH 955
Cdd:pfam05483 497 LlleNKELTqEASDMTLELKKHQEdiINCKKQEERMLKQIENLEEKEMNlRDELESVREEFIQKGDEVKCKLDKSEENAR 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 956 GFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERPQDPLVAPM--TESSAKDMAYEHLI 1033
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKleLELASAKQKFEEII 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1034 DDLlaaQKEILSQQEVIMKLRKDLTEAHSRMSD---LRGELNEKQKMELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKK 1110
Cdd:pfam05483 657 DNY---QKEIEDKKISEEKLLEEVEKAKAIADEavkLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNK 733
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1370451798 1111 DRELKALEEAL-------RASQEKHRLQLNTEKEQKPRKKTQ 1145
Cdd:pfam05483 734 EQEQSSAKAALeielsniKAELLSLKKQLEIEKEEKEKLKME 775
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
658-1126 |
2.17e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 658 LIYLLEHYKKLMSQAQELQIKFNSSQEtQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYiTQER 737
Cdd:TIGR04523 199 LELLLSNLKKKIQKNKSLESQISELKK-QNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK-QKEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 738 NRAKETLEEERKRMQELESLLAQQKKALAKSITQEknrVKEALEEEQTRVQELEERLARQKEVLEssiahekrKAKEALE 817
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKE---LKSELKNQEKKLEEIQNQISQNNKIIS--------QLNEQIS 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 818 SEKRKVQDLEN-HLTQQKEISESNIAYEKrkakeAMEKEKKKVQDLENrLTKQKEELELKEQKEDVLNNKLSDALAMVEE 896
Cdd:TIGR04523 346 QLKKELTNSESeNSEKQRELEEKQNEIEK-----LKKENQSYKQEIKN-LESQINDLESKIQNQEKLNQQKDEQIKKLQQ 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 897 TQKTKATESLKAESLALKLNETLAELETTKTKmimveerLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIV 976
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSV-------KELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELK 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 977 SLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERPQDPLVAPMTESSAKDMAYEHLIDDL----LAAQKEILSQQEVIMK 1052
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFelkkENLEKEIDEKNKEIEE 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1053 LRKDLTEAHSRMSDLRGELNEKQK------MELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKALEEALRASQE 1126
Cdd:TIGR04523 573 LKQTQKSLKKKQEEKQELIDQKEKekkdliKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKE 652
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
275-830 |
2.56e-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: 45.81 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 275 QNEVAELSQKVSETTTSRQNEKEISQKCQvldEDIDAKQKEIQSLKS---QISALQKGYSKVLCQ-TLSERNSEITSLKN 350
Cdd:TIGR00606 425 QEQADEIRDEKKGLGRTIELKKEILEKKQ---EELKFVIKELQQLEGssdRILELDQELRKAERElSKAEKNSLTETLKK 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 351 EGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVShLKSQNKDKDHQLEALGSRCSvlkEELKQEDAHRELREAQEK 430
Cdd:TIGR00606 502 EVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEM-LTKDKMDKDEQIRKIKSRHS---DELTSLLGYFPNKKQLED 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 431 ELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEdsrrKLLQLQEMGNRESvikinleravgQLE 510
Cdd:TIGR00606 578 WLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYED----KLFDVCGSQDEES-----------DLE 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 511 HFRSQVIKATYGRAkPFRDKPVTDQQLIEKIT-----------QVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKL 579
Cdd:TIGR00606 643 RLKEEIEKSSKQRA-MLAGATAVYSQFITQLTdenqsccpvcqRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKK 721
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 580 RTSLDSCQACMKISCCSHDLK-KEVDLLQH--LQVSPPVSGLQKVVLD---VLRHALSWLEEVEQLLRDLGILpsspnKG 653
Cdd:TIGR00606 722 EKRRDEMLGLAPGRQSIIDLKeKEIPELRNklQKVNRDIQRLKNDIEEqetLLGTIMPEEESAKVCLTDVTIM-----ER 796
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 654 FSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSL-LQEKLREHLAEKE---KLNEERLEQEEKLKAKIRQLTEEKAAL 729
Cdd:TIGR00606 797 FQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQeKQHELDTVVSKIElnrKLIQDQQEQIQHLKSKTNELKSEKLQI 876
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 730 EEYItQERNRAKETLEEERKRMQELESLLAQQKK---ALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIA 806
Cdd:TIGR00606 877 GTNL-QRRQQFEEQLVELSTEVQSLIREIKDAKEqdsPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHG 955
|
570 580
....*....|....*....|....
gi 1370451798 807 HEKRKAKEALESEKRKVQDLENHL 830
Cdd:TIGR00606 956 YMKDIENKIQDGKDDYLKQKETEL 979
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
690-796 |
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 1370451798 690 LQEKLREHLAEKEKLNEErleQEEKLKAKIRQLTEEKAALEEYITQERNR-------------AKETLEEERKRMQELES 756
Cdd:COG0542 416 LERRLEQLEIEKEALKKE---QDEASFERLAELRDELAELEEELEALKARweaekelieeiqeLKEELEQRYGKIPELEK 492
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370451798 757 LLAQQKKALAKSITQEKNRVKEA-----------------LEEEQTRVQELEERLAR 796
Cdd:COG0542 493 ELAELEEELAELAPLLREEVTEEdiaevvsrwtgipvgklLEGEREKLLNLEEELHE 549
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
304-442 |
2.66e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.96 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 304 VLDEDIDAKQKEIQSLKSQIS------ALQKGYSKVLCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKdilakd 377
Cdd:PRK09039 43 FLSREISGKDSALDRLNSQIAeladllSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEG------ 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370451798 378 eQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKqedAHRELREAQEKELKLCKTQIQDM 442
Cdd:PRK09039 117 -RAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLA---ALEAALDASEKRDRESQAKIADL 177
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
702-815 |
3.20e-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: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 702 EKLNEERLEQEEKLKAKIRQLTEEKAALEEyITQERNRAKETLEEERKRMQELEsllaQQKKALAKSITQEKNRVKEALE 781
Cdd:COG4942 142 KYLAPARREQAEELRADLAELAALRAELEA-ERAELEALLAELEEERAALEALK----AERQKLLARLEKELAELAAELA 216
|
90 100 110
....*....|....*....|....*....|....
gi 1370451798 782 EEQTRVQELEERLARqkevLESSIAHEKRKAKEA 815
Cdd:COG4942 217 ELQQEAEELEALIAR----LEAEAAAAAERTPAA 246
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
28-110 |
3.56e-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: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 28 FFVLNKSTTIGR---------HENSDLVLQSPD-IDNHHALIEYNEAECSFVLQDFnSRNGTFVNE--CHIQNVAVKLIP 95
Cdd:cd22701 12 YYVQKLEVVLGRnsknssstaADSVDIDLGPSKkISRRHARIFYDFTTQCFELSVL-GRNGVKVDGilVKPGSPPVPLRS 90
|
90
....*....|....*
gi 1370451798 96 GDILRFGSAGLTYEL 110
Cdd:cd22701 91 GSLIQIGGVLFYFLL 105
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
285-533 |
3.81e-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: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 285 VSETTTSRQNEKEISQkcqvLDEDIDAKQKEIQSLKSQISALQKgyskvlcqTLSERNSEITSLKNEGENLKRDNAITSG 364
Cdd:COG4942 16 AAQADAAAEAEAELEQ----LQQEIAELEKELAALKKEEKALLK--------QLAALERRIAALARRIRALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 365 MVSSLQKDILAKDEQVQQLKEEVSHL--KSQNKDKDHQLEALGSRCSVLKEELKQE------DAHRELREAQEKELKLCK 436
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPEDFLDAVRRLQylkylaPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 437 TQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQV 516
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
250
....*....|....*..
gi 1370451798 517 IKATYGRAKPFRDKPVT 533
Cdd:COG4942 244 PAAGFAALKGKLPWPVS 260
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
697-1047 |
3.85e-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: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 697 HLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEyitqernraketLEEERKRMQELESLLAQQKKA----LAKsiTQE 772
Cdd:COG3096 276 HANERRELSERALELRRELFGARRQLAEEQYRLVE------------MARELEELSARESDLEQDYQAasdhLNL--VQT 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 773 KNRVKEALEEEQTRVQELEERLARQKEVLESsiAHEKR-KAKEALESEKRKVQDLENHLT--QQ--KEISESNIAYE--- 844
Cdd:COG3096 342 ALRQQEKIERYQEDLEELTERLEEQEEVVEE--AAEQLaEAEARLEAAEEEVDSLKSQLAdyQQalDVQQTRAIQYQqav 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 845 --KRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQK--------TKATESLKAESLALK 914
Cdd:COG3096 420 qaLEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKayelvckiAGEVERSQAWQTARE 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 915 LNETLAEL-------ETTKTKMIMVEERLILQQKMVKALqdEQESQRHG--------FEEEIMEYKEQIKQHAQTIVSLE 979
Cdd:COG3096 500 LLRRYRSQqalaqrlQQLRAQLAELEQRLRQQQNAERLL--EEFCQRIGqqldaaeeLEELLAELEAQLEELEEQAAEAV 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 980 EKLQKVTQHHKKIEGEIATLKDNDPA-----PKEERPQDPLVAPMTESSAKDMAYEHLID---------DLLAAQKEILS 1045
Cdd:COG3096 578 EQRSELRQQLEQLRARIKELAARAPAwlaaqDALERLREQSGEALADSQEVTAAMQQLLErereatverDELAARKQALE 657
|
..
gi 1370451798 1046 QQ 1047
Cdd:COG3096 658 SQ 659
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
684-835 |
4.72e-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: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 684 ETQQSLLQEKLREHLAEKEKLNEERLEQEEK-------------------LKAKIRQLTEEKAALEeyitqERNRAKETL 744
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQERrealqrlaeyswdeidvasAEREIAELEAELERLD-----ASSDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 745 EEERKRMQELESLLAQQKKALAKSITQEKNRVkEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQ 824
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKEL-EQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE 769
|
170
....*....|.
gi 1370451798 825 DLENHLTQQKE 835
Cdd:COG4913 770 NLEERIDALRA 780
|
|
| FHA_Par42-like |
cd22675 |
forkhead associated (FHA) domain found in Trypanosoma brucei Parvulin 42 (TbPar42) and similar ... |
37-117 |
5.15e-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: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 37 IGRHENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQnvAVKLIP---GDILRFGSAGLTYElVIE 113
Cdd:cd22675 33 FGRSPVCDYVLEHPSISSVHAVLVFHGEQKCFVLMDLGSTNGVKLNGKRIE--KGRPLPlpvGSVIQFGFSARKYK-VRK 109
|
....
gi 1370451798 114 NPPP 117
Cdd:cd22675 110 GPPS 113
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
671-815 |
6.14e-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: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 671 QAQELQIKFNSSQETQQSLLQEKLREHLAE--------------KEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQE 736
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAEllralyrlgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 737 RNR---AKETLEEERKRMQELESLLAQQKKALAKSItQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAK 813
Cdd:COG4942 159 LAElaaLRAELEAERAELEALLAELEEERAALEALK-AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
..
gi 1370451798 814 EA 815
Cdd:COG4942 238 AA 239
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
905-1143 |
6.75e-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: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 905 SLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQrhgfEEEIMEYKEQIKQHAQTIVSLEEKLQK 984
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 985 VTQHHKKIEGEIATLKDN-----DPAPKEERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEIlsqqevIMKLRKDLTE 1059
Cdd:COG4942 88 LEKEIAELRAELEAQKEElaellRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQ------AEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1060 AHSRMSDLRGELNEKQKMELEQnvvlvQQQSKELSVLK-EKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQ 1138
Cdd:COG4942 162 LAALRAELEAERAELEALLAEL-----EEERAALEALKaERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
....*
gi 1370451798 1139 KPRKK 1143
Cdd:COG4942 237 AAAAE 241
|
|
| FHA_DgcB-like |
cd22682 |
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ... |
28-103 |
7.02e-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: 7.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 28 FFVLNKSTTIGRHENSDLVLQSPDIDNHHALIEYNEAECSfvLQDFNSRNGTFVN--------ECHIQNvavklipGDIL 99
Cdd:cd22682 15 FPITESTIVIGRSVESQVQIDDDSVSRYHAKLAVNPSAVS--IIDLGSTNGTIVNgkkipklaSCDLQN-------GDQI 85
|
....
gi 1370451798 100 RFGS 103
Cdd:cd22682 86 KIGN 89
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
707-838 |
7.78e-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: 7.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 707 ERLEQE-EKLKAKIRQLTEEKAALEEYItqernRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQT 785
Cdd:COG4913 238 ERAHEAlEDAREQIELLEPIRELAERYA-----AARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELE 312
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1370451798 786 RVQELEERLARQKEVLESSIAHEKRKAKEALESEkrkVQDLENHLTQQKEISE 838
Cdd:COG4913 313 RLEARLDALREELDELEAQIRGNGGDRLEQLERE---IERLERELEERERRRA 362
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
365-508 |
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 1370451798 365 MVSSLQKDILAKDEQVQQLKEEVSHL-KSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQIQDME 443
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALkKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRY 484
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370451798 444 KEMKKLRAELRKSCTEQSVISRTLREKSKVEE--------------KLQEDSRRKLLQLqemgnrESVIKinlERAVGQ 508
Cdd:COG0542 485 GKIPELEKELAELEEELAELAPLLREEVTEEDiaevvsrwtgipvgKLLEGEREKLLNL------EEELH---ERVIGQ 554
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
300-510 |
1.08e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 300 QKCQVLDEDIDAKQKEIQSLKSQISALQKgyskvLCQTLSERNSEITSLKNegenlkrdnaitsgmVSSLQKDILAKDEQ 379
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEA-----ELDALQERREALQRLAE---------------YSWDEIDVASAERE 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 380 VQQLKEEVSHLKSQNKDkdhqLEALGSRCSVLKEELkqeDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTE 459
Cdd:COG4913 670 IAELEAELERLDASSDD----LAALEEQLEELEAEL---EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1370451798 460 QSVISRTLREKsKVEEKLQEDSRRKLlqLQEMGNRESVIKINLERAVGQLE 510
Cdd:COG4913 743 ARLELRALLEE-RFAAALGDAVEREL--RENLEERIDALRARLNRAEEELE 790
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
271-761 |
1.12e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 271 IANLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAKQ---KEIQSLKSQISALQKGYSKvlcqtLSERNSEITS 347
Cdd:PRK03918 268 IEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELReieKRLSRLEEEINGIEERIKE-----LEEKEERLEE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 348 LKNEGENLKRDNAITSGMVSSLQkDILAKDEQVQQLKEEvshLKSQNKDKdhqlealgsrcsvLKEELKQEDAHRELREA 427
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKR---LTGLTPEK-------------LEKELEELEKAKEEIEE 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 428 QEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVE--EKLQEDSRRKLLQLQEMGNRESVIKINLERA 505
Cdd:PRK03918 406 EISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKEllEEYTAELKRIEKELKEIEEKERKLRKELREL 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 506 VGQLEHFRS-QVIKATYGRAKPFRDKpvTDQQLIEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLD 584
Cdd:PRK03918 486 EKVLKKESElIKLKELAEQLKELEEK--LKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 585 SCQACMKISCCSHDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRhALSWLEEVEQLLRDLGILPSSPNKGFSlYLIYLLEH 664
Cdd:PRK03918 564 KLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLE-LKDAEKELEREEKELKKLEEELDKAFE-ELAETEKR 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 665 YKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQER--NRAKE 742
Cdd:PRK03918 642 LEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEklEKALE 721
|
490
....*....|....*....
gi 1370451798 743 TLEEERKRMQELESLLAQQ 761
Cdd:PRK03918 722 RVEELREKVKKYKALLKER 740
|
|
| FHA_RAD53-like_rpt1 |
cd22689 |
first forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ... |
3-82 |
1.13e-03 |
|
first forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine/threonine-protein kinase RAD53 and similar proteins; RAD53, also called CHEK2 homolog, or serine-protein kinase 1 (Spk1), is a nuclear protein kinase that phosphorylates proteins on serine, threonine, and tyrosine. It controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints and prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. It may be involved in the phosphorylation of RPH1. RAD53 contains two FHA domains. This model corresponds to the first one. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438741 [Multi-domain] Cd Length: 132 Bit Score: 40.72 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 3 SLEPCRLFiYGKTERMKAYLKSAEGFFvlnkstTIGRHENSDLVLQSPDIDNHHALI---EYNEAECSFVLQDFNSrNGT 79
Cdd:cd22689 22 TQEPIRDL-SGDISQVLKEKRSIKKVW------TFGRHPACDYHLGNSRLSNKHFQIllgESDPSDGNVLLNDISS-NGT 93
|
...
gi 1370451798 80 FVN 82
Cdd:cd22689 94 WLN 96
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
684-912 |
1.24e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 684 ETQQSLLQEKLREHLAEKEKLNEE--RLEQE-EKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQ 760
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAEldALQAElEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 761 QKKA-----------LAKSITQEKNRVkEALEEEQTRVQELEERLARQKEVLEssiahekrKAKEALESEKRKVQDLENH 829
Cdd:COG3883 95 LYRSggsvsyldvllGSESFSDFLDRL-SALSKIADADADLLEELKADKAELE--------AKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 830 LTQQKEISESNIAyEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAE 909
Cdd:COG3883 166 LEAAKAELEAQQA-EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
...
gi 1370451798 910 SLA 912
Cdd:COG3883 245 SAA 247
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
436-806 |
1.25e-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: 43.51 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 436 KTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNResviKINLERAVGQLEHFRSQ 515
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD----LARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 516 VIKatygrakpfrdkpvTDQQLIEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDScqacmkiscc 595
Cdd:TIGR02168 752 LSK--------------ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE---------- 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 596 shdLKKEVDLLQ--HLQVSPPVSGLQKVVLDVLRHALSWLEEVEQLLRDLGILPSSPNKgfslyliyLLEHYKKLMSQAQ 673
Cdd:TIGR02168 808 ---LRAELTLLNeeAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE--------LEELIEELESELE 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 674 ELQIKFNSSQE------TQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEE 747
Cdd:TIGR02168 877 ALLNERASLEEalallrSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEA 956
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370451798 748 RKRMQELESLLAQQKKALaKSITQEKNRVK----EALEEeqtrVQELEER---LARQKEVLESSIA 806
Cdd:TIGR02168 957 EALENKIEDDEEEARRRL-KRLENKIKELGpvnlAAIEE----YEELKERydfLTAQKEDLTEAKE 1017
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
694-833 |
1.28e-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: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 694 LREHLAEKEklneERLEQEEKLKAKIRQLTEEKAALEEyitqernrAKETLEEERKRMQELESLLAQQKKALAKSITQEK 773
Cdd:COG4913 666 AEREIAELE----AELERLDASSDDLAALEEQLEELEA--------ELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370451798 774 NRVKEALE-EEQTRVQELEERLARqkEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQ 833
Cdd:COG4913 734 DRLEAAEDlARLELRALLEERFAA--ALGDAVERELRENLEERIDALRARLNRAEEELERA 792
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
261-846 |
1.32e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 261 EIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQkgyskvlcQTLSE 340
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLR--------ETIAE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 341 RNSEITSLKNEgenlkrdnaitsgmvsslqkdILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRcsvlKEELKQEDA 420
Cdd:PRK02224 270 TEREREELAEE---------------------VRDLRERLEELEEERDDLLAEAGLDDADAEAVEAR----REELEDRDE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 421 hrELREaqekELKLCKTQIQDMEKEMKKLRAELRKSCTEqsviSRTLREKSKVEEKLQEDSRRKllqlqemgnresviki 500
Cdd:PRK02224 325 --ELRD----RLEECRVAAQAHNEEAESLREDADDLEER----AEELREEAAELESELEEAREA---------------- 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 501 nLERAVGQLEHFRSQVIKAtygrAKPFRDKPVTDQQLIEKITQVTEDninfqqKKWTLQKETQLSNSKQEEtTENIEKLR 580
Cdd:PRK02224 379 -VEDRREEIEELEEEIEEL----RERFGDAPVDLGNAEDFLEELREE------RDELREREAELEATLRTA-RERVEEAE 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 581 TSLDS--CQACMkisccshdlkkevdllQHLQVSPPVsglqkvvlDVLRHALSWLEEVEQLLRDLGILPSSPNKGfslyl 658
Cdd:PRK02224 447 ALLEAgkCPECG----------------QPVEGSPHV--------ETIEEDRERVEELEAELEDLEEEVEEVEER----- 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 659 IYLLEHYKKLMSQAQELQIKfnssQETQQSLLQEKlREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQER- 737
Cdd:PRK02224 498 LERAEDLVEAEDRIERLEER----REDLEELIAER-RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEARe 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 738 -----NRAKETLEEERKRMQELESLLA-------------QQKKALAKSITQEKNRVKE------ALEEE--QTRVQELE 791
Cdd:PRK02224 573 evaelNSKLAELKERIESLERIRTLLAaiadaedeierlrEKREALAELNDERRERLAEkrerkrELEAEfdEARIEEAR 652
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370451798 792 ERLARQKEVLE--SSIAHEKRKAKEALESEkrkVQDLENHLTQQKEISESNIAYEKR 846
Cdd:PRK02224 653 EDKERAEEYLEqvEEKLDELREERDDLQAE---IGAVENELEELEELRERREALENR 706
|
|
| FHA_PPP1R8 |
cd22674 |
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ... |
33-110 |
1.64e-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: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 33 KSTTIGR-HENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFGSAGLTYEL 110
Cdd:cd22674 27 KYYLFGRnSDVCDFVLDHPSCSRVHAALVYHKHLNRVFLIDLGSTHGTFVGGIRLEpHKPQQLPIDSTLRFGASTRRYIL 106
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
371-845 |
1.69e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 371 KDILAKDEQVQQL----KEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKLcktqiqdMEKEM 446
Cdd:PRK03918 182 EKFIKRTENIEELikekEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELES-------LEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 447 KKLRA---ELRKSCTEQSVISRTLREKSKVEEKLQEDSRRkLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKatygR 523
Cdd:PRK03918 255 RKLEEkirELEERIEELKKEIEELEEKVKELKELKEKAEE-YIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE----R 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 524 AKPFRDKPVTDQQLIEKITQVTEDNINFQQKKWTLQ----KETQLSNSKQEETTENIEKLRTSLDSCQAcmkisccshdl 599
Cdd:PRK03918 330 IKELEEKEERLEELKKKLKELEKRLEELEERHELYEeakaKKEELERLKKRLTGLTPEKLEKELEELEK----------- 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 600 KKEVDLLQHLQVSPPVSGLQKVVLDvLRHALSWLEEVEqllrdlGILPSSPNKgfslyliyLLEHYKKLMSQAQELQIKf 679
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKE-LKKAIEELKKAK------GKCPVCGRE--------LTEEHRKELLEEYTAELK- 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 680 NSSQETQQslLQEKLREHLAEKEKLNEERLEQEE--KLKAKIRQLTEEKAALEEYITQERNRAKE--------------- 742
Cdd:PRK03918 463 RIEKELKE--IEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEELEKKAEeyeklkekliklkge 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 743 --TLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIahEKRKAKEALESEK 820
Cdd:PRK03918 541 ikSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYL--ELKDAEKELEREE 618
|
490 500
....*....|....*....|....*.
gi 1370451798 821 RKVQDLENHLTQ-QKEISESNIAYEK 845
Cdd:PRK03918 619 KELKKLEEELDKaFEELAETEKRLEE 644
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
261-764 |
1.80e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 261 EIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKEISQKCQVLdEDIDAKQKEIQSLKSQISALQKGYSKVLCQTLSE 340
Cdd:TIGR00618 434 ELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTK-EQIHLQETRKKAVVLARLLELQEEPCPLCGSCIH 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 341 RNSEITSLKNEGENLKRDNAITSGmVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELkqeda 420
Cdd:TIGR00618 513 PNPARQDIDNPGPLTRRMQRGEQT-YAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDI----- 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 421 hrelrEAQEKELKLCKTQIQDMEKEMKKLRAELRkscteqsvisrtlREKSKVEEKLqeDSRRKLLQLQEMGNRESVIKI 500
Cdd:TIGR00618 587 -----PNLQNITVRLQDLTEKLSEAEDMLACEQH-------------ALLRKLQPEQ--DLQDVRLHLQQCSQELALKLT 646
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 501 NLERavgQLEHFRSQVIKATYGRAKPFRDKPVTDQQLIEKITQvtedniNFQQKKWTLQKETQLSNSKQEETTENIEKLR 580
Cdd:TIGR00618 647 ALHA---LQLTLTQERVREHALSIRVLPKELLASRQLALQKMQ------SEKEQLTYWKEMLAQCQTLLRELETHIEEYD 717
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 581 TSLDscQACMKISCCSHDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRHALSWLEEVEQLLRDlgilpsspnkgfslyliy 660
Cdd:TIGR00618 718 REFN--EIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTG------------------ 777
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 661 llehyKKLMSQAQELQIKFNSSQETQQSL--LQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERN 738
Cdd:TIGR00618 778 -----AELSHLAAEIQFFNRLREEDTHLLktLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLL 852
|
490 500
....*....|....*....|....*.
gi 1370451798 739 RAKETLEEERKRMQELESLLAQQKKA 764
Cdd:TIGR00618 853 KYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| FHA_Ct664-like |
cd22696 |
forkhead associated (FHA) domain found in Chlamydia trachomatis Ct664 protein and similar ... |
25-103 |
1.82e-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: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 25 AEGFFVLNKSTTIGRHEN-SDLVLQSPDIDNHHALIEYNEAECSFVlQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGS 103
Cdd:cd22696 13 AEFFLESGKTYFIGKDPTvCDIVLQDPSISRQHARLSIDQDNRVFI-EDLSSKNGVLVNGKPIEG-KEEISGSDVISLGT 90
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
663-816 |
1.99e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 663 EHYKKLMSQA-QELQIKFNSSQETQQSLLQ--EKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYItqernr 739
Cdd:PRK12704 64 EEIHKLRNEFeKELRERRNELQKLEKRLLQkeENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELI------ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 740 aketlEEERKRMQELESLLAQQkkalAKSITQEKnrVKEALEEEQTR-VQELEERlarqkevlessiAHE--KRKAKEAL 816
Cdd:PRK12704 138 -----EEQLQELERISGLTAEE----AKEILLEK--VEEEARHEAAVlIKEIEEE------------AKEeaDKKAKEIL 194
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
662-1078 |
2.02e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 662 LEHYKKLMSQAQELQiKFNSSQETQQSLLQE--KLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNR 739
Cdd:PRK01156 321 INKYHAIIKKLSVLQ-KDYNDYIKKKSRYDDlnNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKI 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 740 AKETLEEERKRMQELESLLAQQKKALAkSITQEKNRVKEALEEEQTRVQELEER---------LARQK-EVLESSIAHEK 809
Cdd:PRK01156 400 QEIDPDAIKKELNEINVKLQDISSKVS-SLNQRIRALRENLDELSRNMEMLNGQsvcpvcgttLGEEKsNHIINHYNEKK 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 810 RKAKEALESEKRKVQDLENHLTQQKEISEsniaYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSD 889
Cdd:PRK01156 479 SRLEEKIREIEIEVKDIDEKIVDLKKRKE----YLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNR 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 890 ALAMVEETQKTKATESLKAESL--ALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQ 967
Cdd:PRK01156 555 YKSLKLEDLDSKRTSWLNALAVisLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNK 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 968 IKQhAQTIVSLEEKLQKVTQHHKKiegEIATLKDNDPAPKEerpqdpLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQ 1047
Cdd:PRK01156 635 YNE-IQENKILIEKLRGKIDNYKK---QIAEIDSIIPDLKE------ITSRINDIEDNLKKSRKALDDAKANRARLESTI 704
|
410 420 430
....*....|....*....|....*....|.
gi 1370451798 1048 EVimkLRKDLTEAHSRMSDLRGELNEKQKME 1078
Cdd:PRK01156 705 EI---LRTRINELSDRINDINETLESMKKIK 732
|
|
| FHA_EmbR-like |
cd22669 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis transcriptional ... |
22-109 |
2.13e-03 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis transcriptional regulatory protein EmbR and similar proteins; EmbR is a transcriptional regulator of the embCAB operon encoding cell wall arabinosyltransferases (EmbC, -A, and -B), and is phosphorylated by the cognate mycobacterial serine/threonine protein kinase PknH. It interacts with RNA polymerase and possesses a phosphorylation-dependent ATPase activity. EmbR contains a regulatory C-terminal forkhead-associated (FHA) domain, which mediates binding to a threonine-phosphorylated site in PknH. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438721 [Multi-domain] Cd Length: 89 Bit Score: 38.94 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 22 LKSAEGFFVLNKSTTIGRHENSDLVLQSPDIDNHHALIEYNEAECSfvLQDFNSRNGTFVNECHIQNVAVkLIPGDILRF 101
Cdd:cd22669 5 IASGRGYPLQAAATRIGRLHDNDIVLDSANVSRHHAVIVDTGTNYV--INDLRSSNGVHVQHERIRSAVT-LNDGDHIRI 81
|
....*...
gi 1370451798 102 GSAGLTYE 109
Cdd:cd22669 82 CDHEFTFQ 89
|
|
| FHA_Rv1747-like_rpt2 |
cd22737 |
second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
37-109 |
2.14e-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: 2.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370451798 37 IGRHENSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQnvAVKLIPGDILRFGSAGLTYE 109
Cdd:cd22737 25 IGRASDNDIVIPEGSVSRHHATLVPTPG--GTQIRDLRSTNGTFVNGLRVD--AALLHDGDVVTIGDIDFVFE 93
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
737-819 |
2.30e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 40.16 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 737 RNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQE----LEERLARQKEVLESSIAHEKRKA 812
Cdd:COG0711 33 QEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEEakaeAEAEAERIIAQAEAEIEQERAKA 112
|
....*..
gi 1370451798 813 KEALESE 819
Cdd:COG0711 113 LAELRAE 119
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
314-461 |
2.36e-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: 41.26 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 314 KEIQSLKSQISALQKG------YSKVLCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEV 387
Cdd:pfam17078 3 KVIESLHDQIDALTKTnlqltvQSQNLLSKLEIAQQKESKFLENLASLKHENDNLSSMLNRKERRLKDLEDQLSELKNSY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 388 SHLKSQNKDKDHQLEALGSRCSVLKEELKQE--------DAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTE 459
Cdd:pfam17078 83 EELTESNKQLKKRLENSSASETTLEAELERLqiqydalvDSQNEYKDHYQQEINTLQESLEDLKLENEKQLENYQQRISS 162
|
..
gi 1370451798 460 QS 461
Cdd:pfam17078 163 ND 164
|
|
| FHA_GarA-like |
cd22720 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis glycogen accumulation ... |
29-108 |
2.60e-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: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 29 FVLNKSTT-IGRHENSDLVLQSPDIDNHHAliEYNEAECSFVLQDFNSRNGTFVNECHIqNVAVkLIPGDILRFGSAGLT 107
Cdd:cd22720 19 FLLDQAITsAGRHPDSDIFLDDVTVSRRHA--EFRLENNEFNVVDVGSLNGTYVNREPV-DSAV-LANGDEVQIGKFRLV 94
|
.
gi 1370451798 108 Y 108
Cdd:cd22720 95 F 95
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
261-841 |
2.63e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.73 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 261 EIESKYKDVIiANLQNEVAELsQKVSETTTSRQNEKEISQKCQVLDEDIDAKQ---KEIQSLKSQISALQKGYSkvlcqT 337
Cdd:TIGR01612 1136 EIKKKSENYI-DEIKAQINDL-EDVADKAISNDDPEEIEKKIENIVTKIDKKKniyDEIKKLLNEIAEIEKDKT-----S 1208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 338 LSE-RNSEITSLKNEG----ENLKRDNAITSGMVSSLQKDILAKDEqVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLK 412
Cdd:TIGR01612 1209 LEEvKGINLSYGKNLGklflEKIDEEKKKSEHMIKAMEAYIEDLDE-IKEKSPEIENEMGIEMDIKAEMETFNISHDDDK 1287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 413 EELKQEDAHRE-LREAQEKELKLC-----KTQIQDMEKEMKKLRAELRKSCTEQSvisrtlrekskveeklqedsrrklL 486
Cdd:TIGR01612 1288 DHHIISKKHDEnISDIREKSLKIIedfseESDINDIKKELQKNLLDAQKHNSDIN------------------------L 1343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 487 QLQEMGNRESVIKIN-LERAVGQLEHFRSQVIKATygraKPFRDKPVTDQQLIEKItqvtEDNINFQQKKWTLqkETQLS 565
Cdd:TIGR01612 1344 YLNEIANIYNILKLNkIKKIIDEVKEYTKEIEENN----KNIKDELDKSEKLIKKI----KDDINLEECKSKI--ESTLD 1413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 566 NSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRHALSWL-----EEVEQLL 640
Cdd:TIGR01612 1414 DKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATNDHdfninELKEHID 1493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 641 RDLGI-LPSSPNKGFSLYLIYLLEHYKK----LMSQAQELQIKFNSSQETQQSllqeklREHLAEKEKLNEERLEQEEKL 715
Cdd:TIGR01612 1494 KSKGCkDEADKNAKAIEKNKELFEQYKKdvteLLNKYSALAIKNKFAKTKKDS------EIIIKEIKDAHKKFILEAEKS 1567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 716 KAKIRQLTEEKAALEEYITQ--ERNRA----KETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQE 789
Cdd:TIGR01612 1568 EQKIKEIKKEKFRIEDDAAKndKSNKAaidiQLSLENFENKFLKISDIKKKINDCLKETESIEKKISSFSIDSQDTELKE 1647
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1370451798 790 LEERLARQKEVLESSIAHEK--RKAKEALESEKRKVQDLENHLTQQKEISESNI 841
Cdd:TIGR01612 1648 NGDNLNSLQEFLESLKDQKKniEDKKKELDELDSEIEKIEIDVDQHKKNYEIGI 1701
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
663-905 |
2.75e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 663 EHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKE 742
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 743 TLEEERKRMQEL---ESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELE-----ERLARQKEVLESSIAHEKRKAKE 814
Cdd:PTZ00121 1641 KEAEEKKKAEELkkaEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEalkkeAEEAKKAEELKKKEAEEKKKAEE 1720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 815 ALESEKRKVQDLENHLTQQKEisesniayEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKL--SDALA 892
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEE--------DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELdeEDEKR 1792
|
250
....*....|...
gi 1370451798 893 MVEETQKTKATES 905
Cdd:PTZ00121 1793 RMEVDKKIKDIFD 1805
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
666-836 |
3.02e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 666 KKLMSQAQELQIKFNSSQETQQSLLQE------------------------------KLREHLAEKEKLNEERLEQEEKL 715
Cdd:pfam01576 408 KKLEGQLQELQARLSESERQRAELAEKlsklqselesvssllneaegkniklskdvsSLESQLQDTQELLQEETRQKLNL 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 716 KAKIRQLTEEKAALEEYItQERNRAKETLEeerKRMQELESLLAQQKKALaksitQEKNRVKEALEEEQTRVQELEERLA 795
Cdd:pfam01576 488 STRLRQLEDERNSLQEQL-EEEEEAKRNVE---RQLSTLQAQLSDMKKKL-----EEDAGTLEALEEGKKRLQRELEALT 558
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1370451798 796 RQKEvlessiahEKRKAKEALESEKRKVQ----DLENHLTQQKEI 836
Cdd:pfam01576 559 QQLE--------EKAAAYDKLEKTKNRLQqeldDLLVDLDHQRQL 595
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
661-819 |
3.08e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 661 LLEHYKKLMSQAQELQIKFNSSQEtQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQL------------------ 722
Cdd:COG3883 35 AQAELDALQAELEELNEEYNELQA-ELEALQAEIDKLQAEIAEAEAEIEERREELGERARALyrsggsvsyldvllgses 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 723 ---------------TEEKAALEEYITQER--NRAKETLEEERKRMQELESLLAQQKKALAKSITqEKNRVKEALEEEQT 785
Cdd:COG3883 114 fsdfldrlsalskiaDADADLLEELKADKAelEAKKAELEAKLAELEALKAELEAAKAELEAQQA-EQEALLAQLSAEEA 192
|
170 180 190
....*....|....*....|....*....|....
gi 1370451798 786 RVQELEERLARQKEVLESSIAHEKRKAKEALESE 819
Cdd:COG3883 193 AAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
683-827 |
3.49e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.86 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 683 QETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEE-------YITQERNRAKETLEEERKRMQELE 755
Cdd:pfam15709 357 QEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEeerkqrlQLQAAQERARQQQEEFRRKLQELQ 436
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370451798 756 SLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELEErlarqKEVLESSIAHEKRKAKEALESEKRKVQDLE 827
Cdd:pfam15709 437 RKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAE-----EERLEYQRQKQEAEEKARLEAEERRQKEEE 503
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
287-509 |
3.65e-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: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 287 ETTTSRQNEKEISQKCQVLdedIDAKQKEIQSLKSQISA----LQKGYSKVLCQTLSERN---SEITSLKNEGENLKRDN 359
Cdd:pfam09787 1 NLESAKQELADYKQKAARI---LQSKEKLIASLKEGSGVegldSSTALTLELEELRQERDllrEEIQKLRGQIQQLRTEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 360 AitsGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRelreaqekelklcKTQI 439
Cdd:pfam09787 78 Q---ELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATL-------------QSRI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370451798 440 QDMEKEMKKLRAELR---KSCTEQSVISRTLREkskveekLQEDSRRKLLQLQEMGNRESVIKINLERAVGQL 509
Cdd:pfam09787 142 KDREAEIEKLRNQLTsksQSSSSQSELENRLHQ-------LTETLIQKQTMLEALSTEKNSLVLQLERMEQQI 207
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
662-816 |
3.77e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 662 LEHYKKLMSQAQELQIKFNSSQETQQSLLQE--------KLREHLAEKEKLNEE------RLEQEEKLKAKIRQLTEEKA 727
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREEleklekllQLLPLYQELEALEAElaelpeRLEELEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 728 ALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAksitQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAH 807
Cdd:COG4717 167 ELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ----QRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
....*....
gi 1370451798 808 EKRKAKEAL 816
Cdd:COG4717 243 ERLKEARLL 251
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
692-839 |
3.78e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 692 EKLREHL-AEKEKLNE--ERLEQEEK-LKAKIRQLTEEKaaleeyitQERNRAKETLEEERKRMQE-LESLLAQQKKALA 766
Cdd:PRK00409 505 EEAKKLIgEDKEKLNEliASLEELEReLEQKAEEAEALL--------KEAEKLKEELEEKKEKLQEeEDKLLEEAEKEAQ 576
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370451798 767 KsitqeknRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKA-KEALESekrkvqdLENHLTQQKEISES 839
Cdd:PRK00409 577 Q-------AIKEAKKEADEIIKELRQLQKGGYASVKAHELIEARKRlNKANEK-------KEKKKKKQKEKQEE 636
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
274-481 |
4.17e-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: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 274 LQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQKgyskvlcqTLSERNSEITSLKNEGE 353
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA--------EIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 354 NLKRDNAITSGMVSSLQKDILAKD--EQVQQLkEEVSHLKSQNKDKDHQLEALGSRCSVLKEEL-KQEDAHRELREAQEK 430
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLLGSESfsDFLDRL-SALSKIADADADLLEELKADKAELEAKKAELeAKLAELEALKAELEA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1370451798 431 ELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDS 481
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
683-1206 |
4.50e-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: 41.59 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 683 QETQQSLLQEKLREHLAEKEKLNEERLEQE---EKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQE-LESLL 758
Cdd:TIGR02169 221 REYEGYELLKEKEALERQKEAIERQLASLEeelEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEkIGELE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 759 AQQkkALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAhEKRKAKEALESEKRKVQDLENHLTQQ-KEIS 837
Cdd:TIGR02169 301 AEI--ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIE-EERKRRDKLTEEYAELKEELEDLRAElEEVD 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 838 ESNIAY--EKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKL 915
Cdd:TIGR02169 378 KEFAETrdELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 916 NETLAELETTKTKMIMVEERLILQQKMVKALQ---DEQESQRHGFEEEIMEYK---EQIKQHAQTIVSLEEKLQKV-TQH 988
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKELSKLQrelAEAEAQARASEERVRGGRaveEVLKASIQGVHGTVAQLGSVgERY 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 989 HKKIEGE-------------------IATLKDNDPAP------KEERPQDPLVAPMTESSAKDMAY-------------- 1029
Cdd:TIGR02169 538 ATAIEVAagnrlnnvvveddavakeaIELLKRRKAGRatflplNKMRDERRDLSILSEDGVIGFAVdlvefdpkyepafk 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1030 ------------------------------------------------------------------EHLIDDLLAAQKEI 1043
Cdd:TIGR02169 618 yvfgdtlvvedieaarrlmgkyrmvtlegelfeksgamtggsraprggilfsrsepaelqrlrerlEGLKRELSSLQSEL 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1044 LSQQEVIMKLRKDLTEAHSRMSDLRGELN------EKQKMELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKAL 1117
Cdd:TIGR02169 698 RRIENRLDELSQELSDASRKIGEIEKEIEqleqeeEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKL 777
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 1118 EEAL---RASQEKHRLQ-----LNTEKEQKPRKKTQTCDTSVQIEPVHTEAFSSSQEQQSFSDLGVRCKGSRHE--EVIQ 1187
Cdd:TIGR02169 778 EEALndlEARLSHSRIPeiqaeLSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSieKEIE 857
|
650
....*....|....*....
gi 1370451798 1188 RQKKALSELRARIKELEKA 1206
Cdd:TIGR02169 858 NLNGKKEELEEELEELEAA 876
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
684-787 |
4.61e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.48 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 684 ETQQSLLQEKLREHLAEKEKLNEERLEQEEkLKAKIRQLTEEKAALEEYitqernrAKETLEEERKRMQELESLLAQQKK 763
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQ-SQALAEAQQQELVALEGL-------AAELEEKQQELEAQLEQLQEKAAE 209
|
90 100
....*....|....*....|....*....
gi 1370451798 764 ALAKSITQEKNRVKEA-----LEEEQTRV 787
Cdd:PRK11448 210 TSQERKQKRKEITDQAakrleLSEEETRI 238
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
36-102 |
5.15e-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: 5.15e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370451798 36 TIGRHENS--DLVLQ-SPDIDNHHALIEYNeAECSFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFG 102
Cdd:cd22663 24 TVGRGLGVtyQLVSTcPLMISRNHCVLKKN-DEGQWTIKDNKSLNGVWVNGERIEpLKPYPLNEGDLIQLG 93
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
689-754 |
5.53e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 41.39 E-value: 5.53e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370451798 689 LLQEKLREhlaeKEKLNEERLEQEeKLKAKIRQLTEEKAALEeyitQERNRAKETLEEERKRMQEL 754
Cdd:PLN02316 250 LLEEKRRE----LEKLAKEEAERE-RQAEEQRRREEEKAAME----ADRAQAKAEVEKRREKLQNL 306
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
691-846 |
5.77e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 691 QEKLREHLAEKEKLNEERLEQEE---KLKAKIRQLTEEKAA---LEEYITQERN-----RAKETLEEERKRM-------Q 752
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEErleALEAELDALQERREAlqrLAEYSWDEIDvasaeREIAELEAELERLdassddlA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 753 ELESLLAQQKKALaKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQ 832
Cdd:COG4913 689 ALEEQLEELEAEL-EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767
|
170
....*....|....
gi 1370451798 833 QKEISESNIAYEKR 846
Cdd:COG4913 768 RENLEERIDALRAR 781
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
274-497 |
5.87e-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: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 274 LQNEVAELSQKVSETTTS----RQNEKEISqkcqvLDEDIDAKQKEIQSLKSQISALQkgyskvlcqtlsernSEITSLK 349
Cdd:COG3206 180 LEEQLPELRKELEEAEAAleefRQKNGLVD-----LSEEAKLLLQQLSELESQLAEAR---------------AELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 350 NEGENLKRDNAITSGMVSSLQKD--ILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDahRELREA 427
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEA--QRILAS 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370451798 428 QEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQE-DSRRKLLQLQEMGNRESV 497
Cdd:COG3206 318 LEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESlLQRLEEARLAEALTVGNV 388
|
|
| FlgN |
pfam05130 |
FlgN protein; This family includes the FlgN protein and export chaperone involved in flagellar ... |
741-836 |
6.05e-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: 38.89 E-value: 6.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 741 KETLEEERKRMQELESLLAQQKKALAK-------SITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAK 813
Cdd:pfam05130 4 IELLEEELELLEELLELLEEEQEALKAgdiealeELTEEKQELLQKLAQLEKERRELLAELGLSPEEATLSELLAKEEED 83
|
90 100
....*....|....*....|...
gi 1370451798 814 EALESEKRKVQDLENHLTQQKEI 836
Cdd:pfam05130 84 PELRELWQELLELLERLKELNEL 106
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
684-799 |
6.13e-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: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 684 ETQQSLLQEKLREHLAEKEKLnEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAK--ETLEEERKRMQELESLLAQQ 761
Cdd:COG3206 225 ESQLAEARAELAEAEARLAAL-RAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAElsARYTPNHPDVIALRAQIAAL 303
|
90 100 110
....*....|....*....|....*....|....*...
gi 1370451798 762 KKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKE 799
Cdd:COG3206 304 RAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEA 341
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
307-743 |
6.44e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 307 EDIDAKQKEIQSLKSQISALQKgyskvLCQTLSERNSEITSLKNEGENLKRDnaitsgmvsslqKDILAKDEQVQQLKEE 386
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAE-----LQEELEELEEELEELEAELEELREE------------LEKLEKLLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 387 VSHLKSQNKDKDHQLEALGSRCSVLKEELKQ----EDAHRELREAQEKELKLC----KTQIQDMEKEMKKLRAELRKSCT 458
Cdd:COG4717 134 LEALEAELAELPERLEELEERLEELRELEEEleelEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 459 EQSVISRTLREKSKVEEKLQEDSR-----RKLLQLQEMGNRESVIkINLERAVGQLEHFRSQVIKA--------TYGRAK 525
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELEaaaleERLKEARLLLLIAAAL-LALLGLGGSLLSLILTIAGVlflvlgllALLFLL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 526 PFRDKPVTDQQLIEKITQVTEDNInfQQKKWT-----LQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLK 600
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEEL--EEEELEellaaLGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 601 KEVDLLQHLQVSPpvsglqkvvLDVLRHALSWLEEVEQLLRDLGILPSSPNKGFSLYLIYLLEHYKK-LMSQAQELQIKF 679
Cdd:COG4717 371 EIAALLAEAGVED---------EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEeLEEELEELEEEL 441
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370451798 680 NSSQETQQSLLQEKLR-----EHLAEKEKLnEERLEQEEKLKAKIRQLTEEKAAL---EEYITQERNRAKET 743
Cdd:COG4717 442 EELEEELEELREELAEleaelEQLEEDGEL-AELLQELEELKAELRELAEEWAALklaLELLEEAREEYREE 512
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
673-803 |
6.61e-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: 6.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 673 QELQIKFNSSQETQQSLLQEKLREHLAEkekLNEERLEQEEKLKAK---IRQLTEEKAALEEYITQERNRAKETLEEE-- 747
Cdd:COG3206 247 AQLGSGPDALPELLQSPVIQQLRAQLAE---LEAELAELSARYTPNhpdVIALRAQIAALRAQLQQEAQRILASLEAEle 323
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1370451798 748 --RKRMQELESLLAQQKKALAKsitqeknrvkeaLEEEQTRVQELEERLARQKEVLES 803
Cdd:COG3206 324 alQAREASLQAQLAQLEARLAE------------LPELEAELRRLEREVEVARELYES 369
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
687-846 |
6.79e-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: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 687 QSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEyitqERNRAKETLEEERKRMQELESllaqQKKALA 766
Cdd:pfam09787 17 ARILQSKEKLIASLKEGSGVEGLDSSTALTLELEELRQERDLLRE----EIQKLRGQIQQLRTELQELEA----QQQEEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 767 KSITQEKNRVKEALEEEQTRVQELEERLARQKEVLeSSIAHEKRKAKEALESEKRK----VQDLENHLTQQKEISESNIA 842
Cdd:pfam09787 89 ESSREQLQELEEQLATERSARREAEAELERLQEEL-RYLEEELRRSKATLQSRIKDreaeIEKLRNQLTSKSQSSSSQSE 167
|
....
gi 1370451798 843 YEKR 846
Cdd:pfam09787 168 LENR 171
|
|
| FHA_CHK2 |
cd22666 |
forkhead associated (FHA) domain found in checkpoint kinase 2 (Chk2) and similar proteins; ... |
27-82 |
6.87e-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: 6.87e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370451798 27 GFFVL---NKSTTIGRHENSDLVLQSPDIDNH---------HALI--EYNEAECSFV-LQDFnSRNGTFVN 82
Cdd:cd22666 10 GFSSLdlvKDEYTFGRDKSCDYCFDSPALKKTsyyrtyskkHFRIfrEKGSKNTYPVfLEDH-SSNGTFVN 79
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
243-501 |
7.34e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.96 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 243 KDEIILLLGKEVSRLSDyeiESKYKDVIIANLQNEVAELSQKVSETTTSrqnekeisqkCQVLDEDIDAKQKEIQSLKSQ 322
Cdd:pfam10174 392 KERKINVLQKKIENLQE---QLRDKDKQLAGLKERVKSLQTDSSNTDTA----------LTTLEEALSEKERIIERLKEQ 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 323 ISALQKgyskvlcqtlsERNSEITSLKNEGENLKRDnaitsgmVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLE 402
Cdd:pfam10174 459 REREDR-----------ERLEELESLKKENKDLKEK-------VSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLK 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 403 ALGSRCSVLKEE-LKQEDAHRELREAQEKELKLCK--TQIQDMEKEMKKLRAELRKSCTEQSVISRTLR----EKSKVEE 475
Cdd:pfam10174 521 SLEIAVEQKKEEcSKLENQLKKAHNAEEAVRTNPEinDRIRLLEQEVARYKEESGKAQAEVERLLGILRevenEKNDKDK 600
|
250 260
....*....|....*....|....*.
gi 1370451798 476 KLQEDSRRKLLQLQEMGNRESVIKIN 501
Cdd:pfam10174 601 KIAELESLTLRQMKEQNKKVANIKHG 626
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
376-455 |
7.39e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 376 KDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRK 455
Cdd:COG2433 411 EEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREIERLERELEEERERIEE 490
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
671-783 |
7.68e-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: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 671 QAQELQIKFNSSQE-TQQSLLQekLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERK 749
Cdd:pfam02841 173 KAEEVLQEFLQSKEaVEEAILQ--TDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIE 250
|
90 100 110
....*....|....*....|....*....|....*
gi 1370451798 750 RM-QELESLLAQQKKALAKSITQEKNRVKEALEEE 783
Cdd:pfam02841 251 KMeAEREQLLAEQERMLEHKLQEQEELLKEGFKTE 285
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
690-814 |
8.12e-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: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 690 LQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKEtleeerkrMQEL-ESLLAQQKKALAKS 768
Cdd:smart00787 145 LKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDE--------LEDCdPTELDRAKEKLKKL 216
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1370451798 769 ITQEKNRVKEaLEEEQTRVQELE---ERLARQKEVLESSIAHEKRKAKE 814
Cdd:smart00787 217 LQEIMIKVKK-LEELEEELQELEskiEDLTNKKSELNTEIAEAEKKLEQ 264
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
236-489 |
8.31e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.66 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 236 EDLAQ--QDKDEIILLLGK-EVSRLSDYEIESKYKDviiaNLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAK 312
Cdd:PLN02939 131 EDLVGmiQNAEKNILLLNQaRLQALEDLEKILTEKE----ALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 313 QKEIqslkSQISALQKGYSKVLCQTLSERNSEITSLKNEGENLKrdnaitsGMVSSLQKdilaKDEQVQQLKEEVSHLKS 392
Cdd:PLN02939 207 RNEL----LIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLK-------AELIEVAE----TEERVFKLEKERSLLDA 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 393 QNKDKDHQLeaLGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQI----------QDMEKEMKKLRAELRKSCT--EQ 460
Cdd:PLN02939 272 SLRELESKF--IVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVekaalvldqnQDLRDKVDKLEASLKEANVskFS 349
|
250 260 270
....*....|....*....|....*....|
gi 1370451798 461 SVISRTLREKSK-VEEKLQEDSRRKLLQLQ 489
Cdd:PLN02939 350 SYKVELLQQKLKlLEERLQASDHEIHSYIQ 379
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
236-459 |
9.66e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.30 E-value: 9.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 236 EDLAQQDKDEIILLLGK---EVSRLSDY-EIESKYKDVIIANLQnevaelSQKVSETTTSRQNEKEISQKcqvLDEDIDA 311
Cdd:PRK05771 34 EDLKEELSNERLRKLRSlltKLSEALDKlRSYLPKLNPLREEKK------KVSVKSLEELIKDVEEELEK---IEKEIKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 312 KQKEIQSLKSQISALQKgyskvlcqtlseRNSEITSLKNEGENLK--RDNAITSGMVSSLQKDIlaKDEQVQQLKEEVSH 389
Cdd:PRK05771 105 LEEEISELENEIKELEQ------------EIERLEPWGNFDLDLSllLGFKYVSVFVGTVPEDK--LEELKLESDVENVE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 390 LKSQNKDKDhqlealgsRCSVLKEELKQEDAHRELREAQEKELKL------------CKTQIQDMEKEMKKLRAELRKSC 457
Cdd:PRK05771 171 YISTDKGYV--------YVVVVVLKELSDEVEEELKKLGFERLELeeegtpselireIKEELEEIEKERESLLEELKELA 242
|
..
gi 1370451798 458 TE 459
Cdd:PRK05771 243 KK 244
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
671-867 |
9.86e-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: 9.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 671 QAQELQIKFNSSQETQQSLLQE--KLREHLAEKEKlneeRLeQEEKLKAKIRQLTEEKAALEEYIT---QERNRAKETLE 745
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQlpELRKELEEAEA----AL-EEFRQKNGLVDLSEEAKLLLQQLSeleSQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 746 EERKRMQELESLLAQQKKALAK-SITQEKNRVKEALEEEQTRVQELEER----------LARQKEVLESSIAHEKRKAKE 814
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPElLQSPVIQQLRAQLAELEAELAELSARytpnhpdviaLRAQIAALRAQLQQEAQRILA 316
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1370451798 815 ALESEKRKVQDLENHLTQQKEISESNIAyekrkakeamekekkKVQDLENRLT 867
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLA---------------ELPELEAELR 354
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
302-414 |
9.94e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 9.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451798 302 CQVLDEDIDAKQKEIQSLKSQISALQKGYSKVLC--QTLSERNSEITSLKNEGENLKRDnaitsgmVSSLQKDILAKDEQ 379
Cdd:PHA02562 287 CPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTaiDELEEIMDEFNEQSKKLLELKNK-------ISTNKQSLITLVDK 359
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1370451798 380 VQQLKEEVSHLKSQNKDKD-------HQLEALGSRCSVLKEE 414
Cdd:PHA02562 360 AKKVKAAIEELQAEFVDNAeelaklqDELDKIVKTKSELVKE 401
|
|
| |
