|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
2-97 |
8.30e-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: 173.98 E-value: 8.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 2 KAYLKSAEGFFVLN-KSTTIGRHEdSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQNVAVKLIPGD 80
Cdd:cd22700 1 KGYLKSSDGIFQLDpKVTTIGREG-CDLVLQSPGVEEQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAPGD 79
|
90
....*....|....*..
gi 1622834852 81 ILRFGSAGLTYELVVEN 97
Cdd:cd22700 80 VLRFGFGGLPYELVVDN 96
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
646-1187 |
2.32e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 95.00 E-value: 2.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 646 EHYKKLMSQTQELQIKFNSSQETQQSLLQEKLREHLAEKKQLNEERLEQEEKLKAKIRQLTEEKAALEERIT---QERNR 722
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEeaqAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 723 ANETLEEERKRMQELESLLAQQKKALAESITQENRVKEALEEEQTRVQELEKRLARQKEVLESSIAHEKRKAKEALESEK 802
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 803 RKVQDLENHLTQQKEvsESSIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLSNKLNDALAMVEETQKT 882
Cdd:COG1196 373 ELAEAEEELEELAEE--LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 883 KATESLKAESLALKLNETLAELETTKTKMILmEERLILQQKTVKAVQDEQESQRHGFEEEIMEYKEQIKQHS-------- 954
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAE-LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlagavavl 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 955 --------------------QTIVSLEEKLQKVSQHHKKIEGEIATLKDNDPAQKEERPQDPLVAPTTDSGAKDMAYEhl 1014
Cdd:COG1196 530 igveaayeaaleaalaaalqNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASD-- 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1015 IDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEK---QKMELERNVALVQQQSKELSVLKEKMAQMSSLTEK 1091
Cdd:COG1196 608 LREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVtleGEGGSAGGSLTGGSRRELLAALLEAEAELEELAER 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1092 KDRELKALKEALRASQEKHRLQLNTEKEQKSRKKTQtcDTSVQIEPVHTEAFSSSQEEQSFSDLGVKCKGSRHEEVIQRQ 1171
Cdd:COG1196 688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEE--EALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEL 765
|
570
....*....|....*.
gi 1622834852 1172 KKALSELRARIKELEK 1187
Cdd:COG1196 766 ERELERLEREIEALGP 781
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
18-84 |
4.34e-19 |
|
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 82.62 E-value: 4.34e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622834852 18 TTIGRHEDSDLVLQSPDIDNHHALIEYNEaECSFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRF 84
Cdd:pfam00498 1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDG-GGRFYLEDLGSTNGTFVNGQRLGPEPVRLKDGDVIRL 66
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
11-92 |
5.21e-18 |
|
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: 80.40 E-value: 5.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 11 FFVLNKSTTIGRHEDSDLVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGLT 90
Cdd:cd00060 14 FPLTKGVVTIGRSPDCDIVLDDPSVSRRHARIEVDGGG--VYLEDLGSTNGTFVNGKRITP-PVPLQDGDVIRLGDTTFR 90
|
..
gi 1622834852 91 YE 92
Cdd:cd00060 91 FE 92
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
244-952 |
6.79e-18 |
|
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: 90.12 E-value: 6.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 244 EIESKYKDVIIANLQKEVAELSQKLSETTTSRQNEREISQKCQVLDEDIDAKQKEIQSLKSQISALQKGYSQL------- 316
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALaneisrl 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 317 -------------LCQTLSERNSEITSLKNEGENLKRDNAIASGMVSSLQKDMLAKDEQVQELKEKVNQLKSQNKDKDHQ 383
Cdd:TIGR02168 301 eqqkqilrerlanLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 384 LEALGSRCSVLKEELKQEDAHRELREAQekelklcKTQIQDMEKEMKKLRAELRKSCTEQSV--ISRTLREKSKVEEKLQ 461
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEAR-------LERLEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQ 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 462 EDSRRKLLQLQEMGNRESLIKINLERAVGQLEHFRSQV--IKATYGRAKPFPD--KPVTDQQL-IEKIAQVTEDNINFQq 536
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERELAQLQARLdsLERLQENLEGFSEgvKALLKNQSgLSGILGVLSELISVD- 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 537 KKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQ--ACMKMSCC----TSDLKKEVDLLQHLQVSPPVSG---------- 600
Cdd:TIGR02168 533 EGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKqnELGRVTFLpldsIKGTEIQGNDREILKNIEGFLGvakdlvkfdp 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 601 -LQKVVLDILRHaLSWLEEVEQLLRDLGILPSSAD----------KGFSLY----------------LIYLLEHYKKLMS 653
Cdd:TIGR02168 613 kLRKALSYLLGG-VLVVDDLDNALELAKKLRPGYRivtldgdlvrPGGVITggsaktnssilerrreIEELEEKIEELEE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 654 QTQELQIKFNSSQETQQSLLQE--KLREHLAEKKQLNEERLEQEEKLKAKIRQLTEEKAALEERIT---QERNRANETLE 728
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEEleQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTeleAEIEELEERLE 771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 729 EERKRMQELESLLAQQKKALAESITQENRVKEALEEEQTRVQELEKRLARQKEVLESSIAHEKRKAKEALESEKRKVQDL 808
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS 851
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 809 ENHLTQQKEVSESSIAYEKrkakeamekEKKKVQDLENRLTKQKEELELKEQKEDVLSNKLNDAlamveETQKTKATESL 888
Cdd:TIGR02168 852 EDIESLAAEIEELEELIEE---------LESELEALLNERASLEEALALLRSELEELSEELREL-----ESKRSELRREL 917
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622834852 889 KA-----ESLALKLNETLAELETTKTKmilMEERLILQQKTVKAVQDEQESQRHGFEEEIMEYKEQIKQ 952
Cdd:TIGR02168 918 EElreklAQLELRLEGLEVRIDNLQER---LSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
12-93 |
9.97e-18 |
|
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 79.62 E-value: 9.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 12 FVLNKS-TTIGRHEDSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGLT 90
Cdd:COG1716 16 FPLDGGpLTIGRAPDNDIVLDDPTVSRRHARIRRDGG--GWVLEDLGSTNGTFVNGQRVTE-PAPLRDGDVIRLGKTELR 92
|
...
gi 1622834852 91 YEL 93
Cdd:COG1716 93 FRL 95
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
227-1063 |
7.96e-16 |
|
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: 83.58 E-value: 7.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 227 DEIILLLGKEVSRLS-DYEIESKYKDViiaNLQKEVAELSQKLSETttsRQNEREISQkcqvLDEDIDAKQKEIQSLKSQ 305
Cdd:TIGR02169 190 DLIIDEKRQQLERLRrEREKAERYQAL---LKEKREYEGYELLKEK---EALERQKEA----IERQLASLEEELEKLTEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 306 ISALQKGYSQLLcQTLSERNSEITSL-KNEGENLKRDNAIASGMVSSLQKDMLAKDEQVQELKEKVNQLKSQNKDKDHQL 384
Cdd:TIGR02169 260 ISELEKRLEEIE-QLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEI 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 385 EALGSRcsvLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDS 464
Cdd:TIGR02169 339 EELERE---IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEEL 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 465 RRKLLQLQEMGNRESLIKINLERAVGQLEHFRSQVIKATygrakpfpdkpvtdqqliEKIAQVTEDNINFQQKKWTLQKE 544
Cdd:TIGR02169 416 QRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE------------------WKLEQLAADLSKYEQELYDLKEE 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 545 TQLSNSKQEETTENIEKLRTSLDSCQACMKMSCCTSDLKKE-----VDLLQHL-QVSPPVSG---------LQKVVLD-- 607
Cdd:TIGR02169 478 YDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvHGTVAQLgSVGERYATaievaagnrLNNVVVEdd 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 608 --------------ILRHALSWLEEVEQLLRDLGILPSSADKGFSLYLIYLLEHYKKL-------------MSQTQELQI 660
Cdd:TIGR02169 558 avakeaiellkrrkAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAfkyvfgdtlvvedIEAARRLMG 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 661 KFN-----------SSQETQQSLLQEKLREHLAEKKQLNEERLEQEEKLKAKIRQLTEEKAALEERI---TQERNRANET 726
Cdd:TIGR02169 638 KYRmvtlegelfekSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLdelSQELSDASRK 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 727 LEEERKRMQELESLLAQQKKALAESITQENRVKEALEEEQTRVQELEKRLARQKEVLessiaHEKRKAKEALESEKR--K 804
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL-----HKLEEALNDLEARLShsR 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 805 VQDLENHLTQQKEVsessiayekrkakeamekekkkVQDLENRLTKQKEELELKEQKEDVLSNKLNDALAMVEETQKTKA 884
Cdd:TIGR02169 793 IPEIQAELSKLEEE----------------------VSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 885 TESLKAESLALKLNETLAELETTKTKMILMEERLilqqKTVKAVQDEQESQRHGFEEEIMEYKEQIKQHSQTIVSLEEKL 964
Cdd:TIGR02169 851 SIEKEIENLNGKKEELEEELEELEAALRDLESRL----GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 965 QKVsqhhkkiEGEIATLKDNDPAQKEERPQDPlvapttdsgakdmAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHS 1044
Cdd:TIGR02169 927 EAL-------EEELSEIEDPKGEDEEIPEEEL-------------SLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLK 986
|
890
....*....|....*....
gi 1622834852 1045 RMSDLRGelnEKQKMELER 1063
Cdd:TIGR02169 987 RLDELKE---KRAKLEEER 1002
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
295-1016 |
1.24e-15 |
|
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: 82.80 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 295 KQKEIQSLKSQISALQKGYSQL----LCQTLSERNSEITSLKNEGENLKRDNAIASGMVSSLQKDMLAKDEQVQELKEKV 370
Cdd:TIGR02168 211 KAERYKELKAELRELELALLVLrleeLREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 371 NQLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHREL----REAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVI 446
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEEleskLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 447 SRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESLIKINLERAVGQLEHFRSQviKATYGRAKPFPDKPVTDQQLIEK--- 523
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE--IEELLKKLEEAELKELQAELEELeee 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 524 IAQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKMSCCTSDLKKEVDLLQHL--QVSPPVS-- 599
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsGILGVLSel 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 600 -----------------GLQKVV---LDILRHALSWLEEVEQLLRDLGILPSSADKGFSLYLIYLLEHYKKLMSQTQELQ 659
Cdd:TIGR02168 529 isvdegyeaaieaalggRLQAVVvenLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLV 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 660 IKFNSSQETQQSLLQ-----EKLREHLAEKKQLNEE---------------------------RLEQeeklKAKIRQLTE 707
Cdd:TIGR02168 609 KFDPKLRKALSYLLGgvlvvDDLDNALELAKKLRPGyrivtldgdlvrpggvitggsaktnssILER----RREIEELEE 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 708 EKAALEERITQernrANETLEEERKRMQELESLLAQQKKALAESITQENRVKEALEEEQTRVQELEKRLARQKEVLESSI 787
Cdd:TIGR02168 685 KIEELEEKIAE----LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 788 AHEKRKAKEALESEKRKVQDLENHLTQQKEVSESSIAYEKrkakeamekEKKKVQDLENRLTKQKEELELKEQKEDVLSN 867
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA---------LREALDELRAELTLLNEEAANLRERLESLER 831
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 868 KLNDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMILMEERLILQQKTVKAVQDEQESqrhgFEEEIMEYK 947
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE----LSEELRELE 907
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622834852 948 EQIKQHSQTIVSLEEKLQKVSQHHKKIEGEIATLKDNDPAQKEERPQDPLVAPTTDSGAKDMAYEHLID 1016
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
20-95 |
5.62e-14 |
|
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) family; The Cep170 family includes Cep170 and Cep170B. Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438756 [Multi-domain] Cd Length: 102 Bit Score: 69.27 E-value: 5.62e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622834852 20 IGRhEDSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHI-QNVAVKLIPGDILRFGSAGLTYELVV 95
Cdd:cd22704 21 VGR-EDCDLILQSRSVDKQHAVITYDQIDNEFKIKDLGSLNGTFVNDSRIpEQTYITLKLGDSIRFGYDTNVYRFEQ 96
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
12-86 |
1.60e-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: 64.63 E-value: 1.60e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622834852 12 FVLNKST-TIGRHEDSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIqNVAVKLIPGDILRFGS 86
Cdd:cd22693 13 FPIDKSGiTIGRADDNDLVLSDDFVSSRHARIYLQGS--SWYLEDLGSTNGTFVNGNRV-TQPVVVQPGDTIRIGA 85
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
12-92 |
1.75e-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: 64.94 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 12 FVLNK-STTIGRHEDSDLVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHI--QNVAVKLIPGDILRFGSAG 88
Cdd:cd22665 16 FPLYEgENVIGRDPSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNKVRlkPNVRYELIDGDLLLFGDVK 93
|
....
gi 1622834852 89 LTYE 92
Cdd:cd22665 94 CQYV 97
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
218-788 |
6.33e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 6.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 218 EEDLAQQDKDEIILLLGKEVSRLSDYEIESKYKDVIIANLQKEVAELSQKLSETTTSRQnerEISQKCQVLDEDIDAKQK 297
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA---RLEQDIARLEERRRELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 298 EIQSLKSQISALQKGYSQLLcQTLSERNSEITSLKNEGENLKRDNAIASGMVSSLQKDMLAKDEQVQELKEKVNQLKSQN 377
Cdd:COG1196 317 RLEELEEELAELEEELEELE-EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 378 KDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKlckTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVE 457
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELE---EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 458 EKLQEDSRRKLLQLQEMGNRESLIKINLERAVGQLEHFRSQVIKATYGR-----AKPFPDKPVTDQQLIEKIAQVTEDNI 532
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlagavAVLIGVEAAYEAALEAALAAALQNIV 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 533 NFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKMSCCTSDLKKEVDLLQHLQVSPPVSGLQKVVLDILRHA 612
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARL 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 613 LSWLEEVEQLLRDLGILPSSADKGFSLYLIYLLEHYKKLMSQTQELQikfnssqetQQSLLQEKLREHLAEKKQLNEERL 692
Cdd:COG1196 633 EAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEA---------ELEELAERLAEEELELEEALLAEE 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 693 EQEEKLKAKIRQLTEEKAALEERITQERNRANETLEEERKRMQELESLLAQQKKALAESITQENRVK------------- 759
Cdd:COG1196 704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELErlereiealgpvn 783
|
570 580 590
....*....|....*....|....*....|...
gi 1622834852 760 ----EALEEEQTRVQELEKrlarQKEVLESSIA 788
Cdd:COG1196 784 llaiEEYEELEERYDFLSE----QREDLEEARE 812
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
675-1132 |
3.62e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 68.63 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 675 EKLREHLAEKKQLNEERLEQEEKLKA-KIRQLTEEKAALEEritqERNRANETLEEERKRMQELESLLAQQKKALAESIT 753
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKAEEKKKAdEAKKKAEEAKKADE----AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK 1483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 754 QENRVKEALEEEQTRVQELEKRLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEVSESSIAYEKRKAKEA 833
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEK 1563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 834 MEKEKKKVQDLENRLTKQKEELELKEQKEdvlsnKLNDALAMVEETQKTKATESLKAESLALKLNETLAELEttktkmil 913
Cdd:PTZ00121 1564 KKAEEAKKAEEDKNMALRKAEEAKKAEEA-----RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE-------- 1630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 914 mEERLILQQKTVKAVQDEQESQRHGFEEEIMEYKEQIKQHSQTIVSLEEKLQKVSQHHKKieGEIATLKDNDPAQKEERP 993
Cdd:PTZ00121 1631 -EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK--AAEALKKEAEEAKKAEEL 1707
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 994 QDPLVAPTTDSGAKDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDlTEAHSRMSDLRGELNEKQKMELERNVALVQQQsk 1073
Cdd:PTZ00121 1708 KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD-EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE-- 1784
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622834852 1074 elsvLKEKMAQMSSLTEKKDRELKALKEALRASQEKHRLQLNTEKEQKSRKKTQTCDTS 1132
Cdd:PTZ00121 1785 ----LDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSK 1839
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
683-1461 |
4.78e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.86 E-value: 4.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 683 EKKQLNEERLEQEEKLKAKIRQLTEEKAALEERITQERNRANETLEEERKRMQELESLLAQQKKA-LAESITQENRVKEA 761
Cdd:PTZ00121 1102 EAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAeEARKAEDAKKAEAA 1181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 762 LEEEQTRVQELEKRLARQKEVLESSIAHEKRKAKEALESEK-RKVQDLENHLTQQKEVSESSIAYEKRKAKEAMEKEKKK 840
Cdd:PTZ00121 1182 RKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDaKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEAR 1261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 841 VQDLENRLTKQKEELELKEQK-EDVLSNKLNDALAMVEETQKT-----KATESLKAESLALKLNETLAELETTKTKMILM 914
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADElKKAEEKKKADEAKKAEEKKKAdeakkKAEEAKKADEAKKKAEEAKKKADAAKKKAEEA 1341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 915 EERLILQQKTVKAVQDEQESQRHGFEEEIMEYKEQIKQHSQTIVSLEEKlQKVSQHHKKIEGEIATLKDNDPAQKEERPQ 994
Cdd:PTZ00121 1342 KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK-KKADEAKKKAEEDKKKADELKKAAAAKKKA 1420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 995 DPlvapttdsgAKDMAYEHLIDDLLAAQKEILSQQEvimKLRKDLTEAhSRMSDLRGELNEKQKMELERNVALVQQQSKE 1074
Cdd:PTZ00121 1421 DE---------AKKKAEEKKKADEAKKKAEEAKKAD---EAKKKAEEA-KKAEEAKKKAEEAKKADEAKKKAEEAKKADE 1487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1075 LSVLKEKMAQMSSLTEKKDRELKALKEALRASQEKHRLQLNTEKEQKSRKKTQTCDTSVQIEPVHT-----EAFSSSQEE 1149
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKaeelkKAEEKKKAE 1567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1150 QSFSDLGVKCKGSRHEEVIQRQKKALSELRARIKELEKAHAPDHKDHQNESFLDLKNLRMKSNIQKILLDAKPDLPTlsr 1229
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE--- 1644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1230 ieilapqnglcNARFSSAMEKSGKMDVAEALELSEKLYLDMSKTlgslmnikdmsghVSMKYLSRQERDKVNQLRQRDLD 1309
Cdd:PTZ00121 1645 -----------EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA-------------EEAKKAEEDEKKAAEALKKEAEE 1700
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1310 LvfDKITQLKNQLERKeellrgyEKDVEQLRRSKVSVEMYQSQVAKLEDDIYKEAEEKALLKEALERMEHQLCQEKRINR 1389
Cdd:PTZ00121 1701 A--KKAEELKKKEAEE-------KKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622834852 1390 AIRQQKESVEEHEPKnakeptpcncafKEKEKQRRVFVKMVKNRMQNS-NSQVGTRKASLKMDQEREMLRKET 1461
Cdd:PTZ00121 1772 EIRKEKEAVIEEELD------------EEDEKRRMEVDKKIKDIFDNFaNIIEGGKEGNLVINDSKEMEDSAI 1832
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
213-969 |
9.75e-11 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 66.92 E-value: 9.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 213 AEIYVEEDLAQQDKDEIILLLGKEVSRLSDYEIESKYKDVIIANLQKEVAELSQKLSETTTSRQNEREISQKCQVLDEDI 292
Cdd:pfam02463 244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEK 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 293 DAKQKEIQSLKSQISALQKGYSQLLCQTLSERNSEITSLKNEGENLKRDNAIASGMVSSLQKDMLAKDEQVQELKEKVNQ 372
Cdd:pfam02463 324 KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 373 LKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLRE 452
Cdd:pfam02463 404 EKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQ 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 453 KSKVE---EKLQEDSRRKLLQLQEMGNRESLIKINLERAVGQLEH---FRSQVIKATYGRAKPFPDKPVTDQQLIEKIAQ 526
Cdd:pfam02463 484 EQLELllsRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHgrlGDLGVAVENYKVAISTAVIVEVSATADEVEER 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 527 VTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKMSCCTSDLKKEVDLLQHLQVSPPVSGLQKVV- 605
Cdd:pfam02463 564 QKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKa 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 606 ----LDILRHALSWLEEVEQLLRDLGILPSSADKGFSLYLIYLLEHYKKLMSQTQELQIKFNSSQETQQSLLQEKLREHL 681
Cdd:pfam02463 644 kesgLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELL 723
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 682 AEKKQL-----------------------NEERLEQEEKLKAKIRQLTEEKAALEERITQERNRANETLEEERKRMQELE 738
Cdd:pfam02463 724 ADRVQEaqdkineelkllkqkideeeeeeEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL 803
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 739 SLLAQQKKALAESITQENRVKEALEEEQTRV-QELEKRLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENH-LTQQK 816
Cdd:pfam02463 804 RALEEELKEEAELLEEEQLLIEQEEKIKEEElEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEeLEEQK 883
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 817 EVSESSIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLSNKLNDALAMVEETQKTKATESLKAESLALK 896
Cdd:pfam02463 884 LKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNK 963
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622834852 897 LNETLAELETTKTKMILME--ERLILQQKTVKAVQDEQESQRHGFEEEIMEYKEQIKQHSQTIVSLEEKLQKVSQ 969
Cdd:pfam02463 964 RLLLAKEELGKVNLMAIEEfeEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFF 1038
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
644-1377 |
2.74e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.46 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 644 LLEHYKKLMSQTQELQIKFNSSQeTQQSLLQEKLREHLAEKKQLNEERLEQEEKL---KAKIRQLTEEKAALEERITQ-- 718
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELT-AELQELEEKLEELRLEVSELEEEIEELQKELyalANEISRLEQQKQILRERLANle 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 719 -ERNRANETLEEERKRMQELESLLAQQKKALAESITQENRVKEALEEEQTRVQELEKRLARQKEVLESsiahekrkAKEA 797
Cdd:TIGR02168 316 rQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET--------LRSK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 798 LESEKRKVQDLENHLTQQKEVSESSiayEKRKAKEAMEKEKKKVQDLENRLtkqkEELELKEQKEDVLSNKLNDALAMVE 877
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERL---EDRRERLQQEIEELLKKLEEAEL----KELQAELEELEEELEELQEELERLE 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 878 ETQKTKATESLKAESLALKLNETLAELETTKTKMILMEERLILQQKTVKAVQDEQE--SQRHGFEEEIMEYKEQIKQHSQ 955
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSglSGILGVLSELISVDEGYEAAIE 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 956 TIvsLEEKLQK-VSQHHKKIEGEIATLKDND------------------PAQKEERPQDPLVAPTTDSGAK-DMAYEHLI 1015
Cdd:TIGR02168 541 AA--LGGRLQAvVVENLNAAKKAIAFLKQNElgrvtflpldsikgteiqGNDREILKNIEGFLGVAKDLVKfDPKLRKAL 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1016 DDLLAAQKEILSQQEVIMKLRKdlTEAHSRMSDLRGELNEKQKM---ELERNVALVQQQSKELSVLKEKMAQMSSLTEKK 1092
Cdd:TIGR02168 619 SYLLGGVLVVDDLDNALELAKK--LRPGYRIVTLDGDLVRPGGVitgGSAKTNSSILERRREIEELEEKIEELEEKIAEL 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1093 DRELKALKEALRASQEKHRlQLNTEKEQKSRKKTQTcDTSVQIEPVHTEAFSSSQEEQSFSDLGVKCKGSRHEEVIQRQK 1172
Cdd:TIGR02168 697 EKALAELRKELEELEEELE-QLRKELEELSRQISAL-RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1173 KALSELRARIKELEkAHAPDHKDHQNESFLDLKNLRMKSNIQKILLDAKpdlptLSRIEILAPQNGLCNARFSSAMEKSG 1252
Cdd:TIGR02168 775 EELAEAEAEIEELE-AQIEQLKEELKALREALDELRAELTLLNEEAANL-----RERLESLERRIAATERRLEDLEEQIE 848
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1253 KM-----DVAEALELSEKLYLDMSKTLGSLMNIKDmSGHVSMKYLSRQERDKVNQLRQRDldlvfDKITQLKNQLERKEE 1327
Cdd:TIGR02168 849 ELsedieSLAAEIEELEELIEELESELEALLNERA-SLEEALALLRSELEELSEELRELE-----SKRSELRRELEELRE 922
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622834852 1328 LLRGYEKDVEQLR------------RSKVSVEMYQSQVAKLEDDIYKEAEEKALLKEALERM 1377
Cdd:TIGR02168 923 KLAQLELRLEGLEvridnlqerlseEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
682-1185 |
2.93e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.55 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 682 AEKKQLNEERLEQEEKLKAKIRQLTEEKAALEERITQERNRANETLEEERKRMqelesllAQQKKALAESITQENRVKEA 761
Cdd:PTZ00121 1327 AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK-------ADAAKKKAEEKKKADEAKKK 1399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 762 LEEEQTRVQELEKRLARQKEVLES-SIAHEKRKAKEALE--SEKRKVQDLENHLTQQKEVSESS-IAYEKRKAKEAMEKE 837
Cdd:PTZ00121 1400 AEEDKKKADELKKAAAAKKKADEAkKKAEEKKKADEAKKkaEEAKKADEAKKKAEEAKKAEEAKkKAEEAKKADEAKKKA 1479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 838 KKKVQDLENRLTKQKEELELKEQKEDVLSNKLNDALAMVEEtqKTKATESLKAESlALKLNETLAELETTKTKMILMEER 917
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE--AKKADEAKKAEE-AKKADEAKKAEEKKKADELKKAEE 1556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 918 LILQQKTVKAVQDEQESQRHGFEEEIMEYKEQIKQhsqtivSLEEKLQKVSQHHKKIEGEIATLKDNDPAQKEERPQDPL 997
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE------ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE 1630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 998 VAPTTDSGAKDMAYEhliddllAAQKEILSQQEVIMKLRKDlteahsrmSDLRGELNEKQKMELERNVALVQQQSKELSV 1077
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEE-------KKKAEELKKAEEENKIKAA--------EEAKKAEEDKKKAEEAKKAEEDEKKAAEALK 1695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1078 LKEKMAQMSSLTEKKDRELKALKEALRASQEKHRLQLNTEKEQKSRKKTQTCDTSVQIEPVHTEAFSSSQEEQSFSDLGV 1157
Cdd:PTZ00121 1696 KEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRK 1775
|
490 500
....*....|....*....|....*...
gi 1622834852 1158 KCKGSRHEEVIQRQKKALSELRARIKEL 1185
Cdd:PTZ00121 1776 EKEAVIEEELDEEDEKRRMEVDKKIKDI 1803
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
675-1134 |
3.55e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.16 E-value: 3.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 675 EKLREHLAEKKQLNEERLEQEEKLKAKIRQLTEEKAALEERITQERNRANET---------LEEERKRMQELESLLAQQK 745
Cdd:PTZ00121 1332 DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAkkkaeekkkADEAKKKAEEDKKKADELK 1411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 746 KALAESITQENRVKEALE-----------EEQTRVQELEKRLARQKEVLESS-IAHEKRKAKEALE--SEKRKVQDLENH 811
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEkkkadeakkkaEEAKKADEAKKKAEEAKKAEEAKkKAEEAKKADEAKKkaEEAKKADEAKKK 1491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 812 LTQQKEVSESS--IAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLSNKLNDALAMVEETQKTKATESLK 889
Cdd:PTZ00121 1492 AEEAKKKADEAkkAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKK 1571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 890 AESLALKLNETLAELETTKTKMILMEERLILQQKTVKAVQDEQESQRHGFEEEIMEYKEQIKQHSQTIVSLEEKLQKVSQ 969
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE 1651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 970 HHKkiEGEIATLKDNDPAQKEERPQDPLVAPTTDSGAKDMAYEHLIDDLLAAQKeilsqqevIMKLRKDLTEAHSRMSDL 1049
Cdd:PTZ00121 1652 LKK--AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK--------AEELKKKEAEEKKKAEEL 1721
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1050 RG--ELNEKQKMELERNVALVQQQSKELSV---LKEKMAQMSSLTEKKDRELKALKEALRASQEKHRLQLNTEKEQKSRK 1124
Cdd:PTZ00121 1722 KKaeEENKIKAEEAKKEAEEDKKKAEEAKKdeeEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIK 1801
|
490
....*....|
gi 1622834852 1125 KTQTCDTSVQ 1134
Cdd:PTZ00121 1802 DIFDNFANII 1811
|
|
| FHA_DUN1-like |
cd22683 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ... |
17-85 |
4.12e-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: 57.89 E-value: 4.12e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622834852 17 STTIGRHEDSDLVLQSPDIDNHHALIEYnEAECSFVLqDFNSRNGTFVNECHIQNVAVKLIPGDILRFG 85
Cdd:cd22683 22 VTTIGRSRSCDLVLSDPSISRFHAELRL-EQNGINVI-DNNSANGTFINGKRIKGKTYILKNGDIIVFG 88
|
|
| FHA_PS1-like |
cd22691 |
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) ... |
19-93 |
7.83e-10 |
|
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: 57.81 E-value: 7.83e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622834852 19 TIGRHEDSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFGSAGLTYEL 93
Cdd:cd22691 32 VVGRHPDCDIVLDHPSISRFHLEIRIIPSRRKITLTDLSSVHGTWVNGQRIEpGVPVELEEGDTVRLGASTRVYRL 107
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
18-65 |
1.63e-09 |
|
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.
Pssm-ID: 214578 [Multi-domain] Cd Length: 52 Bit Score: 54.88 E-value: 1.63e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1622834852 18 TTIGRHE-DSDLVLQSPDIDNHHALIEYNEAECsFVLQDFNSRNGTFVN 65
Cdd:smart00240 1 VTIGRSSeDCDIQLDGPSISRRHAVIVYDGGGR-FYLIDLGSTNGTFVN 48
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
19-85 |
2.09e-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: 56.41 E-value: 2.09e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622834852 19 TIGRHEDSDLVLQSPDIDNHHALIEYN----EAECSFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFG 85
Cdd:cd22677 25 VFGRLPGCDVVLEHPSISRYHAVLQYRgdadDHDGGFYLYDLGSTHGTFLNKQRIPpKQYYRLRVGHVLKFG 96
|
|
| FHA_Cep170A |
cd22724 |
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar ... |
20-85 |
5.31e-09 |
|
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: 55.36 E-value: 5.31e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622834852 20 IGRhEDSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHI-QNVAVKLIPGDILRFG 85
Cdd:cd22724 25 VGR-DDCELMLQSRSVDKQHAVINYDASTDEHKVKDLGSLNGTFVNDVRIpEQTYITLKLDDKLRFG 90
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
638-1460 |
5.65e-09 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 61.14 E-value: 5.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 638 SLYLIYLLEHYKKLMSQTQELQIKFNSSQETQQSLLQEKLREHLAEKKQLNEERLEQEEKLKAKIRQLTEEKAALEERIT 717
Cdd:pfam02463 165 SRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 718 QERNRANETLEEERKRMQELESLLAQQKKalaesITQENRVKEALEEEQTRVQELEKRLARQKEVLESSIAHEKRKAKEA 797
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKE-----NKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 798 LESEKRKVQDLENhltQQKEVSESSIayEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLSNKLNDALAMVE 877
Cdd:pfam02463 320 EKEKKKAEKELKK---EKEEIEELEK--ELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 878 ETQKTKATESLKAESLA----LKLNETLAELETTKTKMILMEERLILQQKTVKAVQDEQESQRHGFEE-EIMEYKEQIKQ 952
Cdd:pfam02463 395 EELELKSEEEKEAQLLLelarQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKdELELKKSEDLL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 953 HSQTIVSLEEKLQKVSQHHKKIEGEIATLKDNDPAQKEERPQDPLVAPTTDSGAKDMAYEHLIDDLLAAQKEILSQQEVI 1032
Cdd:pfam02463 475 KETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVS 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1033 MKLRKDLTEAHSRMSDLRGELNE-KQKMELERNVALVQQQSKELSVLKEKMAQMSSLTEKKDRELKALKEA---LRASQE 1108
Cdd:pfam02463 555 ATADEVEERQKLVRALTELPLGArKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVegiLKDTEL 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1109 KHRLQLNTEKEQKSRKKTQTCDTSVQIEPVHTEAFSSSQEEQSFSDLGVKCKGSRHEEVIQRQKKALSELRARIKELEKA 1188
Cdd:pfam02463 635 TKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKK 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1189 HApDHKDHQNESFLDLKNLRMKSNIQKILLDAKPDLPTLSRIEILAPQNGLCNARFSSAMEKSGKMDVA-EALELSEKLY 1267
Cdd:pfam02463 715 LK-LEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKtEKLKVEEEKE 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1268 LDMSKTLGSLMNIKDMSGHVSMKYLSRQERDKVNQLRQ---RDLDLVFDKITQLKNQLERKEELLRGYEKDVEQLRRSKV 1344
Cdd:pfam02463 794 EKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKeeeLEELALELKEEQKLEKLAEEELERLEEEITKEELLQELL 873
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1345 SVEMYQSQVAKLEDDIYKEAEEKALLKEALERMEHQLCQEKRINRAIRQQKESVEEHEPKNAKEPTPCNCAFKEKEKQR- 1423
Cdd:pfam02463 874 LKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEEn 953
|
810 820 830
....*....|....*....|....*....|....*...
gi 1622834852 1424 -RVFVKMVKNRMQNSNSQVGTRKASLKMDQEREMLRKE 1460
Cdd:pfam02463 954 nKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYN 991
|
|
| FHA_Ki67 |
cd22673 |
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ... |
11-92 |
6.25e-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: 54.53 E-value: 6.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 11 FFVLNKSTTIGRHEDSDLVLQSPDIDNHHALIEYNEAECsFVLQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGLT 90
Cdd:cd22673 16 FPLTKKSCTFGRDLSCDIRIQLPGVSREHCRIEVDENGK-AYLENLSTTNPTLVNGKAIEK-SAELKDGDVITIGGRSFR 93
|
..
gi 1622834852 91 YE 92
Cdd:cd22673 94 FE 95
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
17-85 |
6.85e-09 |
|
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: 54.26 E-value: 6.85e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622834852 17 STTIGRHEDSDLVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHIQnvAVKLIPGDILRFG 85
Cdd:cd22694 17 SVRIGRDPDADVRLDDPRVSRRHALLEFDGDG--WVYTDLGSRNGTYLNGRRVQ--QVKLSDGTRVRLG 81
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
19-96 |
7.21e-09 |
|
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: 59.78 E-value: 7.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 19 TIGRHEDSDLVLQSPD--IDNHHALIEYneAECSFVLQDfNSRNGTFVNECHI---QNVAVKLIPGDILRFGSagltYEL 93
Cdd:COG3456 29 TIGRSADCDWVLPDPDrsVSRRHAEIRF--RDGAFCLTD-LSTNGTFLNGSDHplgPGRPVRLRDGDRLRIGD----YEI 101
|
...
gi 1622834852 94 VVE 96
Cdd:COG3456 102 RVE 104
|
|
| FHA_Cep170B |
cd22725 |
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) ... |
20-93 |
1.05e-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: 54.55 E-value: 1.05e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622834852 20 IGRhEDSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQN---VAVKLipGDILRFGSAGLTYEL 93
Cdd:cd22725 25 VGR-EDCELMLQSRSVDKQHAVINYDQDTDEHWVKDLGSLNGTFVNDVRIPDqkyITLKL--NDVIRFGYDSNMYVL 98
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
683-983 |
1.43e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.70 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 683 EKKQLNEERLEQEEKLKAKIRQLTEEKAALEERITQERNRAnETLEEERKRMQELE-SLLAQQKKALAESITQENRVKEA 761
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKA-ERYQALLKEKREYEgYELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 762 LEEEQTRVQELEKRLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEVSESSIAYEKRKAKEAMEKE---- 837
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLakle 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 838 ------KKKVQDLENRLTKQKEELELKEQKEDVLSNKLNDALAMVEETQKTKAT--ESLKAESLAL-KLNETLAELETTK 908
Cdd:TIGR02169 329 aeidklLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAEtrDELKDYREKLeKLKREINELKREL 408
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622834852 909 TKMILMEERLILQQKTVKAVQDEQESQRHGFEEEIMEYKEQIKQHSQTIVSLEEKLQKVSQHHKKIEGEIATLKD 983
Cdd:TIGR02169 409 DRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483
|
|
| FHA_AGGF1 |
cd22686 |
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ... |
11-86 |
2.30e-08 |
|
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: 53.83 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 11 FFVLNKSTTIGRHEDSDLVLQSPD--IDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQNVAVKLIP-----GDILR 83
Cdd:cd22686 21 FIVTATGATIGREKDHGHTIRIPElgVSKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPyplthGDELK 100
|
...
gi 1622834852 84 FGS 86
Cdd:cd22686 101 IGE 103
|
|
| FHA_MEK1-like |
cd22670 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ... |
15-92 |
3.16e-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: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 15 NKSTTIGRHEDSDLVLQSPDIDNHHALIE---YNEAECSFV-LQDfNSRNGTFVNECHI-QNVAVKLIPGDILRF-GSAG 88
Cdd:cd22670 21 NQVITIGRSPSCDIVINDPFVSRTHCRIYsvqFDESSAPLVyVED-LSSNGTYLNGKLIgRNNTVLLSDGDVIEIaHSAT 99
|
....
gi 1622834852 89 LTYE 92
Cdd:cd22670 100 FVYV 103
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
666-969 |
5.83e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 5.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 666 QETQQSLlqEKLREHLAEKKQLNEERLEQEEKLKA------KIRQLTEEKAALEERIT----QERNRANETLEEERKRMQ 735
Cdd:TIGR02168 175 KETERKL--ERTRENLDRLEDILNELERQLKSLERqaekaeRYKELKAELRELELALLvlrlEELREELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 736 ELESLLAQQKKALAESITQENRVKEALEEEQTRVQELEKRLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQ 815
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 816 KEVSES--SIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLSNKLNDALAMVEETQKTKATESLKAESL 893
Cdd:TIGR02168 333 DELAEElaELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622834852 894 ALKLNETLAELETTKTKMILME-ERLILQQKTVKAVQDEQESQRHGFEEEIMEYKEQIKQHSQTIVSLEEKLQKVSQ 969
Cdd:TIGR02168 413 EDRRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
675-1111 |
6.13e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 6.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 675 EKLREHLAEKKQLNEERLEQEEKLKAKIRQLTEEKAALEERIT--QERNRANETLEEERKRMQELESLLAQQKKALAESI 752
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEelEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 753 TQENRVKEALEEEQTRVQELEKRLARQKEVLEssiahEKRKAKEALESEKRKVQDLENHLTQQKEVSEssiaYEKRKAKE 832
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERLEELKK-----KLKELEKRLEELEERHELYEEAKAKKEELER----LKKRLTGL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 833 AMEKEKKKVQDLENRLTKQKEELELKEQKEDVLSNKLNDALAMVEETQKTKA---------TESLKAESLA---LKLNET 900
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgrelTEEHRKELLEeytAELKRI 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 901 LAELETTKTK------------MILMEERLILQQKTVKAVQDEQESQRHGFEEEIMEYK--------------------- 947
Cdd:PRK03918 465 EKELKEIEEKerklrkelreleKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKaeeyeklkekliklkgeiksl 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 948 ----EQIKQHSQTIVSLEEKLQKVSQHHKKIEGEIATLKDNDPAQKEERPQDPLVAPTTDSGAKDMAyehliDDLLAAQK 1023
Cdd:PRK03918 545 kkelEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAE-----KELEREEK 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1024 EILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKM----ELERNVALVQQQSKELSVLKEKMAQMSSLTEKKDRELKAL 1099
Cdd:PRK03918 620 ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699
|
490
....*....|..
gi 1622834852 1100 KEALRASQEKHR 1111
Cdd:PRK03918 700 KEELEEREKAKK 711
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
13-86 |
7.65e-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: 51.59 E-value: 7.65e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622834852 13 VLNKSTTIGRHEDSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVN--ECHIQNVAVKLIPGDILRFGS 86
Cdd:cd22678 20 GTRLPLTIGRIQRGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNgeSISPNGRPVVLSSGDVITLGS 95
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
753-1127 |
1.04e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 753 TQENrvkeaLEEEQTRVQELEKRLARqkevLESsiahEKRKAKEALE-SEKRKVQDLEnhltqqkevsesSIAYEKRKAK 831
Cdd:COG1196 184 TEEN-----LERLEDILGELERQLEP----LER----QAEKAERYRElKEELKELEAE------------LLLLKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 832 EAMEKEKKKVQDLENRltkqkeelelkeqkedvlsnkLNDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKM 911
Cdd:COG1196 239 AELEELEAELEELEAE---------------------LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 912 ILMEERLILQQKTVKAVQDEQESQrhgfEEEIMEYKEQIKQHSQTIVSLEEKLQKVSQHHKKIEGEIATLKDNDPAQKEE 991
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEEL----EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 992 RpqdplvapttdsgakdmayEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELERNVALVQQQ 1071
Cdd:COG1196 374 L-------------------AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622834852 1072 SKELSVLKEKMAQMSSLTEKKDRELKALK--EALRASQEKHRLQLNTEKEQKSRKKTQ 1127
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLEllAELLEEAALLEAALAELLEELAEAAAR 492
|
|
| FHA_SNIP1_DDL-like |
cd22676 |
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA ... |
20-85 |
1.63e-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: 51.14 E-value: 1.63e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622834852 20 IGRHED-SDLVLQSPDIDNHHALIEY-----------NEAECSFVLqDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFG 85
Cdd:cd22676 25 IGRDRRvADIPLDHPSCSKQHAVIQFrevekrnegdvIENIRPYII-DLGSTNGTFLNGEKIEpRRYYELREKDVLKFG 102
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
679-1467 |
1.89e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 679 EHLAEKKQLNEERLEQEEKLKAKIRQLTEEKAALEERITQERNRANETLE-EERKRMQELESLLAQQKKALAESITQENR 757
Cdd:PTZ00121 1080 DFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKaEEARKAEDARKAEEARKAEDAKRVEIARK 1159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 758 VKEALEEEQTRVQELEKRLARQKEVLESSIAHEKRKAKEALESEKRKVQDlenhltQQKEVSESSIAYEKRKAKEAMEKE 837
Cdd:PTZ00121 1160 AEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAE------EERKAEEARKAEDAKKAEAVKKAE 1233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 838 KKKVQDLENRLTKQKEELELKEQKEDVLSNKLNDALAMVEETQKTKATESLKAESlalklnetlaelettktkmilmeer 917
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE------------------------- 1288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 918 lilqqktVKAVQDEQESQRHGFEEEIMEYKEQIKQHSQTIVSLEEKLQKVSQHHKKieGEIATLKDNDPAQKEERPQDPL 997
Cdd:PTZ00121 1289 -------KKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKK--AEEAKKAAEAAKAEAEAAADEA 1359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 998 VAPTTDSGAKDMAYEHLIDDLLAAQKEILSQQEViMKLRKDLTEAHSRMSDLRGELNEKQKMELERNVALVQQQSKELSV 1077
Cdd:PTZ00121 1360 EAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA-DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK 1438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1078 LKEKMAQMSSLtEKKDRELKALKEALRASQEKHRLQLNTEKEQKSRKKTQTCDTSVQIEPVHTEAFSSSQEEQSFSDLGV 1157
Cdd:PTZ00121 1439 KAEEAKKADEA-KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKK 1517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1158 KCKGSRHEEVIQRQKKALSELRARIKELEKAhapdhkdhqnESFLDLKNLRMKSNIQKIlldakpdlptlsrieilapqn 1237
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADEAKKAEEKKKA----------DELKKAEELKKAEEKKKA--------------------- 1566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1238 glcnarfssAMEKSGKMDVAEALELSEKLYLDMSKTLGSLMNIKDMSGHVSMKYLSRQERDKVNQLRQRDLDLVFDKITQ 1317
Cdd:PTZ00121 1567 ---------EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ 1637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1318 LKNQLERKEellrgyeKDVEQLRRSKVSVEMYQSQVAKLEDDIYKEAEEKALLKEALERMEHQLCQEKRINRAIRQQKES 1397
Cdd:PTZ00121 1638 LKKKEAEEK-------KKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1398 VEEhEPKNAKEptpcncaFKEKEKQRRVFVKMVKNRMQNSNSQVGTRKASLKMDQEREMLRKETSSKSSQ 1467
Cdd:PTZ00121 1711 EAE-EKKKAEE-------LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
649-796 |
1.94e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 649 KKLMSQTQELQIKFNSSQ------ETQQSLLQEKLREHLAEKKQLNEERLEQEEKLKAKIRQL----------------- 705
Cdd:COG4942 51 KALLKQLAALERRIAALArriralEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALyrlgrqpplalllsped 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 706 ---TEEKAALEERITQERNRANETLEEERKRMQELESLLAQQKKALAESITQENRVKEALEEEQTRVQELEKRLARQKEV 782
Cdd:COG4942 131 fldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE 210
|
170
....*....|....
gi 1622834852 783 LESSIAHEKRKAKE 796
Cdd:COG4942 211 LAAELAELQQEAEE 224
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
663-1009 |
2.74e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 663 NSSQETQQSLLQEKLREHLAEKKQLNEERLEQEEKLKA--KIRQLTEEKAALEE-RITQERNRANETLEEERKRMQElES 739
Cdd:PTZ00121 1461 EAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKadEAKKAAEAKKKADEaKKAEEAKKADEAKKAEEAKKAD-EA 1539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 740 LLAQQKKAlAESITQENRVKEAleEEQTRVQelEKRLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLT--QQKE 817
Cdd:PTZ00121 1540 KKAEEKKK-ADELKKAEELKKA--EEKKKAE--EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKaeEAKK 1614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 818 VSESSIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLSNKlndaLAMVEETQKTKATESLKAESLALKL 897
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE----EAKKAEEDKKKAEEAKKAEEDEKKA 1690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 898 NETLAELETTKTKMILMEERLILQQKTVKAVQDEQESQRHGFEEEIMEYKEQIKQHSQTIVSLEEKlQKVSQHHKKIEGE 977
Cdd:PTZ00121 1691 AEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK-KKIAHLKKEEEKK 1769
|
330 340 350
....*....|....*....|....*....|....
gi 1622834852 978 IATLKDNDPAQKEE--RPQDPLVAPTTDSGAKDM 1009
Cdd:PTZ00121 1770 AEEIRKEKEAVIEEelDEEDEKRRMEVDKKIKDI 1803
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
682-1215 |
3.10e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 682 AEKKQLNEERLEQEEKLKAKIRQLTEEKAALEERITQERNRANETLEEERKRMQElESLLAQQKKALAESITQENRVKEA 761
Cdd:PTZ00121 1245 AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAE-EKKKADEAKKKAEEAKKADEAKKK 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 762 LEEEQTRVQELEKRLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEVSESSIAYE---------KRKAKE 832
Cdd:PTZ00121 1324 AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEekkkadeakKKAEED 1403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 833 AMEKEKKKVQDLENRLTKQKEELELKEQKEDVLSNKLNDALAmvEETQKTKATESLKAESLALKLNETLAELETTKTKmi 912
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK--ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKA-- 1479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 913 lmEERLILQQKTVKAVQDEQESQRHGFEEEIMEYKEQIKQHSQtivslEEKLQKVSQHHKKIEGEIATLKDNDPAQKEER 992
Cdd:PTZ00121 1480 --EEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE-----AKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 993 PQDPLVAPTTDSGAKDMAYEHLIDDLLAAQKEILSQQE---VIMKLRKDLTEAHSRMSDLRGELNEKQKMELERNVALVQ 1069
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEearIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1070 QQSKELSVLKEKMAQMSSLTEKKDRE--LKALKEALRASQEKHRLQLNTEKEQKSRKKTQTCDTSVQIEPVHTEAFSSSQ 1147
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKKAEEEnkIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA 1712
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622834852 1148 EEQSFSDLGVKCKGSRHEEVIQRQKKALSELR----ARIKELEK---AHAPDHKDHQNESFLDLKNLRMKSNIQK 1215
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKkaeeAKKDEEEKkkiAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
641-944 |
3.57e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 55.13 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 641 LIYLLEHYKKLMSQTQelqikfnssQETQQSLLQEKLREHLAEKKQLNEERLEQEEKLKAKIRQLTEEKA--ALEERITQ 718
Cdd:pfam17380 274 LLHIVQHQKAVSERQQ---------QEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAiyAEQERMAM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 719 ERNRANETL-EEERKR----------------MQELESL-LAQQKKAlaESITQE----NRVKEALEEEQTRVQELEKRL 776
Cdd:pfam17380 345 ERERELERIrQEERKRelerirqeeiameisrMRELERLqMERQQKN--ERVRQEleaaRKVKILEEERQRKIQQQKVEM 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 777 ARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEVSESSIAYEKRKAKEAmekekkkvqDLENRLTKQKEELE 856
Cdd:pfam17380 423 EQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLEL---------EKEKRDRKRAEEQR 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 857 LKEQKEDVLSNKlndaLAMVEETQKTKATE-SLKAESLALKLNETLAELETTKTKMILMEERLILQQKTVKAVQDEQESQ 935
Cdd:pfam17380 494 RKILEKELEERK----QAMIEEERKRKLLEkEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLE 569
|
....*....
gi 1622834852 936 RHGFEEEIM 944
Cdd:pfam17380 570 AMEREREMM 578
|
|
| FHA_GarA_OdhI-like |
cd22684 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium ... |
18-91 |
7.10e-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: 48.92 E-value: 7.10e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622834852 18 TTIGRHEDSDLVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHIQnvAVKLIPGDILRFGSAGLTY 91
Cdd:cd22684 23 TTAGRHPESDIFLDDVTVSRRHAEFRRAEGG--FVVRDVGSLNGTYVNRERID--SAVLRNGDEVQIGKFRLVF 92
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
235-801 |
8.29e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 8.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 235 KEVSRLSDYEIESKykdviiaNLQKEVAELSQKLSETTTSRQNEREISQKCQVLDEDIDAKQKEIQSLKSQISALQKGYS 314
Cdd:PRK03918 152 RQILGLDDYENAYK-------NLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 315 QLlcqtlSERNSEITSLKNEGENLKRDNAIASGMVSSLQKDMLAKDEQVQELKEKVNQLKSQNKDkdhqlealgsrcsvL 394
Cdd:PRK03918 225 KL-----EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE--------------L 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 395 KEELKQEDAHRELREAQEKELKlcktQIQDMEKEMKKLRAELRkscteqsVISRTLREKSKVEEKLQEdSRRKLLQLQEM 474
Cdd:PRK03918 286 KELKEKAEEYIKLSEFYEEYLD----ELREIEKRLSRLEEEIN-------GIEERIKELEEKEERLEE-LKKKLKELEKR 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 475 GNReslikinLERAVGQLEHFRSQVIKATYGRAKpfpDKPVTDQQLIEKIAQVTEDNINFQQKKWTLQKETQLSNSKQEE 554
Cdd:PRK03918 354 LEE-------LEERHELYEEAKAKKEELERLKKR---LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 555 TTENIEKLRTSLDSCQACMKMscCTSDLKKEVDLLQHLQVSPPVSGLQKVVlDILRHALSWLEEVEQLLRDLGILpssad 634
Cdd:PRK03918 424 LKKAIEELKKAKGKCPVCGRE--LTEEHRKELLEEYTAELKRIEKELKEIE-EKERKLRKELRELEKVLKKESEL----- 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 635 kgfsLYLIYLLEHYKKLMSQTQELQIKFNSSQETQQSLLQEKLREHLAEKKQLNEErLEQEEKLKAKIRQLTEEKAALEE 714
Cdd:PRK03918 496 ----IKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE-LEKLEELKKKLAELEKKLDELEE 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 715 R----ITQERNRANETLEEERKRMQELESLLAQQKKaLAESITQENRVKEALEEEQTRVQELEKRLARQKEVLEssiahE 790
Cdd:PRK03918 571 ElaelLKELEELGFESVEELEERLKELEPFYNEYLE-LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE-----E 644
|
570
....*....|.
gi 1622834852 791 KRKAKEALESE 801
Cdd:PRK03918 645 LRKELEELEKK 655
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
394-817 |
8.33e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 8.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 394 LKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKsCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQE 473
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK-LEKLLQLLPLYQELEALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 474 MGNRESLIKiNLERAVGQLEHFRSQVIKAtygRAKPFPDKPVTDQQLIEKIAQVtedninfQQKKWTLQKETQLSNSKQE 553
Cdd:COG4717 155 LEELRELEE-ELEELEAELAELQEELEEL---LEQLSLATEEELQDLAEELEEL-------QQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 554 ETTENIEKLRTSLDScqacmkmscctsdlKKEVDLLQHLQVSPPVSGLQKVVLDILRHALSWLEEVEQLLRDLGilpssa 633
Cdd:COG4717 224 ELEEELEQLENELEA--------------AALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVL------ 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 634 dkGFSLYLIYLLEHYKKLMSQTQELQIKFNSSQETQQSLLQEKLREHLAEKKQLNEERLEQEEKLkAKIRQLTEEKAALE 713
Cdd:COG4717 284 --GLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRI-EELQELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 714 ERITQERNRanetleeerkrmQELESLLAQQKKALAESITQENRVKEALEEEQTRVQELEKRLARQ-KEVLESSIAHEKR 792
Cdd:COG4717 361 EELQLEELE------------QEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELlGELEELLEALDEE 428
|
410 420
....*....|....*....|....*
gi 1622834852 793 KAKEALESEKRKVQDLENHLTQQKE 817
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELRE 453
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
352-826 |
1.21e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 352 LQKDMLAKDEQVQELKEKVNQLKSQNKDKDHQLEALGSRCSVLKEEL----KQEDAHRELREAQEKELKLCKTQIQDMEK 427
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELarleQDIARLEERRRELEERLEELEEELAELEE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 428 EMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESLIKINLERAVGQLEHFRSQVIKATYGRA 507
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 508 kpfpDKPVTDQQLIEKIAQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKmscctSDLKKEVD 587
Cdd:COG1196 411 ----ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA-----LLEAALAE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 588 LLQHLQVSPPVSGLQKVVLD---------ILRHALSWLEEVEQLLRDLGILPSSADKGFSLYLIYLLEHYKKLMSQTQEL 658
Cdd:COG1196 482 LLEELAEAAARLLLLLEAEAdyegflegvKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAA 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 659 QIKFNSSQ------------ETQQSLLQEKLREHLAEKKQLNEERLEQEEKLKAKIRQLTEEKAALEERITQERNRANET 726
Cdd:COG1196 562 AIEYLKAAkagratflpldkIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVT 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 727 LEEERKR---------MQELESLLAQQKKALAESITQENRVKEALEEEQTRVQELEKRLARQKEVLESSIAHEKRKAKEA 797
Cdd:COG1196 642 LAGRLREvtlegeggsAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEEL 721
|
490 500
....*....|....*....|....*....
gi 1622834852 798 LESEKRKVQDLENHLTQQKEVSESSIAYE 826
Cdd:COG1196 722 EEEALEEQLEAEREELLEELLEEEELLEE 750
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
225-826 |
1.55e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 53.16 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 225 DKDEIILLLGKEVSRLSDYEIESKykDVIIANLQKEVAELSQKLSEtttsrqnereisqkcqvLDEDIdakqKEIQSLKS 304
Cdd:COG5022 843 KAEVLIQKFGRSLKAKKRFSLLKK--ETIYLQSAQRVELAERQLQE-----------------LKIDV----KSISSLKL 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 305 QISALQKGYSQLLCQTLSERNSEITSLKNEGENLKRdnAIASGMVSSLQKDMLAKDEQVQELKEKVNQLKSQNKDKDHQL 384
Cdd:COG5022 900 VNLELESEIIELKKSLSSDLIENLEFKTELIARLKK--LLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLL 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 385 EALGSrcsvLKEELKQEdahRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDS 464
Cdd:COG5022 978 KKSTI----LVREGNKA---NSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILKPLQK 1050
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 465 RRKLLQLQEMGNRESLIKINLERAVGQLEHFRSQVIKATYGRAK--PFPDKPVTDQQLIEKIAQVteDNINFQQKKWTLQ 542
Cdd:COG5022 1051 LKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKtiNVKDLEVTNRNLVKPANVL--QFIVAQMIKLNLL 1128
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 543 KETQLSNSKQEETTENIEKLRTSLDScqacmkmsccTSDLKKEVDLLQHLQVSPPVSGLQKVVL---DILRHALSWLEEV 619
Cdd:COG5022 1129 QEISKFLSQLVNTLEPVFQKLSVLQL----------ELDGLFWEANLEALPSPPPFAALSEKRLyqsALYDEKSKLSSSE 1198
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 620 EQLLRDLGILPSSADKGFSLYLIYLLEHYKKLMSQTQELQ-----IKFNSSQETQQSLLQEKLREHLAEKKQLNEERLEQ 694
Cdd:COG5022 1199 VNDLKNELIALFSKIFSGWPRGDKLKKLISEGWVPTEYSTslkgfNNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLE 1278
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 695 EEKLKAKIRQL-TEEKAALEERITQERNRANETLEEERKRMQELESLLAQQKKAlaesitqeNRVKEALEEeqtrvqelE 773
Cdd:COG5022 1279 EEVLPATINSLlQYINVGLFNALRTKASSLRWKSATEVNYNSEELDDWCREFEI--------SDVDEELEE--------L 1342
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622834852 774 KRLARQKEVLESSIAH--EKRKAKEALES-------EKRKVQDLENHLTQQ--KEVSESSIAYE 826
Cdd:COG5022 1343 IQAVKVLQLLKDDLNKldELLDACYSLNPaeiqnlkSRYDPADKENNLPKEilKKIEALLIKQE 1406
|
|
| Yop-YscD_cpl |
pfam16697 |
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ... |
19-86 |
1.58e-06 |
|
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: 47.64 E-value: 1.58e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622834852 19 TIGRHEDSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRFGS 86
Cdd:pfam16697 20 RIGSDPDCDIVLSDKEVSRVHLKLEVDDE--GWRLDDLGSGNGTLVNGQRVTELGIALRPGDRIELGQ 85
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
665-828 |
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 1622834852 665 SQETQQSLLQEKLREHLAEKKQLNEERleqeEKLKAKIRQLTEEKAALEERIT----------QERNRANETLEEERKRM 734
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKEL----AALKKEEKALLKQLAALERRIAalarriraleQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 735 QELESLLAQQKKALAE----------------------------------SITQENRVK-EALEEEQTRVQELEKRLARQ 779
Cdd:COG4942 93 AELRAELEAQKEELAEllralyrlgrqpplalllspedfldavrrlqylkYLAPARREQaEELRADLAELAALRAELEAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622834852 780 KEVLESSIAhEKRKAKEALESEKRKVQDLENHLTQQKEVSESSIAYEKR 828
Cdd:COG4942 173 RAELEALLA-ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
|
| FHA_EspA-like |
cd22698 |
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ... |
15-92 |
2.00e-06 |
|
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA is a histidine protein kinase with a fork head-associated (FHA) domain at the N-terminus and a receiver domain at the C-terminus. It functions as an inhibitor of sporulation during early fruiting body development while cells are aggregating into raised mounds. EspA is part of a two-component signal transduction system that regulates the timing of sporulation initiation. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438750 [Multi-domain] Cd Length: 93 Bit Score: 47.41 E-value: 2.00e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622834852 15 NKSTTIGRHEDSDLVLQSPDIDNHHALIEYNEAECsfVLQDFNSRNGTFVNECHIQNVAVKliPGDILRFGSAGLTYE 92
Cdd:cd22698 20 QDEFTIGRSSNNDIRLNDHSVSRHHARIVRQGDKC--NLTDLGSTNGTFLNGIRVGTHELK--HGDRIQLGETIFRFI 93
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
239-824 |
2.96e-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: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 239 RLSDYEIESKYKDVIIANLQKEVAELSQKLSETTtsRQNEREISQKCQVLDEDIDAKQKEIQSLKSQISALQ---KGYSQ 315
Cdd:pfam12128 259 RLSHLHFGYKSDETLIASRQEERQETSAELNQLL--RTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEdqhGAFLD 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 316 LLCQTLSERNSEITSLKNEGENLKRDNAIASGMVSSLQKDMLAKDEQV-QELKEKVNQLKS----QNKDKDHQLEA---- 386
Cdd:pfam12128 337 ADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIkEQNNRDIAGIKDklakIREARDRQLAVaedd 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 387 LGSRCSVLKEELKQedAHRELREAQEK------ELKL----------CKTQIQDMEKEMKKLRAELRKSCTEQSVISRTL 450
Cdd:pfam12128 417 LQALESELREQLEA--GKLEFNEEEYRlksrlgELKLrlnqatatpeLLLQLENFDERIERAREEQEAANAEVERLQSEL 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 451 REKSKVEEKLQEDSRRKLLQLQEMGNRESLIKINLERAVGQLEHF-RSQVIKATYGRAKpfpdkpVTDQQLI-------E 522
Cdd:pfam12128 495 RQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFlRKEAPDWEQSIGK------VISPELLhrtdldpE 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 523 KIAQVTEDNINFQQKKWTLQK-ETQLSNSKQEETTENIEKLRTSLDSCQACMK-MSCCTSDLKKEVDLLQhLQVSPPVSG 600
Cdd:pfam12128 569 VWDGSVGGELNLYGVKLDLKRiDVPEWAASEEELRERLDKAEEALQSAREKQAaAEEQLVQANGELEKAS-REETFARTA 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 601 LQKVVLDILRhalsWLEEVEQLLRDLGilpssadkgfslylIYLLEHYKKLMSQTQELQIKFNSSQETQQSLLQEKLREH 680
Cdd:pfam12128 648 LKNARLDLRR----LFDEKQSEKDKKN--------------KALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQK 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 681 LAEKKQLNEERLEQEEKLKAKIRQLTEEKAALEEritqERNRANETLEEERKRmqELESLLAQQkkalaESITQENRVKE 760
Cdd:pfam12128 710 REARTEKQAYWQVVEGALDAQLALLKAAIAARRS----GAKAELKALETWYKR--DLASLGVDP-----DVIAKLKREIR 778
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622834852 761 ALEEEQTRVQELEKRLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEVSESSIA 824
Cdd:pfam12128 779 TLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRA 842
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
654-825 |
3.09e-06 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 51.62 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 654 QTQELQIKFnSSQETQQSllqEKLrehLAEKKQLNEERLEQEEKLKAKIRQLTEEKAALEERITQERnranETLEEERKR 733
Cdd:PRK11637 138 EHTGLQLIL-SGEESQRG---ERI---LAYFGYLNQARQETIAELKQTREELAAQKAELEEKQSQQK----TLLYEQQAQ 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 734 MQELESLLAQQKKALAEsitqenrVKEALEEEQTRVQELekrlaRQKEV-LESSIAHEKRKAKEALESEKRKVQDLENhl 812
Cdd:PRK11637 207 QQKLEQARNERKKTLTG-------LESSLQKDQQQLSEL-----RANESrLRDSIARAEREAKARAEREAREAARVRD-- 272
|
170
....*....|...
gi 1622834852 813 tQQKEVSESSIAY 825
Cdd:PRK11637 273 -KQKQAKRKGSTY 284
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
715-1206 |
3.62e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 715 RITQERNRANETLEEERKRMQELESLLAQQKKALAESITQENRVKEALEEEQTRVQELEKRLARQKEVLEssIAHEKRKA 794
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE--EIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 795 KEALESEKRKVQDLENHLTQQKEvsessiayEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLsNKLNDALA 874
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIE--------ELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDEL-REIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 875 MVEETQKTKATESLKAESLALKLNETLAELETTKTKMILMEERLILQQKtVKAVQDEQESQRHGFE-EEIMEYKEQIKQH 953
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEE-AKAKKEELERLKKRLTgLTPEKLEKELEEL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 954 SQTIVSLEEKLQKVSQHHKKIEGEIATLKDNDPAQKEERPQDPLVAPTTDSGAKDMAYEHLIDDLLAAQKEILSQQEVIM 1033
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKER 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1034 KLRKDLTEAH---------SRMSDLRGELNEKQKMELERNVALVQQQSKELSVLKEKMAQMS---SLTEKKDRELKALKE 1101
Cdd:PRK03918 477 KLRKELRELEkvlkkeselIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKgeiKSLKKELEKLEELKK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1102 ALRA------SQEKHRLQLNTEKEQKSRKKTQTCDTSVQ-IEPVHTEAFSSSQEEQSFSDLGVKCKGSRHE-----EVIQ 1169
Cdd:PRK03918 557 KLAElekkldELEEELAELLKELEELGFESVEELEERLKeLEPFYNEYLELKDAEKELEREEKELKKLEEEldkafEELA 636
|
490 500 510
....*....|....*....|....*....|....*..
gi 1622834852 1170 RQKKALSELRARIKELEKAHAPDHKDHQNESFLDLKN 1206
Cdd:PRK03918 637 ETEKRLEELRKELEELEKKYSEEEYEELREEYLELSR 673
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
673-816 |
3.68e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 673 LQEKLREHLAEKKQLNEERLEQE-EKLKAKIRQLTEEKAALEERITQERNRANETLEEERKRMQELESLLAQQKKALAES 751
Cdd:COG4913 267 ARERLAELEYLRAALRLWFAQRRlELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLERE 346
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622834852 752 ITQENRVKEALEEEQTRVQELEKRLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQK 816
Cdd:COG4913 347 IERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAE 411
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
691-814 |
4.01e-06 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 51.62 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 691 RLEQE------EKLKAKIRQLTEEKAALE-ERITQERNRANETLEEERKRMQELESLLAQQKKALaESITQENRVKEALE 763
Cdd:COG0542 403 RMEIDskpeelDELERRLEQLEIEKEALKkEQDEASFERLAELRDELAELEEELEALKARWEAEK-ELIEEIQELKEELE 481
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622834852 764 EEQTRVQELEKRLARQKEVLESSIAHEKRKAKEA-----------------LESEKRKVQDLENHLTQ 814
Cdd:COG0542 482 QRYGKIPELEKELAELEEELAELAPLLREEVTEEdiaevvsrwtgipvgklLEGEREKLLNLEEELHE 549
|
|
| FHA_NBN |
cd22667 |
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ... |
11-91 |
4.49e-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: 4.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 11 FFVLNKSTTIGRHEDSDLVLQSPDIDNHHALI--EYNEAECSF-------VLQDFnSRNGTFVNECHIQNVA-VKLIPGD 80
Cdd:cd22667 15 YLLPGGEYTVGRKDCDIIIVDDSSISRKHATLtvLHPEANLSDpdtrpelTLKDL-SKYGTFVNGEKLKGGSeVTLKDGD 93
|
90
....*....|.
gi 1622834852 81 ILRFGSAGLTY 91
Cdd:cd22667 94 VITFGVLGSKF 104
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
361-982 |
5.08e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.17 E-value: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 361 EQVQELKEKVNQLKSQNKDKDHQLEALGSRCSVLKEELKQEdahRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSC 440
Cdd:TIGR04523 75 NKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKND---KEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 441 TEQSVISRTLREKSKVEEKLQEDsrrKLLQLQEMGNRESLI-KINLERAvgQLEHFRSqVIKATYGRAKPFPDKPVT-DQ 518
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENE---LNLLEKEKLNIQKNIdKIKNKLL--KLELLLS-NLKKKIQKNKSLESQISElKK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 519 QLIEKIAQVTEDNINFQQKKWTLQK-ETQLSNSKQEETTENIEKLRTSLDSCQACMKMSCCTSDLKKEVDLLQHLQvspp 597
Cdd:TIGR04523 226 QNNQLKDNIEKKQQEINEKTTEISNtQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLN---- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 598 vsglQKVVLDILRHALSWLEEVEQLLRDLGILPSSADKGFSlyliyllehykKLMSQTQELQIKFNSSQETQQSLlqekl 677
Cdd:TIGR04523 302 ----NQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIIS-----------QLNEQISQLKKELTNSESENSEK----- 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 678 REHLAEKKQLNEERLEQEEKLKAKIRQLTEEKAALEERITQERNRANETLEEERKRMQELESLLAQQKKALAESITQENR 757
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 758 VKEaLEEEQTRVQELEKRLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEVSEssiayekrkakeameke 837
Cdd:TIGR04523 442 IKD-LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE----------------- 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 838 kkKVQDLENRLTKQKEELELKEQKEDVLSNklndalamvEETQKTKATESLKAESLALKLNETLAELETTKTKMILMEER 917
Cdd:TIGR04523 504 --EKKELEEKVKDLTKKISSLKEKIEKLES---------EKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEE 572
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622834852 918 LILQQKTVKAVQDEQESQRHGFEEEIMEYKEQIKQHSQTIVSLEEKLQKVSQHHKKIEGEIATLK 982
Cdd:TIGR04523 573 LKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIK 637
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
261-817 |
6.77e-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: 50.99 E-value: 6.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 261 VAELSQKLSETTTSRQNEREIS---------QKCQVLDEDIDAKQKEIQSLKS---QISALQKGYSQLLCQTLSERNSEI 328
Cdd:pfam12128 203 VAILEDDGVVPPKSRLNRQQVEhwirdiqaiAGIMKIRPEFTKLQQEFNTLESaelRLSHLHFGYKSDETLIASRQEERQ 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 329 TSLKNEGENLKRDNAIASGMVSSLQKDMLAKDEQVQELKEKVNQLKSQNKdkdhqlEALGSRCSVLKEELKQEDAHRELR 408
Cdd:pfam12128 283 ETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHG------AFLDADIETAAADQEQLPSWQSEL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 409 EAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESLIKINLERA 488
Cdd:pfam12128 357 ENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFN 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 489 VGQLEhfrsqvIKATYGRAKPFPDKPVTDQQLIEKIAqvtedniNFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDs 568
Cdd:pfam12128 437 EEEYR------LKSRLGELKLRLNQATATPELLLQLE-------NFDERIERAREEQEAANAEVERLQSELRQARKRRD- 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 569 cQACMKMSCCT---SDLKKEVDLLQHlQVSPPVSGLqkvvLDILR-HALSWLEeveqllrDLGILPSSAdkgfslyliyl 644
Cdd:pfam12128 503 -QASEALRQASrrlEERQSALDELEL-QLFPQAGTL----LHFLRkEAPDWEQ-------SIGKVISPE----------- 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 645 lehykkLMSQTQELQIKFNSSQETQQSLLQEKLRehlaekkqlneerLEQEEklkakirqlTEEKAALEERITQERNRAN 724
Cdd:pfam12128 559 ------LLHRTDLDPEVWDGSVGGELNLYGVKLD-------------LKRID---------VPEWAASEEELRERLDKAE 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 725 ETLEEERKRMQELESLLAQQKKALAESITQENRVKEALEEEQTRVQELEKRLARQKEVLESSIAHEKRKAKEALESEKRK 804
Cdd:pfam12128 611 EALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQ 690
|
570
....*....|...
gi 1622834852 805 VQDLENHLTQQKE 817
Cdd:pfam12128 691 LKQLDKKHQAWLE 703
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
654-970 |
9.09e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 50.68 E-value: 9.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 654 QTQELQIKFNSSQETQQSLLQEKLREHLA--EKKQLNEERLEQEEK----LKAKIRQLTEEKAALEERITQERNR--ANE 725
Cdd:PRK11281 42 QAQLDALNKQKLLEAEDKLVQQDLEQTLAllDKIDRQKEETEQLKQqlaqAPAKLRQAQAELEALKDDNDEETREtlSTL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 726 TLEEERKRMQELESLLAQQKKALAE-------SITQENRVKEALEEEQTRVQELEKRLARQKEvlessiahekrkAKEAL 798
Cdd:PRK11281 122 SLRQLESRLAQTLDQLQNAQNDLAEynsqlvsLQTQPERAQAALYANSQRLQQIRNLLKGGKV------------GGKAL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 799 ESEKRKVQDLENHLTQQKevsessIAYEKrkakeamekekkkvQDLENrltkqkeelelkeqkedvlsnklNDALAMVEE 878
Cdd:PRK11281 190 RPSQRVLLQAEQALLNAQ------NDLQR--------------KSLEG-----------------------NTQLQDLLQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 879 TQKTKATESLKaeslalKLNETLAELETtktkmILMEERLILQQKTVKAVQDEQESQRHGFEEEIMEYKEQIKQHSQTIV 958
Cdd:PRK11281 227 KQRDYLTARIQ------RLEHQLQLLQE-----AINSKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLL 295
|
330
....*....|..
gi 1622834852 959 SLEEKLQKVSQH 970
Cdd:PRK11281 296 KATEKLNTLTQQ 307
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
675-817 |
9.28e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 9.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 675 EKLREHLAEKKQLNEERLEQEEKLK---AKIRQLTEEKAALEERITQERNRANE---TLEEERKRMQELESLLAQQKKAL 748
Cdd:PRK02224 481 EAELEDLEEEVEEVEERLERAEDLVeaeDRIERLEERREDLEELIAERRETIEEkreRAEELRERAAELEAEAEEKREAA 560
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622834852 749 AEsitqenrVKEALEEEQTRVQELEKRLARQKEVLES-----SIAHEKRKAKEALESEKRKVQDLENHLTQQKE 817
Cdd:PRK02224 561 AE-------AEEEAEEAREEVAELNSKLAELKERIESlerirTLLAAIADAEDEIERLREKREALAELNDERRE 627
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
218-438 |
1.03e-05 |
|
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: 50.45 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 218 EEDLAQQDKDEIILLLGKEVSRLSDYEIESKYKDVIIANLQKEVAELSQKLSEtttSRQNEREISQKCQVLDEDIDAKQK 297
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE---LEEDLSSLEQEIENVKSELKELEA 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 298 EIQSLKSQISALQKGYSQLLCQTLSERNSEITSLKNE-GENLKRDNAIASGMVSSLQKDMLAK---DEQVQELKEKVNQL 373
Cdd:TIGR02169 766 RIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKlEEEVSRIEARLREIEQKLNRLTLEKeylEKEIQELQEQRIDL 845
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622834852 374 KSQNKDKDHQLEALGSRcsvlKEELKQEDAHRELREAQ-EKELKLCKTQIQDMEKEMKKLRAELRK 438
Cdd:TIGR02169 846 KEQIKSIEKEIENLNGK----KEELEEELEELEAALRDlESRLGDLKKERDELEAQLRELERKIEE 907
|
|
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
13-85 |
1.04e-05 |
|
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: 46.49 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 13 VLNKSTTIGRH------EDSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQ-----NVAVKLIPGDI 81
Cdd:cd22679 21 VLDEPVKIGRSvararpAANNAIFDCKVLSRNHALLWYDDG--KFYLQDTKSSNGTFVNNQRLSkgseeSEPRELHSGDI 98
|
....
gi 1622834852 82 LRFG 85
Cdd:cd22679 99 VQFG 102
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
12-85 |
1.48e-05 |
|
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing protein ArnA and similar proteins; ArnA is an FHA domain-containing protein from Sulfolobus acidocaldarius that was shown to strongly interact with ArnB, a von Willebrand domain-containing protein. They act synergistically and negatively to modulate motility. ArnA is involved in regulating archaella expression in S. acidocaldarius. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438732 [Multi-domain] Cd Length: 96 Bit Score: 45.02 E-value: 1.48e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622834852 12 FVLNKST-TIGRHEDSDLVLQSPDIDNHHALIeYNEaECSFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRFG 85
Cdd:cd22680 16 FPFDFSSvSIGRDPENVIVIPDPFVSRNHARI-TVD-SNEIYIEDLGSTNGTFVNDFKRIKGPAKLHPNDIIKLG 88
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
255-997 |
1.51e-05 |
|
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: 49.68 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 255 ANLQKEVAELSQKLSETTTSRQNEREISQKCQVLDEDIDAKQKEIQSLKSQISALQKGySQLLCQTLSERNSEITSLKNE 334
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE-FAETRDELKDYREKLEKLKRE 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 335 GENLKRDnaiasgmVSSLQKDMLAKDEQVQELKEKVNQLKSQNKDKDHQLEALGSRCSVLKEELKQEdahRELREAQEKE 414
Cdd:TIGR02169 401 INELKRE-------LDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL---AADLSKYEQE 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 415 LKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESLIKINLERAVGQLEH 494
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLN 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 495 F-----------------RSQVIKATY-----GRAKPFPDKPVTDQQLIEKIAQVTEDNINFQQKKWTLQKETQLsnskq 552
Cdd:TIGR02169 551 NvvveddavakeaiellkRRKAGRATFlplnkMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLV----- 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 553 eetTENIEKLRTSLDScqacMKMSCCTSDLKKEVDLLQHLQVSPpvSGLQKVVLDILRHALSWLEEVEQLLRDLGILPS- 631
Cdd:TIGR02169 626 ---VEDIEAARRLMGK----YRMVTLEGELFEKSGAMTGGSRAP--RGGILFSRSEPAELQRLRERLEGLKRELSSLQSe 696
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 632 --SADKGFSLYLIYLLEHYKK---LMSQTQELQIKFNSSQE------TQQSLLQEKLREHLAEKKQLNEERLEQEEKLKA 700
Cdd:TIGR02169 697 lrRIENRLDELSQELSDASRKigeIEKEIEQLEQEEEKLKErleeleEDLSSLEQEIENVKSELKELEARIEELEEDLHK 776
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 701 KIRQLTEEKAALEERITQERNRANETLEEERKRmqeLESLLAQQKKALAESITQENRVKEALEEEQTRVQELEKRLARQK 780
Cdd:TIGR02169 777 LEEALNDLEARLSHSRIPEIQAELSKLEEEVSR---IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE 853
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 781 EVLESSIAhEKRKAKEALESEKRKVQDLENHLTQ-QKEVSEssIAYEKRKAKEAMEKEKKKVQDLENRLtkqKEELELKE 859
Cdd:TIGR02169 854 KEIENLNG-KKEELEEELEELEAALRDLESRLGDlKKERDE--LEAQLRELERKIEELEAQIEKKRKRL---SELKAKLE 927
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 860 QKEDVLSNKLNDALAMVEETQKTKATESLKAEslALKLNETLAELETTKTKMILMEERLILQQKTVKAVQDEQESQRHGF 939
Cdd:TIGR02169 928 ALEEELSEIEDPKGEDEEIPEEELSLEDVQAE--LQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAI 1005
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622834852 940 EEEIMEYKEQIKQhsqtivSLEEKLQKVSQHHKKIegeIATLKDNDPAQKEERPQDPL 997
Cdd:TIGR02169 1006 LERIEEYEKKKRE------VFMEAFEAINENFNEI---FAELSGGTGELILENPDDPF 1054
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
664-824 |
1.52e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 664 SSQETQQSLLQEKLREHLAEKKQLNE--ERLEQE-EKLKAKIRQLTEEKAALEERITQERNRANETLEEERKRMQE---- 736
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAelEELNEEyNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAlyrs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 737 -------------------------LESLLAQQKKALAESITQENRV---KEALEEEQTRVQELEKRLARQKEVLESSIA 788
Cdd:COG3883 99 ggsvsyldvllgsesfsdfldrlsaLSKIADADADLLEELKADKAELeakKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622834852 789 hEKRKAKEALESEKRKVQDLENHLTQQKEVSESSIA 824
Cdd:COG3883 179 -EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
645-1111 |
1.63e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 645 LEHYKKLMSQTQELQIKFNSSQETQQSLlqEKLREHLAEKKQLNEERLEQEEKLKAKIR--QLTEEKAALEERITQERNR 722
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEEL--EELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 723 anetLEEERKRMQELESLLAQQKKALAESITQENRVKEALEEEQTRVQELEKRLARQKEVLESsiahEKRKAKEALESEK 802
Cdd:COG4717 148 ----LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ----RLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 803 RKVQDLENHLTQQKEVSESSIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKE-----------QKEDVLSNKLND 871
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAgvlflvlgllaLLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 872 ALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMILMEERLI-LQQKTVKAVQDEQESQRHGFEEEIMEYKEQI 950
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEeLQELLREAEELEEELQLEELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 951 KQHSqtIVSLEEKLQKVSQHHkKIEGEIATLKDNdpaqkeerpqdplvaptTDSGAKDMAYEHLIDDLLAAQKEILSQQE 1030
Cdd:COG4717 380 GVED--EEELRAALEQAEEYQ-ELKEELEELEEQ-----------------LEELLGELEELLEALDEEELEEELEELEE 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1031 VIMKLRKDLTEAHSRMSDLRGELNekqkmELERNVALVQQQsKELSVLKEKMAQMssltEKKDRELKALKEALRASQEKH 1110
Cdd:COG4717 440 ELEELEEELEELREELAELEAELE-----QLEEDGELAELL-QELEELKAELREL----AEEWAALKLALELLEEAREEY 509
|
.
gi 1622834852 1111 R 1111
Cdd:COG4717 510 R 510
|
|
| FHA_FhaA-like |
cd22668 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
17-89 |
1.65e-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: 44.76 E-value: 1.65e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622834852 17 STTIGRHEDSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQnVAVKLIPGDILRFGSAGL 89
Cdd:cd22668 19 SNIIGRGSDADFRLPDTGVSRRHAEIRWDGQ--VAHLTDLGSTNGTTVNNAPVT-PEWRLADGDVITLGHSEI 88
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
649-824 |
1.65e-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: 48.99 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 649 KKLMSQTQELQIKFNSSQETQQSLLQE--KLREHLAEKKQLNEERLEQEEKLKAKIRQLTEEKAALEERITQERNR---- 722
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQlaALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElael 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 723 -----------------ANETLEEERKRMQELESLLAQQKK---ALAESITQENRVKEALEEEQTRVQELEKRLARQKEV 782
Cdd:COG4942 110 lralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREqaeELRADLAELAALRAELEAERAELEALLAELEEERAA 189
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622834852 783 LESSIAhEKRKAKEALESEKRKVQDLENHLTQQKEVSESSIA 824
Cdd:COG4942 190 LEALKA-ERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
216-817 |
1.70e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.58 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 216 YVEEDLAQQDKDEIILLLGKEVSRLSDYEIESKykdvIIANLQKEVaELSQKLSETTTSRQNEREISQKCQVLDEDIDAK 295
Cdd:TIGR00618 245 LTQKREAQEEQLKKQQLLKQLRARIEELRAQEA----VLEETQERI-NRARKAAPLAAHIKAVTQIEQQAQRIHTELQSK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 296 QKEIQSLKSQISALQKGYSQLLCQTLSERNSEITSLKNEGENLKrdnaiasgmvsslQKDMLAKDEQVQELKEKVNQLKS 375
Cdd:TIGR00618 320 MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEV-------------ATSIREISCQQHTLTQHIHTLQQ 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 376 QNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKS- 454
Cdd:TIGR00618 387 QKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAq 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 455 -----------------KVEEKLQEDSRRK-LLQLQEMGNRESLIKINLER-AVGQLEHFRSQVIKATYGRAKPFPDKPV 515
Cdd:TIGR00618 467 slkereqqlqtkeqihlQETRKKAVVLARLlELQEEPCPLCGSCIHPNPARqDIDNPGPLTRRMQRGEQTYAQLETSEED 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 516 TDQQLIEKIAQVTEDNINFQQKKWTLQKETQLSNskqeETTENIEKLRtsldscqacmkmscctsdlkKEVDLLQHLqvs 595
Cdd:TIGR00618 547 VYHQLTSERKQRASLKEQMQEIQQSFSILTQCDN----RSKEDIPNLQ--------------------NITVRLQDL--- 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 596 ppvsglqkvVLDILRHALSWLEEVEQLLRDLGIlpssadkgfslyLIYLLEHYKKLMSQTQELQIKFNSSQETQQSLLQE 675
Cdd:TIGR00618 600 ---------TEKLSEAEDMLACEQHALLRKLQP------------EQDLQDVRLHLQQCSQELALKLTALHALQLTLTQE 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 676 KLREHLAEKKQLNEERLEQ----EEKLKAKIRQLTEEKAALEERITQERNRaNETLEEERKRMQELESLLAQQKKALAES 751
Cdd:TIGR00618 659 RVREHALSIRVLPKELLASrqlaLQKMQSEKEQLTYWKEMLAQCQTLLREL-ETHIEEYDREFNEIENASSSLGSDLAAR 737
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622834852 752 ITQENRVKEALEEEQTRV---QELEKRLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKE 817
Cdd:TIGR00618 738 EDALNQSLKELMHQARTVlkaRTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEA 806
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
15-87 |
1.84e-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: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 15 NKSTTIGR--HEDSD---LVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHIQ------NVAVKLIPGDILR 83
Cdd:cd22702 31 KQPCIIGSdpHQAISgisVVIPSPQVSELHARITCKNGA--FFLTDLGSEHGTWINDNEGRryrappNFPVRLHPSDVIE 108
|
....
gi 1622834852 84 FGSA 87
Cdd:cd22702 109 FGSD 112
|
|
| VI_FHA |
TIGR03354 |
type VI secretion system FHA domain protein; Members of this protein family are FHA ... |
19-100 |
2.08e-05 |
|
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: 48.52 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 19 TIGRHEDSDLVLQSPD--IDNHHALIEYNEAecSFVLQDFnSRNGTFVNECH---IQNVAVKLIPGDILRFGSagltYEL 93
Cdd:TIGR03354 27 TIGRSEDCDWVLPDPErhVSGRHARIRYRDG--AYLLTDL-STNGVFLNGSGsplGRGNPVRLEQGDRLRLGD----YEI 99
|
....*..
gi 1622834852 94 VVENPPP 100
Cdd:TIGR03354 100 RVSLGDP 106
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
287-425 |
2.52e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 48.04 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 287 VLDEDIDAKQKEIQSLKSQIS------ALQKGYSQLLCQTLSERNSEITSLKNEGENLKRDNAIASGMVSSLQKdmlakd 360
Cdd:PRK09039 43 FLSREISGKDSALDRLNSQIAeladllSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEG------ 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622834852 361 eQVQELKEKVNQLKSQNKDKDHQLEALGSRCSVLKEELKqedAHRELREAQEKELKLCKTQIQDM 425
Cdd:PRK09039 117 -RAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLA---ALEAALDASEKRDRESQAKIADL 177
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
254-492 |
2.64e-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: 48.22 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 254 IANLQKEVAELSQKLSETttsRQNEREISQKCQVLDEDIDAKQKEIQSLKSQISALQkgysqllcQTLSERNSEITSLKN 333
Cdd:COG4942 29 LEQLQQEIAELEKELAAL---KKEEKALLKQLAALERRIAALARRIRALEQELAALE--------AELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 334 EgenLKRDNAIASGMVSSLQK-------DMLAKDEQVQELKEKVNQLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRE 406
Cdd:COG4942 98 E---LEAQKEELAELLRALYRlgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 407 LREAQEKELKLCKTQIQDMEKEMKKLRAELRKsctEQSVISRTLREKSKVEEKLQEDSRRklLQLQEMGNRESLIKINLE 486
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEK---ELAELAAELAELQQEAEELEALIAR--LEAEAAAAAERTPAAGFA 249
|
....*.
gi 1622834852 487 RAVGQL 492
Cdd:COG4942 250 ALKGKL 255
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
688-848 |
2.80e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 688 NEERLEQeekLKAKIRQLTEEKAALEERItQERNRANETLEEERKRMQELESLLAQQK--KALAESITQENRVKEALEEE 765
Cdd:COG4913 608 NRAKLAA---LEAELAELEEELAEAEERL-EALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 766 QTRVQELEKRLARQKEVLEssiahEKRKAKEALESEKRKVQD-LENHLTQQKEVsessiayEKRKAKEAMEKEKKKVQDL 844
Cdd:COG4913 684 SDDLAALEEQLEELEAELE-----ELEEELDELKGEIGRLEKeLEQAEEELDEL-------QDRLEAAEDLARLELRALL 751
|
....
gi 1622834852 845 ENRL 848
Cdd:COG4913 752 EERF 755
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
425-764 |
2.81e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 48.77 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 425 MEKEMKKLRAELRKSctEQSVISRTLREKSKVE-----EKLQEDSRRKLLQLQemgnreslikINLERAVGQLEHFRSqv 499
Cdd:PRK05771 2 APVRMKKVLIVTLKS--YKDEVLEALHELGVVHiedlkEELSNERLRKLRSLL----------TKLSEALDKLRSYLP-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 500 ikatYGRAKPFPDKPVTDQQLiEKIAQVTEDNINfqqkkwTLQKETqlsnskqEETTENIEKLRTSLDSCQAcmkmscct 579
Cdd:PRK05771 68 ----KLNPLREEKKKVSVKSL-EELIKDVEEELE------KIEKEI-------KELEEEISELENEIKELEQ-------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 580 sdLKKEVDLLQHLqvSPPVSGLQ-----KVVLDILRHALswLEEVEQLLRDLGILPSSADKGFSLY-LIYLLEHYKKLMS 653
Cdd:PRK05771 122 --EIERLEPWGNF--DLDLSLLLgfkyvSVFVGTVPEDK--LEELKLESDVENVEYISTDKGYVYVvVVVLKELSDEVEE 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 654 QTQELQIKFNSSQEtqQSLLQEKLREHLAEKKQLNEERLEQEEKLKAKIRQLTEEKAALEERITQERNRAN---ETLEEE 730
Cdd:PRK05771 196 ELKKLGFERLELEE--EGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLEIELERAEalsKFLKTD 273
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1622834852 731 R----------KRMQELESLLaqQKKALAESITQENRVKEALEE 764
Cdd:PRK05771 274 KtfaiegwvpeDRVKKLKELI--DKATGGSAYVEFVEPDEEEEE 315
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
254-435 |
3.32e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 254 IANLQKEVAELSQKLSETTTS-------RQNEREISQKCQVLDE------DIDAKQKEIQSLKSQISALQKGYSQL--LC 318
Cdd:COG4913 612 LAALEAELAELEEELAEAEERlealeaeLDALQERREALQRLAEyswdeiDVASAEREIAELEAELERLDASSDDLaaLE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 319 QTLSERNSEITSLKNEGENLKRDnaiasgmVSSLQKDMLAKDEQVQELKEKVNQLksQNKDKDHQLEALGSRCsvlkEEL 398
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGE-------IGRLEKELEQAEEELDELQDRLEAA--EDLARLELRALLEERF----AAA 758
|
170 180 190
....*....|....*....|....*....|....*..
gi 1622834852 399 KQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAE 435
Cdd:COG4913 759 LGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
678-1029 |
3.44e-05 |
|
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: 48.80 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 678 REHLAEKKQLNEERlEQEEKLKAKIRQLTEEKAALEE---------RITQERNRANETLEEERKRMQELESLLAQQKKAL 748
Cdd:COG3096 292 RELFGARRQLAEEQ-YRLVEMARELEELSARESDLEQdyqaasdhlNLVQTALRQQEKIERYQEDLEELTERLEEQEEVV 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 749 AESITQENRVKEALEEEQTRVQELEKRLARQKEVLES--SIAHEKRKAKEALESEKRkvqdlenhLTQQKEVSESSIAYE 826
Cdd:COG3096 371 EEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVqqTRAIQYQQAVQALEKARA--------LCGLPDLTPENAEDY 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 827 KRKAKEAMEKEKKKVQDLENRLTkqkeelelkeqKEDVLSNKLNDALAMVE--------ETQKTKATESLKAeslALKLN 898
Cdd:COG3096 443 LAAFRAKEQQATEEVLELEQKLS-----------VADAARRQFEKAYELVCkiageverSQAWQTARELLRR---YRSQQ 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 899 ETLAELETTKTKMILMEERLILQQKTVKavQDEQESQRHG--------FEEEIMEYKEQIKQHSQTIVSLEEKLQKVSQH 970
Cdd:COG3096 509 ALAQRLQQLRAQLAELEQRLRQQQNAER--LLEEFCQRIGqqldaaeeLEELLAELEAQLEELEEQAAEAVEQRSELRQQ 586
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622834852 971 HKKIEGEIATLKDNDPA-----QKEERPQDPLVAPTTDSGAKDMAYEHLID---------DLLAAQKEILSQQ 1029
Cdd:COG3096 587 LEQLRARIKELAARAPAwlaaqDALERLREQSGEALADSQEVTAAMQQLLErereatverDELAARKQALESQ 659
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
887-1125 |
3.68e-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: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 887 SLKAESLALKLNETLAELETTKTKMILMEERLILQQKTVKAVQDEQESQrhgfEEEIMEYKEQIKQHSQTIVSLEEKLQK 966
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 967 VSQHHKKIEGEIATLKDN-----DPAQKEERPQDPLVAPTTDSGAKDMAYEHLIDDLLAAQKEIlsqqevIMKLRKDLTE 1041
Cdd:COG4942 88 LEKEIAELRAELEAQKEElaellRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQ------AEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1042 ahsrMSDLRGELNEKQKmELERNVALVQQQSKELSVLK-EKMAQMSSLTEKKDRELKALKEALRASQEKHRLQLNTEKEQ 1120
Cdd:COG4942 162 ----LAALRAELEAERA-ELEALLAELEEERAALEALKaERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
....*
gi 1622834852 1121 KSRKK 1125
Cdd:COG4942 237 AAAAE 241
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
675-1194 |
9.29e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 9.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 675 EKLREHLAEKKQLNEERLEQEEKLKAKIRQLTEEKAALEERITQERNRANETLEEERKRMQeleSLLAQQKKALAESITQ 754
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQ---AAIKAEEARKADELKK 1285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 755 ENRVKEALE----EEQTRVQELEKRlarqkevlessiAHEKRKAKEA---LESEKRKVQDLENHLTQQKEVSESSIAYEK 827
Cdd:PTZ00121 1286 AEEKKKADEakkaEEKKKADEAKKK------------AEEAKKADEAkkkAEEAKKKADAAKKKAEEAKKAAEAAKAEAE 1353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 828 RKAKEAMEKEKKKVQDlenRLTKQKEELELKEQKEDVLSNKLNDALAMVEETQKTKATESLKAESLALKLNETLAELETT 907
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAA---EKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEK 1430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 908 KTKmilmEERLILQQKTVKAVQDEQESQRHGFEEEIMEYKEQIKQHSQTIVSLEEKlQKVSQHHKKIEGEIATLKDNDPA 987
Cdd:PTZ00121 1431 KKA----DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEA-KKADEAKKKAEEAKKKADEAKKA 1505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 988 QKEERPQDPLVAPTTDSGAKDM--AYEHLIDDLLAAQKEILSQQEVimKLRKDLTEAHSRMSDLRGELNEKQKMELERNV 1065
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAkkAEEAKKADEAKKAEEKKKADEL--KKAEELKKAEEKKKAEEAKKAEEDKNMALRKA 1583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1066 ALVQQQSK----ELSVLKEKMAQMSSLTEKKDRELKALKEALR-ASQEKHRLQLNTEKEQKSRKKTQTCDTSVQIEPVHT 1140
Cdd:PTZ00121 1584 EEAKKAEEarieEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKA 1663
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1622834852 1141 EAFSSSQEEQSFSDLGVKcKGSRHEEVIQRQKKALSELRARIKELEKAHAPDHK 1194
Cdd:PTZ00121 1664 AEEAKKAEEDKKKAEEAK-KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK 1716
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
254-786 |
1.44e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.55 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 254 IANLQKEVAELSQKLSETTTSRQnerEISQKCQVLDEDIDAKQKEIQSLKSQISALQkgysqLLCQTLSERNSEITSLKN 333
Cdd:TIGR04523 147 IKKKEKELEKLNNKYNDLKKQKE---ELENELNLLEKEKLNIQKNIDKIKNKLLKLE-----LLLSNLKKKIQKNKSLES 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 334 EGENLKRDNAIASGMVSSLQKDMLAKDEQVQELKEKVNQLKSQNKDKDHQLEalgsrcsvlkEELKQEDAHRELREAQEK 413
Cdd:TIGR04523 219 QISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLS----------EKQKELEQNNKKIKELEK 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 414 ELKLCKTQIQDMEKE-----MKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESLIKINLERA 488
Cdd:TIGR04523 289 QLNQLKSEISDLNNQkeqdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEK 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 489 VGQLEhfrsQVIKATYGRAKPFPDKPVTDQQLIEKIAQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDS 568
Cdd:TIGR04523 369 QNEIE----KLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 569 cqacmkMSCCTSDLKKEVDLLQHLQVSppvsgLQKVVLDILRHALSWLEEVEQLLRDLGILPSSADKgfslyliyLLEHY 648
Cdd:TIGR04523 445 ------LTNQDSVKELIIKNLDNTRES-----LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKK--------LNEEK 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 649 KKLMSQTQELQIKFNSSQETQQSLLQEKLREHLaEKKQLNEERLEQEEKLKAKirQLTEEKAALEERITQERNrANETLE 728
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKIEKLESEKKEKES-KISDLEDELNKDDFELKKE--NLEKEIDEKNKEIEELKQ-TQKSLK 581
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622834852 729 EERKRMQELESLLAQQKKALAESITQENRVKEALEEEQTRVQELEKRLARQKEVLESS 786
Cdd:TIGR04523 582 KKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSK 639
|
|
| FHA_Slr1951-like |
cd22697 |
forkhead associated (FHA) domain found in Synechocystis sp. Slr1951 protein and similar ... |
19-92 |
1.46e-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: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 19 TIGRHEDSDLVLQSPDIDNHHALIEY----NEAECSFVLQDF----NSRNGTFVNECHIQNVAvkLIPGDILRFG-SAGL 89
Cdd:cd22697 21 TIGRHPGNDIQIPSQQISRRHATLRRkinpNLDISFWIIDGDlegaESLNGLWVNGERILQHE--LVNGDEIALGpKIVL 98
|
...
gi 1622834852 90 TYE 92
Cdd:cd22697 99 RYQ 101
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
667-1110 |
1.55e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 667 ETQQSLLQEKLREHLAEKKQLN-EERLEQEEKLKAKIRQLTEEKAALEERITQERNRANETLEEERKRMQELESL---LA 742
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKDlHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLeaeIE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 743 QQKKALAESITQENRVKEALEEEQTRVQELEKRL--ARQKEVLESSIAHEKRKAKEALESEKRKVQD-LENHLTQQKEVS 819
Cdd:PRK02224 262 DLRETIAETEREREELAEEVRDLRERLEELEEERddLLAEAGLDDADAEAVEARREELEDRDEELRDrLEECRVAAQAHN 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 820 ESSIAYEKRKAKEAM--EKEKKKVQDLENRLTKQKEELELKEQKEDVLSNKLNDALAMVEETQKTKATESLKAESLALKL 897
Cdd:PRK02224 342 EEAESLREDADDLEEraEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREER 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 898 NETLAELETTKTKMILMEERLILQQKTV---KAVQDEQESQRHGFEEEIMEYKEQIKQHSQTIVSLEEKLQKVSQHH--- 971
Cdd:PRK02224 422 DELREREAELEATLRTARERVEEAEALLeagKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLera 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 972 ---KKIEGEIATLKDNDP------AQKEER-PQDPLVAPTTDSGAKDMAYEHLIDDLLAAQKEILSQ--QEVIMKLRKDL 1039
Cdd:PRK02224 502 edlVEAEDRIERLEERREdleeliAERRETiEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEeaREEVAELNSKL 581
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622834852 1040 TEAHSRMSDLRgelnekqkmELERNVALVQQQSKELSVLKEKMAQMSSLTEKKDRELKALKEALRASQEKH 1110
Cdd:PRK02224 582 AELKERIESLE---------RIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEF 643
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
661-804 |
1.60e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 661 KFNSSQETQQSLLQEKLREHLAEKK----QLNEERLEQEEKLKAKIRQLTEEKAALEERITQER---NRANETLEEERKR 733
Cdd:PRK12704 32 KIKEAEEEAKRILEEAKKEAEAIKKeallEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEenlDRKLELLEKREEE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 734 MQELESLLAQQKKALAEsitQENRVKEALEEEQTRVQE---LEKRLARQK--EVLESSIAHE-----KRKAKEALESEKR 803
Cdd:PRK12704 112 LEKKEKELEQKQQELEK---KEEELEELIEEQLQELERisgLTAEEAKEIllEKVEEEARHEaavliKEIEEEAKEEADK 188
|
.
gi 1622834852 804 K 804
Cdd:PRK12704 189 K 189
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
11-93 |
2.31e-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: 41.84 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 11 FFVLNKSTTIGR---------HEDSDLVLQSPD-IDNHHALIEYNEAECSFVLQDFnSRNGTFVNE--CHIQNVAVKLIP 78
Cdd:cd22701 12 YYVQKLEVVLGRnsknssstaADSVDIDLGPSKkISRRHARIFYDFTTQCFELSVL-GRNGVKVDGilVKPGSPPVPLRS 90
|
90
....*....|....*
gi 1622834852 79 GDILRFGSAGLTYEL 93
Cdd:cd22701 91 GSLIQIGGVLFYFLL 105
|
|
| FHA_Rv1747-like_rpt2 |
cd22737 |
second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
20-92 |
2.67e-04 |
|
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: 41.33 E-value: 2.67e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622834852 20 IGRHEDSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQnvAVKLIPGDILRFGSAGLTYE 92
Cdd:cd22737 25 IGRASDNDIVIPEGSVSRHHATLVPTPG--GTQIRDLRSTNGTFVNGLRVD--AALLHDGDVVTIGDIDFVFE 93
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
658-817 |
2.92e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 658 LQIKFNSSQETQQSLLQE--KLREHLAEKkqlnEERLeQEEKLKAKIRQLTEEKAALEERIT---QERNRANETLEEERK 732
Cdd:COG3206 166 LELRREEARKALEFLEEQlpELRKELEEA----EAAL-EEFRQKNGLVDLSEEAKLLLQQLSeleSQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 733 RMQELESLLAQQKKALAESI---------TQENRVKEALEEEQTR-------VQELEKRLARQKEVLESSIAHEKRKAKE 796
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLqspviqqlrAQLAELEAELAELSARytpnhpdVIALRAQIAALRAQLQQEAQRILASLEA 320
|
170 180
....*....|....*....|.
gi 1622834852 797 ALESEKRKVQDLENHLTQQKE 817
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEA 341
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
244-747 |
3.07e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.34 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 244 EIESKYKDVIIANLQKEVAELSQKLSETTTSRQNEREISQKCQVLdEDIDAKQKEIQSLKSQISALQKGYSQLLCQTLSE 323
Cdd:TIGR00618 434 ELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTK-EQIHLQETRKKAVVLARLLELQEEPCPLCGSCIH 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 324 RNSEITSLKNEGENLKRDNAIASGmVSSLQKDMLAKDEQVQELKEKVNQLKSQNKDKDHQLEALGSRCSVLKEELkqeda 403
Cdd:TIGR00618 513 PNPARQDIDNPGPLTRRMQRGEQT-YAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDI----- 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 404 hrelrEAQEKELKLCKTQIQDMEKEMKKLRAELRkscteqsvisrtlREKSKVEEKLqeDSRRKLLQLQEMGNRESLIKI 483
Cdd:TIGR00618 587 -----PNLQNITVRLQDLTEKLSEAEDMLACEQH-------------ALLRKLQPEQ--DLQDVRLHLQQCSQELALKLT 646
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 484 NLERavgQLEHFRSQVIKATYGRAKPFPDKPVTDQQLIEKIAQvtedniNFQQKKWTLQKETQLSNSKQEETTENIEKLR 563
Cdd:TIGR00618 647 ALHA---LQLTLTQERVREHALSIRVLPKELLASRQLALQKMQ------SEKEQLTYWKEMLAQCQTLLRELETHIEEYD 717
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 564 TSLDscQACMKMSCCTSDLKKEVDLLQHLQVSPPVSGLQKVVLDILRHALSWLEEVEQLLRDlgilpssadkgfslyliy 643
Cdd:TIGR00618 718 REFN--EIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTG------------------ 777
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 644 llehyKKLMSQTQELQIKFNSSQETQQSL--LQEKLREHLAEKKQLNEERLEQEEKLKAKIRQLTEEKAALEERITQERN 721
Cdd:TIGR00618 778 -----AELSHLAAEIQFFNRLREEDTHLLktLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLL 852
|
490 500
....*....|....*....|....*.
gi 1622834852 722 RANETLEEERKRMQELESLLAQQKKA 747
Cdd:TIGR00618 853 KYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
297-483 |
3.14e-04 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 43.96 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 297 KEIQSLKSQISALQKGYSQL------LCQTLSERNSEITSLKNEGENLKRDNAIASGMVSSLQKDMLAKDEQVQELKEKV 370
Cdd:pfam17078 3 KVIESLHDQIDALTKTNLQLtvqsqnLLSKLEIAQQKESKFLENLASLKHENDNLSSMLNRKERRLKDLEDQLSELKNSY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 371 NQLKSQNKDKDHQLEALGSRCSVLKEELKQE--------DAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELrkscte 442
Cdd:pfam17078 83 EELTESNKQLKKRLENSSASETTLEAELERLqiqydalvDSQNEYKDHYQQEINTLQESLEDLKLENEKQLENY------ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622834852 443 qsvISRTLREKSKVEEKLQE--DSRRKLLQLQEMGNRESLIKI 483
Cdd:pfam17078 157 ---QQRISSNDKDIDTKLDSynNKFKNLDNIYVNKNNKLLTKL 196
|
|
| FHA_Par42-like |
cd22675 |
forkhead associated (FHA) domain found in Trypanosoma brucei Parvulin 42 (TbPar42) and similar ... |
20-100 |
4.66e-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: 41.39 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 20 IGRHEDSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQnvAVKLIP---GDILRFGSAGLTYElVVE 96
Cdd:cd22675 33 FGRSPVCDYVLEHPSISSVHAVLVFHGEQKCFVLMDLGSTNGVKLNGKRIE--KGRPLPlpvGSVIQFGFSARKYK-VRK 109
|
....
gi 1622834852 97 NPPP 100
Cdd:cd22675 110 GPPS 113
|
|
| FHA_EmbR-like |
cd22669 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis transcriptional ... |
5-92 |
4.90e-04 |
|
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: 40.48 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 5 LKSAEGFFVLNKSTTIGRHEDSDLVLQSPDIDNHHALIEYNEAECSfvLQDFNSRNGTFVNECHIQNVAVkLIPGDILRF 84
Cdd:cd22669 5 IASGRGYPLQAAATRIGRLHDNDIVLDSANVSRHHAVIVDTGTNYV--INDLRSSNGVHVQHERIRSAVT-LNDGDHIRI 81
|
....*...
gi 1622834852 85 GSAGLTYE 92
Cdd:cd22669 82 CDHEFTFQ 89
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
254-439 |
5.03e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 254 IANLQKEVAELSQKLSETTtsrqnereisQKCQVLDEDIDAKQKEIQSLKSQISALQKGYSQLLcQTLSERNSeitSLKN 333
Cdd:COG3883 32 LEAAQAELDALQAELEELN----------EEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR-EELGERAR---ALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 334 EGENLKR--------------DNAIASGMVSSLQKDMLakdEQVQELKEKVNQLKSQNKDKDHQLEALGSRCSVLKEELK 399
Cdd:COG3883 98 SGGSVSYldvllgsesfsdflDRLSALSKIADADADLL---EELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622834852 400 QedahreLREAQEKELKLCKTQIQDMEKEMKKLRAELRKS 439
Cdd:COG3883 175 A------QQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
|
|
| FHA_GarA-like |
cd22720 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis glycogen accumulation ... |
12-91 |
5.05e-04 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis glycogen accumulation regulator GarA and similar proteins; GarA is an FHA domain-containing protein involved in the regulation of glutamate metabolism. It acts as a phosphorylation-dependent ON/OFF molecular switch that modulates the activities of KGD, GDH and GltB. Its FHA domain has dual specificity. It binds to both phosphorylated upstream partners, such as the kinases PknB and PknG, and nonphosphorylated downstream partners, such as the 2-oxoglutarate decarboxylase KGD. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438772 [Multi-domain] Cd Length: 100 Bit Score: 40.76 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 12 FVLNKSTT-IGRHEDSDLVLQSPDIDNHHAliEYNEAECSFVLQDFNSRNGTFVNECHIqNVAVkLIPGDILRFGSAGLT 90
Cdd:cd22720 19 FLLDQAITsAGRHPDSDIFLDDVTVSRRHA--EFRLENNEFNVVDVGSLNGTYVNREPV-DSAV-LANGDEVQIGKFRLV 94
|
.
gi 1622834852 91 Y 91
Cdd:cd22720 95 F 95
|
|
| FHA_DgcB-like |
cd22682 |
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ... |
11-86 |
5.17e-04 |
|
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB and similar proteins; DgcB is a GGDEF enzyme that produces cyclic-di-GMP in response to an unknown stimulus. It appends the C-terminal GGDEF enzymatic domain with an N-terminal forkhead-associated (FHA) domain that acts as a consensus phosphopeptide sensor. The GGDEF and sensory FHA domains form an asymmetrical dimer.
Pssm-ID: 438734 [Multi-domain] Cd Length: 96 Bit Score: 40.59 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 11 FFVLNKSTTIGRHEDSDLVLQSPDIDNHHALIEYNEAECSfvLQDFNSRNGTFVN--------ECHIQNvavklipGDIL 82
Cdd:cd22682 15 FPITESTIVIGRSVESQVQIDDDSVSRYHAKLAVNPSAVS--IIDLGSTNGTIVNgkkipklaSCDLQN-------GDQI 85
|
....
gi 1622834852 83 RFGS 86
Cdd:cd22682 86 KIGN 89
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
673-778 |
5.54e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.69 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 673 LQEKLREHLAEKKQLNEER----LEQEEKLKAKIRQLTEEKAALEERITQERNRANE-------------TLEEERKRMQ 735
Cdd:COG0542 416 LERRLEQLEIEKEALKKEQdeasFERLAELRDELAELEEELEALKARWEAEKELIEEiqelkeeleqrygKIPELEKELA 495
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1622834852 736 ELESLLAQQKKALAESITQEN------R-----VKEALEEEQTRVQELEKRLAR 778
Cdd:COG0542 496 ELEEELAELAPLLREEVTEEDiaevvsRwtgipVGKLLEGEREKLLNLEEELHE 549
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
656-971 |
5.87e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.51 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 656 QELQIKFNSSQETQQSLLQ-EKLREHL--AEKK--QLNEERLEQEEKLKakirQLTEEKAALEERITQERNRANETLE-- 728
Cdd:PLN02939 111 IDNEQQTNSKDGEQLSDFQlEDLVGMIqnAEKNilLLNQARLQALEDLE----KILTEKEALQGKINILEMRLSETDAri 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 729 ----EERKRMQELESLLAQQKKALAESITQENRVKEALEEEQTRVQELEKRLARQKEVLESSIAHEKRKAKEALESEKRK 804
Cdd:PLN02939 187 klaaQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFKLEKER 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 805 ------VQDLENHL-TQQKEVSE-SSIAYEkrkakeameKEKKKVQDLENRLtkqkeelelkeqkeDVLSNKLNDALAMV 876
Cdd:PLN02939 267 slldasLRELESKFiVAQEDVSKlSPLQYD---------CWWEKVENLQDLL--------------DRATNQVEKAALVL 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 877 EETQKTKAteslKAEslalKLNETLAELETTKTKMILMEerlILQQKtVKAVQDEQESQRHGFEEEIMEYKEQIKQHSQT 956
Cdd:PLN02939 324 DQNQDLRD----KVD----KLEASLKEANVSKFSSYKVE---LLQQK-LKLLEERLQASDHEIHSYIQLYQESIKEFQDT 391
|
330
....*....|....*
gi 1622834852 957 IVSLEEKLQKVSQHH 971
Cdd:PLN02939 392 LSKLKEESKKRSLEH 406
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
350-1133 |
7.51e-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: 44.19 E-value: 7.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 350 SSLQKDMLAKDEQVQELKEKVNQLKSQNKDKDHQLEALGSRCSVLKEELKQE-DAHRELREAQEKELKLCKTQIQDMEKE 428
Cdd:TIGR00618 162 SKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMpDTYHERKQVLEKELKHLREALQQTQQS 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 429 MKKLRAE---------LRKSCTEQSVISRTLREKSKVEEKLQE--DSRRKLLQLQEMGNRESLIKINLERAVGQLEHFRS 497
Cdd:TIGR00618 242 HAYLTQKreaqeeqlkKQQLLKQLRARIEELRAQEAVLEETQEriNRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMR 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 498 QVIKATYGRAKPFPDK-PVTDQQLIEKIAQVTEDNINFQQKKWTLQKETQlsnSKQEETTENIEKLRTSLDSCQACMKMS 576
Cdd:TIGR00618 322 SRAKLLMKRAAHVKQQsSIEEQRRLLQTLHSQEIHIRDAHEVATSIREIS---CQQHTLTQHIHTLQQQKTTLTQKLQSL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 577 CCTSD------------LKKEVDLLQHLQVSPPVSGLQKVVLDILRHALSwLEEVEQLLRDLGILPSSADKGFSLYLIYL 644
Cdd:TIGR00618 399 CKELDilqreqatidtrTSAFRDLQGQLAHAKKQQELQQRYAELCAAAIT-CTAQCEKLEKIHLQESAQSLKEREQQLQT 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 645 LEHYKKLMSQTQELQIKFNSSQETQQSLLQEKLREHLAEKKQLNEERLEQE--EKLKAKIRQLTEEKAALEERITQERNR 722
Cdd:TIGR00618 478 KEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRrmQRGEQTYAQLETSEEDVYHQLTSERKQ 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 723 ANEtLEEERKRMQELESLLAQQKKALAESITQENRVKEALEEEQTRVQELEKRLA----RQKEVLESSIA------HEKR 792
Cdd:TIGR00618 558 RAS-LKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLAceqhALLRKLQPEQDlqdvrlHLQQ 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 793 KAKEALESEKRKVQDLENHLTQQKEVSESSIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLSNKLNDA 872
Cdd:TIGR00618 637 CSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEY 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 873 LAMVEETQKTKATESLKAESLALKLNETLAELETTKtKMILMEERLILQQKTVKAVQDEQESQRhgFEEEIMEYKEQIKQ 952
Cdd:TIGR00618 717 DREFNEIENASSSLGSDLAAREDALNQSLKELMHQA-RTVLKARTEAHFNNNEEVTAALQTGAE--LSHLAAEIQFFNRL 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 953 HSQTIVSLEEKLQKVSQHHKKIEGeIATLKDNDPAQKEERPQDPLVAPTTDSGAKDMAYEHLiddllaaqkeilsqqevi 1032
Cdd:TIGR00618 794 REEDTHLLKTLEAEIGQEIPSDED-ILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKY------------------ 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1033 mklrkdlteahsrmsdlrgELNEKQKMELERNVALVQQQSKELSVLKEKMAQM-SSLTEKKDRELKALKEALRASQEKHR 1111
Cdd:TIGR00618 855 -------------------EECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFdGDALIKFLHEITLYANVRLANQSEGR 915
|
810 820
....*....|....*....|..
gi 1622834852 1112 LQLNTEKEQKSRKKTQTCDTSV 1133
Cdd:TIGR00618 916 FHGRYADSHVNARKYQGLALLV 937
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
254-544 |
8.16e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 44.07 E-value: 8.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 254 IANLQKEVAELSQKLSET--TTSRQNEREISQKCQVLDEDIDAKQKEI---QSLKSQISALQKGYS------QLLCQTLS 322
Cdd:PLN03229 431 VRELEGEVEKLKEQILKAkeSSSKPSELALNEMIEKLKKEIDLEYTEAviaMGLQERLENLREEFSkansqdQLMHPVLM 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 323 ERnseITSLKNE-GENLKRDNAIASGMVSSLQKDMLAKDEQVQELKEKVNQLKsqnKDKDHQLEALGSRCSVLK--EELK 399
Cdd:PLN03229 511 EK---IEKLKDEfNKRLSRAPNYLSLKYKLDMLNEFSRAKALSEKKSKAEKLK---AEINKKFKEVMDRPEIKEkmEALK 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 400 QEDAHRELREAQEKELKLcKTQIQDMEKEMKKLRAELRKSCTEQsVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRES 479
Cdd:PLN03229 585 AEVASSGASSGDELDDDL-KEKVEKMKKEIELELAGVLKSMGLE-VIGVTKKNKDTAEQTPPPNLQEKIESLNEEINKKI 662
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622834852 480 LIKINLERAVGQLEHFRSQVIKATYGRAKPFPDKPVT-DQQLIEKIAQVTeDNINFQQKKWTLQKE 544
Cdd:PLN03229 663 ERVIRSSDLKSKIELLKLEVAKASKTPDVTEKEKIEAlEQQIKQKIAEAL-NSSELKEKFEELEAE 727
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
244-823 |
8.50e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 44.27 E-value: 8.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 244 EIESKYKDVIiANLQKEVAELsQKLSETTTSRQNEREISQKCQVLDEDIDAKQ---KEIQSLKSQISALQKGYSQLlcqt 320
Cdd:TIGR01612 1136 EIKKKSENYI-DEIKAQINDL-EDVADKAISNDDPEEIEKKIENIVTKIDKKKniyDEIKKLLNEIAEIEKDKTSL---- 1209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 321 LSERNSEITSLKNEG----ENLKRDNAIASGMVSSLQKDMLAKDEqVQELKEKVNQLKSQNKDKDHQLEALGSRCSVLKE 396
Cdd:TIGR01612 1210 EEVKGINLSYGKNLGklflEKIDEEKKKSEHMIKAMEAYIEDLDE-IKEKSPEIENEMGIEMDIKAEMETFNISHDDDKD 1288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 397 ELKQEDAHRE-LREAQEKELKLC-----KTQIQDMEKEMKKLRAELRKSCTEQSvisrtlrekskveeklqedsrrklLQ 470
Cdd:TIGR01612 1289 HHIISKKHDEnISDIREKSLKIIedfseESDINDIKKELQKNLLDAQKHNSDIN------------------------LY 1344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 471 LQEMGNRESLIKIN-LERAVGQLEHFRSQVIKATygraKPFPDKPVTDQQLIEKIaqvtEDNINFQQKKWTLqkETQLSN 549
Cdd:TIGR01612 1345 LNEIANIYNILKLNkIKKIIDEVKEYTKEIEENN----KNIKDELDKSEKLIKKI----KDDINLEECKSKI--ESTLDD 1414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 550 SKQEETTENIEKLRTSLDSCQACMKMSCCTSDLKKEVDLLQHLQVSPPVSGLQKVVLDILRHALS----WLEEVEQLLRD 625
Cdd:TIGR01612 1415 KDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATNdhdfNINELKEHIDK 1494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 626 LGILPSSADKGFSLYL--IYLLEHYKK----LMSQTQELQIKFNSSQETQQSllqeklREHLAEKKQLNEERLEQEEKLK 699
Cdd:TIGR01612 1495 SKGCKDEADKNAKAIEknKELFEQYKKdvteLLNKYSALAIKNKFAKTKKDS------EIIIKEIKDAHKKFILEAEKSE 1568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 700 AKIRQLTEEKAALEERITQErNRANE-------TLEEERKRMQELESLLAQQKKALAESITQENRVKE-ALEEEQTRVQE 771
Cdd:TIGR01612 1569 QKIKEIKKEKFRIEDDAAKN-DKSNKaaidiqlSLENFENKFLKISDIKKKINDCLKETESIEKKISSfSIDSQDTELKE 1647
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1622834852 772 LEKRLARQKEVLESSIAHEK--RKAKEALESEKRKVQDLENHLTQQKEVSESSI 823
Cdd:TIGR01612 1648 NGDNLNSLQEFLESLKDQKKniEDKKKELDELDSEIEKIEIDVDQHKKNYEIGI 1701
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
233-827 |
8.64e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 8.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 233 LGKEVSRLSDYEIESKYKDVIIANLQKEVAELSQKLSETTTSRQNEREISQKCQVLDEDIDAKQKEIQSLKSQISALQkg 312
Cdd:PRK03918 181 LEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLE-- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 313 ysqllcQTLSERNSEITSLKNEGENLKRdnaiasgmvsslQKDMLAKDEQVQELKEKVNQLKSQNKDKDHQLEALGSRCS 392
Cdd:PRK03918 259 ------EKIRELEERIEELKKEIEELEE------------KVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 393 VLKEELKQEDAHRELREAQEKELklcKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQ 472
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEEL---KKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 473 EMGNRESLIKINLERAVGQLEHFRSQVIKATYGRAKPFPDKPVTDQQLiekiaqvTEDNINFQQKKWTLqkETQLSNSKQ 552
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGREL-------TEEHRKELLEEYTA--ELKRIEKEL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 553 EETTENIEKLRTSLDSCQACMKMSCCTSDLKKEVDLLQHLQvsppvSGLQKVVLDILRHALSWLEEVEQLLRDLgilpss 632
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELE-----EKLKKYNLEELEKKAEEYEKLKEKLIKL------ 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 633 adKGFSLYLIYLLEHYKKLMSQTQELQIKFNSSQETQQSLLQEKLREHLAEKKQLnEERLEQEEKLKAKIRQLTEEKAAL 712
Cdd:PRK03918 538 --KGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEEL-EERLKELEPFYNEYLELKDAEKEL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 713 EERItQERNRANETLEEERKRMQELESLLAQQKKALAEsiTQENRVKEALEEEQTRVQELEKRLARQKEVLESsiahekr 792
Cdd:PRK03918 615 EREE-KELKKLEEELDKAFEELAETEKRLEELRKELEE--LEKKYSEEEYEELREEYLELSRELAGLRAELEE------- 684
|
570 580 590
....*....|....*....|....*....|....*
gi 1622834852 793 kAKEALESEKRKVQDLENHLTQQKEVSESSIAYEK 827
Cdd:PRK03918 685 -LEKRREEIKKTLEKLKEELEEREKAKKELEKLEK 718
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
394-975 |
9.48e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 9.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 394 LKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKscteqsvISRTLREKSKVEEKLQEDSRRKLLQLQE 473
Cdd:PRK03918 181 LEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEK-------LEKEVKELEELKEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 474 MGNRESLIK---INLERAVGQLEHFRSQV--------IKATYGRAKPFPDKPVTDQQLIEKIAQVTEDNINFQQKKWtlq 542
Cdd:PRK03918 254 KRKLEEKIReleERIEELKKEIEELEEKVkelkelkeKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI--- 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 543 KETQLSNSKQEETTENIEKLRTSLdscqacmkmscctSDLKKEVDLLQHLQVsppvsglQKVVLDILRHALSwLEEVEQL 622
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRL-------------EELEERHELYEEAKA-------KKEELERLKKRLT-GLTPEKL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 623 LRDLGILPSSADKgfslyliyLLEHYKKLMSQTQELQIKFNSSQETQQSLLQEKLREHLAEKKQLNEERLEQEEKLKAKI 702
Cdd:PRK03918 390 EKELEELEKAKEE--------IEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAEL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 703 RQLTEEKAALEERITQERNRANEtLEEERKRMQELESL--LAQQKKALAESITQENrvKEALEEEQTRVQELEKRLARQK 780
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRE-LEKVLKKESELIKLkeLAEQLKELEEKLKKYN--LEELEKKAEEYEKLKEKLIKLK 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 781 ---EVLESSIAHEK--RKAKEALESEKRKVQD-LENHLTQQKEVSESSiayekrkakeamekekkkVQDLENRLTKQKEE 854
Cdd:PRK03918 539 geiKSLKKELEKLEelKKKLAELEKKLDELEEeLAELLKELEELGFES------------------VEELEERLKELEPF 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 855 LELKeqkedvlsNKLNDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKmiLMEERLILQQKTVKAVQDEQES 934
Cdd:PRK03918 601 YNEY--------LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKE--LEELEKKYSEEEYEELREEYLE 670
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1622834852 935 QRH---GFEEEIMEYKEQIKQHSQTIVSLEEKLQKVSQHHKKIE 975
Cdd:PRK03918 671 LSRelaGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE 714
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
359-1127 |
1.00e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.81 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 359 KDEQVQELKEKVnqlKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRaelrk 438
Cdd:pfam02463 168 KRKKKEALKKLI---EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERI----- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 439 scteqsvisRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESLIKINLERAVGQLEhfrsqvikatygrakpfpdkpVTDQ 518
Cdd:pfam02463 240 ---------DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQE---------------------EELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 519 QLIEKIAQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKmsccTSDLKKEVDLLQHLQVSppv 598
Cdd:pfam02463 290 LLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELK----ELEIKREAEEEEEEELE--- 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 599 sglqkvvlDILRHALSWLEEVEQLLRDLGILPSSADKGFslyliyllehykklmSQTQELQIKFNSSQETQQSLLQEKLR 678
Cdd:pfam02463 363 --------KLQEKLEQLEEELLAKKKLESERLSSAAKLK---------------EEELELKSEEEKEAQLLLELARQLED 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 679 EHLAEKKQLNEERLEQEEKLKAKIRQLTEEKAALEERiTQERNRANETLEEERKRMQELESLLAQQKKALAESITQENRV 758
Cdd:pfam02463 420 LLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQ-ELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEER 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 759 KEALEEEQTRVQELEKRLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEVSESSIAYEKRKAKEAMEKEK 838
Cdd:pfam02463 499 SQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGAR 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 839 KKVQDLENRLTKQKEELELKEQKEDVLSNKLNDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMI-LMEER 917
Cdd:pfam02463 579 KLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVsLEEGL 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 918 LILQQKTVKAVQDEQESQRHGFEEEIMEYKEQIKQHSQTIVSLEEKLQKVSQHHKKIEGEIATLKDNDPAQKEERPQDPL 997
Cdd:pfam02463 659 AEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEEL 738
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 998 VAPTTDSGAKDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRM------SDLRGELNEKQKMELERNVALVQQQ 1071
Cdd:pfam02463 739 KLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKveeekeEKLKAQEEELRALEEELKEEAELLE 818
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622834852 1072 SKELSVLKEKMAQMSSLTEKKDRELKALKEALRASQEKHRLQLNTEKEQKSRKKTQ 1127
Cdd:pfam02463 819 EEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLL 874
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
710-801 |
1.09e-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: 40.93 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 710 AALEERitqeRNRANETLEEERKRMQELESLLAQQKKALAESITQENRV-----KEALEEEQTRVQELEKRLARQKEVLE 784
Cdd:COG0711 27 KALDER----QEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIiaearKEAEAIAEEAKAEAEAEAERIIAQAE 102
|
90
....*....|....*..
gi 1622834852 785 SSIAHEKRKAKEALESE 801
Cdd:COG0711 103 AEIEQERAKALAELRAE 119
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
684-992 |
1.13e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.35 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 684 KKQLNEERLEQEEKLKAKIRQLTEEKAALEERITQERNRANETLEEERK----RMQELESLLAQQK-------------K 746
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRelesRVAELKEELRQSRekheeleekykelS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 747 ALAESITQENRV-KEALEEEQTRVQELE---KRLARQKEVLESSIAHEKRKAKEAL------ESEKRKVQdLENHLTQQK 816
Cdd:pfam07888 108 ASSEELSEEKDAlLAQRAAHEARIRELEediKTLTQRVLERETELERMKERAKKAGaqrkeeEAERKQLQ-AKLQQTEEE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 817 EVSESSIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLSNKLNDALAMVEETQKTKATESLKAESLALK 896
Cdd:pfam07888 187 LRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQ 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 897 LNETLAEL-----ETTKTKMILMEERLILQQKTVKAVQDEQESQRHGFEEeimeyKEQIKQHSQTIVSLEEKLQKVSQHH 971
Cdd:pfam07888 267 RDRTQAELhqarlQAAQLTLQLADASLALREGRARWAQERETLQQSAEAD-----KDRIEKLSAELQRLEERLQEERMER 341
|
330 340
....*....|....*....|.
gi 1622834852 972 KKIEGEIATLKDNDPAQKEER 992
Cdd:pfam07888 342 EKLEVELGREKDCNRVQLSES 362
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
926-1111 |
1.24e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 43.48 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 926 KAVQDEQESQRHGfEEEIMEYKEQIKQHSQTIVSLEEKLQKVSQHHKKIEGEIATLKdndpAQKEERPQDPLVapttdsg 1005
Cdd:pfam05667 321 TKVETEEELQQQR-EEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELK----EQNEELEKQYKV------- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1006 aKDMAYEHLIDDllaaqkeilsqQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELERNVALVQQQSK----------EL 1075
Cdd:pfam05667 389 -KKKTLDLLPDA-----------EENIAKLQALVDASAQRLVELAGQWEKHRVPLIEEYRALKEAKSNkedesqrkleEI 456
|
170 180 190
....*....|....*....|....*....|....*..
gi 1622834852 1076 SVLKEKMAQMSSLTEKKDRELKALKEAL-RASQEKHR 1111
Cdd:pfam05667 457 KELREKIKEVAEEAKQKEELYKQLVAEYeRLPKDVSR 493
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
518-754 |
1.29e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 518 QQLIEKIAQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKmscctsDLKKEVDLLQhlqvspp 597
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA------ELEKEIAELR------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 598 vsGLQKVVLDILRHALSWLEEVEQLLRDLGILPSSADKGFSLYLIYLLEHYKKLMSQTQELQIKFNSSQETQQSLLQEKl 677
Cdd:COG4942 97 --AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER- 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622834852 678 rehlAEKKQLNEERLEQEEKLKAKIRQLTEEKAALEERITQERNRANETLEEERKRMQELESLLAQQKKALAESITQ 754
Cdd:COG4942 174 ----AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
700-927 |
1.29e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 700 AKIRQLTEEKAALEERITQERNRANETLEEERKRMQELESL---LAQQKKALAESITQENRVKEALEEEQTRVQELEKRL 776
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALerrIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 777 ARQKEVLessiahekrkAKEALESEKRKVQDLENHLTQQKEVSES--SIAYEKRKAKEAMEKEKKKVQDLEnRLTKQKEE 854
Cdd:COG4942 100 EAQKEEL----------AELLRALYRLGRQPPLALLLSPEDFLDAvrRLQYLKYLAPARREQAEELRADLA-ELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622834852 855 LELKEQKEDVLSNKLNDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMILMEERLILQQKTVKA 927
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
643-774 |
1.35e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 643 YLLEHYKKLMSQTQElqiKFN---SSQETQQSLLQEKLREH---LAEKKQLNEERLEQEEKLKAKIRQLteeKAALEERI 716
Cdd:PRK00409 502 NIIEEAKKLIGEDKE---KLNeliASLEELERELEQKAEEAealLKEAEKLKEELEEKKEKLQEEEDKL---LEEAEKEA 575
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 717 TQERNRANETLEEERKRMQELEsllAQQKKALAESITQENR--VKEALEEEQTRVQELEK 774
Cdd:PRK00409 576 QQAIKEAKKEADEIIKELRQLQ---KGGYASVKAHELIEARkrLNKANEKKEKKKKKQKE 632
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
257-464 |
1.37e-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: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 257 LQKEVAELSQKLSETTTSRQNEREISQKCQVLDEDIDAKQKEIQSLKSQISALQKgysqllcqTLSERNSEITSLKNEGE 336
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA--------EIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 337 NLKRDNAIASGMVSSLqkDMLAKDEQVQELKEK---VNQLKSQNKDKDHQLEALGSRCSVLKEEL-KQEDAHRELREAQE 412
Cdd:COG3883 90 ERARALYRSGGSVSYL--DVLLGSESFSDFLDRlsaLSKIADADADLLEELKADKAELEAKKAELeAKLAELEALKAELE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622834852 413 KELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDS 464
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
677-810 |
1.51e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 677 LREHLAEKKQLN----------EERLEQEEKLKAKIRQLTEEkaaleerITQERNRANETLEEERKRMQELESLLAQQKK 746
Cdd:PRK12704 24 VRKKIAEAKIKEaeeeakrileEAKKEAEAIKKEALLEAKEE-------IHKLRNEFEKELRERRNELQKLEKRLLQKEE 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622834852 747 ALaesitqeNRVKEALEEEQTRVQELEKRLARQKEVLESsiahekrKAKEALESEKRKVQDLEN 810
Cdd:PRK12704 97 NL-------DRKLELLEKREEELEKKEKELEQKQQELEK-------KEEELEELIEEQLQELER 146
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
678-796 |
1.53e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.92 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 678 REHLAEKKQLNEERLEQEEKLKAKIRQLTEEKAALEERITQERNRANETLEEERKRMQELESLlaqqkKALAESItqeNR 757
Cdd:COG2433 405 ERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREI-----SRLDREI---ER 476
|
90 100 110
....*....|....*....|....*....|....*....
gi 1622834852 758 VKEALEEEQTRVQELEKRLARQKEVLESSIAHEKRKAKE 796
Cdd:COG2433 477 LERELEEERERIEELKRKLERLKELWKLEHSGELVPVKV 515
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
359-438 |
1.54e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.92 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 359 KDEQVQELKEKVNQLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRK 438
Cdd:COG2433 411 EEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREIERLERELEEERERIEE 490
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
656-785 |
1.86e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 656 QELQIKFNSSQETQQSLLQEKLREHLAekkQLNEERLEQEEKLKAK---IRQLTEEKAALEERITQERNRANETLEEE-- 730
Cdd:COG3206 247 AQLGSGPDALPELLQSPVIQQLRAQLA---ELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQEAQRILASLEAEle 323
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622834852 731 --RKRMQELESLLAQQKKALAEsitqenrvkeaLEEEQTRVQELEKRLARQKEVLES 785
Cdd:COG3206 324 alQAREASLQAQLAQLEARLAE-----------LPELEAELRRLEREVEVARELYES 369
|
|
| ATG14 |
pfam10186 |
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ... |
654-797 |
1.92e-03 |
|
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localization of this complex at the PAS is controlled by Atg14. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex.
Pssm-ID: 462986 [Multi-domain] Cd Length: 347 Bit Score: 42.44 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 654 QTQELQIKFNSSQETQQSLLQEKLrehlaEKKQLNEERLEQEEKLKAKIRQLTEEKAALEERITQERNRA---NETLEEE 730
Cdd:pfam10186 23 ELRVDLARLLSEKDSLKKKVEEAL-----EGKEEGEQLEDNIGNKKLKLRLLKSEVAISNERLNEIKDKLdqlRREIAEK 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622834852 731 RKRMQELESLLAqQKKALAESITqeNRVKEALEEEQTRVQELEKRLARQKEVLESSIAHEKR-KAKEA 797
Cdd:pfam10186 98 KKKIEKLRSSLK-QRRSDLESAS--YQLEERRASQLAKLQNSIKRIKQKWTALHSKTAESRSfLCREL 162
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
646-796 |
2.12e-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: 42.63 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 646 EHYKKLMSQTQELQIKFNSSQETQQSLLQEKLRehlAEKKQLNEERLEQEEKLKAKIRQLT-----------EEKAALEE 714
Cdd:pfam15709 358 EEQRRLQQEQLERAEKMREELELEQQRRFEEIR---LRKQRLEEERQRQEEEERKQRLQLQaaqerarqqqeEFRRKLQE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 715 RITQERNRANETLEEERKRMQELESLLAQQKKALAEsITQENRV---KEALEEEQTRVQELEKRLARQKEVLESSIAHEK 791
Cdd:pfam15709 435 LQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLME-MAEEERLeyqRQKQEAEEKARLEAEERRQKEEEAARLALEEAM 513
|
....*
gi 1622834852 792 RKAKE 796
Cdd:pfam15709 514 KQAQE 518
|
|
| PRK13709 |
PRK13709 |
conjugal transfer nickase/helicase TraI; Provisional |
675-781 |
2.35e-03 |
|
conjugal transfer nickase/helicase TraI; Provisional
Pssm-ID: 237478 [Multi-domain] Cd Length: 1747 Bit Score: 42.86 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 675 EKLREHLAEKKQLNEE-RLEQEEKLKAKIRQLTEEKAALEERITQERNRanETLEEERKRMQELESLLAQQKKALAESIT 753
Cdd:PRK13709 1637 EPVTAEVLAQRQAEEAiRRETERRADEIVRKMAENKPDLPDGKTEQAVR--DIAGQERDRAAISEREAALPESVLREPQR 1714
|
90 100 110
....*....|....*....|....*....|..
gi 1622834852 754 QENRVKEALEE--EQTRVQELEKRLAR--QKE 781
Cdd:PRK13709 1715 EREAVREVAREnlLRERLQQMERDMVRdlQKE 1746
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
268-474 |
2.49e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 268 LSETTTSRQNEREISQkcqvLDEDIDAKQKEIQSLKSQISALQKGYSQLLcQTLSERNSEITSLKNEGENLKRDNAIASG 347
Cdd:COG4942 16 AAQADAAAEAEAELEQ----LQQEIAELEKELAALKKEEKALLKQLAALE-RRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 348 MVSSLQKDMLAKDEQVQELKEKVNQLKSQNK-----------DKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELK 416
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPlalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622834852 417 LCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEM 474
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
666-820 |
2.60e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.10 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 666 QETQQSLLQEKLREHLAEKKQLNEERLEQEEKLKAKI---RQLTEEKAALEERITQERNRANETLEEERKRMQELESLLA 742
Cdd:PRK09510 85 EQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEeaaKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 743 QQKKALAESITQ-------------ENRVKEALEEEQTRVQELEKR---LARQKEVLESSIAHEKRKAKEALESEKRKVQ 806
Cdd:PRK09510 165 AEAKKKAEAEAAkkaaaeakkkaeaEAAAKAAAEAKKKAEAEAKKKaaaEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAA 244
|
170
....*....|....
gi 1622834852 807 DLENHLTQQKEVSE 820
Cdd:PRK09510 245 KAAEKAAAAKAAAE 258
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
670-793 |
2.79e-03 |
|
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.
Pssm-ID: 462259 [Multi-domain] Cd Length: 353 Bit Score: 41.90 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 670 QSLLQEklrEHLAEKKQLNEERLEQEEKLKAKIRQLTEEKAALEERITQERNRANETLEEERKRMQElesllAQQKKALA 749
Cdd:pfam07767 198 QELLQK---AVEAEKKRLKEEEKLERVLEKIAESAATAEAREEKRKTKAQRNKEKRRKEEEREAKEE-----KALKKKLA 269
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1622834852 750 ESITQENRVKEALEEEQTRVQELEKRLARQKEVLESSIAHEKRK 793
Cdd:pfam07767 270 QLERLKEIAKEIAEKEKEREEKAEARKREKRKKKKEEKKLRPRK 313
|
|
| FHA_OdhI-like |
cd22721 |
forkhead associated (FHA) domain found in Corynebacterium glutamicum oxoglutarate ... |
11-65 |
2.82e-03 |
|
forkhead associated (FHA) domain found in Corynebacterium glutamicum oxoglutarate dehydrogenase inhibitor (OdhI) and similar proteins; OdhI is an essential component of the PknG signaling pathway. It regulates glutamate production under biotin non-limiting conditions. It can inhibit the activity of 2-oxoglutarate dehydrogenase only when it is unphosphorylated. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438773 [Multi-domain] Cd Length: 102 Bit Score: 38.92 E-value: 2.82e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1622834852 11 FFVLNKSTTIGRHEDSDLVLQSPDIDNHHAliEYNEAECSFVLQDFNSRNGTFVN 65
Cdd:cd22721 24 FLLDQPTTTAGRHPESDIFLDDVTVSRRHA--EFRINEGEFEVVDVGSLNGTYVN 76
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
673-779 |
3.00e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 673 LQEKLREHLAEKKQLNE-----ERLEQE--------EKLKAKIRQLTEEKAALEERITQ---ERNRANETLEEERKRMQE 736
Cdd:COG4913 666 AEREIAELEAELERLDAssddlAALEEQleeleaelEELEEELDELKGEIGRLEKELEQaeeELDELQDRLEAAEDLARL 745
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1622834852 737 LESLLAQQKKALAESITQENRVKEALEEEQTRVQELEKRLARQ 779
Cdd:COG4913 746 ELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
709-801 |
3.09e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 39.34 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 709 KAALEERitqeRNRANETLEEERKRMQELESLLAQQKKALAESITQ-----ENRVKEALEEEQTRVQELEKRLARQKEVL 783
Cdd:cd06503 25 LKALDER----EEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEaqeiiEEARKEAEKIKEEILAEAKEEAERILEQA 100
|
90
....*....|....*...
gi 1622834852 784 ESSIAHEKRKAKEALESE 801
Cdd:cd06503 101 KAEIEQEKEKALAELRKE 118
|
|
| FHA_CHK2 |
cd22666 |
forkhead associated (FHA) domain found in checkpoint kinase 2 (Chk2) and similar proteins; ... |
10-65 |
3.44e-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: 38.76 E-value: 3.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622834852 10 GFFVL---NKSTTIGRHEDSDLVLQSPDIDNH---------HALI--EYNEAECSFV-LQDFnSRNGTFVN 65
Cdd:cd22666 10 GFSSLdlvKDEYTFGRDKSCDYCFDSPALKKTsyyrtyskkHFRIfrEKGSKNTYPVfLEDH-SSNGTFVN 79
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
15-85 |
3.66e-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: 38.49 E-value: 3.66e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622834852 15 NKSTTIGRHEDS--DLVLQ-SPDIDNHHALIEYNeAECSFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFG 85
Cdd:cd22663 20 GKEVTVGRGLGVtyQLVSTcPLMISRNHCVLKKN-DEGQWTIKDNKSLNGVWVNGERIEpLKPYPLNEGDLIQLG 93
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
617-1127 |
3.80e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.02 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 617 EEVEQLLRDLGILPSSADKGFSLYLIYLLEHYKKLMSQT---QELQIKFNSSQEtQQSLLQEKLREHLAEKKQLNEERle 693
Cdd:pfam05483 222 EKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTfllEESRDKANQLEE-KTKLQDENLKELIEKKDHLTKEL-- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 694 qeEKLKAKIRQLTEEKAALEERITQERNRANETLEEERKRMQELESLLAQQKKALAESITQENRVKEALEEEQTRVQ--- 770
Cdd:pfam05483 299 --EDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEkne 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 771 --------ELEKRLARQKEVL-------------------ESSIAHEKRKAKEALESEKRKVQDLeNHLTQQKEVSESSI 823
Cdd:pfam05483 377 dqlkiitmELQKKSSELEEMTkfknnkeveleelkkilaeDEKLLDEKKQFEKIAEELKGKEQEL-IFLLQAREKEIHDL 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 824 AYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLS--NK--LNDALAMVEETQKTKA--TESLKAESLALKL 897
Cdd:pfam05483 456 EIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLleNKelTQEASDMTLELKKHQEdiINCKKQEERMLKQ 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 898 NETLAELETT-KTKMILMEERLILQQKTVKAVQDEQESQRHGFEEEIMEYKEQIKQHSQTIVSLEEKLQKVSQHHKKIEG 976
Cdd:pfam05483 536 IENLEEKEMNlRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQ 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 977 EIATLKDNDPAQKEE---------RPQDPLVAPTTDSGAKDMAYEHLIDDLLAAQKEILSQQEV-------IMKLRKDLT 1040
Cdd:pfam05483 616 ENKALKKKGSAENKQlnayeikvnKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKakaiadeAVKLQKEID 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1041 EAHSRMSDLRGELNEKQKMELERnvaLVQQQSKELSVLKEKMAQMSSLTEKKDRELKALKEALRASQEkhrlQLNTEKEQ 1120
Cdd:pfam05483 696 KRCQHKIAEMVALMEKHKHQYDK---IIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKK----QLEIEKEE 768
|
....*..
gi 1622834852 1121 KSRKKTQ 1127
Cdd:pfam05483 769 KEKLKME 775
|
|
| FHA_PPP1R8 |
cd22674 |
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ... |
16-93 |
4.00e-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: 38.40 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 16 KSTTIGR-HEDSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFGSAGLTYEL 93
Cdd:cd22674 27 KYYLFGRnSDVCDFVLDHPSCSRVHAALVYHKHLNRVFLIDLGSTHGTFVGGIRLEpHKPQQLPIDSTLRFGASTRRYIL 106
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
283-502 |
4.78e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 283 QKCQVLDEDIDAKQKEIQSLKSQISALQKgysqlLCQTLSERNSEITSLKNegenlkrdnaiasgmVSSLQKDMLAKDEQ 362
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEA-----ELDALQERREALQRLAE---------------YSWDEIDVASAERE 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 363 VQELKEKVNQLKSQNKDkdhqLEALGSRCSVLKEELkqeDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTE 442
Cdd:COG4913 670 IAELEAELERLDASSDD----LAALEEQLEELEAEL---EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 443 QSVISRTLREKSKVEEKLQEDSRRKLLQLQEmgnreslikiNLERAVGQLEHFRSQVIKA 502
Cdd:COG4913 743 ARLELRALLEERFAAALGDAVERELRENLEE----------RIDALRARLNRAEEELERA 792
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
673-800 |
5.24e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 673 LQEKLREHLAEKKQLNEERLEQE---EKLKAKIRQLTEEKAALEERITQERNRANET------------LEEERKRMQEL 737
Cdd:COG1579 29 LPAELAELEDELAALEARLEAAKtelEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyealqkeIESLKRRISDL 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622834852 738 ESLLAQQKKALAESITQENRVKEALEEEQTRVQELEKRLARQKEVLESSIAHEKRKAKEALES 800
Cdd:COG1579 109 EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
279-462 |
5.51e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 279 REISQKCQVLDEDIDAKQKEIQSLKSQISALQKGYSqllcQTLSERNSEITSLKNEGENLKRDNAIASGMVSSLQKDMLA 358
Cdd:PHA02562 177 RELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNG----ENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 359 KDEQVQELKEKVNQLKSQNK--DKDHQLEALGSRCSVLKEELKQED-----AHRELREAQeKELKLCKTQIQDMEKEM-- 429
Cdd:PHA02562 253 PSAALNKLNTAAAKIKSKIEqfQKVIKMYEKGGVCPTCTQQISEGPdritkIKDKLKELQ-HSLEKLDTAIDELEEIMde 331
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622834852 430 -----KKLRAELRKSCTEQSVISRTLREKSKVEEKLQE 462
Cdd:PHA02562 332 fneqsKKLLELKNKISTNKQSLITLVDKAKKVKAAIEE 369
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
228-803 |
5.62e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 228 EIILLLGKEVSRLSDYEIESKYKDVIIANLQKEVAELSQKLSETTTSRQNEREISQKCQVLDEDIDAKQKEIQSLKSQIS 307
Cdd:PRK01156 173 DVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKN 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 308 ALQK--GYSQLLCQTLSERNSEITSLKNEGENLKRDNAIAS-----------GMVSSLQKDMLAKDEQVQELKEKVNQLK 374
Cdd:PRK01156 253 RYESeiKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNrnyindyfkykNDIENKKQILSNIDAEINKYHAIIKKLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 375 SQNKDKDhQLEALGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTL-REK 453
Cdd:PRK01156 333 VLQKDYN-DYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIkKEL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 454 SKVEEKLQE-DSRRKLLQLQEMGNRESLIKI--NLERAVGQ---------LEHFRSQVIKATYGRAKpfpdkpvtdQQLI 521
Cdd:PRK01156 412 NEINVKLQDiSSKVSSLNQRIRALRENLDELsrNMEMLNGQsvcpvcgttLGEEKSNHIINHYNEKK---------SRLE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 522 EKIAQVTEDNINFQQKKWTLQKETQLSNSKQeettenIEKLRTSLDscqacmKMSCCTSDLKKEVDLL-----QHLQVSP 596
Cdd:PRK01156 483 EKIREIEIEVKDIDEKIVDLKKRKEYLESEE------INKSINEYN------KIESARADLEDIKIKInelkdKHDKYEE 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 597 PVSGLQKVVLDILRHA-LSWLEEVEQL-LRDLGILPSSADKgfslyliyLLEHYKKLMSQTQELQIKFNSSQETQQSLLQ 674
Cdd:PRK01156 551 IKNRYKSLKLEDLDSKrTSWLNALAVIsLIDIETNRSRSNE--------IKKQLNDLESRLQEIEIGFPDDKSYIDKSIR 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 675 EKLRE--HLAEKKQLNEERLEQEEKLKAKIRQLTEEKAALEERItqernranETLEEERKRMQELESLLAQQKKALAESI 752
Cdd:PRK01156 623 EIENEanNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSII--------PDLKEITSRINDIEDNLKKSRKALDDAK 694
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1622834852 753 TQENRVKEALEEEQTRVQELEKRLARQKEVLESsiaheKRKAKEALESEKR 803
Cdd:PRK01156 695 ANRARLESTIEILRTRINELSDRINDINETLES-----MKKIKKAIGDLKR 740
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
257-561 |
5.96e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.26 E-value: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 257 LQKEVAELSQK----------LSETTTSRQ-NEREI---SQKCQVLDEDIDAKQKEIQSLKSQISALQkgYSQLLCQTL- 321
Cdd:pfam15921 477 LRKVVEELTAKkmtlessertVSDLTASLQeKERAIeatNAEITKLRSRVDLKLQELQHLKNEGDHLR--NVQTECEALk 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 322 ---SERNSEITSLKNEGENLKRDNAIASGMVSSLQKDMLAKDEQVQELKEKVNQLKSQNKDKDHQLEALGSRCSVLK-EE 397
Cdd:pfam15921 555 lqmAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElEK 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 398 LKQEDAHRELREAqekeLKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSkveEKLQEDSRRKLLQLQEMGNR 477
Cdd:pfam15921 635 VKLVNAGSERLRA----VKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKS---EEMETTTNKLKMQLKSAQSE 707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 478 ESLIKINLERAVGQLEHfrsqVIKATYGRAKPFPDKPVTDQQLIEKIAQVTEDNINFQQKKWTLQKETqlSNSKQEETTE 557
Cdd:pfam15921 708 LEQTRNTLKSMEGSDGH----AMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEK--NKLSQELSTV 781
|
....
gi 1622834852 558 NIEK 561
Cdd:pfam15921 782 ATEK 785
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
226-484 |
6.29e-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: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 226 KDEIILLLGKEVSRLSDyeiESKYKDVIIANLQKEVAELSQKLSETTTSrqnereisqkCQVLDEDIDAKQKEIQSLKSQ 305
Cdd:pfam10174 392 KERKINVLQKKIENLQE---QLRDKDKQLAGLKERVKSLQTDSSNTDTA----------LTTLEEALSEKERIIERLKEQ 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 306 ISALQKgysqllcqtlsERNSEITSLKNEGENLKRDnaiasgmVSSLQKDMLAKDEQVQELKEKVNQLKSQNKDKDHQLE 385
Cdd:pfam10174 459 REREDR-----------ERLEELESLKKENKDLKEK-------VSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLK 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 386 ALGSRCSVLKEE-LKQEDAHRELREAQEKELKLCK--TQIQDMEKEMKKLRAELRKSCTEQSVISRTLR----EKSKVEE 458
Cdd:pfam10174 521 SLEIAVEQKKEEcSKLENQLKKAHNAEEAVRTNPEinDRIRLLEQEVARYKEESGKAQAEVERLLGILRevenEKNDKDK 600
|
250 260
....*....|....*....|....*.
gi 1622834852 459 KLQEDSRRKLLQLQEMGNRESLIKIN 484
Cdd:pfam10174 601 KIAELESLTLRQMKEQNKKVANIKHG 626
|
|
| FHA_Ct664-like |
cd22696 |
forkhead associated (FHA) domain found in Chlamydia trachomatis Ct664 protein and similar ... |
8-86 |
7.04e-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: 37.47 E-value: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 8 AEGFFVLNKSTTIGRHED-SDLVLQSPDIDNHHALIEYNEAECSFVlQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGS 86
Cdd:cd22696 13 AEFFLESGKTYFIGKDPTvCDIVLQDPSISRQHARLSIDQDNRVFI-EDLSSKNGVLVNGKPIEG-KEEISGSDVISLGT 90
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
610-828 |
7.72e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 7.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 610 RHALSWLEEVEQLLRdlgiLPSSADKGFSLYLIYLLEHYKKLMSQTQELQIKFNSSQETQ----------QSLLQEKLRE 679
Cdd:PRK04863 417 QQAVQALERAKQLCG----LPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHsqfeqayqlvRKIAGEVSRS 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 680 HLAEKKQLNEERLEQEEKLKAKIRQLTEEKAALEERITQERnRANETLEEERKRMQ-------ELESLLAQQKKAL---- 748
Cdd:PRK04863 493 EAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQ-RAERLLAEFCKRLGknlddedELEQLQEELEARLesls 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 749 ---AESITQENRVKEALEEEQTRVQELEKRlARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEVSESSIAY 825
Cdd:PRK04863 572 esvSEARERRMALRQQLEQLQARIQRLAAR-APAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDEL 650
|
...
gi 1622834852 826 EKR 828
Cdd:PRK04863 651 AAR 653
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
667-848 |
7.86e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 667 ETQQSLLqeKLREHLAEKKQLNEERleqeEKLKAKIRQLTEEKAALEERITqernRANETLEEERKRMQELESLLAQQKK 746
Cdd:COG1579 4 EDLRALL--DLQELDSELDRLEHRL----KELPAELAELEDELAALEARLE----AAKTELEDLEKEIKRLELEIEEVEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 747 ALAESITQENRVK-----EALEEE----QTRVQELEKRLARQKEVLEssiahekrKAKEALESEKRKVQDLENHLTQQKE 817
Cdd:COG1579 74 RIKKYEEQLGNVRnnkeyEALQKEieslKRRISDLEDEILELMERIE--------ELEEELAELEAELAELEAELEEKKA 145
|
170 180 190
....*....|....*....|....*....|.
gi 1622834852 818 VSESSIAYEKRKAKEAMEKEKKKVQDLENRL 848
Cdd:COG1579 146 ELDEELAELEAELEELEAEREELAAKIPPEL 176
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
667-1134 |
9.33e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.49 E-value: 9.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 667 ETQQSLLQEKLREHLAEKKQLNEERLEQEEKLKAKIRQL--TEEKAALEERITQ---ERNRANET--------LEEERKR 733
Cdd:pfam15921 348 EKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLhkREKELSLEKEQNKrlwDRDTGNSItidhlrreLDDRNME 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 734 MQELESLLAQQKKALAESITQENRVKEALEEEQTRVQELEKRLARQKEVLESsIAHEKRKAKEALESEKRKVQDLENHLT 813
Cdd:pfam15921 428 VQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRK-VVEELTAKKMTLESSERTVSDLTASLQ 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 814 QQKEVSESSIAY---------EKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLSNKLNDALAMVEETQKTKA 884
Cdd:pfam15921 507 EKERAIEATNAEitklrsrvdLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAG 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 885 TESLKAESLALKLNETLAELETTK-------TKMILMEERLI-LQQKTVKAVQDEQESQR--HGFEEEIMEYKEQIKQHS 954
Cdd:pfam15921 587 AMQVEKAQLEKEINDRRLELQEFKilkdkkdAKIRELEARVSdLELEKVKLVNAGSERLRavKDIKQERDQLLNEVKTSR 666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 955 QTIVSLEEKLQKVSQHHKKIEGEIATlKDNDPAQKEERPQDPLVAPTTDSGAKDMAYEHLIDDLLAAQKEILSQQEVIMK 1034
Cdd:pfam15921 667 NELNSLSEDYEVLKRNFRNKSEEMET-TTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDA 745
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 1035 LRKDLTEAHSRMSDLrgelnEKQKMELERNVALVQQQSKELSVLKEKMAQMSSLTEKKDRELKALKEALRASQEKHRLQL 1114
Cdd:pfam15921 746 LQSKIQFLEEAMTNA-----NKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQF 820
|
490 500
....*....|....*....|
gi 1622834852 1115 NTEKEQKSRKKTQTCDTSVQ 1134
Cdd:pfam15921 821 AECQDIIQRQEQESVRLKLQ 840
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
294-492 |
9.46e-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: 39.74 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 294 AKQKEIQSLKSQISA----LQKGYSQLLCQTLSERN---SEITSLKNEGENLKRDNAiasGMVSSLQKDMLAKDEQVQEL 366
Cdd:pfam09787 22 SKEKLIASLKEGSGVegldSSTALTLELEELRQERDllrEEIQKLRGQIQQLRTELQ---ELEAQQQEEAESSREQLQEL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 367 KEKVNQLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRelreaqekelklcKTQIQDMEKEMKKLRAELR---KSCTEQ 443
Cdd:pfam09787 99 EEQLATERSARREAEAELERLQEELRYLEEELRRSKATL-------------QSRIKDREAEIEKLRNQLTsksQSSSSQ 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622834852 444 SVISRTLREkskveekLQEDSRRKLLQLQEMGNRESLIKINLERAVGQL 492
Cdd:pfam09787 166 SELENRLHQ-------LTETLIQKQTMLEALSTEKNSLVLQLERMEQQI 207
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
254-494 |
9.72e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 9.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 254 IANLQKEVAELSQklsetttSRQNEREISQKCQVLdEDIDAKQKEIQSLKSQISALQKGYSQLlcqTLSERNSEITSLKN 333
Cdd:COG4913 227 ADALVEHFDDLER-------AHEALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAAL---RLWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 334 EGENLKRDnaiasgmVSSLQKDMLAKDEQVQELKEKVNQLKSQnkdkdhQLEALGSRCSVLKEELKQEDAHRELREAQEK 413
Cdd:COG4913 296 ELEELRAE-------LARLEAELERLEARLDALREELDELEAQ------IRGNGGDRLEQLEREIERLERELEERERRRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834852 414 EL-KLCKT---QIQDMEKEMKKLRAELRKSCT----EQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESLIKINL 485
Cdd:COG4913 363 RLeALLAAlglPLPASAEEFAALRAEAAALLEaleeELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442
|
....*....
gi 1622834852 486 ERAVGQLEH 494
Cdd:COG4913 443 LALRDALAE 451
|
|
| |
