|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
2-97 |
9.98e-49 |
|
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 (FHAD1) and similar proteins; FHAD1, also called FHA domain-containing protein 1, is an uncharacterized FHA domain-containing protein. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438752 [Multi-domain] Cd Length: 96 Bit Score: 168.20 E-value: 9.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 2 KAYLKSADGFFVLN-KSTTIGKHaDSDLVLQSADIDNHHALIEFNEAEGTFVLQDFNSRNGTFVNECHIQNVAVKLIPGD 80
Cdd:cd22700 1 KGYLKSSDGIFQLDpKVTTIGRE-GCDLVLQSPGVEEQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAPGD 79
|
90
....*....|....*..
gi 568931432 81 ILRFGSAGMTYELVIEN 97
Cdd:cd22700 80 VLRFGFGGLPYELVVDN 96
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
18-84 |
2.00e-17 |
|
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 77.62 E-value: 2.00e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568931432 18 TTIGKHADSDLVLQSADIDNHHALIEFNEaEGTFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRF 84
Cdd:pfam00498 1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDG-GGRFYLEDLGSTNGTFVNGQRLGPEPVRLKDGDVIRL 66
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
285-1035 |
4.52e-17 |
|
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: 87.42 E-value: 4.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 285 DDLRQKEIESMKSQINALQKGYSQVLSQtLAERNTEIESLKNEGENLKRDHAItsgmvtsLQKDMSARNEQVQQLQEEVN 364
Cdd:TIGR02168 220 AELRELELALLVLRLEELREELEELQEE-LKEAEEELEELTAELQELEEKLEE-------LRLEVSELEEEIEELQKELY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 365 RLRIENREKEYQLEALSSRCSVMKEELRKEEAQ----KDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNYMGQNIIS 440
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLANLERQLEELEAQleelESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 441 KTLREKNKVEEKLQEDSRRKLLQLQEMGNRENLIKINLERAVGQLENFRNQVIKATFGKTKPFRDKPITDQQLIEKII-Q 519
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELeE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 520 VTEDNLSFQQRKWTLQRE-THLHPKQEETMHSVEKLRVLLDKCQACMRDSCSSIDLKKEVELLQHLPlsplvSGLQKTVV 598
Cdd:TIGR02168 452 LQEELERLEEALEELREElEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGL-----SGILGVLS 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 599 NILRVSLSWLEETEQLLGD--------------LDIE-LSDSDKGFSLCLIYLLEHYKKIMSQSQDLQAQMNASRETQKS 663
Cdd:TIGR02168 527 ELISVDEGYEAAIEAALGGrlqavvvenlnaakKAIAfLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKD 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 664 LRQE-------------HLAEKEKLAEKLEQEEKLKAKIQQLTEE------------KAALEESIGQEKSRseeALEKAQ 718
Cdd:TIGR02168 607 LVKFdpklrkalsyllgGVLVVDDLDNALELAKKLRPGYRIVTLDgdlvrpggvitgGSAKTNSSILERRR---EIEELE 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 719 ARVRELENHLASQKEALeNSVAQEKRKMREMLEAERRKAQDLENQLTQQKEisenntyEKLKMRDTLEKEKRKIQDLENR 798
Cdd:TIGR02168 684 EKIEELEEKIAELEKAL-AELRKELEELEEELEQLRKELEELSRQISALRK-------DLARLEAEVEQLEERIAQLSKE 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 799 LTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQmkttESQRAETLALKLKETLAELEttktkMILTDDRLKLQQQSMKA 878
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEA----QIEQLKEELKALREALDELR-----AELTLLNEEAANLRERL 826
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 879 LQDEResQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAGPPLDSGDK 958
Cdd:TIGR02168 827 ESLER--RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568931432 959 EIAcdhliDDLLMAQKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQKMELERQVALVRQQSGELSMLKAKVAQ 1035
Cdd:TIGR02168 905 ELE-----SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
11-92 |
6.54e-17 |
|
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.
Pssm-ID: 438714 [Multi-domain] Cd Length: 92 Bit Score: 77.32 E-value: 6.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 11 FFVLNKSTTIGKHADSDLVLQSADIDNHHALIEFNeaEGTFVLQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGMT 90
Cdd:cd00060 14 FPLTKGVVTIGRSPDCDIVLDDPSVSRRHARIEVD--GGGVYLEDLGSTNGTFVNGKRITP-PVPLQDGDVIRLGDTTFR 90
|
..
gi 568931432 91 YE 92
Cdd:cd00060 91 FE 92
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
12-93 |
1.36e-16 |
|
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 76.54 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 12 FVLNKS-TTIGKHADSDLVLQSADIDNHHALIEFNeaEGTFVLQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGMT 90
Cdd:COG1716 16 FPLDGGpLTIGRAPDNDIVLDDPTVSRRHARIRRD--GGGWVLEDLGSTNGTFVNGQRVTE-PAPLRDGDVIRLGKTELR 92
|
...
gi 568931432 91 YEL 93
Cdd:COG1716 93 FRL 95
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
646-894 |
5.35e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.75 E-value: 5.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 646 QSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEksrsEEALEKAQARVRELE 725
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL----EEELEELEEELEEAE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 726 NHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENntyeklkmRDTLEKEKRKIQDLENRLTKQKEE 805
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL--------AAQLEELEEAEEALLERLERLEEE 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 806 IELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKmILTDDRLKLQQQSMKALQDERES 885
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA-LAELLEELAEAAARLLLLLEAEA 501
|
....*....
gi 568931432 886 QKHGFEEEI 894
Cdd:COG1196 502 DYEGFLEGV 510
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
213-903 |
7.79e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.02 E-value: 7.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 213 SQQDKDEIILLLGREVNRLSDFEMESKYKDALIMN----LQAEVADLSQRLSETAAVAAAR--QSNRCDPKLQGVDEGDD 286
Cdd:TIGR02168 282 EIEELQKELYALANEISRLEQQKQILRERLANLERqleeLEAQLEELESKLDELAEELAELeeKLEELKEELESLEAELE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 287 LRQKEIESMKSQINALQKGYSQV------LSQTLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSarNEQVQQLQ 360
Cdd:TIGR02168 362 ELEAELEELESRLEELEEQLETLrskvaqLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 361 EEVNRLRIENREKEYQLEALSSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNYMGQNIIS 440
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 441 K---TLREKNKVEEKLQ------------------EDSRRKLLQLQEMGNRENLIKINLERAVGQLENFRNQVIKATFGK 499
Cdd:TIGR02168 520 GilgVLSELISVDEGYEaaieaalggrlqavvvenLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEG 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 500 TKPFRDKPITDQQLIEKIIQ-------VTED---------NLSFQQRKWTLQREThLHP------KQEETMHSVEKLRVL 557
Cdd:TIGR02168 600 FLGVAKDLVKFDPKLRKALSyllggvlVVDDldnalelakKLRPGYRIVTLDGDL-VRPggvitgGSAKTNSSILERRRE 678
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 558 LDKCQACMRDSCSSIDLKKevellqhlplsplvsglqkTVVNILRVSLSWLEETEQLLGDLDIELSDSDKGFSLCLIYLL 637
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELE-------------------KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE 739
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 638 EHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALeesigqeksrsEEALEKA 717
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL-----------REALDEL 808
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 718 QARVRELENHLASQKEALENSVAQekrkmremLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLEN 797
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERR--------IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN 880
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 798 RLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMiltDDRLKLQQQSMK 877
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL---SEEYSLTLEEAE 957
|
730 740
....*....|....*....|....*.
gi 568931432 878 ALQDERESQKHGFEEEISEYKEQIKQ 903
Cdd:TIGR02168 958 ALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
224-863 |
1.04e-13 |
|
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: 76.65 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 224 LGREVNRLSDFEMeskykdaliMNLQAEVADLS--QRLSETAAVAAARQSNRCDPKLQGVDEGDDLRQKEIESMKSQINA 301
Cdd:TIGR02169 277 LNKKIKDLGEEEQ---------LRVKEKIGELEaeIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 302 LQKGYSQvLSQTLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLE--- 378
Cdd:TIGR02169 348 ERKRRDK-LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELAdln 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 379 -----------ALSSRCSVMKEELRKEEAQ----KDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNYMGQNIISKTL 443
Cdd:TIGR02169 427 aaiagieakinELEEEKEDKALEIKKQEWKleqlAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 444 REKNKVEEKLQEDSRRKLLQLQEMGNRENLIKINLERAVGQLENF-----------------RNQVIKATF---GKTKPF 503
Cdd:TIGR02169 507 RGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNvvveddavakeaiellkRRKAGRATFlplNKMRDE 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 504 RDKP--ITDQQLIEKIIQVTEDNLSFQQRKWTLQRETHLHPKQEETMHSVEKLRV------LLDKCQACM--RDSCSSID 573
Cdd:TIGR02169 587 RRDLsiLSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVEDIEAARRLMGKYRMvtlegeLFEKSGAMTggSRAPRGGI 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 574 LKKEVELLQHLPLSPLVSGLQKTvvniLRVSLSWLEETEQLLGDLDIELSDSDKGFSLcliyllehykkIMSQSQDLQAQ 653
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGLKRE----LSSLQSELRRIENRLDELSQELSDASRKIGE-----------IEKEIEQLEQE 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 654 MNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQ-EKSRSEEALEKAQARVRELENHLASQK 732
Cdd:TIGR02169 732 EEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlEARLSHSRIPEIQAELSKLEEEVSRIE 811
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 733 EALE------NSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEI 806
Cdd:TIGR02169 812 ARLReieqklNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER 891
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 568931432 807 ELKEQKENVLNNKLKDALVMVEDA-QQMKTTESQRAEtlalkLKETLAELETTKTKMI 863
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQIEKKrKRLSELKAKLEA-----LEEELSEIEDPKGEDE 944
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
235-934 |
1.11e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 76.25 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 235 EMESKYKDALIMNLQAEVADLSQRLSETAAvaAARQSNRCDPKLQGVDEGDDLRQKEIESMKSQINALQKGYsQVLSQTL 314
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKE--AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL-YALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 315 AERNTEIESLKNEGENLKRDHAITSGMVTS-------LQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSR---C 384
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEEleskldeLAEELAELEEKLEELKEELESLEAELEELEAELEELESRleeL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 385 SVMKEELRKEEAQKDRREAQ-EKELKLCRSQMQDMEKEVRKLREELKKNYMGQ-----NIISKTLREKNKVEEKLQEDSR 458
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASlNNEIERLEARLERLEDRRERLQQEIEELLKKLeeaelKELQAELEELEEELEELQEELE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 459 RKLLQLQEMGNRENLIKINLERAVGQLE--NFRNQVIKATFGKTKPFRD--KPITDQQL-IEKIIQVTEDNLSFQQrKWT 533
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAqlQARLDSLERLQENLEGFSEgvKALLKNQSgLSGILGVLSELISVDE-GYE 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 534 LQRETHLhpkqEETMHSVeklrvLLDKCQACMRDscssIDLKKEVELLQHLPLsPLVSGLQKTVVNILRVSLSWLEETEQ 613
Cdd:TIGR02168 537 AAIEAAL----GGRLQAV-----VVENLNAAKKA----IAFLKQNELGRVTFL-PLDSIKGTEIQGNDREILKNIEGFLG 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 614 LLGDLDielsDSDKGFSLCLIYLLEHY----------------------------------------------------- 640
Cdd:TIGR02168 603 VAKDLV----KFDPKLRKALSYLLGGVlvvddldnalelakklrpgyrivtldgdlvrpggvitggsaktnssilerrre 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 641 --------KKIMSQSQDLQAQMNASRETQKSLRQEhLAEKEKLAEKLEQE--------EKLKAKIQQLTEEKAALEESIG 704
Cdd:TIGR02168 679 ieeleekiEELEEKIAELEKALAELRKELEELEEE-LEQLRKELEELSRQisalrkdlARLEAEVEQLEERIAQLSKELT 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 705 ---QEKSRSEEALEKAQARVRELENHLASQKEALENsvaqekrkMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKM 781
Cdd:TIGR02168 758 eleAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ--------LKEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 782 RDTLEKEKRKIQDLENRLTKQKEEIELKEQ---KENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETT 858
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAAeieELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK 909
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568931432 859 KTKMiltDDRLKLQQQSMKALQDEREsqkhGFEEEISEYKEQI-KQHSQTIVSLEERLCQVTQYYQKIEGEITTLKN 934
Cdd:TIGR02168 910 RSEL---RRELEELREKLAQLELRLE----GLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
25-93 |
2.53e-13 |
|
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) family; The Cep170 family includes Cep170 and Cep170B. Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438756 [Multi-domain] Cd Length: 102 Bit Score: 67.34 E-value: 2.53e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 25 DSDLVLQSADIDNHHALIEFNEAEGTFVLQDFNSRNGTFVNECHI-QNVAVKLIPGDILRFGSAGMTYEL 93
Cdd:cd22704 25 DCDLILQSRSVDKQHAVITYDQIDNEFKIKDLGSLNGTFVNDSRIpEQTYITLKLGDSIRFGYDTNVYRF 94
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
249-799 |
4.23e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.59 E-value: 4.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 249 QAEVA----DLSQRLSETAAVAAARQsnrcdpklqgvdegDDLRQKEIESMKSQINALQKGySQVLSQTLAERNTEIESL 324
Cdd:COG1196 208 QAEKAeryrELKEELKELEAELLLLK--------------LRELEAELEELEAELEELEAE-LEELEAELAELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 325 KNEGENLKRDhaitsgmVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSRCSVMKEELRKEEAQKDRREAQ 404
Cdd:COG1196 273 RLELEELELE-------LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 405 EKELKLCRSQMQDMEKEVRKLREELKKNYMGQNIISKTLREKNKVEEKLQEDSRRKLLQLQEMGNRENLIKINLERAVGQ 484
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 485 LENFRNQVIKATFGKTKPFRDKPITDQQLIEKIIQVTEDNLSFQQRKWTLQ---------------RETHLHPKQEETMH 549
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEaalaelleelaeaaaRLLLLLEAEADYEG 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 550 SVEKLRVLLDKCQACMRDSCSSIDLKKEVELLQHLPLSPLVSGLQKTV-------------------------VNILRVS 604
Cdd:COG1196 506 FLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVeddevaaaaieylkaakagratflpLDKIRAR 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 605 LSWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEK 684
Cdd:COG1196 586 AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 685 LKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEALEnsvaQEKRKMREMLEAERRKAQDLENQL 764
Cdd:COG1196 666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERL----EEELEEEALEEQLEAEREELLEEL 741
|
570 580 590
....*....|....*....|....*....|....*
gi 568931432 765 TQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRL 799
Cdd:COG1196 742 LEEEELLEEEALEELPEPPDLEELERELERLEREI 776
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
633-887 |
5.10e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.20 E-value: 5.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 633 LIYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHL---AEKEKLAEKLEQEEK----LKAKIQQLTEEKAALEESI-- 703
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAeleAELEELRLELEELELeleeAQAEEYELLAELARLEQDIar 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 704 -GQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTyEKLKMR 782
Cdd:COG1196 307 lEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE-ELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 783 DTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKM 862
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260
....*....|....*....|....*
gi 568931432 863 ILTDDRLKLQQQSMKALQDERESQK 887
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAA 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
637-1349 |
1.12e-12 |
|
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: 73.17 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 637 LEHYKKIMSQSQDLQAQMNASRETQKSLRQEHL-AEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQ---EKSRSEE 712
Cdd:TIGR02168 202 LKSLERQAEKAERYKELKAELRELELALLVLRLeELREELEELQEELKEAEEELEELTAELQELEEKLEElrlEVSELEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 713 ALEKAQAR-------VRELENHLASQKEALENSVAQEKRKMREMLEAERRKaQDLENQLTQQKEISENNTYEKLKMRDTL 785
Cdd:TIGR02168 282 EIEELQKElyalaneISRLEQQKQILRERLANLERQLEELEAQLEELESKL-DELAEELAELEEKLEELKEELESLEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 786 EKEKRKIQDLENRLTKQKEEIE-------LKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKEtlAELETT 858
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLEtlrskvaQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE--AELKEL 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 859 KTKMILTDDRLKLQQQSMKALQDERESQKHGFEE---EISEYKEQIKQHSQTIVSLEERLCQVTQYYqkiEGEITTLKNN 935
Cdd:TIGR02168 439 QAELEELEEELEELQEELERLEEALEELREELEEaeqALDAAERELAQLQARLDSLERLQENLEGFS---EGVKALLKNQ 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 936 DTGPKEEAS-QDLTAGPPLDSGDKEIACDHLIDDLLMAQKEilSQQEIIMKLR-TDLGEAH-SRMSDLRGELSEKQKMEL 1012
Cdd:TIGR02168 516 SGLSGILGVlSELISVDEGYEAAIEAALGGRLQAVVVENLN--AAKKAIAFLKqNELGRVTfLPLDSIKGTEIQGNDREI 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1013 ERQVALVRQQSGELSMLKAKVAQTTGLMEKKDRELKVLREALrasqekprphlstEQKPRTLSQKCDISLQIEPAHPDSF 1092
Cdd:TIGR02168 594 LKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNAL-------------ELAKKLRPGYRIVTLDGDLVRPGGV 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1093 SSFQ-EEQSFSDLGVKCKGSRHEETIQRQRKALSELRTRVRELEKANScNHKDHVNESFLELRTLRMEKNVQKILLDAKp 1171
Cdd:TIGR02168 661 ITGGsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELE-ELEEELEQLRKELEELSRQISALRKDLARL- 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1172 dLTTLARVEIRPPQNSPFNSGSTLVMEKSVKTDAGEALELSEKLytDMIKTLGSLMNiKDMSSHTSLKHLSPKEREKVNH 1251
Cdd:TIGR02168 739 -EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE--AEIEELEAQIE-QLKEELKALREALDELRAELTL 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1252 LRQKDLDLVFdKITQLKTRLQRKEELLKGYEQELEQLRH--SKVSVQM--YQTQVAKLEDDVHKEAEEKALLKEALERTE 1327
Cdd:TIGR02168 815 LNEEAANLRE-RLESLERRIAATERRLEDLEEQIEELSEdiESLAAEIeeLEELIEELESELEALLNERASLEEALALLR 893
|
730 740
....*....|....*....|..
gi 568931432 1328 QQLSQERRFNRVFKQQKDRGED 1349
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRR 915
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
254-1014 |
3.98e-12 |
|
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: 71.25 E-value: 3.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 254 DLSQRLSETAAVAAARQSNRCDPKLQGVDEGDDLRQKEIESMKSQINALQKGYSQvLSQTLAERNTEIESL-KNEGENLK 332
Cdd:TIGR02169 215 ALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEE-IEQLLEELNKKIKDLgEEEQLRVK 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 333 RDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSRcsvMKEELRKEEAQKDRREAQEKELKLCR 412
Cdd:TIGR02169 294 EKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE---IEEERKRRDKLTEEYAELKEELEDLR 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 413 SQMQDMEKEVRKLREELKKNymgQNIISKTLREKNKveekLQEDSRRKLLQLQEMGNRENLIKINLERAVGQLENFRNQV 492
Cdd:TIGR02169 371 AELEEVDKEFAETRDELKDY---REKLEKLKREINE----LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 493 ------IKATFGKTKPFRDKPITDQQLIEKI---IQVTEDNLSFQQRKWTlQRETHLHPKQEETMHSVEKLRVLLDKCQA 563
Cdd:TIGR02169 444 edkaleIKKQEWKLEQLAADLSKYEQELYDLkeeYDRVEKELSKLQRELA-EAEAQARASEERVRGGRAVEEVLKASIQG 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 564 CMRDSCSSIDLKKEVELLQHLPLSplvSGLQKTVV----------------NILRVSLSWLEETEQLLGDLDIELSDSDK 627
Cdd:TIGR02169 523 VHGTVAQLGSVGERYATAIEVAAG---NRLNNVVVeddavakeaiellkrrKAGRATFLPLNKMRDERRDLSILSEDGVI 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 628 GFSLCLIYLLEHYKKIMSQsqdlqaqmnASRETQkslrqehlaekekLAEKLEQEEKLKAKIQQLTEEKAALEES----- 702
Cdd:TIGR02169 600 GFAVDLVEFDPKYEPAFKY---------VFGDTL-------------VVEDIEAARRLMGKYRMVTLEGELFEKSgamtg 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 703 ------IGQEKSRSEEA-LEKAQARVRELENHLAS---QKEALENSVAQEKRKMRE---MLEAERRKAQDLENQLTQQKE 769
Cdd:TIGR02169 658 gsraprGGILFSRSEPAeLQRLRERLEGLKRELSSlqsELRRIENRLDELSQELSDasrKIGEIEKEIEQLEQEEEKLKE 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 770 ISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQR--------- 840
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSriearlrei 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 841 -AETLALKLKETLAELETTKTKMILTDdrLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSL-------E 912
Cdd:TIGR02169 818 eQKLNRLTLEKEYLEKEIQELQEQRID--LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLkkerdelE 895
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 913 ERLCQVTQYYQKIEGEITTLKNND---TGPKEEASQDLTA-GPPLDSGDKEIACDHLIDDLLMA----QKEILSQQEIIM 984
Cdd:TIGR02169 896 AQLRELERKIEELEAQIEKKRKRLselKAKLEALEEELSEiEDPKGEDEEIPEEELSLEDVQAElqrvEEEIRALEPVNM 975
|
810 820 830
....*....|....*....|....*....|
gi 568931432 985 KLRTDLGEAHSRMSDLRgelSEKQKMELER 1014
Cdd:TIGR02169 976 LAIQEYEEVLKRLDELK---EKRAKLEEER 1002
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
674-915 |
4.99e-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: 4.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 674 KLAEKLEQEEKLKAKIQQLTEEKAALEEsigqEKSRSEEALEKAQARVRELENHLASQKEAlENSVAQEKRKMREMLEAE 753
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEA----ELAELEAELEELRLELEELELELEEAQAE-EYELLAELARLEQDIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 754 RRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDAlvmvEDAQQM 833
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA----EEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 834 KTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEE 913
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
..
gi 568931432 914 RL 915
Cdd:COG1196 464 LL 465
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
12-92 |
8.95e-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: 62.63 E-value: 8.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 12 FVLNK-STTIGKHADSDLVLQSADIDNHHALIEFneAEGTFVLQDFNSRNGTFVNECHI--QNVAVKLIPGDILRFGSAG 88
Cdd:cd22665 16 FPLYEgENVIGRDPSCSVVLPDKSVSKQHACIEV--DGGTHLIEDLGSTNGTRIGNKVRlkPNVRYELIDGDLLLFGDVK 93
|
....
gi 568931432 89 MTYE 92
Cdd:cd22665 94 CQYV 97
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
676-950 |
9.84e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 9.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 676 AEKLEQEEKLKAKIQQLTEEKAALE--------ESIGQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMR 747
Cdd:COG1196 209 AEKAERYRELKEELKELEAELLLLKlreleaelEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 748 EMLEAERRKAQdLENQLTQQKEISENNtyeklkmRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMV 827
Cdd:COG1196 289 EEYELLAELAR-LEQDIARLEERRREL-------EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 828 EDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQkhgfEEEISEYKEQIKQHSQT 907
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL----EEELEELEEALAELEEE 436
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 568931432 908 IVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAG 950
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
658-945 |
1.47e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.32 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 658 RETQKSLR--QEHLA-------EKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIG----QEKSRSEEALEKAQARVREL 724
Cdd:TIGR02168 175 KETERKLErtRENLDrledilnELERQLKSLERQAEKAERYKELKAELRELELALLvlrlEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 725 ENHLASQKEALENSVAQEKRKMREM----------LEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQD 794
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELeeeieelqkeLYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 795 LENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQ 874
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568931432 875 SMKALQDERESQKHGFEE-EISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQ 945
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
12-86 |
5.38e-11 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaB and similar proteins; FhaB, also called FtsZ-interacting protein A (FipA), is a putative virulence factor involved in regulating cell shape. It can interact with polyketide-associated protein PapA5, a putative membrane protein involved in the biosynthesis of virulence enhancing lipids. FhaB regulates growth and cell division. It is probably required for divisomal protein assembly under oxidative stress. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438745 [Multi-domain] Cd Length: 91 Bit Score: 60.39 E-value: 5.38e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568931432 12 FVLNKST-TIGKHADSDLVLQSADIDNHHALIEFNEaeGTFVLQDFNSRNGTFVNECHIqNVAVKLIPGDILRFGS 86
Cdd:cd22693 13 FPIDKSGiTIGRADDNDLVLSDDFVSSRHARIYLQG--SSWYLEDLGSTNGTFVNGNRV-TQPVVVQPGDTIRIGA 85
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
657-933 |
5.96e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.40 E-value: 5.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 657 SRETQKSLR-QEHLAEKEKLA--EKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKE 733
Cdd:TIGR02169 204 RREREKAERyQALLKEKREYEgyELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 734 ALENSVAQEKRKMREmLEAERRKAQD----LENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELK 809
Cdd:TIGR02169 284 LGEEEQLRVKEKIGE-LEAEIASLERsiaeKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAEL 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 810 EQKENVLNNKLKDalvMVEDAQQMKTTESQRAETLAlKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHG 889
Cdd:TIGR02169 363 KEELEDLRAELEE---VDKEFAETRDELKDYREKLE-KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE 438
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 568931432 890 FEE-------EISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLK 933
Cdd:TIGR02169 439 LEEekedkalEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
671-1070 |
1.46e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.32 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 671 EKEKLAEKLEQEEKLKAKIQQL---TEEKAALEESI--GQEKSRSEEALEKAQARvRELENhlaSQKEALENSVAQEKRK 745
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAkkkAEEKKKADEAKkkAEEAKKADEAKKKAEEA-KKAEE---AKKKAEEAKKADEAKK 1477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 746 MREmleaERRKAQDLENQLTQQKEISEN--NTYEKLKMRDTLEK--EKRKIQDLENRLTKQKEEiELKEQKENVLNNKLK 821
Cdd:PTZ00121 1478 KAE----EAKKADEAKKKAEEAKKKADEakKAAEAKKKADEAKKaeEAKKADEAKKAEEAKKAD-EAKKAEEKKKADELK 1552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 822 DALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQI 901
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 902 KQHSQTIVSLEERLCQVTQYyqKIEGEITTLKNNDTGPKEEASQDLTAGPPLDSGDKEIACDHLIDDLLMAQK-EILSQQ 980
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEEL--KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKaEELKKK 1710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 981 EIIMKLRTDLGEAHSRMSDLRGELSEKQKMELERQVALVRQQSGElsmlKAKVAQTTGLMEKKDRELK-----VLREALR 1055
Cdd:PTZ00121 1711 EAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE----KKKIAHLKKEEEKKAEEIRkekeaVIEEELD 1786
|
410
....*....|....*
gi 568931432 1056 ASQEKPRPHLSTEQK 1070
Cdd:PTZ00121 1787 EEDEKRRMEVDKKIK 1801
|
|
| FHA_DUN1-like |
cd22683 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ... |
17-85 |
2.18e-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: 58.66 E-value: 2.18e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568931432 17 STTIGKHADSDLVLQSADIDNHHALIEFnEAEGTFVLqDFNSRNGTFVNECHIQNVAVKLIPGDILRFG 85
Cdd:cd22683 22 VTTIGRSRSCDLVLSDPSISRFHAELRL-EQNGINVI-DNNSANGTFINGKRIKGKTYILKNGDIIVFG 88
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
315-884 |
9.14e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.52 E-value: 9.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 315 AERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALssrcsvmkeELRKE 394
Cdd:PRK02224 247 EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAV---------EARRE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 395 EAQKDRREAQEkELKLCRSQMQDMEKEVRKLREELKKnymgQNIISKTLREKNKVEEKLQEDSRRKLlqlqemGNRENLI 474
Cdd:PRK02224 318 ELEDRDEELRD-RLEECRVAAQAHNEEAESLREDADD----LEERAEELREEAAELESELEEAREAV------EDRREEI 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 475 KInLERAVGQLEnfrnqvikatfgktKPFRDKPITDQQLIEKIIQVTEDnlsfqqRKWTLQRETHLHPKQEETMHSVEKL 554
Cdd:PRK02224 387 EE-LEEEIEELR--------------ERFGDAPVDLGNAEDFLEELREE------RDELREREAELEATLRTARERVEEA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 555 RVLLD--KCQACMrdscssidlkkevellQHLPLSPLVSGlqktvvnilrvslswLEETEQLLGDLDIELSDsdkgfslc 632
Cdd:PRK02224 446 EALLEagKCPECG----------------QPVEGSPHVET---------------IEEDRERVEELEAELED-------- 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 633 liyllehykkIMSQSQDLQAQMNASRETQKSLRQ-EHLAEKEKLAEKL--EQEEKLKAK---IQQLTEEKAALEESiGQE 706
Cdd:PRK02224 487 ----------LEEEVEEVEERLERAEDLVEAEDRiERLEERREDLEELiaERRETIEEKrerAEELRERAAELEAE-AEE 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 707 K----SRSEEALEKAQARVRELENHLASQKEALENSvaqekRKMREMLEAERRKAQDLENQLTQQKEISENNTYEklkmR 782
Cdd:PRK02224 556 KreaaAEAEEEAEEAREEVAELNSKLAELKERIESL-----ERIRTLLAAIADAEDEIERLREKREALAELNDER----R 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 783 DTLEKEKRKIQDLENRLTKQKEEiELKEQKENvlnnkLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKM 862
Cdd:PRK02224 627 ERLAEKRERKRELEAEFDEARIE-EAREDKER-----AEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERR 700
|
570 580
....*....|....*....|..
gi 568931432 863 iltdDRLKLQQQSMKALQDERE 884
Cdd:PRK02224 701 ----EALENRVEALEALYDEAE 718
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
17-85 |
1.45e-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: 56.18 E-value: 1.45e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568931432 17 STTIGKHADSDLVLQSADIDNHHALIEFneAEGTFVLQDFNSRNGTFVNECHIQnvAVKLIPGDILRFG 85
Cdd:cd22694 17 SVRIGRDPDADVRLDDPRVSRRHALLEF--DGDGWVYTDLGSRNGTYLNGRRVQ--QVKLSDGTRVRLG 81
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
638-1335 |
1.59e-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: 62.68 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 638 EHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKA 717
Cdd:pfam02463 286 EELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQ 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 718 QARVRELENHLASQKEALENSVAQEKRKMREMLEAER-RKAQDLENQLTQQKEISENNtyEKLKMRDTLEKEKRKIQDLE 796
Cdd:pfam02463 366 EKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEeEKEAQLLLELARQLEDLLKE--EKKEELEILEEEEESIELKQ 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 797 NRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELET--------TKTKMILTDDR 868
Cdd:pfam02463 444 GKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKarsglkvlLALIKDGVGGR 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 869 LKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLT 948
Cdd:pfam02463 524 IISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPIL 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 949 AGPPLDSGDKEIACDH-------LIDDLLMAQKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQkMELERQVALVRQ 1021
Cdd:pfam02463 604 NLAQLDKATLEADEDDkrakvveGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSE-LTKELLEIQELQ 682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1022 QSGELSMLKAKVAQTTGLMEKKD----RELKVLREALRASQEKPRPHLSTEQKPRTLSQKCDISLQIEPAHPDSFSSFQE 1097
Cdd:pfam02463 683 EKAESELAKEEILRRQLEIKKKEqrekEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEK 762
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1098 EQSFSDLGVKCKGSRHEETIQRQRKALSELRTRVRELEK-----ANSCNHKDHVNESFLELRTLRMEKNVQKILLDAKPD 1172
Cdd:pfam02463 763 EEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEelralEEELKEEAELLEEEQLLIEQEEKIKEEELEELALEL 842
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1173 LTTLARVEIRPpQNSPFNSGSTLVMEKSVKTDAGEALELSEKLYTDMIKTLGSLMNIKDMSSHTSLKHLSPKEREKVNHL 1252
Cdd:pfam02463 843 KEEQKLEKLAE-EELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEE 921
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1253 RQKDLDLVFDKITQLKTRLQRKEELLKGYEQE-LEQLRHSKVSVQMYQTQVAKLEDDVHKEAEEKALLKEALERTEQQLS 1331
Cdd:pfam02463 922 RIKEEAEILLKYEEEPEELLLEEADEKEKEENnKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLE 1001
|
....
gi 568931432 1332 QERR 1335
Cdd:pfam02463 1002 EEKK 1005
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
638-997 |
1.99e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.47 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 638 EHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQ--EEKLKAK-IQQLTEEKAALEESI--GQEKSRSEE 712
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKkaEEAKKAEeAKKKAEEAKKADEAKkkAEEAKKADE 1487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 713 ALEKAQ---ARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEK-- 787
Cdd:PTZ00121 1488 AKKKAEeakKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKae 1567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 788 EKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVE------------DAQQMKTTESQRAETLALKLKETLAEL 855
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKaeeakkaeeakiKAEELKKAEEEKKKVEQLKKKEAEEKK 1647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 856 ETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYK-EQIKQHSQTIVSLEERLCQVTQYYQKIEG-----EI 929
Cdd:PTZ00121 1648 KAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAaEALKKEAEEAKKAEELKKKEAEEKKKAEElkkaeEE 1727
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568931432 930 TTLKNNDTGPKEEASQDLTAGPPLDSGDKEiACDHLIDDLLMAQKEILSQQEIIMKLRTDLGEAHSRM 997
Cdd:PTZ00121 1728 NKIKAEEAKKEAEEDKKKAEEAKKDEEEKK-KIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRM 1794
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
604-1059 |
3.29e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 3.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 604 SLSWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQDLQAQMNASRETQKsLRQEHLAEKEKLAEKLEQEE 683
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKK-KLKELEKRLEELEERHELYE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 684 KLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREmLEAERRKAQDLENQ 763
Cdd:PRK03918 366 EAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE-LKKAKGKCPVCGRE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 764 LTQQKEISENNTYeKLKMRDtLEKEKRKIQDLENRLTKQKEEIELKEQKENVLnnklkdaLVMVEDAQQMKTTESQRAET 843
Cdd:PRK03918 445 LTEEHRKELLEEY-TAELKR-IEKELKEIEEKERKLRKELRELEKVLKKESEL-------IKLKELAEQLKELEEKLKKY 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 844 LALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQD------ERESQKHGFEEEISEYKEQIKQHS-QTIVSLEERLC 916
Cdd:PRK03918 516 NLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkklaELEKKLDELEEELAELLKELEELGfESVEELEERLK 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 917 QVTQYYQkiegEITTLKNndtGPKEeasqdltagppLDSGDKEIacDHLIDDLLMAQKEILSQQEIIMKLRTDLGEAHSR 996
Cdd:PRK03918 596 ELEPFYN----EYLELKD---AEKE-----------LEREEKEL--KKLEEELDKAFEELAETEKRLEELRKELEELEKK 655
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 997 MSDLRGELSEKQKMELERQVALVRQQSGELSMLKAKVAQT-------TGLMEKKDRELKVLREALRASQE 1059
Cdd:PRK03918 656 YSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTleklkeeLEEREKAKKELEKLEKALERVEE 725
|
|
| FHA_Ki67 |
cd22673 |
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ... |
11-92 |
4.79e-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: 54.91 E-value: 4.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 11 FFVLNKSTTIGKHADSDLVLQSADIDNHHALIEFNEaEGTFVLQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGMT 90
Cdd:cd22673 16 FPLTKKSCTFGRDLSCDIRIQLPGVSREHCRIEVDE-NGKAYLENLSTTNPTLVNGKAIEK-SAELKDGDVITIGGRSFR 93
|
..
gi 568931432 91 YE 92
Cdd:cd22673 94 FE 95
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
219-905 |
7.50e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 7.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 219 EIILLLGREVNRLSDFEMESKYKDALIMNLQAEVADLSQRLSETAAVAaarqsnrcdPKLQGVDEGDDLRQKEIESMKSQ 298
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSEL---------PELREELEKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 299 INALQKgysqvlsqtlaerntEIESLKNEGENLKRDhaitsgmVTSLQKDMSARNEQVQQLQEEVNRLR-IENREKEYql 377
Cdd:PRK03918 240 IEELEK---------------ELESLEGSKRKLEEK-------IRELEERIEELKKEIEELEEKVKELKeLKEKAEEY-- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 378 EALSSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKknymgqniisKTLREKNKVEEKLQ--E 455
Cdd:PRK03918 296 IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK----------ELEKRLEELEERHElyE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 456 DSRRKLLQLQEMgnRENLIKINLERAVGQLENFRNqvikatfgktkpfRDKPITDQqlIEKIIqvtednlsfqqrkwtlQ 535
Cdd:PRK03918 366 EAKAKKEELERL--KKRLTGLTPEKLEKELEELEK-------------AKEEIEEE--ISKIT----------------A 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 536 RETHLHPKQEETMHSVEKLRVLLDKCQACMRDscssIDLKKEVELLQHLPLSplvsglqktvvniLRVSLSWLEETEQLL 615
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKKAKGKCPVCGRE----LTEEHRKELLEEYTAE-------------LKRIEKELKEIEEKE 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 616 GDLDIELSDSDKgfslcliyLLEHYKKIMSQsQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQE-EKLKAKIQQLTE 694
Cdd:PRK03918 476 RKLRKELRELEK--------VLKKESELIKL-KELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKlIKLKGEIKSLKK 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 695 EKAALEESigqeKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERR--KAQDLENQLTQQKEise 772
Cdd:PRK03918 547 ELEKLEEL----KKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEylELKDAEKELEREEK--- 619
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 773 nntyEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLN-NKLKDALVMVEDAQQMKTTESQRAETLALKLKET 851
Cdd:PRK03918 620 ----ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKT 695
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 568931432 852 LAELETTKTKMILTDDRLKLQQQSMKALQDEResqkhgfeEEISEYKEQIKQHS 905
Cdd:PRK03918 696 LEKLKEELEEREKAKKELEKLEKALERVEELR--------EKVKKYKALLKERA 741
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
19-181 |
1.20e-08 |
|
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal transduction mechanisms, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442679 [Multi-domain] Cd Length: 402 Bit Score: 59.00 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 19 TIGKHADSDLVLQSAD--IDNHHALIEFneAEGTFVLQDfNSRNGTFVNECHI---QNVAVKLIPGDILRFGSagmtYEL 93
Cdd:COG3456 29 TIGRSADCDWVLPDPDrsVSRRHAEIRF--RDGAFCLTD-LSTNGTFLNGSDHplgPGRPVRLRDGDRLRIGD----YEI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 94 ---VIENPSPVSCPWVRGPAPWPSPQPHLS--SSPPDMPFHHGIQPATVQRSWSQGCPRPTMVPPAPHQRPMSASGKMFS 168
Cdd:COG3456 102 rveISGEDEGADDPLAAAPEPAVSSPSNLSdtEAAPDAALAFSFSLDPLEALDEAATEAPATADDPPSLLPEDWLPSAAP 181
|
170
....*....|...
gi 568931432 169 FVMDPKSPVINQV 181
Cdd:COG3456 182 VADEAAAQAIDQL 194
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
645-806 |
2.04e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.31 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 645 SQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQ---EKSRSEEALEKAQARV 721
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEleaQLRELERKIEELEAQI 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 722 RELENHLASQKEALENSVAQEK----------------------RKMREMLEAERRKAQDLENQLTQQKEISENNTYEKL 779
Cdd:TIGR02169 913 EKKRKRLSELKAKLEALEEELSeiedpkgedeeipeeelsledvQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELK 992
|
170 180
....*....|....*....|....*..
gi 568931432 780 KMRDTLEKEKRKIQDLENRLTKQKEEI 806
Cdd:TIGR02169 993 EKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
599-1033 |
2.06e-08 |
|
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: 58.88 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 599 NILRVSLSWLEETEQLLGDLDIELSDSDKGFSLcliyLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEK 678
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKSLESQISELKKQNNQ----LKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 679 LEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKaqarvrELENHLASQKEALENSVAQekrkmremLEAERRKAQ 758
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNK------ELKSELKNQEKKLEEIQNQ--------ISQNNKIIS 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 759 DLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLEN----------RLTKQKEEIELKEQKENVLNNKLKDALVMVE 828
Cdd:TIGR04523 339 QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKenqsykqeikNLESQINDLESKIQNQEKLNQQKDEQIKKLQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 829 DAQQMKTTESQRAETLALKLKETLAELETTKTKMILT----DDRLKLQQQSMKALQDERESQKHGFEE----------EI 894
Cdd:TIGR04523 419 QEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIiknlDNTRESLETQLKVLSRSINKIKQNLEQkqkelkskekEL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 895 SEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAgppLDSGDKEIACDHL---IDDLLM 971
Cdd:TIGR04523 499 KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFE---LKKENLEKEIDEKnkeIEELKQ 575
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568931432 972 AQKEILSQQEiimKLRTDLGEAHSRMSDLRGELSEK--QKMELERQVALVRQQSGELSMLKAKV 1033
Cdd:TIGR04523 576 TQKSLKKKQE---EKQELIDQKEKEKKDLIKEIEEKekKISSLEKELEKAKKENEKLSSIIKNI 636
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
670-1022 |
2.28e-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: 58.93 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 670 AEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEkAQARVRELENHLasqkealensVAQEKRKMREM 749
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQA-LLKEKREYEGYE----------LLKEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 750 LEAERRKAQDLENQLTQ-QKEISENNTyEKLKMRDTLEKEKRKIQDL-ENRLTKQKEEIELKEQKENVLNNKLKDALVMV 827
Cdd:TIGR02169 239 KEAIERQLASLEEELEKlTEEISELEK-RLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 828 EDAQ-QMKTTESQRAETLAlKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEE---EISEYKEQIKQ 903
Cdd:TIGR02169 318 EDAEeRLAKLEAEIDKLLA-EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAEtrdELKDYREKLEK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 904 HSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQdltagppldsgdkeiacdhLIDDLLMAQKEILSQQEII 983
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE-------------------LEEEKEDKALEIKKQEWKL 457
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 568931432 984 MKLRTDLGEAHSRMSDLRGELS--EKQKMELERQVALVRQQ 1022
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDrvEKELSKLQRELAEAEAQ 498
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
645-856 |
2.64e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.85 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 645 SQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIgqekSRSEEALEKAQARVREL 724
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL----AALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 725 ENHLASQKEALENSVA---QEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTK 801
Cdd:COG4942 96 RAELEAQKEELAELLRalyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568931432 802 QKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETL---ALKLKETLAELE 856
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELqqeAEELEALIARLE 233
|
|
| FHA_GarA_OdhI-like |
cd22684 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium ... |
18-91 |
2.86e-08 |
|
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: 52.77 E-value: 2.86e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568931432 18 TTIGKHADSDLVLQSADIDNHHAliEFNEAEGTFVLQDFNSRNGTFVNECHIQnvAVKLIPGDILRFGSAGMTY 91
Cdd:cd22684 23 TTAGRHPESDIFLDDVTVSRRHA--EFRRAEGGFVVRDVGSLNGTYVNRERID--SAVLRNGDEVQIGKFRLVF 92
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
366-1026 |
4.38e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 4.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 366 LRIENREKEYQ-----LEALSSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKnymgqniIS 440
Cdd:PRK03918 155 LGLDDYENAYKnlgevIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEK-------LE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 441 KTLREKNKVEEKLQEDSRRKLLQLQEMGNRENLIKinleravgQLENFRNQVIKATfgktkpfrdkpitdQQLIEKIIQV 520
Cdd:PRK03918 228 KEVKELEELKEEIEELEKELESLEGSKRKLEEKIR--------ELEERIEELKKEI--------------EELEEKVKEL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 521 TEdnlsfqqrkwtlqrethLHPKQEETMHSVEKLRVLLDKCQacmrdscssiDLKKEVEllqhlPLSPLVSGLQKtvvni 600
Cdd:PRK03918 286 KE-----------------LKEKAEEYIKLSEFYEEYLDELR----------EIEKRLS-----RLEEEINGIEE----- 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 601 lrvSLSWLEETEQLLGDLDIELSDSDKGFSlcliyLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKle 680
Cdd:PRK03918 329 ---RIKELEEKEERLEELKKKLKELEKRLE-----ELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEK-- 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 681 QEEKLKAKIQQLTEEKAALEESIGQEKSRSEEaLEKAQARV----RELENH-----LASQKEALENsVAQEKRKMREMLE 751
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKELKKAIEE-LKKAKGKCpvcgRELTEEhrkelLEEYTAELKR-IEKELKEIEEKER 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 752 AERRKAQDLENQLTQQKEISEN--------NTYEKLKMRDT--LEKEKRKIQDLENRLTKQKEEIE-LKE--QKENVLNN 818
Cdd:PRK03918 477 KLRKELRELEKVLKKESELIKLkelaeqlkELEEKLKKYNLeeLEKKAEEYEKLKEKLIKLKGEIKsLKKelEKLEELKK 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 819 KLKDALVMVEDAQQMKTTESQRAETLALK----LKETLAELETTKTKMIltddRLKLQQQSMKALQDERESQkhgfEEEI 894
Cdd:PRK03918 557 KLAELEKKLDELEEELAELLKELEELGFEsveeLEERLKELEPFYNEYL----ELKDAEKELEREEKELKKL----EEEL 628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 895 SEYKEQIKQHSQTIVSLEERLCQVTQYY-----QKIEGEITTLKNNDTGPKEEASQdltagppLDSGDKEIACDhlIDDL 969
Cdd:PRK03918 629 DKAFEELAETEKRLEELRKELEELEKKYseeeyEELREEYLELSRELAGLRAELEE-------LEKRREEIKKT--LEKL 699
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 568931432 970 LMAQKEILSQQEIIMKlrtdLGEAHSRMSDLRGELSEKQKMELERQVALVRQQSGEL 1026
Cdd:PRK03918 700 KEELEEREKAKKELEK----LEKALERVEELREKVKKYKALLKERALSKVGEIASEI 752
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
653-1403 |
4.45e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 653 QMNASRETQKSLRQEHLAEKEKLAE--KLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLAS 730
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTEtgKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 731 QKEALENSVAQEKRKMREMLEAER-RKAQDLEnQLTQQKEISENNTYEKLKMRDTLEK--EKRKIQDLEnRLTKQKEEIE 807
Cdd:PTZ00121 1163 ARKAEEARKAEDAKKAEAARKAEEvRKAEELR-KAEDARKAEAARKAEEERKAEEARKaeDAKKAEAVK-KAEEAKKDAE 1240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 808 LKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAEtlalklkETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQK 887
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE-------EARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE 1313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 888 HGFEEEISEYKEQIKQHSQTIVSLEERlcqvtqyyQKIEGEITTLKNNDTGPKEEASQDLTAGPPLDSGDKEIACDHLid 967
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAAKKKAEE--------AKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA-- 1383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 968 dllmaqKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQKMELERQVALVRQQSGELSMlKAKVAQTTGLMEKKDREL 1047
Cdd:PTZ00121 1384 ------KKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK-KAEEAKKADEAKKKAEEA 1456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1048 KVLREALRASQEKPRP-HLSTEQKPRTLSQKCDISLQIEPAHPDSFSSFQEEQSFSDLGVKCKGSRHEETIQRqrkalSE 1126
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKAdEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK-----AE 1531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1127 LRTRVRELEKANSCNHKDHVNESfLELRTLRMEKNVQKilldakpdlttlarveirppqnspfnsgstlvmEKSVKTDAG 1206
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKADELKKA-EELKKAEEKKKAEE---------------------------------AKKAEEDKN 1577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1207 EALELSEKLYTDMIKTLGSLMNIKDMSSHTSLKHLSPKEREKVNHLRQKDLDLVFDKITQLKTRlqRKEELLKGyeqelE 1286
Cdd:PTZ00121 1578 MALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK--EAEEKKKA-----E 1650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1287 QLRHSKVSVQMYQTQVAKLEDDVHKEAEEKALLKEALERTEQQLSQE----RRFNRVFKQQKDRGEDPEQRNMSYSPFKD 1362
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEaeeaKKAEELKKKEAEEKKKAEELKKAEEENKI 1730
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 568931432 1363 NEKQRRLFVEMVKSKMQNSSVQAGAKKATLKTGQERETKKE 1403
Cdd:PTZ00121 1731 KAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
|
| FHA_Cep170A |
cd22724 |
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar ... |
25-85 |
5.06e-08 |
|
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar proteins; Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438776 [Multi-domain] Cd Length: 106 Bit Score: 52.28 E-value: 5.06e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568931432 25 DSDLVLQSADIDNHHALIEFNEAEGTFVLQDFNSRNGTFVNECHI-QNVAVKLIPGDILRFG 85
Cdd:cd22724 29 DCELMLQSRSVDKQHAVINYDASTDEHKVKDLGSLNGTFVNDVRIpEQTYITLKLDDKLRFG 90
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
669-933 |
5.45e-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: 57.77 E-value: 5.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 669 LAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESI-GQEKSRSEEALEKAQARVRELENHLASQKEALENsVAQEKRKMR 747
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAERYQALLKEKREYEGYElLKEKEALERQKEAIERQLASLEEELEKLTEEISE-LEKRLEEIE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 748 EMLEAERRKAQDL--ENQLTQQKEISENnTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIE-LKEQKENVLN-----NK 819
Cdd:TIGR02169 272 QLLEELNKKIKDLgeEEQLRVKEKIGEL-EAEIASLERSIAEKERELEDAEERLAKLEAEIDkLLAEIEELEReieeeRK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 820 LKDALV-MVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMiltdDRLKLQQQSMKALQDERESQKHGFEEEISEYK 898
Cdd:TIGR02169 351 RRDKLTeEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL----EKLKREINELKRELDRLQEELQRLSEELADLN 426
|
250 260 270
....*....|....*....|....*....|....*
gi 568931432 899 EQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLK 933
Cdd:TIGR02169 427 AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
656-886 |
6.36e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 6.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 656 ASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIgqekSRSEEALEKAQARVRELENHLAS---QK 732
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI----AALARRIRALEQELAALEAELAElekEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 733 EALENSVAQEKRKMREMLeaerRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQK 812
Cdd:COG4942 93 AELRAELEAQKEELAELL----RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568931432 813 ENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQ 886
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
608-900 |
9.29e-08 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 56.23 E-value: 9.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 608 LEETEQLLGDLDIELSDSDKGFSLCLIYLLEHykkiMSQSQDLQAQMNASRETQKSLRQE--HLAEKEKLAEKLEQE--- 682
Cdd:pfam19220 85 LEELVARLAKLEAALREAEAAKEELRIELRDK----TAQAEALERQLAAETEQNRALEEEnkALREEAQAAEKALQRaeg 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 683 ------------EKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQ--------- 741
Cdd:pfam19220 161 elatarerlallEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQleeaveahr 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 742 -EKRKMREMLEAERRKAQDLENQLTQQkeisenntyeklkmRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKL 820
Cdd:pfam19220 241 aERASLRMKLEALTARAAATEQLLAEA--------------RNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 821 KDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRlklqqqsMKALQDERESQKHGFEEEISEYKEQ 900
Cdd:pfam19220 307 ERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDR-------IAELTKRFEVERAALEQANRRLKEE 379
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
18-65 |
9.31e-08 |
|
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.
Pssm-ID: 214578 [Multi-domain] Cd Length: 52 Bit Score: 49.87 E-value: 9.31e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568931432 18 TTIGKH-ADSDLVLQSADIDNHHALIEFNEaEGTFVLQDFNSRNGTFVN 65
Cdd:smart00240 1 VTIGRSsEDCDIQLDGPSISRRHAVIVYDG-GGRFYLIDLGSTNGTFVN 48
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
637-912 |
9.51e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 56.67 E-value: 9.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 637 LEHYKKIMSQSQDLQAQMNasRETQKSLRQEHLA-EKEKLAEKLEQEEKlKAKIQQLTEEKAALE--------------- 700
Cdd:pfam17380 312 VERRRKLEEAEKARQAEMD--RQAAIYAEQERMAmERERELERIRQEER-KRELERIRQEEIAMEisrmrelerlqmerq 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 701 ---ESIGQE-------KSRSEEALEKAQARVRELENHLASQKEALENSVAQ-EKRKMREMleaERRKAQDLENQltQQKE 769
Cdd:pfam17380 389 qknERVRQEleaarkvKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRlEEERAREM---ERVRLEEQERQ--QQVE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 770 ISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEiELKEQKENVLNNKLKDALV--MVEDAQQMKTTESQRAETlalk 847
Cdd:pfam17380 464 RLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK-ELEERKQAMIEEERKRKLLekEMEERQKAIYEEERRREA---- 538
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568931432 848 lketlaelETTKTKMILTDDRLKLQQQSMKAlqDERESQKHGFEEEiSEYKEQIKQHSQTIVSLE 912
Cdd:pfam17380 539 --------EEERRKQQEMEERRRIQEQMRKA--TEERSRLEAMERE-REMMRQIVESEKARAEYE 592
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
662-1154 |
9.57e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 9.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 662 KSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQ---EKSRSEEALEKAQARVRELENH------LASQK 732
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEissELPELREELEKLEKEVKELEELkeeieeLEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 733 EALENSVAQEKRKMRE---MLEAERRKAQDLENQLTQQKEISEN-NTYEKL-KMRDTLEKEKRKIQDLENRLTKQKEEIE 807
Cdd:PRK03918 248 ESLEGSKRKLEEKIREleeRIEELKKEIEELEEKVKELKELKEKaEEYIKLsEFYEEYLDELREIEKRLSRLEEEINGIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 808 LKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLAlKLKETLAELETTKTKM-ILTDDRLKLQQQSMKALQDERESQ 886
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLtGLTPEKLEKELEELEKAKEEIEEE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 887 KHGFEEEISEYKEQIKQHSQTIVSLE--ERLCQV-----------------TQYYQKIEGEITTLKNNDTGPKEEASQdl 947
Cdd:PRK03918 407 ISKITARIGELKKEIKELKKAIEELKkaKGKCPVcgrelteehrkelleeyTAELKRIEKELKEIEEKERKLRKELRE-- 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 948 tagppldsgdkeiacdhlIDDLLMAQKEILSQQEIIMKLRtdlgEAHSRMSDLRGELSEKQKMELERQVALVRQQSGELS 1027
Cdd:PRK03918 485 ------------------LEKVLKKESELIKLKELAEQLK----ELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1028 MLKAKVAQTTGLMEKKDRELKVLREAlrasqEKPRPHLSTEQKPRTLSQKCDISLQI---EPAHPDSFSSFQEEQSFSDL 1104
Cdd:PRK03918 543 SLKKELEKLEELKKKLAELEKKLDEL-----EEELAELLKELEELGFESVEELEERLkelEPFYNEYLELKDAEKELERE 617
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 568931432 1105 GVKCKGSRHE-----ETIQRQRKALSELRTRVRELEKANSCNHKDHVNESFLELR 1154
Cdd:PRK03918 618 EKELKKLEEEldkafEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELS 672
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
638-1256 |
1.10e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 638 EHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQ-EEKLKAKIQQLTEEKAALEES--IGQEKSRSEEAL 714
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAaEEKAEAAEKKKEEAKKKADAAkkKAEEKKKADEAK 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 715 EKAQ---ARVRELENHLASQKEALE-NSVAQEKRKMREMleaeRRKAQDLENQLTQQKEISENNTYEKLKMRdtlEKEKR 790
Cdd:PTZ00121 1398 KKAEedkKKADELKKAAAAKKKADEaKKKAEEKKKADEA----KKKAEEAKKADEAKKKAEEAKKAEEAKKK---AEEAK 1470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 791 KIQDLENRLTKQKEEIELKEQKENVLN--NKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDR 868
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADEAKKKAEEAKKkaDEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADE 1550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 869 LKLQQQSMKALQDERESQKHGFEEEiseyKEQIKQHSQTIVSLEERlcqvtqyyqKIEGEITTLKNNDTGPKEEASQDLT 948
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEED----KNMALRKAEEAKKAEEA---------RIEEVMKLYEEEKKMKAEEAKKAEE 1617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 949 AGPPLDSGDKEIACDHLIDDLLMAQKEILSQQEiimKLRTDLGEAHSRMSDL-RGELSEKQKMELERQVALVRQQSGELS 1027
Cdd:PTZ00121 1618 AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE---ELKKAEEENKIKAAEEaKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1028 MLKAKVAQTTGLMEKKDRELKVLREALRASQEKPRPHLSTEQKPRTLSQKCDISLQIEPAHPDSFSSF-QEEQSFSDLGV 1106
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLkKEEEKKAEEIR 1774
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1107 KCKGSRHEETIQRQRKALSELRTRVRELEKANSCNHKDHVNESFLELRTLR-MEKNVQKILLDAKpdltTLARVEIRPPQ 1185
Cdd:PTZ00121 1775 KEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKeMEDSAIKEVADSK----NMQLEEADAFE 1850
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568931432 1186 NSPFNSGSTLVMEKSVKTDAGEALELSEK-----LYTDMIKTLgslmNIKDMSSHTSLKHLSPKEREKVNHLRQKD 1256
Cdd:PTZ00121 1851 KHKFNKNNENGEDGNKEADFNKEKDLKEDdeeeiEEADEIEKI----DKDDIEREIPNNNMAGKNNDIIDDKLDKD 1922
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
406-945 |
1.10e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.57 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 406 KELKLCRSQMQDMEKEVRKLREELKKNYMGQNIISKTLREKNKVEEKLQEDSRRKLLQLQEMGNRENLIKINLERAVGQL 485
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 486 ENFRNQVIKATFG----KTKPFRDKPITDQ--QLIEKIIQVTEDNLSFQQRKWTLQRETHLHPKQEETMHSVEK--LRVL 557
Cdd:TIGR04523 190 DKIKNKLLKLELLlsnlKKKIQKNKSLESQisELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNkiKKQL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 558 LDKCQACMRDSCSSIDLKKEVELLQhlplSPLVSGLQKTVVNILRVSLSWLEETEQLLGDLDIELSDSDKGFSlcliyll 637
Cdd:TIGR04523 270 SEKQKELEQNNKKIKELEKQLNQLK----SEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIIS------- 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 638 ehykKIMSQSQDLQAQMNASRETQKSLRQEhLAEKEKLAEKLEQE-EKLKAKIQQLTEEKAALEESIGQEKSRSE----- 711
Cdd:TIGR04523 339 ----QLNEQISQLKKELTNSESENSEKQRE-LEEKQNEIEKLKKEnQSYKQEIKNLESQINDLESKIQNQEKLNQqkdeq 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 712 --------EALEKAQARVRELENHLASQKEALENSVAQEKRKMREM---LEAERRKAQDLENQLTQQKEISENNTYEKLK 780
Cdd:TIGR04523 414 ikklqqekELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLdntRESLETQLKVLSRSINKIKQNLEQKQKELKS 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 781 MRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKdalvmvEDAQQMKTTESqraETLALKLKETLAELETTKT 860
Cdd:TIGR04523 494 KEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKK------EKESKISDLED---ELNKDDFELKKENLEKEID 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 861 KMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPK 940
Cdd:TIGR04523 565 EKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLK 644
|
....*
gi 568931432 941 EEASQ 945
Cdd:TIGR04523 645 QEVKQ 649
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
310-1140 |
1.65e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 56.28 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 310 LSQTLAERNTEIESLKnegenlkrdhaitsGMVTSLQKDMSARNEQVQQ-----LQEEVNRLRIENREKEYQLEALSSRC 384
Cdd:pfam15921 222 ISKILRELDTEISYLK--------------GRIFPVEDQLEALKSESQNkiellLQQHQDRIEQLISEHEVEITGLTEKA 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 385 SVMKEELRKEEAQKDRREAQEK-ELKLCRSQMQDMEKEVRKLREELKKnymgqniisktlrEKNKVEEKLQEDSRRKLLQ 463
Cdd:pfam15921 288 SSARSQANSIQSQLEIIQEQARnQNSMYMRQLSDLESTVSQLRSELRE-------------AKRMYEDKIEELEKQLVLA 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 464 LQEmgnrenlikinLERAVGQLENFRNQVikatfGKTKPFRDKPITDQQLIEKiiqvtEDNLSFQQRKWTLQRET----- 538
Cdd:pfam15921 355 NSE-----------LTEARTERDQFSQES-----GNLDDQLQKLLADLHKREK-----ELSLEKEQNKRLWDRDTgnsit 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 539 --HLHPKQEETMHSVEKLRVLL----DKCQACMRDSCSSIDLKKEvellQHLPLSPLVSGLQKT------VVNILRVSLS 606
Cdd:pfam15921 414 idHLRRELDDRNMEVQRLEALLkamkSECQGQMERQMAAIQGKNE----SLEKVSSLTAQLESTkemlrkVVEELTAKKM 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 607 WLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQDLQaQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLK 686
Cdd:pfam15921 490 TLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQ-HLKNEGDHLRNVQTECEALKLQMAEKDKVIEILR 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 687 AKIQQLTE--------------EKAALEESIGQEKSRSEE---ALEKAQARVRELE---NHLASQKEALENSVAQEKRKM 746
Cdd:pfam15921 569 QQIENMTQlvgqhgrtagamqvEKAQLEKEINDRRLELQEfkiLKDKKDAKIRELEarvSDLELEKVKLVNAGSERLRAV 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 747 REMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIelkEQKENVLnnklkdalvm 826
Cdd:pfam15921 649 KDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSEL---EQTRNTL---------- 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 827 vedaqqmKTTESqrAETLALKLKETLAELETTKTKMIltdDRLKLQQQSMKALQDERESQKHGFEEEISEykeqikqhsq 906
Cdd:pfam15921 716 -------KSMEG--SDGHAMKVAMGMQKQITAKRGQI---DALQSKIQFLEEAMTNANKEKHFLKEEKNK---------- 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 907 tivsLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAgppLDSGDKEIA-CDHLIddllmaQKEilSQQEIIMK 985
Cdd:pfam15921 774 ----LSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVA---LDKASLQFAeCQDII------QRQ--EQESVRLK 838
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 986 LRTDL------GEAHSRMSDLRGELseKQKMELERQVALVRQQSGELSMLKAKVAQTTGLMEKKDRELKVLREALRAS-Q 1058
Cdd:pfam15921 839 LQHTLdvkelqGPGYTSNSSMKPRL--LQPASFTRTHSNVPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQELRSViN 916
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1059 EKPRPHLS-TEQKPRTLS--------QKCDISLQIEPAHPDSFSSFqeeqsfsdlgVKCKGSRHEETIQRQRKALselrt 1129
Cdd:pfam15921 917 EEPTVQLSkAEDKGRAPSlgalddrvRDCIIESSLRSDICHSSSNS----------LQTEGSKSSETCSREPVLL----- 981
|
890
....*....|.
gi 568931432 1130 RVRELEKANSC 1140
Cdd:pfam15921 982 HAGELEDPSSC 992
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
641-838 |
1.68e-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: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 641 KKIMSQSQDLQAQMNASRETQKSLRQ--EHLAEKEKLAEKLEQE-EKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKA 717
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAAleRRIAALARRIRALEQElAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 718 QARVR-ELENHLASQKEALE--------NSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKE 788
Cdd:COG4942 114 YRLGRqPPLALLLSPEDFLDavrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568931432 789 K----RKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTES 838
Cdd:COG4942 194 KaerqKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
645-1377 |
1.99e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 55.75 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 645 SQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEklkakiqqltEEKAALEESIGQEKSRSEEALEKAQARV--R 722
Cdd:pfam02463 237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENK----------EEEKEKKLQEEELKLLAKEEEELKSELLklE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 723 ELENHLASQKEALENSVAQEKRKmremLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKiqdLENRLTKQ 802
Cdd:pfam02463 307 RRKVDDEEKLKESEKEKKKAEKE----LKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQL---EEELLAKK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 803 KEEIELKEQKENVLNNKLKDALVMvEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDE 882
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEE-EKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQEL 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 883 RESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQvtqyyQKIEGEITTLKNNDTGPKEEASQDLTAGPPLDSGDKEIAC 962
Cdd:pfam02463 459 KLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQ-----KLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGD 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 963 DHLIDDLLMAQKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQKMELERQVALVRQQSGELSmlkakVAQTTGLMEK 1042
Cdd:pfam02463 534 LGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLE-----IDPILNLAQL 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1043 KDRELKVLREALRAsqekprphlsteqKPRTLSQKCDISLQIEPAHPDSFSSFQEEQSFSDLGVKCKGSRHEETIQRQRK 1122
Cdd:pfam02463 609 DKATLEADEDDKRA-------------KVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKEL 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1123 ALSELRTRVRELEKANSCNHKDHVNESFLELRTLRMEKNVQKILLDAKPDLTTLARVEIrPPQNSPFNSGSTLVMEKSVK 1202
Cdd:pfam02463 676 LEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKI-NEELKLLKQKIDEEEEEEEK 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1203 T--DAGEALELSEKLYTDMIKTLGSLMNIKDMSSHTSLKHLSPKEREKVNHLRQKDLdlvfDKITQLKTRLQRKEELLKG 1280
Cdd:pfam02463 755 SrlKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELK----EEAELLEEEQLLIEQEEKI 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1281 YEQELEQLRHSKVSVQMYQTQVAKLEDDVHKEAEEKALLKEALERTEQQLSQERRFNRVFKQQKDRGEDPEQRNMSYSPF 1360
Cdd:pfam02463 831 KEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLN 910
|
730
....*....|....*..
gi 568931432 1361 KDNEKQRRLFVEMVKSK 1377
Cdd:pfam02463 911 LLEEKENEIEERIKEEA 927
|
|
| FHA_Cep170B |
cd22725 |
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) ... |
25-93 |
2.08e-07 |
|
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: 50.70 E-value: 2.08e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568931432 25 DSDLVLQSADIDNHHALIEFNEAEGTFVLQDFNSRNGTFVNECHIQN---VAVKLipGDILRFGSAGMTYEL 93
Cdd:cd22725 29 DCELMLQSRSVDKQHAVINYDQDTDEHWVKDLGSLNGTFVNDVRIPDqkyITLKL--NDVIRFGYDSNMYVL 98
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
19-85 |
2.55e-07 |
|
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also called human lung cancer oncogene 3 protein (HLC-3), kidney anion exchanger adapter protein, or solute carrier family 4 anion exchanger member 1 adapter protein (SLC4A1AP), is a nuclear protein widely expressed in mammalian tissues. It was originally isolated as a kidney Cl-/HCO3- anion exchanger 1 (kAE1)-binding protein. It is a highly mobile nucleocytoplasmic shuttling and multilocalizing protein. Its role in mammalian cells remains unclear. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438729 [Multi-domain] Cd Length: 106 Bit Score: 50.25 E-value: 2.55e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568931432 19 TIGKHADSDLVLQSADIDNHHALIEFN----EAEGTFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFG 85
Cdd:cd22677 25 VFGRLPGCDVVLEHPSISRYHAVLQYRgdadDHDGGFYLYDLGSTHGTFLNKQRIPpKQYYRLRVGHVLKFG 96
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
659-1390 |
2.94e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 659 ETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQqltEEKAALEESIGQEKSRSEEALEKAQARvRELENHLASQKEALENS 738
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAEAVKKAEEAKKDAE---EAKKAEEERNNEEIRKFEEARMAHFAR-RQAAIKAEEARKADELK 1284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 739 VAQEKRKMREMLEA-ERRKAQDLENQLTQQKEISEnntyeklkMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLN 817
Cdd:PTZ00121 1285 KAEEKKKADEAKKAeEKKKADEAKKKAEEAKKADE--------AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAA 1356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 818 NKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKtkmiltddrlklqqqsmKALQDERESQKHGFEEEISEY 897
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKK-----------------KAEEDKKKADELKKAAAAKKK 1419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 898 KEQIKQHSQTIVSLEErlcqvtqyyqkiegeiTTLKNNDTGPKEEASQDLTAGPPLDSGDKEIACDHLIDDLLMAQKEIL 977
Cdd:PTZ00121 1420 ADEAKKKAEEKKKADE----------------AKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK 1483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 978 SQQEIIMKLRtdlgEAHSRMSDLRGELSEKQKMELERQVALVRQQSGELSMLKAKVAQTTGLME--KKDRELKVLREALR 1055
Cdd:PTZ00121 1484 KADEAKKKAE----EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEekKKADELKKAEELKK 1559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1056 ASQEKPRPHLSTEQKPRTLS-QKCDISLQIEPAHPDSFSSFQEEQsfsdlgvkcKGSRHEETIQRQRKALSELRTRVREL 1134
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMAlRKAEEAKKAEEARIEEVMKLYEEE---------KKMKAEEAKKAEEAKIKAEELKKAEE 1630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1135 EKANSCNHKDHVNESFLELRTLRMEKNVQKIlldAKPDLTTLARVEIRPPQNSPFNSGSTLVMEKSVKTDAGEALELSEk 1214
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELKKAEEENKI---KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE- 1706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1215 lytdmiktlgslmnikdmsshtsLKHLSPKEREKVNHLRQKDlDLVFDKITQLKtrlqRKEELLKGYEQELEQLRHSKVS 1294
Cdd:PTZ00121 1707 -----------------------LKKKEAEEKKKAEELKKAE-EENKIKAEEAK----KEAEEDKKKAEEAKKDEEEKKK 1758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1295 VQMYQTQVAKLEDDVHKEAEekALLKEALERTEQQLSQErrFNRVFKQQKDRGEDPEQRNMSYSPFKDNEKQrrLFVEMV 1374
Cdd:PTZ00121 1759 IAHLKKEEEKKAEEIRKEKE--AVIEEELDEEDEKRRME--VDKKIKDIFDNFANIIEGGKEGNLVINDSKE--MEDSAI 1832
|
730
....*....|....*.
gi 568931432 1375 KSKMQNSSVQAGAKKA 1390
Cdd:PTZ00121 1833 KEVADSKNMQLEEADA 1848
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
392-760 |
3.15e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 392 RKEEAQKDRREAQEKELKLC------RSQMQDMEKEVRK------LREELKK---NYMGQNI--ISKTLREKNKVEEKLQ 454
Cdd:COG1196 173 RKEEAERKLEATEENLERLEdilgelERQLEPLERQAEKaeryreLKEELKEleaELLLLKLreLEAELEELEAELEELE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 455 EDSRRKLLQLQEMGNRENLIKINLERAVGQLENFRNQVIKATfgktkpfrdkpITDQQLIEKIIQVTEDNLSFQQRKWTL 534
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL-----------AELARLEQDIARLEERRRELEERLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 535 QREthlhpkQEETMHSVEKLRVLLDKCQAcmrdscSSIDLKKEVELLQHlplspLVSGLQKTVVNILRVSLSWLEETEQL 614
Cdd:COG1196 322 EEE------LAELEEELEELEEELEELEE------ELEEAEEELEEAEA-----ELAEAEEALLEAEAELAEAEEELEEL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 615 LGDLDIELSDSDKgfslcliyLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTE 694
Cdd:COG1196 385 AEELLEALRAAAE--------LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568931432 695 EKAALEESIgQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDL 760
Cdd:COG1196 457 EEEALLELL-AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
663-1404 |
3.31e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 55.36 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 663 SLRQEHLAEKEKLAEKLEQE-EKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVREL-------ENHLASQKEA 734
Cdd:pfam02463 162 AAGSRLKRKKKEALKKLIEEtENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEyllyldyLKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 735 LE---NSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQ 811
Cdd:pfam02463 242 LQellRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 812 KENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFE 891
Cdd:pfam02463 322 EKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKS 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 892 EEISEYKEQIkQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAGPPLDSGDKEIACDHLIDDLLM 971
Cdd:pfam02463 402 EEEKEAQLLL-ELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLV 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 972 AQKEILSQQEIIMKLRTDL-GEAHSRMSDLRGELSEKQKMELERQVALVRQQSGELSMLKAKVAQTTGLMEKKDRELKVL 1050
Cdd:pfam02463 481 KLQEQLELLLSRQKLEERSqKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEV 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1051 REALRASQEKP---------RPHLSTEQKPRTLSQKCDISLQIEPAHPDSFSSFQEEQSFSDLGVKCKGSRHEETIQRQR 1121
Cdd:pfam02463 561 EERQKLVRALTelplgarklRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKES 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1122 -KALSELRTRVRELEKANSCNHKDHVNESFLELRTLRMEKNVQKILLDAKPdLTTLARVEIRPPQNSPFNSGSTLVMEKS 1200
Cdd:pfam02463 641 aKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAK-EEILRRQLEIKKKEQREKEELKKLKLEA 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1201 VKTDAGEALELSEKLYTDMIKTLGSLMNIKDMSSHTSLKHLSPKEREKVNHLRQKDLDLVFDKITQLKTRLQRKEELLKG 1280
Cdd:pfam02463 720 EELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQ 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1281 YEQELEQLRHSKVSVQMYQTQVAKLEDDVH-KEAEEKALLKEALERTEQQLSQERRFNRVFKQQKDRGEDPEQRNMSYSP 1359
Cdd:pfam02463 800 EEELRALEEELKEEAELLEEEQLLIEQEEKiKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEEL 879
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 568931432 1360 FKDNEKQRRLFVEMVKSKMQNSSVQAGAKKATLKTGQERETKKEA 1404
Cdd:pfam02463 880 EEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIK 924
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
13-86 |
4.32e-07 |
|
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: 49.67 E-value: 4.32e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568931432 13 VLNKSTTIGKHADSDLVLQSADIDNHHALIEFNEAEGTFVLQDFNSRNGTFVN--ECHIQNVAVKLIPGDILRFGS 86
Cdd:cd22678 20 GTRLPLTIGRIQRGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNgeSISPNGRPVVLSSGDVITLGS 95
|
|
| FHA_MEK1-like |
cd22670 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ... |
15-87 |
4.41e-07 |
|
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: 49.53 E-value: 4.41e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568931432 15 NKSTTIGKHADSDLVLQSADIDNHHALIE---FNEAEGTFV-LQDfNSRNGTFVNECHI-QNVAVKLIPGDILRFGSA 87
Cdd:cd22670 21 NQVITIGRSPSCDIVINDPFVSRTHCRIYsvqFDESSAPLVyVED-LSSNGTYLNGKLIgRNNTVLLSDGDVIEIAHS 97
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
711-865 |
5.67e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 54.01 E-value: 5.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 711 EEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAE----RRKAQDLENQLTQQKEISENNTyeklkmrDTLE 786
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKElrerRNELQKLEKRLLQKEENLDRKL-------ELLE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 787 KEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMV-----EDAQQM---KTTESQRAETLAL-KLKETLAELET 857
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIsgltaEEAKEIlleKVEEEARHEAAVLiKEIEEEAKEEA 186
|
....*....
gi 568931432 858 TKT-KMILT 865
Cdd:PRK12704 187 DKKaKEILA 195
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
356-806 |
6.93e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 6.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 356 VQQLQEEVNRL-RIENREKEYQLEALSSrcsvMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKnYM 434
Cdd:COG4717 48 LERLEKEADELfKPQGRKPELNLKELKE----LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK-LE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 435 GQNIISKTLREKNKVEEKLQEDSRRKLLQLQEMGNRENLIKiNLERAVGQLENFRNQVIKATFGKTKPFRDkpiTDQQLI 514
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEE-ELEELEAELAELQEELEELLEQLSLATEE---ELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 515 EKIIQVTEDNLSFQQRKWTLQRETHLHPKQEETMHSVEKLRVLLDKCQACMRDSCS-SIDLKKEVELLQHLPLSPLVSGL 593
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIaAALLALLGLGGSLLSLILTIAGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 594 QKTVVNILRVSLSWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQDLQAQMNASRETQKSLrQEHLAEKE 673
Cdd:COG4717 279 LFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL-QELLREAE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 674 KLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEAlEKAQARVRELENHLASQ-KEALENSVAQEKRKMREMLEA 752
Cdd:COG4717 358 ELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY-QELKEELEELEEQLEELlGELEELLEALDEEELEEELEE 436
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 568931432 753 ERRKAQDLENQLTQ-QKEISE-NNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEI 806
Cdd:COG4717 437 LEEELEELEEELEElREELAElEAELEQLEEDGELAELLQELEELKAELRELAEEW 492
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
649-823 |
8.13e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 8.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 649 DLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEA---LEKAQARVRELE 725
Cdd:COG3206 209 DLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAeleAELAELSARYTP 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 726 NH-----LASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEisenntyeklkmrdTLEKEKRKIQDLENRLT 800
Cdd:COG3206 289 NHpdviaLRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLA--------------QLEARLAELPELEAELR 354
|
170 180
....*....|....*....|...
gi 568931432 801 KQKEEIELKEQKENVLNNKLKDA 823
Cdd:COG3206 355 RLEREVEVARELYESLLQRLEEA 377
|
|
| FHA_PS1-like |
cd22691 |
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) ... |
19-93 |
8.83e-07 |
|
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) and similar proteins; PS1 is an FHA domain-containing protein required for normal spindle orientation at male meiosis II and normal formation of tetrad of microspores. It is not involved in female meiosis. Mutations in PS1 lead to the production of diploid pollen grains. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438743 [Multi-domain] Cd Length: 113 Bit Score: 48.95 E-value: 8.83e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568931432 19 TIGKHADSDLVLQSADIDNHHALIEFNEAEGTFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFGSAGMTYEL 93
Cdd:cd22691 32 VVGRHPDCDIVLDHPSISRFHLEIRIIPSRRKITLTDLSSVHGTWVNGQRIEpGVPVELEEGDTVRLGASTRVYRL 107
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
650-846 |
1.11e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 650 LQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEEsigqEKSRSEEALEKAQARVRELENHLA 729
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEE----ELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 730 -----SQKEALENSVAQEKRKMREMLEAE------RRKAQDLENQLTQ-QKEISENNTYEKLKMRDTLEKEKRKIQDLEN 797
Cdd:COG4717 127 llplyQELEALEAELAELPERLEELEERLeelrelEEELEELEAELAElQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568931432 798 RLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLAL 846
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIA 255
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
638-1331 |
1.15e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.58 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 638 EHYKKIMS----QSQDLQAQMNASREtqkslrqehLAEKEKLAEKlEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEA 713
Cdd:pfam15921 74 EHIERVLEeyshQVKDLQRRLNESNE---------LHEKQKFYLR-QSVIDLQTKLQEMQMERDAMADIRRRESQSQEDL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 714 LEKAQARVRELENHLASQKEALENSVAQEKrKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTlekekrKIQ 793
Cdd:pfam15921 144 RNQLQNTVHELEAAKCLKEDMLEDSNTQIE-QLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTM------HFR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 794 DLENRLTKQKEEIELKEqkenvlnNKLKDALVMVEDAQQMKTTESQRAETLAL-----KLKETLAELETTKTKMILTDDR 868
Cdd:pfam15921 217 SLGSAISKILRELDTEI-------SYLKGRIFPVEDQLEALKSESQNKIELLLqqhqdRIEQLISEHEVEITGLTEKASS 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 869 LKLQQQSmkaLQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQ----KIEGEITTLKNNDTGPKEEAS 944
Cdd:pfam15921 290 ARSQANS---IQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEdkieELEKQLVLANSELTEARTERD 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 945 QDltagpPLDSGDKEIACDHLIDDLLMAQKEILSQQE--------------IIMKLRTDLGEAH---SRMSDLRGELSEK 1007
Cdd:pfam15921 367 QF-----SQESGNLDDQLQKLLADLHKREKELSLEKEqnkrlwdrdtgnsiTIDHLRRELDDRNmevQRLEALLKAMKSE 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1008 QKMELERQVALVRQQSGEL---SMLKAKVAQTTGLMEKKDRELKVLREALRAS-----------QEKPRPHLSTEQKPRT 1073
Cdd:pfam15921 442 CQGQMERQMAAIQGKNESLekvSSLTAQLESTKEMLRKVVEELTAKKMTLESSertvsdltaslQEKERAIEATNAEITK 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1074 LSQKCDISLQiEPAHPDSfssfqEEQSFSDLGVKCKGSRHEETiqRQRKALSELRTRVRELEKANScNHKDHVNESFLEL 1153
Cdd:pfam15921 522 LRSRVDLKLQ-ELQHLKN-----EGDHLRNVQTECEALKLQMA--EKDKVIEILRQQIENMTQLVG-QHGRTAGAMQVEK 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1154 RTLRMEKNVQKILLDAKPDLTTLARVEIRPPQNSPfnsgSTLVMEKSVKTDAGealelSEKLYT--DMIKTLGSLMNiKD 1231
Cdd:pfam15921 593 AQLEKEINDRRLELQEFKILKDKKDAKIRELEARV----SDLELEKVKLVNAG-----SERLRAvkDIKQERDQLLN-EV 662
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1232 MSSHTSLKHLSPKEREKVNHLRQKDLDLvfdKITQLKTRLQrkeelLKGYEQELEQLRHS------------KVSVQM-- 1297
Cdd:pfam15921 663 KTSRNELNSLSEDYEVLKRNFRNKSEEM---ETTTNKLKMQ-----LKSAQSELEQTRNTlksmegsdghamKVAMGMqk 734
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 568931432 1298 -----------YQTQVAKLEDDVHKEAEEKALLKEALERTEQQLS 1331
Cdd:pfam15921 735 qitakrgqidaLQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELS 779
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
315-899 |
1.18e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 315 AERNTEIESLKNEGENLKR-DHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSRCSVMKEELRK 393
Cdd:PTZ00121 1298 AEEKKKADEAKKKAEEAKKaDEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 394 EEAQKDRREAQEK----ELKLCRSQMQDMEKEVRKLREELKKNYMGQNI---ISKTLREKNKVEEKLQEDSRRKllQLQE 466
Cdd:PTZ00121 1378 KKADAAKKKAEEKkkadEAKKKAEEDKKKADELKKAAAAKKKADEAKKKaeeKKKADEAKKKAEEAKKADEAKK--KAEE 1455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 467 MGNRENLIKINLE-RAVGQLENFRNQVIKATFGKTKPFRDKPITDQ--QLIEKIIQVTEDNLSFQQRKWTLQRETHLHPK 543
Cdd:PTZ00121 1456 AKKAEEAKKKAEEaKKADEAKKKAEEAKKADEAKKKAEEAKKKADEakKAAEAKKKADEAKKAEEAKKADEAKKAEEAKK 1535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 544 QEETMHSVEKLRV-LLDKCQACMR-DSCSSIDLKKEVELLQHLPLSPLVSGLQKTVVNILRVSLSWLEETEQLLGDLDIE 621
Cdd:PTZ00121 1536 ADEAKKAEEKKKAdELKKAEELKKaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 622 LSDSDKGFSLcliYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKlkaKIQQLTEEKAALEE 701
Cdd:PTZ00121 1616 EEAKIKAEEL---KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK---KAEEAKKAEEDEKK 1689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 702 SIGQEKSRSEEALEKAQARVRELENHLASQ---KEALENSVAQEKRKMREmlEAERRKAQDL------ENQLTQQKEISE 772
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEELKKKEAEEKKKAEelkKAEEENKIKAEEAKKEA--EEDKKKAEEAkkdeeeKKKIAHLKKEEE 1767
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 773 NNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVmVEDAQQMKTTESQRAETLALKLKETL 852
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLV-INDSKEMEDSAIKEVADSKNMQLEEA 1846
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 568931432 853 AELEttktKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKE 899
Cdd:PTZ00121 1847 DAFE----KHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADE 1889
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
637-1076 |
1.26e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 637 LEHYKKIMSQSQDLQAQMNASRETQKSLRQ--EHLAEKEKLAEKLEQEEKLKAKIQQ---LTEEKAALEESIGQEKSRSE 711
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEEleEELEELEAELEELREELEKLEKLLQllpLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 712 EaLEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRK 791
Cdd:COG4717 150 E-LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 792 IQDLENRLTKQKEEIELKEQKE----------------NVLNNKLKDA--------LVMVEDAQQMKTTESQRAETLALK 847
Cdd:COG4717 229 LEQLENELEAAALEERLKEARLllliaaallallglggSLLSLILTIAgvlflvlgLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 848 LKETLAELETTKTKMILTDDRLK-----------------LQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSqtIVS 910
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPpdlspeellelldrieeLQELLREAEELEEELQLEELEQEIAALLAEAGVED--EEE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 911 LEERLCQVTQyYQKIEGEITTLKNNdtgpkeeasqdltagppLDSGDKEIACDHLIDDLLMAQKEILSQQEIIMKLRTDL 990
Cdd:COG4717 387 LRAALEQAEE-YQELKEELEELEEQ-----------------LEELLGELEELLEALDEEELEEELEELEEELEELEEEL 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 991 GEAHSRMSDLRGELSEkqkMELERQVALVRQqsgELSMLKAKVAQttglMEKKDRELKVLREALRASQEkprpHLSTEQK 1070
Cdd:COG4717 449 EELREELAELEAELEQ---LEEDGELAELLQ---ELEELKAELRE----LAEEWAALKLALELLEEARE----EYREERL 514
|
....*.
gi 568931432 1071 PRTLSQ 1076
Cdd:COG4717 515 PPVLER 520
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
659-923 |
1.52e-06 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 52.76 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 659 ETQKSLRqehlAEKEKLAEKLEQEEKL-KAKIQQLTEEKAALEEsigqEKsrseealEKAQARVRELENHLASQKEALEN 737
Cdd:pfam15070 4 ESLKQLQ----TERDQYAENLKEEGAVwQQKMQQLSEQVRTLRE----EK-------ERSVSQVQELETSLAELKNQAAV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 738 SVAQEKRKMREMLEAERRKAQDLEnQLTQQKEISENNTYEKLKMRDTL-----EKEKRkIQDLENRLTKQKEEIELKEQk 812
Cdd:pfam15070 69 PPAEEEQPPAGPSEEEQRLQEEAE-QLQKELEALAGQLQAQVQDNEQLsrlnqEQEQR-LLELERAAERWGEQAEDRKQ- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 813 envlnnklkdalvMVEDAQQMKTTESqRAETLALKLKETLAELETTKTKmiLTDDRLKLqqqsMKALQDERESQKH---- 888
Cdd:pfam15070 146 -------------ILEDMQSDRATIS-RALSQNRELKEQLAELQNGFVK--LTNENMEL----TSALQSEQHVKKElakk 205
|
250 260 270
....*....|....*....|....*....|....*..
gi 568931432 889 --GFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQ 923
Cdd:pfam15070 206 lgQLQEELGELKETLELKSQEAQSLQEQRDQYLAHLQ 242
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
321-431 |
1.72e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 52.55 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 321 IESLKNEGENLKRDHAITsgMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSRCSVMKEEL---RKEEAQ 397
Cdd:COG2433 382 LEELIEKELPEEEPEAER--EKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELseaRSEERR 459
|
90 100 110
....*....|....*....|....*....|....*...
gi 568931432 398 KDRREAQ----EKELKLCRSQMQDMEKEVRKLREELKK 431
Cdd:COG2433 460 EIRKDREisrlDREIERLERELEEERERIEELKRKLER 497
|
|
| FHA_NBN |
cd22667 |
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ... |
11-91 |
2.55e-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: 47.71 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 11 FFVLNKSTTIG-KHADsDLVLQSADIDNHHALI-----EFNEAEG----TFVLQDFnSRNGTFVNECHIQNVA-VKLIPG 79
Cdd:cd22667 15 YLLPGGEYTVGrKDCD-IIIVDDSSISRKHATLtvlhpEANLSDPdtrpELTLKDL-SKYGTFVNGEKLKGGSeVTLKDG 92
|
90
....*....|..
gi 568931432 80 DILRFGSAGMTY 91
Cdd:cd22667 93 DVITFGVLGSKF 104
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
637-913 |
3.68e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 51.83 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 637 LEHYKKIMSQSQDLQAQMNA-SRETQKSLRQEHLAEKEKLAEKL--EQEEKLKAKIQQLTEEKAALEESIGQEKS--RSE 711
Cdd:PLN02939 155 LEDLEKILTEKEALQGKINIlEMRLSETDARIKLAAQEKIHVEIleEQLEKLRNELLIRGATEGLCVHSLSKELDvlKEE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 712 EALEKAQARVreLENHLASQKEALENSVAQEKRkmREMLEAERRkaqDLENQL-TQQKEISENNTYEKlkmrDTLEKEKR 790
Cdd:PLN02939 235 NMLLKDDIQF--LKAELIEVAETEERVFKLEKE--RSLLDASLR---ELESKFiVAQEDVSKLSPLQY----DCWWEKVE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 791 KIQDLENRLTKQKEEIELKEQKENVLNNKLKdalvmvedaqqmkttesqraetlalKLKETLAELETTKtkmiLTDDRLK 870
Cdd:PLN02939 304 NLQDLLDRATNQVEKAALVLDQNQDLRDKVD-------------------------KLEASLKEANVSK----FSSYKVE 354
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 568931432 871 LQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEE 913
Cdd:PLN02939 355 LLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKE 397
|
|
| FHA_AGGF1 |
cd22686 |
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ... |
11-86 |
4.26e-06 |
|
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 (AGGF1) and similar proteins; AGGF1, also called angiogenic factor VG5Q, or G patch domain-containing protein 7 (GPATC7), or vasculogenesis gene on 5q protein, is an angiogenic factor involved in vascular development, angiogenesis, specification of hemangioblasts, and differentiation of veins. It promotes angiogenesis and the proliferation of endothelial cells. It inhibits inflammatory effect and preserve vascular integrity in non-nervous system diseases. Mutated AGGF1 causes susceptibility to Klippel-Trenaunay syndrome, a vascular disorder. Increased AGGF1 expression is associated with tumor angiogenesis. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438738 [Multi-domain] Cd Length: 123 Bit Score: 47.28 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 11 FFVLNKSTTIGKHADSDLVLQSAD--IDNHHALIEFNEAEGTFVLQDFNSRNGTFVNECHIQNVAVKLIP-----GDILR 83
Cdd:cd22686 21 FIVTATGATIGREKDHGHTIRIPElgVSKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPyplthGDELK 100
|
...
gi 568931432 84 FGS 86
Cdd:cd22686 101 IGE 103
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
645-812 |
4.26e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 645 SQSQDLQAQMNASRETQKSLRQEhlaekekLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVREL 724
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAE-------LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 725 ENH------------------LASQKEALENSVAQEKRKMREmLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLE 786
Cdd:COG3883 96 YRSggsvsyldvllgsesfsdFLDRLSALSKIADADADLLEE-LKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180
....*....|....*....|....*.
gi 568931432 787 KEKRKIQDLENRLTKQKEEIELKEQK 812
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAE 200
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
643-778 |
5.22e-06 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 51.17 E-value: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 643 IMSQSQDLQAQMNASRETQKSlrQEHLaEKEKLAEKLEQEEKlKAKIQQLTEEKAALE---ESIGQEKSRSEEALEKAQA 719
Cdd:PTZ00491 659 ITTKSQEAAARHQAELLEQEA--RGRL-ERQKMHDKAKAEEQ-RTKLLELQAESAAVEssgQSRAEALAEAEARLIEAEA 734
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568931432 720 RVRELEnhLASQKEALENSVAQEKRKMREMLEAERRKAQDlENQLTQQKEIS--ENNTYEK 778
Cdd:PTZ00491 735 EVEQAE--LRAKALRIEAEAELEKLRKRQELELEYEQAQN-ELEIAKAKELAdiEATKFER 792
|
|
| Yop-YscD_cpl |
pfam16697 |
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ... |
19-86 |
5.37e-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: 46.10 E-value: 5.37e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568931432 19 TIGKHADSDLVLQSADIDNHHALIEFnEAEGtFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRFGS 86
Cdd:pfam16697 20 RIGSDPDCDIVLSDKEVSRVHLKLEV-DDEG-WRLDDLGSGNGTLVNGQRVTELGIALRPGDRIELGQ 85
|
|
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
13-85 |
8.62e-06 |
|
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and similar proteins; SLMAP, also called sarcolemmal-associated protein (SLAP), is a tail-anchored protein involved in fundamental cellular processes, such as myoblast fusion, cell cycle progression, and chromosomal inheritance. It is a cardiac membrane protein that plays an important role in E-C coupling and the adrenergic response of the heart. Overexpression of the SLMAP gene has been associated with diabetes and endothelial dysfunction of macro- and micro-blood vessels. SLMAP contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438731 [Multi-domain] Cd Length: 126 Bit Score: 46.49 E-value: 8.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 13 VLNKSTTIGKH------ADSDLVLQSADIDNHHALIEFNEaeGTFVLQDFNSRNGTFVNECHIQ-----NVAVKLIPGDI 81
Cdd:cd22679 21 VLDEPVKIGRSvararpAANNAIFDCKVLSRNHALLWYDD--GKFYLQDTKSSNGTFVNNQRLSkgseeSEPRELHSGDI 98
|
....
gi 568931432 82 LRFG 85
Cdd:cd22679 99 VQFG 102
|
|
| FHA_SNIP1_DDL-like |
cd22676 |
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA ... |
20-93 |
8.71e-06 |
|
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA domain-containing protein DDL, and similar proteins; SNIP1 is an FHA domain-containing protein required for pre-mRNA splicing as a component of the spliceosome. It inhibits NF-kappaB signaling by competing for its binding to the C/H1 domain of CBP/p300 transcriptional co-activators. It is involved in microRNA (miRNA) biogenesis. SNIP1 is a regulator of the cell cycle and cyclin D1 expression and may be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. This family also includes Arabidopsis thaliana FHA domain-containing protein DDL and similar proteins. DDL, also called protein DAWDLE, is involved in the microRNA (miRNA) and short interfering RNA (siRNA) biogenesis. It may facilitate DCL1 to access or recognize primary miRNAs. DDL binds RNA non-specifically. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438728 [Multi-domain] Cd Length: 111 Bit Score: 46.14 E-value: 8.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 20 IGKHAD-SDLVLQSADIDNHHALIEF----NEAEGTFVLQ------DFNSRNGTFVNECHIQ-NVAVKLIPGDILRFGSA 87
Cdd:cd22676 25 IGRDRRvADIPLDHPSCSKQHAVIQFreveKRNEGDVIENirpyiiDLGSTNGTFLNGEKIEpRRYYELREKDVLKFGLS 104
|
....*.
gi 568931432 88 GMTYEL 93
Cdd:cd22676 105 TREYVL 110
|
|
| FHA_EspA-like |
cd22698 |
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ... |
15-86 |
1.06e-05 |
|
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA is a histidine protein kinase with a fork head-associated (FHA) domain at the N-terminus and a receiver domain at the C-terminus. It functions as an inhibitor of sporulation during early fruiting body development while cells are aggregating into raised mounds. EspA is part of a two-component signal transduction system that regulates the timing of sporulation initiation. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438750 [Multi-domain] Cd Length: 93 Bit Score: 45.48 E-value: 1.06e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568931432 15 NKSTTIGKHADSDLVLQSADIDNHHALIEfnEAEGTFVLQDFNSRNGTFVNECHIQNVAVKliPGDILRFGS 86
Cdd:cd22698 20 QDEFTIGRSSNNDIRLNDHSVSRHHARIV--RQGDKCNLTDLGSTNGTFLNGIRVGTHELK--HGDRIQLGE 87
|
|
| VI_FHA |
TIGR03354 |
type VI secretion system FHA domain protein; Members of this protein family are FHA ... |
19-159 |
1.15e-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: 49.29 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 19 TIGKHADSDLVLQSAD--IDNHHALIEFNEaeGTFVLQDFnSRNGTFVNECH---IQNVAVKLIPGDILRFGSagmtYEL 93
Cdd:TIGR03354 27 TIGRSEDCDWVLPDPErhVSGRHARIRYRD--GAYLLTDL-STNGVFLNGSGsplGRGNPVRLEQGDRLRLGD----YEI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 94 VIENPSP------------VSCPWVRGP-APWPSPQPHL---------SSSPPDMPFhhgiQPATVQRSWSQGCP----- 146
Cdd:TIGR03354 100 RVSLGDPlvsrqasesradTSLPTAGGPpTPDPAPLAQLdplkaldqePLSAADLDD----LSAPLFPPLDARLPafaap 175
|
170 180
....*....|....*....|.
gi 568931432 147 ---RPTMVP-----PAPHQRP 159
Cdd:TIGR03354 176 idaEPTMVPpfvplPAPEPAP 196
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
354-1098 |
1.21e-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: 49.97 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 354 EQVQQLQEEVNRLRIENREKEYQLEALSSRCSVMKEEL-RKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKn 432
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTpCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREA- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 433 ymgqniisktLREKNKVEEKLQEDSRR-KLLQLQEMGNRENLIKINLERAVGQLENFRNQVIKATFgktkpfrdkpitDQ 511
Cdd:TIGR00618 252 ----------QEEQLKKQQLLKQLRARiEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQ------------QA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 512 QLIEKIIQVTEDNLS--FQQRKWTLQRETHLHPKQ--EETMHSVEKLRVLLDKCQACMRDscssiDLKKEVELLQHLpls 587
Cdd:TIGR00618 310 QRIHTELQSKMRSRAklLMKRAAHVKQQSSIEEQRrlLQTLHSQEIHIRDAHEVATSIRE-----ISCQQHTLTQHI--- 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 588 pLVSGLQKTVVNILRVSLSWLEETEQ-LLGDLDIELSDsdkgFSLCLIYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQ 666
Cdd:TIGR00618 382 -HTLQQQKTTLTQKLQSLCKELDILQrEQATIDTRTSA----FRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKL 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 667 EHLAEKE---KLAEKLEQEEKLKAKIQQLTEEKAA----LEESIGQEKSRSEEALEKAQARVRELENH-LASQKEALENS 738
Cdd:TIGR00618 457 EKIHLQEsaqSLKEREQQLQTKEQIHLQETRKKAVvlarLLELQEEPCPLCGSCIHPNPARQDIDNPGpLTRRMQRGEQT 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 739 VA---QEKRKMREMLEAERRKAQDLENQLTqqkeiSENNTYEKLKMRDTLEKEK-RKIQDLENRLTKQKEEIELKEQKEN 814
Cdd:TIGR00618 537 YAqleTSEEDVYHQLTSERKQRASLKEQMQ-----EIQQSFSILTQCDNRSKEDiPNLQNITVRLQDLTEKLSEAEDMLA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 815 VLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFE-EE 893
Cdd:TIGR00618 612 CEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEkEQ 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 894 ISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAGPPL-------DSGDKEIACDHLI 966
Cdd:TIGR00618 692 LTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQartvlkaRTEAHFNNNEEVT 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 967 DDLLMAQKEILSQQEIIMKLRtDLGEAHSRMSDLRGELSEKQKMELERQVALVRQQSGELSMLKAKVAQTTGLMEKKDRE 1046
Cdd:TIGR00618 772 AALQTGAELSHLAAEIQFFNR-LREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQ 850
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 568931432 1047 LKVLREALRASQEKPRPHLSTEQKPRTLSQKCDISLQIEpahPDSFSSFQEE 1098
Cdd:TIGR00618 851 LLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFD---GDALIKFLHE 899
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
292-1059 |
1.33e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 292 IESMKSQINALQKGysqvlsqtlAERNTEIESLKNEGENLkrDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENR 371
Cdd:TIGR02168 195 LNELERQLKSLERQ---------AEKAERYKELKAELREL--ELALLVLRLEELREELEELQEELKEAEEELEELTAELQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 372 EKEYQLEALSSRCSVMKEELrkeeaqkdrrEAQEKELKLCRSQMQDMEKEVRKLREELKKnymgqniISKTLREKNKVEE 451
Cdd:TIGR02168 264 ELEEKLEELRLEVSELEEEI----------EELQKELYALANEISRLEQQKQILRERLAN-------LERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 452 KLQEDSRRKLLQLQEMGNRENLIKINLERAVGQLENFRNQVikatfgktKPFRDKPITDQQLIEkiiqvtednlsfqqrk 531
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL--------EELESRLEELEEQLE---------------- 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 532 wTLQRETHLHPKQEETmhsveklrvlldkcqacmrdscssidLKKEVELLqhlplSPLVSGLQKTVvnilrvslswlEET 611
Cdd:TIGR02168 383 -TLRSKVAQLELQIAS--------------------------LNNEIERL-----EARLERLEDRR-----------ERL 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 612 EQLLGDLDIELSDSDKgfslcliyllehyKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQ 691
Cdd:TIGR02168 420 QQEIEELLKKLEEAEL-------------KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 692 LTEEKAALEesigqeksRSEEALEKAQARVRELENHlASQKEALENSVAQ----EKRKMREMLEAERRKAQDL--ENQLT 765
Cdd:TIGR02168 487 LQARLDSLE--------RLQENLEGFSEGVKALLKN-QSGLSGILGVLSElisvDEGYEAAIEAALGGRLQAVvvENLNA 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 766 QQKEIS---ENNT-------YEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVM--VEDAQQM 833
Cdd:TIGR02168 558 AKKAIAflkQNELgrvtflpLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVddLDNALEL 637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 834 K-----------------------TTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGF 890
Cdd:TIGR02168 638 AkklrpgyrivtldgdlvrpggviTGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL 717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 891 EEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQdltAGPPLDSGDKEIA-----CDHL 965
Cdd:TIGR02168 718 RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE---AEEELAEAEAEIEeleaqIEQL 794
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 966 IDDLLMAQKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQKmELERQVALVRQQSGELSMLKAKVAQTTGLMEKKDR 1045
Cdd:TIGR02168 795 KEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER-RLEDLEEQIEELSEDIESLAAEIEELEELIEELES 873
|
810
....*....|....
gi 568931432 1046 ELKVLREALRASQE 1059
Cdd:TIGR02168 874 ELEALLNERASLEE 887
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
680-913 |
1.33e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 49.72 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 680 EQEEKLKAKIQQLTEEKAALEEsIGQEKSRSEEALEKAQARVRELENHLASQK--EALENSVAQEKRKMREMLEAERRKA 757
Cdd:pfam05483 374 KNEDQLKIITMELQKKSSELEE-MTKFKNNKEVELEELKKILAEDEKLLDEKKqfEKIAEELKGKEQELIFLLQAREKEI 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 758 QDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQD---------LENRLTKQKEE---IELKEQKENVLNNKlKDALV 825
Cdd:pfam05483 453 HDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIEltahcdkllLENKELTQEASdmtLELKKHQEDIINCK-KQEER 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 826 MVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMiltdDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHS 905
Cdd:pfam05483 532 MLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKL----DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKN 607
|
....*...
gi 568931432 906 QTIVSLEE 913
Cdd:pfam05483 608 KNIEELHQ 615
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
208-467 |
1.50e-05 |
|
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: 49.74 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 208 MDHDLSQQDKDEiillLGREVNRLSDFEMESKYKDALiMNLQAEVADLSQRLsetaavaaARQSNRCDPKLQGVD---EG 284
Cdd:pfam17380 296 MEQERLRQEKEE----KAREVERRRKLEEAEKARQAE-MDRQAAIYAEQERM--------AMERERELERIRQEErkrEL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 285 DDLRQKEIESMKSQINALQKgySQVLSQTLAER-NTEIESLKN----EGENLKRDHAITSGMVTSLQKDMSARNEQVQQL 359
Cdd:pfam17380 363 ERIRQEEIAMEISRMRELER--LQMERQQKNERvRQELEAARKvkilEEERQRKIQQQKVEMEQIRAEQEEARQREVRRL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 360 QEE----VNRLRIENREKEYQLEAL--------SSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLRE 427
Cdd:pfam17380 441 EEErareMERVRLEEQERQQQVERLrqqeeerkRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEK 520
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 568931432 428 ELKKNymgQNIISKTLREKNKVEE--KLQEDSRRKLLQLQEM 467
Cdd:pfam17380 521 EMEER---QKAIYEEERRREAEEErrKQQEMEERRRIQEQMR 559
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
636-822 |
1.68e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 636 LLEHYKKIMS---------QSQDLQAQMNASRETQKSLRQEhLAEKEKLAEKLEQE------EKLKAKIQQLTEEKAALE 700
Cdd:COG4913 230 LVEHFDDLERahealedarEQIELLEPIRELAERYAAARER-LAELEYLRAALRLWfaqrrlELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 701 EsigqEKSRSEEALEKAQARVRELENHLAS----QKEALENSVAQEKRKMREMleaeRRKAQDLENQLTQQKEISENN-- 774
Cdd:COG4913 309 A----ELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEER----ERRRARLEALLAALGLPLPASae 380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568931432 775 TYEKLK--MRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKD 822
Cdd:COG4913 381 EFAALRaeAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
648-788 |
1.99e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 648 QDLQAQMNASRETQKSLRQEHLAEKEKLAE-KLEQEEKLKAKIQQLTEEKAALE----------ESIGQEKSRSEEALEK 716
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERErrrarleallAALGLPLPASAEEFAA 384
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568931432 717 AQARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNtyekLKMRDTLEKE 788
Cdd:COG4913 385 LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL----LALRDALAEA 452
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
651-914 |
2.29e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 651 QAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKA-KIQQLTEEKAALEESIGQEKSRSEEALEKAQA--RVRELENH 727
Cdd:PTZ00121 1244 KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAdELKKAEEKKKADEAKKAEEKKKADEAKKKAEEakKADEAKKK 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 728 LASQKEALE--NSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEK---EKRKIQDLENRLTKQ 802
Cdd:PTZ00121 1324 AEEAKKKADaaKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaeEKKKADEAKKKAEED 1403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 803 KEEI-ELK---EQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKET--LAELETTKTKMILTDDRLKLQQQSM 876
Cdd:PTZ00121 1404 KKKAdELKkaaAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAkkAEEAKKKAEEAKKADEAKKKAEEAK 1483
|
250 260 270
....*....|....*....|....*....|....*...
gi 568931432 877 KALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEER 914
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEA 1521
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
644-1136 |
2.47e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 644 MSQSQDLQAQMNAsRETQKSLRQEHLAEKEKLAEKLEQEEKLKA-KIQQLTEEKAALEESigqeKSRSEEALEKAQARVR 722
Cdd:PTZ00121 1262 MAHFARRQAAIKA-EEARKADELKKAEEKKKADEAKKAEEKKKAdEAKKKAEEAKKADEA----KKKAEEAKKKADAAKK 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 723 ELEnhlaSQKEALENSVAQEKRKMREMLEAERR-KAQDLENQLTQQKEISENNTYEKLKMRDTL----EKEKRKIQDLEN 797
Cdd:PTZ00121 1337 KAE----EAKKAAEAAKAEAEAAADEAEAAEEKaEAAEKKKEEAKKKADAAKKKAEEKKKADEAkkkaEEDKKKADELKK 1412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 798 RLTKQKEEIELKEQKENVlnNKLKDALVMVEDAQQM-----KTTESQRAETLALKLKETLAELETTKTkmilTDDRLKLQ 872
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEK--KKADEAKKKAEEAKKAdeakkKAEEAKKAEEAKKKAEEAKKADEAKKK----AEEAKKAD 1486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 873 QQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAGPP 952
Cdd:PTZ00121 1487 EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKA 1566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 953 LDSGDKEIACDHLIDDLLMAQKEILSQQEIIMKLRTDlgEAHSRMSDLRGELSEKQKMELERQVALVRQQSGELSMLKAK 1032
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE--EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE 1644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1033 VAQTTGLMEKKDRELKVLREALRASQEKPRPHLSTEQKPRTLSQKCDISLQIEpahpdsfssfqEEQSFSDLGVKCKGSR 1112
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE-----------AEEAKKAEELKKKEAE 1713
|
490 500
....*....|....*....|....
gi 568931432 1113 HEETIQRQRKALSELRTRVRELEK 1136
Cdd:PTZ00121 1714 EKKKAEELKKAEEENKIKAEEAKK 1737
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
288-501 |
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 568931432 288 RQKEIESMKSQINALQKgysqvlsqTLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLR 367
Cdd:COG4942 25 AEAELEQLQQEIAELEK--------ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 368 IENREKEYQLEAL------SSRCSVMKEELRKE----------------EAQKDRREAQEKELKLCRSQMQDMEKEVRKL 425
Cdd:COG4942 97 AELEAQKEELAELlralyrLGRQPPLALLLSPEdfldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568931432 426 REELKKNYMGQNIISKTLREKNKVEEKLQEDSRRKLLQLQEMGNRENLIKINLERAVGQLENFRNQVIKATFGKTK 501
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
670-856 |
2.94e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 670 AEKEKLAEKLEQEEKLKAKIQQLTEEKAALEEsigqEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREM 749
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNE----EYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 750 LEAERRK-----------AQDLENQLTQQKEISENNtyeklkmRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNN 818
Cdd:COG3883 96 YRSGGSVsyldvllgsesFSDFLDRLSALSKIADAD-------ADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 568931432 819 KLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELE 856
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
608-769 |
3.62e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 608 LEETEQLLGDLDIELSDsdkgfslcLIYLLEHYKKIMSQSQDLQAQMNASRETQkSLRQEHLAEKEKLAEKLEQEEKLKA 687
Cdd:COG3206 221 LSELESQLAEARAELAE--------AEARLAALRAQLGSGPDALPELLQSPVIQ-QLRAQLAELEAELAELSARYTPNHP 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 688 KIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERRK--AQDLENQLT 765
Cdd:COG3206 292 DVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVevARELYESLL 371
|
....
gi 568931432 766 QQKE 769
Cdd:COG3206 372 QRLE 375
|
|
| FHA_GarA-like |
cd22720 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis glycogen accumulation ... |
12-65 |
3.89e-05 |
|
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: 43.84 E-value: 3.89e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 568931432 12 FVLNKSTT-IGKHADSDLVLQSADIDNHHAliEFNEAEGTFVLQDFNSRNGTFVN 65
Cdd:cd22720 19 FLLDQAITsAGRHPDSDIFLDDVTVSRRHA--EFRLENNEFNVVDVGSLNGTYVN 71
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
594-855 |
3.92e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.51 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 594 QKTVVNILRVSLSWLEETEQLLGDLDielsdsdkgfslcliylleHYKKIMSQ----SQDLQAQMNASRETQKSLRqEHL 669
Cdd:PRK10929 43 QAEIVEALQSALNWLEERKGSLERAK-------------------QYQQVIDNfpklSAELRQQLNNERDEPRSVP-PNM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 670 AEKEklaekLEQeEKLKAKIQQLTEEKAALEEsigQEKSR----SEEALEKAQARVRELENHLASQKEALENS---VAQE 742
Cdd:PRK10929 103 STDA-----LEQ-EILQVSSQLLEKSRQAQQE---QDRAReisdSLSQLPQQQTEARRQLNEIERRLQTLGTPntpLAQA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 743 KRKMREMlEAERRKAQDLENQLTQqkeISENNTYEKLKMRDTLEKEKR-----KIQDLENRLTKQ-KEEIE--------L 808
Cdd:PRK10929 174 QLTALQA-ESAALKALVDELELAQ---LSANNRQELARLRSELAKKRSqqldaYLQALRNQLNSQrQREAEralestelL 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 568931432 809 KEQKENV---------LNNKLKDALvmVEDAQQMKTTESQR--AETLALKLKETLAEL 855
Cdd:PRK10929 250 AEQSGDLpksivaqfkINRELSQAL--NQQAQRMDLIASQQrqAASQTLQVRQALNTL 305
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
315-703 |
4.31e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 315 AERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSRCSVMKEELRKE 394
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 395 EAQKDRR-------EAQEKELKLCRSQMQDMEKEVRKLREELKKNYMGQNI----ISKTLREKNKVEEKLQEDSRRKLLQ 463
Cdd:TIGR02168 746 EERIAQLskeltelEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEelkaLREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 464 LQEMGNRENLIKINLERAVGQLENFRNQVIKATfgktkpfrdKPITDQQ-LIEKIIQVTEdnlSFQQRKWTLQRETHLHP 542
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLA---------AEIEELEeLIEELESELE---ALLNERASLEEALALLR 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 543 KQEETMhsVEKLRVLLDKCQacmrdscssiDLKKEVELLQHLpLSPLVSGLQKTVVNILRVslswleeTEQLLGDLDIEL 622
Cdd:TIGR02168 894 SELEEL--SEELRELESKRS----------ELRRELEELREK-LAQLELRLEGLEVRIDNL-------QERLSEEYSLTL 953
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 623 SDsdkgfslcliyLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEES 702
Cdd:TIGR02168 954 EE-----------AEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEA 1022
|
.
gi 568931432 703 I 703
Cdd:TIGR02168 1023 I 1023
|
|
| FHA_FhaA-like |
cd22668 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
17-87 |
4.59e-05 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaA and similar proteins; FhaA regulates cell growth and peptidoglycan synthesis by binding to MviN. It may inhibit the late stages of peptidoglycan synthesis. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438720 [Multi-domain] Cd Length: 91 Bit Score: 43.61 E-value: 4.59e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568931432 17 STTIGKHADSDLVLQSADIDNHHALIEFNEaeGTFVLQDFNSRNGTFVNECHIQnVAVKLIPGDILRFGSA 87
Cdd:cd22668 19 SNIIGRGSDADFRLPDTGVSRRHAEIRWDG--QVAHLTDLGSTNGTTVNNAPVT-PEWRLADGDVITLGHS 86
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
596-726 |
4.62e-05 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 47.32 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 596 TVVNILRVSLSWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQDLqaqMNASRETQKSLRQEHLAEKEKL 675
Cdd:smart00787 151 ENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTE---LDRAKEKLKKLLQEIMIKVKKL 227
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 568931432 676 AEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEA-------LEKAQARVRELEN 726
Cdd:smart00787 228 EELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCrgftfkeIEKLKEQLKLLQS 285
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
663-886 |
5.54e-05 |
|
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: 46.67 E-value: 5.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 663 SLRQEHLAEKEKLAEKLEQEEKLKAKIQQ---------LTEEKAALEESiGQEKSRSEEALEKAQARVRELEN---HLAS 730
Cdd:pfam09787 4 SAKQELADYKQKAARILQSKEKLIASLKEgsgvegldsSTALTLELEEL-RQERDLLREEIQKLRGQIQQLRTelqELEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 731 QKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLekeKRKIQDLENRLTKQKEEIELKE 810
Cdd:pfam09787 83 QQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATL---QSRIKDREAEIEKLRNQLTSKS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568931432 811 QkenvlnnklkdalvmvEDAQQMKTTESQRAETLALKLKETLAE-LETTKTKMILTDDRLklqQQSMKALQDERESQ 886
Cdd:pfam09787 160 Q----------------SSSSQSELENRLHQLTETLIQKQTMLEaLSTEKNSLVLQLERM---EQQIKELQGEGSNG 217
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
651-758 |
5.86e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.17 E-value: 5.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 651 QAQMNASRETQKSLRQehLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELEnhlas 730
Cdd:COG2268 223 AEEAELEQEREIETAR--IAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQ----- 295
|
90 100
....*....|....*....|....*...
gi 568931432 731 QKEAlENSVAQEKRKMREMLEAERRKAQ 758
Cdd:COG2268 296 EKEA-EREEAELEADVRKPAEAEKQAAE 322
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
656-1159 |
6.72e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 6.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 656 ASRETQKSLRQEHLAEKEKLAEkLEQE-EKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEA 734
Cdd:PRK02224 234 ETRDEADEVLEEHEERREELET-LEAEiEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAV 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 735 LENSVAQEKRK--MREMLEAERRKAQDLENQ---LTQQKEISENNTYEKLKMRDTLEKEkrkIQDLENRLTKQKEEIELK 809
Cdd:PRK02224 313 EARREELEDRDeeLRDRLEECRVAAQAHNEEaesLREDADDLEERAEELREEAAELESE---LEEAREAVEDRREEIEEL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 810 EQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETtktkmilTDDRLKLQQQsmkaLQDERESQKHG 889
Cdd:PRK02224 390 EEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRT-------ARERVEEAEA----LLEAGKCPECG 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 890 FEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNndtgpkeeasqdltagppLDSGDKEIacDHLIDDL 969
Cdd:PRK02224 459 QPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED------------------LVEAEDRI--ERLEERR 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 970 LMAQKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQK--MELERQVALVRQQSGELSMLKA----------KVAQTT 1037
Cdd:PRK02224 519 EDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREaaAEAEEEAEEAREEVAELNSKLAelkeriesleRIRTLL 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1038 GLMEKKDRELKVLREALRASQEKprphlsTEQKPRTLSQKCDISLQIEPAHPDsfSSFQEEQSfsdlgvkcKGSRHEETI 1117
Cdd:PRK02224 599 AAIADAEDEIERLREKREALAEL------NDERRERLAEKRERKRELEAEFDE--ARIEEARE--------DKERAEEYL 662
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 568931432 1118 QRQRKALSELRTRVRELEKANSCnhkdhVNESFLELRTLRME 1159
Cdd:PRK02224 663 EQVEEKLDELREERDDLQAEIGA-----VENELEELEELRER 699
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
667-917 |
8.38e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 8.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 667 EHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIG-QEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRk 745
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELAERYAAARERLAeLEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELER- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 746 mremLEAERRKAQDLENQLTQQkeISENNTyeklkmrdtlekekRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDA-L 824
Cdd:COG4913 314 ----LEARLDALREELDELEAQ--IRGNGG--------------DRLEQLEREIERLERELEERERRRARLEALLAALgL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 825 VMVEDAQQMKTTESQRAETLAlKLKETLAELETTKtkmiltdDRLKLQQQsmkALQDERESQkhgfEEEISEYKEQIKQH 904
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLE-ALEEELEALEEAL-------AEAEAALR---DLRRELREL----EAEIASLERRKSNI 438
|
250
....*....|...
gi 568931432 905 SQTIVSLEERLCQ 917
Cdd:COG4913 439 PARLLALRDALAE 451
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
669-796 |
8.90e-05 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 46.13 E-value: 8.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 669 LAEKEKLAEKLEQEE----KLKAKIQQLTEEKAALEESIGQ-------------EKSRSEEALEKAQARVRELENHLASQ 731
Cdd:pfam02841 154 LEERDKLEAKYNQVPrkgvKAEEVLQEFLQSKEAVEEAILQtdqaltakekaieAERAKAEAAEAEQELLREKQKEEEQM 233
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568931432 732 KEALENSVAQEKRKMREMLEAERRKAQDlENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLE 796
Cdd:pfam02841 234 MEAQERSYQEHVKQLIEKMEAEREQLLA-EQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
248-433 |
9.12e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 9.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 248 LQAEVADLSQRLSETAAVAAA---------RQSNRCDpKLQGVDEGD-DLR--QKEIESMKSQINALQKGYSQV--LSQT 313
Cdd:COG4913 615 LEAELAELEEELAEAEERLEAleaeldalqERREALQ-RLAEYSWDEiDVAsaEREIAELEAELERLDASSDDLaaLEEQ 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 314 LAERNTEIESLKNEGENLKRDHAitsgmvtSLQKDMSARNEQVQQLQEEVNrlRIENREKEYQLEALSSRCsvmkEELRK 393
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIG-------RLEKELEQAEEELDELQDRLE--AAEDLARLELRALLEERF----AAALG 760
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568931432 394 EEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNY 433
Cdd:COG4913 761 DAVERELRENLEERIDALRARLNRAEEELERAMRAFNREW 800
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
672-900 |
9.27e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 9.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 672 KEKLAEKLEQEEKLKAKIQQLTEEKAALEesigqeksRSEEALEKAQARVRELENHLASQKEalensvaqekrkmremLE 751
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALE--------AELDALQERREALQRLAEYSWDEID----------------VA 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 752 AERRKAQDLENQLTQqkeISENNtyeklkmrDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQ 831
Cdd:COG4913 665 SAEREIAELEAELER---LDASS--------DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 832 -QMKTTESQRAETLALKLKETLAELETTKtkmILTDDRLKLQQQsMKALQDERESQKHGFEEEISEYKEQ 900
Cdd:COG4913 734 dRLEAAEDLARLELRALLEERFAAALGDA---VERELRENLEER-IDALRARLNRAEEELERAMRAFNRE 799
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
339-1058 |
9.72e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.96 E-value: 9.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 339 SGMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSRCSVMKEELRKEEAQKDRREAQEKELklcrsqmQDM 418
Cdd:TIGR00606 404 EDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRI-------LEL 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 419 EKEVRKLREELKKNYMGQNIISKTLREKNKVEEKLQED-SRRKLLQLQEMGNRENLIKINLER-------AVGQLENFRN 490
Cdd:TIGR00606 477 DQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDrKLRKLDQEMEQLNHHTTTRTQMEMltkdkmdKDEQIRKIKS 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 491 QVIKATFGKTKPFRDKPITDQQL--IEKIIQVTEDNLSFQQRKWTLQRETHLHPKQEEtmhsvEKLRVLLDKCQACMRDS 568
Cdd:TIGR00606 557 RHSDELTSLLGYFPNKKQLEDWLhsKSKEINQTRDRLAKLNKELASLEQNKNHINNEL-----ESKEEQLSSYEDKLFDV 631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 569 CSSIDLKKEVELLqhlplsplvsglqKTVVNILRVSLSWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQ 648
Cdd:TIGR00606 632 CGSQDEESDLERL-------------KEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFIS 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 649 DLQAQMNASRETQKSLrqehlaekEKLAEKLEQEEKLkakIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHL 728
Cdd:TIGR00606 699 DLQSKLRLAPDKLKST--------ESELKKKEKRRDE---MLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDI 767
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 729 ASQKEALENSVAQEKRK---MREMLEAERRKAQDLENQLTQQKEISENNTYEklkMRDTLEKEKRKIQDLENRLTKQKEE 805
Cdd:TIGR00606 768 EEQETLLGTIMPEEESAkvcLTDVTIMERFQMELKDVERKIAQQAAKLQGSD---LDRTVQQVNQEKQEKQHELDTVVSK 844
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 806 IEL-----KEQKENVLN-----NKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQS 875
Cdd:TIGR00606 845 IELnrkliQDQQEQIQHlksktNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE 924
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 876 MKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQK-IEGEITTLK---NNDTGPKEEASQDL-TAG 950
Cdd:TIGR00606 925 KEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKqKETELNTVNaqlEECEKHQEKINEDMrLMR 1004
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 951 PPLDSGDKeiacdhliddllmaQKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQKMELERQVALVRQqsgELSMLK 1030
Cdd:TIGR00606 1005 QDIDTQKI--------------QERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEE---NIDLIK 1067
|
730 740
....*....|....*....|....*...
gi 568931432 1031 AKVAQTTGLMEKKDRELKVLREALRASQ 1058
Cdd:TIGR00606 1068 RNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
671-1332 |
1.04e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 671 EKEKLAEKLEQEEKLKAKIQQLTEEKAALEES--IGQEKSRSEEALEKAQARVRELENHLASQKEALEN--SVAQEKRKM 746
Cdd:PRK03918 136 EIDAILESDESREKVVRQILGLDDYENAYKNLgeVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEvlREINEISSE 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 747 REMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNnklkdalvm 826
Cdd:PRK03918 216 LPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK--------- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 827 vedaqqmkttESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQkhgfEEEISEYKEQIKQhsq 906
Cdd:PRK03918 287 ----------ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK----EERLEELKKKLKE--- 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 907 tivsLEERLCQVTQYYQKIEgEITTLKNNdtgpKEEASQDLTAGPPldsgdkeiacDHLIDDLLMAQKEILSQQEIIMKL 986
Cdd:PRK03918 350 ----LEKRLEELEERHELYE-EAKAKKEE----LERLKKRLTGLTP----------EKLEKELEELEKAKEEIEEEISKI 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 987 RTDLGEAHSRMSDLRGELSEKQK-----------MELERQVALVRQQSGELSMLKAKVAQTTGLMEKKDRELKVLrEALR 1055
Cdd:PRK03918 411 TARIGELKKEIKELKKAIEELKKakgkcpvcgreLTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL-EKVL 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1056 ASQEKPRPHLSTEQKPRTLSQKCDiSLQIEPAHPDSFSSFQEEQSFSDLGVKCKGSRHE-ETIQRQRKALSELRTRVREL 1134
Cdd:PRK03918 490 KKESELIKLKELAEQLKELEEKLK-KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKElEKLEELKKKLAELEKKLDEL 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1135 EKANSCNHKDHVNESF-----LELRTLRMEKNVQKI--LLDAKPDLTtlarveirppqnspfnsgSTLVMEKSVKTDAGE 1207
Cdd:PRK03918 569 EEELAELLKELEELGFesveeLEERLKELEPFYNEYleLKDAEKELE------------------REEKELKKLEEELDK 630
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1208 ALELSEKLYTDMIKTLGSLMNIKDMSSHTSLKHLSPKEREKVNHLRQKDldlvfDKITQLKTRLQRKEELLKGYEQELEQ 1287
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLR-----AELEELEKRREEIKKTLEKLKEELEE 705
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 568931432 1288 LRHSKVSVQMYQTQVAKLEDDVHKEAEEKALLKE-ALERTEQQLSQ 1332
Cdd:PRK03918 706 REKAKKELEKLEKALERVEELREKVKKYKALLKErALSKVGEIASE 751
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
638-830 |
1.05e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.97 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 638 EHYKKimsQSQDLQAQMNASRETQKSLRQEH----LAEKEKLAEkleQEEKLKAKIQQLTEEKAALEESIGQEKSRSEE- 712
Cdd:PRK10929 211 ELAKK---RSQQLDAYLQALRNQLNSQRQREaeraLESTELLAE---QSGDLPKSIVAQFKINRELSQALNQQAQRMDLi 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 713 ALEKAQA-----RVRELENHLASQK----------EALENSVAQ--EKRKM----REM--LEAERRKAQDLENQLTQQKE 769
Cdd:PRK10929 285 ASQQRQAasqtlQVRQALNTLREQSqwlgvsnalgEALRAQVARlpEMPKPqqldTEMaqLRVQRLRYEDLLNKQPQLRQ 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568931432 770 ISENNTYeklkmrdTLEKEKRKIqdLENRLTKQKEEIE----------LKEQKENVLNNKLKDALVMVEDA 830
Cdd:PRK10929 365 IRQADGQ-------PLTAEQNRI--LDAQLRTQRELLNsllsggdtliLELTKLKVANSQLEDALKEVNEA 426
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
673-874 |
1.26e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 673 EKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELEnhlaSQKEALENSVAQEKRKMREMLEA 752
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELE----EELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 753 ERRKAQDLENQLTQQKEISENNTYEKLKMR-DTLEKEKRKIQDLENRLTKQKEEI-ELKEQKENVLNNKLKDALVMVEDA 830
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLEELEERlEELRELEEELEELEAELAELQEELeELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568931432 831 QQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQ 874
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
|
|
| FHA_OdhI-like |
cd22721 |
forkhead associated (FHA) domain found in Corynebacterium glutamicum oxoglutarate ... |
11-65 |
1.31e-04 |
|
forkhead associated (FHA) domain found in Corynebacterium glutamicum oxoglutarate dehydrogenase inhibitor (OdhI) and similar proteins; OdhI is an essential component of the PknG signaling pathway. It regulates glutamate production under biotin non-limiting conditions. It can inhibit the activity of 2-oxoglutarate dehydrogenase only when it is unphosphorylated. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438773 [Multi-domain] Cd Length: 102 Bit Score: 42.38 E-value: 1.31e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 568931432 11 FFVLNKSTTIGKHADSDLVLQSADIDNHHAliEFNEAEGTFVLQDFNSRNGTFVN 65
Cdd:cd22721 24 FLLDQPTTTAGRHPESDIFLDDVTVSRRHA--EFRINEGEFEVVDVGSLNGTYVN 76
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
656-842 |
1.32e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 656 ASRETQKSLRQEHLAEKEKLAEKLEQE-EKLKAKIQQLTEEKAALEESIgqekSRSEEALEKAQARVRELENHLASQKEA 734
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAElDALQAELEELNEEYNELQAEL----EALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 735 LENSVAQEKRKMR---------------------EMLEAERRKAQDLENQLTQQKEISENntyEKLKMRDTLEKEKRKIQ 793
Cdd:COG3883 88 LGERARALYRSGGsvsyldvllgsesfsdfldrlSALSKIADADADLLEELKADKAELEA---KKAELEAKLAELEALKA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568931432 794 DLEnrltKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAE 842
Cdd:COG3883 165 ELE----AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
373-940 |
1.43e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 373 KEYQLEALSSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNYMGQNIISKTLREKNKVEEK 452
Cdd:PRK01156 136 GQGEMDSLISGDPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSI 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 453 LQEDSRRKLLQLQEMGNRENLIKINLERAVGQLE--NFRNQVIKATFGKTKPFRDKPITDQQLIEKIIQVTEDNLSFQQR 530
Cdd:PRK01156 216 TLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDmkNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRN 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 531 K----WTLQRETHLHPKQEETMHS-VEKLRVLLDKCQACMRDSCSSIDLKKEVELLQH--LPLSPLVSGLQKTVVNILRV 603
Cdd:PRK01156 296 YindyFKYKNDIENKKQILSNIDAeINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNqiLELEGYEMDYNSYLKSIESL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 604 SLsWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQeHLAEKEKLAEKLEQEE 683
Cdd:PRK01156 376 KK-KIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRE-NLDELSRNMEMLNGQS 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 684 KLKAKIQQLTEEKAA-LEESIGQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKmremLEAERRKAQDLEN 762
Cdd:PRK01156 454 VCPVCGTTLGEEKSNhIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINK----SINEYNKIESARA 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 763 QLTQQKeISENntyeklkmrdTLEKEKRKIQDLENRLTKQKEEIeLKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAE 842
Cdd:PRK01156 530 DLEDIK-IKIN----------ELKDKHDKYEEIKNRYKSLKLED-LDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLN 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 843 TLALKLKETLAELETTKT----KMILTDDRLKLQQQSMKALQDEReSQKHGFEEEISEYKEQIKQHSQTIVSLEE---RL 915
Cdd:PRK01156 598 DLESRLQEIEIGFPDDKSyidkSIREIENEANNLNNKYNEIQENK-ILIEKLRGKIDNYKKQIAEIDSIIPDLKEitsRI 676
|
570 580
....*....|....*....|....*
gi 568931432 916 CQVTQYYQKIEGEITTLKNNDTGPK 940
Cdd:PRK01156 677 NDIEDNLKKSRKALDDAKANRARLE 701
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
12-85 |
1.47e-04 |
|
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing protein ArnA and similar proteins; ArnA is an FHA domain-containing protein from Sulfolobus acidocaldarius that was shown to strongly interact with ArnB, a von Willebrand domain-containing protein. They act synergistically and negatively to modulate motility. ArnA is involved in regulating archaella expression in S. acidocaldarius. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438732 [Multi-domain] Cd Length: 96 Bit Score: 42.33 E-value: 1.47e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568931432 12 FVLNKST-TIGKHADSDLVLQSADIDNHHALIEFNEaeGTFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRFG 85
Cdd:cd22680 16 FPFDFSSvSIGRDPENVIVIPDPFVSRNHARITVDS--NEIYIEDLGSTNGTFVNDFKRIKGPAKLHPNDIIKLG 88
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
641-815 |
1.66e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 641 KKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIG------QEKSRSE--- 711
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraralYRSGGSVsyl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 712 ----------------EALEKAQARVRELENHLASQKEALENSVAQEKRKMREmLEAERRKAQDLENQLTQQKEisennt 775
Cdd:COG3883 106 dvllgsesfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAE-LEALKAELEAAKAELEAQQA------ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568931432 776 yEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENV 815
Cdd:COG3883 179 -EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
259-471 |
1.90e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 259 LSETAAVAAARQSNRCDPKLQGVDEGDDLRQKEIESMKSQINALQKGYSQVLSQtLAERNTEIESLKNE----GENLKRD 334
Cdd:COG3883 6 LAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE-LEALQAEIDKLQAEiaeaEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 335 HAITSGMVTSLQKDMSARNE-----QVQQLQEEVNRLRIENREKEYQLEALSSrcsvMKEELRKEEAQKDRREAQEKELK 409
Cdd:COG3883 85 REELGERARALYRSGGSVSYldvllGSESFSDFLDRLSALSKIADADADLLEE----LKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568931432 410 LCRSQMQDMEKEVRKLREELkknymgQNIISKTLREKNKVEEKLQEDSRRKLLQLQEMGNRE 471
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQ------EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
667-812 |
2.54e-04 |
|
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: 44.15 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 667 EHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSR---SEEALEKAQARVRELENHLASQKEALENSVAQ-- 741
Cdd:COG1579 4 EDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARleaAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlg 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568931432 742 EKRKMREM------LEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQK 812
Cdd:COG1579 84 NVRNNKEYealqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
648-829 |
2.81e-04 |
|
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: 44.15 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 648 QDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRsEEALEKAQARV---REL 724
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR-IKKYEEQLGNVrnnKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 725 ENhLASQKEALENSVAQEKRKMREMLEaerrKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKE 804
Cdd:COG1579 92 EA-LQKEIESLKRRISDLEDEILELME----RIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
170 180 190
....*....|....*....|....*....|.
gi 568931432 805 EI------ELKEQKENVLNNKLKDALVMVED 829
Cdd:COG1579 167 ELaakippELLALYERIRKRKNGLAVVPVEG 197
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
683-807 |
2.87e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.46 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 683 EKLKAKIQQLTEEKAALEESigqEKSRSEEALEKAQARVRELENHLASQKEALEN--SVAQEKRKMREMLEAERRKAQDL 760
Cdd:COG0542 414 DELERRLEQLEIEKEALKKE---QDEASFERLAELRDELAELEEELEALKARWEAekELIEEIQELKEELEQRYGKIPEL 490
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568931432 761 ENQLTQ-QKEISENNTYEKL--------------------KMrdtLEKEKRKIQDLENRLTK----QKEEIE 807
Cdd:COG0542 491 EKELAElEEELAELAPLLREevteediaevvsrwtgipvgKL---LEGEREKLLNLEEELHErvigQDEAVE 559
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
658-808 |
2.96e-04 |
|
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: 45.33 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 658 RETQKSLRQEHLAEKEKLAEKLEQE-----EKLKAKIQQLTEEKAALEEsigqEKSRSEEALEKAQARVRELENHLASQK 732
Cdd:pfam15709 357 QEEQRRLQQEQLERAEKMREELELEqqrrfEEIRLRKQRLEEERQRQEE----EERKQRLQLQAAQERARQQQEEFRRKL 432
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568931432 733 EALENSVAQEKrkmREMLEAERRKAQDLENQLT-QQKEISENNTYEKLK-MRDTLEKEKRKIQDLENRLTKQKEEIEL 808
Cdd:pfam15709 433 QELQRKKQQEE---AERAEAEKQRQKELEMQLAeEQKRLMEMAEEERLEyQRQKQEAEEKARLEAEERRQKEEEAARL 507
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
665-1159 |
3.08e-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: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 665 RQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLA--------------- 729
Cdd:TIGR00618 213 MPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAvleetqerinrarka 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 730 -------------SQKEALENSVAQEKRKMREML----------EAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLE 786
Cdd:TIGR00618 293 aplaahikavtqiEQQAQRIHTELQSKMRSRAKLlmkraahvkqQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISC 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 787 KEKrkiqDLENRLTKQKEEIELKEQKENVLNNKLKdalvmVEDAQQmKTTESQRAETLALKLKETLAELETTKTKMILTD 866
Cdd:TIGR00618 373 QQH----TLTQHIHTLQQQKTTLTQKLQSLCKELD-----ILQREQ-ATIDTRTSAFRDLQGQLAHAKKQQELQQRYAEL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 867 DRLKLQQQSMKALQDERESQKhgFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQD 946
Cdd:TIGR00618 443 CAAAITCTAQCEKLEKIHLQE--SAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDI 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 947 LTAGPpldsgdkeiacdhLIDDLLMAQKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQKmELERQVALVRQQSGEL 1026
Cdd:TIGR00618 521 DNPGP-------------LTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQ-SFSILTQCDNRSKEDI 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 1027 SMLKAKVAQTTGLMEKKDRELKVLREALRASQEKPRPHLSTEQKPRTLsQKCDISLQIEPAHPDSFSS--FQEEQSFSDL 1104
Cdd:TIGR00618 587 PNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHL-QQCSQELALKLTALHALQLtlTQERVREHAL 665
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 568931432 1105 GVKCKGSRHEETIQRQRKAL-SELRTRVRELEKANSCNHKDH-VNESFLELRTLRME 1159
Cdd:TIGR00618 666 SIRVLPKELLASRQLALQKMqSEKEQLTYWKEMLAQCQTLLReLETHIEEYDREFNE 722
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
641-903 |
3.21e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 44.84 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 641 KKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEklkAKIQQLTEEKAALEESIGQEKSRSEEALEKAQAR 720
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQ---ARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 721 VrelenhlASQKEALENSVAQEKrkmremlEAERRKAQDLENQLTQQKEISENntyeklkmrdtlEKEKRKIQDLENRLT 800
Cdd:TIGR02794 123 E-------AKAKQAAEAKAKAEA-------EAERKAKEEAAKQAEEEAKAKAA------------AEAKKKAEEAKKKAE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 801 KQKEEIELKEQKENVLNNKLKdalvmvedAQQMKTTESQRAETLALKLKETLAELETTKTKMILT-DDRLKLQQQSMKAL 879
Cdd:TIGR02794 177 AEAKAKAEAEAKAKAEEAKAK--------AEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAElGDIFGLASGSNAEK 248
|
250 260
....*....|....*....|....
gi 568931432 880 QDERESQKHGfeEEISEYKEQIKQ 903
Cdd:TIGR02794 249 QGGARGAAAG--SEVDKYAAIIQQ 270
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
15-87 |
3.25e-04 |
|
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar proteins; ZEP, also called protein ABA DEFICIENT 1, ABA1, protein IMPAIRED IN BABA-INDUCED STERILITY 3, protein LOW EXPRESSION OF OSMOTIC STRESS-RESPONSIVE GENES 6, or protein NON-PHOTOCHEMICAL QUENCHING 2, plays an important role in the xanthophyll cycle and abscisic acid (ABA) biosynthesis. It converts zeaxanthin into antheraxanthin and subsequently violaxanthin. ZEP is required for resistance to osmotic and drought stresses, ABA-dependent stomatal closure, seed development and dormancy, modulation of defense gene expression, and disease resistance and non-photochemical quencing (NPQ). The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438754 [Multi-domain] Cd Length: 123 Bit Score: 42.03 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 15 NKSTTIGKHADSD-----LVLQSADIDNHHALIEFNEaeGTFVLQDFNSRNGTFVNECHIQ------NVAVKLIPGDILR 83
Cdd:cd22702 31 KQPCIIGSDPHQAisgisVVIPSPQVSELHARITCKN--GAFFLTDLGSEHGTWINDNEGRryrappNFPVRLHPSDVIE 108
|
....
gi 568931432 84 FGSA 87
Cdd:cd22702 109 FGSD 112
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
289-923 |
3.26e-04 |
|
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: 45.21 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 289 QKEIESMKSQINALQ---KGY--SQVLSQTLAERNTEIESLKNEGENLKRDHAITSgmVTSLQKDMSARNEQVQQLQEEV 363
Cdd:pfam12128 247 QQEFNTLESAELRLShlhFGYksDETLIASRQEERQETSAELNQLLRTLDDQWKEK--RDELNGELSAADAAVAKDRSEL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 364 NRlrIENREKEYQLEALSSRcsvmKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNYMGQNIISKTL 443
Cdd:pfam12128 325 EA--LEDQHGAFLDADIETA----AADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 444 REKNKVEEKLQEDSRRKLLQLQEMGNRENLIKINLERAVGQLEnfrnqvIKATFGKTKPFRDKPITDQQLIEKIiQVTED 523
Cdd:pfam12128 399 LAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYR------LKSRLGELKLRLNQATATPELLLQL-ENFDE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 524 NLSFQQRKWTLQRETHLHPKQEETmhsveKLRVLLDKCQACMRD-SCSSIDLKKEVELLQHLpLSPLVSGLQ---KTVVN 599
Cdd:pfam12128 472 RIERAREEQEAANAEVERLQSELR-----QARKRRDQASEALRQaSRRLEERQSALDELELQ-LFPQAGTLLhflRKEAP 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 600 ILRVSLSWLEETEQLL-GDLDIELSDSDKGFSLCLIYLLEHYKKImsqsqdlqaqmnasretqkslrqehlaekeKLAEK 678
Cdd:pfam12128 546 DWEQSIGKVISPELLHrTDLDPEVWDGSVGGELNLYGVKLDLKRI------------------------------DVPEW 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 679 LEQEEKLKAKIQQLteekaaleesigqeksrsEEALEKAQARVRELENHLASQKEALENSVAqekrkmremleAERRKAQ 758
Cdd:pfam12128 596 AASEEELRERLDKA------------------EEALQSAREKQAAAEEQLVQANGELEKASR-----------EETFART 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 759 DLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELK------EQKENVLNNKLkdalvmvEDAQQ 832
Cdd:pfam12128 647 ALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKhqawleEQKEQKREART-------EKQAY 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 833 MKTTESQRAETLALkLKETLAELETTKtkmiltDDRLKLQQQSMKalqdeRESQKHGFEEE-ISEYKEQIKQHSQTIVSL 911
Cdd:pfam12128 720 WQVVEGALDAQLAL-LKAAIAARRSGA------KAELKALETWYK-----RDLASLGVDPDvIAKLKREIRTLERKIERI 787
|
650
....*....|..
gi 568931432 912 EERLCQVTQYYQ 923
Cdd:pfam12128 788 AVRRQEVLRYFD 799
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
648-920 |
3.26e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.29 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 648 QDLQAQMNASREtqkslrQEHLAEKEKLAEK-LEQEEKLKAKIQQLTEEKAALEESIGQeksrSEEALEKAQARVRELEN 726
Cdd:PRK11281 39 ADVQAQLDALNK------QKLLEAEDKLVQQdLEQTLALLDKIDRQKEETEQLKQQLAQ----APAKLRQAQAELEALKD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 727 HLASQ-KEALEN-SVAQEKRKMREMLEAERRKAQDLE-------NQLTQ----QKEISENNTyeklkmrdtlekekrKIQ 793
Cdd:PRK11281 109 DNDEEtRETLSTlSLRQLESRLAQTLDQLQNAQNDLAeynsqlvSLQTQperaQAALYANSQ---------------RLQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 794 DLENRLTKQK-EEIELKEQKENVLNNKLkdALVMVEDAQQMKTTE----------SQRAEtlaLKLKETLAELETTKTKM 862
Cdd:PRK11281 174 QIRNLLKGGKvGGKALRPSQRVLLQAEQ--ALLNAQNDLQRKSLEgntqlqdllqKQRDY---LTARIQRLEHQLQLLQE 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 568931432 863 ILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQ 920
Cdd:PRK11281 249 AINSKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLLKATEKLNTLTQ 306
|
|
| FHA_PML1-like |
cd22681 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ... |
27-95 |
3.49e-04 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 (PML1) and similar proteins; PML1 is an FHA domain-containing protein required for efficient splicing and pre-mRNA nuclear retention. It is a component of the pre-mRNA retention and splicing (RES) complex composed of at least BUD13, IST3, and PML1. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438733 [Multi-domain] Cd Length: 129 Bit Score: 42.04 E-value: 3.49e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568931432 27 DLVLQSADIDNHHALIEFNEAEGTFV--LQDFNSRNGTFVNECHI-QNVAVKLIPGDILRFgSAGMTYELVI 95
Cdd:cd22681 58 DIGIPEETCSKQHCVIQFRNVKGILKpyIMDLDSSNGTCLNDNVIpSSRYVELRSGDVITF-SKSNDYELVF 128
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
706-935 |
4.00e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 706 EKSRSEEALEKAQARVRELENHlasqKEALENsvAQEKRKMREMLEAERRKAQDLENQLTQQkeisenntyEKLKMRDTL 785
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERA----HEALED--AREQIELLEPIRELAERYAAARERLAEL---------EYLRAALRL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 786 EKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDA-QQMKTTESQRAETLALKLKETLAELETTKTKMIL 864
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELeAQIRGNGGDRLEQLEREIERLERELEERERRRAR 363
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568931432 865 TDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNN 935
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
658-900 |
4.22e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.81 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 658 RETQKSLRQEHLAEKEKLAEKL-EQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKaQARVRELENHLASQKEALE 736
Cdd:pfam10174 456 KEQREREDRERLEELESLKKENkDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKK-DSKLKSLEIAVEQKKEECS 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 737 NSVAQEKrKMREMLEAERRKA------QDLENQLTQQKEISENNTYEKLKMRDTL---EKEK----RKIQDLENRLTKQ- 802
Cdd:pfam10174 535 KLENQLK-KAHNAEEAVRTNPeindriRLLEQEVARYKEESGKAQAEVERLLGILrevENEKndkdKKIAELESLTLRQm 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 803 KEEIELKEQKENVLNNKLKDALVMVEDAQqmKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMK----- 877
Cdd:pfam10174 614 KEQNKKVANIKHGQQEMKKKGAQLLEEAR--RREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAekdgh 691
|
250 260
....*....|....*....|....*
gi 568931432 878 --ALQDERESQKhgfeEEISEYKEQ 900
Cdd:pfam10174 692 ltNLRAERRKQL----EEILEMKQE 712
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
667-849 |
4.32e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 45.21 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 667 EHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIgqekSRSEEALEKAQARVreLENHLASQKEALE---NSVAQEK 743
Cdd:NF012221 1549 KHAKQDDAAQNALADKERAEADRQRLEQEKQQQLAAI----SGSQSQLESTDQNA--LETNGQAQRDAILeesRAVTKEL 1622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 744 RKMREMLEAERRKAQ-------------------DLENQL--------TQQKEISENNTYEKLKMRDTLEKEK------- 789
Cdd:NF012221 1623 TTLAQGLDALDSQATyagesgdqwrnpfagglldRVQEQLddakkisgKQLADAKQRHVDNQQKVKDAVAKSEagvaqge 1702
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568931432 790 RKIQDLENRLTKQKEEIELKEQ----KENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLK 849
Cdd:NF012221 1703 QNQANAEQDIDDAKADAEKRKDdalaKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQ 1766
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
730-952 |
8.10e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 8.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 730 SQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQ-QKEIsenntyeklkmrDTLEKEkrkIQDLENRLTKQKEEIE- 807
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEAlQAEI------------DKLQAE---IAEAEAEIEERREELGe 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 808 -LKEQKENVLNNKLKDALVMVED-------AQQMKTTESQRAETLAlKLKETLAELETTKTKMILTDDRLKLQQQSMKAL 879
Cdd:COG3883 91 rARALYRSGGSVSYLDVLLGSESfsdfldrLSALSKIADADADLLE-ELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568931432 880 QDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAGPP 952
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
636-948 |
8.39e-04 |
|
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: 43.73 E-value: 8.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 636 LLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALE 715
Cdd:pfam07888 46 LLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 716 KAQARVRELENHLAS------QKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEK 789
Cdd:pfam07888 126 AHEARIRELEEDIKTltqrvlERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRD 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 790 RKIQDLENRLTKQKEEIELKEQKENVLNNKLKDalvmVEDAQQMKTTESQRAETLALKLKETL------------AELET 857
Cdd:pfam07888 206 TQVLQLQDTITTLTQKLTTAHRKEAENEALLEE----LRSLQERLNASERKVEGLGEELSSMAaqrdrtqaelhqARLQA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 858 TKTKMILTDDRLKLQQQSMKALQdERESQKHGFEEEiseyKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDT 937
Cdd:pfam07888 282 AQLTLQLADASLALREGRARWAQ-ERETLQQSAEAD----KDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNR 356
|
330
....*....|.
gi 568931432 938 GPKEEASQDLT 948
Cdd:pfam07888 357 VQLSESRRELQ 367
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
11-93 |
8.90e-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: 40.30 E-value: 8.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 11 FFVLNKSTTIG-----------KHADSDLVLqSADIDNHHALIEFNEAEGTFVLQDFnSRNGTFVNE--CHIQNVAVKLI 77
Cdd:cd22701 12 YYVQKLEVVLGrnsknssstaaDSVDIDLGP-SKKISRRHARIFYDFTTQCFELSVL-GRNGVKVDGilVKPGSPPVPLR 89
|
90
....*....|....*.
gi 568931432 78 PGDILRFGSAGMTYEL 93
Cdd:cd22701 90 SGSLIQIGGVLFYFLL 105
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
705-863 |
9.33e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.54 E-value: 9.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 705 QEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEIsenntyeklkmrdt 784
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQ-------------- 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568931432 785 LEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQmkttesqrAETLALKLKETLAELETTKTKMI 863
Cdd:PRK12705 93 LDARAEKLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTP--------EQARKLLLKLLDAELEEEKAQRV 163
|
|
| FHA_Rv1747-like_rpt2 |
cd22737 |
second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
20-92 |
9.56e-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: 39.79 E-value: 9.56e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568931432 20 IGKHADSDLVLQSADIDNHHALIEfnEAEGTFVLQDFNSRNGTFVNECHIQnvAVKLIPGDILRFGSAGMTYE 92
Cdd:cd22737 25 IGRASDNDIVIPEGSVSRHHATLV--PTPGGTQIRDLRSTNGTFVNGLRVD--AALLHDGDVVTIGDIDFVFE 93
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
666-796 |
9.65e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 42.95 E-value: 9.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 666 QEHLAEKEKLAEKLEQEEK--LKAK--IQQLTEEKAALEESIGQ-------------EKSRSEEALEKAQARVRELENHL 728
Cdd:cd16269 145 QLYLEDREKLVEKYRQVPRkgVKAEevLQEFLQSKEAEAEAILQadqaltekekeieAERAKAEAAEQERKLLEEQQREL 224
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568931432 729 ASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEiSENNTYEKLKMRDTLEKEKRKIQDLE 796
Cdd:cd16269 225 EQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERALESKL-KEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
319-808 |
9.95e-04 |
|
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227569 [Multi-domain] Cd Length: 669 Bit Score: 43.52 E-value: 9.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 319 TEIESLKNEGENLKR----DHAITSGMVTSLQKDMSA-RNEQVQQLQEEVNRLRIENREKEYQLEALSSRCSVMKEELRK 393
Cdd:COG5244 130 EEIVELRRENEELDKinlsLRERISSEEPELNKDGSKlSYDELKEFVEESRVQVYDMVELVSDISETLNRNGSIQRSSVR 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 394 EEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELK------KNYMGQNIISKTLREKNKVEEKLQEDSRRKLLQLQEM 467
Cdd:COG5244 210 ECERSNIHDVLFLVNGILDGVIDELNGELERLRRQLVslmsshGIEVEENSRLKATLEKFQSLELKVNTLQEELYQNKLL 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 468 GNRENLIKINLERAVGQLENFRNQVIKAT-FGKTKPFRDKPITDQQL-IEKIIQVTEDNLSFQQRKWTLQRETHLHP--- 542
Cdd:COG5244 290 KKFYQIYEPFAQAALSSQLQYLAEVIESEnFGKLENIEIHIILKVLSsISYALHIYTIKNTPDHLETTLQCFVNIAPism 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 543 --KQEETMHSVEKLRVLLDKCQAcMRDSCSSIDLKK------EVELLQHLPLSPLVSGLQKTVVNILRVSLSWLEETEQL 614
Cdd:COG5244 370 wlSEFLQRKFSSKQETAFSICQF-LEDNKDVTLILKilhpilETTVPKLLAFLRTNSNFNDNDTLCLIGSLYEIARIDKL 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 615 LGDLDIELSDSDKG-FSLCLIYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKakiQQLT 693
Cdd:COG5244 449 IGKEEISKQDNRLFlYPSCDITLSSILTILFSDKLEVFFQGIESLLENITIFPEQPSQQTSDSENIKENSLLS---DRLN 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 694 EEKAALEESIGQEKSRSEEALEKAQARVRELENhlASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISEN 773
Cdd:COG5244 526 EENIRLKEVLVQKENMLTEETKIKIIIGRDLER--KTLEENIKTLKVELNNKNNKLKEENFNLVNRLKNMELKLYQIKDN 603
|
490 500 510
....*....|....*....|....*....|....*
gi 568931432 774 NTYEKLKMrdTLEKEKRKIQDLENRLTKQKEEIEL 808
Cdd:COG5244 604 NTLNKIYL--DLVSEIMELRETIRRQIKEQKRVSI 636
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
649-934 |
1.00e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 44.05 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 649 DLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEK----LKAKIQQLTEEKAALEESIGQE----------------KS 708
Cdd:PTZ00440 956 NLKMQIEKTLEYYDKSKENINGNDGTHLEKLDKEKDewehFKSEIDKLNVNYNILNKKIDDLikkqhddiielidkliKE 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 709 RSEEALEKAQARVRELEN--------HLASQKEALENSVAQEK-RKMREMLEAERRKAQDLENQLTQQKEISENNTY--- 776
Cdd:PTZ00440 1036 KGKEIEEKVDQYISLLEKmktklssfHFNIDIKKYKNPKIKEEiKLLEEKVEALLKKIDENKNKLIEIKNKSHEHVVnad 1115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 777 -EKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNN----KLKDALVMVEDAQQMKTTESQRAETLALKLKET 851
Cdd:PTZ00440 1116 kEKNKQTEHYNKKKKSLEKIYKQMEKTLKELENMNLEDITLNEvneiEIEYERILIDHIVEQINNEAKKSKTIMEEIESY 1195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 852 LAELETTKTKMILTD----DRLKLQQQSMKALQDERE----SQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQ 923
Cdd:PTZ00440 1196 KKDIDQVKKNMSKERndhlTTFEYNAYYDKATASYENieelTTEAKGLKGEANRSTNVDELKEIKLQVFSYLQQVIKENN 1275
|
330
....*....|.
gi 568931432 924 KIEGEITTLKN 934
Cdd:PTZ00440 1276 KMENALHEIKN 1286
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
15-85 |
1.16e-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: 40.03 E-value: 1.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568931432 15 NKSTTIGKHADS--DLVLQ-SADIDNHHALIEFNeAEGTFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFG 85
Cdd:cd22663 20 GKEVTVGRGLGVtyQLVSTcPLMISRNHCVLKKN-DEGQWTIKDNKSLNGVWVNGERIEpLKPYPLNEGDLIQLG 93
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
641-903 |
1.32e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 641 KKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQAR 720
Cdd:COG1340 11 EELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 721 VRELENHLASQKEalENSVAQEKRKMREMLEAERRKAQ------DLENQLTQQ-KEISenntyEKLKMRDTLEKEKRKIQ 793
Cdd:COG1340 91 REELDELRKELAE--LNKAGGSIDKLRKEIERLEWRQQtevlspEEEKELVEKiKELE-----KELEKAKKALEKNEKLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 794 DLENRLTKQKEEI-ELKEQKENVLN--NKLKDALV-MVEDAQQMKttesQRAETLALKLKETLAELETTKTKMILTDDRL 869
Cdd:COG1340 164 ELRAELKELRKEAeEIHKKIKELAEeaQELHEEMIeLYKEADELR----KEADELHKEIVEAQEKADELHEEIIELQKEL 239
|
250 260 270
....*....|....*....|....*....|....*
gi 568931432 870 -KLQQQSMKALQDERESQKHGFEEEISEYKEQIKQ 903
Cdd:COG1340 240 rELRKELKKLRKKQRALKREKEKEELEEKAEEIFE 274
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
666-802 |
2.03e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 666 QEHLAEKEKLAEKLE-----------QEEKLKAKIQQLTEEKAALEESIGQeksrseeaLEKAQARVRELENHLASQKEA 734
Cdd:COG4913 667 EREIAELEAELERLDassddlaaleeQLEELEAELEELEEELDELKGEIGR--------LEKELEQAEEELDELQDRLEA 738
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568931432 735 LENSVAQEkrkMREMLEaERRKAQDLENqltQQKEISENntyeklkMRDTLEKEKRKIQDLENRLTKQ 802
Cdd:COG4913 739 AEDLARLE---LRALLE-ERFAAALGDA---VERELREN-------LEERIDALRARLNRAEEELERA 792
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
649-915 |
2.25e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 649 DLQAQMNASRETQKSLRQEHLAEKEKLA---------EKLEQ-EEKLKAKIQQLTEEKAALEESIGQeKSRSEEALEKAQ 718
Cdd:PRK04863 311 EMARELAELNEAESDLEQDYQAASDHLNlvqtalrqqEKIERyQADLEELEERLEEQNEVVEEADEQ-QEENEARAEAAE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 719 ARVRELENHLASQKEALEnsvAQEKR--------------------------KMREMLEAERRKAQDLENQLTQ--QK-- 768
Cdd:PRK04863 390 EEVDELKSQLADYQQALD---VQQTRaiqyqqavqalerakqlcglpdltadNAEDWLEEFQAKEQEATEELLSleQKls 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 769 ---------------------EISENN----------TYEKLKMRD-TLEKEKRKIQDLENRLTKQKEEIELKEQKENVL 816
Cdd:PRK04863 467 vaqaahsqfeqayqlvrkiagEVSRSEawdvarellrRLREQRHLAeQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRL 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 817 NNKLKDALV----------MVEDAQQMKTTESQRAETLALKLKET---LAELETTKTKMILTDDRL-KLQQQS------- 875
Cdd:PRK04863 547 GKNLDDEDEleqlqeeleaRLESLSESVSEARERRMALRQQLEQLqarIQRLAARAPAWLAAQDALaRLREQSgeefeds 626
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 568931432 876 ------MKALQD-ERESQ--KHGFEEEISEYKEQIKQHSQTIVSLEERL 915
Cdd:PRK04863 627 qdvteyMQQLLErERELTveRDELAARKQALDEEIERLSQPGGSEDPRL 675
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
671-794 |
2.47e-03 |
|
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues of a family of proteins of unknown function possibly containing a coiled-coil domain.
Pssm-ID: 401633 [Multi-domain] Cd Length: 304 Bit Score: 41.74 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 671 EKEKLAEKLEQEEK-----LKAKIQQLTEEKAALEESIGQEKSRseealekaqarvreLENHLASQKEALENSVAQEKRK 745
Cdd:pfam09755 93 EKETLAMNYEQEEEfltndLSRKLTQLRQEKVELEQTLEQEQEY--------------QVNKLMRKIEKLEAETLNKQTN 158
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568931432 746 mremLEAERRKAQDLENQLTQQKEISENNTYEKLkmrDTLEKEKRKIQD 794
Cdd:pfam09755 159 ----LEQLRREKVELENTLEQEQEALVNRLWKRM---DKLEAEKRLLQE 200
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
658-894 |
2.56e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 658 RETQKSLRQEHLAEKEKLAEKLEQEEK-LKAKIQQLTEEKAALEESIGQEK---SRSEEALEKAQARVRELENHLASQKE 733
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKeLEKKHQQLCEEKNALQEQLQAETelcAEAEEMRARLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 734 ALE------NSVAQEKRKMREMLeaerrkaQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIE 807
Cdd:pfam01576 83 RLEeeeersQQLQNEKKKMQQHI-------QDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 808 LKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLK---ETLAELETTKTKMILTDDRLKLQQQSMKALQDERE 884
Cdd:pfam01576 156 LLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKkeeKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELR 235
|
250
....*....|
gi 568931432 885 SQKHGFEEEI 894
Cdd:pfam01576 236 AQLAKKEEEL 245
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
248-469 |
2.68e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 248 LQAEVADLSQRLSETAAVAAARQsnrcdpklqgvdegdDLRQ-----KEIESMKSQINALQKGYSQvLSQTLAERNTEIE 322
Cdd:PRK11281 41 VQAQLDALNKQKLLEAEDKLVQQ---------------DLEQtlallDKIDRQKEETEQLKQQLAQ-APAKLRQAQAELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 323 SLKNEG-ENLKRDHAITSgmVTSLQKDMSARNEQVQQLQEEVNrlrienrekEY--QLEALSSrcsvmkeelRKEEAQKD 399
Cdd:PRK11281 105 ALKDDNdEETRETLSTLS--LRQLESRLAQTLDQLQNAQNDLA---------EYnsQLVSLQT---------QPERAQAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568931432 400 RREAQEkelklcRSQmqdmekevrKLREELKKNYMGQNIISKTLREKNKVEEKL---QEDSRRKLL----QLQEMGN 469
Cdd:PRK11281 165 LYANSQ------RLQ---------QIRNLLKGGKVGGKALRPSQRVLLQAEQALlnaQNDLQRKSLegntQLQDLLQ 226
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
777-908 |
3.03e-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: 41.06 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 777 EKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENvlnnKLKDALVMVEDAQQMK------TTESQRAETLALKLKE 850
Cdd:COG1579 39 ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK----KYEEQLGNVRNNKEYEalqkeiESLKRRISDLEDEILE 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 568931432 851 TLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTI 908
Cdd:COG1579 115 LMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
727-934 |
3.21e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 727 HLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLtqQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEI 806
Cdd:PRK05771 32 HIEDLKEELSNERLRKLRSLLTKLSEALDKLRSYLPKL--NPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 807 -ELKEQKENVLNNK-----LKDALVMVEDAQQMKTT--------ESQRAETLALKLKETLAELETTKTKM--ILTDDRLK 870
Cdd:PRK05771 110 sELENEIKELEQEIerlepWGNFDLDLSLLLGFKYVsvfvgtvpEDKLEELKLESDVENVEYISTDKGYVyvVVVVLKEL 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568931432 871 LQQQsmkalqdERESQKHGFEE-EISEykeqIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKN 934
Cdd:PRK05771 190 SDEV-------EEELKKLGFERlELEE----EGTPSELIREIKEELEEIEKERESLLEELKELAK 243
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
662-814 |
3.28e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 662 KSLRQEHLAEKEKLAEKLEQEEKLKA------KIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEAL 735
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAeaikkeALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 736 EnsvaqekrKMREMLEAERRKAQDLENQLTQQKEisennTYEKL--KMRDTLEK-------EKRKI--QDLENRLTKQK- 803
Cdd:PRK12704 106 E--------KREEELEKKEKELEQKQQELEKKEE-----ELEELieEQLQELERisgltaeEAKEIllEKVEEEARHEAa 172
|
170
....*....|....
gi 568931432 804 ---EEIElKEQKEN 814
Cdd:PRK12704 173 vliKEIE-EEAKEE 185
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
289-937 |
3.51e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.96 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 289 QKEIESMKSQINALQKGYSQVLSQTLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSAR-NEQVQQLQEEVNRLR 367
Cdd:TIGR01612 798 QINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKEKiDSEHEQFAELTNKIK 877
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 368 IENREK-----EYQLEALSSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEK---EVRKLREELKKNYmgqnii 439
Cdd:TIGR01612 878 AEISDDklndyEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEYIKICENTKESIEKfhnKQNILKEILNKNI------ 951
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 440 sKTLREKNKVEEKLQEDSRRKLLQlqemgNRENLIKINLERAVGQLENFRNQVI------KATFGKTK------PFRDKP 507
Cdd:TIGR01612 952 -DTIKESNLIEKSYKDKFDNTLID-----KINELDKAFKDASLNDYEAKNNELIkyfndlKANLGKNKenmlyhQFDEKE 1025
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 508 ITDQQLIEKIIQVTEDNLSFQqrkwtLQRETHLHPKQEETMHSVEKLRVLLDKcQACMRDSCSSIDLKKEVELLQHLPLS 587
Cdd:TIGR01612 1026 KATNDIEQKIEDANKNIPNIE-----IAIHTSIYNIIDEIEKEIGKNIELLNK-EILEEAEINITNFNEIKEKLKHYNFD 1099
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 588 PLVSglqktvvnilRVSLSWLEETEQLLGDLDIELSDSDKGFSlcliYLLEHYKKIMSQSQDLQAQMNASRE-TQKSLRQ 666
Cdd:TIGR01612 1100 DFGK----------EENIKYADEINKIKDDIKNLDQKIDHHIK----ALEEIKKKSENYIDEIKAQINDLEDvADKAISN 1165
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 667 EHLAEKEKLAEKL-----------EQEEKLKAKIQQLTEEKAALE------------------ESIGQEKSRSEEALEKA 717
Cdd:TIGR01612 1166 DDPEEIEKKIENIvtkidkkkniyDEIKKLLNEIAEIEKDKTSLEevkginlsygknlgklflEKIDEEKKKSEHMIKAM 1245
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 718 QARVRELENhLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQK-------------EISENNtYEKLKMRD- 783
Cdd:TIGR01612 1246 EAYIEDLDE-IKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKhdenisdirekslKIIEDF-SEESDINDi 1323
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 784 --TLEKEKRKIQDLENRLTKQKEEIE-----LKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAeLE 856
Cdd:TIGR01612 1324 kkELQKNLLDAQKHNSDINLYLNEIAniyniLKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDIN-LE 1402
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 857 TTKTKMILTDDRLKLQQqsmkALQDERESQKHGFEEE--ISEYKEQIKQHSQTIVSL---EERLCQVTQYYQKIEgeitt 931
Cdd:TIGR01612 1403 ECKSKIESTLDDKDIDE----CIKKIKELKNHILSEEsnIDTYFKNADENNENVLLLfknIEMADNKSQHILKIK----- 1473
|
....*.
gi 568931432 932 lKNNDT 937
Cdd:TIGR01612 1474 -KDNAT 1478
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
743-1047 |
3.67e-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: 42.03 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 743 KRKMREMLEAERRKAQDLENQLTQQKEISENNTY------------------EKLKMRDTLEKEKRKIQDLENRLTKQKE 804
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFylrqsvidlqtklqemqmERDAMADIRRRESQSQEDLRNQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 805 EIE-LKEQKENVLNnklkDALVMVEDAQQMKTTEsqraETLALKLKETLAELETTKTKMILTDDrlKLQQQSMKALQDER 883
Cdd:pfam15921 153 ELEaAKCLKEDMLE----DSNTQIEQLRKMMLSH----EGVLQEIRSILVDFEEASGKKIYEHD--SMSTMHFRSLGSAI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 884 ESQKHGFEEEISEYK----------EQIKQHSQTIVSLeerlcQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAGPPL 953
Cdd:pfam15921 223 SKILRELDTEISYLKgrifpvedqlEALKSESQNKIEL-----LLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSI 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 954 DSgdkeiacdhlidDLLMAQKEILSQQEIIMKLRTDLgeaHSRMSDLRGELSEKQKM------ELERQVALVRQQSGELS 1027
Cdd:pfam15921 298 QS------------QLEIIQEQARNQNSMYMRQLSDL---ESTVSQLRSELREAKRMyedkieELEKQLVLANSELTEAR 362
|
330 340
....*....|....*....|
gi 568931432 1028 MLKAKVAQTTGLMEKKDREL 1047
Cdd:pfam15921 363 TERDQFSQESGNLDDQLQKL 382
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
681-887 |
3.76e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 681 QEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQA-RVRELENHLASQKEALENSVAQEKRKMREmLEAERRKAQD 759
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfRQKNGLVDLSEEAKLLLQQLSELESQLAE-ARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 760 LENQLTQQ--------KEISENNTYEKLkmRDTLEKEKRKIQDLENRLTKQKEEI-ELKEQKENVLNNKLKdalvmvEDA 830
Cdd:COG3206 241 RLAALRAQlgsgpdalPELLQSPVIQQL--RAQLAELEAELAELSARYTPNHPDViALRAQIAALRAQLQQ------EAQ 312
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568931432 831 QQMKTTESQRaETLALKLKETLAELETTKTKMiltdDRLKLQQQSMKALQDERESQK 887
Cdd:COG3206 313 RILASLEAEL-EALQAREASLQAQLAQLEARL----AELPELEAELRRLEREVEVAR 364
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
223-490 |
4.24e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.64 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 223 LLGREVNRLSDFEMESKYKDALIMNLQAEVADlSQRLSETAAVAAARQSNRCDPKLQGV----DEGDDLR--QKEIESMK 296
Cdd:pfam15921 476 MLRKVVEELTAKKMTLESSERTVSDLTASLQE-KERAIEATNAEITKLRSRVDLKLQELqhlkNEGDHLRnvQTECEALK 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 297 SQinalqkgysqvlsqtLAERNTEIESLKNEGENLKR---DHAITSGmvtSLQKDMSARNEQVQQLQEEVNRLRIENREK 373
Cdd:pfam15921 555 LQ---------------MAEKDKVIEILRQQIENMTQlvgQHGRTAG---AMQVEKAQLEKEINDRRLELQEFKILKDKK 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 374 EYQLEALSSRCSVMK-----------EELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVrklrEELKKNYmgqniiskt 442
Cdd:pfam15921 617 DAKIRELEARVSDLElekvklvnagsERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDY----EVLKRNF--------- 683
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 568931432 443 lreKNKVEeklqedsrrkllqlqEMGNRENLIKINLERAVGQLENFRN 490
Cdd:pfam15921 684 ---RNKSE---------------EMETTTNKLKMQLKSAQSELEQTRN 713
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
641-759 |
4.51e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.95 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 641 KKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKlAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQAR 720
Cdd:PRK09510 83 KKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQ-KKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAK 161
|
90 100 110
....*....|....*....|....*....|....*....
gi 568931432 721 VRELENHLASQKEALENSVAQEKRKMREmlEAERRKAQD 759
Cdd:PRK09510 162 KAAAEAKKKAEAEAAKKAAAEAKKKAEA--EAAAKAAAE 198
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
671-925 |
4.52e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.95 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 671 EKEKLAEKLEQE-EKLKAKIQQLTEEKAALEESIGQ-EKSRSE--EALEKAQARVRELENhlasQKEAleNSVAQEKRKM 746
Cdd:pfam15905 91 EQDKRLQALEEElEKVEAKLNAAVREKTSLSASVASlEKQLLEltRVNELLKAKFSEDGT----QKKM--SSLSMELMKL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 747 REMLEAERRKAQDLENQLTQQKEISENNtyeklkmrdtLEKEKRKIQDLENRL-TKQKEEIELKEQKENVLNNKLKdaLV 825
Cdd:pfam15905 165 RNKLEAKMKEVMAKQEGMEGKLQVTQKN----------LEHSKGKVAQLEEKLvSTEKEKIEEKSETEKLLEYITE--LS 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 826 MVEDAQQMKTTESQRAETLalkLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKhgfEEEISEYKEQIKQHS 905
Cdd:pfam15905 233 CVSEQVEKYKLDIAQLEEL---LKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEK---EELLREYEEKEQTLN 306
|
250 260
....*....|....*....|
gi 568931432 906 QTIVSLEERLCQVTQYYQKI 925
Cdd:pfam15905 307 AELEELKEKLTLEEQEHQKL 326
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
663-764 |
4.68e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 663 SLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIG---------QEKSRSEEALEKAQARVRELENHLASQKE 733
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQaasdhlnlvQTALRQQEKIERYQADLEELEERLEEQNE 369
|
90 100 110
....*....|....*....|....*....|....*
gi 568931432 734 ALENsvAQEkrkMREMLEAERRKAQ----DLENQL 764
Cdd:PRK04863 370 VVEE--ADE---QQEENEARAEAAEeevdELKSQL 399
|
|
| FHA_EmbR-like |
cd22669 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis transcriptional ... |
18-92 |
4.68e-03 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis transcriptional regulatory protein EmbR and similar proteins; EmbR is a transcriptional regulator of the embCAB operon encoding cell wall arabinosyltransferases (EmbC, -A, and -B), and is phosphorylated by the cognate mycobacterial serine/threonine protein kinase PknH. It interacts with RNA polymerase and possesses a phosphorylation-dependent ATPase activity. EmbR contains a regulatory C-terminal forkhead-associated (FHA) domain, which mediates binding to a threonine-phosphorylated site in PknH. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438721 [Multi-domain] Cd Length: 89 Bit Score: 37.78 E-value: 4.68e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568931432 18 TTIGKHADSDLVLQSADIDNHHALIefNEAEGTFVLQDFNSRNGTFVNECHIQNVAVkLIPGDILRFGSAGMTYE 92
Cdd:cd22669 18 TRIGRLHDNDIVLDSANVSRHHAVI--VDTGTNYVINDLRSSNGVHVQHERIRSAVT-LNDGDHIRICDHEFTFQ 89
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
635-843 |
4.73e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 40.47 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 635 YLLEHYKKIMSQSQDLQAQMNASretqKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEAL 714
Cdd:pfam06008 27 QLQEYLSPENAHKIQIEILEKEL----SSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEIN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 715 EKA--------QARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQL-TQQKEISENNTYEKLKMRDTL 785
Cdd:pfam06008 103 EKVatlgendfALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRIqTWFQSPQEENKALANALRDSL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568931432 786 EKEKRKIQDLENRLtkqkEEIELKEQKENVLNNKLKDALVMVEdaQQMKTTESQRAET 843
Cdd:pfam06008 183 AEYEAKLSDLRELL----REAAAKTRDANRLNLANQANLREFQ--RKKEEVSEQKNQL 234
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
590-879 |
5.26e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.60 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 590 VSGLQKTVvnILRVSLSWLEETEQLLGDLDIELSDSD--KGFSLCLIYLLEHYKKIMSQS--QDLQAQMNASRETQKSLR 665
Cdd:COG5022 861 FSLLKKET--IYLQSAQRVELAERQLQELKIDVKSISslKLVNLELESEIIELKKSLSSDliENLEFKTELIARLKKLLN 938
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 666 QEHLAE--------KEKLAEKLEQEEKLKakiqQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLaSQKEALEN 737
Cdd:COG5022 939 NIDLEEgpsieyvkLPELNKLHEVESKLK----ETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELS-KQYGALQE 1013
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 738 SVAQEKRKMREMLEAerrkaqdlenqltqqkeiseNNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEeiELKEQKENVLN 817
Cdd:COG5022 1014 STKQLKELPVEVAEL--------------------QSASKIISSESTELSILKPLQKLKGLLLLENN--QLQARYKALKL 1071
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568931432 818 NKlKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDD---RLKLQQQSMKAL 879
Cdd:COG5022 1072 RR-ENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVAqmiKLNLLQEISKFL 1135
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
289-399 |
5.56e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 289 QKEIESMKSQINALQKgYSQVLSQTLAERNTEIESLKNEGENLKRdhaitsgmvtSLQKDMSARNEqVQQLQEEVNRLRI 368
Cdd:COG2433 412 EEEIRRLEEQVERLEA-EVEELEAELEEKDERIERLERELSEARS----------EERREIRKDRE-ISRLDREIERLER 479
|
90 100 110
....*....|....*....|....*....|.
gi 568931432 369 ENREKEYQLEALSSRCSVMKeELRKEEAQKD 399
Cdd:COG2433 480 ELEEERERIEELKRKLERLK-ELWKLEHSGE 509
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
609-917 |
5.87e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 609 EETEQLLGDLDIELSDSDKgfslCLIYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAK 688
Cdd:pfam01576 71 QELEEILHELESRLEEEEE----RSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 689 IQQLTEEKAALEESIGQEKSRSEEALEKAQArVRELENHLASQKEALENSVAQEKRKMREMLEAERR---KAQDLENQLT 765
Cdd:pfam01576 147 NSKLSKERKLLEERISEFTSNLAEEEEKAKS-LSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKlegESTDLQEQIA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 766 -QQKEISEnntyeklkMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTtesqRAETL 844
Cdd:pfam01576 226 eLQAQIAE--------LRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARN----KAEKQ 293
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568931432 845 ALKLKEtlaELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQ----HSQTIVSLEERLCQ 917
Cdd:pfam01576 294 RRDLGE---ELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEmrqkHTQALEELTEQLEQ 367
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
637-736 |
6.00e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 41.20 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 637 LEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQE--EKLKAKIQQLTEEKAALEESIG---QEKSRSE 711
Cdd:pfam13166 357 LDSVDAKIESINDLVASINELIAKHNEITDNFEEEKNKAKKKLRLHlvEEFKSEIDEYKDKYAGLEKAINsleKEIKNLE 436
|
90 100
....*....|....*....|....*
gi 568931432 712 EALEKAQARVRELENHLASQKEALE 736
Cdd:pfam13166 437 AEIKKLREEIKELEAQLRDHKPGAD 461
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
663-764 |
6.74e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.09 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 663 SLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIG---------QEKSRSEEALEKAQARVRELENHLASQKE 733
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQaasdhlnlvQTALRQQEKIERYQEDLEELTERLEEQEE 368
|
90 100 110
....*....|....*....|....*....|....*
gi 568931432 734 ALENsvAQEKrkmREMLEAERRKAQD----LENQL 764
Cdd:COG3096 369 VVEE--AAEQ---LAEAEARLEAAEEevdsLKSQL 398
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
342-1060 |
7.21e-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: 41.11 E-value: 7.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 342 VTSLQKDMSARNEQVQQLQEEVNRLRIENRE--KEYQLEALSSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDME 419
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEElkLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 420 KEVRKLREELKKNYMGQNIISKTLREKNKV------EEKLQE------DSRRKLLQLQEMGNRENLIKINLERAVGQLEN 487
Cdd:pfam02463 244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKEnkeeekEKKLQEeelkllAKEEEELKSELLKLERRKVDDEEKLKESEKEK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 488 FRNQVIKATFGKTKPFRDKPITDQQLIEKIIQVTEDNLSFQQRKWTLQRETHLHPKQEETMHSVEKLRVLLDKCQACMRD 567
Cdd:pfam02463 324 KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 568 SCSSIDLKKEVELLQHLPLSPLVSGLQKTVVNILRVSLSWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKiMSQS 647
Cdd:pfam02463 404 EKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQ-LVKL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 648 QDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEK--------------SRSEEA 713
Cdd:pfam02463 483 QEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKvaistavivevsatADEVEE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 714 LEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQ 793
Cdd:pfam02463 563 RQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAK 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 794 DLENRLTKQKEEIELKEQKenvlnNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQ 873
Cdd:pfam02463 643 AKESGLRKGVSLEEGLAEK-----SEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 874 QSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVS--------LEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQ 945
Cdd:pfam02463 718 EAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKsrlkkeekEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLK 797
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 946 DLTAGP-PLDSGDKEIACDHLIDDLLMAQKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQKMELERQVALVRQQSG 1024
Cdd:pfam02463 798 AQEEELrALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEE 877
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 568931432 1025 EL----SMLKAKVAQTTGLMEKKDRELKVLREALRASQEK 1060
Cdd:pfam02463 878 ELeeqkLKDELESKEEKEKEEKKELEEESQKLNLLEEKEN 917
|
|
| FHA_DgcB-like |
cd22682 |
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ... |
11-86 |
7.54e-03 |
|
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: 37.51 E-value: 7.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 11 FFVLNKSTTIGKHADSDLVLQSADIDNHHALIEFNEAEGTfvLQDFNSRNGTFVN--------ECHIQNvavklipGDIL 82
Cdd:cd22682 15 FPITESTIVIGRSVESQVQIDDDSVSRYHAKLAVNPSAVS--IIDLGSTNGTIVNgkkipklaSCDLQN-------GDQI 85
|
....
gi 568931432 83 RFGS 86
Cdd:cd22682 86 KIGN 89
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
630-763 |
8.31e-03 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 39.03 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 630 SLCLIYLL---EHYKKIMSQSQDLQAQMNASRETQKslrQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQE 706
Cdd:pfam06785 47 SLCLLLLLyywEDALKEKFEKSFLEEKEAKLTELDA---EGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQL 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 568931432 707 KSRSEEALEKAQARVRELENHLAsQKEALENSVAQEKRKMREMLEAERRKAQDLENQ 763
Cdd:pfam06785 124 QIQLQQISQDFAEFRLESEEQLA-EKQLLINEYQQTIEEQRSVLEKRQDQIENLESK 179
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
639-934 |
8.38e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 40.61 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 639 HYKKIMSQSQDLQAQMNASRETQKSLRQEhlaekekLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQ 718
Cdd:pfam06160 80 RFKKAKKALDEIEELLDDIEEDIKQILEE-------LDELLESEEKNREEVEELKDKYRELRKTLLANRFSYGPAIDELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 719 ARVRELE-------------NHLASQK--EALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEisennTYEKLKMR- 782
Cdd:pfam06160 153 KQLAEIEeefsqfeeltesgDYLEAREvlEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKE-----GYREMEEEg 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 783 ---DTLEKEKRkIQDLENRLTKQKEEI---ELKEQKENVLN-----NKLKDALVMVEDAQQ-----MKTTESQRAETLAl 846
Cdd:pfam06160 228 yalEHLNVDKE-IQQLEEQLEENLALLenlELDEAEEALEEieeriDQLYDLLEKEVDAKKyveknLPEIEDYLEHAEE- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 847 KLKETLAELETTKTKMILTDDRLKLQQQsmkaLQDERESQKHGFEeeisEYKEQIKQHSQTIVSLEERLCQVTQYYQKIE 926
Cdd:pfam06160 306 QNKELKEELERVQQSYTLNENELERVRG----LEKQLEELEKRYD----EIVERLEEKEVAYSELQEELEEILEQLEEIE 377
|
....*...
gi 568931432 927 GEITTLKN 934
Cdd:pfam06160 378 EEQEEFKE 385
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
215-465 |
8.56e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.66 E-value: 8.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 215 QDKDEIILLLGR-EVNRLSDFEMESKYKDALimnlQAEVADLSQRLSETAA---VAAARQSNrcdpklqgVDEGDDLRQK 290
Cdd:PLN02939 138 QNAEKNILLLNQaRLQALEDLEKILTEKEAL----QGKINILEMRLSETDArikLAAQEKIH--------VEILEEQLEK 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 291 EIESMKSQInALQKGYSQVLSQTLAERNTEIESLKNEGENLKR---DHAITSGMVTSLQKDMSARNEQVQQLQEEVnrlr 367
Cdd:PLN02939 206 LRNELLIRG-ATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAeliEVAETEERVFKLEKERSLLDASLRELESKF---- 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 368 IENREKEYQLEALSSRCsvMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELK--KNYMGQNIISKTLRE 445
Cdd:PLN02939 281 IVAQEDVSKLSPLQYDC--WWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKeaNVSKFSSYKVELLQQ 358
|
250 260
....*....|....*....|.
gi 568931432 446 KNK-VEEKLQEDSRRKLLQLQ 465
Cdd:PLN02939 359 KLKlLEERLQASDHEIHSYIQ 379
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
636-812 |
9.56e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.44 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 636 LLEHYKKIMSQSQDLQAQMNASRETQKSLRQEH------LAEKEKLA------EKLEQEEKLKAKIQQLTEEKAALEESI 703
Cdd:COG0497 156 LLEEYREAYRAWRALKKELEELRADEAERARELdllrfqLEELEAAAlqpgeeEELEEERRRLSNAEKLREALQEALEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568931432 704 GQEKSRSEEALEKAQARVRELENH---LASQKEALENS------VAQEKRKMREMLEAERRKAQDLENQLTQQKEISE-- 772
Cdd:COG0497 236 SGGEGGALDLLGQALRALERLAEYdpsLAELAERLESAlieleeAASELRRYLDSLEFDPERLEEVEERLALLRRLARky 315
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568931432 773 NNTYEKL-KMRDTLEKEKRKIQDLENRLTKQKEEIELKEQK 812
Cdd:COG0497 316 GVTVEELlAYAEELRAELAELENSDERLEELEAELAEAEAE 356
|
|
| |
