|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
2-97 |
1.03e-48 |
|
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: 1.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 2 KAYLKSADGFFVLN-KSTTIGKHaDSDLVLQSADIDNHHALIEFNEAEGTFVLQDFNSRNGTFVNECHIQNVAVKLIPGD 80
Cdd:cd22700 1 KGYLKSSDGIFQLDpKVTTIGRE-GCDLVLQSPGVEEQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAPGD 79
|
90
....*....|....*..
gi 1720409123 81 ILRFGSAGMTYELVIEN 97
Cdd:cd22700 80 VLRFGFGGLPYELVVDN 96
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
18-84 |
2.05e-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: 2.05e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720409123 18 TTIGKHADSDLVLQSADIDNHHALIEFNEaEGTFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRF 84
Cdd:pfam00498 1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDG-GGRFYLEDLGSTNGTFVNGQRLGPEPVRLKDGDVIRL 66
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
11-92 |
6.73e-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: 6.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 11 FFVLNKSTTIGKHADSDLVLQSADIDNHHALIEFNeaEGTFVLQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGMT 90
Cdd:cd00060 14 FPLTKGVVTIGRSPDCDIVLDDPSVSRRHARIEVD--GGGVYLEDLGSTNGTFVNGKRITP-PVPLQDGDVIRLGDTTFR 90
|
..
gi 1720409123 91 YE 92
Cdd:cd00060 91 FE 92
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
12-93 |
1.40e-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: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 12 FVLNKS-TTIGKHADSDLVLQSADIDNHHALIEFNeaEGTFVLQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGMT 90
Cdd:COG1716 16 FPLDGGpLTIGRAPDNDIVLDDPTVSRRHARIRRD--GGGWVLEDLGSTNGTFVNGQRVTE-PAPLRDGDVIRLGKTELR 92
|
...
gi 1720409123 91 YEL 93
Cdd:COG1716 93 FRL 95
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
285-973 |
2.36e-16 |
|
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: 85.11 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 285 DDLRQKEIESMKSQINALQKGYSQVLSQtLAERNTEIESLKNEGENLKRDHAItsgmvtsLQKDMSARNEQVQQLQEEVN 364
Cdd:TIGR02168 220 AELRELELALLVLRLEELREELEELQEE-LKEAEEELEELTAELQELEEKLEE-------LRLEVSELEEEIEELQKELY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 365 RLRIENREKEYQLEALSSRCSVMKEELRKEEAQ----KDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNYMGQNIIS 440
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLANLERQLEELEAQleelESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 441 KTLREKNKVEEKLQEDSRRKLLQLQEMGNRENLIKINLERAVGQLENFRNQVIKATFGKTKPFRDK-----PITDQQRQH 515
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaelEELEEELEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 516 LRACIPPHRARTCAPTLQSLPRRAGCLETSYCLSSGQLIEKIIQVTEDNLSFQQR---KWTLQRE--THLHPKQEETMHS 590
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEgvkALLKNQSglSGILGVLSELISV 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 591 VEKLR-------------VLLDKCQACMRDscssIDLKKEVELLQHLPLsPLVSGLQKTVVNILRVSLSWLEETEQLLGD 657
Cdd:TIGR02168 532 DEGYEaaieaalggrlqaVVVENLNAAKKA----IAFLKQNELGRVTFL-PLDSIKGTEIQGNDREILKNIEGFLGVAKD 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 658 LDielsDSDKGFSLCLIYLLEHYKKIMS--QSQDLQAQMNAS---------------RETQKSLRQEH--LAEKEKLAEK 718
Cdd:TIGR02168 607 LV----KFDPKLRKALSYLLGGVLVVDDldNALELAKKLRPGyrivtldgdlvrpggVITGGSAKTNSsiLERRREIEEL 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 719 LEQEEKLKAKIQQLTEEKAALEesigQEKSRSEEALEKAQARVRELENHLASQKEALENsVAQEKRKMREMLEAERRKAQ 798
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELR----KELEELEEELEQLRKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELT 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 799 DLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEI-----ELKEQKENVLN--NKLKDALVMVEDAQ 871
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALdelraELTLLNEEAANlrERLESLERRIAATE 837
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 872 QMKTTESQRAETLAL---KLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTI 948
Cdd:TIGR02168 838 RRLEDLEEQIEELSEdieSLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
730 740
....*....|....*....|....*
gi 1720409123 949 VSLEERLCQVTQYYQKIEGEITTLK 973
Cdd:TIGR02168 918 EELREKLAQLELRLEGLEVRIDNLQ 942
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
686-934 |
3.30e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.52 E-value: 3.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 686 QSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEksrsEEALEKAQARVRELE 765
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL----EEELEELEEELEEAE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 766 NHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENntyeklkmRDTLEKEKRKIQDLENRLTKQKEE 845
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL--------AAQLEELEEAEEALLERLERLEEE 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 846 IELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKmILTDDRLKLQQQSMKALQDERES 925
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA-LAELLEELAEAAARLLLLLEAEA 501
|
....*....
gi 1720409123 926 QKHGFEEEI 934
Cdd:COG1196 502 DYEGFLEGV 510
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
213-943 |
1.12e-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: 79.72 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 213 SQQDKDEIILLLGREVNRLSDFEMESKYKDALIMN----LQAEVADLSQRLSETAAVAAAR--QSNRCDPKLQGVDEGDD 286
Cdd:TIGR02168 282 EIEELQKELYALANEISRLEQQKQILRERLANLERqleeLEAQLEELESKLDELAEELAELeeKLEELKEELESLEAELE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 287 LRQKEIESMKSQINALQKGYSQV------LSQTLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSarNEQVQQLQ 360
Cdd:TIGR02168 362 ELEAELEELESRLEELEEQLETLrskvaqLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 361 EEVNRLRIENREKEYQLEALSSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNYMGQNIIS 440
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 441 K---TLREKNKVEEKLqedsrRKLLQLQEMGNRENLIKINLERAVGQLENFR-NQVIKATF-------GKTKPFRDKPIT 509
Cdd:TIGR02168 520 GilgVLSELISVDEGY-----EAAIEAALGGRLQAVVVENLNAAKKAIAFLKqNELGRVTFlpldsikGTEIQGNDREIL 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 510 DQQRQHLRACIPPhraRTCAPTLQSLprragcleTSYCLSSGQLIEKIIQVTED--NLSFQQRKWTLQREThLHP----- 582
Cdd:TIGR02168 595 KNIEGFLGVAKDL---VKFDPKLRKA--------LSYLLGGVLVVDDLDNALELakKLRPGYRIVTLDGDL-VRPggvit 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 583 -KQEETMHSVEKLRVLLDKCQACMRDSCSSIDLKKevellqhlplsplvsglqkTVVNILRVSLSWLEETEQLLGDLDIE 661
Cdd:TIGR02168 663 gGSAKTNSSILERRREIEELEEKIEELEEKIAELE-------------------KALAELRKELEELEEELEQLRKELEE 723
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 662 LSDSDKGFSLCLIYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALee 741
Cdd:TIGR02168 724 LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL-- 801
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 742 sigqeksrsEEALEKAQARVRELENHLASQKEALENSVAQekrkmremLEAERRKAQDLENQLTQQKEISENNTYEKLKM 821
Cdd:TIGR02168 802 ---------REALDELRAELTLLNEEAANLRERLESLERR--------IAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 822 RDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTK 901
Cdd:TIGR02168 865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1720409123 902 MiltDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQ 943
Cdd:TIGR02168 945 L---SEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
25-93 |
2.44e-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: 2.44e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 25 DSDLVLQSADIDNHHALIEFNEAEGTFVLQDFNSRNGTFVNECHI-QNVAVKLIPGDILRFGSAGMTYEL 93
Cdd:cd22704 25 DCDLILQSRSVDKQHAVITYDQIDNEFKIKDLGSLNGTFVNDSRIpEQTYITLKLGDSIRFGYDTNVYRF 94
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
677-1389 |
3.46e-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: 74.71 E-value: 3.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 677 LEHYKKIMSQSQDLQAQMNASRETQKSLRQEHL-AEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQ---EKSRSEE 752
Cdd:TIGR02168 202 LKSLERQAEKAERYKELKAELRELELALLVLRLeELREELEELQEELKEAEEELEELTAELQELEEKLEElrlEVSELEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 753 ALEKAQAR-------VRELENHLASQKEALENSVAQEKRKMREMLEAERRKaQDLENQLTQQKEISENNTYEKLKMRDTL 825
Cdd:TIGR02168 282 EIEELQKElyalaneISRLEQQKQILRERLANLERQLEELEAQLEELESKL-DELAEELAELEEKLEELKEELESLEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 826 EKEKRKIQDLENRLTKQKEEIE-------LKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKEtlAELETT 898
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLEtlrskvaQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE--AELKEL 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 899 KTKMILTDDRLKLQQQSMKALQDERESQKHGFEE---EISEYKEQIKQHSQTIVSLEERLCQVTQYYqkiEGEITTLKNN 975
Cdd:TIGR02168 439 QAELEELEEELEELQEELERLEEALEELREELEEaeqALDAAERELAQLQARLDSLERLQENLEGFS---EGVKALLKNQ 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 976 DTGPKEEAS-QDLTAGPPLDSGDKEIACDHLIDDLLMAQKEilSQQEIIMKLR-TDLGEAH-SRMSDLRGELSEKQKMEL 1052
Cdd:TIGR02168 516 SGLSGILGVlSELISVDEGYEAAIEAALGGRLQAVVVENLN--AAKKAIAFLKqNELGRVTfLPLDSIKGTEIQGNDREI 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1053 ERQVALVRQQSGELSMLKAKVAQTTGLMEKKDRELKVLREALrasqekprphlstEQKPRTLSQKCDISLQIEPAHPDSF 1132
Cdd:TIGR02168 594 LKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNAL-------------ELAKKLRPGYRIVTLDGDLVRPGGV 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1133 SSFQ-EEQSFSDLGVKCKGSRHEETIQRQRKALSELRTRVRELEKANScNHKDHVNESFLELRTLRMEKNVQKILLDAKp 1211
Cdd:TIGR02168 661 ITGGsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELE-ELEEELEQLRKELEELSRQISALRKDLARL- 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1212 dLTTLARVEIRPPQNSPFNSGSTLVMEKSVKTDAGEALELSEKLytDMIKTLGSLMNiKDMSSHTSLKHLSPKEREKVNH 1291
Cdd:TIGR02168 739 -EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE--AEIEELEAQIE-QLKEELKALREALDELRAELTL 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1292 LRQKDLDLVFdKITQLKTRLQRKEELLKGYEQELEQLRH--SKVSVQM--YQTQVAKLEDDVHKEAEEKALLKEALERTE 1367
Cdd:TIGR02168 815 LNEEAANLRE-RLESLERRIAATERRLEDLEEQIEELSEdiESLAAEIeeLEELIEELESELEALLNERASLEEALALLR 893
|
730 740
....*....|....*....|..
gi 1720409123 1368 QQLSQERRFNRVFKQQKDRGED 1389
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRR 915
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
673-927 |
3.64e-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: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 673 LIYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHL---AEKEKLAEKLEQEEK----LKAKIQQLTEEKAALEESI-- 743
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAeleAELEELRLELEELELeleeAQAEEYELLAELARLEQDIar 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 744 -GQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTyEKLKMR 822
Cdd:COG1196 307 lEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE-ELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 823 DTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKM 902
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260
....*....|....*....|....*
gi 1720409123 903 ILTDDRLKLQQQSMKALQDERESQK 927
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAA 490
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
224-903 |
4.76e-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: 74.33 E-value: 4.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 224 LGREVNRLSDFEMeskykdaliMNLQAEVADLS--QRLSETAAVAAARQSNRCDPKLQGVDEGDDLRQKEIESMKSQINA 301
Cdd:TIGR02169 277 LNKKIKDLGEEEQ---------LRVKEKIGELEaeIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 302 LQKGYSQvLSQTLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLE--- 378
Cdd:TIGR02169 348 ERKRRDK-LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELAdln 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 379 -----------ALSSRCSVMKEELRKEEAQ----KDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNYMGQNIISKTL 443
Cdd:TIGR02169 427 aaiagieakinELEEEKEDKALEIKKQEWKleqlAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 444 REKNKVEEKLQEDSRRKLLQLQEMGNRENLIKINLERAVGqleNFRNQVIKATFGKTKpfrdKPIT-DQQRQHLRACIPP 522
Cdd:TIGR02169 507 RGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAG---NRLNNVVVEDDAVAK----EAIElLKRRKAGRATFLP 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 523 HRARTCAPTLQSLPRRAGCletsyclssgqlIEKIIQVTEDNLSFQQRKWTLQRETHLHPKQEETMHSVEKLRV------ 596
Cdd:TIGR02169 580 LNKMRDERRDLSILSEDGV------------IGFAVDLVEFDPKYEPAFKYVFGDTLVVEDIEAARRLMGKYRMvtlege 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 597 LLDKCQACM--RDSCSSIDLKKEVELLQHLPLSPLVSGLQKTvvniLRVSLSWLEETEQLLGDLDIELSDSDKGFSLcli 674
Cdd:TIGR02169 648 LFEKSGAMTggSRAPRGGILFSRSEPAELQRLRERLEGLKRE----LSSLQSELRRIENRLDELSQELSDASRKIGE--- 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 675 yllehykkIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQ-EKSRSEEA 753
Cdd:TIGR02169 721 --------IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlEARLSHSR 792
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 754 LEKAQARVRELENHLASQKEALENSVAQEKRK--MREMLEAERRKAQDLENQLTQQK-----EISENNTyEKLKMRDTLE 826
Cdd:TIGR02169 793 IPEIQAELSKLEEEVSRIEARLREIEQKLNRLtlEKEYLEKEIQELQEQRIDLKEQIksiekEIENLNG-KKEELEEELE 871
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720409123 827 KEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDA-QQMKTTESQRAEtlalkLKETLAELETTKTKMI 903
Cdd:TIGR02169 872 ELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKrKRLSELKAKLEA-----LEEELSEIEDPKGEDE 944
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
214-1072 |
8.33e-13 |
|
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: 73.47 E-value: 8.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 214 QQDKDEIILLLGREVNRLSDFEMESKYKDALIMNLQAEVADLSQRlsetaavaAARQSNRCDPKLQGVDEGDDLRQKEIE 293
Cdd:pfam02463 183 ENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLL--------YLDYLKLNEERIDLLQELLRDEQEEIE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 294 SMKSQINALQKGYSQVLsQTLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIE-NRE 372
Cdd:pfam02463 255 SSKQEIEKEEEKLAQVL-KENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKElKKE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 373 KEYQLEALSSrcsvMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKnymGQNIISKTLREKNKVE-- 450
Cdd:pfam02463 334 KEEIEELEKE----LKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSS---AAKLKEEELELKSEEEke 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 451 -EKLQEDSRRKLLQLQEMGNRENLIKINLERAVGQLENFRNQVIKATFGKTKPFRDKPITDQQRQHLRA---CIPPHRAR 526
Cdd:pfam02463 407 aQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKetqLVKLQEQL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 527 TCAPTLQSLPRRAGCLETSYCLSSGQLIEKIIQVTEDNLSFQQRKWTLQ-----RETHLHPKQEETMHSVEKLRVLLDKC 601
Cdd:pfam02463 487 ELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGvavenYKVAISTAVIVEVSATADEVEERQKL 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 602 QACMRDSCSSIDLKKEVELLQHLPLSPLVSGLQKTVVNILRVSLSWLEETEQLLGdldiELSDSDKGFSLCLIYLLEHYK 681
Cdd:pfam02463 567 VRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKR----AKVVEGILKDTELTKLKESAK 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 682 KIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQE----EKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKA 757
Cdd:pfam02463 643 AKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEkaesELAKEEILRRQLEIKKKEQREKEELKKLKLEAEEL 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 758 QARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQ--KEISENNTYEKLKMRDTLEKEKRKIQDL 835
Cdd:pfam02463 723 LADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKekELAEEREKTEKLKVEEEKEEKLKAQEEE 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 836 ENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQS 915
Cdd:pfam02463 803 LRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQ 882
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 916 MKalqDERESQKHGFEEEISEYKEQIKQHSQTIVSLEErlcqvtqyyqKIEGEITTLKNNDTGPKEEasqdltagPPLDS 995
Cdd:pfam02463 883 KL---KDELESKEEKEKEEKKELEEESQKLNLLEEKEN----------EIEERIKEEAEILLKYEEE--------PEELL 941
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720409123 996 GDKEIACDHLIDDLLMAQKEILSQQEIIMKLRTDLGEAHSRMSDLRgELSEKQKMELERQVALVRQQSGELSMLKAK 1072
Cdd:pfam02463 942 LEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKE-ERYNKDELEKERLEEEKKKLIRAIIEETCQ 1017
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
292-1094 |
1.60e-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: 72.78 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 292 IESMKSQINALQKgysqvlsQtlAERNTEIESLKNEGENLkrDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENR 371
Cdd:TIGR02168 195 LNELERQLKSLER-------Q--AEKAERYKELKAELREL--ELALLVLRLEELREELEELQEELKEAEEELEELTAELQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 372 EKEYQLEALSSRCSVMKEELrkeeaqkdrrEAQEKELKLCRSQMQDMEKEVRKLREELKKNYMGQNIISKTLREKNKVEE 451
Cdd:TIGR02168 264 ELEEKLEELRLEVSELEEEI----------EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 452 KLQEDSRRKLLQLQEMGNRENLIKINLERAVGQLENFRNQVIKATFGKTKPFRDKPITDQQRQHLRAcipphRARTCAPT 531
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN-----EIERLEAR 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 532 LQSLPRRAGCLETSYCLSSGQLIEKIIQVTEDNLSfqqrkwTLQRETH-LHPKQEETMHSVEKLRVLLDKCQACMRDSCS 610
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLKKLEEAELKELQAELE------ELEEELEeLQEELERLEEALEELREELEEAEQALDAAER 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 611 SID-LKKEVELLQHLPLSplVSGLQKTVVNILRvSLSWLEETEQLLGDLdIElsdSDKGFSLCL-IYLLEHYKKIMS--- 685
Cdd:TIGR02168 483 ELAqLQARLDSLERLQEN--LEGFSEGVKALLK-NQSGLSGILGVLSEL-IS---VDEGYEAAIeAALGGRLQAVVVenl 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 686 ----QSQDLQAQMNASRETQKSLRQEHLAEKE-KLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRS------EEAL 754
Cdd:TIGR02168 556 naakKAIAFLKQNELGRVTFLPLDSIKGTEIQgNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVlvvddlDNAL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 755 EKA-----QARVRELENHLAS------QKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEklkMRD 823
Cdd:TIGR02168 636 ELAkklrpGYRIVTLDGDLVRpggvitGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEE---LEE 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 824 TLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETtktkmi 903
Cdd:TIGR02168 713 ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE------ 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 904 ltddrlklQQQSMKALQDERESQkhgfEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNdtgpKEEA 983
Cdd:TIGR02168 787 --------LEAQIEQLKEELKAL----REALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ----IEEL 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 984 SQDLtAGPPLDSGDKEIACDHLIDDLLMAQKEILSQQEIIMKLR-------TDLGEAHSRMSDLRGELSEKQ----KMEL 1052
Cdd:TIGR02168 851 SEDI-ESLAAEIEELEELIEELESELEALLNERASLEEALALLRseleelsEELRELESKRSELRRELEELReklaQLEL 929
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 1720409123 1053 ERQVALVR----------QQSGELSMLKAKVAQTTGLMEKKDRELKVLREAL 1094
Cdd:TIGR02168 930 RLEGLEVRidnlqerlseEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
714-955 |
3.59e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 714 KLAEKLEQEEKLKAKIQQLTEEKAALEEsigqEKSRSEEALEKAQARVRELENHLASQKEAlENSVAQEKRKMREMLEAE 793
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEA----ELAELEAELEELRLELEELELELEEAQAE-EYELLAELARLEQDIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 794 RRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDAlvmvEDAQQM 873
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA----EEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 874 KTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEE 953
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
..
gi 1720409123 954 RL 955
Cdd:COG1196 464 LL 465
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
716-990 |
7.26e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 7.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 716 AEKLEQEEKLKAKIQQLTEEKAALE--------ESIGQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMR 787
Cdd:COG1196 209 AEKAERYRELKEELKELEAELLLLKlreleaelEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 788 EMLEAERRKAQdLENQLTQQKEISENNtyeklkmRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMV 867
Cdd:COG1196 289 EEYELLAELAR-LEQDIARLEERRREL-------EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 868 EDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQkhgfEEEISEYKEQIKQHSQT 947
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL----EEELEELEEALAELEEE 436
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1720409123 948 IVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAG 990
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
698-985 |
8.41e-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: 70.47 E-value: 8.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 698 RETQKSLR--QEHLA-------EKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIG----QEKSRSEEALEKAQARVREL 764
Cdd:TIGR02168 175 KETERKLErtRENLDrledilnELERQLKSLERQAEKAERYKELKAELRELELALLvlrlEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 765 ENHLASQKEALENSVAQEKRKMREM----------LEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQD 834
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELeeeieelqkeLYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 835 LENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQ 914
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720409123 915 SMKALQDERESQKHGFEE-EISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQ 985
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
12-92 |
9.21e-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: 9.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 12 FVLNK-STTIGKHADSDLVLQSADIDNHHALIEFneAEGTFVLQDFNSRNGTFVNECHI--QNVAVKLIPGDILRFGSAG 88
Cdd:cd22665 16 FPLYEgENVIGRDPSCSVVLPDKSVSKQHACIEV--DGGTHLIEDLGSTNGTRIGNKVRlkPNVRYELIDGDLLLFGDVK 93
|
....
gi 1720409123 89 MTYE 92
Cdd:cd22665 94 CQYV 97
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
249-839 |
1.34e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 249 QAEVA----DLSQRLSETAAVAAARQsnrcdpklqgvdegDDLRQKEIESMKSQINALQKGySQVLSQTLAERNTEIESL 324
Cdd:COG1196 208 QAEKAeryrELKEELKELEAELLLLK--------------LRELEAELEELEAELEELEAE-LEELEAELAELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 325 KNEGENLKRDhaitsgmVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSRCSVMKEELRKEEAQKDRREAQ 404
Cdd:COG1196 273 RLELEELELE-------LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 405 EKELKLCRSQMQDMEKEVRKLREELKKNymgQNIISKTLREKNKVEEKLQEDSRRKLLQLQEMGNRENLIKINLERAVGQ 484
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAE---LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 485 LENFRNQVIKAtfgktkpfRDKPITDQQRQHLRACippHRARTCAPTLQSLPRRAGCLEtsyclSSGQLIEKIIQVTEDN 564
Cdd:COG1196 423 LEELEEALAEL--------EEEEEEEEEALEEAAE---EEAELEEEEEALLELLAELLE-----EAALLEAALAELLEEL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 565 LSFQQRKWTLQREthlhpkQEETMHSVEKLRVLLDKCQACMRDSCSSIDLKKEVELLQHLPLSPLVSGLQKTV------- 637
Cdd:COG1196 487 AEAAARLLLLLEA------EADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVeddevaa 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 638 ------------------VNILRVSLSWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQDLQAQMNASRE 699
Cdd:COG1196 561 aaieylkaakagratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 700 TQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEALEnsv 779
Cdd:COG1196 641 TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERL--- 717
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 780 aQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRL 839
Cdd:COG1196 718 -EEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
697-973 |
3.06e-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: 68.56 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 697 SRETQKSLR-QEHLAEKEKLA--EKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKE 773
Cdd:TIGR02169 204 RREREKAERyQALLKEKREYEgyELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 774 ALENSVAQEKRKMREmLEAERRKAQD----LENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELK 849
Cdd:TIGR02169 284 LGEEEQLRVKEKIGE-LEAEIASLERsiaeKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAEL 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 850 EQKENVLNNKLKDalvMVEDAQQMKTTESQRAETLAlKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHG 929
Cdd:TIGR02169 363 KEELEDLRAELEE---VDKEFAETRDELKDYREKLE-KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE 438
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1720409123 930 FEE-------EISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLK 973
Cdd:TIGR02169 439 LEEekedkalEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
12-86 |
5.54e-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: 5.54e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720409123 12 FVLNKST-TIGKHADSDLVLQSADIDNHHALIEFNEaeGTFVLQDFNSRNGTFVNECHIqNVAVKLIPGDILRFGS 86
Cdd:cd22693 13 FPIDKSGiTIGRADDNDLVLSDDFVSSRHARIYLQG--SSWYLEDLGSTNGTFVNGNRV-TQPVVVQPGDTIRIGA 85
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
711-1110 |
9.01e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.09 E-value: 9.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 711 EKEKLAEKLEQEEKLKAKIQQL---TEEKAALEESI--GQEKSRSEEALEKAQARvRELENhlaSQKEALENSVAQEKRK 785
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAkkkAEEKKKADEAKkkAEEAKKADEAKKKAEEA-KKAEE---AKKKAEEAKKADEAKK 1477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 786 MREmleaERRKAQDLENQLTQQKEISEN--NTYEKLKMRDTLEK--EKRKIQDLENRLTKQKEEiELKEQKENVLNNKLK 861
Cdd:PTZ00121 1478 KAE----EAKKADEAKKKAEEAKKKADEakKAAEAKKKADEAKKaeEAKKADEAKKAEEAKKAD-EAKKAEEKKKADELK 1552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 862 DALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQI 941
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 942 KQHSQTIVSLEERLCQVTQYyqKIEGEITTLKNNDTGPKEEASQDLTAGPPLDSGDKEIACDHLIDDLLMAQK-EILSQQ 1020
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEEL--KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKaEELKKK 1710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1021 EIIMKLRTDLGEAHSRMSDLRGELSEKQKMELERQVALVRQQSGElsmlKAKVAQTTGLMEKKDRELK-----VLREALR 1095
Cdd:PTZ00121 1711 EAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE----KKKIAHLKKEEEKKAEEIRkekeaVIEEELD 1786
|
410
....*....|....*
gi 1720409123 1096 ASQEKPRPHLSTEQK 1110
Cdd:PTZ00121 1787 EEDEKRRMEVDKKIK 1801
|
|
| FHA_DUN1-like |
cd22683 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ... |
17-85 |
2.24e-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: 2.24e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720409123 17 STTIGKHADSDLVLQSADIDNHHALIEFnEAEGTFVLqDFNSRNGTFVNECHIQNVAVKLIPGDILRFG 85
Cdd:cd22683 22 VTTIGRSRSCDLVLSDPSISRFHAELRL-EQNGINVI-DNNSANGTFINGKRIKGKTYILKNGDIIVFG 88
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
678-1375 |
3.36e-10 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 64.99 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 678 EHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKA 757
Cdd:pfam02463 286 EELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQ 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 758 QARVRELENHLASQKEALENSVAQEKRKMREMLEAER-RKAQDLENQLTQQKEISENNtyEKLKMRDTLEKEKRKIQDLE 836
Cdd:pfam02463 366 EKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEeEKEAQLLLELARQLEDLLKE--EKKEELEILEEEEESIELKQ 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 837 NRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELET--------TKTKMILTDDR 908
Cdd:pfam02463 444 GKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKarsglkvlLALIKDGVGGR 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 909 LKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLT 988
Cdd:pfam02463 524 IISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPIL 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 989 AGPPLDSGDKEIACDH-------LIDDLLMAQKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQkMELERQVALVRQ 1061
Cdd:pfam02463 604 NLAQLDKATLEADEDDkrakvveGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSE-LTKELLEIQELQ 682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1062 QSGELSMLKAKVAQTTGLMEKKD----RELKVLREALRASQEKPRPHLSTEQKPRTLSQKCDISLQIEPAHPDSFSSFQE 1137
Cdd:pfam02463 683 EKAESELAKEEILRRQLEIKKKEqrekEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEK 762
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1138 EQSFSDLGVKCKGSRHEETIQRQRKALSELRTRVRELEK-----ANSCNHKDHVNESFLELRTLRMEKNVQKILLDAKPD 1212
Cdd:pfam02463 763 EEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEelralEEELKEEAELLEEEQLLIEQEEKIKEEELEELALEL 842
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1213 LTTLARVEIRPpQNSPFNSGSTLVMEKSVKTDAGEALELSEKLYTDMIKTLGSLMNIKDMSSHTSLKHLSPKEREKVNHL 1292
Cdd:pfam02463 843 KEEQKLEKLAE-EELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEE 921
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1293 RQKDLDLVFDKITQLKTRLQRKEELLKGYEQE-LEQLRHSKVSVQMYQTQVAKLEDDVHKEAEEKALLKEALERTEQQLS 1371
Cdd:pfam02463 922 RIKEEAEILLKYEEEPEELLLEEADEKEKEENnKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLE 1001
|
....
gi 1720409123 1372 QERR 1375
Cdd:pfam02463 1002 EEKK 1005
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
644-1099 |
1.08e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 644 SLSWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQDLQAQMNASRETQKsLRQEHLAEKEKLAEKLEQEE 723
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKK-KLKELEKRLEELEERHELYE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 724 KLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREmLEAERRKAQDLENQ 803
Cdd:PRK03918 366 EAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE-LKKAKGKCPVCGRE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 804 LTQQKEISENNTYeKLKMRDtLEKEKRKIQDLENRLTKQKEEIELKEQKENVLnnklkdaLVMVEDAQQMKTTESQRAET 883
Cdd:PRK03918 445 LTEEHRKELLEEY-TAELKR-IEKELKEIEEKERKLRKELRELEKVLKKESEL-------IKLKELAEQLKELEEKLKKY 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 884 LALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQD------ERESQKHGFEEEISEYKEQIKQHS-QTIVSLEERLC 956
Cdd:PRK03918 516 NLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkklaELEKKLDELEEELAELLKELEELGfESVEELEERLK 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 957 QVTQYYQkiegEITTLKNndtGPKEeasqdltagppLDSGDKEIacDHLIDDLLMAQKEILSQQEIIMKLRTDLGEAHSR 1036
Cdd:PRK03918 596 ELEPFYN----EYLELKD---AEKE-----------LEREEKEL--KKLEEELDKAFEELAETEKRLEELRKELEELEKK 655
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1037 MSDLRGELSEKQKMELERQVALVRQQSGELSMLKAKVAQT-------TGLMEKKDRELKVLREALRASQE 1099
Cdd:PRK03918 656 YSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTleklkeeLEEREKAKKELEKLEKALERVEE 725
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
213-846 |
1.10e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.55 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 213 SQQDKDEIILLLGREVNRLSDFEMESKYKDAL---IMNLQAEVADLSQRLSETAAVAAARqsnrcdpklqgVDEGDDlRQ 289
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLteeYAELKEELEDLRAELEEVDKEFAET-----------RDELKD-YR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 290 KEIESMKSQINALQKGYSQvLSQTLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIE 369
Cdd:TIGR02169 392 EKLEKLKREINELKRELDR-LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 370 NREKEYQLEALSSRCSVMKEELRKEEAQkdrreaqekelklcRSQMQDMEKEVRKLREELKKNYMGqniISKTLREKNKV 449
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKLQRELAEAEAQ--------------ARASEERVRGGRAVEEVLKASIQG---VHGTVAQLGSV 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 450 EEKLQ----------------ED----------------SRRKLLQLQEMGNRENLI-KINLERAVGQLEN-------FR 489
Cdd:TIGR02169 534 GERYAtaievaagnrlnnvvvEDdavakeaiellkrrkaGRATFLPLNKMRDERRDLsILSEDGVIGFAVDlvefdpkYE 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 490 NqVIKATFGKTKPFRD----KPITDQQRQ-----------------HLRACIPPHRARTCAPTLQSLPRRAGCL--ETSY 546
Cdd:TIGR02169 614 P-AFKYVFGDTLVVEDieaaRRLMGKYRMvtlegelfeksgamtggSRAPRGGILFSRSEPAELQRLRERLEGLkrELSS 692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 547 CLSSGQLIEKIIQVTEDNLSFQQRKW-TLQRETHLHPKQEETMHS-VEKLRVLLDKCQACMRDSCSSI-DLKKEVELLQ- 622
Cdd:TIGR02169 693 LQSELRRIENRLDELSQELSDASRKIgEIEKEIEQLEQEEEKLKErLEELEEDLSSLEQEIENVKSELkELEARIEELEe 772
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 623 -----HLPLSPLVSGLQKTVVNILRVSLSWLEET----EQLLGDLDIELSDSDkgfslcliyLLEHYKKimSQSQDLQAQ 693
Cdd:TIGR02169 773 dlhklEEALNDLEARLSHSRIPEIQAELSKLEEEvsriEARLREIEQKLNRLT---------LEKEYLE--KEIQELQEQ 841
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 694 MNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQ---EKSRSEEALEKAQARVRELENHLAS 770
Cdd:TIGR02169 842 RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEleaQLRELERKIEELEAQIEKKRKRLSE 921
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 771 QKEALENSVAQEK----------------------RKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKE 828
Cdd:TIGR02169 922 LKAKLEALEEELSeiedpkgedeeipeeelsledvQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEE 1001
|
730
....*....|....*...
gi 1720409123 829 KRKIQDLENRLTKQKEEI 846
Cdd:TIGR02169 1002 RKAILERIEEYEKKKREV 1019
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
678-1037 |
1.21e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 678 EHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQ--EEKLKAK-IQQLTEEKAALEESI--GQEKSRSEE 752
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKkaEEAKKAEeAKKKAEEAKKADEAKkkAEEAKKADE 1487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 753 ALEKAQ---ARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEK-- 827
Cdd:PTZ00121 1488 AKKKAEeakKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKae 1567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 828 EKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVE------------DAQQMKTTESQRAETLALKLKETLAEL 895
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKaeeakkaeeakiKAEELKKAEEEKKKVEQLKKKEAEEKK 1647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 896 ETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYK-EQIKQHSQTIVSLEERLCQVTQYYQKIEG-----EI 969
Cdd:PTZ00121 1648 KAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAaEALKKEAEEAKKAEELKKKEAEEKKKAEElkkaeEE 1727
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720409123 970 TTLKNNDTGPKEEASQDLTAGPPLDSGDKEiACDHLIDDLLMAQKEILSQQEIIMKLRTDLGEAHSRM 1037
Cdd:PTZ00121 1728 NKIKAEEAKKEAEEDKKKAEEAKKDEEEKK-KIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRM 1794
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
17-85 |
1.49e-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: 1.49e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720409123 17 STTIGKHADSDLVLQSADIDNHHALIEFneAEGTFVLQDFNSRNGTFVNECHIQnvAVKLIPGDILRFG 85
Cdd:cd22694 17 SVRIGRDPDADVRLDDPRVSRRHALLEF--DGDGWVYTDLGSRNGTYLNGRRVQ--QVKLSDGTRVRLG 81
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
639-1073 |
3.12e-09 |
|
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: 61.57 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 639 NILRVSLSWLEETEQLLGDLDIELSDSDKGFSLcliyLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEK 718
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKSLESQISELKKQNNQ----LKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 719 LEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKaqarvrELENHLASQKEALENSVAQekrkmremLEAERRKAQ 798
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNK------ELKSELKNQEKKLEEIQNQ--------ISQNNKIIS 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 799 DLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLEN----------RLTKQKEEIELKEQKENVLNNKLKDALVMVE 868
Cdd:TIGR04523 339 QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKenqsykqeikNLESQINDLESKIQNQEKLNQQKDEQIKKLQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 869 DAQQMKTTESQRAETLALKLKETLAELETTKTKMILT----DDRLKLQQQSMKALQDERESQKHGFEE----------EI 934
Cdd:TIGR04523 419 QEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIiknlDNTRESLETQLKVLSRSINKIKQNLEQkqkelkskekEL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 935 SEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAgppLDSGDKEIACDHL---IDDLLM 1011
Cdd:TIGR04523 499 KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFE---LKKENLEKEIDEKnkeIEELKQ 575
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720409123 1012 AQKEILSQQEiimKLRTDLGEAHSRMSDLRGELSEK--QKMELERQVALVRQQSGELSMLKAKV 1073
Cdd:TIGR04523 576 TQKSLKKKQE---EKQELIDQKEKEKKDLIKEIEEKekKISSLEKELEKAKKENEKLSSIIKNI 636
|
|
| FHA_Ki67 |
cd22673 |
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ... |
11-92 |
4.93e-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: 4.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 11 FFVLNKSTTIGKHADSDLVLQSADIDNHHALIEFNEaEGTFVLQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGMT 90
Cdd:cd22673 16 FPLTKKSCTFGRDLSCDIRIQLPGVSREHCRIEVDE-NGKAYLENLSTTNPTLVNGKAIEK-SAELKDGDVITIGGRSFR 93
|
..
gi 1720409123 91 YE 92
Cdd:cd22673 94 FE 95
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
710-1062 |
1.14e-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: 60.08 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 710 AEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEkAQARVRELENHLasqkealensVAQEKRKMREM 789
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQA-LLKEKREYEGYE----------LLKEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 790 LEAERRKAQDLENQLTQ-QKEISENNTyEKLKMRDTLEKEKRKIQDL-ENRLTKQKEEIELKEQKENVLNNKLKDALVMV 867
Cdd:TIGR02169 239 KEAIERQLASLEEELEKlTEEISELEK-RLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 868 EDAQ-QMKTTESQRAETLAlKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEE---EISEYKEQIKQ 943
Cdd:TIGR02169 318 EDAEeRLAKLEAEIDKLLA-EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAEtrdELKDYREKLEK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 944 HSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQdltagppldsgdkeiacdhLIDDLLMAQKEILSQQEII 1023
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE-------------------LEEEKEDKALEIKKQEWKL 457
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1720409123 1024 MKLRTDLGEAHSRMSDLRGELS--EKQKMELERQVALVRQQ 1062
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDrvEKELSKLQRELAEAEAQ 498
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
19-181 |
1.28e-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: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 19 TIGKHADSDLVLQSAD--IDNHHALIEFneAEGTFVLQDfNSRNGTFVNECHI---QNVAVKLIPGDILRFGSagmtYEL 93
Cdd:COG3456 29 TIGRSADCDWVLPDPDrsVSRRHAEIRF--RDGAFCLTD-LSTNGTFLNGSDHplgPGRPVRLRDGDRLRIGD----YEI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 94 ---VIENPSPVSCPWVRGPAPWPSPQPHLS--SSPPDMPFHHGIQPATVQRSWSQGCPRPTMVPPAPHQRPMSASGKMFS 168
Cdd:COG3456 102 rveISGEDEGADDPLAAAPEPAVSSPSNLSdtEAAPDAALAFSFSLDPLEALDEAATEAPATADDPPSLLPEDWLPSAAP 181
|
170
....*....|...
gi 1720409123 169 FVMDPKSPVINQV 181
Cdd:COG3456 182 VADEAAAQAIDQL 194
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
685-896 |
1.99e-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: 58.24 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 685 SQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIgqekSRSEEALEKAQARVREL 764
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL----AALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 765 ENHLASQKEALENSVA---QEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTK 841
Cdd:COG4942 96 RAELEAQKEELAELLRalyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720409123 842 QKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETL---ALKLKETLAELE 896
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELqqeAEELEALIARLE 233
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
693-1442 |
2.38e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 693 QMNASRETQKSLRQEHLAEKEKLAE--KLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLAS 770
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTEtgKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 771 QKEALENSVAQEKRKMREMLEAER-RKAQDLEnQLTQQKEISENNTYEKLKMRDTLEK--EKRKIQDLEnRLTKQKEEIE 847
Cdd:PTZ00121 1163 ARKAEEARKAEDAKKAEAARKAEEvRKAEELR-KAEDARKAEAARKAEEERKAEEARKaeDAKKAEAVK-KAEEAKKDAE 1240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 848 LKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAEtlalklkETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQK 927
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE-------EARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE 1313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 928 HGFEEEISEYKEQIKQHSQTIVSLEERlcqvtqyyQKIEGEITTLKNNDTGPKEEASQDLTAGPPLDSGDKEIACDHLid 1007
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAAKKKAEE--------AKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA-- 1383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1008 dllmaqKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQKMELERQVALVRQQSGELSMlKAKVAQTTGLMEKKDREL 1087
Cdd:PTZ00121 1384 ------KKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK-KAEEAKKADEAKKKAEEA 1456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1088 KVLREALRASQEKPRP-HLSTEQKPRTLSQKCDISLQIEPAHPDSFSSFQEEQSFSDLGVKCKGSRHEETIQRqrkalSE 1166
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKAdEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK-----AE 1531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1167 LRTRVRELEKANSCNHKDHVNESfLELRTLRMEKNVQKILLDAKPDLTTLARVEIRPPQNSPFNSGSTLVMEKSVKTDAG 1246
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKADELKKA-EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1247 EAL-ELSEKLYTDMIKtlgslmniKDMSSHTSLKHLSPKEREKVNHLRQKDLDLVFDKITqlKTRLQRKEELLKgyeQEL 1325
Cdd:PTZ00121 1611 EAKkAEEAKIKAEELK--------KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK--AAEEAKKAEEDK---KKA 1677
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1326 EQLRHSKVSVQMYQTQVAKLEDDVHKEAEEKALLKEALERTEqQLSQERRFNRVFKQQKDRGEDPEQRNMSYSPFKDNEK 1405
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE-ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756
|
730 740 750
....*....|....*....|....*....|....*..
gi 1720409123 1406 QRrlFVEMVKSKMQNSSVQAGAKKATLKTGQERETKK 1442
Cdd:PTZ00121 1757 KK--IAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEK 1791
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
702-1194 |
2.57e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 702 KSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQ---EKSRSEEALEKAQARVRELENH------LASQK 772
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEissELPELREELEKLEKEVKELEELkeeieeLEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 773 EALENSVAQEKRKMRE---MLEAERRKAQDLENQLTQQKEISEN-NTYEKL-KMRDTLEKEKRKIQDLENRLTKQKEEIE 847
Cdd:PRK03918 248 ESLEGSKRKLEEKIREleeRIEELKKEIEELEEKVKELKELKEKaEEYIKLsEFYEEYLDELREIEKRLSRLEEEINGIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 848 LKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLAlKLKETLAELETTKTKM-ILTDDRLKLQQQSMKALQDERESQ 926
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLtGLTPEKLEKELEELEKAKEEIEEE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 927 KHGFEEEISEYKEQIKQHSQTIVSLE--ERLCQV-----------------TQYYQKIEGEITTLKNNDTGPKEEASQdl 987
Cdd:PRK03918 407 ISKITARIGELKKEIKELKKAIEELKkaKGKCPVcgrelteehrkelleeyTAELKRIEKELKEIEEKERKLRKELRE-- 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 988 tagppldsgdkeiacdhlIDDLLMAQKEILSQQEIIMKLRtdlgEAHSRMSDLRGELSEKQKMELERQVALVRQQSGELS 1067
Cdd:PRK03918 485 ------------------LEKVLKKESELIKLKELAEQLK----ELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1068 MLKAKVAQTTGLMEKKDRELKVLREAlrasqEKPRPHLSTEQKPRTLSQKCDISLQI---EPAHPDSFSSFQEEQSFSDL 1144
Cdd:PRK03918 543 SLKKELEKLEELKKKLAELEKKLDEL-----EEELAELLKELEELGFESVEELEERLkelEPFYNEYLELKDAEKELERE 617
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1720409123 1145 GVKCKGSRHE-----ETIQRQRKALSELRTRVRELEKANSCNHKDHVNESFLELR 1194
Cdd:PRK03918 618 EKELKKLEEEldkafEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELS 672
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
648-899 |
2.82e-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: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 648 LEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQDLQAQMN---ASRETQKSLRQEHLAEKEKLAEKLE-QEE 723
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKekiGELEAEIASLERSIAEKERELEDAEeRLA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 724 KLKAKIQQLTEEKAALEESIGQEKSRSE---EALEKAQARVRELENHLASQKEALENSVaQEKRKMREMLEAERRKAQDL 800
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDkltEEYAELKEELEDLRAELEEVDKEFAETR-DELKDYREKLEKLKREINEL 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 801 ENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDAlvmvEDAQQMKTTESQR 880
Cdd:TIGR02169 405 KRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY----EQELYDLKEEYDR 480
|
250
....*....|....*....
gi 1720409123 881 AETLALKLKETLAELETTK 899
Cdd:TIGR02169 481 VEKELSKLQRELAEAEAQA 499
|
|
| FHA_GarA_OdhI-like |
cd22684 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium ... |
18-91 |
2.95e-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: 2.95e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720409123 18 TTIGKHADSDLVLQSADIDNHHAliEFNEAEGTFVLQDFNSRNGTFVNECHIQnvAVKLIPGDILRFGSAGMTY 91
Cdd:cd22684 23 TTAGRHPESDIFLDDVTVSRRHA--EFRRAEGGFVVRDVGSLNGTYVNRERID--SAVLRNGDEVQIGKFRLVF 92
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
709-973 |
3.01e-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: 58.54 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 709 LAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEES-IGQEKSRSEEALEKAQARVRELENHLASQKEALENsVAQEKRKMR 787
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAERYQALLKEKREYEGYeLLKEKEALERQKEAIERQLASLEEELEKLTEEISE-LEKRLEEIE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 788 EMLEAERRKAQDL--ENQLTQQKEISENnTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIE-LKEQKENVLN-----NK 859
Cdd:TIGR02169 272 QLLEELNKKIKDLgeEEQLRVKEKIGEL-EAEIASLERSIAEKERELEDAEERLAKLEAEIDkLLAEIEELEReieeeRK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 860 LKDALV-MVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMiltdDRLKLQQQSMKALQDERESQKHGFEEEISEYK 938
Cdd:TIGR02169 351 RRDKLTeEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL----EKLKREINELKRELDRLQEELQRLSEELADLN 426
|
250 260 270
....*....|....*....|....*....|....*
gi 1720409123 939 EQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLK 973
Cdd:TIGR02169 427 AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
254-1054 |
3.04e-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: 58.54 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 254 DLSQRLSETAAVAAARQSNRCDPKLQGVDEGDDLRQKEIESMKSQINALQKGYSQvLSQTLAERNTEIESL-KNEGENLK 332
Cdd:TIGR02169 215 ALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEE-IEQLLEELNKKIKDLgEEEQLRVK 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 333 RDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSRcsvMKEELRKEEAQKDRREAQEKELKLCR 412
Cdd:TIGR02169 294 EKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE---IEEERKRRDKLTEEYAELKEELEDLR 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 413 SQMQDMEKEVRKLREELKKNymgQNIISKTLREKNKveekLQEDSRRKLLQLQEMGNRENLIKINLERAVGQLENFRNQV 492
Cdd:TIGR02169 371 AELEEVDKEFAETRDELKDY---REKLEKLKREINE----LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 493 ------IKATFGKTKPFRDKpITDQQRQHLRacipphrartcaptlqslprragcletsyclssgqlIEKIIQVTEDNLS 566
Cdd:TIGR02169 444 edkaleIKKQEWKLEQLAAD-LSKYEQELYD------------------------------------LKEEYDRVEKELS 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 567 FQQRKWTlQRETHLHPKQEETMHSVEKLRVLLDKCQACMRDSCSSIDLKKEVELLQHLPLSplvSGLQKTVV-------- 638
Cdd:TIGR02169 487 KLQRELA-EAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAG---NRLNNVVVeddavake 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 639 --------NILRVSLSWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMSQsqdlqaqmnASRETQkslrqehla 710
Cdd:TIGR02169 563 aiellkrrKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKY---------VFGDTL--------- 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 711 ekekLAEKLEQEEKLKAKIQQLTEEKAALEES-----------IGQEKSRSEEA-LEKAQARVRELENHLAS---QKEAL 775
Cdd:TIGR02169 625 ----VVEDIEAARRLMGKYRMVTLEGELFEKSgamtggsraprGGILFSRSEPAeLQRLRERLEGLKRELSSlqsELRRI 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 776 ENSVAQEKRKMRE---MLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQK 852
Cdd:TIGR02169 701 ENRLDELSQELSDasrKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEA 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 853 ENVLNNKLKDALVMVEDAQQMKTTESQR----------AETLALKLKETLAELETTKTKMILTDdrLKLQQQSMKALQDE 922
Cdd:TIGR02169 781 LNDLEARLSHSRIPEIQAELSKLEEEVSriearlreieQKLNRLTLEKEYLEKEIQELQEQRID--LKEQIKSIEKEIEN 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 923 RESQKHGFEEEISEYKEQIKQHSQTIVSL-------EERLCQVTQYYQKIEGEITTLKNND---TGPKEEASQDLTA-GP 991
Cdd:TIGR02169 859 LNGKKEELEEELEELEAALRDLESRLGDLkkerdelEAQLRELERKIEELEAQIEKKRKRLselKAKLEALEEELSEiED 938
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720409123 992 PLDSGDKEIACDHLIDDLLMA----QKEILSQQEIIMKLRTDLGEAHSRMSDLRgelSEKQKMELER 1054
Cdd:TIGR02169 939 PKGEDEEIPEEELSLEDVQAElqrvEEEIRALEPVNMLAIQEYEEVLKRLDELK---EKRAKLEEER 1002
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
685-1417 |
3.26e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 58.44 E-value: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 685 SQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEklkakiqqltEEKAALEESIGQEKSRSEEALEKAQARV--R 762
Cdd:pfam02463 237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENK----------EEEKEKKLQEEELKLLAKEEEELKSELLklE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 763 ELENHLASQKEALENSVAQEKRKmremLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKiqdLENRLTKQ 842
Cdd:pfam02463 307 RRKVDDEEKLKESEKEKKKAEKE----LKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQL---EEELLAKK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 843 KEEIELKEQKENVLNNKLKDALVMvEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDE 922
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEE-EKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQEL 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 923 RESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQvtqyyQKIEGEITTLKNNDTGPKEEASQDLTAGPPLDSGDKEIAC 1002
Cdd:pfam02463 459 KLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQ-----KLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGD 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1003 DHLIDDLLMAQKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQKMELERQVALVRQQSGELSmlkakVAQTTGLMEK 1082
Cdd:pfam02463 534 LGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLE-----IDPILNLAQL 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1083 KDRELKVLREALRAsqekprphlsteqKPRTLSQKCDISLQIEPAHPDSFSSFQEEQSFSDLGVKCKGSRHEETIQRQRK 1162
Cdd:pfam02463 609 DKATLEADEDDKRA-------------KVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKEL 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1163 ALSELRTRVRELEKANSCNHKDHVNESFLELRTLRMEKNVQKILLDAKPDLTTLARVEIrPPQNSPFNSGSTLVMEKSVK 1242
Cdd:pfam02463 676 LEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKI-NEELKLLKQKIDEEEEEEEK 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1243 T--DAGEALELSEKLYTDMIKTLGSLMNIKDMSSHTSLKHLSPKEREKVNHLRQKDLdlvfDKITQLKTRLQRKEELLKG 1320
Cdd:pfam02463 755 SrlKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELK----EEAELLEEEQLLIEQEEKI 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1321 YEQELEQLRHSKVSVQMYQTQVAKLEDDVHKEAEEKALLKEALERTEQQLSQERRFNRVFKQQKDRGEDPEQRNMSYSPF 1400
Cdd:pfam02463 831 KEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLN 910
|
730
....*....|....*..
gi 1720409123 1401 KDNEKQRRLFVEMVKSK 1417
Cdd:pfam02463 911 LLEEKENEIEERIKEEA 927
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
699-985 |
3.46e-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: 58.11 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 699 ETQKSLRQEHLAEKEKLAEKLEQE-EKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQArvrelenhLASQKEALEn 777
Cdd:TIGR04523 355 ESENSEKQRELEEKQNEIEKLKKEnQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK--------LQQEKELLE- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 778 svaQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLN 857
Cdd:TIGR04523 426 ---KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLN 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 858 NK----------LKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTD---------DRLKLQQQSMKA 918
Cdd:TIGR04523 503 EEkkeleekvkdLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKeideknkeiEELKQTQKSLKK 582
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720409123 919 LQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQ 985
Cdd:TIGR04523 583 KQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| FHA_Cep170A |
cd22724 |
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar ... |
25-85 |
4.64e-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: 52.67 E-value: 4.64e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720409123 25 DSDLVLQSADIDNHHALIEFNEAEGTFVLQDFNSRNGTFVNECHI-QNVAVKLIPGDILRFG 85
Cdd:cd22724 29 DCELMLQSRSVDKQHAVINYDASTDEHKVKDLGSLNGTFVNDVRIpEQTYITLKLDDKLRFG 90
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
696-926 |
4.67e-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: 57.08 E-value: 4.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 696 ASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIgqekSRSEEALEKAQARVRELENHLAS---QK 772
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI----AALARRIRALEQELAALEAELAElekEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 773 EALENSVAQEKRKMREMLeaerRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQK 852
Cdd:COG4942 93 AELRAELEAQKEELAELL----RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720409123 853 ENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQ 926
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
678-1296 |
6.02e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 6.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 678 EHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQ-EEKLKAKIQQLTEEKAALEES--IGQEKSRSEEAL 754
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAaEEKAEAAEKKKEEAKKKADAAkkKAEEKKKADEAK 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 755 EKAQ---ARVRELENHLASQKEALE-NSVAQEKRKMREMleaeRRKAQDLENQLTQQKEISENNTYEKLKMRdtlEKEKR 830
Cdd:PTZ00121 1398 KKAEedkKKADELKKAAAAKKKADEaKKKAEEKKKADEA----KKKAEEAKKADEAKKKAEEAKKAEEAKKK---AEEAK 1470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 831 KIQDLENRLTKQKEEIELKEQKENVLN--NKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDR 908
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADEAKKKAEEAKKkaDEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADE 1550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 909 LKLQQQSMKALQDERESQKHGFEEEiseyKEQIKQHSQTIVSLEERlcqvtqyyqKIEGEITTLKNNDTGPKEEASQDLT 988
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEED----KNMALRKAEEAKKAEEA---------RIEEVMKLYEEEKKMKAEEAKKAEE 1617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 989 AGPPLDSGDKEIACDHLIDDLLMAQKEILSQQEiimKLRTDLGEAHSRMSDL-RGELSEKQKMELERQVALVRQQSGELS 1067
Cdd:PTZ00121 1618 AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE---ELKKAEEENKIKAAEEaKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1068 MLKAKVAQTTGLMEKKDRELKVLREALRASQEKPRPHLSTEQKPRTLSQKCDISLQIEPAHPDSFSSF-QEEQSFSDLGV 1146
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLkKEEEKKAEEIR 1774
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1147 KCKGSRHEETIQRQRKALSELRTRVRELEKANSCNHKDHVNESFLELRTLR-MEKNVQKILLDAKpdltTLARVEIRPPQ 1225
Cdd:PTZ00121 1775 KEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKeMEDSAIKEVADSK----NMQLEEADAFE 1850
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720409123 1226 NSPFNSGSTLVMEKSVKTDAGEALELSEK-----LYTDMIKTLgslmNIKDMSSHTSLKHLSPKEREKVNHLRQKD 1296
Cdd:PTZ00121 1851 KHKFNKNNENGEDGNKEADFNKEKDLKEDdeeeiEEADEIEKI----DKDDIEREIPNNNMAGKNNDIIDDKLDKD 1922
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
648-940 |
7.58e-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: 56.61 E-value: 7.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 648 LEETEQLLGDLDIELSDSDKGFSLCLIYLLEHykkiMSQSQDLQAQMNASRETQKSLRQE--HLAEKEKLAEKLEQE--- 722
Cdd:pfam19220 85 LEELVARLAKLEAALREAEAAKEELRIELRDK----TAQAEALERQLAAETEQNRALEEEnkALREEAQAAEKALQRaeg 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 723 ------------EKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQ--------- 781
Cdd:pfam19220 161 elatarerlallEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQleeaveahr 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 782 -EKRKMREMLEAERRKAQDLENQLTQQkeisenntyeklkmRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKL 860
Cdd:pfam19220 241 aERASLRMKLEALTARAAATEQLLAEA--------------RNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 861 KDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRlklqqqsMKALQDERESQKHGFEEEISEYKEQ 940
Cdd:pfam19220 307 ERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDR-------IAELTKRFEVERAALEQANRRLKEE 379
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
677-943 |
7.87e-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: 57.06 E-value: 7.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 677 LEHYKKIMSQSQDLQAQMNasRETQKSLRQEHLA-EKEKLAEKLEQEEKlKAKIQQLTEEKAALE--------------- 740
Cdd:pfam17380 312 VERRRKLEEAEKARQAEMD--RQAAIYAEQERMAmERERELERIRQEER-KRELERIRQEEIAMEisrmrelerlqmerq 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 741 ---ESIGQE-------KSRSEEALEKAQARVRELENHLASQKEALENSVAQ-EKRKMREMleaERRKAQDLENQltQQKE 809
Cdd:pfam17380 389 qknERVRQEleaarkvKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRlEEERAREM---ERVRLEEQERQ--QQVE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 810 ISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEiELKEQKENVLNNKLKDALV--MVEDAQQMKTTESQRAETlalk 887
Cdd:pfam17380 464 RLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK-ELEERKQAMIEEERKRKLLekEMEERQKAIYEEERRREA---- 538
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720409123 888 lketlaelETTKTKMILTDDRLKLQQQSMKAlqDERESQKHGFEEEiSEYKEQIKQ 943
Cdd:pfam17380 539 --------EEERRKQQEMEERRRIQEQMRKA--TEERSRLEAMERE-REMMRQIVE 583
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
703-1444 |
8.26e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 57.29 E-value: 8.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 703 SLRQEHLAEKEKLAEKLEQE-EKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVREL-------ENHLASQKEA 774
Cdd:pfam02463 162 AAGSRLKRKKKEALKKLIEEtENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEyllyldyLKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 775 LE---NSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQ 851
Cdd:pfam02463 242 LQellRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 852 KENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFE 931
Cdd:pfam02463 322 EKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKS 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 932 EEISEYKEQIkQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAGPPLDSGDKEIACDHLIDDLLM 1011
Cdd:pfam02463 402 EEEKEAQLLL-ELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLV 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1012 AQKEILSQQEIIMKLRTDL-GEAHSRMSDLRGELSEKQKMELERQVALVRQQSGELSMLKAKVAQTTGLMEKKDRELKVL 1090
Cdd:pfam02463 481 KLQEQLELLLSRQKLEERSqKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEV 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1091 REALRASQEKP---------RPHLSTEQKPRTLSQKCDISLQIEPAHPDSFSSFQEEQSFSDLGVKCKGSRHEETIQRQR 1161
Cdd:pfam02463 561 EERQKLVRALTelplgarklRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKES 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1162 -KALSELRTRVRELEKANSCNHKDHVNESFLELRTLRMEKNVQKILLDAKPdLTTLARVEIRPPQNSPFNSGSTLVMEKS 1240
Cdd:pfam02463 641 aKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAK-EEILRRQLEIKKKEQREKEELKKLKLEA 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1241 VKTDAGEALELSEKLYTDMIKTLGSLMNIKDMSSHTSLKHLSPKEREKVNHLRQKDLDLVFDKITQLKTRLQRKEELLKG 1320
Cdd:pfam02463 720 EELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQ 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1321 YEQELEQLRHSKVSVQMYQTQVAKLEDDVH-KEAEEKALLKEALERTEQQLSQERRFNRVFKQQKDRGEDPEQRNMSYSP 1399
Cdd:pfam02463 800 EEELRALEEELKEEAELLEEEQLLIEQEEKiKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEEL 879
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1720409123 1400 FKDNEKQRRLFVEMVKSKMQNSSVQAGAKKATLKTGQERETKKEA 1444
Cdd:pfam02463 880 EEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIK 924
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
18-65 |
9.58e-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: 9.58e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1720409123 18 TTIGKH-ADSDLVLQSADIDNHHALIEFNEaEGTFVLQDFNSRNGTFVN 65
Cdd:smart00240 1 VTIGRSsEDCDIQLDGPSISRRHAVIVYDG-GGRFYLIDLGSTNGTFVN 48
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
681-878 |
1.17e-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: 55.93 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 681 KKIMSQSQDLQAQMNASRETQKSLRQ--EHLAEKEKLAEKLEQE-EKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKA 757
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAAleRRIAALARRIRALEQElAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 758 QARVR-ELENHLASQKEALE--------NSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKE 828
Cdd:COG4942 114 YRLGRqPPLALLLSPEDFLDavrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1720409123 829 K----RKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTES 878
Cdd:COG4942 194 KaerqKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
699-1430 |
1.37e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 699 ETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQqltEEKAALEESIGQEKSRSEEALEKAQARvRELENHLASQKEALENS 778
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAEAVKKAEEAKKDAE---EAKKAEEERNNEEIRKFEEARMAHFAR-RQAAIKAEEARKADELK 1284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 779 VAQEKRKMREMLEA-ERRKAQDLENQLTQQKEISEnntyeklkMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLN 857
Cdd:PTZ00121 1285 KAEEKKKADEAKKAeEKKKADEAKKKAEEAKKADE--------AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAA 1356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 858 NKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKtkmiltddrlklqqqsmKALQDERESQKHGFEEEISEY 937
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKK-----------------KAEEDKKKADELKKAAAAKKK 1419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 938 KEQIKQHSQTIVSLEErlcqvtqyyqkiegeiTTLKNNDTGPKEEASQDLTAGPPLDSGDKEIACDHLIDDLLMAQKEIL 1017
Cdd:PTZ00121 1420 ADEAKKKAEEKKKADE----------------AKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK 1483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1018 SQQEIIMKLRtdlgEAHSRMSDLRGELSEKQKMELERQVALVRQQSGELSMLKAKVAQTTGLME--KKDRELKVLREALR 1095
Cdd:PTZ00121 1484 KADEAKKKAE----EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEekKKADELKKAEELKK 1559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1096 ASQEKPRPHLSTEQKPRTLS-QKCDISLQIEPAHPDSFSSFQEEQsfsdlgvkcKGSRHEETIQRQRKALSELRTRVREL 1174
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMAlRKAEEAKKAEEARIEEVMKLYEEE---------KKMKAEEAKKAEEAKIKAEELKKAEE 1630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1175 EKANSCNHKDHVNESFLELRTLRMEKNVQKIlldAKPDLTTLARVEIRPPQNSPFNSGSTLVMEKSVKTDAGEALELSEk 1254
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELKKAEEENKI---KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE- 1706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1255 lytdmiktlgslmnikdmsshtsLKHLSPKEREKVNHLRQKDlDLVFDKITQLKtrlqRKEELLKGYEQELEQLRHSKVS 1334
Cdd:PTZ00121 1707 -----------------------LKKKEAEEKKKAEELKKAE-EENKIKAEEAK----KEAEEDKKKAEEAKKDEEEKKK 1758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1335 VQMYQTQVAKLEDDVHKEAEekALLKEALERTEQQLSQErrFNRVFKQQKDRGEDPEQRNMSYSPFKDNEKQrrLFVEMV 1414
Cdd:PTZ00121 1759 IAHLKKEEEKKAEEIRKEKE--AVIEEELDEEDEKRRME--VDKKIKDIFDNFANIIEGGKEGNLVINDSKE--MEDSAI 1832
|
730
....*....|....*.
gi 1720409123 1415 KSKMQNSSVQAGAKKA 1430
Cdd:PTZ00121 1833 KEVADSKNMQLEEADA 1848
|
|
| 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 1720409123 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 |
2.62e-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: 2.62e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720409123 19 TIGKHADSDLVLQSADIDNHHALIEFN----EAEGTFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFG 85
Cdd:cd22677 25 VFGRLPGCDVVLEHPSISRYHAVLQYRgdadDHDGGFYLYDLGSTHGTFLNKQRIPpKQYYRLRVGHVLKFG 96
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
751-905 |
4.12e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 54.40 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 751 EEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAE----RRKAQDLENQLTQQKEISENNTyeklkmrDTLE 826
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKElrerRNELQKLEKRLLQKEENLDRKL-------ELLE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 827 KEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMV-----EDAQQM---KTTESQRAETLAL-KLKETLAELET 897
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIsgltaEEAKEIlleKVEEEARHEAAVLiKEIEEEAKEEA 186
|
....*....
gi 1720409123 898 TKT-KMILT 905
Cdd:PRK12704 187 DKKaKEILA 195
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
678-1371 |
4.40e-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: 54.74 E-value: 4.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 678 EHYKKIMS----QSQDLQAQMNASREtqkslrqehLAEKEKLAEKlEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEA 753
Cdd:pfam15921 74 EHIERVLEeyshQVKDLQRRLNESNE---------LHEKQKFYLR-QSVIDLQTKLQEMQMERDAMADIRRRESQSQEDL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 754 LEKAQARVRELENHLASQKEALENSVAQEKrKMREMLEAERRKAQDLENQLTQQKEISENNTYEK--------------- 818
Cdd:pfam15921 144 RNQLQNTVHELEAAKCLKEDMLEDSNTQIE-QLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHdsmstmhfrslgsai 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 819 LKMRDTLEKE----KRKIQDLENRLTKQKEEIE-----LKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLk 889
Cdd:pfam15921 223 SKILRELDTEisylKGRIFPVEDQLEALKSESQnkielLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQL- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 890 ETLAELETTKTKMILTddRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEI 969
Cdd:pfam15921 302 EIIQEQARNQNSMYMR--QLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQL 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 970 TTLKNNDTGPKEEASQDLTAGPPL---DSGDkEIACDHLIDDLLMAQKEILSQQEIIMKLRTDL-GEAHSRMSDLRGels 1045
Cdd:pfam15921 380 QKLLADLHKREKELSLEKEQNKRLwdrDTGN-SITIDHLRRELDDRNMEVQRLEALLKAMKSECqGQMERQMAAIQG--- 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1046 ekQKMELERQVALVRQQSGELSMLKAKVAQTTG---LMEKKDRELKVLREALrasQEKPRPHLSTEQKPRTLSQKCDISL 1122
Cdd:pfam15921 456 --KNESLEKVSSLTAQLESTKEMLRKVVEELTAkkmTLESSERTVSDLTASL---QEKERAIEATNAEITKLRSRVDLKL 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1123 QiEPAHPDSfssfqEEQSFSDLGVKCKGSRHEETiqRQRKALSELRTRVRELEKANScNHKDHVNESFLELRTLRMEKNV 1202
Cdd:pfam15921 531 Q-ELQHLKN-----EGDHLRNVQTECEALKLQMA--EKDKVIEILRQQIENMTQLVG-QHGRTAGAMQVEKAQLEKEIND 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1203 QKILLDAKPDLTTLARVEIRPPQNSPfnsgSTLVMEKSVKTDAGealelSEKLYT--DMIKTLGSLMNiKDMSSHTSLKH 1280
Cdd:pfam15921 602 RRLELQEFKILKDKKDAKIRELEARV----SDLELEKVKLVNAG-----SERLRAvkDIKQERDQLLN-EVKTSRNELNS 671
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1281 LSPKEREKVNHLRQKDLDLvfdKITQLKTRLQrkeelLKGYEQELEQLRHS------------KVSVQM----------- 1337
Cdd:pfam15921 672 LSEDYEVLKRNFRNKSEEM---ETTTNKLKMQ-----LKSAQSELEQTRNTlksmegsdghamKVAMGMqkqitakrgqi 743
|
730 740 750
....*....|....*....|....*....|....*.
gi 1720409123 1338 --YQTQVAKLEDDVHKEAEEKALLKEALERTEQQLS 1371
Cdd:pfam15921 744 daLQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELS 779
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
13-86 |
4.45e-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: 4.45e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720409123 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 |
4.54e-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: 4.54e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720409123 15 NKSTTIGKHADSDLVLQSADIDNHHALIE---FNEAEGTFV-LQDfNSRNGTFVNECHI-QNVAVKLIPGDILRFGSA 87
Cdd:cd22670 21 NQVITIGRSPSCDIVINDPFVSRTHCRIYsvqFDESSAPLVyVED-LSSNGTYLNGKLIgRNNTVLLSDGDVIEIAHS 97
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
677-1116 |
5.89e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 5.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 677 LEHYKKIMSQSQDLQAQMNASRETQKSLRQ--EHLAEKEKLAEKLEQEEKLKAKIQQ---LTEEKAALEESIGQEKSRSE 751
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEEleEELEELEAELEELREELEKLEKLLQllpLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 752 EaLEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRK 831
Cdd:COG4717 150 E-LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 832 IQDLENRLTKQKEEIELKEQKE----------------NVLNNKLKDA--------LVMVEDAQQMKTTESQRAETLALK 887
Cdd:COG4717 229 LEQLENELEAAALEERLKEARLllliaaallallglggSLLSLILTIAgvlflvlgLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 888 LKETLAELETTKTKMILTDDRLK-----------------LQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSqtIVS 950
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPpdlspeellelldrieeLQELLREAEELEEELQLEELEQEIAALLAEAGVED--EEE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 951 LEERLCQVTQyYQKIEGEITTLKNNdtgpkeeasqdltagppLDSGDKEIACDHLIDDLLMAQKEILSQQEIIMKLRTDL 1030
Cdd:COG4717 387 LRAALEQAEE-YQELKEELEELEEQ-----------------LEELLGELEELLEALDEEELEEELEELEEELEELEEEL 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1031 GEAHSRMSDLRGELSEkqkMELERQVALVRQqsgELSMLKAKVAQttglMEKKDRELKVLREALRASQEkprpHLSTEQK 1110
Cdd:COG4717 449 EELREELAELEAELEQ---LEEDGELAELLQ---ELEELKAELRE----LAEEWAALKLALELLEEARE----EYREERL 514
|
....*.
gi 1720409123 1111 PRTLSQ 1116
Cdd:COG4717 515 PPVLER 520
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
689-863 |
6.90e-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: 6.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 689 DLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEA---LEKAQARVRELE 765
Cdd:COG3206 209 DLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAeleAELAELSARYTP 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 766 NH-----LASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEisenntyeklkmrdTLEKEKRKIQDLENRLT 840
Cdd:COG3206 289 NHpdviaLRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLA--------------QLEARLAELPELEAELR 354
|
170 180
....*....|....*....|...
gi 1720409123 841 KQKEEIELKEQKENVLNNKLKDA 863
Cdd:COG3206 355 RLEREVEVARELYESLLQRLEEA 377
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
690-886 |
7.22e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 7.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 690 LQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEEsigqEKSRSEEALEKAQARVRELENHLA 769
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEE----ELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 770 -----SQKEALENSVAQEKRKMREMLEAE------RRKAQDLENQLTQ-QKEISENNTYEKLKMRDTLEKEKRKIQDLEN 837
Cdd:COG4717 127 llplyQELEALEAELAELPERLEELEERLeelrelEEELEELEAELAElQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720409123 838 RLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLAL 886
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIA 255
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
699-963 |
8.63e-07 |
|
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: 53.53 E-value: 8.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 699 ETQKSLRqehlAEKEKLAEKLEQEEKL-KAKIQQLTEEKAALEEsigqEKsrseealEKAQARVRELENHLASQKEALEN 777
Cdd:pfam15070 4 ESLKQLQ----TERDQYAENLKEEGAVwQQKMQQLSEQVRTLRE----EK-------ERSVSQVQELETSLAELKNQAAV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 778 SVAQEKRKMREMLEAERRKAQDLEnQLTQQKEISENNTYEKLKMRDTL-----EKEKRkIQDLENRLTKQKEEIELKEQk 852
Cdd:pfam15070 69 PPAEEEQPPAGPSEEEQRLQEEAE-QLQKELEALAGQLQAQVQDNEQLsrlnqEQEQR-LLELERAAERWGEQAEDRKQ- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 853 envlnnklkdalvMVEDAQQMKTTESqRAETLALKLKETLAELETTKTKmiLTDDRLKLqqqsMKALQDERESQKH---- 928
Cdd:pfam15070 146 -------------ILEDMQSDRATIS-RALSQNRELKEQLAELQNGFVK--LTNENMEL----TSALQSEQHVKKElakk 205
|
250 260 270
....*....|....*....|....*....|....*..
gi 1720409123 929 --GFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQ 963
Cdd:pfam15070 206 lgQLQEELGELKETLELKSQEAQSLQEQRDQYLAHLQ 242
|
|
| FHA_PS1-like |
cd22691 |
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) ... |
19-93 |
9.09e-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: 9.09e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720409123 19 TIGKHADSDLVLQSADIDNHHALIEFNEAEGTFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFGSAGMTYEL 93
Cdd:cd22691 32 VVGRHPDCDIVLDHPSISRFHLEIRIIPSRRKITLTDLSSVHGTWVNGQRIEpGVPVELEEGDTVRLGASTRVYRL 107
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
321-431 |
1.40e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 52.94 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 321 IESLKNEGENLKRDHAITsgMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALSSRCSVMKEEL---RKEEAQ 397
Cdd:COG2433 382 LEELIEKELPEEEPEAER--EKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELseaRSEERR 459
|
90 100 110
....*....|....*....|....*....|....*...
gi 1720409123 398 KDRREAQ----EKELKLCRSQMQDMEKEVRKLREELKK 431
Cdd:COG2433 460 EIRKDREisrlDREIERLERELEEERERIEELKRKLER 497
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
698-925 |
2.28e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 698 RETQKSLRQEHLAEKEKLAEKLEQEEKLK---AKIQQLTEEKAALEESIGQEKSRSEEALEKAQArvrelenhLASQKEA 774
Cdd:PRK02224 477 VEELEAELEDLEEEVEEVEERLERAEDLVeaeDRIERLEERREDLEELIAERRETIEEKRERAEE--------LRERAAE 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 775 LEnSVAQEKR----KMREMLEAERRKAQDLENQLTQQKEISEN-NTYEKL-----KMRDTLEKEKRKIQDLENRLTKQKE 844
Cdd:PRK02224 549 LE-AEAEEKReaaaEAEEEAEEAREEVAELNSKLAELKERIESlERIRTLlaaiaDAEDEIERLREKREALAELNDERRE 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 845 EIELKEQKENVLNNKLKDAlvMVEDAQQMKttesQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERE 924
Cdd:PRK02224 628 RLAEKRERKRELEAEFDEA--RIEEAREDK----ERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERRE 701
|
.
gi 1720409123 925 S 925
Cdd:PRK02224 702 A 702
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
366-953 |
2.61e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 366 LRIENREKEYQ-----LEALSSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKnymgqniIS 440
Cdd:PRK03918 155 LGLDDYENAYKnlgevIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEK-------LE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 441 KTLREKNKVEEKLQEDSRRKLLQLQEMGNRENLIK-----IN--------LERAVGQLENFRNQviKATFGKTKPFRDKP 507
Cdd:PRK03918 228 KEVKELEELKEEIEELEKELESLEGSKRKLEEKIReleerIEelkkeieeLEEKVKELKELKEK--AEEYIKLSEFYEEY 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 508 ITDQQRQHLRACIPPHRARTCAPTLQ---SLPRRAGCLETSYclssGQLIEKIIQVTEDNLSFQQRKWTLQRETHLhpKQ 584
Cdd:PRK03918 306 LDELREIEKRLSRLEEEINGIEERIKeleEKEERLEELKKKL----KELEKRLEELEERHELYEEAKAKKEELERL--KK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 585 EETMHSVEKLRVLLDKCQacmrdscssiDLKKEVElLQHLPLSPLVSGLqKTVVNILRVSLSWLEETEQLLGDLDIELSD 664
Cdd:PRK03918 380 RLTGLTPEKLEKELEELE----------KAKEEIE-EEISKITARIGEL-KKEIKELKKAIEELKKAKGKCPVCGRELTE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 665 SDKGfslcliYLLEHYKKIMSqsqDLQAQMNASRETQKSLRQEhLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIG 744
Cdd:PRK03918 448 EHRK------ELLEEYTAELK---RIEKELKEIEEKERKLRKE-LRELEKVLKKESELIKLKELAEQLKELEEKLKKYNL 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 745 QEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRK---MREMLEAERRKAqDLENQLTQQKEISENNTYEKLKM 821
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLaelEKKLDELEEELA-ELLKELEELGFESVEELEERLKE 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 822 RDTLEKE-------KRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTES-QRAETLALKLKETLA 893
Cdd:PRK03918 597 LEPFYNEylelkdaEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELA 676
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 894 ELETTKtkmiltdDRLKLQQQSMKALQDERESQKhgfeEEISEYKEQIKQHSQTIVSLEE 953
Cdd:PRK03918 677 GLRAEL-------EELEKRREEIKKTLEKLKEEL----EEREKAKKELEKLEKALERVEE 725
|
|
| FHA_NBN |
cd22667 |
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ... |
11-91 |
2.63e-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: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 11 FFVLNKSTTIG-KHADsDLVLQSADIDNHHALI-----EFNEAEG----TFVLQDFnSRNGTFVNECHIQNVA-VKLIPG 79
Cdd:cd22667 15 YLLPGGEYTVGrKDCD-IIIVDDSSISRKHATLtvlhpEANLSDPdtrpELTLKDL-SKYGTFVNGEKLKGGSeVTLKDG 92
|
90
....*....|..
gi 1720409123 80 DILRFGSAGMTY 91
Cdd:cd22667 93 DVITFGVLGSKF 104
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
685-852 |
2.70e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 685 SQSQDLQAQMNASRETQKSLRQEhlaekekLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVREL 764
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAE-------LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 765 ENH------------------LASQKEALENSVAQEKRKMREmLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLE 826
Cdd:COG3883 96 YRSggsvsyldvllgsesfsdFLDRLSALSKIADADADLLEE-LKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180
....*....|....*....|....*.
gi 1720409123 827 KEKRKIQDLENRLTKQKEEIELKEQK 852
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAE 200
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
677-953 |
3.52e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 51.83 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 677 LEHYKKIMSQSQDLQAQMNA-SRETQKSLRQEHLAEKEKLAEKL--EQEEKLKAKIQQLTEEKAALEESIGQEKS--RSE 751
Cdd:PLN02939 155 LEDLEKILTEKEALQGKINIlEMRLSETDARIKLAAQEKIHVEIleEQLEKLRNELLIRGATEGLCVHSLSKELDvlKEE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 752 EALEKAQARVreLENHLASQKEALENSVAQEKRkmREMLEAERRkaqDLENQL-TQQKEISENNTYEKlkmrDTLEKEKR 830
Cdd:PLN02939 235 NMLLKDDIQF--LKAELIEVAETEERVFKLEKE--RSLLDASLR---ELESKFiVAQEDVSKLSPLQY----DCWWEKVE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 831 KIQDLENRLTKQKEEIELKEQKENVLNNKLKdalvmvedaqqmkttesqraetlalKLKETLAELETTKtkmiLTDDRLK 910
Cdd:PLN02939 304 NLQDLLDRATNQVEKAALVLDQNQDLRDKVD-------------------------KLEASLKEANVSK----FSSYKVE 354
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1720409123 911 LQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEE 953
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 |
4.39e-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: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 11 FFVLNKSTTIGKHADSDLVLQSAD--IDNHHALIEFNEAEGTFVLQDFNSRNGTFVNECHIQNVAVKLIP-----GDILR 83
Cdd:cd22686 21 FIVTATGATIGREKDHGHTIRIPElgVSKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPyplthGDELK 100
|
...
gi 1720409123 84 FGS 86
Cdd:cd22686 101 IGE 103
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
308-917 |
4.48e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.51 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 308 QVLSQTLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKE---------YQLE 378
Cdd:TIGR00618 310 QRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTltqhihtlqQQKT 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 379 ALSSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKlreELKKNYMGQNIISKTLREKNKVEEKLQEDSR 458
Cdd:TIGR00618 390 TLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQEL---QQRYAELCAAAITCTAQCEKLEKIHLQESAQ 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 459 RKLLQLQEMGNRENLIKinLERAVGQLENFRNQVIKatfgktkpfrdkpitDQQRQHLRACIPPHRARTCAPTLQSLPRR 538
Cdd:TIGR00618 467 SLKEREQQLQTKEQIHL--QETRKKAVVLARLLELQ---------------EEPCPLCGSCIHPNPARQDIDNPGPLTRR 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 539 AGCLETSYclssGQLIEKIIQVTEDNLSFQQRKWTLQREthlhpkQEETMHSVEKLRVLLDkcqacmRDSCSSIDLKKEV 618
Cdd:TIGR00618 530 MQRGEQTY----AQLETSEEDVYHQLTSERKQRASLKEQ------MQEIQQSFSILTQCDN------RSKEDIPNLQNIT 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 619 ELLQHlpLSPLVSGLQKTVVNILRVSlswLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHykkimsqsqDLQAQMNASR 698
Cdd:TIGR00618 594 VRLQD--LTEKLSEAEDMLACEQHAL---LRKLQPEQDLQDVRLHLQQCSQELALKLTALH---------ALQLTLTQER 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 699 ETQKSLRQEHLaEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESigQEKSRSEEALEKAQAR-VRELENHLASQKEALEn 777
Cdd:TIGR00618 660 VREHALSIRVL-PKELLASRQLALQKMQSEKEQLTYWKEMLAQC--QTLLRELETHIEEYDReFNEIENASSSLGSDLA- 735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 778 svaQEKRKMREMLEAERRKAQDlenQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLN 857
Cdd:TIGR00618 736 ---AREDALNQSLKELMHQART---VLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIG 809
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 858 NKLKDALVMVEDAQQmktTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMK 917
Cdd:TIGR00618 810 QEIPSDEDILNLQCE---TLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQ 866
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
683-818 |
4.87e-06 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 51.17 E-value: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 683 IMSQSQDLQAQMNASRETQKSlrQEHLaEKEKLAEKLEQEEKlKAKIQQLTEEKAALE---ESIGQEKSRSEEALEKAQA 759
Cdd:PTZ00491 659 ITTKSQEAAARHQAELLEQEA--RGRL-ERQKMHDKAKAEEQ-RTKLLELQAESAAVEssgQSRAEALAEAEARLIEAEA 734
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720409123 760 RVRELEnhLASQKEALENSVAQEKRKMREMLEAERRKAQDlENQLTQQKEIS--ENNTYEK 818
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 |
5.64e-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: 5.64e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720409123 19 TIGKHADSDLVLQSADIDNHHALIEFnEAEGtFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRFGS 86
Cdd:pfam16697 20 RIGSDPDCDIVLSDKEVSRVHLKLEV-DDEG-WRLDDLGSGNGTLVNGQRVTELGIALRPGDRIELGQ 85
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
717-953 |
6.73e-06 |
|
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: 50.88 E-value: 6.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 717 EKLEQ-EEKLKAKIQQLTEEKAALEEsIGQEKSRSEEALEKAQARVRELENHLASQK--EALENSVAQEKRKMREMLEAE 793
Cdd:pfam05483 370 QRLEKnEDQLKIITMELQKKSSELEE-MTKFKNNKEVELEELKKILAEDEKLLDEKKqfEKIAEELKGKEQELIFLLQAR 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 794 RRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQD---------LENRLTKQKEE---IELKEQKENVLNNKlK 861
Cdd:pfam05483 449 EKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIEltahcdkllLENKELTQEASdmtLELKKHQEDIINCK-K 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 862 DALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMiltdDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQI 941
Cdd:pfam05483 528 QEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKL----DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQI 603
|
250
....*....|..
gi 1720409123 942 KQHSQTIVSLEE 953
Cdd:pfam05483 604 ENKNKNIEELHQ 615
|
|
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
13-85 |
8.87e-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: 8.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 13 VLNKSTTIGKH------ADSDLVLQSADIDNHHALIEFNEaeGTFVLQDFNSRNGTFVNECHIQ-----NVAVKLIPGDI 81
Cdd:cd22679 21 VLDEPVKIGRSvararpAANNAIFDCKVLSRNHALLWYDD--GKFYLQDTKSSNGTFVNNQRLSkgseeSEPRELHSGDI 98
|
....
gi 1720409123 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 |
8.87e-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: 8.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 20 IGKHAD-SDLVLQSADIDNHHALIEF----NEAEGTFVLQ------DFNSRNGTFVNECHIQ-NVAVKLIPGDILRFGSA 87
Cdd:cd22676 25 IGRDRRvADIPLDHPSCSKQHAVIQFreveKRNEGDVIENirpyiiDLGSTNGTFLNGEKIEpRRYYELREKDVLKFGLS 104
|
....*.
gi 1720409123 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 |
9.51e-06 |
|
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA is a histidine protein kinase with a fork head-associated (FHA) domain at the N-terminus and a receiver domain at the C-terminus. It functions as an inhibitor of sporulation during early fruiting body development while cells are aggregating into raised mounds. EspA is part of a two-component signal transduction system that regulates the timing of sporulation initiation. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438750 [Multi-domain] Cd Length: 93 Bit Score: 45.48 E-value: 9.51e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720409123 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 |
1.19e-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: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 19 TIGKHADSDLVLQSAD--IDNHHALIEFNEaeGTFVLQDFnSRNGTFVNECH---IQNVAVKLIPGDILRFGSagmtYEL 93
Cdd:TIGR03354 27 TIGRSEDCDWVLPDPErhVSGRHARIRYRD--GAYLLTDL-STNGVFLNGSGsplGRGNPVRLEQGDRLRLGD----YEI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 94 VIENPSP------------VSCPWVRGP-APWPSPQPHL---------SSSPPDMPFhhgiQPATVQRSWSQGCP----- 146
Cdd:TIGR03354 100 RVSLGDPlvsrqasesradTSLPTAGGPpTPDPAPLAQLdplkaldqePLSAADLDD----LSAPLFPPLDARLPafaap 175
|
170 180
....*....|....*....|.
gi 1720409123 147 ---RPTMVP-----PAPHQRP 159
Cdd:TIGR03354 176 idaEPTMVPpfvplPAPEPAP 196
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
350-945 |
1.31e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 350 SARNEQVQQLQEEVNRLRIENREKEYQLEALSSRCSVMKEELRKEEAQKDRREAQEKELKlcrsQMQDMEKEVRKLREEL 429
Cdd:PRK03918 227 EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK----ELKEKAEEYIKLSEFY 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 430 KKNYMGQNIISKTL----REKNKVEEKLQEDSRRKlLQLQEMGNRENLIKINLERAVGQLENFrnqvikatfgktkpfrd 505
Cdd:PRK03918 303 EEYLDELREIEKRLsrleEEINGIEERIKELEEKE-ERLEELKKKLKELEKRLEELEERHELY----------------- 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 506 kpitdqqrqhlracippHRARTCAPTLQSLPRRAGCLETsyclssGQLIEKIIQVTEDNLSFQ-QRKWTLQRETHLHPKQ 584
Cdd:PRK03918 365 -----------------EEAKAKKEELERLKKRLTGLTP------EKLEKELEELEKAKEEIEeEISKITARIGELKKEI 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 585 EETMHSVEKLRVLLDKCQACMRDscssIDLKKEVELLQHLPLSplvsglqktvvniLRVSLSWLEETEQLLGDLDIELSD 664
Cdd:PRK03918 422 KELKKAIEELKKAKGKCPVCGRE----LTEEHRKELLEEYTAE-------------LKRIEKELKEIEEKERKLRKELRE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 665 SDKgfslcliyLLEHYKKIMSQsQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQE-EKLKAKIQQLTEEKAALEESi 743
Cdd:PRK03918 485 LEK--------VLKKESELIKL-KELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKlIKLKGEIKSLKKELEKLEEL- 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 744 gqeKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERR--KAQDLENQLTQQKEisenntyEKLKM 821
Cdd:PRK03918 555 ---KKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEylELKDAEKELEREEK-------ELKKL 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 822 RDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLN-NKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKT 900
Cdd:PRK03918 625 EEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE 704
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1720409123 901 KMILTDDRLKLQQQSMKALQDEResqkhgfeEEISEYKEQIKQHS 945
Cdd:PRK03918 705 EREKAKKELEKLEKALERVEELR--------EKVKKYKALLKERA 741
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
676-862 |
1.33e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 676 LLEHYKKIMS---------QSQDLQAQMNASRETQKSLRQEhLAEKEKLAEKLEQE------EKLKAKIQQLTEEKAALE 740
Cdd:COG4913 230 LVEHFDDLERahealedarEQIELLEPIRELAERYAAARER-LAELEYLRAALRLWfaqrrlELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 741 EsigqEKSRSEEALEKAQARVRELENHLAS----QKEALENSVAQEKRKMREMleaeRRKAQDLENQLTQQKEISENN-- 814
Cdd:COG4913 309 A----ELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEER----ERRRARLEALLAALGLPLPASae 380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1720409123 815 TYEKLK--MRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKD 862
Cdd:COG4913 381 EFAALRaeAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
208-467 |
1.45e-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: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 208 MDHDLSQQDKDEiillLGREVNRLSDFEMESKYKDALiMNLQAEVADLSQRLsetaavaaARQSNRCDPKLQGVD---EG 284
Cdd:pfam17380 296 MEQERLRQEKEE----KAREVERRRKLEEAEKARQAE-MDRQAAIYAEQERM--------AMERERELERIRQEErkrEL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 285 DDLRQKEIESMKSQINALQKgySQVLSQTLAER-NTEIESLKN----EGENLKRDHAITSGMVTSLQKDMSARNEQVQQL 359
Cdd:pfam17380 363 ERIRQEEIAMEISRMRELER--LQMERQQKNERvRQELEAARKvkilEEERQRKIQQQKVEMEQIRAEQEEARQREVRRL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 360 QEE----VNRLRIENREKEYQLEAL--------SSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLRE 427
Cdd:pfam17380 441 EEErareMERVRLEEQERQQQVERLrqqeeerkRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEK 520
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1720409123 428 ELKKNymgQNIISKTLREKNKVEE--KLQEDSRRKLLQLQEM 467
Cdd:pfam17380 521 EMEER---QKAIYEEERRREAEEErrKQQEMEERRRIQEQMR 559
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
691-954 |
1.58e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 691 QAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKA-KIQQLTEEKAALEESIGQEKSRSEEALEKAQA--RVRELENH 767
Cdd:PTZ00121 1244 KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAdELKKAEEKKKADEAKKAEEKKKADEAKKKAEEakKADEAKKK 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 768 LASQKEALE--NSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEK---EKRKIQDLENRLTKQ 842
Cdd:PTZ00121 1324 AEEAKKKADaaKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaeEKKKADEAKKKAEED 1403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 843 KEEI-ELK---EQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKET--LAELETTKTKMILTDDRLKLQQQSM 916
Cdd:PTZ00121 1404 KKKAdELKkaaAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAkkAEEAKKKAEEAKKADEAKKKAEEAK 1483
|
250 260 270
....*....|....*....|....*....|....*...
gi 1720409123 917 KALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEER 954
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEA 1521
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
684-1176 |
1.60e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 684 MSQSQDLQAQMNAsRETQKSLRQEHLAEKEKLAEKLEQEEKLKA-KIQQLTEEKAALEESigqeKSRSEEALEKAQARVR 762
Cdd:PTZ00121 1262 MAHFARRQAAIKA-EEARKADELKKAEEKKKADEAKKAEEKKKAdEAKKKAEEAKKADEA----KKKAEEAKKKADAAKK 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 763 ELEnhlaSQKEALENSVAQEKRKMREMLEAERR-KAQDLENQLTQQKEISENNTYEKLKMRDTL----EKEKRKIQDLEN 837
Cdd:PTZ00121 1337 KAE----EAKKAAEAAKAEAEAAADEAEAAEEKaEAAEKKKEEAKKKADAAKKKAEEKKKADEAkkkaEEDKKKADELKK 1412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 838 RLTKQKEEIELKEQKENVlnNKLKDALVMVEDAQQM-----KTTESQRAETLALKLKETLAELETTKTkmilTDDRLKLQ 912
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEK--KKADEAKKKAEEAKKAdeakkKAEEAKKAEEAKKKAEEAKKADEAKKK----AEEAKKAD 1486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 913 QQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAGPP 992
Cdd:PTZ00121 1487 EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKA 1566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 993 LDSGDKEIACDHLIDDLLMAQKEILSQQEIIMKLRTDlgEAHSRMSDLRGELSEKQKMELERQVALVRQQSGELSMLKAK 1072
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE--EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE 1644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1073 VAQTTGLMEKKDRELKVLREALRASQEKPRPHLSTEQKPRTLSQKCDISLQIEpahpdsfssfqEEQSFSDLGVKCKGSR 1152
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE-----------AEEAKKAEELKKKEAE 1713
|
490 500
....*....|....*....|....
gi 1720409123 1153 HEETIQRQRKALSELRTRVRELEK 1176
Cdd:PTZ00121 1714 EKKKAEELKKAEEENKIKAEEAKK 1737
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
710-896 |
1.82e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 710 AEKEKLAEKLEQEEKLKAKIQQLTEEKAALEEsigqEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREM 789
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNE----EYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 790 LEAERRK-----------AQDLENQLTQQKEISENNtyeklkmRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNN 858
Cdd:COG3883 96 YRSGGSVsyldvllgsesFSDFLDRLSALSKIADAD-------ADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 1720409123 859 KLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELE 896
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
688-828 |
1.86e-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: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 688 QDLQAQMNASRETQKSLRQEHLAEKEKLAE-KLEQEEKLKAKIQQLTEEKAALE----------ESIGQEKSRSEEALEK 756
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERErrrarleallAALGLPLPASAEEFAA 384
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720409123 757 AQARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNtyekLKMRDTLEKE 828
Cdd:COG4913 385 LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL----LALRDALAEA 452
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
288-501 |
1.96e-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: 48.61 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 288 RQKEIESMKSQINALQKgysqvlsqTLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLR 367
Cdd:COG4942 25 AEAELEQLQQEIAELEK--------ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 368 --IENREKEY--QLEAL--SSRCSVMKEELRKE----------------EAQKDRREAQEKELKLCRSQMQDMEKEVRKL 425
Cdd:COG4942 97 aeLEAQKEELaeLLRALyrLGRQPPLALLLSPEdfldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720409123 426 REELKKNYMGQNIISKTLREKNKVEEKLQEDSRRKLLQLQEMGNRENLIKINLERAVGQLENFRNQVIKATFGKTK 501
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
711-1372 |
2.34e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 711 EKEKLAEKLEQEEKLKAKIQQLTEEKAALEES--IGQEKSRSEEALEKAQARVRELENHLASQKEALEN--SVAQEKRKM 786
Cdd:PRK03918 136 EIDAILESDESREKVVRQILGLDDYENAYKNLgeVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEvlREINEISSE 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 787 REMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNnklkdalvm 866
Cdd:PRK03918 216 LPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK--------- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 867 vedaqqmkttESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQkhgfEEEISEYKEQIKQhsq 946
Cdd:PRK03918 287 ----------ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK----EERLEELKKKLKE--- 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 947 tivsLEERLCQVTQYYQKIEgEITTLKNNdtgpKEEASQDLTAGPPldsgdkeiacDHLIDDLLMAQKEILSQQEIIMKL 1026
Cdd:PRK03918 350 ----LEKRLEELEERHELYE-EAKAKKEE----LERLKKRLTGLTP----------EKLEKELEELEKAKEEIEEEISKI 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1027 RTDLGEAHSRMSDLRGELSEKQK-----------MELERQVALVRQQSGELSMLKAKVAQTTGLMEKKDRELKVLrEALR 1095
Cdd:PRK03918 411 TARIGELKKEIKELKKAIEELKKakgkcpvcgreLTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL-EKVL 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1096 ASQEKPRPHLSTEQKPRTLSQKCDiSLQIEPAHPDSFSSFQEEQSFSDLGVKCKGSRHE-ETIQRQRKALSELRTRVREL 1174
Cdd:PRK03918 490 KKESELIKLKELAEQLKELEEKLK-KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKElEKLEELKKKLAELEKKLDEL 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1175 EKANSCNHKDHVNESF-----LELRTLRMEKNVQKI--LLDAKPDLTtlarveirppqnspfnsgSTLVMEKSVKTDAGE 1247
Cdd:PRK03918 569 EEELAELLKELEELGFesveeLEERLKELEPFYNEYleLKDAEKELE------------------REEKELKKLEEELDK 630
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1248 ALELSEKLYTDMIKTLGSLMNIKDMSSHTSLKHLSPKEREKVNHLRQKDldlvfDKITQLKTRLQRKEELLKGYEQELEQ 1327
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLR-----AELEELEKRREEIKKTLEKLKEELEE 705
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1720409123 1328 LRHSKVSVQMYQTQVAKLEDDVHKEAEEKALLKE-ALERTEQQLSQ 1372
Cdd:PRK03918 706 REKAKKELEKLEKALERVEELREKVKKYKALLKErALSKVGEIASE 751
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
315-924 |
2.87e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 315 AERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALssrcsvmkeELRKE 394
Cdd:PRK02224 247 EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAV---------EARRE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 395 EAQKDRREAQEkELKLCRSQMQDMEKEVRKLREELKKnymgQNIISKTLREKNKVEEKLQEDSRRKLlqlqemGNRENLI 474
Cdd:PRK02224 318 ELEDRDEELRD-RLEECRVAAQAHNEEAESLREDADD----LEERAEELREEAAELESELEEAREAV------EDRREEI 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 475 KInLERAVGQLEnfrnqvikatfgktKPFRDKPITDQQRQHLRACIPPHRARtcaptlqslprragcletsyclssgqli 554
Cdd:PRK02224 387 EE-LEEEIEELR--------------ERFGDAPVDLGNAEDFLEELREERDE---------------------------- 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 555 ekiiqvtednlsfqqrkwTLQRETHLHPKQEETMHSVEKLRVLLD--KCQACMrdscssidlkkevellQHLPLSPLVSG 632
Cdd:PRK02224 424 ------------------LREREAELEATLRTARERVEEAEALLEagKCPECG----------------QPVEGSPHVET 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 633 lqktvvnilrvslswLEETEQLLGDLDIELSDsdkgfslcliyllehykkIMSQSQDLQAQMNASRETQKSLRQ-EHLAE 711
Cdd:PRK02224 470 ---------------IEEDRERVEELEAELED------------------LEEEVEEVEERLERAEDLVEAEDRiERLEE 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 712 KEKLAEKL--EQEEKLKAK---IQQLTEEKAALEESiGQEK----SRSEEALEKAQARVRELENHLASQKEALENSvaqe 782
Cdd:PRK02224 517 RREDLEELiaERRETIEEKrerAEELRERAAELEAE-AEEKreaaAEAEEEAEEAREEVAELNSKLAELKERIESL---- 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 783 kRKMREMLEAERRKAQDLENQLTQQKEISENNTYEklkmRDTLEKEKRKIQDLENRLTKQKEEiELKEQKENvlnnkLKD 862
Cdd:PRK02224 592 -ERIRTLLAAIADAEDEIERLREKREALAELNDER----RERLAEKRERKRELEAEFDEARIE-EAREDKER-----AEE 660
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720409123 863 ALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMiltdDRLKLQQQSMKALQDERE 924
Cdd:PRK02224 661 YLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERR----EALENRVEALEALYDEAE 718
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
648-809 |
3.15e-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: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 648 LEETEQLLGDLDIELSDsdkgfslcLIYLLEHYKKIMSQSQDLQAQMNASRETQkSLRQEHLAEKEKLAEKLEQEEKLKA 727
Cdd:COG3206 221 LSELESQLAEARAELAE--------AEARLAALRAQLGSGPDALPELLQSPVIQ-QLRAQLAELEAELAELSARYTPNHP 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 728 KIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERRK--AQDLENQLT 805
Cdd:COG3206 292 DVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVevARELYESLL 371
|
....
gi 1720409123 806 QQKE 809
Cdd:COG3206 372 QRLE 375
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
636-766 |
3.17e-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: 47.70 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 636 TVVNILRVSLSWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQDLqaqMNASRETQKSLRQEHLAEKEKL 715
Cdd:smart00787 151 ENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTE---LDRAKEKLKKLLQEIMIKVKKL 227
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720409123 716 AEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEA-------LEKAQARVRELEN 766
Cdd:smart00787 228 EELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCrgftfkeIEKLKEQLKLLQS 285
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
634-895 |
3.59e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.51 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 634 QKTVVNILRVSLSWLEETEQLLGDLDielsdsdkgfslcliylleHYKKIMSQ----SQDLQAQMNASRETQKSLRqEHL 709
Cdd:PRK10929 43 QAEIVEALQSALNWLEERKGSLERAK-------------------QYQQVIDNfpklSAELRQQLNNERDEPRSVP-PNM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 710 AEKEklaekLEQeEKLKAKIQQLTEEKAALEEsigQEKSR----SEEALEKAQARVRELENHLASQKEALENS---VAQE 782
Cdd:PRK10929 103 STDA-----LEQ-EILQVSSQLLEKSRQAQQE---QDRAReisdSLSQLPQQQTEARRQLNEIERRLQTLGTPntpLAQA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 783 KRKMREMlEAERRKAQDLENQLTQqkeISENNTYEKLKMRDTLEKEKR-----KIQDLENRLTKQ-KEEIE--------L 848
Cdd:PRK10929 174 QLTALQA-ESAALKALVDELELAQ---LSANNRQELARLRSELAKKRSqqldaYLQALRNQLNSQrQREAEralestelL 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720409123 849 KEQKENV---------LNNKLKDALvmVEDAQQMKTTESQR--AETLALKLKETLAEL 895
Cdd:PRK10929 250 AEQSGDLpksivaqfkINRELSQAL--NQQAQRMDLIASQQrqAASQTLQVRQALNTL 305
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
703-926 |
3.94e-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: 47.45 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 703 SLRQEHLAEKEKLAEKLEQEEKLKAKIQQ---------LTEEKAALEESiGQEKSRSEEALEKAQARVRELEN---HLAS 770
Cdd:pfam09787 4 SAKQELADYKQKAARILQSKEKLIASLKEgsgvegldsSTALTLELEEL-RQERDLLREEIQKLRGQIQQLRTelqELEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 771 QKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLekeKRKIQDLENRLTKQKEEIELKE 850
Cdd:pfam09787 83 QQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATL---QSRIKDREAEIEKLRNQLTSKS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720409123 851 QkenvlnnklkdalvmvEDAQQMKTTESQRAETLALKLKETLAE-LETTKTKMILTDDRLklqQQSMKALQDERESQ 926
Cdd:pfam09787 160 Q----------------SSSSQSELENRLHQLTETLIQKQTMLEaLSTEKNSLVLQLERM---EQQIKELQGEGSNG 217
|
|
| FHA_GarA-like |
cd22720 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis glycogen accumulation ... |
12-65 |
4.00e-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: 4.00e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1720409123 12 FVLNKSTT-IGKHADSDLVLQSADIDNHHAliEFNEAEGTFVLQDFNSRNGTFVN 65
Cdd:cd22720 19 FLLDQAITsAGRHPDSDIFLDDVTVSRRHA--EFRLENNEFNVVDVGSLNGTYVN 71
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
696-1199 |
4.07e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 696 ASRETQKSLRQEHLAEKEKLAEkLEQE-EKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELE------NHL 768
Cdd:PRK02224 234 ETRDEADEVLEEHEERREELET-LEAEiEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlddadaEAV 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 769 ASQKEALENsvaqEKRKMREMLEAERRKAQDLENQ---LTQQKEISENNTYEKLKMRDTLEKEkrkIQDLENRLTKQKEE 845
Cdd:PRK02224 313 EARREELED----RDEELRDRLEECRVAAQAHNEEaesLREDADDLEERAEELREEAAELESE---LEEAREAVEDRREE 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 846 IELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETtktkmilTDDRLKLQQQsmkaLQDERES 925
Cdd:PRK02224 386 IEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRT-------ARERVEEAEA----LLEAGKC 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 926 QKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNndtgpkeeasqdltagppLDSGDKEIacDHL 1005
Cdd:PRK02224 455 PECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED------------------LVEAEDRI--ERL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1006 IDDLLMAQKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQK--MELERQVALVRQQSGELSMLKA----------KV 1073
Cdd:PRK02224 515 EERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREaaAEAEEEAEEAREEVAELNSKLAelkeriesleRI 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1074 AQTTGLMEKKDRELKVLREALRASQEKprphlsTEQKPRTLSQKCDISLQIEPAHPDsfSSFQEEQSfsdlgvkcKGSRH 1153
Cdd:PRK02224 595 RTLLAAIADAEDEIERLREKREALAEL------NDERRERLAEKRERKRELEAEFDE--ARIEEARE--------DKERA 658
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1720409123 1154 EETIQRQRKALSELRTRVRELEKANSCnhkdhVNESFLELRTLRME 1199
Cdd:PRK02224 659 EEYLEQVEEKLDELREERDDLQAEIGA-----VENELEELEELRER 699
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
691-798 |
4.28e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.95 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 691 QAQMNASRETQKSLRQehLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELEnhlas 770
Cdd:COG2268 223 AEEAELEQEREIETAR--IAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQ----- 295
|
90 100
....*....|....*....|....*...
gi 1720409123 771 QKEAlENSVAQEKRKMREMLEAERRKAQ 798
Cdd:COG2268 296 EKEA-EREEAELEADVRKPAEAEKQAAE 322
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
287-763 |
4.39e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 287 LRQKEIESMKSQINALQKGYSQV--LSQTLAERNTEIESLKNEGENLKRDHAITSGMVT--SLQKDMSARNEQVQQLQEE 362
Cdd:COG4717 68 LNLKELKELEEELKEAEEKEEEYaeLQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 363 VNRLRIEN---REKEYQLEALSSRCSVMKEELrkEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNymgQNII 439
Cdd:COG4717 148 LEELEERLeelRELEEELEELEAELAELQEEL--EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA---QEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 440 SKTLREKNKVEEKLQEDSRRKLLQLQEMGNRENLIKINLERAVGQLENFRNQVIKATF--------GKTKPFRDKPITDQ 511
Cdd:COG4717 223 EELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFlvlgllalLFLLLAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 512 QRQHLRAciPPHRARTCAPTLQSLPRRAGCLETSYCLSSGQLIEKIIQVTEDNLSFQQRKWTLQRETHLHPKQEetmhsv 591
Cdd:COG4717 303 EAEELQA--LPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAA------ 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 592 eklrvLLDKCQACMRDscssiDLKKEVELLQHLplsplvsglqktvvnilrvslswlEETEQLLGDLDIELSDSDKGFSL 671
Cdd:COG4717 375 -----LLAEAGVEDEE-----ELRAALEQAEEY------------------------QELKEELEELEEQLEELLGELEE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 672 CLIYLLEHykKIMSQSQDLQAQMNASRETQKSLRQE---------HLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALees 742
Cdd:COG4717 421 LLEALDEE--ELEEELEELEEELEELEEELEELREElaeleaeleQLEEDGELAELLQELEELKAELRELAEEWAAL--- 495
|
490 500
....*....|....*....|.
gi 1720409123 743 igqekSRSEEALEKAQARVRE 763
Cdd:COG4717 496 -----KLALELLEEAREEYRE 511
|
|
| FHA_FhaA-like |
cd22668 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
17-87 |
4.72e-05 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaA and similar proteins; FhaA regulates cell growth and peptidoglycan synthesis by binding to MviN. It may inhibit the late stages of peptidoglycan synthesis. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438720 [Multi-domain] Cd Length: 91 Bit Score: 43.61 E-value: 4.72e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720409123 17 STTIGKHADSDLVLQSADIDNHHALIEFNEaeGTFVLQDFNSRNGTFVNECHIQnVAVKLIPGDILRFGSA 87
Cdd:cd22668 19 SNIIGRGSDADFRLPDTGVSRRHAEIRWDG--QVAHLTDLGSTNGTTVNNAPVT-PEWRLADGDVITLGHS 86
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
709-836 |
5.94e-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: 46.90 E-value: 5.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 709 LAEKEKLAEKLEQEE----KLKAKIQQLTEEKAALEESIGQ-------------EKSRSEEALEKAQARVRELENHLASQ 771
Cdd:pfam02841 154 LEERDKLEAKYNQVPrkgvKAEEVLQEFLQSKEAVEEAILQtdqaltakekaieAERAKAEAAEAEQELLREKQKEEEQM 233
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720409123 772 KEALENSVAQEKRKMREMLEAERRKAQDlENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLE 836
Cdd:pfam02841 234 MEAQERSYQEHVKQLIEKMEAEREQLLA-EQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
707-957 |
7.06e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 7.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 707 EHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIG-QEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRk 785
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELAERYAAARERLAeLEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELER- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 786 mremLEAERRKAQDLENQLTQQkeISENNTyeklkmrdtlekekRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDA-L 864
Cdd:COG4913 314 ----LEARLDALREELDELEAQ--IRGNGG--------------DRLEQLEREIERLERELEERERRRARLEALLAALgL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 865 VMVEDAQQMKTTESQRAETLAlKLKETLAELETTKtkmiltdDRLKLQQQsmkALQDERESQkhgfEEEISEYKEQIKQH 944
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLE-ALEEELEALEEAL-------AEAEAALR---DLRRELREL----EAEIASLERRKSNI 438
|
250
....*....|...
gi 1720409123 945 SQTIVSLEERLCQ 957
Cdd:COG4913 439 PARLLALRDALAE 451
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
712-940 |
7.88e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 712 KEKLAEKLEQEEKLKAKIQQLTEEKAALEesigqeksRSEEALEKAQARVRELENHLASQKEalensvaqekrkmremLE 791
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALE--------AELDALQERREALQRLAEYSWDEID----------------VA 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 792 AERRKAQDLENQLTQqkeISENNtyeklkmrDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQ 871
Cdd:COG4913 665 SAEREIAELEAELER---LDASS--------DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 872 -QMKTTESQRAETLALKLKETLAELETTKtkmILTDDRLKLQQQsMKALQDERESQKHGFEEEISEYKEQ 940
Cdd:COG4913 734 dRLEAAEDLARLELRALLEERFAAALGDA---VERELRENLEER-IDALRARLNRAEEELERAMRAFNRE 799
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
696-882 |
8.11e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 8.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 696 ASRETQKSLRQEHLAEKEKLAEKLEQE-EKLKAKIQQLTEEKAALEESIgqekSRSEEALEKAQARVRELENHLASQKEA 774
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAElDALQAELEELNEEYNELQAEL----EALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 775 LENSVAQEKRKMR---------------------EMLEAERRKAQDLENQLTQQKEISENntyEKLKMRDTLEKEKRKIQ 833
Cdd:COG3883 88 LGERARALYRSGGsvsyldvllgsesfsdfldrlSALSKIADADADLLEELKADKAELEA---KKAELEAKLAELEALKA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720409123 834 DLEnrltKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAE 882
Cdd:COG3883 165 ELE----AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
248-433 |
8.58e-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: 8.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 248 LQAEVADLSQRLSETAAVAAA---------RQSNRCDpKLQGVDEGD-DLR--QKEIESMKSQINALQKGYSQV--LSQT 313
Cdd:COG4913 615 LEAELAELEEELAEAEERLEAleaeldalqERREALQ-RLAEYSWDEiDVAsaEREIAELEAELERLDASSDDLaaLEEQ 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 314 LAERNTEIESLKNEGENLKRDHAitsgmvtSLQKDMSARNEQVQQLQEEVNrlRIENREKEYQLEALSSRCsvmkEELRK 393
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIG-------RLEKELEQAEEELDELQDRLE--AAEDLARLELRALLEERF----AAALG 760
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1720409123 394 EEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKNY 433
Cdd:COG4913 761 DAVERELRENLEERIDALRARLNRAEEELERAMRAFNREW 800
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
681-855 |
9.64e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 9.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 681 KKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIG------QEKSRSE--- 751
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraralYRSGGSVsyl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 752 ----------------EALEKAQARVRELENHLASQKEALENSVAQEKRKMREmLEAERRKAQDLENQLTQQKEisennt 815
Cdd:COG3883 106 dvllgsesfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAE-LEALKAELEAAKAELEAQQA------ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1720409123 816 yEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENV 855
Cdd:COG3883 179 -EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
713-914 |
9.79e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 9.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 713 EKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELEnhlaSQKEALENSVAQEKRKMREMLEA 792
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELE----EELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 793 ERRKAQDLENQLTQQKEISENNTYEKLKMR-DTLEKEKRKIQDLENRLTKQKEEI-ELKEQKENVLNNKLKDALVMVEDA 870
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLEELEERlEELRELEEELEELEAELAELQEELeELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1720409123 871 QQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQ 914
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
678-870 |
9.82e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.97 E-value: 9.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 678 EHYKKimsQSQDLQAQMNASRETQKSLRQEH----LAEKEKLAEkleQEEKLKAKIQQLTEEKAALEESIGQEKSRSEE- 752
Cdd:PRK10929 211 ELAKK---RSQQLDAYLQALRNQLNSQRQREaeraLESTELLAE---QSGDLPKSIVAQFKINRELSQALNQQAQRMDLi 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 753 ALEKAQA-----RVRELENHLASQK----------EALENSVAQ--EKRKM----REM--LEAERRKAQDLENQLTQQKE 809
Cdd:PRK10929 285 ASQQRQAasqtlQVRQALNTLREQSqwlgvsnalgEALRAQVARlpEMPKPqqldTEMaqLRVQRLRYEDLLNKQPQLRQ 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720409123 810 ISENNTYeklkmrdTLEKEKRKIqdLENRLTKQKEEIE----------LKEQKENVLNNKLKDALVMVEDA 870
Cdd:PRK10929 365 IRQADGQ-------PLTAEQNRI--LDAQLRTQRELLNsllsggdtliLELTKLKVANSQLEDALKEVNEA 426
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
282-1098 |
1.16e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.96 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 282 DEGDDL--RQKEIESMKSQINALQ---------KGYSQVLSQTLAERNTEI-----ESLKNEGENLKRDHAITSGMVTSL 345
Cdd:TIGR00606 245 NELDPLknRLKEIEHNLSKIMKLDneikalksrKKQMEKDNSELELKMEKVfqgtdEQLNDLYHNHQRTVREKERELVDC 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 346 QKDMSARNEQVQQLQEEvnRLRIENREKEYQLEALSSRCSVMKEELRKEEAQ----------------------KDRREA 403
Cdd:TIGR00606 325 QRELEKLNKERRLLNQE--KTELLVEQGRLQLQADRHQEHIRARDSLIQSLAtrleldgfergpfserqiknfhTLVIER 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 404 QEKELKLCRSQMQDMEKEVRKLREELKKNYMGQNIISKTLREKNKVEEKLQEDSRRKLLQLQEM-GNRENLIKinLERAV 482
Cdd:TIGR00606 403 QEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLeGSSDRILE--LDQEL 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 483 GQLENFRNQVIKATFGKTKPFRDKPITDQQRQHLRacipphRARTCAPTLQSLPRRAGCLETSYCLS-----SGQLIEKI 557
Cdd:TIGR00606 481 RKAERELSKAEKNSLTETLKKEVKSLQNEKADLDR------KLRKLDQEMEQLNHHTTTRTQMEMLTkdkmdKDEQIRKI 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 558 IQVTEDNLSFQQR--KWTLQRETHLHPKQEETMHSVEKLRVLLDKCQAC--MRDSCSSIDLKKEVELLQHLPLSPLVSGL 633
Cdd:TIGR00606 555 KSRHSDELTSLLGyfPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLeqNKNHINNELESKEEQLSSYEDKLFDVCGS 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 634 QKTVVNILRV---------SLSWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQDLQAQMNASRETQKSL 704
Cdd:TIGR00606 635 QDEESDLERLkeeieksskQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKST 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 705 rqehlaekEKLAEKLEQEEKLkakIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKR 784
Cdd:TIGR00606 715 --------ESELKKKEKRRDE---MLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEES 783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 785 K---MREMLEAERRKAQDLENQLTQQKEISENNTYEklkMRDTLEKEKRKIQDLENRLTKQKEEIEL-----KEQKENVL 856
Cdd:TIGR00606 784 AkvcLTDVTIMERFQMELKDVERKIAQQAAKLQGSD---LDRTVQQVNQEKQEKQHELDTVVSKIELnrkliQDQQEQIQ 860
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 857 N-----NKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFE 931
Cdd:TIGR00606 861 HlksktNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQ 940
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 932 EEISEYKEQIKQHSQTIVSLEERLCQVTQYYQK-IEGEITTLK---NNDTGPKEEASQDL-TAGPPLDSGDKeiacdhli 1006
Cdd:TIGR00606 941 DKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKqKETELNTVNaqlEECEKHQEKINEDMrLMRQDIDTQKI-------- 1012
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1007 ddllmaQKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQKMELERQVALVRQqsgELSMLKAKVAQTTGLMEKKDRE 1086
Cdd:TIGR00606 1013 ------QERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEE---NIDLIKRNHVLALGRQKGYEKE 1083
|
890
....*....|..
gi 1720409123 1087 LKVLREALRASQ 1098
Cdd:TIGR00606 1084 IKHFKKELREPQ 1095
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
259-471 |
1.21e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 259 LSETAAVAAARQSNRCDPKLQGVDEGDDLRQKEIESMKSQINALQKGYSQVLSQtLAERNTEIESLKNE----GENLKRD 334
Cdd:COG3883 6 LAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE-LEALQAEIDKLQAEiaeaEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 335 HAITSGMVTSLQKDMSARNE-----QVQQLQEEVNRLRIENREKEYQLEALSSrcsvMKEELRKEEAQKDRREAQEKELK 409
Cdd:COG3883 85 REELGERARALYRSGGSVSYldvllGSESFSDFLDRLSALSKIADADADLLEE----LKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720409123 410 LCRSQMQDMEKEVRKLREELkknymgQNIISKTLREKNKVEEKLQEDSRRKLLQLQEMGNRE 471
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQ------EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
12-85 |
1.22e-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: 1.22e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720409123 12 FVLNKST-TIGKHADSDLVLQSADIDNHHALIEFNEaeGTFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRFG 85
Cdd:cd22680 16 FPFDFSSvSIGRDPENVIVIPDPFVSRNHARITVDS--NEIYIEDLGSTNGTFVNDFKRIKGPAKLHPNDIIKLG 88
|
|
| FHA_OdhI-like |
cd22721 |
forkhead associated (FHA) domain found in Corynebacterium glutamicum oxoglutarate ... |
7-65 |
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: 42.77 E-value: 1.31e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 7 SADGFFVLNK-STTIGKHADSDLVLQSADIDNHHAliEFNEAEGTFVLQDFNSRNGTFVN 65
Cdd:cd22721 19 NAGARFLLDQpTTTAGRHPESDIFLDDVTVSRRHA--EFRINEGEFEVVDVGSLNGTYVN 76
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
707-852 |
1.58e-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: 44.92 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 707 EHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSR---SEEALEKAQARVRELENHLASQKEALENSVAQ-- 781
Cdd:COG1579 4 EDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARleaAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlg 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720409123 782 EKRKMREM------LEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQK 852
Cdd:COG1579 84 NVRNNKEYealqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
688-869 |
1.62e-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: 44.92 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 688 QDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRsEEALEKAQARV---REL 764
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR-IKKYEEQLGNVrnnKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 765 ENhLASQKEALENSVAQEKRKMREM---LEAERRKAQDLENQLTQQKEISEnntyeklKMRDTLEKEKRKIQDLENRLTK 841
Cdd:COG1579 92 EA-LQKEIESLKRRISDLEDEILELmerIEELEEELAELEAELAELEAELE-------EKKAELDEELAELEAELEELEA 163
|
170 180 190
....*....|....*....|....*....|....
gi 1720409123 842 QKEEI------ELKEQKENVLNNKLKDALVMVED 869
Cdd:COG1579 164 EREELaakippELLALYERIRKRKNGLAVVPVEG 197
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
705-1199 |
1.63e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.50 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 705 RQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLA--------------- 769
Cdd:TIGR00618 213 MPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAvleetqerinrarka 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 770 -------------SQKEALENSVAQEKRKMREML----------EAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLE 826
Cdd:TIGR00618 293 aplaahikavtqiEQQAQRIHTELQSKMRSRAKLlmkraahvkqQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISC 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 827 KEKrkiqDLENRLTKQKEEIELKEQKENVLNNKLKdalvmVEDAQQmKTTESQRAETLALKLKETLAELETTKTKMILTD 906
Cdd:TIGR00618 373 QQH----TLTQHIHTLQQQKTTLTQKLQSLCKELD-----ILQREQ-ATIDTRTSAFRDLQGQLAHAKKQQELQQRYAEL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 907 DRLKLQQQSMKALQDERESQKhgFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQD 986
Cdd:TIGR00618 443 CAAAITCTAQCEKLEKIHLQE--SAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDI 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 987 LTAGPpldsgdkeiacdhLIDDLLMAQKEILSQQEIIMKLRTDLGEAHSRMSDLRGELSEKQKmELERQVALVRQQSGEL 1066
Cdd:TIGR00618 521 DNPGP-------------LTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQ-SFSILTQCDNRSKEDI 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1067 SMLKAKVAQTTGLMEKKDRELKVLREALRASQEKPRPHLSTEQKPRTLsQKCDISLQIEPAHPDSFSS--FQEEQSFSDL 1144
Cdd:TIGR00618 587 PNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHL-QQCSQELALKLTALHALQLtlTQERVREHAL 665
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720409123 1145 GVKCKGSRHEETIQRQRKAL-SELRTRVRELEKANSCNHKDH-VNESFLELRTLRME 1199
Cdd:TIGR00618 666 SIRVLPKELLASRQLALQKMqSEKEQLTYWKEMLAQCQTLLReLETHIEEYDREFNE 722
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
698-848 |
2.03e-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: 45.71 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 698 RETQKSLRQEHLAEKEKLAEKLEQE-----EKLKAKIQQLTEEKAALEEsigqEKSRSEEALEKAQARVRELENHLASQK 772
Cdd:pfam15709 357 QEEQRRLQQEQLERAEKMREELELEqqrrfEEIRLRKQRLEEERQRQEE----EERKQRLQLQAAQERARQQQEEFRRKL 432
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720409123 773 EALENSVAQEKrkmREMLEAERRKAQDLENQLT-QQKEISENNTYEKLK-MRDTLEKEKRKIQDLENRLTKQKEEIEL 848
Cdd:pfam15709 433 QELQRKKQQEE---AERAEAEKQRQKELEMQLAeEQKRLMEMAEEERLEyQRQKQEAEEKARLEAEERRQKEEEAARL 507
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
681-943 |
2.08e-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: 45.22 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 681 KKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEklkAKIQQLTEEKAALEESIGQEKSRSEEALEKAQAR 760
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQ---ARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 761 VrelenhlASQKEALENSVAQEKrkmremlEAERRKAQDLENQLTQQKEISENntyeklkmrdtlEKEKRKIQDLENRLT 840
Cdd:TIGR02794 123 E-------AKAKQAAEAKAKAEA-------EAERKAKEEAAKQAEEEAKAKAA------------AEAKKKAEEAKKKAE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 841 KQKEEIELKEQKENVLNNKLKdalvmvedAQQMKTTESQRAETLALKLKETLAELETTKTKMILT-DDRLKLQQQSMKAL 919
Cdd:TIGR02794 177 AEAKAKAEAEAKAKAEEAKAK--------AEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAElGDIFGLASGSNAEK 248
|
250 260
....*....|....*....|....
gi 1720409123 920 QDERESQKHGfeEEISEYKEQIKQ 943
Cdd:TIGR02794 249 QGGARGAAAG--SEVDKYAAIIQQ 270
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
723-847 |
2.63e-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: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 723 EKLKAKIQQLTEEKAALEESigqEKSRSEEALEKAQARVRELENHLASQKEALEN--SVAQEKRKMREMLEAERRKAQDL 800
Cdd:COG0542 414 DELERRLEQLEIEKEALKKE---QDEASFERLAELRDELAELEEELEALKARWEAekELIEEIQELKEELEQRYGKIPEL 490
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720409123 801 ENQLTQ-QKEISENNTYEKL--------------------KMrdtLEKEKRKIQDLENRLTK----QKEEIE 847
Cdd:COG0542 491 EKELAElEEELAELAPLLREevteediaevvsrwtgipvgKL---LEGEREKLLNLEEELHErvigQDEAVE 559
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
688-960 |
2.66e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 688 QDLQAQMNASREtqkslrQEHLAEKEKLAEK-LEQEEKLKAKIQQLTEEKAALEESIGQeksrSEEALEKAQARVRELEN 766
Cdd:PRK11281 39 ADVQAQLDALNK------QKLLEAEDKLVQQdLEQTLALLDKIDRQKEETEQLKQQLAQ----APAKLRQAQAELEALKD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 767 HLASQ-KEALEN-SVAQEKRKMREMLEAERRKAQDLE-------NQLTQ----QKEISENNTyeklkmrdtlekekrKIQ 833
Cdd:PRK11281 109 DNDEEtRETLSTlSLRQLESRLAQTLDQLQNAQNDLAeynsqlvSLQTQperaQAALYANSQ---------------RLQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 834 DLENRLTKQK-EEIELKEQKENVLNNKLkdALVMVEDAQQMKTTE----------SQRAEtlaLKLKETLAELETTKTKM 902
Cdd:PRK11281 174 QIRNLLKGGKvGGKALRPSQRVLLQAEQ--ALLNAQNDLQRKSLEgntqlqdllqKQRDY---LTARIQRLEHQLQLLQE 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720409123 903 ILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQ 960
Cdd:PRK11281 249 AINSKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLLKATEKLNTLTQ 306
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
735-963 |
2.91e-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: 45.60 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 735 EKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEALENSVAqekrkmremleAERRKAQDLENQLTQQKEISENN 814
Cdd:pfam12128 594 EWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASR-----------EETFARTALKNARLDLRRLFDEK 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 815 TYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELK------EQKENVLNNKLkdalvmvEDAQQMKTTESQRAETLALkL 888
Cdd:pfam12128 663 QSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKhqawleEQKEQKREART-------EKQAYWQVVEGALDAQLAL-L 734
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720409123 889 KETLAELETTKtkmiltDDRLKLQQQSMKalqdeRESQKHGFEEE-ISEYKEQIKQHSQTIVSLEERLCQVTQYYQ 963
Cdd:pfam12128 735 KAAIAARRSGA------KAELKALETWYK-----RDLASLGVDPDvIAKLKREIRTLERKIERIAVRRQEVLRYFD 799
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
15-87 |
3.35e-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: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 15 NKSTTIGKHADSD-----LVLQSADIDNHHALIEFNEaeGTFVLQDFNSRNGTFVNECHIQ------NVAVKLIPGDILR 83
Cdd:cd22702 31 KQPCIIGSDPHQAisgisVVIPSPQVSELHARITCKN--GAFFLTDLGSEHGTWINDNEGRryrappNFPVRLHPSDVIE 108
|
....
gi 1720409123 84 FGSA 87
Cdd:cd22702 109 FGSD 112
|
|
| FHA_PML1-like |
cd22681 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ... |
27-95 |
3.39e-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: 3.39e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720409123 27 DLVLQSADIDNHHALIEFNEAEGTFV--LQDFNSRNGTFVNECHI-QNVAVKLIPGDILRFgSAGMTYELVI 95
Cdd:cd22681 58 DIGIPEETCSKQHCVIQFRNVKGILKpyIMDLDSSNGTCLNDNVIpSSRYVELRSGDVITF-SKSNDYELVF 128
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
345-799 |
3.57e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 345 LQKDMSARNEQVQQLQEEVNRLRIENREKEYQLEALS--SRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEV 422
Cdd:COG4717 93 LQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRELEEELEELEAEL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 423 RKLREELKknymgqniisktlREKNKVEEKLQEDSRRKLLQLQEMGNRENLIKINLERAVGQLENFRNQVikatfgktKP 502
Cdd:COG4717 173 AELQEELE-------------ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL--------EQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 503 FRDKPITDQQRQHLRACipphRARTCAPTLQSLPRRAGCLETSYCLSSGQLIEKIIQVTEDNLSFQQRKwtlqrethlHP 582
Cdd:COG4717 232 LENELEAAALEERLKEA----RLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLARE---------KA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 583 KQEETMHSVEKLRVLLDKCQACMRDSCSSIDLKKEVELLQHLPLSPLVSGLQKTVVNI--LRVSLSWLEETEQLLGDLDI 660
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAeeLEEELQLEELEQEIAALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 661 ELSDSDKGFSLCLIyLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAE--KEKLAEKLEQEEKLKAKIQQLTEEKAA 738
Cdd:COG4717 379 AGVEDEEELRAALE-QAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELEELREELAE 457
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720409123 739 LEESIgqEKSRSEEALEKAQARVRELENHLASQKEAlensvAQEKRKMREMLEAERRKAQD 799
Cdd:COG4717 458 LEAEL--EQLEEDGELAELLQELEELKAELRELAEE-----WAALKLALELLEEAREEYRE 511
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
746-975 |
3.80e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 746 EKSRSEEALEKAQARVRELENHlasqKEALENsvAQEKRKMREMLEAERRKAQDLENQLTQQkeisenntyEKLKMRDTL 825
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERA----HEALED--AREQIELLEPIRELAERYAAARERLAEL---------EYLRAALRL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 826 EKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDA-QQMKTTESQRAETLALKLKETLAELETTKTKMIL 904
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELeAQIRGNGGDRLEQLEREIERLERELEERERRRAR 363
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720409123 905 TDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNN 975
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
689-974 |
3.93e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 45.21 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 689 DLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEK----LKAKIQQLTEEKAALEESIGQE----------------KS 748
Cdd:PTZ00440 956 NLKMQIEKTLEYYDKSKENINGNDGTHLEKLDKEKDewehFKSEIDKLNVNYNILNKKIDDLikkqhddiielidkliKE 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 749 RSEEALEKAQARVRELEN--------HLASQKEALENSVAQEK-RKMREMLEAERRKAQDLENQLTQQKEISENNTY--- 816
Cdd:PTZ00440 1036 KGKEIEEKVDQYISLLEKmktklssfHFNIDIKKYKNPKIKEEiKLLEEKVEALLKKIDENKNKLIEIKNKSHEHVVnad 1115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 817 -EKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNN----KLKDALVMVEDAQQMKTTESQRAETLALKLKET 891
Cdd:PTZ00440 1116 kEKNKQTEHYNKKKKSLEKIYKQMEKTLKELENMNLEDITLNEvneiEIEYERILIDHIVEQINNEAKKSKTIMEEIESY 1195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 892 LAELETTKTKMILTD----DRLKLQQQSMKALQDERE----SQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQ 963
Cdd:PTZ00440 1196 KKDIDQVKKNMSKERndhlTTFEYNAYYDKATASYENieelTTEAKGLKGEANRSTNVDELKEIKLQVFSYLQQVIKENN 1275
|
330
....*....|.
gi 1720409123 964 KIEGEITTLKN 974
Cdd:PTZ00440 1276 KMENALHEIKN 1286
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
403-835 |
4.03e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 403 AQEKELKLCRSQMQDMEKEVRKLREELKKNYMGQNIISKTLREKNKVEEKLQEDSRRKLLQLQEMGNRENLIKINLERAV 482
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 483 GQLENFRNQVIKATFGKTKPFRDKPITDQQRQHLRACIPPHRARtcaptLQSLPRRAGCLETsyclssgqliekiiQVTE 562
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE-----LKALREALDELRA--------------ELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 563 DNLSFQQRKWTLQREthlhpkqEETMHSVEKLRVLLDKcqacmrdscSSIDLKKEVELLQHLplsplvsglqktvvnilr 642
Cdd:TIGR02168 815 LNEEAANLRERLESL-------ERRIAATERRLEDLEE---------QIEELSEDIESLAAE------------------ 860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 643 vslswLEETEQLLGDLDIELSDSDKGFSlcliYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQE 722
Cdd:TIGR02168 861 -----IEELEELIEELESELEALLNERA----SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL 931
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 723 EKLKAKIQQ----LTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLAS----QKEALENSVAQEKRKmrEMLEAER 794
Cdd:TIGR02168 932 EGLEVRIDNlqerLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvNLAAIEEYEELKERY--DFLTAQK 1009
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1720409123 795 RKAQDLENQLtqQKEISENNTYEKLKMRDTLEKEKRKIQDL 835
Cdd:TIGR02168 1010 EDLTEAKETL--EEAIEEIDREARERFKDTFDQVNENFQRV 1048
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
707-889 |
4.46e-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: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 707 EHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIgqekSRSEEALEKAQARVreLENHLASQKEALE---NSVAQEK 783
Cdd:NF012221 1549 KHAKQDDAAQNALADKERAEADRQRLEQEKQQQLAAI----SGSQSQLESTDQNA--LETNGQAQRDAILeesRAVTKEL 1622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 784 RKMREMLEAERRKAQ-------------------DLENQL--------TQQKEISENNTYEKLKMRDTLEKEK------- 829
Cdd:NF012221 1623 TTLAQGLDALDSQATyagesgdqwrnpfagglldRVQEQLddakkisgKQLADAKQRHVDNQQKVKDAVAKSEagvaqge 1702
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720409123 830 RKIQDLENRLTKQKEEIELKEQ----KENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLK 889
Cdd:NF012221 1703 QNQANAEQDIDDAKADAEKRKDdalaKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQ 1766
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
681-943 |
4.49e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 681 KKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQAR 760
Cdd:COG1340 11 EELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 761 VRELENHLASQKEalENSVAQEKRKMREMLEAERRKAQ------DLENQLTQQ-KEISenntyEKLKMRDTLEKEKRKIQ 833
Cdd:COG1340 91 REELDELRKELAE--LNKAGGSIDKLRKEIERLEWRQQtevlspEEEKELVEKiKELE-----KELEKAKKALEKNEKLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 834 DLENRLTKQKEEI-ELKEQKENVLN--NKLKDALV-MVEDAQQMKttesQRAETLALKLKETLAELETTKTKMILTDDRL 909
Cdd:COG1340 164 ELRAELKELRKEAeEIHKKIKELAEeaQELHEEMIeLYKEADELR----KEADELHKEIVEAQEKADELHEEIIELQKEL 239
|
250 260 270
....*....|....*....|....*....|....*
gi 1720409123 910 -KLQQQSMKALQDERESQKHGFEEEISEYKEQIKQ 943
Cdd:COG1340 240 rELRKELKKLRKKQRALKREKEKEELEEKAEEIFE 274
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
770-992 |
5.01e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 770 SQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQ-QKEIsenntyeklkmrDTLEKEkrkIQDLENRLTKQKEEIE- 847
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEAlQAEI------------DKLQAE---IAEAEAEIEERREELGe 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 848 -LKEQKENVLNNKLKDALVMVED-------AQQMKTTESQRAETLAlKLKETLAELETTKTKMILTDDRLKLQQQSMKAL 919
Cdd:COG3883 91 rARALYRSGGSVSYLDVLLGSESfsdfldrLSALSKIADADADLLE-ELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720409123 920 QDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAGPP 992
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
662-1180 |
5.38e-04 |
|
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: 44.72 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 662 LSDSDKGFSLCLIYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAK-----------IQ 730
Cdd:pfam15921 403 LWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQlestkemlrkvVE 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 731 QLTEEKAALEESIG---------QEKSRSEEA----LEKAQARV----RELEnHLASQKEALENSVAQ---------EKR 784
Cdd:pfam15921 483 ELTAKKMTLESSERtvsdltaslQEKERAIEAtnaeITKLRSRVdlklQELQ-HLKNEGDHLRNVQTEcealklqmaEKD 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 785 KMREMLeaeRRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLenRLTKQKEEIELKEQKENV--------- 855
Cdd:pfam15921 562 KVIEIL---RQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEF--KILKDKKDAKIRELEARVsdlelekvk 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 856 LNNKLKDALVMVEDAQQ--------MKTTE------SQRAETLALKLKETLAELETT--KTKMILTDDRLKLQQ-----Q 914
Cdd:pfam15921 637 LVNAGSERLRAVKDIKQerdqllneVKTSRnelnslSEDYEVLKRNFRNKSEEMETTtnKLKMQLKSAQSELEQtrntlK 716
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 915 SMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEE---------------------RLCQVTQYYQKIEGEITTLK 973
Cdd:pfam15921 717 SMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEamtnankekhflkeeknklsqELSTVATEKNKMAGELEVLR 796
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 974 NNDTGPKEEASQDLTAgppLDSGDKEIA-CDHLIddllmaQKEilSQQEIIMKLRTDL------GEAHSRMSDLRGELse 1046
Cdd:pfam15921 797 SQERRLKEKVANMEVA---LDKASLQFAeCQDII------QRQ--EQESVRLKLQHTLdvkelqGPGYTSNSSMKPRL-- 863
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1047 KQKMELERQVALVRQQSGELSMLKAKVAQTTGLMEKKDRELKVLREALRAS-QEKPRPHLS-TEQKPRTLS--------Q 1116
Cdd:pfam15921 864 LQPASFTRTHSNVPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQELRSViNEEPTVQLSkAEDKGRAPSlgalddrvR 943
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720409123 1117 KCDISLQIEPAHPDSFSSFqeeqsfsdlgVKCKGSRHEETIQRQRKALselrtRVRELEKANSC 1180
Cdd:pfam15921 944 DCIIESSLRSDICHSSSNS----------LQTEGSKSSETCSREPVLL-----HAGELEDPSSC 992
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
706-836 |
6.34e-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: 43.33 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 706 QEHLAEKEKLAEKLEQEEK--LKAK--IQQLTEEKAALEESIGQ-------------EKSRSEEALEKAQARVRELENHL 768
Cdd:cd16269 145 QLYLEDREKLVEKYRQVPRkgVKAEevLQEFLQSKEAEAEAILQadqaltekekeieAERAKAEAAEQERKLLEEQQREL 224
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720409123 769 ASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEiSENNTYEKLKMRDTLEKEKRKIQDLE 836
Cdd:cd16269 225 EQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERALESKL-KEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
676-988 |
6.41e-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: 44.12 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 676 LLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALE 755
Cdd:pfam07888 46 LLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 756 KAQARVRELENHLAS------QKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEK 829
Cdd:pfam07888 126 AHEARIRELEEDIKTltqrvlERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRD 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 830 RKIQDLENRLTKQKEEIELKEQKENVLNNKLKDalvmVEDAQQMKTTESQRAETLALKLKETL------------AELET 897
Cdd:pfam07888 206 TQVLQLQDTITTLTQKLTTAHRKEAENEALLEE----LRSLQERLNASERKVEGLGEELSSMAaqrdrtqaelhqARLQA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 898 TKTKMILTDDRLKLQQQSMKALQdERESQKHGFEEEiseyKEQIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKNNDT 977
Cdd:pfam07888 282 AQLTLQLADASLALREGRARWAQ-ERETLQQSAEAD----KDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNR 356
|
330
....*....|.
gi 1720409123 978 GPKEEASQDLT 988
Cdd:pfam07888 357 VQLSESRRELQ 367
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
745-903 |
6.95e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.93 E-value: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 745 QEKSRSEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEIsenntyeklkmrdt 824
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQ-------------- 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720409123 825 LEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQmkttesqrAETLALKLKETLAELETTKTKMI 903
Cdd:PRK12705 93 LDARAEKLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTP--------EQARKLLLKLLDAELEEEKAQRV 163
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
11-93 |
9.16e-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: 9.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 11 FFVLNKSTTIG-----------KHADSDLVLqSADIDNHHALIEFNEAEGTFVLQDFnSRNGTFVNE--CHIQNVAVKLI 77
Cdd:cd22701 12 YYVQKLEVVLGrnsknssstaaDSVDIDLGP-SKKISRRHARIFYDFTTQCFELSVL-GRNGVKVDGilVKPGSPPVPLR 89
|
90
....*....|....*.
gi 1720409123 78 PGDILRFGSAGMTYEL 93
Cdd:cd22701 90 SGSLIQIGGVLFYFLL 105
|
|
| FHA_Rv1747-like_rpt2 |
cd22737 |
second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
20-92 |
9.84e-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: 9.84e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720409123 20 IGKHADSDLVLQSADIDNHHALIEfnEAEGTFVLQDFNSRNGTFVNECHIQnvAVKLIPGDILRFGSAGMTYE 92
Cdd:cd22737 25 IGRASDNDIVIPEGSVSRHHATLV--PTPGGTQIRDLRSTNGTFVNGLRVD--AALLHDGDVVTIGDIDFVFE 93
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
15-85 |
1.11e-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: 1.11e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720409123 15 NKSTTIGKHADS--DLVLQ-SADIDNHHALIEFNeAEGTFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFG 85
Cdd:cd22663 20 GKEVTVGRGLGVtyQLVSTcPLMISRNHCVLKKN-DEGQWTIKDNKSLNGVWVNGERIEpLKPYPLNEGDLIQLG 93
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
214-471 |
1.36e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 214 QQDKDEIILLLGRE---VNRLSDFEMESKYKDALIMNLQAEVADLSQRLSETAAVAAARQSnrcdpKLQGVDEGDDLRQK 290
Cdd:COG1196 277 EELELELEEAQAEEyelLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE-----ELEELEEELEEAEE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 291 EIESMKSQINALQKGYSQVLSQtLAERNTEIESLKNEGENLKRDHAITsgmvtslqkdmsARNEQVQQLQEEVNRLRIEN 370
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAE-LAEAEEELEELAEELLEALRAAAEL------------AAQLEELEEAEEALLERLER 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 371 REKEYQLEALSSRcsvmKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKnymgqniisktLREKNKVE 450
Cdd:COG1196 419 LEEELEELEEALA----ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL-----------EAALAELL 483
|
250 260
....*....|....*....|.
gi 1720409123 451 EKLQEDSRRKLLQLQEMGNRE 471
Cdd:COG1196 484 EELAEAAARLLLLLEAEADYE 504
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
698-934 |
1.66e-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: 43.24 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 698 RETQKSLRQEHLAEKEKLAEKLEQEEK-LKAKIQQLTEEKAALEESIGQEK---SRSEEALEKAQARVRELENHLASQKE 773
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKeLEKKHQQLCEEKNALQEQLQAETelcAEAEEMRARLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 774 ALE------NSVAQEKRKMREMLeaerrkaQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIE 847
Cdd:pfam01576 83 RLEeeeersQQLQNEKKKMQQHI-------QDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 848 LKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLK---ETLAELETTKTKMILTDDRLKLQQQSMKALQDERE 924
Cdd:pfam01576 156 LLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKkeeKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELR 235
|
250
....*....|
gi 1720409123 925 SQKHGFEEEI 934
Cdd:pfam01576 236 AQLAKKEEEL 245
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
706-842 |
1.80e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 706 QEHLAEKEKLAEKLE-----------QEEKLKAKIQQLTEEKAALEESIGQeksrseeaLEKAQARVRELENHLASQKEA 774
Cdd:COG4913 667 EREIAELEAELERLDassddlaaleeQLEELEAELEELEEELDELKGEIGR--------LEKELEQAEEELDELQDRLEA 738
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720409123 775 LENSVAQEkrkMREMLEaERRKAQDLENqltQQKEISENntyeklkMRDTLEKEKRKIQDLENRLTKQ 842
Cdd:COG4913 739 AEDLARLE---LRALLE-ERFAAALGDA---VERELREN-------LEERIDALRARLNRAEEELERA 792
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
689-955 |
1.83e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 689 DLQAQMNASRETQKSLRQEHLAEKEKLA---------EKLEQ-EEKLKAKIQQLTEEKAALEESIGQeKSRSEEALEKAQ 758
Cdd:PRK04863 311 EMARELAELNEAESDLEQDYQAASDHLNlvqtalrqqEKIERyQADLEELEERLEEQNEVVEEADEQ-QEENEARAEAAE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 759 ARVRELENHLASQKEALEnsvAQEKR--------------------------KMREMLEAERRKAQDLENQLTQ--QK-- 808
Cdd:PRK04863 390 EEVDELKSQLADYQQALD---VQQTRaiqyqqavqalerakqlcglpdltadNAEDWLEEFQAKEQEATEELLSleQKls 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 809 ---------------------EISENN----------TYEKLKMRD-TLEKEKRKIQDLENRLTKQKEEIELKEQKENVL 856
Cdd:PRK04863 467 vaqaahsqfeqayqlvrkiagEVSRSEawdvarellrRLREQRHLAeQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRL 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 857 NNKLKDALV----------MVEDAQQMKTTESQRAETLALKLKET---LAELETTKTKMILTDDRL-KLQQQS------- 915
Cdd:PRK04863 547 GKNLDDEDEleqlqeeleaRLESLSESVSEARERRMALRQQLEQLqarIQRLAARAPAWLAAQDALaRLREQSgeefeds 626
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1720409123 916 ------MKALQD-ERESQ--KHGFEEEISEYKEQIKQHSQTIVSLEERL 955
Cdd:PRK04863 627 qdvteyMQQLLErERELTveRDELAARKQALDEEIERLSQPGGSEDPRL 675
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
711-834 |
1.86e-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: 42.12 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 711 EKEKLAEKLEQEEK-----LKAKIQQLTEEKAALEESIGQEKSRseealekaqarvreLENHLASQKEALENSVAQEKRK 785
Cdd:pfam09755 93 EKETLAMNYEQEEEfltndLSRKLTQLRQEKVELEQTLEQEQEY--------------QVNKLMRKIEKLEAETLNKQTN 158
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1720409123 786 mremLEAERRKAQDLENQLTQQKEISENNTYEKLkmrDTLEKEKRKIQD 834
Cdd:pfam09755 159 ----LEQLRREKVELENTLEQEQEALVNRLWKRM---DKLEAEKRLLQE 200
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
817-948 |
2.03e-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: 41.45 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 817 EKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENvlnnKLKDALVMVEDAQQMK------TTESQRAETLALKLKE 890
Cdd:COG1579 39 ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK----KYEEQLGNVRNNKEYEalqkeiESLKRRISDLEDEILE 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720409123 891 TLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTI 948
Cdd:COG1579 115 LMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
219-842 |
2.13e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 219 EIILLLGREVNRLSDFEMESKYKDALIMNLQAEVADLSQRLSETAAVAaarqsnrcdPKLQGVDEGDDLRQKEIESMKSQ 298
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSEL---------PELREELEKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 299 INALQKGYSQVLSQ--TLAERNTEIESLKNEGENLKRDHAITSGMVTSLQKDMsarnEQVQQLQEEVNRLRIENREKEYQ 376
Cdd:PRK03918 240 IEELEKELESLEGSkrKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKA----EEYIKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 377 LEALSSRCSVMKEELRKEEAQKDRREAQEKELKlcrsqmqDMEKEVRKLREEL--------KKNYMGQNIISKTLREKNK 448
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERLEELKKKLK-------ELEKRLEELEERHelyeeakaKKEELERLKKRLTGLTPEK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 449 VEEKLQEDSRRKlLQLQEMGNRENLIKINLERAVGQLENFRNQVIKATfgKTKPFRDKPITDQQRQHLRAcipphrartc 528
Cdd:PRK03918 389 LEKELEELEKAK-EEIEEEISKITARIGELKKEIKELKKAIEELKKAK--GKCPVCGRELTEEHRKELLE---------- 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 529 aptlqslprragcletSYCLSSGQLIEKIIQVTEDNLSFQQRKWTLQRETHLHPKqeetmhsVEKLRVLLDKCQAcMRDS 608
Cdd:PRK03918 456 ----------------EYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESE-------LIKLKELAEQLKE-LEEK 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 609 CSSIDLKK-EVELLQHLPLSPLVSGLQKTVVNILRvSLSWLEETEQLLGDLDIELSDSDKGFSLCLIYLLEH-YKKIMSQ 686
Cdd:PRK03918 512 LKKYNLEElEKKAEEYEKLKEKLIKLKGEIKSLKK-ELEKLEELKKKLAELEKKLDELEEELAELLKELEELgFESVEEL 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 687 SQDLQAQMNASRETQKSLRQEH-LAEKEKLAEKLeqEEKLKAKIQQLTEEKAALEESIGQ----EKSRSEEALEKAQARV 761
Cdd:PRK03918 591 EERLKELEPFYNEYLELKDAEKeLEREEKELKKL--EEELDKAFEELAETEKRLEELRKEleelEKKYSEEEYEELREEY 668
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 762 RELENHLASQKEALEnsvaqekrKMREMLEAERRKAQDLENQLTQQKEISENntYEKL-KMRDTLEKEKRKIQDLENRLT 840
Cdd:PRK03918 669 LELSRELAGLRAELE--------ELEKRREEIKKTLEKLKEELEEREKAKKE--LEKLeKALERVEELREKVKKYKALLK 738
|
..
gi 1720409123 841 KQ 842
Cdd:PRK03918 739 ER 740
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
711-965 |
2.15e-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: 42.11 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 711 EKEKLAEKLEQE-EKLKAKIQQLTEEKAALEESIGQ-EKSRSE--EALEKAQARVRELENhlasQKEAleNSVAQEKRKM 786
Cdd:pfam15905 91 EQDKRLQALEEElEKVEAKLNAAVREKTSLSASVASlEKQLLEltRVNELLKAKFSEDGT----QKKM--SSLSMELMKL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 787 REMLEAERRKAQDLENQLTQQKEISENNtyeklkmrdtLEKEKRKIQDLENRL-TKQKEEIELKEQKENVLNNKLKdaLV 865
Cdd:pfam15905 165 RNKLEAKMKEVMAKQEGMEGKLQVTQKN----------LEHSKGKVAQLEEKLvSTEKEKIEEKSETEKLLEYITE--LS 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 866 MVEDAQQMKTTESQRAETLalkLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKhgfEEEISEYKEQIKQHS 945
Cdd:pfam15905 233 CVSEQVEKYKLDIAQLEEL---LKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEK---EELLREYEEKEQTLN 306
|
250 260
....*....|....*....|
gi 1720409123 946 QTIVSLEERLCQVTQYYQKI 965
Cdd:pfam15905 307 AELEELKEKLTLEEQEHQKL 326
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
248-469 |
2.20e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 248 LQAEVADLSQRLSETAAVAAARQsnrcdpklqgvdegdDLRQ-----KEIESMKSQINALQKGYSQvLSQTLAERNTEIE 322
Cdd:PRK11281 41 VQAQLDALNKQKLLEAEDKLVQQ---------------DLEQtlallDKIDRQKEETEQLKQQLAQ-APAKLRQAQAELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 323 SLKNEG-ENLKRDHAITSgmVTSLQKDMSARNEQVQQLQEEVNrlrienrekEY--QLEALSSrcsvmkeelRKEEAQKD 399
Cdd:PRK11281 105 ALKDDNdEETRETLSTLS--LRQLESRLAQTLDQLQNAQNDLA---------EYnsQLVSLQT---------QPERAQAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720409123 400 RREAQEkelklcRSQmqdmekevrKLREELKKNYMGQNIISKTLREKNKVEEKL---QEDSRRKLL----QLQEMGN 469
Cdd:PRK11281 165 LYANSQ------RLQ---------QIRNLLKGGKVGGKALRPSQRVLLQAEQALlnaQNDLQRKSLegntQLQDLLQ 226
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
783-1175 |
2.26e-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: 42.80 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 783 KRKMREMLEAERRKAQDLENQLTQQKEISENNTY------------------EKLKMRDTLEKEKRKIQDLENRLTKQKE 844
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFylrqsvidlqtklqemqmERDAMADIRRRESQSQEDLRNQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 845 EIE-LKEQKENVLNnklkDALVMVEDAQQMKTTEsqraETLALKLKETLAELETTKTKMILTDDrlKLQQQSMKALQDER 923
Cdd:pfam15921 153 ELEaAKCLKEDMLE----DSNTQIEQLRKMMLSH----EGVLQEIRSILVDFEEASGKKIYEHD--SMSTMHFRSLGSAI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 924 ESQKHGFEEEISEYK----------EQIKQHSQTIVSLeerlcQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAGPPL 993
Cdd:pfam15921 223 SKILRELDTEISYLKgrifpvedqlEALKSESQNKIEL-----LLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSI 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 994 DSgdkeiacdhlidDLLMAQKEILSQQEIIMKLRTDLgeaHSRMSDLRGELSEKQKM------ELERQVALVRQQSGELS 1067
Cdd:pfam15921 298 QS------------QLEIIQEQARNQNSMYMRQLSDL---ESTVSQLRSELREAKRMyedkieELEKQLVLANSELTEAR 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1068 MLKAKVAQTTGLMEkkDRELKVLREALRASQEKPrphLSTEQKPRTLSQKCDISLQIEPAHPDSFSSFQEEQSFSDL--- 1144
Cdd:pfam15921 363 TERDQFSQESGNLD--DQLQKLLADLHKREKELS---LEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALlka 437
|
410 420 430
....*....|....*....|....*....|....
gi 1720409123 1145 -GVKCKGS--RHEETIQRQRKALSELRTRVRELE 1175
Cdd:pfam15921 438 mKSECQGQmeRQMAAIQGKNESLEKVSSLTAQLE 471
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
702-854 |
2.53e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 702 KSLRQEHLAEKEKLAEKLEQEEKLKA------KIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEAL 775
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAeaikkeALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 776 EnsvaqekrKMREMLEAERRKAQDLENQLTQQKEisennTYEKL--KMRDTLEK-------EKRKI--QDLENRLTKQK- 843
Cdd:PRK12704 106 E--------KREEELEKKEKELEQKQQELEKKEE-----ELEELieEQLQELERisgltaeEAKEIllEKVEEEARHEAa 172
|
170
....*....|....
gi 1720409123 844 ---EEIElKEQKEN 854
Cdd:PRK12704 173 vliKEIE-EEAKEE 185
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
223-490 |
2.61e-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: 42.41 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 223 LLGREVNRLSDFEMESKYKDALIMNLQAEVADlSQRLSETAAVAAARQSNRCDPKLQGV----DEGDDLR--QKEIESMK 296
Cdd:pfam15921 476 MLRKVVEELTAKKMTLESSERTVSDLTASLQE-KERAIEATNAEITKLRSRVDLKLQELqhlkNEGDHLRnvQTECEALK 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 297 SQinalqkgysqvlsqtLAERNTEIESLKNEGENLKR---DHAITSGmvtSLQKDMSARNEQVQQLQEEVNRLRIENREK 373
Cdd:pfam15921 555 LQ---------------MAEKDKVIEILRQQIENMTQlvgQHGRTAG---AMQVEKAQLEKEINDRRLELQEFKILKDKK 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 374 EYQLEALSSRCSVMK-----------EELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVrklrEELKKNYmgqniiskt 442
Cdd:pfam15921 617 DAKIRELEARVSDLElekvklvnagsERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDY----EVLKRNF--------- 683
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1720409123 443 lreKNKVEeklqedsrrkllqlqEMGNRENLIKINLERAVGQLENFRN 490
Cdd:pfam15921 684 ---RNKSE---------------EMETTTNKLKMQLKSAQSELEQTRN 713
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
354-1138 |
2.89e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 354 EQVQQLQEEVNRLRIENREKEYQLEALSSRCSVMKEEL-RKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELKKn 432
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTpCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREA- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 433 ymgqniisktLREKNKVEEKLQEDSRR-KLLQLQEMGNRENLIKINLERAVGQLENFRNQVIKATFGKTKPFRDKPITDQ 511
Cdd:TIGR00618 252 ----------QEEQLKKQQLLKQLRARiEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMR 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 512 QRQHLRACIPPHRARTcaptlQSLPRRAGCLETSYclssGQLIEKIIQVTEDNLSFQQRKWTLQRETHLHPKQEETMHSV 591
Cdd:TIGR00618 322 SRAKLLMKRAAHVKQQ-----SSIEEQRRLLQTLH----SQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLT 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 592 EKLRVLldkcqacmrdscSSIDLKKEVELLQHLPlsplvsglQKTVVNILRVSLSWLEETEQLlgdldielsdSDKGFSL 671
Cdd:TIGR00618 393 QKLQSL------------CKELDILQREQATIDT--------RTSAFRDLQGQLAHAKKQQEL----------QQRYAEL 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 672 CLIYllehykkIMSQSQDLQAQMNASRETQKSLRQ--EHLAEKEKLAEKLEQEEKLKAK-IQQLTEEKAALEESIGQEKS 748
Cdd:TIGR00618 443 CAAA-------ITCTAQCEKLEKIHLQESAQSLKEreQQLQTKEQIHLQETRKKAVVLArLLELQEEPCPLCGSCIHPNP 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 749 RSEEALEKA--QARVRELENHLASQKEALENSVAQ--EKRKMREMLEAERRKAQDLENQLTQQ----KEISENNTYEKLK 820
Cdd:TIGR00618 516 ARQDIDNPGplTRRMQRGEQTYAQLETSEEDVYHQltSERKQRASLKEQMQEIQQSFSILTQCdnrsKEDIPNLQNITVR 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 821 MRDTLEKEkrkiqdLENRLTKQKEEIELKEQKENVLNNKLKDAlvmvedAQQMKTTESQRAETLALKLKETLAELETTKT 900
Cdd:TIGR00618 596 LQDLTEKL------SEAEDMLACEQHALLRKLQPEQDLQDVRL------HLQQCSQELALKLTALHALQLTLTQERVREH 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 901 KMILTDDRLKLQQQSMKALQDE--RESQKHGFEEEISEYKE---QIKQHSQTIVSLEERLCQVTQYY-QKIEGEITTLKN 974
Cdd:TIGR00618 664 ALSIRVLPKELLASRQLALQKMqsEKEQLTYWKEMLAQCQTllrELETHIEEYDREFNEIENASSSLgSDLAAREDALNQ 743
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 975 NDTGPKEEASQDLTAgpplDSGDKEIACDHLIDDLLMAQKEILSQQEIIMKLRtDLGEAHSRMSDLRGELSEKQKMELER 1054
Cdd:TIGR00618 744 SLKELMHQARTVLKA----RTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNR-LREEDTHLLKTLEAEIGQEIPSDEDI 818
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1055 QVALVRQQSGELSMLKAKVAQTTGLMEKKDRELKVLREALRASQEKPRPHLSTEQKPRTLSQKCDISLQIEpahPDSFSS 1134
Cdd:TIGR00618 819 LNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFD---GDALIK 895
|
....
gi 1720409123 1135 FQEE 1138
Cdd:TIGR00618 896 FLHE 899
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
721-927 |
2.98e-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: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 721 QEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQA-RVRELENHLASQKEALENSVAQEKRKMREmLEAERRKAQD 799
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfRQKNGLVDLSEEAKLLLQQLSELESQLAE-ARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 800 LENQLTQQ--------KEISENNTYEKLkmRDTLEKEKRKIQDLENRLTKQKEEI-ELKEQKENVLNNKLKdalvmvEDA 870
Cdd:COG3206 241 RLAALRAQlgsgpdalPELLQSPVIQQL--RAQLAELEAELAELSARYTPNHPDViALRAQIAALRAQLQQ------EAQ 312
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720409123 871 QQMKTTESQRaETLALKLKETLAELETTKTKMiltdDRLKLQQQSMKALQDERESQK 927
Cdd:COG3206 313 RILASLEAEL-EALQAREASLQAQLAQLEARL----AELPELEAELRRLEREVEVAR 364
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
675-883 |
3.04e-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: 41.24 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 675 YLLEHYKKIMSQSQDLQAQMNASretqKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEAL 754
Cdd:pfam06008 27 QLQEYLSPENAHKIQIEILEKEL----SSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEIN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 755 EKA--------QARVRELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQL-TQQKEISENNTYEKLKMRDTL 825
Cdd:pfam06008 103 EKVatlgendfALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRIqTWFQSPQEENKALANALRDSL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720409123 826 EKEKRKIQDLENRLtkqkEEIELKEQKENVLNNKLKDALVMVEdaQQMKTTESQRAET 883
Cdd:pfam06008 183 AEYEAKLSDLRELL----REAAAKTRDANRLNLANQANLREFQ--RKKEEVSEQKNQL 234
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
677-882 |
3.08e-03 |
|
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: 42.03 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 677 LEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEK 756
Cdd:pfam17380 385 MERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVER 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 757 -------AQARVRELENHLASQKEA-------LENSVAQEKRKMREmleaERRKAQDLENQLtqqkEISENNTYEKLKMR 822
Cdd:pfam17380 465 lrqqeeeRKRKKLELEKEKRDRKRAeeqrrkiLEKELEERKQAMIE----EERKRKLLEKEM----EERQKAIYEEERRR 536
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 823 DTlEKEKRKIQDLENRLTKQKEEIELKEQKenvlnNKLKDALVMVEDAQQMKTTESQRAE 882
Cdd:pfam17380 537 EA-EEERRKQQEMEERRRIQEQMRKATEER-----SRLEAMEREREMMRQIVESEKARAE 590
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
767-974 |
3.31e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 767 HLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLtqQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEI 846
Cdd:PRK05771 32 HIEDLKEELSNERLRKLRSLLTKLSEALDKLRSYLPKL--NPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 847 -ELKEQKENVLNNK-----LKDALVMVEDAQQMKTT--------ESQRAETLALKLKETLAELETTKTKM--ILTDDRLK 910
Cdd:PRK05771 110 sELENEIKELEQEIerlepWGNFDLDLSLLLGFKYVsvfvgtvpEDKLEELKLESDVENVEYISTDKGYVyvVVVVLKEL 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720409123 911 LQQQsmkalqdERESQKHGFEE-EISEykeqIKQHSQTIVSLEERLCQVTQYYQKIEGEITTLKN 974
Cdd:PRK05771 190 SDEV-------EEELKKLGFERlELEE----EGTPSELIREIKEELEEIEKERESLLEELKELAK 243
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
649-957 |
3.38e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 649 EETEQLLGDLDIELSDSDKgfslCLIYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAK 728
Cdd:pfam01576 71 QELEEILHELESRLEEEEE----RSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 729 IQQLTEEKAALEESIGQEKSRSEEALEKAQArVRELENHLASQKEALENSVAQEKRKMREMLEAERR---KAQDLENQLT 805
Cdd:pfam01576 147 NSKLSKERKLLEERISEFTSNLAEEEEKAKS-LSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKlegESTDLQEQIA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 806 -QQKEISEnntyeklkMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTtesqRAETL 884
Cdd:pfam01576 226 eLQAQIAE--------LRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARN----KAEKQ 293
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720409123 885 ALKLKEtlaELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQ----HSQTIVSLEERLCQ 957
Cdd:pfam01576 294 RRDLGE---ELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEmrqkHTQALEELTEQLEQ 367
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
681-799 |
3.41e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.72 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 681 KKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKlAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQAR 760
Cdd:PRK09510 83 KKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQ-KKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAK 161
|
90 100 110
....*....|....*....|....*....|....*....
gi 1720409123 761 VRELENHLASQKEALENSVAQEKRKMREmlEAERRKAQD 799
Cdd:PRK09510 162 KAAAEAKKKAEAEAAKKAAAEAKKKAEA--EAAAKAAAE 198
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
630-919 |
3.47e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.99 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 630 VSGLQKTVvnILRVSLSWLEETEQLLGDLDIELSDSD--KGFSLCLIYLLEHYKKIMSQS--QDLQAQMNASRETQKSLR 705
Cdd:COG5022 861 FSLLKKET--IYLQSAQRVELAERQLQELKIDVKSISslKLVNLELESEIIELKKSLSSDliENLEFKTELIARLKKLLN 938
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 706 QEHLAE--------KEKLAEKLEQEEKLKakiqQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLaSQKEALEN 777
Cdd:COG5022 939 NIDLEEgpsieyvkLPELNKLHEVESKLK----ETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELS-KQYGALQE 1013
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 778 SVAQEKRKMREMLEAerrkaqdlenqltqqkeiseNNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEeiELKEQKENVLN 857
Cdd:COG5022 1014 STKQLKELPVEVAEL--------------------QSASKIISSESTELSILKPLQKLKGLLLLENN--QLQARYKALKL 1071
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720409123 858 NKlKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDD---RLKLQQQSMKAL 919
Cdd:COG5022 1072 RR-ENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVAqmiKLNLLQEISKFL 1135
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
679-974 |
3.59e-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: 41.76 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 679 HYKKIMSQSQDLQAQMNASRETQKSLRQEhlaekekLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQ 758
Cdd:pfam06160 80 RFKKAKKALDEIEELLDDIEEDIKQILEE-------LDELLESEEKNREEVEELKDKYRELRKTLLANRFSYGPAIDELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 759 ARVRELE-------------NHLASQK--EALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEisennTYEKLKMR- 822
Cdd:pfam06160 153 KQLAEIEeefsqfeeltesgDYLEAREvlEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKE-----GYREMEEEg 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 823 ---DTLEKEKRkIQDLENRLTKQKEEI---ELKEQKENVLN-----NKLKDALVMVEDAQQ-----MKTTESQRAETLAl 886
Cdd:pfam06160 228 yalEHLNVDKE-IQQLEEQLEENLALLenlELDEAEEALEEieeriDQLYDLLEKEVDAKKyveknLPEIEDYLEHAEE- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 887 KLKETLAELETTKTKMILTDDRLKLQQQsmkaLQDERESQKHGFEeeisEYKEQIKQHSQTIVSLEERLCQVTQYYQKIE 966
Cdd:pfam06160 306 QNKELKEELERVQQSYTLNENELERVRG----LEKQLEELEKRYD----EIVERLEEKEVAYSELQEELEEILEQLEEIE 377
|
....*...
gi 1720409123 967 GEITTLKN 974
Cdd:pfam06160 378 EEQEEFKE 385
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
342-1110 |
3.88e-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: 41.88 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 342 VTSLQKDMSARNEQVQQLQEEVNRLRIENRE--KEYQLEALSSRCSVMKEELRKEEAQKDRREAQEKELKLCRSQMQDME 419
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEElkLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 420 KEVRKLREELKKNYMGQNIISKTLREKNKV------EEKLQED-----------SRRKLLQLQEMGNRENLIKINLERAV 482
Cdd:pfam02463 244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKEnkeeekEKKLQEEelkllakeeeeLKSELLKLERRKVDDEEKLKESEKEK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 483 GQLENFRNQVI---------KATFGKTKPFRDKPITDQQRQHLRACIPPHRARTCAPTLQSLPRRAGCLETSYclSSGQL 553
Cdd:pfam02463 324 KKAEKELKKEKeeieelekeLKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEE--LELKS 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 554 IEKIIQVTEDNLSFQQRKWTLQRETHLHPKQEETMHSVEKLRVLLDKCQAcMRDSCSSIDLKKEVELLQHLPLSPLVSGL 633
Cdd:pfam02463 402 EEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKE-ELEKQELKLLKDELELKKSEDLLKETQLV 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 634 QKTVVNILRVSLSWLEETEQLL----GDLDIELSDSDKGFSLCLIYLLEHYKKIMSQSQDLQAQMNASRETQKSLRQEHL 709
Cdd:pfam02463 481 KLQEQLELLLSRQKLEERSQKEskarSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEV 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 710 AEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEA--LENSVAQEKRKMR 787
Cdd:pfam02463 561 EERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVegILKDTELTKLKES 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 788 EMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMV 867
Cdd:pfam02463 641 AKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAE 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 868 EDAQQMKTTESQRAETLALKLKETLAELETTKTKMILtddRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQT 947
Cdd:pfam02463 721 ELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRL---KKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLK 797
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 948 IVSLEERLCQVTQYYQKIEGEITTLKNNDTGPKEEASQDLTAGPPLDSG-DKEIACDHLIDDLLMAQKEILSQQEIIMKL 1026
Cdd:pfam02463 798 AQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQkLEKLAEEELERLEEEITKEELLQELLLKEE 877
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1027 RTDLGEAHSRMSDLRGELSEKQKMELERQVALVRQQSGELSmLKAKVAQTTGLMEKKDRELKVLREALRASQEKPRPHLS 1106
Cdd:pfam02463 878 ELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENE-IEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE 956
|
....
gi 1720409123 1107 TEQK 1110
Cdd:pfam02463 957 EEEE 960
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
349-940 |
3.99e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.73 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 349 MSARNEQVQQLQEEVnrlrienrekeyQLEALSSRCSVMKEELRKEEAQKDRReAQEKElklcrSQMQDMEKEVRKLREE 428
Cdd:pfam10174 153 LGARDESIKKLLEML------------QSKGLPKKSGEEDWERTRRIAEAEMQ-LGHLE-----VLLDQKEKENIHLREE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 429 LKKNYMGQNIISKTLREKNKVEEK------LQEDSRRKLLQLQEMGNRENLIKINLERAVGQLENFRNQvikATFGKTKp 502
Cdd:pfam10174 215 LHRRNQLQPDPAKTKALQTVIEMKdtkissLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSH---SKFMKNK- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 503 frdkpiTDQQRQHLracippHRARTCAPTLQSLprragcLETSYCLSSGQliEKIIQVTEDNLSF-QQRKWTLQRETHLH 581
Cdd:pfam10174 291 ------IDQLKQEL------SKKESELLALQTK------LETLTNQNSDC--KQHIEVLKESLTAkEQRAAILQTEVDAL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 582 PKQEETMHSV--EKLRVLLDKCQACMRDSCSSIDLKKEVELLQHlplspLVSGLQKTVVNI---LRVSLSWLEETEQLLG 656
Cdd:pfam10174 351 RLRLEEKESFlnKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKER-----KINVLQKKIENLqeqLRDKDKQLAGLKERVK 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 657 DLDIELSDSDKGFSLCLIYLLEHYKKImsqsqdlqaqmNASRETQKSLRQEHLAEKEKLAEKL-EQEEKLKAKIQQLTEE 735
Cdd:pfam10174 426 SLQTDSSNTDTALTTLEEALSEKERII-----------ERLKEQREREDRERLEELESLKKENkDLKEKVSALQPELTEK 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 736 KAALEESIGQEKSRSEEALEKaQARVRELENHLASQKEALENSVAQEKrKMREMLEAERRKA------QDLENQLTQQKE 809
Cdd:pfam10174 495 ESSLIDLKEHASSLASSGLKK-DSKLKSLEIAVEQKKEECSKLENQLK-KAHNAEEAVRTNPeindriRLLEQEVARYKE 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 810 ISENNTYEKLKMRDTL---EKEK----RKIQDLENRLTKQ-KEEIELKEQKENVLNNKLKDALVMVEDAqqMKTTESQRA 881
Cdd:pfam10174 573 ESGKAQAEVERLLGILrevENEKndkdKKIAELESLTLRQmKEQNKKVANIKHGQQEMKKKGAQLLEEA--RRREDNLAD 650
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720409123 882 ETLALKLKETLAELETTKTKMILTDDRLKLQQQSMK-------ALQDERESQKhgfeEEISEYKEQ 940
Cdd:pfam10174 651 NSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAekdghltNLRAERRKQL----EEILEMKQE 712
|
|
| FHA_EmbR-like |
cd22669 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis transcriptional ... |
18-92 |
4.00e-03 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis transcriptional regulatory protein EmbR and similar proteins; EmbR is a transcriptional regulator of the embCAB operon encoding cell wall arabinosyltransferases (EmbC, -A, and -B), and is phosphorylated by the cognate mycobacterial serine/threonine protein kinase PknH. It interacts with RNA polymerase and possesses a phosphorylation-dependent ATPase activity. EmbR contains a regulatory C-terminal forkhead-associated (FHA) domain, which mediates binding to a threonine-phosphorylated site in PknH. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438721 [Multi-domain] Cd Length: 89 Bit Score: 38.17 E-value: 4.00e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720409123 18 TTIGKHADSDLVLQSADIDNHHALIefNEAEGTFVLQDFNSRNGTFVNECHIQNVAVkLIPGDILRFGSAGMTYE 92
Cdd:cd22669 18 TRIGRLHDNDIVLDSANVSRHHAVI--VDTGTNYVINDLRSSNGVHVQHERIRSAVT-LNDGDHIRICDHEFTFQ 89
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
703-973 |
4.25e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 703 SLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIG---------QEKSRSEEALEKAQARVRELENHLASQKE 773
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQaasdhlnlvQTALRQQEKIERYQADLEELEERLEEQNE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 774 ALENsvAQEkrkMREMLEAERRKAQ----DLENQLT--------QQKEISENN----TYEKLK------------MRDTL 825
Cdd:PRK04863 370 VVEE--ADE---QQEENEARAEAAEeevdELKSQLAdyqqaldvQQTRAIQYQqavqALERAKqlcglpdltadnAEDWL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 826 EKEKRKIQDLENRL--TKQKEEI--ELKEQKENVLN--NKLKDAlVMVEDAQQ-----MKTTESQRAETLALK-LKETLA 893
Cdd:PRK04863 445 EEFQAKEQEATEELlsLEQKLSVaqAAHSQFEQAYQlvRKIAGE-VSRSEAWDvarelLRRLREQRHLAEQLQqLRMRLS 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 894 ELEttktkmiltdDRLKLQQQSMKALQDerESQKHG--------FEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKI 965
Cdd:PRK04863 524 ELE----------QRLRQQQRAERLLAE--FCKRLGknlddedeLEQLQEELEARLESLSESVSEARERRMALRQQLEQL 591
|
....*...
gi 1720409123 966 EGEITTLK 973
Cdd:PRK04863 592 QARIQRLA 599
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
673-940 |
4.38e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.48 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 673 LIYLLEHYKKIMSQSQDlQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSR--- 749
Cdd:COG5185 287 LIKQFENTKEKIAEYTK-SIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEien 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 750 --SEEALEKAQARVRELENHLASQKEALENSVAQEKRKMREMLEAERR--KAQDLE-NQLTQQKEISENNTYEKLKMRDT 824
Cdd:COG5185 366 ivGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDtlKAADRQiEELQRQIEQATSSNEEVSKLLNE 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 825 LEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKlkdalvmvEDAQQmkttESQRAETLALKLKETLAELETTKTKMI- 903
Cdd:COG5185 446 LISELNKVMREADEESQSRLEEAYDEINRSVRSKK--------EDLNE----ELTQIESRVSTLKATLEKLRAKLERQLe 513
|
250 260 270
....*....|....*....|....*....|....*...
gi 1720409123 904 LTDDRLKLQQQSMKALQDERE-SQKHGFEEEISEYKEQ 940
Cdd:COG5185 514 GVRSKLDQVAESLKDFMRARGyAHILALENLIPASELI 551
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
677-776 |
4.84e-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: 41.58 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 677 LEHYKKIMSQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQE--EKLKAKIQQLTEEKAALEESIG---QEKSRSE 751
Cdd:pfam13166 357 LDSVDAKIESINDLVASINELIAKHNEITDNFEEEKNKAKKKLRLHlvEEFKSEIDEYKDKYAGLEKAINsleKEIKNLE 436
|
90 100
....*....|....*....|....*
gi 1720409123 752 EALEKAQARVRELENHLASQKEALE 776
Cdd:pfam13166 437 AEIKKLREEIKELEAQLRDHKPGAD 461
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
289-399 |
4.84e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 289 QKEIESMKSQINALQKgYSQVLSQTLAERNTEIESLKNEGENLKRdhaitsgmvtSLQKDMSARNEqVQQLQEEVNRLRI 368
Cdd:COG2433 412 EEEIRRLEEQVERLEA-EVEELEAELEEKDERIERLERELSEARS----------EERREIRKDRE-ISRLDREIERLER 479
|
90 100 110
....*....|....*....|....*....|.
gi 1720409123 369 ENREKEYQLEALSSRCSVMKeELRKEEAQKD 399
Cdd:COG2433 480 ELEEERERIEELKRKLERLK-ELWKLEHSGE 509
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
685-924 |
4.89e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 685 SQSQDLQAQMNASRETQKSLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQ---EKSRSEEALEKAQARV 761
Cdd:COG4372 73 SELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQleaQIAELQSEIAEREEEL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 762 RELENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTK 841
Cdd:COG4372 153 KELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 842 QKEEIELKEQKENVLNNKLKDALVMVEDAQQMKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQD 921
Cdd:COG4372 233 LALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGA 312
|
...
gi 1720409123 922 ERE 924
Cdd:COG4372 313 LED 315
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
679-1183 |
5.63e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.25 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 679 HYKKIMSQSqDLQAQMNASRETQKSLRQEHLAEKEKL---AEKLEQEEKLKAKIQQLTEEKAALEE-SIGQEKS--RSEE 752
Cdd:pfam05483 60 HYQEGLKDS-DFENSEGLSRLYSKLYKEAEKIKKWKVsieAELKQKENKLQENRKIIEAQRKAIQElQFENEKVslKLEE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 753 ALEKAQARVRE--LENHLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLTQQ----KEISENNTYEKLKMRDTLE 826
Cdd:pfam05483 139 EIQENKDLIKEnnATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMilafEELRVQAENARLEMHFKLK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 827 KEKRKIQDLENrltKQKEEIELKEQKENVL-------NNKLKDALVMVEDAQQMKTTESQRAETLALKLKETL------- 892
Cdd:pfam05483 219 EDHEKIQHLEE---EYKKEINDKEKQVSLLliqitekENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIekkdhlt 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 893 AELETTKTKMILT-------DDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLEERLCQVTQYYQKI 965
Cdd:pfam05483 296 KELEDIKMSLQRSmstqkalEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKN 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 966 EG-----------------EITTLKNNDTGPKEEASQDLTAGPPLDSGDKEI--------ACDHLIDDLLMAQKEILSQQ 1020
Cdd:pfam05483 376 EDqlkiitmelqkksseleEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFekiaeelkGKEQELIFLLQAREKEIHDL 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1021 EIIMKLRTDLGEAHSR-MSDLRGELSEKQ-----------KMELERQvALVRQQSGELSMLKAKVAQTTGLMEKKDRELK 1088
Cdd:pfam05483 456 EIQLTAIKTSEEHYLKeVEDLKTELEKEKlknieltahcdKLLLENK-ELTQEASDMTLELKKHQEDIINCKKQEERMLK 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 1089 VLrEALRASQEKPRPHLST---EQKPRTLSQKCDISLQIEPAHPDSFSSFQEEQSFSDLGVKCKGSRHEetIQRQRKALS 1165
Cdd:pfam05483 535 QI-ENLEEKEMNLRDELESvreEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQ--IENKNKNIE 611
|
570
....*....|....*...
gi 1720409123 1166 ELRTRVRELEKANSCNHK 1183
Cdd:pfam05483 612 ELHQENKALKKKGSAENK 629
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
670-803 |
6.32e-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: 39.42 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 670 SLCLIYLL---EHYKKIMSQSQDLQAQMNASRETQKslrQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQE 746
Cdd:pfam06785 47 SLCLLLLLyywEDALKEKFEKSFLEEKEAKLTELDA---EGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQL 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720409123 747 KSRSEEALEKAQARVRELENHLAsQKEALENSVAQEKRKMREMLEAERRKAQDLENQ 803
Cdd:pfam06785 124 QIQLQQISQDFAEFRLESEEQLA-EKQLLINEYQQTIEEQRSVLEKRQDQIENLESK 179
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
703-804 |
6.39e-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: 6.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 703 SLRQEHLAEKEKLAEKLEQEEKLKAKIQQLTEEKAALEESIG---------QEKSRSEEALEKAQARVRELENHLASQKE 773
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQaasdhlnlvQTALRQQEKIERYQEDLEELTERLEEQEE 368
|
90 100 110
....*....|....*....|....*....|....*
gi 1720409123 774 ALENsvAQEKrkmREMLEAERRKAQD----LENQL 804
Cdd:COG3096 369 VVEE--AAEQ---LAEAEARLEAAEEevdsLKSQL 398
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
713-971 |
6.40e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 713 EKLAEKLEQEEKLKAKIQQLTEEKAALEESIGQEKSRSEEALEKAQARVRELENHLASQKEALEnsvaqEKRKMREMLEA 792
Cdd:COG4372 38 FELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE-----ELESLQEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 793 ERRKAQDLENQLTQQKEISENNTYEKLKMRDTLEKEKRKIQDLENRLTKQKEEIELKEQKENVLNNKLKDALVMVEDAQQ 872
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 873 MKTTESQRAETLALKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDERESQKHGFEEEISEYKEQIKQHSQTIVSLE 952
Cdd:COG4372 193 NRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKD 272
|
250
....*....|....*....
gi 1720409123 953 ERLCQVTQYYQKIEGEITT 971
Cdd:COG4372 273 TEEEELEIAALELEALEEA 291
|
|
| FHA_DgcB-like |
cd22682 |
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ... |
11-86 |
7.18e-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: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 11 FFVLNKSTTIGKHADSDLVLQSADIDNHHALIEFNEAEGTfvLQDFNSRNGTFVN--------ECHIQNvavklipGDIL 82
Cdd:cd22682 15 FPITESTIVIGRSVESQVQIDDDSVSRYHAKLAVNPSAVS--IIDLGSTNGTIVNgkkipklaSCDLQN-------GDQI 85
|
....
gi 1720409123 83 RFGS 86
Cdd:cd22682 86 KIGN 89
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
676-977 |
7.34e-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: 41.19 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 676 LLEHYKKIMSQSQDLQAQMNASRE-TQKSLRQEHLAEKEKLAEKL-----------EQEEKLKAKIQQLTEEKAALE--- 740
Cdd:TIGR01612 1134 LEEIKKKSENYIDEIKAQINDLEDvADKAISNDDPEEIEKKIENIvtkidkkkniyDEIKKLLNEIAEIEKDKTSLEevk 1213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 741 ---------------ESIGQEKSRSEEALEKAQARVRELENhLASQKEALENSVAQEKRKMREMLEAERRKAQDLENQLT 805
Cdd:TIGR01612 1214 ginlsygknlgklflEKIDEEKKKSEHMIKAMEAYIEDLDE-IKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHII 1292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 806 QQK-------------EISENNtYEKLKMRD---TLEKEKRKIQDLENRLTKQKEEIE-----LKEQKENVLNNKLKDAL 864
Cdd:TIGR01612 1293 SKKhdenisdirekslKIIEDF-SEESDINDikkELQKNLLDAQKHNSDINLYLNEIAniyniLKLNKIKKIIDEVKEYT 1371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 865 VMVEDAQQMKTTESQRAETLALKLKETLAeLETTKTKMILTDDRLKLQQqsmkALQDERESQKHGFEEE--ISEYKEQIK 942
Cdd:TIGR01612 1372 KEIEENNKNIKDELDKSEKLIKKIKDDIN-LEECKSKIESTLDDKDIDE----CIKKIKELKNHILSEEsnIDTYFKNAD 1446
|
330 340 350
....*....|....*....|....*....|....*...
gi 1720409123 943 QHSQTIVSL---EERLCQVTQYYQKIEgeittlKNNDT 977
Cdd:TIGR01612 1447 ENNENVLLLfknIEMADNKSQHILKIK------KDNAT 1478
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
709-922 |
7.55e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.05 E-value: 7.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 709 LAEKEKLAEKLEQEEKLKAKIQQLTEEkaaLEESIGQEKSRSEEALEKaqarVRELENHLASQKEALENSvaqeKRKMRE 788
Cdd:cd22656 99 LIDDLADATDDEELEEAKKTIKALLDD---LLKEAKKYQDKAAKVVDK----LTDFENQTEKDQTALETL----EKALKD 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 789 MLEAE-----RRKAQDLENQLTQQKEIsenntyEKLKMRDTLEKEKRKIQDLENRLTKQKEEIE-LKEQKENV--LNNKL 860
Cdd:cd22656 168 LLTDEggaiaRKEIKDLQKELEKLNEE------YAAKLKAKIDELKALIADDEAKLAAALRLIAdLTAADTDLdnLLALI 241
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720409123 861 KDALVMVedaQQMKTTESQRAETLAlKLKETLAELETTKTKMILTDDRLKLQQQSMKALQDE 922
Cdd:cd22656 242 GPAIPAL---EKLQGAWQAIATDLD-SLKDLLEDDISKIPAAILAKLELEKAIEKWNELAEK 299
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
676-852 |
7.83e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.44 E-value: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 676 LLEHYKKIMSQSQDLQAQMNASRETQKSLRQEH------LAEKEKLA------EKLEQEEKLKAKIQQLTEEKAALEESI 743
Cdd:COG0497 156 LLEEYREAYRAWRALKKELEELRADEAERARELdllrfqLEELEAAAlqpgeeEELEEERRRLSNAEKLREALQEALEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 744 GQEKSRSEEALEKAQARVRELENH---LASQKEALENS------VAQEKRKMREMLEAERRKAQDLENQLTQQKEISE-- 812
Cdd:COG0497 236 SGGEGGALDLLGQALRALERLAEYdpsLAELAERLESAlieleeAASELRRYLDSLEFDPERLEEVEERLALLRRLARky 315
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720409123 813 NNTYEKL-KMRDTLEKEKRKIQDLENRLTKQKEEIELKEQK 852
Cdd:COG0497 316 GVTVEELlAYAEELRAELAELENSDERLEELEAELAEAEAE 356
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
215-465 |
7.98e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.66 E-value: 7.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 215 QDKDEIILLLGR-EVNRLSDFEMESKYKDALimnlQAEVADLSQRLSETAA---VAAARQSNrcdpklqgVDEGDDLRQK 290
Cdd:PLN02939 138 QNAEKNILLLNQaRLQALEDLEKILTEKEAL----QGKINILEMRLSETDArikLAAQEKIH--------VEILEEQLEK 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 291 EIESMKSQInALQKGYSQVLSQTLAERNTEIESLKNEGENLKR---DHAITSGMVTSLQKDMSARNEQVQQLQEEVnrlr 367
Cdd:PLN02939 206 LRNELLIRG-ATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAeliEVAETEERVFKLEKERSLLDASLRELESKF---- 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 368 IENREKEYQLEALSSRCsvMKEELRKEEAQKDRREAQEKELKLCRSQMQDMEKEVRKLREELK--KNYMGQNIISKTLRE 445
Cdd:PLN02939 281 IVAQEDVSKLSPLQYDC--WWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKeaNVSKFSSYKVELLQQ 358
|
250 260
....*....|....*....|.
gi 1720409123 446 KNK-VEEKLQEDSRRKLLQLQ 465
Cdd:PLN02939 359 KLKlLEERLQASDHEIHSYIQ 379
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
686-896 |
9.24e-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: 40.54 E-value: 9.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 686 QSQDLQAQMnasRETQKSLRQEHLAEKEKLAEKLEQEEKLK---AKIQQLTEEKAALEESIGQ-EKSRSEEALEKA---- 757
Cdd:pfam01576 799 QLKKLQAQM---KDLQRELEEARASRDEILAQSKESEKKLKnleAELLQLQEDLAASERARRQaQQERDELADEIAsgas 875
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 758 -----QARVRELENHLASQKEALENS-------------VAQEKRKMREMLEAERRKAQDLENQlTQQKEISENNTYEKL 819
Cdd:pfam01576 876 gksalQDEKRRLEARIAQLEEELEEEqsntellndrlrkSTLQVEQLTTELAAERSTSQKSESA-RQQLERQNKELKAKL 954
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409123 820 KMRDTLEKEKRK--IQDLENRLTKQKEEIElKEQKENVLNN--------KLKDALVMVEDAQQMKTTESQRAETLALKLK 889
Cdd:pfam01576 955 QEMEGTVKSKFKssIAALEAKIAQLEEQLE-QESRERQAANklvrrtekKLKEVLLQVEDERRHADQYKDQAEKGNSRMK 1033
|
....*..
gi 1720409123 890 ETLAELE 896
Cdd:pfam01576 1034 QLKRQLE 1040
|
|
| |
