|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
19-114 |
4.89e-51 |
|
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 (FHAD1) and similar proteins; FHAD1, also called FHA domain-containing protein 1, is an uncharacterized FHA domain-containing protein. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438752 [Multi-domain] Cd Length: 96 Bit Score: 174.75 E-value: 4.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 19 KAYLKSAEGFFVLN-KSTTIGRHeNSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQNVAVKLIPGD 97
Cdd:cd22700 1 KGYLKSSDGIFQLDpKVTTIGRE-GCDLVLQSPGVEEQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAPGD 79
|
90
....*....|....*..
gi 1370451826 98 ILRFGSAGLTYELVIEN 114
Cdd:cd22700 80 VLRFGFGGLPYELVVDN 96
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
35-101 |
1.49e-18 |
|
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 81.08 E-value: 1.49e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370451826 35 TTIGRHENSDLVLQSPDIDNHHALIEYNEaECSFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRF 101
Cdd:pfam00498 1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDG-GGRFYLEDLGSTNGTFVNGQRLGPEPVRLKDGDVIRL 66
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
28-109 |
1.19e-17 |
|
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.
Pssm-ID: 438714 [Multi-domain] Cd Length: 92 Bit Score: 79.24 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 28 FFVLNKSTTIGRHENSDLVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGLT 107
Cdd:cd00060 14 FPLTKGVVTIGRSPDCDIVLDDPSVSRRHARIEVDGGG--VYLEDLGSTNGTFVNGKRITP-PVPLQDGDVIRLGDTTFR 90
|
..
gi 1370451826 108 YE 109
Cdd:cd00060 91 FE 92
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
29-110 |
4.52e-17 |
|
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 77.69 E-value: 4.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 29 FVLNKS-TTIGRHENSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGLT 107
Cdd:COG1716 16 FPLDGGpLTIGRAPDNDIVLDDPTVSRRHARIRRDGG--GWVLEDLGSTNGTFVNGQRVTE-PAPLRDGDVIRLGKTELR 92
|
...
gi 1370451826 108 YEL 110
Cdd:COG1716 93 FRL 95
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
292-1058 |
5.38e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 80.88 E-value: 5.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 292 RQNEKEISQkcqvLDEDIDAKQKEIQSLKSQISALQKGYSKVLcQTLSERNSEITSL-KNEGENLKRDNAITSGMVSSLQ 370
Cdd:TIGR02169 233 EALERQKEA----IERQLASLEEELEKLTEEISELEKRLEEIE-QLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 371 KDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRcsvLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLR 450
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE---IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 451 AELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATygrakpfrdk 530
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE---------- 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 531 pvtdqqliEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKE-----VDL 605
Cdd:TIGR02169 455 --------WKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvHGT 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 606 LQHL-QVSPPVSG---------LQKVVLD---VLRHALSWLEEVE---------QLLRDLGILPSSPNKDQVQQFSGN-- 661
Cdd:TIGR02169 527 VAQLgSVGERYATaievaagnrLNNVVVEddaVAKEAIELLKRRKagratflplNKMRDERRDLSILSEDGVIGFAVDlv 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 662 -------SAV------------FTAGKAAGASGR----EGE--------------AERGEARARGEAQSQNQATDGREGG 704
Cdd:TIGR02169 607 efdpkyePAFkyvfgdtlvvedIEAARRLMGKYRmvtlEGElfeksgamtggsraPRGGILFSRSEPAELQRLRERLEGL 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 705 KALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALaKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIA 784
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI-EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 785 hEKRKAKEALESEKRKVQDLENHLTQQKeISESNIAYEKrkakeamekEKKKVQDLENRLTKQKEELELKEQKEDVLNNK 864
Cdd:TIGR02169 766 -RIEELEEDLHKLEEALNDLEARLSHSR-IPEIQAELSK---------LEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 865 LSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLIlqqkmvkalqdeqesqrhGFEEEIMEYKE 944
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG------------------DLKKERDELEA 896
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 945 QIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDndpapkEERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQ 1024
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSELKAKLEALEE------ELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
|
810 820 830
....*....|....*....|....*....|....
gi 1370451826 1025 QEVIMKLRKDLTEAHSRMSDLRGelnEKQKMELE 1058
Cdd:TIGR02169 971 EPVNMLAIQEYEEVLKRLDELKE---KRAKLEEE 1001
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
261-980 |
1.09e-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: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 261 EIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQKGYsKVLCQTLSE 340
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL-YALANEISR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 341 RNSEITSLKNEGENLKRDNAITSGMVSSL--QKDILAKD-----EQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKE 413
Cdd:TIGR02168 300 LEQQKQILRERLANLERQLEELEAQLEELesKLDELAEElaeleEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 414 ELKQE----DAHRELREAQEKELKLCKTQIQDMEKEMKKLRAEL-----RKSCTEQSVISRTLREKSKVEEKLQEDSRRK 484
Cdd:TIGR02168 380 QLETLrskvAQLELQIASLNNEIERLEARLERLEDRRERLQQEIeellkKLEEAELKELQAELEELEEELEELQEELERL 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 485 LLQLQEMGNRESVIKINLERAVGQLEHFRSQ--VIKATYGRAKPFRD--KPVTDQQL-IEKITQVTEDNINFQqKKWTLQ 559
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQARldSLERLQENLEGFSEgvKALLKNQSgLSGILGVLSELISVD-EGYEAA 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 560 KETQLSNSKQEETTENIEKLRTSLDSCQ--ACMKISCCSHDLKKEVDLL-QHLQVSPPVSGLQKVVLDVLRHALSWLEEV 636
Cdd:TIGR02168 539 IEAALGGRLQAVVVENLNAAKKAIAFLKqnELGRVTFLPLDSIKGTEIQgNDREILKNIEGFLGVAKDLVKFDPKLRKAL 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 637 EQLLRDLGILPS--SPNKDQVQQFSGNSAVFTAGKAAGASGregeaergeARARGEAQSQNQatdgreggkaleeyiTQE 714
Cdd:TIGR02168 619 SYLLGGVLVVDDldNALELAKKLRPGYRIVTLDGDLVRPGG---------VITGGSAKTNSS---------------ILE 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 715 RNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEA---LEEEQTRVQELEERLAR---QKEVLESSIAHEKR 788
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLrkeLEELSRQISALRKDLARleaEVEQLEERIAQLSK 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 789 KAKEaLESEKRKVQDLENHLTQQKEISESNIAYEKRK---AKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKL 865
Cdd:TIGR02168 755 ELTE-LEAEIEELEERLEEAEEELAEAEAEIEELEAQieqLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 866 SDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESqrhgFEEEIMEYKEQ 945
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE----LSEELRELESK 909
|
730 740 750
....*....|....*....|....*....|....*
gi 1370451826 946 IKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDN 980
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
37-110 |
3.58e-13 |
|
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) family; The Cep170 family includes Cep170 and Cep170B. Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438756 [Multi-domain] Cd Length: 102 Bit Score: 66.96 E-value: 3.58e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370451826 37 IGRhENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHI-QNVAVKLIPGDILRFGSAGLTYEL 110
Cdd:cd22704 21 VGR-EDCDLILQSRSVDKQHAVITYDQIDNEFKIKDLGSLNGTFVNDSRIpEQTYITLKLGDSIRFGYDTNVYRF 94
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
676-1183 |
5.99e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 5.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 676 REGEAERGEARARGEAQSQNQATDGREGGKALEEYitQERNRAKETLEEERKRMQELESLLAQQKKALAksitQEKNRVK 755
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAEE--YELLAELARLEQDIARLEERRRELEERLEELE----EELAELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 756 EALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEisESNIAYEKRKAKEAMEKEKK 835
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE--LLEALRAAAELAAQLEELEE 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 836 KVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMImVEERLI 915
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA-ELLEEL 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 916 LQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQH------------------AQTIVSLEEKLQKVTQHHKKIEGEIATL 977
Cdd:COG1196 487 AEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglagavavligveaayeaALEAALAAALQNIVVEDDEVAAAAIEYL 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 978 KDNDPAPKEERP----QDPLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQ 1053
Cdd:COG1196 567 KAAKAGRATFLPldkiRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRL 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1054 KMELEQNVVLVQQQS-------KELSVLKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLntEKEQKPRKKTQTCD 1126
Cdd:COG1196 647 REVTLEGEGGSAGGSltggsrrELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA--EAEEERLEEELEEE 724
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370451826 1127 TSVQIEPVHTEAFSSSQEQQSFSDLGVRCKGSRHEEVIQRQKKALSELRARIKELEK 1183
Cdd:COG1196 725 ALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGP 781
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
29-109 |
3.44e-12 |
|
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; MDC1, also called nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438717 [Multi-domain] Cd Length: 97 Bit Score: 63.79 E-value: 3.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 29 FVLNK-STTIGRHENSDLVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHI--QNVAVKLIPGDILRFGSAG 105
Cdd:cd22665 16 FPLYEgENVIGRDPSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNKVRlkPNVRYELIDGDLLLFGDVK 93
|
....
gi 1370451826 106 LTYE 109
Cdd:cd22665 94 CQYV 97
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
303-847 |
6.17e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 6.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 303 QVLDEDIDAKQKEIQSLKSQISALQKgyskvlcqTLSERNSEITSLKNEGENLKRDnaitsgmVSSLQKDILAKDEQVQQ 382
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEA--------ELAELEAELEELRLELEELELE-------LEEAQAEEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 383 LKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKlckTQIQDMEKEMKKLRAELRKSCTEQSV 462
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE---EELEEAEAELAEAEEALLEAEAELAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 463 ISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATygrakpfrdkpVTDQQLIEKIT 542
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE-----------EEEEEEEEALE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 543 QVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQAcmkisccSHDLKKEVDLLQHLQVSPP----VSGL 618
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA-------RLLLLLEAEADYEGFLEGVkaalLLAG 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 619 QKVVLDVLRHALSWLEEVEQLL----------------------------RDLGILPSSPNKDQVQQFSGNSAVFTAGKA 670
Cdd:COG1196 519 LRGLAGAVAVLIGVEAAYEAALeaalaaalqnivveddevaaaaieylkaAKAGRATFLPLDKIRARAALAAALARGAIG 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 671 AGASGREGEAERGEARARGEAQSQNQATDGREGGKALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQE 750
Cdd:COG1196 599 AAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 751 KNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEAM 830
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
|
570
....*....|....*..
gi 1370451826 831 EKEKKKVQDLENRLTKQ 847
Cdd:COG1196 759 PPDLEELERELERLERE 775
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
29-103 |
6.86e-12 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaB and similar proteins; FhaB, also called FtsZ-interacting protein A (FipA), is a putative virulence factor involved in regulating cell shape. It can interact with polyketide-associated protein PapA5, a putative membrane protein involved in the biosynthesis of virulence enhancing lipids. FhaB regulates growth and cell division. It is probably required for divisomal protein assembly under oxidative stress. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438745 [Multi-domain] Cd Length: 91 Bit Score: 62.71 E-value: 6.86e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370451826 29 FVLNKST-TIGRHENSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIqNVAVKLIPGDILRFGS 103
Cdd:cd22693 13 FPIDKSGiTIGRADDNDLVLSDDFVSSRHARIYLQGS--SWYLEDLGSTNGTFVNGNRV-TQPVVVQPGDTIRIGA 85
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
254-806 |
1.30e-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: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 254 VSRLSDYEIESKYKDVIIANLQNEVAELSQKVSETTTSRQnekEISQKCQVLDEDIDAKQKEIQSLKSQISALQKGySKV 333
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYELLAELARLEQD-IAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 334 LCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKE 413
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 414 ELKQEDAHRELREAQEKELKL----CKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQ 489
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEaeeaLLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 490 EMGNRESVIKINLERAVGQLEHFRSQ--VIKATYGRAKPFRD--KPVTDQQLIEKITQVTEDNInfqqkKWTLQKETQLS 565
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARllLLLEAEADYEGFLEgvKAALLLAGLRGLAGAVAVLI-----GVEAAYEAALE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 566 NSKQEETTENIEKLRTSLDSCQACMKisccshDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRHALSWLEEVEQLLRDLgi 645
Cdd:COG1196 542 AALAAALQNIVVEDDEVAAAAIEYLK------AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADA-- 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 646 lpssPNKDQVQQFSGNSAVFTAGKAAGASGREGEAERGEARARGEAQSQNQATDGREGGKALEEYITQERNRAKETLEEE 725
Cdd:COG1196 614 ----RYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 726 RKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSI----AHEKRKAKEALESEKRKV 801
Cdd:COG1196 690 EEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELleeeALEELPEPPDLEELEREL 769
|
....*
gi 1370451826 802 QDLEN 806
Cdd:COG1196 770 ERLER 774
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
277-822 |
2.84e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 277 EVAELSQKVSETTTSRQNE------KEISQKCQVLDEDIDAKQKEIQSLKSQISALQKGYSKVLcQTLSERNSEITSLKN 350
Cdd:COG1196 210 EKAERYRELKEELKELEAEllllklRELEAELEELEAELEELEAELEELEAELAELEAELEELR-LELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 351 EGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEK 430
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 431 ELklcKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLE 510
Cdd:COG1196 369 EA---EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 511 HFRSQVIKATygrakpfrdkpvTDQQLIEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDScqacm 590
Cdd:COG1196 446 EAAEEEAELE------------EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE----- 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 591 kisccshDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRHALSWLEEVEQLL-----------------RDLGILPSSPNKD 653
Cdd:COG1196 509 -------GVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIvveddevaaaaieylkaAKAGRATFLPLDK 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 654 QVQQFSGNSAVFTAGKAAGASGREGEAERGEARARGEAQSQNQATDGREGGKALEEYITQERNRAKETLEEERKRMQELE 733
Cdd:COG1196 582 IRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 734 SLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKE 813
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
....*....
gi 1370451826 814 ISESNIAYE 822
Cdd:COG1196 742 LEEEELLEE 750
|
|
| FHA_DUN1-like |
cd22683 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ... |
34-102 |
1.25e-10 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein kinase DUN1 and similar proteins; DUN1 is a protein kinase that controls the DNA damage response in yeast. It phosphorylates SML1 on serine residues and cooperates with the PAN deadenylation complex in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438735 [Multi-domain] Cd Length: 96 Bit Score: 59.43 E-value: 1.25e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370451826 34 STTIGRHENSDLVLQSPDIDNHHALIEYnEAECSFVLqDFNSRNGTFVNECHIQNVAVKLIPGDILRFG 102
Cdd:cd22683 22 VTTIGRSRSCDLVLSDPSISRFHAELRL-EQNGINVI-DNNSANGTFINGKRIKGKTYILKNGDIIVFG 88
|
|
| FHA_PS1-like |
cd22691 |
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) ... |
36-110 |
1.33e-09 |
|
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) and similar proteins; PS1 is an FHA domain-containing protein required for normal spindle orientation at male meiosis II and normal formation of tetrad of microspores. It is not involved in female meiosis. Mutations in PS1 lead to the production of diploid pollen grains. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438743 [Multi-domain] Cd Length: 113 Bit Score: 57.04 E-value: 1.33e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370451826 36 TIGRHENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFGSAGLTYEL 110
Cdd:cd22691 32 VVGRHPDCDIVLDHPSISRFHLEIRIIPSRRKITLTDLSSVHGTWVNGQRIEpGVPVELEEGDTVRLGASTRVYRL 107
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
36-102 |
2.25e-09 |
|
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also called human lung cancer oncogene 3 protein (HLC-3), kidney anion exchanger adapter protein, or solute carrier family 4 anion exchanger member 1 adapter protein (SLC4A1AP), is a nuclear protein widely expressed in mammalian tissues. It was originally isolated as a kidney Cl-/HCO3- anion exchanger 1 (kAE1)-binding protein. It is a highly mobile nucleocytoplasmic shuttling and multilocalizing protein. Its role in mammalian cells remains unclear. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438729 [Multi-domain] Cd Length: 106 Bit Score: 56.03 E-value: 2.25e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370451826 36 TIGRHENSDLVLQSPDIDNHHALIEYN----EAECSFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFG 102
Cdd:cd22677 25 VFGRLPGCDVVLEHPSISRYHAVLQYRgdadDHDGGFYLYDLGSTHGTFLNKQRIPpKQYYRLRVGHVLKFG 96
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
35-82 |
3.70e-09 |
|
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.
Pssm-ID: 214578 [Multi-domain] Cd Length: 52 Bit Score: 53.72 E-value: 3.70e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1370451826 35 TTIGRHENS-DLVLQSPDIDNHHALIEYNEAECsFVLQDFNSRNGTFVN 82
Cdd:smart00240 1 VTIGRSSEDcDIQLDGPSISRRHAVIVYDGGGR-FYLIDLGSTNGTFVN 48
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
711-1116 |
4.67e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 4.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 711 ITQERNRAKETLEEER---KRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAhEK 787
Cdd:COG1196 194 ILGELERQLEPLERQAekaERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE-EL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 788 RKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAkeamekekkkvQDLENRLTKQKEELelkeqkedvlnnklsd 867
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERR-----------RELEERLEELEEEL---------------- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 868 alamvEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIK 947
Cdd:COG1196 326 -----AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 948 QHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERpqdplvapmtessakdMAYEHLIDDLLAAQKEILSQQEV 1027
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE----------------EALEEAAEEEAELEEEEEALLEL 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1028 IMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDREL----KALEEALRASQ 1103
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLigveAAYEAALEAAL 544
|
410
....*....|...
gi 1370451826 1104 EKHRLQLNTEKEQ 1116
Cdd:COG1196 545 AAALQNIVVEDDE 557
|
|
| FHA_Ki67 |
cd22673 |
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ... |
28-109 |
9.00e-09 |
|
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar proteins; Ki-67, also called antigen identified by monoclonal antibody Ki-67, antigen KI-67, or antigen Ki67, acts as a biological surfactant to disperse mitotic chromosomes. It is required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. Ki-67 binds DNA with a preference for supercoiled DNA and AT-rich DNA. It may also play a role in chromatin organization. Ki-67 contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438725 [Multi-domain] Cd Length: 95 Bit Score: 54.14 E-value: 9.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 28 FFVLNKSTTIGRHENSDLVLQSPDIDNHHALIEYNEAECsFVLQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGLT 107
Cdd:cd22673 16 FPLTKKSCTFGRDLSCDIRIQLPGVSREHCRIEVDENGK-AYLENLSTTNPTLVNGKAIEK-SAELKDGDVITIGGRSFR 93
|
..
gi 1370451826 108 YE 109
Cdd:cd22673 94 FE 95
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
36-174 |
1.20e-08 |
|
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal transduction mechanisms, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442679 [Multi-domain] Cd Length: 402 Bit Score: 59.00 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 36 TIGRHENSDLVLQSPD--IDNHHALIEYneAECSFVLQDfNSRNGTFVNECHI---QNVAVKLIPGDILRFGSagltYEL 110
Cdd:COG3456 29 TIGRSADCDWVLPDPDrsVSRRHAEIRF--RDGAFCLTD-LSTNGTFLNGSDHplgPGRPVRLRDGDRLRIGD----YEI 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370451826 111 V--IENPPPVSFPWMRGPAPWPGPQPPRATQQPNqAPPPshiPFHQGVQPAPMQRSWSQAFPRPTV 174
Cdd:COG3456 102 RveISGEDEGADDPLAAAPEPAVSSPSNLSDTEA-APDA---ALAFSFSLDPLEALDEAATEAPAT 163
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
711-1202 |
1.24e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 711 ITQERNRAKETLEEERKRMQELESLLAQQKKALA------KSITQEKNRVKEALEEEQTRVQELEER------LARQKEV 778
Cdd:PRK03918 170 VIKEIKRRIERLEKFIKRTENIEELIKEKEKELEevlreiNEISSELPELREELEKLEKEVKELEELkeeieeLEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 779 LESSIAHEKRKAKE---ALESEKRKVQDLENHLTQQKEISESNIAYEKrkAKEAMEKEKKKVQDLENRLTkqkeelelke 855
Cdd:PRK03918 250 LEGSKRKLEEKIREleeRIEELKKEIEELEEKVKELKELKEKAEEYIK--LSEFYEEYLDELREIEKRLS---------- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 856 qkedvlnnKLSDALAMVEETQKtkateslKAESLALKLNETLAELETTKTKMIMVEERLILQQkMVKALQDEQESQRHGF 935
Cdd:PRK03918 318 --------RLEEEINGIEERIK-------ELEEKEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 936 E-EEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERPQDPLV-APMTESSAKDMAYEHLIdD 1013
Cdd:PRK03918 382 TgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCgRELTEEHRKELLEEYTA-E 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1014 LLAAQKEILSQQEVIMKLRKDLTEAH---------SRMSDLRGELNEKQKMELEQNVVLVQQQSKELSVLKEKMAQMS-- 1082
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEkvlkkeselIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKge 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1083 -SLVEKKDRELKALEEALRA------SQEKHRLQLNTEKEQKPRKKTQTCDTSVQ-IEPVHTEAFSSSQEQQSFSDLGVR 1154
Cdd:PRK03918 541 iKSLKKELEKLEELKKKLAElekkldELEEELAELLKELEELGFESVEELEERLKeLEPFYNEYLELKDAEKELEREEKE 620
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1370451826 1155 CKGSRHE-----EVIQRQKKALSELRARIKELEKARSPDHKDHQNESFLDLKN 1202
Cdd:PRK03918 621 LKKLEEEldkafEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSR 673
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
708-1387 |
1.38e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.69 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 708 EEYITQERNRAKETLEEERKRMQELESLLAQQKKALaKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEK 787
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKEL-YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 788 RKAKEALESEKRKVQDLENHLTQQKEISESNIAYEkrkakeameKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSD 867
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELESLEAELEELEAELE---------ELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 868 ALAMVEETQKTKATESLKAESLALKLNET-LAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQI 946
Cdd:TIGR02168 405 LEARLERLEDRRERLQQEIEELLKKLEEAeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 947 KQHAQTIVSLEEKLQK----------VTQHHKKIEGEIATLKDNDPAPKE----------ERPQDPLVApmTESSAKDmA 1006
Cdd:TIGR02168 485 AQLQARLDSLERLQENlegfsegvkaLLKNQSGLSGILGVLSELISVDEGyeaaieaalgGRLQAVVVE--NLNAAKK-A 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1007 YEHL-----------------IDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMS--------------DLRGELNEKQKM 1055
Cdd:TIGR02168 562 IAFLkqnelgrvtflpldsikGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvdDLDNALELAKKL 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1056 ELEQNVV----------------------LVQQQSKELSVLKEKMAQMSSLVEKKDRELKALEEALRASQEKHRlQLNTE 1113
Cdd:TIGR02168 642 RPGYRIVtldgdlvrpggvitggsaktnsSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE-QLRKE 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1114 KEQKPRKKTQTcDTSVQIEPVHTEAFSSSQEQQSFSDLGVRCKGSRHEEVIQRQKKALSELRARIKELEkARSPDHKDHQ 1193
Cdd:TIGR02168 721 LEELSRQISAL-RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE-AQIEQLKEEL 798
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1194 NESFLDLKNLRMENNVQKILLDAKpdlptLSRIEILAPQNGLCNARFGSAMEKSGKM-----DVAEALELSEKLYLDMSK 1268
Cdd:TIGR02168 799 KALREALDELRAELTLLNEEAANL-----RERLESLERRIAATERRLEDLEEQIEELsedieSLAAEIEELEELIEELES 873
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1269 TLGSLMNIKnMSGHVSMKYLSRQEREKVNQLRQRDldlvfDKITQLKNQLGRKEELLRGYEKDVEQLrrsKVSIEMYQSQ 1348
Cdd:TIGR02168 874 ELEALLNER-ASLEEALALLRSELEELSEELRELE-----SKRSELRRELEELREKLAQLELRLEGL---EVRIDNLQER 944
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1370451826 1349 VAKLEDDIYKEAEEKALLKEA-LERMEHQLcqeKRINRAI 1387
Cdd:TIGR02168 945 LSEEYSLTLEEAEALENKIEDdEEEARRRL---KRLENKI 981
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
714-1104 |
1.72e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.31 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 714 ERNRAKETLEEERKRMQELESLLAqqkkalaksitqEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEA 793
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIID------------EKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 794 LESEKRKVQDLENHLTQ-QKEISESNIAYEKRkakeamekeKKKVQDLENRLTKQKEELELKeqkedvLNNKLSDALAMV 872
Cdd:TIGR02169 239 KEAIERQLASLEEELEKlTEEISELEKRLEEI---------EQLLEELNKKIKDLGEEEQLR------VKEKIGELEAEI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 873 EETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQT 952
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 953 ---IVSLEEKLQKVTQHHKKIEGEIatlkdndpapkeerpqdplvapmtessakdmayEHLIDDLLAAQKEILSQQEVIM 1029
Cdd:TIGR02169 384 rdeLKDYREKLEKLKREINELKREL---------------------------------DRLQEELQRLSEELADLNAAIA 430
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370451826 1030 KLRKDLTEAHSRMSDLRGELnEKQKMELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKALEEALRASQE 1104
Cdd:TIGR02169 431 GIEAKINELEEEKEDKALEI-KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
669-1128 |
1.85e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.38 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 669 KAAGASGREGEAERGEARARGEAQSQNQATDGREGGKALEEyiTQERNRAKETLE--EERKRMQELESLLAQQKKA-LAK 745
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKK--AEEAKKADEAKKkaEEAKKAEEAKKKAEEAKKAdEAK 1476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 746 SITQEKNRVKEA---LEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYE 822
Cdd:PTZ00121 1477 KKAEEAKKADEAkkkAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE 1556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 823 KRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEdvlnnKLSDALAMVEETQKTKATESLKAESLALKLNETLAELEt 902
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEA-----RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE- 1630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 903 tktkmimvEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKieGEIATLKDNDP 982
Cdd:PTZ00121 1631 --------EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK--AAEALKKEAEE 1700
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 983 APKEERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVV 1062
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370451826 1063 LVQQqskelsvLKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQTCDTS 1128
Cdd:PTZ00121 1781 IEEE-------LDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSK 1839
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
667-1419 |
2.10e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.38 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 667 AGKAAGASGREGEAERGEARARGEAQSQNQATDGREGGKALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKS 746
Cdd:PTZ00121 1145 ARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAK 1224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 747 ITQEKNRVKEAL-EEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENhLTQQKEISESNIAYEKRK 825
Cdd:PTZ00121 1225 KAEAVKKAEEAKkDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK-AEEKKKADEAKKAEEKKK 1303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 826 AKeamekekkkvqdlenrltkQKEELELKEQKEDVLNNKLSDALAMVEETQKtKATESLKAESLALKLNETLA-ELETTK 904
Cdd:PTZ00121 1304 AD-------------------EAKKKAEEAKKADEAKKKAEEAKKKADAAKK-KAEEAKKAAEAAKAEAEAAAdEAEAAE 1363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 905 TKMIMVEERLILQQKMVKALQDEQESQRHGfeEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEgEIATLKDNDPAP 984
Cdd:PTZ00121 1364 EKAEAAEKKKEEAKKKADAAKKKAEEKKKA--DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE-EKKKADEAKKKA 1440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 985 KEERPQDPLVAPMTES----SAKDMAYEHLIDDLLAAQKEILSQQEvimKLRKDLTEAHSRMSDLRGELNEKQKMEleqn 1060
Cdd:PTZ00121 1441 EEAKKADEAKKKAEEAkkaeEAKKKAEEAKKADEAKKKAEEAKKAD---EAKKKAEEAKKKADEAKKAAEAKKKAD---- 1513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1061 vvlvqqqskELSVLKEKmaqmsslveKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQTCDTSVQIEPVHTEAFS 1140
Cdd:PTZ00121 1514 ---------EAKKAEEA---------KKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED 1575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1141 ssqeqqsfsdlgvRCKGSRHEEVIQRQKKALSELRARIKELEKARSPDHKDHQNESFLDLKNLRMENNVQKILLDAKPDL 1220
Cdd:PTZ00121 1576 -------------KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKE 1642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1221 PTlsrieilapqnglcNARFGSAMEKSGKMDVAEALELSEKLYLDMSKTlgslmniknmsghVSMKYLSRQEREKVNQLR 1300
Cdd:PTZ00121 1643 AE--------------EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA-------------EEAKKAEEDEKKAAEALK 1695
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1301 QrdldlvfdkitqlKNQLGRKEELLRGYE----KDVEQLRRSKVSIEMYQSQVAKLEDDIYKEAEEKALLKEALERMEHQ 1376
Cdd:PTZ00121 1696 K-------------EAEEAKKAEELKKKEaeekKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHL 1762
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 1370451826 1377 LCQEKRINRAIRQQKVGTRKASLKMDQEREMLRKETSSKSSQS 1419
Cdd:PTZ00121 1763 KKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFD 1805
|
|
| FHA_Cep170A |
cd22724 |
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar ... |
37-102 |
2.32e-08 |
|
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar proteins; Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438776 [Multi-domain] Cd Length: 106 Bit Score: 53.44 E-value: 2.32e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370451826 37 IGRhENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHI-QNVAVKLIPGDILRFG 102
Cdd:cd22724 25 VGR-DDCELMLQSRSVDKQHAVINYDASTDEHKVKDLGSLNGTFVNDVRIpEQTYITLKLDDKLRFG 90
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
235-774 |
2.38e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 235 EEDLAQQDKDEIILLLGKEVSRLSDYEIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKEISQKcqvLDEDIDAKQK 314
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE---LEERLEELEE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 315 EIQSLKSQISALQkgyskvlcQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQN 394
Cdd:COG1196 324 ELAELEEELEELE--------EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 395 KDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKlckTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVE 474
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELE---EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 475 EKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATYGR-----AKPFRDKPVTDQQLIEKITQVTEDNI 549
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlagavAVLIGVEAAYEAALEAALAAALQNIV 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 550 NFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRHA 629
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARL 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 630 LSWLEEVEQLLRDLGILpsspnkdqvqqFSGNSAVFTAGKAAGASGREGEAERGEARARGEAQSQNQATDGREGGKALEE 709
Cdd:COG1196 633 EAALRRAVTLAGRLREV-----------TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370451826 710 yiTQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEE--------------QTRVQELEERLAR 774
Cdd:COG1196 702 --EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEaleelpeppdleelERELERLEREIEA 778
|
|
| FHA_MEK1-like |
cd22670 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ... |
32-109 |
2.54e-08 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine/threonine-protein kinase MEK1 and similar proteins; MEK1 (EC 2.7.11.1), also known as MRE4, is a meiosis-specific protein kinase required for chromosome synapsis and meiotic recombination. The recruitment and activation of MEK1 require the phosphorylation of the chromosome axis protein Hop1 at Thr318 (pT318), which is necessary for recognition by the MEK1 FHA domain. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438722 [Multi-domain] Cd Length: 105 Bit Score: 53.00 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 32 NKSTTIGRHENSDLVLQSPDIDNHHALIE---YNEAECSFV-LQDfNSRNGTFVNECHI-QNVAVKLIPGDILRF-GSAG 105
Cdd:cd22670 21 NQVITIGRSPSCDIVINDPFVSRTHCRIYsvqFDESSAPLVyVED-LSSNGTYLNGKLIgRNNTVLLSDGDVIEIaHSAT 99
|
....
gi 1370451826 106 LTYE 109
Cdd:cd22670 100 FVYV 103
|
|
| FHA_Cep170B |
cd22725 |
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) ... |
37-110 |
4.04e-08 |
|
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) and similar proteins; Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438777 [Multi-domain] Cd Length: 106 Bit Score: 52.62 E-value: 4.04e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370451826 37 IGRhENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQN---VAVKLipGDILRFGSAGLTYEL 110
Cdd:cd22725 25 VGR-EDCELMLQSRSVDKQHAVINYDQDTDEHWVKDLGSLNGTFVNDVRIPDqkyITLKL--NDVIRFGYDSNMYVL 98
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
34-102 |
4.98e-08 |
|
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the first FHA domain. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438746 [Multi-domain] Cd Length: 93 Bit Score: 51.94 E-value: 4.98e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370451826 34 STTIGRHENSDLVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHIQnvAVKLIPGDILRFG 102
Cdd:cd22694 17 SVRIGRDPDADVRLDDPRVSRRHALLEFDGDG--WVYTDLGSRNGTYLNGRRVQ--QVKLSDGTRVRLG 81
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
30-103 |
5.97e-08 |
|
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 (AtPP2C70) and similar proteins; AtPP2C70, also called kinase-associated protein phosphatase, or protein ROOT ATTENUATED GROWTH 1, dephosphorylates the serine/threonine receptor-like kinase RLK5. It may function as a signaling component in a pathway involving RLK5. It acts as a negative regulator of the CLAVATA1 signaling in plant development by binding and dephosphorylating CLAVATA1. It is also a component of a signaling pathway which mediates adaptation to NaCl stress. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438730 [Multi-domain] Cd Length: 102 Bit Score: 51.98 E-value: 5.97e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370451826 30 VLNKSTTIGRHENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVN--ECHIQNVAVKLIPGDILRFGS 103
Cdd:cd22678 20 GTRLPLTIGRIQRGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNgeSISPNGRPVVLSSGDVITLGS 95
|
|
| FHA_AGGF1 |
cd22686 |
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ... |
6-103 |
1.48e-07 |
|
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 (AGGF1) and similar proteins; AGGF1, also called angiogenic factor VG5Q, or G patch domain-containing protein 7 (GPATC7), or vasculogenesis gene on 5q protein, is an angiogenic factor involved in vascular development, angiogenesis, specification of hemangioblasts, and differentiation of veins. It promotes angiogenesis and the proliferation of endothelial cells. It inhibits inflammatory effect and preserve vascular integrity in non-nervous system diseases. Mutated AGGF1 causes susceptibility to Klippel-Trenaunay syndrome, a vascular disorder. Increased AGGF1 expression is associated with tumor angiogenesis. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438738 [Multi-domain] Cd Length: 123 Bit Score: 51.51 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 6 PCRLFIYGKTERMKAylksaeG--FFVLNKSTTIGRHENSDLVLQSPD--IDNHHALIEYNEAECSFVLQDFNSRNGTFV 81
Cdd:cd22686 3 PCIRVIVVESPSLQV------GslFIVTATGATIGREKDHGHTIRIPElgVSKFHAEIYYDDDEQSYTIVDLGSQNGTYL 76
|
90 100
....*....|....*....|....*..
gi 1370451826 82 NECHIQNVAVKLIP-----GDILRFGS 103
Cdd:cd22686 77 NGVRISQPKEKSDPyplthGDELKIGE 103
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
711-1411 |
1.71e-07 |
|
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: 56.22 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 711 ITQERNRAKETLEEERK---RMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAhEK 787
Cdd:TIGR02168 194 ILNELERQLKSLERQAEkaeRYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLE-EL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 788 RKAKEALESEKRKVQDLENHLTQQkeisesniayekrkakeamekekkkVQDLENRLTKQKEELELKEQKEDVLNNKLSD 867
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYALANE-------------------------ISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 868 ALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLilqqkmvkalqDEQESQRHGFEEEIMEYKEQIK 947
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL-----------EELEEQLETLRSKVAQLELQIA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 948 QHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERPQdplvapmTESSAKDMAYEHLIDDLLAAQKEILSQQEV 1027
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ-------AELEELEEELEELQEELERLEEALEELREE 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1028 IMKLRKDLTEAHSRMSDLRGELNEKQKM--ELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKALEEALR----- 1100
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLERLqeNLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGgrlqa 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1101 -------------ASQEKHR------LQLNTEKEQKP------RKKTQTCDTSVQIEPVHTEAFSSSQEQQSFSDL---- 1151
Cdd:TIGR02168 550 vvvenlnaakkaiAFLKQNElgrvtfLPLDSIKGTEIqgndreILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVlvvd 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1152 -----------------------------GVRCKGSRHEE-VIQRQKKALSELRARIKELE--------KARSPDHKDHQ 1193
Cdd:TIGR02168 630 dldnalelakklrpgyrivtldgdlvrpgGVITGGSAKTNsSILERRREIEELEEKIEELEekiaelekALAELRKELEE 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1194 NESFLDLKNLRMENNVQKILLDAKPDLPTLSRIEILAPQNGLCNARFGSAMEKSGKMD---------VAEALELSEKLYL 1264
Cdd:TIGR02168 710 LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEerleeaeeeLAEAEAEIEELEA 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1265 DMSKTLGSLMNIKNMSGHVSMKYlsRQEREKVNQLRQRDLDLVFDkITQLKNQLGRKEELLRGYEKDVEQLRRSkvsIEM 1344
Cdd:TIGR02168 790 QIEQLKEELKALREALDELRAEL--TLLNEEAANLRERLESLERR-IAATERRLEDLEEQIEELSEDIESLAAE---IEE 863
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370451826 1345 YQSQVAKLEDDIYKEAEEKALLKEALERMEHQLCQEKRINRAIRQQKvgtrkasLKMDQEREMLRKE 1411
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR-------SELRRELEELREK 923
|
|
| FHA_SNIP1_DDL-like |
cd22676 |
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA ... |
37-102 |
3.35e-07 |
|
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA domain-containing protein DDL, and similar proteins; SNIP1 is an FHA domain-containing protein required for pre-mRNA splicing as a component of the spliceosome. It inhibits NF-kappaB signaling by competing for its binding to the C/H1 domain of CBP/p300 transcriptional co-activators. It is involved in microRNA (miRNA) biogenesis. SNIP1 is a regulator of the cell cycle and cyclin D1 expression and may be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. This family also includes Arabidopsis thaliana FHA domain-containing protein DDL and similar proteins. DDL, also called protein DAWDLE, is involved in the microRNA (miRNA) and short interfering RNA (siRNA) biogenesis. It may facilitate DCL1 to access or recognize primary miRNAs. DDL binds RNA non-specifically. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438728 [Multi-domain] Cd Length: 111 Bit Score: 49.99 E-value: 3.35e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370451826 37 IGRHE-NSDLVLQSPDIDNHHALIEY-----------NEAECSFVLqDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFG 102
Cdd:cd22676 25 IGRDRrVADIPLDHPSCSKQHAVIQFrevekrnegdvIENIRPYII-DLGSTNGTFLNGEKIEpRRYYELREKDVLKFG 102
|
|
| VI_FHA |
TIGR03354 |
type VI secretion system FHA domain protein; Members of this protein family are FHA ... |
36-202 |
3.63e-07 |
|
type VI secretion system FHA domain protein; Members of this protein family are FHA (forkhead-associated) domain-containing proteins that are part of type VI secretion loci in a considerable number of bacteria, most of which are known pathogens. Species include Pseudomonas aeruginosa PAO1, Aeromonas hydrophila, Yersinia pestis, Burkholderia mallei, etc. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274537 [Multi-domain] Cd Length: 396 Bit Score: 54.30 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 36 TIGRHENSDLVLQSPD--IDNHHALIEYNEAecSFVLQDFnSRNGTFVNECH---IQNVAVKLIPGDILRFGSagltYEL 110
Cdd:TIGR03354 27 TIGRSEDCDWVLPDPErhVSGRHARIRYRDG--AYLLTDL-STNGVFLNGSGsplGRGNPVRLEQGDRLRLGD----YEI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 111 VIENPPPVSFPWMRGPAPWPGPQPPRATQQPNQAPPPSHIPF----HQGVQPAPMQRSWSQAFPRPTVVLPAsHRRPVSA 186
Cdd:TIGR03354 100 RVSLGDPLVSRQASESRADTSLPTAGGPPTPDPAPLAQLDPLkaldQEPLSAADLDDLSAPLFPPLDARLPA-FAAPIDA 178
|
170
....*....|....*.
gi 1370451826 187 NKEMFSFVVDDARKPP 202
Cdd:TIGR03354 179 EPTMVPPFVPLPAPEP 194
|
|
| FHA_GarA_OdhI-like |
cd22684 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium ... |
35-108 |
7.79e-07 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium glutamicum OdhI and similar proteins; This family includes Mycobacterium tuberculosis glycogen accumulation regulator GarA and Corynebacterium glutamicum oxoglutarate dehydrogenase inhibitor (OdhI). GarA is involved in the regulation of glutamate metabolism. It acts as a phosphorylation-dependent molecular switch that modulates the activities of Kgd, Gdh and GltB. GarA binds to Kgd, Gdh, GltB, PknB, and the N-terminal region of PknG via its FHA domain. OdhI is an essential component of the PknG signaling pathway. It can inhibit the activity of 2-oxoglutarate dehydrogenase only when it is unphosphorylated. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438736 [Multi-domain] Cd Length: 94 Bit Score: 48.53 E-value: 7.79e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370451826 35 TTIGRHENSDLVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHIQnvAVKLIPGDILRFGSAGLTY 108
Cdd:cd22684 23 TTAGRHPESDIFLDDVTVSRRHAEFRRAEGG--FVVRDVGSLNGTYVNRERID--SAVLRNGDEVQIGKFRLVF 92
|
|
| FHA_EspA-like |
cd22698 |
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ... |
8-109 |
8.68e-07 |
|
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA is a histidine protein kinase with a fork head-associated (FHA) domain at the N-terminus and a receiver domain at the C-terminus. It functions as an inhibitor of sporulation during early fruiting body development while cells are aggregating into raised mounds. EspA is part of a two-component signal transduction system that regulates the timing of sporulation initiation. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438750 [Multi-domain] Cd Length: 93 Bit Score: 48.56 E-value: 8.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 8 RLFIYGKTERMKAYLKSAEgffvlnksTTIGRHENSDLVLQSPDIDNHHALIEYNEAECsfVLQDFNSRNGTFVNECHIQ 87
Cdd:cd22698 4 LIEQKGSEEGKDYELDQDE--------FTIGRSSNNDIRLNDHSVSRHHARIVRQGDKC--NLTDLGSTNGTFLNGIRVG 73
|
90 100
....*....|....*....|..
gi 1370451826 88 NVAVKliPGDILRFGSAGLTYE 109
Cdd:cd22698 74 THELK--HGDRIQLGETIFRFI 93
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
278-968 |
9.24e-07 |
|
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: 53.69 E-value: 9.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 278 VAELSQKVSETTTSRQNEKEIS---------QKCQVLDEDIDAKQKEIQSLKS---QISALQKGYSKVLCQTLSERNSEI 345
Cdd:pfam12128 203 VAILEDDGVVPPKSRLNRQQVEhwirdiqaiAGIMKIRPEFTKLQQEFNTLESaelRLSHLHFGYKSDETLIASRQEERQ 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 346 TSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKdkdhqlEALGSRCSVLKEELKQEDAHRELR 425
Cdd:pfam12128 283 ETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHG------AFLDADIETAAADQEQLPSWQSEL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 426 EAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERA 505
Cdd:pfam12128 357 ENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFN 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 506 VGQLEhfrsqvIKATYGRAKPFRDKPVTDQQLIEKITqvtedniNFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDs 585
Cdd:pfam12128 437 EEEYR------LKSRLGELKLRLNQATATPELLLQLE-------NFDERIERAREEQEAANAEVERLQSELRQARKRRD- 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 586 cQACMKISCCSHDLKKEVDLLQ--HLQVSPPVSGLqkvvLDVLR-HALSWLEEV------EQLLR-DLgilpsSPNKDqv 655
Cdd:pfam12128 503 -QASEALRQASRRLEERQSALDelELQLFPQAGTL----LHFLRkEAPDWEQSIgkvispELLHRtDL-----DPEVW-- 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 656 qqfsgnsavftagkaagASGREGEAERGEARARGEAQSQNQATDgreggkaLEEYITQERNRAKETLEEERKRMQELESL 735
Cdd:pfam12128 571 -----------------DGSVGGELNLYGVKLDLKRIDVPEWAA-------SEEELRERLDKAEEALQSAREKQAAAEEQ 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 736 LAQQKKALAKSitqeknrvKEALEEEQTRVQELEERLARQKEVLESsiahEKRKAKEALESEKRKVQDLENHLTQQKEIS 815
Cdd:pfam12128 627 LVQANGELEKA--------SREETFARTALKNARLDLRRLFDEKQS----EKDKKNKALAERKDSANERLNSLEAQLKQL 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 816 ESNIAYEKRKAKEamekekkkvQDLENRLTKQKEELelkeqkedVLNNKLSDALAMVEETqKTKATESLKAESLALK--L 893
Cdd:pfam12128 695 DKKHQAWLEEQKE---------QKREARTEKQAYWQ--------VVEGALDAQLALLKAA-IAARRSGAKAELKALEtwY 756
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 894 NETLAELETTKTKMIMVE-ERLILQQKMVKALQDEQES------QRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQH 966
Cdd:pfam12128 757 KRDLASLGVDPDVIAKLKrEIRTLERKIERIAVRRQEVlryfdwYQETWLQRRPRLATQLSNIERAISELQQQLARLIAD 836
|
..
gi 1370451826 967 HK 968
Cdd:pfam12128 837 TK 838
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
680-1224 |
9.87e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 9.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 680 AERGEARARGEAQSQNQATDGREGGKALEEYITQERNRAKETLE--EERKRMQELESLLAQQKKAL--AKSITQEKNRVK 755
Cdd:PTZ00121 1266 ARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKkaEEAKKADEAKKKAEEAKKKAdaAKKKAEEAKKAA 1345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 756 EALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALE--SEKRKVQDLENHLTQQK----EISESNIAYEKRKAKEA 829
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKkkadELKKAAAAKKKADEAKK 1425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 830 MEKEKKKVQDLENRLTKQKEELELKEQKEDvlNNKLSDALAMVEETQKT-----KATESLKAESLALKLNETLAELETTK 904
Cdd:PTZ00121 1426 KAEEKKKADEAKKKAEEAKKADEAKKKAEE--AKKAEEAKKKAEEAKKAdeakkKAEEAKKADEAKKKAEEAKKKADEAK 1503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 905 TKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQ-----HAQTIVSLEEKlQKVTQHHKKIEGEIATLKD 979
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKadelkKAEELKKAEEK-KKAEEAKKAEEDKNMALRK 1582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 980 NDPAPKEERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEvimKLRKDLTEAHSRMSDLRGELNEKQKMELEQ 1059
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE---EEKKKVEQLKKKEAEEKKKAEELKKAEEEN 1659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1060 NVVLVQQQSKElsvlKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQTCDTSVQIEPVHTEAF 1139
Cdd:PTZ00121 1660 KIKAAEEAKKA----EEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA 1735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1140 SSSQEQQSFSDLGVRCKGSRHEEVIQRQKKALSELRARIKELEKA--RSPDHKDHQNESFLDLKNLRMENNVQKILLDAK 1217
Cdd:PTZ00121 1736 KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVieEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGK 1815
|
....*..
gi 1370451826 1218 PDLPTLS 1224
Cdd:PTZ00121 1816 EGNLVIN 1822
|
|
| FHA_NBN |
cd22667 |
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ... |
28-108 |
3.61e-06 |
|
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also called cell cycle regulatory protein p95, or Nijmegen breakage syndrome protein 1 (NBS1), is a novel DNA double-strand break repair protein that is mutated in Nijmegen breakage syndrome. It is a component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. Nibrin modulates the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-dependent protein kinase catalytic subunit (DNA-PKcs) to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. Nibrin also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. Nibrin is a major player in the control of intra-S-phase checkpoint. This subfamily also includes Schizosaccharomyces pombe DNA repair and telomere maintenance protein Nbs1 and Arabidopsis thaliana AtNbs1. SpNbs1 is an FHA domain-containing protein required for DNA damage repair and S-phase DNA damage checkpoint. It is involved in telomere length maintenance and maintenance of chromatin structure. AtNbs1 is a component of MRN complex. It also functions in the very early stages of meiosis. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438719 [Multi-domain] Cd Length: 108 Bit Score: 46.94 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 28 FFVLNKSTTIGRHENSDLVLQSPDIDNHHALI--EYNEAECSF-------VLQDFnSRNGTFVNECHIQNVA-VKLIPGD 97
Cdd:cd22667 15 YLLPGGEYTVGRKDCDIIIVDDSSISRKHATLtvLHPEANLSDpdtrpelTLKDL-SKYGTFVNGEKLKGGSeVTLKDGD 93
|
90
....*....|.
gi 1370451826 98 ILRFGSAGLTY 108
Cdd:cd22667 94 VITFGVLGSKF 104
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
230-963 |
3.90e-06 |
|
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: 51.51 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 230 AEIYVEEDLAQQDKDEIILLLGKEVSRLSDYEIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDI 309
Cdd:pfam02463 244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEK 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 310 DAKQKEIQSLKSQISALQKGYSKVLCQTLSERNSEITSLKNEGENLKRDNAITSGmVSSLQKDILAKDEQVQQLKEEVSH 389
Cdd:pfam02463 324 KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAK-KKLESERLSSAAKLKEEELELKSE 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 390 LKSQNKDKDHQLEALGSRCSVL-KEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLR 468
Cdd:pfam02463 403 EEKEAQLLLELARQLEDLLKEEkKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKL 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 469 EKSKvEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATYGRAKP----------FRDKPVTDQQLI 538
Cdd:pfam02463 483 QEQL-ELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVEnykvaistavIVEVSATADEVE 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 539 EKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISC--------CSHDLKKEVDLLQHLQ 610
Cdd:pfam02463 562 ERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEddkrakvvEGILKDTELTKLKESA 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 611 VSPPVSGLQKVVLDVLRHALSWLEEVEQLLRDLGILPSSPNKDQVQQFSGNSAVFTAGKAAGASGREGEAERGEARARGE 690
Cdd:pfam02463 642 KAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEE 721
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 691 AQSQNQATDGREGGKALEEYITQERNRAKETLEEERKRMQELESLLA--QQKKALAKSITQEKNRVKEALEEEQTRVQEL 768
Cdd:pfam02463 722 LLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSElsLKEKELAEEREKTEKLKVEEEKEEKLKAQEE 801
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 769 EER-----------LARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYE----KRKAKEAMEKE 833
Cdd:pfam02463 802 ELRaleeelkeeaeLLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEellqELLLKEEELEE 881
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 834 KKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEER 913
Cdd:pfam02463 882 QKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEER 961
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1370451826 914 LILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKV 963
Cdd:pfam02463 962 NKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAI 1011
|
|
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
30-102 |
5.95e-06 |
|
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and similar proteins; SLMAP, also called sarcolemmal-associated protein (SLAP), is a tail-anchored protein involved in fundamental cellular processes, such as myoblast fusion, cell cycle progression, and chromosomal inheritance. It is a cardiac membrane protein that plays an important role in E-C coupling and the adrenergic response of the heart. Overexpression of the SLMAP gene has been associated with diabetes and endothelial dysfunction of macro- and micro-blood vessels. SLMAP contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438731 [Multi-domain] Cd Length: 126 Bit Score: 46.88 E-value: 5.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 30 VLNKSTTIGRHEN------SDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQ-----NVAVKLIPGDI 98
Cdd:cd22679 21 VLDEPVKIGRSVArarpaaNNAIFDCKVLSRNHALLWYDDG--KFYLQDTKSSNGTFVNNQRLSkgseeSEPRELHSGDI 98
|
....
gi 1370451826 99 LRFG 102
Cdd:cd22679 99 VQFG 102
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
688-1410 |
1.08e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 688 RGEAQSQNQATDGREGGKALEEYITQERNRAKETLEEERKRMQELESLLA-----QQKKALAKSITQEKNRVKEALEEEQ 762
Cdd:PTZ00121 1059 KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETgkaeeARKAEEAKKKAEDARKAEEARKAED 1138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 763 TRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKvqdlenHLTQQKEISESNIAYEKRKAKEAMEKEKKKVQDLEN 842
Cdd:PTZ00121 1139 ARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAK------KAEAARKAEEVRKAEELRKAEDARKAEAARKAEEER 1212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 843 RLTKQKEELELkeqkedvlnnKLSDALAMVEETQKtKATESLKAESLalKLNETLAELETTKTKMIMVEERLILQQKMVK 922
Cdd:PTZ00121 1213 KAEEARKAEDA----------KKAEAVKKAEEAKK-DAEEAKKAEEE--RNNEEIRKFEEARMAHFARRQAAIKAEEARK 1279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 923 ALQDEQESQRHGFEE----EIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIE-----GEIATLKDNDPAPKEERPQDPL 993
Cdd:PTZ00121 1280 ADELKKAEEKKKADEakkaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADaakkkAEEAKKAAEAAKAEAEAAADEA 1359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 994 VAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEViMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQQSKELSV 1073
Cdd:PTZ00121 1360 EAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA-DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK 1438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1074 lKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQTCDTSVQIEPVHTEAFSSSQEQQSFSDLGV 1153
Cdd:PTZ00121 1439 -KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKK 1517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1154 RCKGSRHEEVIQRQKKALSELRARIKELEKArspdhkdhqnESFLDLKNLRMENNVQKilldakpdlptlsrieilAPQN 1233
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADEAKKAEEKKKA----------DELKKAEELKKAEEKKK------------------AEEA 1569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1234 GLCNARFGSAMEKSGKMDVAEALELSEklyldmsktlgslmniknmsghvSMKYLSRQEREKVNQLRQRDLDlvfdkitQ 1313
Cdd:PTZ00121 1570 KKAEEDKNMALRKAEEAKKAEEARIEE-----------------------VMKLYEEEKKMKAEEAKKAEEA-------K 1619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1314 LKNQLGRKEELLRgyeKDVEQLRRSkvsiemyQSQVAKLEDDIYKEAEEKALLKEALERMEHqlcQEKRINRAIRQQKVG 1393
Cdd:PTZ00121 1620 IKAEELKKAEEEK---KKVEQLKKK-------EAEEKKKAEELKKAEEENKIKAAEEAKKAE---EDKKKAEEAKKAEED 1686
|
730
....*....|....*..
gi 1370451826 1394 TRKASLKMDQEREMLRK 1410
Cdd:PTZ00121 1687 EKKAAEALKKEAEEAKK 1703
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
271-503 |
1.26e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.02 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 271 IANLQNEVAELSQKVSETTTSRQNEKEisqKCQVLDEDIDAKQKEIQSLKSQISALQKGYSKVlcQTLSERN----SEIT 346
Cdd:TIGR04523 147 IKKKEKELEKLNNKYNDLKKQKEELEN---ELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNL--KKKIQKNksleSQIS 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 347 SLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQ--------------NKDKDHQLEALGSRCSVLK 412
Cdd:TIGR04523 222 ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQlsekqkeleqnnkkIKELEKQLNQLKSEISDLN 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 413 EElKQEDAHRELRE---AQEKELKLCKTQIQDMEK-------EMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSR 482
Cdd:TIGR04523 302 NQ-KEQDWNKELKSelkNQEKKLEEIQNQISQNNKiisqlneQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQ 380
|
250 260
....*....|....*....|.
gi 1370451826 483 RKLLQLQEMGNRESVIKINLE 503
Cdd:TIGR04523 381 SYKQEIKNLESQINDLESKIQ 401
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
29-102 |
1.54e-05 |
|
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing protein ArnA and similar proteins; ArnA is an FHA domain-containing protein from Sulfolobus acidocaldarius that was shown to strongly interact with ArnB, a von Willebrand domain-containing protein. They act synergistically and negatively to modulate motility. ArnA is involved in regulating archaella expression in S. acidocaldarius. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438732 [Multi-domain] Cd Length: 96 Bit Score: 45.02 E-value: 1.54e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370451826 29 FVLNKST-TIGRHENSDLVLQSPDIDNHHALIeYNEaECSFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRFG 102
Cdd:cd22680 16 FPFDFSSvSIGRDPENVIVIPDPFVSRNHARI-TVD-SNEIYIEDLGSTNGTFVNDFKRIKGPAKLHPNDIIKLG 88
|
|
| Yop-YscD_cpl |
pfam16697 |
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ... |
36-103 |
1.55e-05 |
|
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.
Pssm-ID: 465238 [Multi-domain] Cd Length: 94 Bit Score: 44.94 E-value: 1.55e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370451826 36 TIGRHENSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRFGS 103
Cdd:pfam16697 20 RIGSDPDCDIVLSDKEVSRVHLKLEVDDE--GWRLDDLGSGNGTLVNGQRVTELGIALRPGDRIELGQ 85
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
32-104 |
1.95e-05 |
|
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar proteins; ZEP, also called protein ABA DEFICIENT 1, ABA1, protein IMPAIRED IN BABA-INDUCED STERILITY 3, protein LOW EXPRESSION OF OSMOTIC STRESS-RESPONSIVE GENES 6, or protein NON-PHOTOCHEMICAL QUENCHING 2, plays an important role in the xanthophyll cycle and abscisic acid (ABA) biosynthesis. It converts zeaxanthin into antheraxanthin and subsequently violaxanthin. ZEP is required for resistance to osmotic and drought stresses, ABA-dependent stomatal closure, seed development and dormancy, modulation of defense gene expression, and disease resistance and non-photochemical quencing (NPQ). The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438754 [Multi-domain] Cd Length: 123 Bit Score: 45.49 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 32 NKSTTIGR--HENSD---LVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHIQ------NVAVKLIPGDILR 100
Cdd:cd22702 31 KQPCIIGSdpHQAISgisVVIPSPQVSELHARITCKNGA--FFLTDLGSEHGTWINDNEGRryrappNFPVRLHPSDVIE 108
|
....
gi 1370451826 101 FGSA 104
Cdd:cd22702 109 FGSD 112
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
679-978 |
2.81e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 679 EAERGEARARGEAQSQNQATDGREGGKALEEYITQERNRAKE--TLEEERKRMQELESLLAQQKKALAKSITQEKNRVKE 756
Cdd:TIGR02169 204 RREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQlaSLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 757 ALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISES--NIAYEKRKAKEAMEKEK 834
Cdd:TIGR02169 284 LGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREieEERKRRDKLTEEYAELK 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 835 KKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERL 914
Cdd:TIGR02169 364 EELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370451826 915 ilqqkmvKALQDEQESQrhgfEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLK 978
Cdd:TIGR02169 444 -------EDKALEIKKQ----EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
271-509 |
3.08e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 271 IANLQNEVAELSQKVSETttsRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQkgyskvlcQTLSERNSEITSLKN 350
Cdd:COG4942 29 LEQLQQEIAELEKELAAL---KKEEKALLKQLAALERRIAALARRIRALEQELAALE--------AELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 351 EgenLKRDNAITSGMVSSLQK-------DILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRE 423
Cdd:COG4942 98 E---LEAQKEELAELLRALYRlgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 424 LREAQEKELKLCKTQIQDMEKEMKKLRAELRKsctEQSVISRTLREKSKVEEKLQEDSRRklLQLQEMGNRESVIKINLE 503
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEK---ELAELAAELAELQQEAEELEALIAR--LEAEAAAAAERTPAAGFA 249
|
....*.
gi 1370451826 504 RAVGQL 509
Cdd:COG4942 250 ALKGKL 255
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
411-816 |
3.44e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 411 LKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKsCTEQSVISRTLREKSKVEEKLQEDSRRkllqLQE 490
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK-LEKLLQLLPLYQELEALEAELAELPER----LEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 491 MGNRESvikiNLERAVGQLEHFRSQVIKATYGRAKPFRDKPVTDQQLIEKITQVTEDninfqqkkwtLQKETQLSNSKQE 570
Cdd:COG4717 151 LEERLE----ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE----------LQQRLAELEEELE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 571 ETTENIEKLRTSLDSCQAcmkisccSHDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRHALSWLEEVEQLLRD-LGILPSS 649
Cdd:COG4717 217 EAQEELEELEEELEQLEN-------ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLvLGLLALL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 650 PNKDQVQQFSGNSAVFTAGKAAGASGREgEAERGEARARGEAQSQNQATDGREGGKALEEYitQERNRAKETLEEERKRM 729
Cdd:COG4717 290 FLLLAREKASLGKEAEELQALPALEELE-EEELEELLAALGLPPDLSPEELLELLDRIEEL--QELLREAEELEEELQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 730 QELESLLAQQKKALAKSITQ--EKNRVKEALEEEQTRVQELEERLARQ-KEVLESSIAHEKRKAKEALESEKRKVQDLEN 806
Cdd:COG4717 367 ELEQEIAALLAEAGVEDEEElrAALEQAEEYQELKEELEELEEQLEELlGELEELLEALDEEELEEELEELEEELEELEE 446
|
410
....*....|.
gi 1370451826 807 HLTQ-QKEISE 816
Cdd:COG4717 447 ELEElREELAE 457
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
684-967 |
3.67e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 48.36 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 684 EARARGEAQSQNQATDGREGGKALEEYITQERNRAKETLEEERKRMQELESL--LAQQKKALAKSITQEKNRVKEALE-- 759
Cdd:PLN02939 107 AIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLekILTEKEALQGKINILEMRLSETDAri 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 760 ----EEQTRVQELEERLAR------QKEVLESSIAHEKRKAKEALESE----KRKVQDLENHLTQQKEISESNIAYEKrk 825
Cdd:PLN02939 187 klaaQEKIHVEILEEQLEKlrnellIRGATEGLCVHSLSKELDVLKEEnmllKDDIQFLKAELIEVAETEERVFKLEK-- 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 826 akeAMEKEKKKVQDLENRLTKQKEelelkeqkeDVLnnKLS----DAL-AMVEETQKTKATESLKAESLAL--------- 891
Cdd:PLN02939 265 ---ERSLLDASLRELESKFIVAQE---------DVS--KLSplqyDCWwEKVENLQDLLDRATNQVEKAALvldqnqdlr 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 892 ----KLNETLAELETTKTKMIMVEerlILQQKMvKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHH 967
Cdd:PLN02939 331 dkvdKLEASLKEANVSKFSSYKVE---LLQQKL-KLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEESKKRSLEH 406
|
|
| FHA_FhaA-like |
cd22668 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
34-106 |
8.21e-05 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaA and similar proteins; FhaA regulates cell growth and peptidoglycan synthesis by binding to MviN. It may inhibit the late stages of peptidoglycan synthesis. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438720 [Multi-domain] Cd Length: 91 Bit Score: 42.84 E-value: 8.21e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370451826 34 STTIGRHENSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQnVAVKLIPGDILRFGSAGL 106
Cdd:cd22668 19 SNIIGRGSDADFRLPDTGVSRRHAEIRWDGQ--VAHLTDLGSTNGTTVNNAPVT-PEWRLADGDVITLGHSEI 88
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
404-1096 |
8.78e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 8.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 404 LGSRCSVLKEELKQEDAHRELR-EAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSR 482
Cdd:COG1196 198 LERQLEPLERQAEKAERYRELKeELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 483 RKLLQLQEMGNRESVIKINLERAVGQLEHfrsqvikatygrakpfrdkpvtdqqliekitqVTEDNINFQQKKWTLQKET 562
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIAR--------------------------------LEERRRELEERLEELEEEL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 563 QLSNSKQEETTENIEKLRTSLDscqacmkisccshDLKKEVDLLQHLqvsppvsglqkvvldvlrhalswLEEVEQLLRD 642
Cdd:COG1196 326 AELEEELEELEEELEELEEELE-------------EAEEELEEAEAE-----------------------LAEAEEALLE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 643 LgilpsspnkdqvqqfsgnsavftagkAAGASGREGEAERGEARARGEAQSQNQATDGREGGKALEEYITQERNRAKETL 722
Cdd:COG1196 370 A--------------------------EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 723 EEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQ 802
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 803 DLEnhltqqkeiSESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNN--KLSDALAMVEETQKTKA 880
Cdd:COG1196 504 EGF---------LEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDdeVAAAAIEYLKAAKAGRA 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 881 TESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEyKEQIKQHAQTIVSLEEKL 960
Cdd:COG1196 575 TFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA-LRRAVTLAGRLREVTLEG 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 961 QKVTQHHKKIEGEIATLKDNDPAPKEERpqdplvapmTESSAKDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHS 1040
Cdd:COG1196 654 EGGSAGGSLTGGSRRELLAALLEAEAEL---------EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEE 724
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370451826 1041 RMSDLRGELNEKQKMELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKALE 1096
Cdd:COG1196 725 ALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
705-816 |
1.04e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 705 KALEEYITQERNRAKETLEEERKRMQEL--ESLLAQQKKALaksitQEKNRVKEALEEEQTRVQELEERLARQKEVLEss 782
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKEAEAIkkEALLEAKEEIH-----KLRNEFEKELRERRNELQKLEKRLLQKEENLD-- 99
|
90 100 110
....*....|....*....|....*....|....
gi 1370451826 783 iahekrKAKEALESEKRKVQDLENHLTQQKEISE 816
Cdd:PRK12704 100 ------RKLELLEKREEELEKKEKELEQKQQELE 127
|
|
| FHA_Slr1951-like |
cd22697 |
forkhead associated (FHA) domain found in Synechocystis sp. Slr1951 protein and similar ... |
36-109 |
1.14e-04 |
|
forkhead associated (FHA) domain found in Synechocystis sp. Slr1951 protein and similar proteins; This subfamily corresponds to a group of uncharacterized FHA domain-containing proteins which show high sequence similarity with Synechocystis sp. protein Slr1951 and protein Sll1895. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438749 [Multi-domain] Cd Length: 102 Bit Score: 42.84 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 36 TIGRHENSDLVLQSPDIDNHHALIEY----NEAECSFVLQDF----NSRNGTFVNECHIQNVAvkLIPGDILRFG-SAGL 106
Cdd:cd22697 21 TIGRHPGNDIQIPSQQISRRHATLRRkinpNLDISFWIIDGDlegaESLNGLWVNGERILQHE--LVNGDEIALGpKIVL 98
|
...
gi 1370451826 107 TYE 109
Cdd:cd22697 99 RYQ 101
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
635-1411 |
1.43e-04 |
|
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: 46.50 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 635 EVEQLLRDLGILPSSPN----KDQVQQFSGNSAVFTAgKAAGASGREGEAERGEARARGEAQSQNQatdgreggKALEEY 710
Cdd:pfam02463 120 EVAELLESQGISPEAYNflvqGGKIEIIAMMKPERRL-EIEEEAAGSRLKRKKKEALKKLIEETEN--------LAELII 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 711 ITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKA 790
Cdd:pfam02463 191 DLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQV 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 791 KEALESEKRKVQDLENHLTQQKEISESNIAyEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALA 870
Cdd:pfam02463 271 LKENKEEEKEKKLQEEELKLLAKEEEELKS-ELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEI 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 871 MVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHA 950
Cdd:pfam02463 350 KREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEEL 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 951 QTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEVIMK 1030
Cdd:pfam02463 430 EILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGL 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1031 LRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQL 1110
Cdd:pfam02463 510 KVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKL 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1111 NTEKEQKPrkktqtcdTSVQIEPVHTEAFSSSQEQQSFSDLGVRCKGSRHEEVIQRQ--KKALSELRARIKELEKARSPD 1188
Cdd:pfam02463 590 PLKSIAVL--------EIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKesAKAKESGLRKGVSLEEGLAEK 661
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1189 HKDHQNESFLDLKNLRMENNVQKILLDAKPdLPTLSRIEILAPQNGLCNARFGSAMEKSGKMDVAEALELSEKLYLDMSK 1268
Cdd:pfam02463 662 SEVKASLSELTKELLEIQELQEKAESELAK-EEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKL 740
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1269 TLGSLMNIKNMSGHVSMKYLSRQEREKVNQLRQRDLDLVFDKITQLKNQLGRKEELLRGYEKDVEQLRRSKVSIEMYQSQ 1348
Cdd:pfam02463 741 LKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEE 820
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370451826 1349 ---VAKLEDDIYKEAEEKALLKEALERMEHQLCQEKRINRAIRQQKVGTRKASLKMDQEREMLRKE 1411
Cdd:pfam02463 821 qllIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKD 886
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
677-951 |
1.95e-04 |
|
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: 45.88 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 677 EGEAERGEARARGEAQSQNQATDGREGGKALEEYITQERNRAKETLEEER-----KRMQELESLLA--QQKKALAKSITQ 749
Cdd:pfam17380 320 EAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEiameiSRMRELERLQMerQQKNERVRQELE 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 750 EKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEA 829
Cdd:pfam17380 400 AARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLEL 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 830 mekekkkvqDLENRLTKQKEELELKEQKEDVLNNKlsdaLAMVEETQKTKATE-SLKAESLALKLNETLAELETTKTKMI 908
Cdd:pfam17380 480 ---------EKEKRDRKRAEEQRRKILEKELEERK----QAMIEEERKRKLLEkEMEERQKAIYEEERRREAEEERRKQQ 546
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1370451826 909 MVEERLILQQKMVKALQDEQESQRHGFEEEIM-EYKEQIKQHAQ 951
Cdd:pfam17380 547 EMEERRRIQEQMRKATEERSRLEAMEREREMMrQIVESEKARAE 590
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
709-792 |
2.50e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 709 EYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNRvKEALEEEQTRVQELEERLARQKEVLESSIAHEKR 788
Cdd:COG4942 142 KYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE-RAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
....
gi 1370451826 789 KAKE 792
Cdd:COG4942 221 EAEE 224
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
242-591 |
2.67e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.84 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 242 DKDEIILLLGKEVSRLSDYEIESKykDVIIANLQNEVAELSQKVSEtttsrqnekeisqkcqvLDEDIdakqKEIQSLKS 321
Cdd:COG5022 843 KAEVLIQKFGRSLKAKKRFSLLKK--ETIYLQSAQRVELAERQLQE-----------------LKIDV----KSISSLKL 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 322 QISALQKGYSKVLCQTLSERNSEITSLKNEGENLKRdnAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQL 401
Cdd:COG5022 900 VNLELESEIIELKKSLSSDLIENLEFKTELIARLKK--LLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLL 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 402 EALGSrcsvLKEELKQEdahRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDS 481
Cdd:COG5022 978 KKSTI----LVREGNKA---NSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILKPLQK 1050
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 482 RRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATYGRAK--PFRDKPVTDQQLIEKITQVteDNINFQQKKWTLQ 559
Cdd:COG5022 1051 LKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKtiNVKDLEVTNRNLVKPANVL--QFIVAQMIKLNLL 1128
|
330 340 350
....*....|....*....|....*....|..
gi 1370451826 560 KETQLSNSKQEETTENIEKLRTSLDSCQACMK 591
Cdd:COG5022 1129 QEISKFLSQLVNTLEPVFQKLSVLQLELDGLF 1160
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
304-442 |
2.88e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.96 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 304 VLDEDIDAKQKEIQSLKSQIS------ALQKGYSKVLCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKdilakd 377
Cdd:PRK09039 43 FLSREISGKDSALDRLNSQIAeladllSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEG------ 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370451826 378 eQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKqedAHRELREAQEKELKLCKTQIQDM 442
Cdd:PRK09039 117 -RAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLA---ALEAALDASEKRDRESQAKIADL 177
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
285-533 |
3.16e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 285 VSETTTSRQNEKEISQkcqvLDEDIDAKQKEIQSLKSQISALQKgyskvlcqTLSERNSEITSLKNEGENLKRDNAITSG 364
Cdd:COG4942 16 AAQADAAAEAEAELEQ----LQQEIAELEKELAALKKEEKALLK--------QLAALERRIAALARRIRALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 365 MVSSLQKDILAKDEQVQQLKEEVSHL--KSQNKDKDHQLEALGSRCSVLKEELKQE------DAHRELREAQEKELKLCK 436
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPEDFLDAVRRLQylkylaPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 437 TQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHFRSQV 516
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
250
....*....|....*..
gi 1370451826 517 IKATYGRAKPFRDKPVT 533
Cdd:COG4942 244 PAAGFAALKGKLPWPVS 260
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
28-110 |
3.46e-04 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 (FKH1), 2 (FKH2) and similar proteins; This family includes FKH1 and FKH2, as well as pre-rRNA-processing protein FHL1. FKH1 and FKH2 are forkhead transcription factors that regulate the expression of the CLB2 cluster of genes during the G2/M phase of the mitotic cell cycle. The CLB2 cluster of genes includes mitotic regulators such as CLB1, CLB2, CDC5 and CDC20, as well as SWI5 and ACE2. FKH1 and FKH2 are involved in HMRa silencing. They associate with the coding regions of active genes and influence, in opposing ways, transcriptional elongation and termination, and coordinate early transcription elongation and pre-mRNA processing. Both FKH1 and FKH2 play a role as regulators of lifespan in collaboration with the anaphase-promoting complex (APC), likely through combined regulation of stress response, genomic stability, and cell cycle regulation. They also function in controlling yeast cell morphology by preventing pseudohyphal growth and act as rate-limiting replication origin activators via their interaction with the origin recognition complex (ORC). FHL1 is a forkhead protein that controls the pre-rRNA processing machinery in conjunction with IFH1. It might act as a transcriptional regulator of genes specifically involved in that process. IFH1 convert FHL1 from a repressor to an activator. This family also includes AtFHA1 and AtFHA2, which may play a role in the control of plant organ development. AtFHA2 is specifically involved in the regulation of stamen development. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438753 [Multi-domain] Cd Length: 106 Bit Score: 41.46 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 28 FFVLNKSTTIGR---------HENSDLVLQSPD-IDNHHALIEYNEAECSFVLQDFnSRNGTFVNE--CHIQNVAVKLIP 95
Cdd:cd22701 12 YYVQKLEVVLGRnsknssstaADSVDIDLGPSKkISRRHARIFYDFTTQCFELSVL-GRNGVKVDGilVKPGSPPVPLRS 90
|
90
....*....|....*
gi 1370451826 96 GDILRFGSAGLTYEL 110
Cdd:cd22701 91 GSLIQIGGVLFYFLL 105
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
712-996 |
3.89e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 712 TQERNRAKETLEEERKRMQELESLLAQQKKAlAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSiahekrkak 791
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAEL--------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 792 ealeseKRKVQDLENHLTQQKEisesniayekrkakeamekekkkvqDLENRLTKQKEELELKEQKEDVLNNKLSDALAM 871
Cdd:COG4942 89 ------EKEIAELRAELEAQKE-------------------------ELAELLRALYRLGRQPPLALLLSPEDFLDAVRR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 872 VEETQktkateslkaeSLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQ 951
Cdd:COG4942 138 LQYLK-----------YLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEK 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1370451826 952 TIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERPQDPLVAP 996
Cdd:COG4942 207 ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
670-974 |
4.04e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 670 AAGASGREGEAERGEARARGEAQSQ--NQATDGREGGKALEEYITQERNRAKE-------TLEEERKRMQELESLLAQQK 740
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEIEELRErfGDAPVDLGNAEDFLEELREERDELREreaeleaTLRTARERVEEAEALLEAGK 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 741 KALAKSITQEKNRVkEALEEEQTRVQELEERLArQKEVLESSIAHEKRKAKEALESEKR------KVQDLENHLTQQKEI 814
Cdd:PRK02224 454 CPECGQPVEGSPHV-ETIEEDRERVEELEAELE-DLEEEVEEVEERLERAEDLVEAEDRierleeRREDLEELIAERRET 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 815 SEsniayEKRKAKEAMEKEKKKV----QDLENRLTKQKEELELKEQKEDVLNNKLS------DALAMVEETQKTKATESL 884
Cdd:PRK02224 532 IE-----EKRERAEELRERAAELeaeaEEKREAAAEAEEEAEEAREEVAELNSKLAelkeriESLERIRTLLAAIADAED 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 885 KAESLALKLnETLAELETTKtkmimvEERLILQQKMVKALQDEQEsqrhgfEEEIMEYKEQIKQHAQTIVSLEEKLQKVT 964
Cdd:PRK02224 607 EIERLREKR-EALAELNDER------RERLAEKRERKRELEAEFD------EARIEEAREDKERAEEYLEQVEEKLDELR 673
|
330
....*....|
gi 1370451826 965 QHHKKIEGEI 974
Cdd:PRK02224 674 EERDDLQAEI 683
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
252-797 |
4.29e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 252 KEVSRLSDYEIESKykdviiaNLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQKGYS 331
Cdd:PRK03918 152 RQILGLDDYENAYK-------NLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 332 KVlcqtlSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDkdhqlealgsrcsvL 411
Cdd:PRK03918 225 KL-----EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE--------------L 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 412 KEELKQEDAHRELREAQEKELKlcktQIQDMEKEMKKLRAELRkscteqsVISRTLREKSKVEEKLQEDSRRkllqLQEM 491
Cdd:PRK03918 286 KELKEKAEEYIKLSEFYEEYLD----ELREIEKRLSRLEEEIN-------GIEERIKELEEKEERLEELKKK----LKEL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 492 GNRESVIKINLEravgqlEHFRSQVIKATYGRAKPfRDKPVTDQQLIEKITQVTEDNINFQQKKWTLQKETQLSNSKQEE 571
Cdd:PRK03918 351 EKRLEELEERHE------LYEEAKAKKEELERLKK-RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 572 TTENIEKLRTSLDSCQAC-----------------MKISCCSHDLKKEVDLLQHLQVsppvsglQKVVLDVLRHALSWLE 634
Cdd:PRK03918 424 LKKAIEELKKAKGKCPVCgrelteehrkelleeytAELKRIEKELKEIEEKERKLRK-------ELRELEKVLKKESELI 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 635 EVEQLLRDLGILPSSPNKDQVQQFSGNSAVF--TAGKAAGASGR----EGEAERGEARARGEAQSQNQAtdgREGGKALE 708
Cdd:PRK03918 497 KLKELAEQLKELEEKLKKYNLEELEKKAEEYekLKEKLIKLKGEikslKKELEKLEELKKKLAELEKKL---DELEEELA 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 709 EYITQERNRAKETLEEERKRMQELESllAQQKKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLEssiahEKR 788
Cdd:PRK03918 574 ELLKELEELGFESVEELEERLKELEP--FYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE-----ELR 646
|
....*....
gi 1370451826 789 KAKEALESE 797
Cdd:PRK03918 647 KELEELEKK 655
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
883-1121 |
4.87e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 883 SLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQrhgfEEEIMEYKEQIKQHAQTIVSLEEKLQK 962
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 963 VTQHHKKIEGEIATLKDN-----DPAPKEERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEIlsqqevIMKLRKDLTE 1037
Cdd:COG4942 88 LEKEIAELRAELEAQKEElaellRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQ------AEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1038 AHSRMSDLRGELNEKQKMELEQnvvlvQQQSKELSVLK-EKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQ 1116
Cdd:COG4942 162 LAALRAELEAERAELEALLAEL-----EEERAALEALKaERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
....*
gi 1370451826 1117 KPRKK 1121
Cdd:COG4942 237 AAAAE 241
|
|
| FHA_Par42-like |
cd22675 |
forkhead associated (FHA) domain found in Trypanosoma brucei Parvulin 42 (TbPar42) and similar ... |
37-117 |
5.01e-04 |
|
forkhead associated (FHA) domain found in Trypanosoma brucei Parvulin 42 (TbPar42) and similar proteins; TbPar42 is a nuclear protein that plays a key role in parasite cell proliferation. It exhibits an N-terminal forkhead associated (FHA)-domain and a peptidyl-prolyl-cis/trans-isomerase (PPIase) domain, both connected by a linker. Its PPIase domain adopts a parvulin fold and reflects structural elements of Pin1-type proteins but is catalytically inactive. Its FHA domain may be involved in the binding of phosphorylated target proteins. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438727 [Multi-domain] Cd Length: 113 Bit Score: 41.00 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 37 IGRHENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQnvAVKLIP---GDILRFGSAGLTYElVIE 113
Cdd:cd22675 33 FGRSPVCDYVLEHPSISSVHAVLVFHGEQKCFVLMDLGSTNGVKLNGKRIE--KGRPLPlpvGSVIQFGFSARKYK-VRK 109
|
....
gi 1370451826 114 NPPP 117
Cdd:cd22675 110 GPPS 113
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
674-1074 |
6.18e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 6.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 674 SGREGEAERGEARARGEAQS-QNQATDGREGGKALEEYITQERNRA----------KETLEEERKRMQELESLLAQQKKA 742
Cdd:PRK02224 320 EDRDEELRDRLEECRVAAQAhNEEAESLREDADDLEERAEELREEAaeleseleeaREAVEDRREEIEELEEEIEELRER 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 743 LA-------------KSITQEKNRVKEALEEEQTRVQELEERLARQKEVLES----------------SIAHEKRKAKEA 793
Cdd:PRK02224 400 FGdapvdlgnaedflEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphvETIEEDRERVEE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 794 LESE----KRKVQDLENHLTQQKEISESniayEKRkakeaMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDAL 869
Cdd:PRK02224 480 LEAEledlEEEVEEVEERLERAEDLVEA----EDR-----IERLEERREDLEELIAERRETIEEKRERAEELRERAAELE 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 870 AMVEETQKTKATESLKAESLALK---LNETLAELETTKTKMIMVEERLILQQKMVKALQDEQEsQRHGFEEEIMEYKEQI 946
Cdd:PRK02224 551 AEAEEKREAAAEAEEEAEEAREEvaeLNSKLAELKERIESLERIRTLLAAIADAEDEIERLRE-KREALAELNDERRERL 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 947 KQHAQTIVSLEEK-----LQKVTQHHKKIEGEIATLKDNDPAPKEERpqdplvapmtessakdmayehliDDLLA---AQ 1018
Cdd:PRK02224 630 AEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREER-----------------------DDLQAeigAV 686
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370451826 1019 KEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQQSKELSVL 1074
Cdd:PRK02224 687 ENELEELEELRERREALENRVEALEALYDEAEELESMYGDLRAELRQRNVETLERM 742
|
|
| FHA_DgcB-like |
cd22682 |
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ... |
28-103 |
7.03e-04 |
|
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB and similar proteins; DgcB is a GGDEF enzyme that produces cyclic-di-GMP in response to an unknown stimulus. It appends the C-terminal GGDEF enzymatic domain with an N-terminal forkhead-associated (FHA) domain that acts as a consensus phosphopeptide sensor. The GGDEF and sensory FHA domains form an asymmetrical dimer.
Pssm-ID: 438734 [Multi-domain] Cd Length: 96 Bit Score: 40.20 E-value: 7.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 28 FFVLNKSTTIGRHENSDLVLQSPDIDNHHALIEYNEAECSfvLQDFNSRNGTFVN--------ECHIQNvavklipGDIL 99
Cdd:cd22682 15 FPITESTIVIGRSVESQVQIDDDSVSRYHAKLAVNPSAVS--IIDLGSTNGTIVNgkkipklaSCDLQN-------GDQI 85
|
....
gi 1370451826 100 RFGS 103
Cdd:cd22682 86 KIGN 89
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
367-1109 |
7.05e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.19 E-value: 7.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 367 SSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQE-DAHRELREAQEKELKlcktQIQDMEKE 445
Cdd:TIGR00618 162 SKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMpDTYHERKQVLEKELK----HLREALQQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 446 MKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEdsrrklLQLQEMGNRESVIKINLERAVGQLEHFRSQVIKATYGRAK 525
Cdd:TIGR00618 238 TQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEE------LRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQR 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 526 PFRdkpvTDQQLIEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETteniEKLRTSLDSCQACMKISCCSHDLKKEVDL 605
Cdd:TIGR00618 312 IHT----ELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQE----IHIRDAHEVATSIREISCQQHTLTQHIHT 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 606 LQH-LQVSPPVSGLQKVVLDVLRHALSWLEEVEQLLRDLGILPSSPNKDQVQQFSgnsavfTAGKAAGASGREGEAERGE 684
Cdd:TIGR00618 384 LQQqKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQR------YAELCAAAITCTAQCEKLE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 685 ARARGEAQsqnQATDGREGGKALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNrvkeaLEEEQTR 764
Cdd:TIGR00618 458 KIHLQESA---QSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDN-----PGPLTRR 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 765 VQELEERLARQKEVLES--SIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIayekrkakeamekekKKVQDLEN 842
Cdd:TIGR00618 530 MQRGEQTYAQLETSEEDvyHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDI---------------PNLQNITV 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 843 RLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVK 922
Cdd:TIGR00618 595 RLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKEL 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 923 ALQDEQESQRHGFEEEIMEY-KEQIKQHAQTIVSLEEKLQKVTQHHKKIE----GEIATLKDNDPAP----KEERPQDPL 993
Cdd:TIGR00618 675 LASRQLALQKMQSEKEQLTYwKEMLAQCQTLLRELETHIEEYDREFNEIEnassSLGSDLAAREDALnqslKELMHQART 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 994 VAPMTESSAKDMAYEHLIDDLLAAQKEILSQQevIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQQSKELSV 1073
Cdd:TIGR00618 755 VLKARTEAHFNNNEEVTAALQTGAELSHLAAE--IQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQ 832
|
730 740 750
....*....|....*....|....*....|....*.
gi 1370451826 1074 LKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQ 1109
Cdd:TIGR00618 833 FLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQ 868
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
314-490 |
7.17e-04 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 42.81 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 314 KEIQSLKSQISALQKG------YSKVLCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEV 387
Cdd:pfam17078 3 KVIESLHDQIDALTKTnlqltvQSQNLLSKLEIAQQKESKFLENLASLKHENDNLSSMLNRKERRLKDLEDQLSELKNSY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 388 SHLKSQNKDKDHQLEALGSRCSVLKEELKQE--------DAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELrkscte 459
Cdd:pfam17078 83 EELTESNKQLKKRLENSSASETTLEAELERLqiqydalvDSQNEYKDHYQQEINTLQESLEDLKLENEKQLENY------ 156
|
170 180 190
....*....|....*....|....*....|..
gi 1370451826 460 qsvISRTLREKSKVEEKLQE-DSRRKLLQLQE 490
Cdd:pfam17078 157 ---QQRISSNDKDIDTKLDSyNNKFKNLDNIY 185
|
|
| FHA_RAD53-like_rpt1 |
cd22689 |
first forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ... |
3-82 |
9.36e-04 |
|
first forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine/threonine-protein kinase RAD53 and similar proteins; RAD53, also called CHEK2 homolog, or serine-protein kinase 1 (Spk1), is a nuclear protein kinase that phosphorylates proteins on serine, threonine, and tyrosine. It controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints and prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. It may be involved in the phosphorylation of RPH1. RAD53 contains two FHA domains. This model corresponds to the first one. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438741 [Multi-domain] Cd Length: 132 Bit Score: 40.72 E-value: 9.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 3 SLEPCRLFiYGKTERMKAYLKSAEGFFvlnkstTIGRHENSDLVLQSPDIDNHHALI---EYNEAECSFVLQDFNSrNGT 79
Cdd:cd22689 22 TQEPIRDL-SGDISQVLKEKRSIKKVW------TFGRHPACDYHLGNSRLSNKHFQIllgESDPSDGNVLLNDISS-NGT 93
|
...
gi 1370451826 80 FVN 82
Cdd:cd22689 94 WLN 96
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
365-508 |
9.65e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.92 E-value: 9.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 365 MVSSLQKDILAKDEQVQQLKEEVSHL-KSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQIQDME 443
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALkKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRY 484
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370451826 444 KEMKKLRAELRKSCTEQSVISRTLREKSKVEE--------------KLQEDSRRKLLQLqemgnrESVIKinlERAVGQ 508
Cdd:COG0542 485 GKIPELEKELAELEEELAELAPLLREEVTEEDiaevvsrwtgipvgKLLEGEREKLLNL------EEELH---ERVIGQ 554
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
273-585 |
9.72e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.86 E-value: 9.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 273 NLQNEVAELSQKVSETTTSRQNEKE----ISQKCQVLDEDIDAKQKEIQSLKSQISALQKGYSKVLCQtLSERNSE---- 344
Cdd:TIGR04523 229 QLKDNIEKKQQEINEKTTEISNTQTqlnqLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSE-ISDLNNQkeqd 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 345 -ITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEalgSRCSVLKEELKQEDAHRE 423
Cdd:TIGR04523 308 wNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELE---EKQNEIEKLKKENQSYKQ 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 424 LREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEdsrrkllQLQEMGNRESVIKINLE 503
Cdd:TIGR04523 385 EIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNS-------EIKDLTNQDSVKELIIK 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 504 RAVGQLEHFRSQVIKATYGRAKPFRDKPVTDQQLIEK---ITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLR 580
Cdd:TIGR04523 458 NLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKekeLKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKE 537
|
....*
gi 1370451826 581 TSLDS 585
Cdd:TIGR04523 538 SKISD 542
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
705-797 |
1.01e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 41.31 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 705 KALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQE----LEERLARQKEVLE 780
Cdd:COG0711 23 PPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEEakaeAEAEAERIIAQAE 102
|
90
....*....|....*..
gi 1370451826 781 SSIAHEKRKAKEALESE 797
Cdd:COG0711 103 AEIEQERAKALAELRAE 119
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
300-510 |
1.02e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 300 QKCQVLDEDIDAKQKEIQSLKSQISALQKgyskvLCQTLSERNSEITSLKNegenlkrdnaitsgmVSSLQKDILAKDEQ 379
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEA-----ELDALQERREALQRLAE---------------YSWDEIDVASAERE 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 380 VQQLKEEVSHLKSQNKDkdhqLEALGSRCSVLKEELkqeDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTE 459
Cdd:COG4913 670 IAELEAELERLDASSDD----LAALEEQLEELEAEL---EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1370451826 460 QSVISRTLREKsKVEEKLQEDSRRKLlqLQEMGNRESVIKINLERAVGQLE 510
Cdd:COG4913 743 ARLELRALLEE-RFAAALGDAVEREL--RENLEERIDALRARLNRAEEELE 790
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
411-970 |
1.36e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 411 LKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKscteqsvISRTLREKSKVEEKLQEDSRRKLLQLQE 490
Cdd:PRK03918 181 LEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEK-------LEKEVKELEELKEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 491 MGNRESVIK-------------INLERAVGQLEHFRSQviKATYGRAKPFRDKPVTDQQLIEKITQVTEDNINFQQKKWt 557
Cdd:PRK03918 254 KRKLEEKIReleerieelkkeiEELEEKVKELKELKEK--AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI- 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 558 lqKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRHALSWLEEVE 637
Cdd:PRK03918 331 --KELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEIS 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 638 QLLRDLGILPSSPNkdqvqqfSGNSAVFTAGKAAG---ASGRE-GEAERGEARARGEAQSQNQATDGREGGKALEEYITQ 713
Cdd:PRK03918 409 KITARIGELKKEIK-------ELKKAIEELKKAKGkcpVCGRElTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 714 ERNRAKETLEEER-KRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRkaKE 792
Cdd:PRK03918 482 LRELEKVLKKESElIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKK--LA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 793 ALESEKRKVQD-LENHLTQQKEISESNIayekrkakeamEKEKKKVQDLE------NRLTKQKEELELKEQKEDVLNNKL 865
Cdd:PRK03918 560 ELEKKLDELEEeLAELLKELEELGFESV-----------EELEERLKELEpfyneyLELKDAEKELEREEKELKKLEEEL 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 866 SDALAMVEETQktKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFeEEIMEYKEQ 945
Cdd:PRK03918 629 DKAFEELAETE--KRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTL-EKLKEELEE 705
|
570 580
....*....|....*....|....*
gi 1370451826 946 IKQHAQTIVSLEEKLQKVTQHHKKI 970
Cdd:PRK03918 706 REKAKKELEKLEKALERVEELREKV 730
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
287-509 |
1.56e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 42.44 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 287 ETTTSRQNEKEISQKCQVLdedIDAKQKEIQSLKSQISA----LQKGYSKVLCQTLSERN---SEITSLKNEGENLKRDN 359
Cdd:pfam09787 1 NLESAKQELADYKQKAARI---LQSKEKLIASLKEGSGVegldSSTALTLELEELRQERDllrEEIQKLRGQIQQLRTEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 360 AitsGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRelreaqekelklcKTQI 439
Cdd:pfam09787 78 Q---ELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATL-------------QSRI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370451826 440 QDMEKEMKKLRAELR---KSCTEQSVISRTLREkskveekLQEDSRRKLLQLQEMGNRESVIKINLERAVGQL 509
Cdd:pfam09787 142 KDREAEIEKLRNQLTsksQSSSSQSELENRLHQ-------LTETLIQKQTMLEALSTEKNSLVLQLERMEQQI 207
|
|
| FHA_PPP1R8 |
cd22674 |
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ... |
33-110 |
1.60e-03 |
|
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 (PPP1R8) and similar proteins; PPP1R8, also called nuclear inhibitor of protein phosphatase 1 (NIPP-1), is an inhibitor subunit of the major nuclear protein phosphatase-1 (PP-1). It has RNA-binding activity but does not cleave RNA and may target PP-1 to RNA-associated substrates. It may also be involved in pre-mRNA splicing and binds DNA and might act as a transcriptional repressor. PPP1R8 seems to be required for cell proliferation. PPP1R8 contains an FHA domain that mediates interactions with threonine-phosphorylated maternal embryonic leucine zipper kinase (MELK). The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438726 [Multi-domain] Cd Length: 108 Bit Score: 39.56 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 33 KSTTIGR-HENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFGSAGLTYEL 110
Cdd:cd22674 27 KYYLFGRnSDVCDFVLDHPSCSRVHAALVYHKHLNRVFLIDLGSTHGTFVGGIRLEpHKPQQLPIDSTLRFGASTRRYIL 106
|
|
| FHA_Ct664-like |
cd22696 |
forkhead associated (FHA) domain found in Chlamydia trachomatis Ct664 protein and similar ... |
25-103 |
1.77e-03 |
|
forkhead associated (FHA) domain found in Chlamydia trachomatis Ct664 protein and similar proteins; This subfamily corresponds to a group of uncharacterized FHA domain-containing proteins which show high sequence similarity with Chlamydia trachomatis Ct664 protein. Ct664 situates within the type III secretion system cluster that also encodes an STPK (CT673 in C. trachomatis), suggesting a role of CT664 in the chlamydial type III secretion system by mediating phosphorylation-dependent protein-protein interactions. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438748 [Multi-domain] Cd Length: 97 Bit Score: 39.01 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 25 AEGFFVLNKSTTIGRHEN-SDLVLQSPDIDNHHALIEYNEAECSFVlQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGS 103
Cdd:cd22696 13 AEFFLESGKTYFIGKDPTvCDIVLQDPSISRQHARLSIDQDNRVFI-EDLSSKNGVLVNGKPIEG-KEEISGSDVISLGT 90
|
|
| FHA_EmbR-like |
cd22669 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis transcriptional ... |
22-109 |
2.05e-03 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis transcriptional regulatory protein EmbR and similar proteins; EmbR is a transcriptional regulator of the embCAB operon encoding cell wall arabinosyltransferases (EmbC, -A, and -B), and is phosphorylated by the cognate mycobacterial serine/threonine protein kinase PknH. It interacts with RNA polymerase and possesses a phosphorylation-dependent ATPase activity. EmbR contains a regulatory C-terminal forkhead-associated (FHA) domain, which mediates binding to a threonine-phosphorylated site in PknH. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438721 [Multi-domain] Cd Length: 89 Bit Score: 38.94 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 22 LKSAEGFFVLNKSTTIGRHENSDLVLQSPDIDNHHALIEYNEAECSfvLQDFNSRNGTFVNECHIQNVAVkLIPGDILRF 101
Cdd:cd22669 5 IASGRGYPLQAAATRIGRLHDNDIVLDSANVSRHHAVIVDTGTNYV--INDLRSSNGVHVQHERIRSAVT-LNDGDHIRI 81
|
....*...
gi 1370451826 102 GSAGLTYE 109
Cdd:cd22669 82 CDHEFTFQ 89
|
|
| FHA_Rv1747-like_rpt2 |
cd22737 |
second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
37-109 |
2.08e-03 |
|
second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the second FHA domain, which has a circularly permuted FHA domain fold with a conserved pThr-binding interface.
Pssm-ID: 439356 [Multi-domain] Cd Length: 93 Bit Score: 39.01 E-value: 2.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370451826 37 IGRHENSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQnvAVKLIPGDILRFGSAGLTYE 109
Cdd:cd22737 25 IGRASDNDIVIPEGSVSRHHATLVPTPG--GTQIRDLRSTNGTFVNGLRVD--AALLHDGDVVTIGDIDFVFE 93
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
256-512 |
2.11e-03 |
|
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: 42.90 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 256 RLSDYEIESKYKDVIIANLQNEVAELSQKVSETTtsRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQ---KGYSK 332
Cdd:pfam12128 259 RLSHLHFGYKSDETLIASRQEERQETSAELNQLL--RTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEdqhGAFLD 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 333 VLCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQV-QQLKEEVSHLKS----QNKDKDHQLEA---- 403
Cdd:pfam12128 337 ADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIkEQNNRDIAGIKDklakIREARDRQLAVaedd 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 404 LGSRCSVLKEELKQedAHRELREAQEK------ELKL----------CKTQIQDMEKEMKKLRAELRKSCTEQSVISRTL 467
Cdd:pfam12128 417 LQALESELREQLEA--GKLEFNEEEYRlksrlgELKLrlnqatatpeLLLQLENFDERIERAREEQEAANAEVERLQSEL 494
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1370451826 468 REKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEHF 512
Cdd:pfam12128 495 RQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHF 539
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
664-824 |
2.42e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 664 VFTAGKAAGASGREGEAERGEARARGEAQSQNQATDGREGGKALEEY----------------ITQERNRAKETLEEERK 727
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLaalerriaalarriraLEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 728 RMQELESLLAQQKKALA----------------------------------KSITQEKNRVKEALEEEQTRVQELEERLA 773
Cdd:COG4942 91 EIAELRAELEAQKEELAellralyrlgrqpplalllspedfldavrrlqylKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1370451826 774 RQKEVLESSIAhEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKR 824
Cdd:COG4942 171 AERAELEALLA-ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
708-1122 |
2.48e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 708 EEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNR--VKEALEEEQTRVQELEERL--ARQKEVLESSI 783
Cdd:PRK02224 229 REQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREReeLAEEVRDLRERLEELEEERddLLAEAGLDDAD 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 784 AHEKRKAKEALESEKRKVQD-LENHLTQQKEISESNIAYEKRKAKEAMEKEKKKVQ--DLENRLTKQKEELELKEQKEDV 860
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDrLEECRVAAQAHNEEAESLREDADDLEERAEELREEaaELESELEEAREAVEDRREEIEE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 861 LNNKLSDALAMVE--ETQKTKATESLkaESLALKLNETLAELETTKTKMIMVEERLilqqKMVKALQDE-------QESQ 931
Cdd:PRK02224 389 LEEEIEELRERFGdaPVDLGNAEDFL--EELREERDELREREAELEATLRTARERV----EEAEALLEAgkcpecgQPVE 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 932 RHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHH------KKIEGEIATLKDNdpapkeerpqdplvapmtessakdm 1005
Cdd:PRK02224 463 GSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLeraedlVEAEDRIERLEER------------------------- 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1006 ayEHLIDDLLAAQKEIL-SQQEVIMKLRKDLTEAHSRMSDLRgELNEKQKMELEQNVVLVQQQSKELSVLKE------KM 1078
Cdd:PRK02224 518 --REDLEELIAERRETIeEKRERAEELRERAAELEAEAEEKR-EAAAEAEEEAEEAREEVAELNSKLAELKEriesleRI 594
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1370451826 1079 AQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKT 1122
Cdd:PRK02224 595 RTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRE 638
|
|
| FHA_GarA-like |
cd22720 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis glycogen accumulation ... |
29-108 |
2.53e-03 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis glycogen accumulation regulator GarA and similar proteins; GarA is an FHA domain-containing protein involved in the regulation of glutamate metabolism. It acts as a phosphorylation-dependent ON/OFF molecular switch that modulates the activities of KGD, GDH and GltB. Its FHA domain has dual specificity. It binds to both phosphorylated upstream partners, such as the kinases PknB and PknG, and nonphosphorylated downstream partners, such as the 2-oxoglutarate decarboxylase KGD. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438772 [Multi-domain] Cd Length: 100 Bit Score: 38.83 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 29 FVLNKSTT-IGRHENSDLVLQSPDIDNHHAliEYNEAECSFVLQDFNSRNGTFVNECHIqNVAVkLIPGDILRFGSAGLT 107
Cdd:cd22720 19 FLLDQAITsAGRHPDSDIFLDDVTVSRRHA--EFRLENNEFNVVDVGSLNGTYVNREPV-DSAV-LANGDEVQIGKFRLV 94
|
.
gi 1370451826 108 Y 108
Cdd:cd22720 95 F 95
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
353-1130 |
2.55e-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: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 353 ENLKRDNAITSGMVSSLQKDILAKDE--QVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEk 430
Cdd:pfam15921 74 EHIERVLEEYSHQVKDLQRRLNESNElhEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVH- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 431 ELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVIsrtLREKSKVEEKLQEDSRRKLlqlQEMGNRESVIKINLERAVGQLe 510
Cdd:pfam15921 153 ELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGV---LQEIRSILVDFEEASGKKI---YEHDSMSTMHFRSLGSAISKI- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 511 hFRSQVIKATYGRAKPFrdkPVTDQqlIEKITQVTEDNINFQQKKWTLQKETQLSNSKQEET--TENIEKLRTSLDSCQA 588
Cdd:pfam15921 226 -LRELDTEISYLKGRIF---PVEDQ--LEALKSESQNKIELLLQQHQDRIEQLISEHEVEITglTEKASSARSQANSIQS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 589 CMKISCCSHDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRHALSWLEEVEQ--LLRDLGILPSSPNKDQVQQFSGNSAVFT 666
Cdd:pfam15921 300 QLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKqlVLANSELTEARTERDQFSQESGNLDDQL 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 667 AGKAAGASGREGEAERgearargeAQSQNQATDGREGGKAleeyITQERNRAKetLEEERKRMQELESLLAQQKKALAKS 746
Cdd:pfam15921 380 QKLLADLHKREKELSL--------EKEQNKRLWDRDTGNS----ITIDHLRRE--LDDRNMEVQRLEALLKAMKSECQGQ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 747 ITQEKNRVkEALEEEQTRVQELEERLARQKEVLESsIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAY----- 821
Cdd:pfam15921 446 MERQMAAI-QGKNESLEKVSSLTAQLESTKEMLRK-VVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEitklr 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 822 ----EKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETL 897
Cdd:pfam15921 524 srvdLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRR 603
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 898 AELETTK-------TKMIMVEERLI-LQQKMVKALQDEQESQR--HGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHH 967
Cdd:pfam15921 604 LELQEFKilkdkkdAKIRELEARVSdLELEKVKLVNAGSERLRavKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNF 683
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 968 KKIEGEIATlKDNDPAPKEERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLrg 1047
Cdd:pfam15921 684 RNKSEEMET-TTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNA-- 760
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1048 elnEKQKMELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQTCDT 1127
Cdd:pfam15921 761 ---NKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRL 837
|
...
gi 1370451826 1128 SVQ 1130
Cdd:pfam15921 838 KLQ 840
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
669-964 |
2.71e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.16 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 669 KAAGASGREGEAERGEARARGEAQSQNQATDGREGGKALEEYITQErnraKETLEEERKRMQELESLLAQQKKalakSIT 748
Cdd:pfam02029 51 KPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDPTIADE----KESVAERKENNEEEENSSWEKEE----KRD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 749 QEKNRVKEalEEEQTRVQELEERLARQKEV-LESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEisESNIAYE-KRKA 826
Cdd:pfam02029 123 SRLGRYKE--EETEIREKEYQENKWSTEVRqAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKK--EKKVKYEsKVFL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 827 KEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTK-------ATESLKAESLALKLNETLAE 899
Cdd:pfam02029 199 DQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEelrrrrqEKESEEFEKLRQKQQEAELE 278
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370451826 900 LETTKTKMimVEERLILQQKMVKALQDEQESQRHGfEEEIMEYKEQIKQHAQTIVsleEKLQKVT 964
Cdd:pfam02029 279 LEELKKKR--EERRKLLEEEEQRRKQEEAERKLRE-EEEKRRMKEEIERRRAEAA---EKRQKLP 337
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
705-1107 |
2.84e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 705 KALEEYITQERNRAKET------LEEERKRMQELESLLAQQKK--ALAKSITQEKNRVKEALEEEQTRVQELEERLARQK 776
Cdd:PRK03918 255 RKLEEKIRELEERIEELkkeieeLEEKVKELKELKEKAEEYIKlsEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 777 EvlESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQ 856
Cdd:PRK03918 335 E--KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITA 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 857 KEDVLNNKLSDALAMVEETQKTKA---------TESLKAESLA---LKLNETLAELETTKT-------------KMIMVE 911
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKKAKGkcpvcgrelTEEHRKELLEeytAELKRIEKELKEIEEkerklrkelreleKVLKKE 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 912 ERLILQQKMVKALQD-EQESQRHGFEEEIMEYKE-----------------------QIKQHAQTIVSLEEKLQKVTQHH 967
Cdd:PRK03918 493 SELIKLKELAEQLKElEEKLKKYNLEELEKKAEEyeklkekliklkgeikslkkeleKLEELKKKLAELEKKLDELEEEL 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 968 KKIEGEIATLKDNDPAPKEERPQDPLVAPMTESSAKDMAyehliDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRG 1047
Cdd:PRK03918 573 AELLKELEELGFESVEELEERLKELEPFYNEYLELKDAE-----KELEREEKELKKLEEELDKAFEELAETEKRLEELRK 647
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370451826 1048 ELNEKQKM----ELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKALEEALRASQEKHR 1107
Cdd:PRK03918 648 ELEELEKKyseeEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKK 711
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
243-501 |
2.85e-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: 42.12 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 243 KDEIILLLGKEVSRLSDyeiESKYKDVIIANLQNEVAELSQKVSETTTSrqnekeisqkCQVLDEDIDAKQKEIQSLKSQ 322
Cdd:pfam10174 392 KERKINVLQKKIENLQE---QLRDKDKQLAGLKERVKSLQTDSSNTDTA----------LTTLEEALSEKERIIERLKEQ 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 323 ISALQKgyskvlcqtlsERNSEITSLKNEGENLKRDnaitsgmVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLE 402
Cdd:pfam10174 459 REREDR-----------ERLEELESLKKENKDLKEK-------VSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLK 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 403 ALGSRCSVLKEE-LKQEDAHRELREAQEKELKLCK--TQIQDMEKEMKKLRAELRKSCTEQSVISRTLR----EKSKVEE 475
Cdd:pfam10174 521 SLEIAVEQKKEEcSKLENQLKKAHNAEEAVRTNPEinDRIRLLEQEVARYKEESGKAQAEVERLLGILRevenEKNDKDK 600
|
250 260
....*....|....*....|....*.
gi 1370451826 476 KLQEDSRRKLLQLQEMGNRESVIKIN 501
Cdd:pfam10174 601 KIAELESLTLRQMKEQNKKVANIKHG 626
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
261-456 |
2.98e-03 |
|
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: 41.93 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 261 EIESKYKDviIANLQNEVAELSQKVSETTtsrQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQKGYSKVLCQT-LS 339
Cdd:TIGR04523 490 ELKSKEKE--LKKLNEEKKELEEKVKDLT---KKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKeID 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 340 ERNSEITSLKNEGENLKRDN-------AITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLK 412
Cdd:TIGR04523 565 EKNKEIEELKQTQKSLKKKQeekqeliDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLK 644
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1370451826 413 EELKQ----EDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKS 456
Cdd:TIGR04523 645 QEVKQiketIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLH 692
|
|
| FlgN |
pfam05130 |
FlgN protein; This family includes the FlgN protein and export chaperone involved in flagellar ... |
719-814 |
3.41e-03 |
|
FlgN protein; This family includes the FlgN protein and export chaperone involved in flagellar synthesis.
Pssm-ID: 428323 [Multi-domain] Cd Length: 140 Bit Score: 39.27 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 719 KETLEEERKRMQELESLLAQQKKALAK-------SITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAK 791
Cdd:pfam05130 4 IELLEEELELLEELLELLEEEQEALKAgdiealeELTEEKQELLQKLAQLEKERRELLAELGLSPEEATLSELLAKEEED 83
|
90 100
....*....|....*....|...
gi 1370451826 792 EALESEKRKVQDLENHLTQQKEI 814
Cdd:pfam05130 84 PELRELWQELLELLERLKELNEL 106
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
428-809 |
3.69e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 428 QEKELKLCKTQiQDMEKeMKKLRAELRKSCteqsvisRTLREKSKVEEKLQEdSRRKLLQLQEmgnreSVIKINLERAVG 507
Cdd:TIGR02168 175 KETERKLERTR-ENLDR-LEDILNELERQL-------KSLERQAEKAERYKE-LKAELRELEL-----ALLVLRLEELRE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 508 QLEHFRSQVIKATYGRAKPFRDKPVTDQQLIEKITQVTEDninfQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQ 587
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL----EEEIEELQKELYALANEISRLEQQKQILRERLANLE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 588 ACmkisccshdlkkevdllqhlqvsppvsglQKVVLDVLRHALSWLEEVEQLLRDLgilpsspnKDQVQQFSGNSAVFTA 667
Cdd:TIGR02168 316 RQ-----------------------------LEELEAQLEELESKLDELAEELAEL--------EEKLEELKEELESLEA 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 668 gKAAGASGREGEAERGEARARGEAQSQNQATDGREGGKALEEyITQERNRA-KETLEEERKRM-QELESLLAQQKKALAK 745
Cdd:TIGR02168 359 -ELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN-NEIERLEArLERLEDRRERLqQEIEELLKKLEEAELK 436
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370451826 746 SITQEKNRVKEALEEEQTRVQELEERLARQKEvlessiahEKRKAKEALESEKRKVQDLENHLT 809
Cdd:TIGR02168 437 ELQAELEELEEELEELQEELERLEEALEELRE--------ELEEAEQALDAAERELAQLQARLD 492
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
274-497 |
3.95e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 274 LQNEVAELSQKVSETTTS----RQNEKEISqkcqvLDEDIDAKQKEIQSLKSQISALQkgyskvlcqtlsernSEITSLK 349
Cdd:COG3206 180 LEEQLPELRKELEEAEAAleefRQKNGLVD-----LSEEAKLLLQQLSELESQLAEAR---------------AELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 350 NEGENLKRDNAITSGMVSSLQKD--ILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDahRELREA 427
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEA--QRILAS 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370451826 428 QEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQE-DSRRKLLQLQEMGNRESV 497
Cdd:COG3206 318 LEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESlLQRLEEARLAEALTVGNV 388
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
32-102 |
4.09e-03 |
|
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is a telomere-associated E3 ubiquitin-protein ligase that plays an important role in DNA double-strand break (DSB) repair via histone ubiquitination. It is localized in the nucleus and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3), but not with other E2s (UbcH5, UbcH7, UbcH10, hCdc34, and hBendless). It recruits UBC13 for lysine 63-based self polyubiquitylation. Its deficiency causes neuronal pathology and cognitive decline, and its loss results in neuron degeneration. RNF8, together with RNF168, catalyzes a series of ubiquitylation events on substrates such as H2A and H2AX, with the H2AK13/15 ubiquitylation being particularly important for recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of DSBs. Specially, RNF8 mediates the ubiquitination of gammaH2AX, and recruits 53BP1 and BRCA1 to DNA damage sites which promotes DNA damage response (DDR) and inhibits chromosomal instability. Moreover, RNF8 interacts with retinoid X receptor alpha (RXR alpha) and enhances its transcription-stimulating activity. It also regulates the rate of exit from mitosis and cytokinesis. RNF8 contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438715 [Multi-domain] Cd Length: 110 Bit Score: 38.49 E-value: 4.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370451826 32 NKSTTIGRHENS--DLVLQ-SPDIDNHHALIEYNeAECSFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFG 102
Cdd:cd22663 20 GKEVTVGRGLGVtyQLVSTcPLMISRNHCVLKKN-DEGQWTIKDNKSLNGVWVNGERIEpLKPYPLNEGDLIQLG 93
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
704-797 |
4.21e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 39.22 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 704 GKALEE---YITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNRV----KEALEEEQTRVQELEERLARQk 776
Cdd:PRK07353 31 GKVVEEredYIRTNRAEAKERLAEAEKLEAQYEQQLASARKQAQAVIAEAEAEAdklaAEALAEAQAEAQASKEKARRE- 109
|
90 100
....*....|....*....|.
gi 1370451826 777 evlessIAHEKRKAKEALESE 797
Cdd:PRK07353 110 ------IEQQKQAALAQLEQQ 124
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
677-1181 |
4.38e-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: 41.49 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 677 EGEAERGEARARGEAQSQNQATDGREGGKALEEYITQErnraketLEEERKRMQELESLLAQQKKALaksitQEKNRVKE 756
Cdd:TIGR00618 193 HGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKH-------LREALQQTQQSHAYLTQKREAQ-----EEQLKKQQ 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 757 ALEEEQTRVQELEERLARQkEVLESSIAHEKRKAKEALESE---KRKVQDLENHLTQQKEISESNIAYEKRKAKEAMEKE 833
Cdd:TIGR00618 261 LLKQLRARIEELRAQEAVL-EETQERINRARKAAPLAAHIKavtQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSS 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 834 KKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEER 913
Cdd:TIGR00618 340 IEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAF 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 914 LILQQKMVKALQDEQESQRHG----------FEEEIMEYKEQIKQhAQTIVSLEEKLQKVTQHH------KKIEGEIATL 977
Cdd:TIGR00618 420 RDLQGQLAHAKKQQELQQRYAelcaaaitctAQCEKLEKIHLQES-AQSLKEREQQLQTKEQIHlqetrkKAVVLARLLE 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 978 KDNDPAPKEERPQDPLVApMTESSAKdmayEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLrgelnEKQKMEL 1057
Cdd:TIGR00618 499 LQEEPCPLCGSCIHPNPA-RQDIDNP----GPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASL-----KEQMQEI 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1058 EQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTE-KEQKPRKKTQTCDTSVQIEPVHT 1136
Cdd:TIGR00618 569 QQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEqDLQDVRLHLQQCSQELALKLTAL 648
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1370451826 1137 EAFSSSQEQQSFSDLGVRCKGSRHEEVIQRQKKaLSELRARIKEL 1181
Cdd:TIGR00618 649 HALQLTLTQERVREHALSIRVLPKELLASRQLA-LQKMQSEKEQL 692
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1291-1421 |
4.81e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1291 QEREKVNQLRQ---RDLDLVFDKITQLKNQLGRKEELLrgyEKDVEQLRRSKVSIEMYQSQVAKLEDDIYKEAEE-KALL 1366
Cdd:PRK12704 61 EAKEEIHKLRNefeKELRERRNELQKLEKRLLQKEENL---DRKLELLEKREEELEKKEKELEQKQQELEKKEEElEELI 137
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370451826 1367 KEALERMEH--QLCQEKRINRAIRQQKVGTRKASLKMDQEREMLRKETSSKSSQSLL 1421
Cdd:PRK12704 138 EEQLQELERisGLTAEEAKEILLEKVEEEARHEAAVLIKEIEEEAKEEADKKAKEIL 194
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
677-979 |
5.11e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.03 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 677 EGEAERGEARARGEAQSQNQATDGREGGKALEEY---ITQERNRAKETLEEERKRMQELESLLAQQK--KALAKSITQEK 751
Cdd:pfam07888 38 ECLQERAELLQAQEAANRQREKEKERYKRDREQWerqRRELESRVAELKEELRQSREKHEELEEKYKelSASSEELSEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 752 NRVKEALEEEQTRVQELEE---RLARQKEVLESSIAHEKRKAKEAL------ESEKRKVQdLENHLTQQKEISESNIAYE 822
Cdd:pfam07888 118 DALLAQRAAHEARIRELEEdikTLTQRVLERETELERMKERAKKAGaqrkeeEAERKQLQ-AKLQQTEEELRSLSKEFQE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 823 KRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELET 902
Cdd:pfam07888 197 LRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQ 276
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370451826 903 TKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKD 979
Cdd:pfam07888 277 ARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKD 353
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
236-459 |
5.21e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 236 EDLAQQDKDEIILLLGK---EVSRLSDY-EIESKYKDVIIANLQnevaelSQKVSETTTSRQNEKEISQKcqvLDEDIDA 311
Cdd:PRK05771 34 EDLKEELSNERLRKLRSlltKLSEALDKlRSYLPKLNPLREEKK------KVSVKSLEELIKDVEEELEK---IEKEIKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 312 KQKEIQSLKSQISALQKgyskvlcqtlseRNSEITSLKNEGENLK--RDNAITSGMVSSLQKDIlaKDEQVQQLKEEVSH 389
Cdd:PRK05771 105 LEEEISELENEIKELEQ------------EIERLEPWGNFDLDLSllLGFKYVSVFVGTVPEDK--LEELKLESDVENVE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 390 LKSQNKDKDhqlealgsRCSVLKEELKQEDAHRELREAQEKELKL------------CKTQIQDMEKEMKKLRAELRKSC 457
Cdd:PRK05771 171 YISTDKGYV--------YVVVVVLKELSDEVEEELKKLGFERLELeeegtpselireIKEELEEIEKERESLLEELKELA 242
|
..
gi 1370451826 458 TE 459
Cdd:PRK05771 243 KK 244
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
236-489 |
6.31e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.04 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 236 EDLAQ--QDKDEIILLLGK-EVSRLSDYEIESKYKDviiaNLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAK 312
Cdd:PLN02939 131 EDLVGmiQNAEKNILLLNQaRLQALEDLEKILTEKE----ALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 313 QKEIqslkSQISALQKGYSKVLCQTLSERNSEITSLKNEGENLKrdnaitsGMVSSLQKdilaKDEQVQQLKEEVSHLKS 392
Cdd:PLN02939 207 RNEL----LIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLK-------AELIEVAE----TEERVFKLEKERSLLDA 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 393 QNKDKDHQLeaLGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQI----------QDMEKEMKKLRAELRKSCT--EQ 460
Cdd:PLN02939 272 SLRELESKF--IVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVekaalvldqnQDLRDKVDKLEASLKEANVskFS 349
|
250 260 270
....*....|....*....|....*....|
gi 1370451826 461 SVISRTLREKSK-VEEKLQEDSRRKLLQLQ 489
Cdd:PLN02939 350 SYKVELLQQKLKlLEERLQASDHEIHSYIQ 379
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
679-814 |
6.39e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.85 E-value: 6.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 679 EAERGEARARGEAQSQNQATDGReggkaLEEYITQERNRAKETLEEERKRMQELESLLAQQKKAL---AKSITQEKNRVK 755
Cdd:PRK12705 34 EAERILQEAQKEAEEKLEAALLE-----AKELLLRERNQQRQEARREREELQREEERLVQKEEQLdarAEKLDNLENQLE 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370451826 756 EALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALesekrkVQDLENHLTQQKEI 814
Cdd:PRK12705 109 EREKALSARELELEELEKQLDNELYRVAGLTPEQARKLL------LKLLDAELEEEKAQ 161
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
274-481 |
6.56e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 6.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 274 LQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQKgyskvlcqTLSERNSEITSLKNEGE 353
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA--------EIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 354 NLKRDNAITSGMVSSLQKDILAKD--EQVQQLkEEVSHLKSQNKDKDHQLEALGSRCSVLKEEL-KQEDAHRELREAQEK 430
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLLGSESfsDFLDRL-SALSKIADADADLLEELKADKAELEAKKAELeAKLAELEALKAELEA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1370451826 431 ELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKLQEDS 481
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
302-414 |
6.57e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 6.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 302 CQVLDEDIDAKQKEIQSLKSQISALQKGYSKVLC--QTLSERNSEITSLKNEGENLKRDnaitsgmVSSLQKDILAKDEQ 379
Cdd:PHA02562 287 CPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTaiDELEEIMDEFNEQSKKLLELKNK-------ISTNKQSLITLVDK 359
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1370451826 380 VQQLKEEVSHLKSQNKDKD-------HQLEALGSRCSVLKEE 414
Cdd:PHA02562 360 AKKVKAAIEELQAEFVDNAeelaklqDELDKIVKTKSELVKE 401
|
|
| FHA_CHK2 |
cd22666 |
forkhead associated (FHA) domain found in checkpoint kinase 2 (Chk2) and similar proteins; ... |
27-82 |
6.67e-03 |
|
forkhead associated (FHA) domain found in checkpoint kinase 2 (Chk2) and similar proteins; Chk2, also called Hucds1, Cds1 homolog, or serine/threonine-protein kinase Chk2, plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438718 [Multi-domain] Cd Length: 112 Bit Score: 37.99 E-value: 6.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370451826 27 GFFVL---NKSTTIGRHENSDLVLQSPDIDNH---------HALI--EYNEAECSFV-LQDFnSRNGTFVN 82
Cdd:cd22666 10 GFSSLdlvKDEYTFGRDKSCDYCFDSPALKKTsyyrtyskkHFRIfrEKGSKNTYPVfLEDH-SSNGTFVN 79
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
376-455 |
6.87e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 376 KDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRK 455
Cdd:COG2433 411 EEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREIERLERELEEERERIEE 490
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
255-477 |
7.21e-03 |
|
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: 40.77 E-value: 7.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 255 SRLSDYEIESKYKDVIIANLQNEVAELS---QKVSETTTSRQNE-KEISQKCQVLDEDIDAKQKEIQSLKSQISALQKGY 330
Cdd:TIGR04523 398 SKIQNQEKLNQQKDEQIKKLQQEKELLEkeiERLKETIIKNNSEiKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSI 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 331 SKVLcQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALgsrcsv 410
Cdd:TIGR04523 478 NKIK-QNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKD------ 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 411 lKEELKQEDAHRELREAQEKELKLCKTQ-------------IQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKVEEKL 477
Cdd:TIGR04523 551 -DFELKKENLEKEIDEKNKEIEELKQTQkslkkkqeekqelIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKL 629
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
261-585 |
7.93e-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: 40.81 E-value: 7.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 261 EIESKYKDVIiANLQNEVAELsQKVSETTTSRQNEKEISQKCQVLDEDIDAKQ---KEIQSLKSQISALQKGYSkvlcqT 337
Cdd:TIGR01612 1136 EIKKKSENYI-DEIKAQINDL-EDVADKAISNDDPEEIEKKIENIVTKIDKKKniyDEIKKLLNEIAEIEKDKT-----S 1208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 338 LSE-RNSEITSLKNEG----ENLKRDNAITSGMVSSLQKDILAKDEqVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLK 412
Cdd:TIGR01612 1209 LEEvKGINLSYGKNLGklflEKIDEEKKKSEHMIKAMEAYIEDLDE-IKEKSPEIENEMGIEMDIKAEMETFNISHDDDK 1287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 413 EELKQEDAHRE-LREAQEKELKLC-----KTQIQDMEKEMKKLRAELRKSCTEQSvisrtlrekskveeklqedsrrklL 486
Cdd:TIGR01612 1288 DHHIISKKHDEnISDIREKSLKIIedfseESDINDIKKELQKNLLDAQKHNSDIN------------------------L 1343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 487 QLQEMGNRESVIKIN-LERAVGQLEHFRSQVIKATygraKPFRDKPVTDQQLIEKItqvtEDNINFQQKKWTLqkETQLS 565
Cdd:TIGR01612 1344 YLNEIANIYNILKLNkIKKIIDEVKEYTKEIEENN----KNIKDELDKSEKLIKKI----KDDINLEECKSKI--ESTLD 1413
|
330 340
....*....|....*....|
gi 1370451826 566 NSKQEETTENIEKLRTSLDS 585
Cdd:TIGR01612 1414 DKDIDECIKKIKELKNHILS 1433
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
676-1107 |
8.20e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 8.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 676 REGEAERGEARAR-GEAQSQNQATDGREGGKALEEYITQERNRAKE------TLEEERKRMQELESLLAQQKKALAKSIT 748
Cdd:COG4717 105 EELEAELEELREElEKLEKLLQLLPLYQELEALEAELAELPERLEEleerleELRELEEELEELEAELAELQEELEELLE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 749 QEKNRVKEALEEEQTRVQELEERLARQKEVLEssiahEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKE 828
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELE-----EAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 829 AMEKEKKKVQDLENRLTKQKEELE-LKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKM 907
Cdd:COG4717 260 ALLGLGGSLLSLILTIAGVLFLVLgLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEEL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 908 IMVEERLI-LQQKMVKALQDEQESQRHGFEEEIMEYKEQIKqhAQTIVSLEEKLQKVtQHHKKIEGEIATLKDndpapke 986
Cdd:COG4717 340 LELLDRIEeLQELLREAEELEEELQLEELEQEIAALLAEAG--VEDEEELRAALEQA-EEYQELKEELEELEE------- 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 987 erpqdplvapMTESSAKDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNekqkmELEQNVVLVQQ 1066
Cdd:COG4717 410 ----------QLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELE-----QLEEDGELAEL 474
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1370451826 1067 QsKELSVLKEKMAQMsslvEKKDRELKALEEALRASQEKHR 1107
Cdd:COG4717 475 L-QELEELKAELREL----AEEWAALKLALELLEEAREEYR 510
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
715-797 |
8.64e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 38.19 E-value: 8.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 715 RNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQEL----EERLARQKEVLESSIAHEKRKA 790
Cdd:cd06503 32 EEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKIKEEIlaeaKEEAERILEQAKAEIEQEKEKA 111
|
....*..
gi 1370451826 791 KEALESE 797
Cdd:cd06503 112 LAELRKE 118
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
369-511 |
8.75e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 369 LQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEAL--------GSRCSVLKEELKQEDAHRELREAQEKEL-KLCKT-- 437
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELeaqirgngGDRLEQLEREIERLERELEERERRRARLeALLAAlg 372
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370451826 438 -QIQDMEKEMKKLRAELRKSCT----EQSVISRTLREKSKVEEKLQEDSRRKLLQLQEMGNRESVIKINLERAVGQLEH 511
Cdd:COG4913 373 lPLPASAEEFAALRAEAAALLEaleeELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAE 451
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
925-1119 |
8.91e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 40.40 E-value: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 925 QDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKdndpAPKEERPQDPLVapmtessaKD 1004
Cdd:pfam05667 323 VETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELK----EQNEELEKQYKV--------KK 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 1005 MAYEHLIDDllaaqkeilsqQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQQSKELSVLKEKMAQMSSL 1084
Cdd:pfam05667 391 KTLDLLPDA-----------EENIAKLQALVDASAQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDESQRKLEEIKEL 459
|
170 180 190
....*....|....*....|....*....|....*
gi 1370451826 1085 vekkDRELKALEEALRASQEKHRlQLNTEKEQKPR 1119
Cdd:pfam05667 460 ----REKIKEVAEEAKQKEELYK-QLVAEYERLPK 489
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
271-561 |
8.97e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 40.61 E-value: 8.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 271 IANLQNEVAELSQKVSET--TTSRQNEKEISQKCQVLDEDIDAKQKEI---QSLKSQISALQKGYSKVLCQ------TLS 339
Cdd:PLN03229 431 VRELEGEVEKLKEQILKAkeSSSKPSELALNEMIEKLKKEIDLEYTEAviaMGLQERLENLREEFSKANSQdqlmhpVLM 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 340 ERnseITSLKNE-GENLKRDNAITS-----GMVS--SLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALgsrcSVL 411
Cdd:PLN03229 511 EK---IEKLKDEfNKRLSRAPNYLSlkyklDMLNefSRAKALSEKKSKAEKLKAEINKKFKEVMDRPEIKEKM----EAL 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 412 KEELKQEDAHRElrEAQEKELKlckTQIQDMEKEMKKLRAELRKSCTEQsVISRTLREKSKVEEKLQEDSRRKLLQLQEM 491
Cdd:PLN03229 584 KAEVASSGASSG--DELDDDLK---EKVEKMKKEIELELAGVLKSMGLE-VIGVTKKNKDTAEQTPPPNLQEKIESLNEE 657
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370451826 492 GNRESVIKINLERAVGQLEHFRSQVIKATYGRAKPFRDKPVT-DQQLIEKITQVTeDNINFQQKKWTLQKE 561
Cdd:PLN03229 658 INKKIERVIRSSDLKSKIELLKLEVAKASKTPDVTEKEKIEAlEQQIKQKIAEAL-NSSELKEKFEELEAE 727
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
270-390 |
9.09e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 9.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451826 270 IIANLQNEVAELSQKVSETTTSRQNEKEIsqkcqvLDEdIDAKQKEIQSLKSQISALQkgyskvlcQTLSERNSEITSLK 349
Cdd:PHA02562 300 RITKIKDKLKELQHSLEKLDTAIDELEEI------MDE-FNEQSKKLLELKNKISTNK--------QSLITLVDKAKKVK 364
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1370451826 350 NEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHL 390
Cdd:PHA02562 365 AAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR 405
|
|
| |
