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Conserved domains on  [gi|334184921|ref|NP_001189750|]
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SMAD/FHA domain-containing protein [Arabidopsis thaliana]

Protein Classification

FHA domain-containing protein; FOXK family forkhead box protein( domain architecture ID 1018961)

FHA (forkhead-associated) domain-containing protein participates in signal transduction pathways via protein-protein interactions involving recognition of pThr and pTyr phosphopeptides| FOXK family forkhead box protein functions as a transcription factor, similar to FOXK1, one of the transcription factors managing the passage from the normal cellular respiration (complete glucose oxidation) to generating ATP and intermediaries for many other biochemical pathways

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FHA super family cl00062
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
 71-185 3.81e-14

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.


The actual alignment was detected with superfamily member cd22690:

Pssm-ID: 469597 [Multi-domain]  Cd Length: 105  Bit Score: 69.24  E-value: 3.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  71 WGVLTAISsnarKRRQGIniLLTSDEHCLGRLP-CHasYQVESNAISGNHCKVFRKPVTGGDGDdvtVFMVDTSTNGTFL 149
Cdd:cd22690    1 WGRLKSLN----PSYPDI--ELTQNTTFIGRSKdCD--EEITDPRISKHHCIITRKRSGKGLDD---VYVTDTSTNGTFI 69

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 334184921 150 NWERLTKnGPEVRVQHGDIISLAVPPEHEKAFAFVY 185
Cdd:cd22690   70 NNNRLGK-GSQSLLQDGDEIVLIWDKNNKEKIGFIF 104
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 242-512 7.68e-13

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 72.66  E-value: 7.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 242 RKQLEAQVLTIDTLRNESRSI---VEHHESDYLSISTEISLHLQEIKQIKEstaksfhnELIELRDQLDTKQKELAQVNK 318
Cdd:COG1196  224 ELEAELLLLKLRELEAELEELeaeLEELEAELEELEAELAELEAELEELRL--------ELEELELELEEAQAEEYELLA 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 319 LSAEQKNSIDELGERVSASLQTLSEANEVIQSQKASIAELKTGLDEERN---------QRREERETAIAELKAAIHRCQI 389
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEeleeaeeelEEAEAELAEAEEALLEAEAELA 375

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 390 EAQEELKRFSDAAMRHEREQQEVINKMKESEKEKSmQVETLMSKLEDTRQRLvcsENRNRLLEAQVSEEQLAFADAQKKL 469
Cdd:COG1196  376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEE-ALLERLERLEEELEEL---EEALAELEEEEEEEEEALEEAAEEE 451

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 334184921 470 EELDLQVKRLQKDLDSEKQAAREEAWAKVSALELEISAAVRDL 512
Cdd:COG1196  452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
 
Name Accession Description Interval E-value
FHA_RAD53-like_rpt2 cd22690
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ...
 71-185 3.81e-14

second 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 second one. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438742 [Multi-domain]  Cd Length: 105  Bit Score: 69.24  E-value: 3.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  71 WGVLTAISsnarKRRQGIniLLTSDEHCLGRLP-CHasYQVESNAISGNHCKVFRKPVTGGDGDdvtVFMVDTSTNGTFL 149
Cdd:cd22690    1 WGRLKSLN----PSYPDI--ELTQNTTFIGRSKdCD--EEITDPRISKHHCIITRKRSGKGLDD---VYVTDTSTNGTFI 69

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 334184921 150 NWERLTKnGPEVRVQHGDIISLAVPPEHEKAFAFVY 185
Cdd:cd22690   70 NNNRLGK-GSQSLLQDGDEIVLIWDKNNKEKIGFIF 104
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 242-512 7.68e-13

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 72.66  E-value: 7.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 242 RKQLEAQVLTIDTLRNESRSI---VEHHESDYLSISTEISLHLQEIKQIKEstaksfhnELIELRDQLDTKQKELAQVNK 318
Cdd:COG1196  224 ELEAELLLLKLRELEAELEELeaeLEELEAELEELEAELAELEAELEELRL--------ELEELELELEEAQAEEYELLA 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 319 LSAEQKNSIDELGERVSASLQTLSEANEVIQSQKASIAELKTGLDEERN---------QRREERETAIAELKAAIHRCQI 389
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEeleeaeeelEEAEAELAEAEEALLEAEAELA 375

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 390 EAQEELKRFSDAAMRHEREQQEVINKMKESEKEKSmQVETLMSKLEDTRQRLvcsENRNRLLEAQVSEEQLAFADAQKKL 469
Cdd:COG1196  376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEE-ALLERLERLEEELEEL---EEALAELEEEEEEEEEALEEAAEEE 451

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 334184921 470 EELDLQVKRLQKDLDSEKQAAREEAWAKVSALELEISAAVRDL 512
Cdd:COG1196  452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 226-503 6.87e-12

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 69.70  E-value: 6.87e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   226 ISLDDFKSLQRSNTELRKQLEAQVLTIDTLRNE--------SRSIVEHHE---------SDYLSISTEISLHLQEIKQIK 288
Cdd:TIGR02168  229 LLVLRLEELREELEELQEELKEAEEELEELTAElqeleeklEELRLEVSEleeeieelqKELYALANEISRLEQQKQILR 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   289 EStAKSFHNELIELRDQLDTKQKELAQVNKLSAEQKNSIDELGERVSASLQTLSEANEVIQSQKASIAELKTGLDeernq 368
Cdd:TIGR02168  309 ER-LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE----- 382

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   369 rreERETAIAELKAAIHRCQIEAQEELKRFSDAAMRHEREQQEV---INKMKESEKEK-SMQVETLMSKLEDTRQRLVCS 444
Cdd:TIGR02168  383 ---TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIeelLKKLEEAELKElQAELEELEEELEELQEELERL 459

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 334184921   445 ENRNRLLEAQVSEEQLAFADAQKKLEELDLQVKRLQKDLDSEKQAAREEAWAKVSALEL 503
Cdd:TIGR02168  460 EEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGL 518
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
90-172 2.53e-10

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 58.05  E-value: 2.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  90 ILLTSDEHCLGRLPcHASYQVESNAISGNHCKVFRkpvtggDGDDVTVfmVDT-STNGTFLNWERLTKngpEVRVQHGDI 168
Cdd:COG1716   16 FPLDGGPLTIGRAP-DNDIVLDDPTVSRRHARIRR------DGGGWVL--EDLgSTNGTFVNGQRVTE---PAPLRDGDV 83


                 ....
gi 334184921 169 ISLA 172
Cdd:COG1716   84 IRLG 87
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
 99-171 7.43e-08

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 49.88  E-value: 7.43e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334184921   99 LGRLPcHASYQVESNAISGNHCKVFRKpvtggdgDDVTVFMVDT-STNGTFLNWERLTKNgpEVRVQHGDIISL 171
Cdd:pfam00498   3 IGRSP-DCDIVLDDPSVSRRHAEIRYD-------GGGRFYLEDLgSTNGTFVNGQRLGPE--PVRLKDGDVIRL 66
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
228-563 6.61e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 50.04  E-value: 6.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 228 LDDFKSLQRSN----TELRKQLEAQVLTIDTLRNESRSIVEHHESDYLSISTEISLHLQEIKQIKESTAKsFHNELIELR 303
Cdd:PRK02224 410 AEDFLEELREErdelREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEE-LEAELEDLE 488

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 304 DQLDTKQKELAQVNKLsAEQKNSIDELGERVSASLQTLSEANEVIQSQKASIAELKTGLDEERNQRREERETAiAELKAA 383
Cdd:PRK02224 489 EEVEEVEERLERAEDL-VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAA-AEAEEE 566

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 384 IHRCQIEAQE-ELKRfsdAAMRHEREQQEVINKMKESEKEKSMQVETLMSKLED-------TRQRLVCSENRNRLLEAQV 455
Cdd:PRK02224 567 AEEAREEVAElNSKL---AELKERIESLERIRTLLAAIADAEDEIERLREKREAlaelndeRRERLAEKRERKRELEAEF 643

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 456 SEEqlAFADAQKKLEELDLQVKRLQKDLDsEKQAAREEAWAKVSALELEISaavrdldvERQRHRGARERIMLRETQMRA 535
Cdd:PRK02224 644 DEA--RIEEAREDKERAEEYLEQVEEKLD-ELREERDDLQAEIGAVENELE--------ELEELRERREALENRVEALEA 712

                        330       340       350
                 ....*....|....*....|....*....|...
gi 334184921 536 FYSTTEEISALFAK-----QQEQLKTMQRTLED 563
Cdd:PRK02224 713 LYDEAEELESMYGDlraelRQRNVETLERMLNE 745
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 377-565 1.79e-04

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 43.35  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  377 IAELKAAIHRCQIEAQEeLKRFSDAAMRHEREQQEVINKMKESEKEKSMQVETLMSKLEDTRQRLVCSENRNRLLEAQVS 456
Cdd:pfam15619  13 IKELQNELAELQSKLEE-LRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQEKERDLERKLK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  457 EeqlafadAQKKLEELDLQVKRLQKdLDSEKQAA-REEAWAKVSALELEISAAVRDL-DVERQ--------RHRGARERI 526
Cdd:pfam15619  92 E-------KEAELLRLRDQLKRLEK-LSEDKNLAeREELQKKLEQLEAKLEDKDEKIqDLERKlelenksfRRQLAAEKK 163

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 334184921  527 MLRETQmrafysttEEISALfakqQEQLKTMQRTLEDED 565
Cdd:pfam15619 164 KHKEAQ--------EEVKIL----QEEIERLQQKLKEKE 190
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
 99-154 6.88e-04

Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 38.31  E-value: 6.88e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 334184921    99 LGRLPCHASYQVESNAISGNHCKVFRKpvtggDGDDVTVFMVDtSTNGTFLNWERL 154
Cdd:smart00240   3 IGRSSEDCDIQLDGPSISRRHAVIVYD-----GGGRFYLIDLG-STNGTFVNGKRI 52
VI_FHA TIGR03354
type VI secretion system FHA domain protein; Members of this protein family are FHA ...
 73-171 3.11e-03

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: 40.82  E-value: 3.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   73 VLTAISSNARKRRQGINILLTSDEHCLGRLP-CHASYQVESNAISGNHCKVfrkpvTGGDGddvTVFMVDTSTNGTFLNW 151
Cdd:TIGR03354   2 VLTVLNAHQLTPGIAAQKTFGTNGGTIGRSEdCDWVLPDPERHVSGRHARI-----RYRDG---AYLLTDLSTNGVFLNG 73

                          90       100
                  ....*....|....*....|..
gi 334184921  152 E--RLTKnGPEVRVQHGDIISL 171
Cdd:TIGR03354  74 SgsPLGR-GNPVRLEQGDRLRL 94
 
Name Accession Description Interval E-value
FHA_RAD53-like_rpt2 cd22690
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ...
 71-185 3.81e-14

second 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 second one. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438742 [Multi-domain]  Cd Length: 105  Bit Score: 69.24  E-value: 3.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  71 WGVLTAISsnarKRRQGIniLLTSDEHCLGRLP-CHasYQVESNAISGNHCKVFRKPVTGGDGDdvtVFMVDTSTNGTFL 149
Cdd:cd22690    1 WGRLKSLN----PSYPDI--ELTQNTTFIGRSKdCD--EEITDPRISKHHCIITRKRSGKGLDD---VYVTDTSTNGTFI 69

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 334184921 150 NWERLTKnGPEVRVQHGDIISLAVPPEHEKAFAFVY 185
Cdd:cd22690   70 NNNRLGK-GSQSLLQDGDEIVLIWDKNNKEKIGFIF 104
FHA_CHFR cd22672
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ...
 71-171 5.12e-14

forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains protein (CHFR); CHFR, also called RING finger protein 196 (RNF196), is a checkpoint protein that delays entry into mitosis in response to stress. It functions as an E3 ubiquitin ligase that ubiquitinates and degrades its target proteins, such as Aurora-A, Plk1, Kif22 and PARP-1, which are critical for proper mitotic transitions. It also plays an important role in cell cycle progression and tumor suppression and is negatively regulated by SUMOylation-mediated proteasomal ubiquitylation. Moreover, CHFR is involved in the early stage of the DNA damage response, which mediates the crosstalk between ubiquitination and poly-ADP-ribosylation. CHFR contains a fork head associated-(FHA) domain and a RING-HC finger. The CHFR FHA domain has been crystallized as a segment-swapped dimer. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438724 [Multi-domain]  Cd Length: 108  Bit Score: 68.86  E-value: 5.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  71 WGVLTAISSNARKRrqginILLTSDEHCLGRLPcHASYQVESNA-ISGNHCKVFRKPVTGgdgddvtVFMVDTSTNGTFL 149
Cdd:cd22672    2 WGQLVRLTEESSPP-----ILLRKDEFTIGRAK-DCDLSFPGNKlVSGDHCKIIRDEKGQ-------VWLEDTSTNGTLV 68

                         90       100
                 ....*....|....*....|..
gi 334184921 150 NWERLTKnGPEVRVQHGDIISL 171
Cdd:cd22672   69 NKVKVVK-GQKVELKHGDVIYL 89
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 242-512 7.68e-13

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 72.66  E-value: 7.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 242 RKQLEAQVLTIDTLRNESRSI---VEHHESDYLSISTEISLHLQEIKQIKEstaksfhnELIELRDQLDTKQKELAQVNK 318
Cdd:COG1196  224 ELEAELLLLKLRELEAELEELeaeLEELEAELEELEAELAELEAELEELRL--------ELEELELELEEAQAEEYELLA 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 319 LSAEQKNSIDELGERVSASLQTLSEANEVIQSQKASIAELKTGLDEERN---------QRREERETAIAELKAAIHRCQI 389
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEeleeaeeelEEAEAELAEAEEALLEAEAELA 375

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 390 EAQEELKRFSDAAMRHEREQQEVINKMKESEKEKSmQVETLMSKLEDTRQRLvcsENRNRLLEAQVSEEQLAFADAQKKL 469
Cdd:COG1196  376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEE-ALLERLERLEEELEEL---EEALAELEEEEEEEEEALEEAAEEE 451

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 334184921 470 EELDLQVKRLQKDLDSEKQAAREEAWAKVSALELEISAAVRDL 512
Cdd:COG1196  452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 226-503 6.87e-12

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 69.70  E-value: 6.87e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   226 ISLDDFKSLQRSNTELRKQLEAQVLTIDTLRNE--------SRSIVEHHE---------SDYLSISTEISLHLQEIKQIK 288
Cdd:TIGR02168  229 LLVLRLEELREELEELQEELKEAEEELEELTAElqeleeklEELRLEVSEleeeieelqKELYALANEISRLEQQKQILR 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   289 EStAKSFHNELIELRDQLDTKQKELAQVNKLSAEQKNSIDELGERVSASLQTLSEANEVIQSQKASIAELKTGLDeernq 368
Cdd:TIGR02168  309 ER-LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE----- 382

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   369 rreERETAIAELKAAIHRCQIEAQEELKRFSDAAMRHEREQQEV---INKMKESEKEK-SMQVETLMSKLEDTRQRLVCS 444
Cdd:TIGR02168  383 ---TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIeelLKKLEEAELKElQAELEELEEELEELQEELERL 459

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 334184921   445 ENRNRLLEAQVSEEQLAFADAQKKLEELDLQVKRLQKDLDSEKQAAREEAWAKVSALEL 503
Cdd:TIGR02168  460 EEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGL 518
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 271-564 1.95e-11

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 68.16  E-value: 1.95e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   271 LSISTEISLHLQEIKQIkESTAKSFHNELIELRDQLDTKQKELAQVNKLSAEQKNSIDELGE---RVSASLQTLSEANEV 347
Cdd:TIGR02168  673 LERRREIEELEEKIEEL-EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdlaRLEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   348 IQSQKASIAELKTGLDEERNQRREERETA---IAELKAAIHRCQIEAQ---EELKRFSDAAMRHEREQQEVINKMKESEK 421
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAeaeIEELEAQIEQLKEELKalrEALDELRAELTLLNEEAANLRERLESLER 831

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   422 EKsmqvetlmsklEDTRQRLVCSENRNRLLEAQVSEEQLAFADAQKKLEELDLQVKRLQKDLDSekqaaREEAWAKVSAL 501
Cdd:TIGR02168  832 RI-----------AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS-----LEEALALLRSE 895

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334184921   502 ELEISAAVRDLDVERQRHRGARERIMLRETQMRAfysTTEEISALFAKQQEQLKTMQRTLEDE 564
Cdd:TIGR02168  896 LEELSEELRELESKRSELRRELEELREKLAQLEL---RLEGLEVRIDNLQERLSEEYSLTLEE 955
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
90-172 2.53e-10

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 58.05  E-value: 2.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  90 ILLTSDEHCLGRLPcHASYQVESNAISGNHCKVFRkpvtggDGDDVTVfmVDT-STNGTFLNWERLTKngpEVRVQHGDI 168
Cdd:COG1716   16 FPLDGGPLTIGRAP-DNDIVLDDPTVSRRHARIRR------DGGGWVL--EDLgSTNGTFVNGQRVTE---PAPLRDGDV 83


                 ....
gi 334184921 169 ISLA 172
Cdd:COG1716   84 IRLG 87
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
 85-172 2.74e-10

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: 57.67  E-value: 2.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  85 RQGINILLTSDEHCLGRLPcHASYQVESNAISGNHCKVFRkpvtggdgDDVTVFMVDT-STNGTFLNWERLTkngPEVRV 163
Cdd:cd00060    9 GGGREFPLTKGVVTIGRSP-DCDIVLDDPSVSRRHARIEV--------DGGGVYLEDLgSTNGTFVNGKRIT---PPVPL 76


                 ....*....
gi 334184921 164 QHGDIISLA 172
Cdd:cd00060   77 QDGDVIRLG 85
FHA_CHK2 cd22666
forkhead associated (FHA) domain found in checkpoint kinase 2 (Chk2) and similar proteins; ...
 71-186 7.20e-10

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: 57.25  E-value: 7.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  71 WGVLTAIssnarkrRQGI-NILLTSDEHCLGR------------LPCHASYQvesnAISGNHCKVFRKPvtgGDGDDVTV 137
Cdd:cd22666    1 WGRLFPL-------GSGFsSLDLVKDEYTFGRdkscdycfdspaLKKTSYYR----TYSKKHFRIFREK---GSKNTYPV 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 334184921 138 FMVDTSTNGTFLNWERLTKNGPEVrVQHGDIISLAVPpeHEKAFAFVYR 186
Cdd:cd22666   67 FLEDHSSNGTFVNGEKIGKGKKRP-LNNNDEIALSLP--KNKVFVFMDL 112
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 301-564 7.82e-10

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.03  E-value: 7.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 301 ELRDQLDT--KQKELA-QVNKLSAEQK--------NSIDELGERVSASLQTLSEANEVIQSQKASIAELKTGLDeernQR 369
Cdd:COG1196  197 ELERQLEPleRQAEKAeRYRELKEELKeleaelllLKLRELEAELEELEAELEELEAELEELEAELAELEAELE----EL 272

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 370 REeretAIAELKAAIHRCQIEAQEELKRFSDAAMRHEREQQEVINkMKESEKEKSMQVETLMSKLEDTRQRLVCSENRNR 449
Cdd:COG1196  273 RL----ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE-LEERLEELEEELAELEEELEELEEELEELEEELE 347

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 450 LLEAQVSEEQLAFADAQKKLEELDLQVKRLQKDLDSEKQAAREEAWAKVSALELEISAAVRDLDVERQRHRGARERIMLR 529
Cdd:COG1196  348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 334184921 530 ETQMRAfystTEEISALFAKQQEQLKTMQRTLEDE 564
Cdd:COG1196  428 EALAEL----EEEEEEEEEALEEAAEEEAELEEEE 458
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 229-515 1.07e-09

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.65  E-value: 1.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 229 DDFKSLQRSNTELRKQLEAQVLTIDTLRNEsrsiVEHHESDYLSISTEISlHLQEIKQIKESTAKSFHNELIELRDQLDT 308
Cdd:COG1196  253 AELEELEAELAELEAELEELRLELEELELE----LEEAQAEEYELLAELA-RLEQDIARLEERRRELEERLEELEEELAE 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 309 KQKELAQVNKLSAEQKNSIDELGERVSASLQTLSEANEVIQSQKASIAELktgLDEERNQRReeretAIAELKAAIHRCQ 388
Cdd:COG1196  328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA---EEELEELAE-----ELLEALRAAAELA 399

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 389 IEAQEELKRFSDAAMRHEREQQEVINKmKESEKEKSMQVETLMSKLEDTRQRLVCSENRNRLLEAQVSEEQLAFADAQKK 468
Cdd:COG1196  400 AQLEELEEAEEALLERLERLEEELEEL-EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 334184921 469 LEELDLQVKRLQKDLDSEKQAAREEAWAKVSALELEISAAVRDLDVE 515
Cdd:COG1196  479 LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
FHA_MEK1-like cd22670
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ...
 72-188 1.72e-09

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: 56.08  E-value: 1.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  72 GVLTAISSNARKRRqgINILLTSDEHClGRLPcHASYQVESNAISGNHCkVFRKPVTGGDGDDVtVFMVDTSTNGTFLNW 151
Cdd:cd22670    2 GKLEVSSPGSTDIV--LPIYKNQVITI-GRSP-SCDIVINDPFVSRTHC-RIYSVQFDESSAPL-VYVEDLSSNGTYLNG 75

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 334184921 152 ERLTKNGPeVRVQHGDIISLAvppeheKAFAFVYREV 188
Cdd:cd22670   76 KLIGRNNT-VLLSDGDVIEIA------HSATFVYVHN 105
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 276-558 1.83e-09

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.88  E-value: 1.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 276 EISLHLQEIKQIKEsTAKSFHNELIELRDQLDTKQKELAQVNKLSAEQKNSIDELGERVSASLQTLSEANEVIQSQKASI 355
Cdd:COG1196  226 EAELLLLKLRELEA-ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 356 AELKtgldeERNQRREERETAIAELKAAIHRCQIEAQEELKRFSDAAMRHEREQQEVINKMKESEKEKSMQVETLMSKLE 435
Cdd:COG1196  305 ARLE-----ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 436 DT---RQRLVCSENRNRLLEAQVSEEQLAFADAQKKLEELDLQVKRLQKDLDSEKQAAREEAWAKVSALELEISAAVRDL 512
Cdd:COG1196  380 ELeelAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 334184921 513 DVERQRHRgARERIMLRETQMRAFYSTTEEISALFAKQQEQLKTMQ 558
Cdd:COG1196  460 ALLELLAE-LLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 297-562 3.99e-09

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: 60.84  E-value: 3.99e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   297 NELIELRDQLDTKQKELAqvnklsaeqKNSIDELGERVSASLQTLSEANEVIQSQKASIAELKTGLDeernqrreERETA 376
Cdd:TIGR02168  213 ERYKELKAELRELELALL---------VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLE--------ELRLE 275

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   377 IAELKAAIHrcqiEAQEELKRFSDAAMRHEREQQEVINKMKESE---KEKSMQVETLMSKLEDTRQRLVCSENRNRLLEA 453
Cdd:TIGR02168  276 VSELEEEIE----ELQKELYALANEISRLEQQKQILRERLANLErqlEELEAQLEELESKLDELAEELAELEEKLEELKE 351

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   454 QVSEEQLAFADAQKKLEELDLQVKRLQKDLDSEKQAARE------EAWAKVSALELEISAAVRDLDVERQRHRGARERim 527
Cdd:TIGR02168  352 ELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQlelqiaSLNNEIERLEARLERLEDRRERLQQEIEELLKK-- 429

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 334184921   528 LRETQMRAFYSTTEEISALFAKQQEQLKTMQRTLE 562
Cdd:TIGR02168  430 LEEAELKELQAELEELEEELEELQEELERLEEALE 464
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
289-540 1.70e-08

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 58.49  E-value: 1.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 289 ESTAKSFHNELIELRDQLDTKQKELAQVnklsaEQKNSIDELGERVSASLQTLSEANEVIQSQKASIAELKTGLDEERNQ 368
Cdd:COG3206  174 RKALEFLEEQLPELRKELEEAEAALEEF-----RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQ 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 369 RREERETA--------IAELKAAIHRCQIEAQEELKRFSDaamRHEreqqevinkmkesekeksmQVETLMSKLEDTRQR 440
Cdd:COG3206  249 LGSGPDALpellqspvIQQLRAQLAELEAELAELSARYTP---NHP-------------------DVIALRAQIAALRAQ 306

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 441 LvcsenrnrlleaqVSEEQLAFADAQKKLEELDLQVKRLQKDLDSEKQAAREeawakVSALELEISAAVRDLDVERQRHR 520
Cdd:COG3206  307 L-------------QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAE-----LPELEAELRRLEREVEVARELYE 368

                        250       260
                 ....*....|....*....|
gi 334184921 521 GARERimLRETQMRAFYSTT 540
Cdd:COG3206  369 SLLQR--LEEARLAEALTVG 386
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 301-564 3.54e-08

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.64  E-value: 3.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 301 ELRDQLDTKQKELA-----QVNKLSAEQKNSIDELGERVSASLQTLSEANEVIQSQKASIAELKTGLDEernqrREER-- 373
Cdd:COG1196  217 ELKEELKELEAELLllklrELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE-----AQAEey 291

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 374 --ETAIAELKAAIHRCQ---IEAQEELKRFSDAAMRHEREQQEVINKMKESEKEKSM---QVETLMSKLEDTRQRLVCSE 445
Cdd:COG1196  292 elLAELARLEQDIARLEerrRELEERLEELEEELAELEEELEELEEELEELEEELEEaeeELEEAEAELAEAEEALLEAE 371

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 446 NRNRLLEAQVSEEQLAFADAQKKLEELDLQVKRLQKDLDSEKQaAREEAWAKVSALELEISAAVRDLDVERQRHRGARER 525
Cdd:COG1196  372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE-RLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 334184921 526 IMLRETQMRAFYSTTEEISALFAKQQEQLKTMQRTLEDE 564
Cdd:COG1196  451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 289-562 3.91e-08

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 57.39  E-value: 3.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   289 ESTAKSFHNELIELRDQLDTKQKELAQVNKLSAEQKNSIDELGERVSASLQTLSEANEVIQSQKASIAELKtgldeernq 368
Cdd:TIGR02169  666 ILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK--------- 736

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   369 rreereTAIAELKAAIHRCQiEAQEELKRFSDAAMRHEREQQEVINKMKESE--------KEKSMQVETLMSKLEDTRQR 440
Cdd:TIGR02169  737 ------ERLEELEEDLSSLE-QEIENVKSELKELEARIEELEEDLHKLEEALndlearlsHSRIPEIQAELSKLEEEVSR 809

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   441 LvcsENRNRLLEAQVSEEQLAFADAQKKLEELDLQVKRLQKDLDSEKQAArEEAWAKVSALELEIS---AAVRDLDVERQ 517
Cdd:TIGR02169  810 I---EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI-ENLNGKKEELEEELEeleAALRDLESRLG 885

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 334184921   518 RHRGARERimlRETQMRAFYSTTEEISALFAKQQEQLKTMQRTLE 562
Cdd:TIGR02169  886 DLKKERDE---LEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
 99-171 7.43e-08

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 49.88  E-value: 7.43e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334184921   99 LGRLPcHASYQVESNAISGNHCKVFRKpvtggdgDDVTVFMVDT-STNGTFLNWERLTKNgpEVRVQHGDIISL 171
Cdd:pfam00498   3 IGRSP-DCDIVLDDPSVSRRHAEIRYD-------GGGRFYLEDLgSTNGTFVNGQRLGPE--PVRLKDGDVIRL 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 342-564 9.32e-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: 56.22  E-value: 9.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   342 SEANEVIQSQKASIAELKTGLDEERNqrreeretAIAELKAAIHRCQIEAQEELKRFSDAAMRHEREQQEvINKMKESEK 421
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEELEE--------KIAELEKALAELRKELEELEEELEQLRKELEELSRQ-ISALRKDLA 736

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   422 EKSMQVETLMSKLEDTRQRLVCSENRNRLLEAQVSEEQLAFADAQKKLEELDLQVKRLQKDLDSEKQ---AAREEawakV 498
Cdd:TIGR02168  737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREaldELRAE----L 812

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334184921   499 SALELEISAAVRDLDVERQRHRGARERIMLRETQMRafySTTEEISALfAKQQEQLKTMQRTLEDE 564
Cdd:TIGR02168  813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIE---ELSEDIESL-AAEIEELEELIEELESE 874
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 297-500 2.67e-07

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 54.00  E-value: 2.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 297 NELIELRDQLDTKQKELAQVNKLSAEQKNSIDELGERVSASLQTLSEANEVIQSQKASIAELKTGLDEERNQRREEREtA 376
Cdd:COG4942   27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE-E 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 377 IAELKAAIHRCQIEAQEEL----KRFSDAAMR---------HEREQQEVINKMKESEKEKSMQVETLMSKLEDTRQRLvc 443
Cdd:COG4942  106 LAELLRALYRLGRQPPLALllspEDFLDAVRRlqylkylapARREQAEELRADLAELAALRAELEAERAELEALLAEL-- 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 334184921 444 sENRNRLLEAQVSEEQLAFADAQKKLEELDLQVKRLQKDLDS-EKQAAREEAWAKVSA 500
Cdd:COG4942  184 -EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEElEALIARLEAEAAAAA 240
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 281-565 4.21e-07

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 53.92  E-value: 4.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   281 LQEIKQIKESTAKsfhNELI--ELRDQLDTKQKELAQVNKLSAEQKNSIDELGERVSASLQTLSEANEVIQSQKASIAEL 358
Cdd:TIGR02169  176 LEELEEVEENIER---LDLIidEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEE 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   359 KTGLDEERNQRREERETAIAELKAAIHRC-------QIEAQEELKRFSDAAMRHEREQQEVINKMKESEKEKS---MQVE 428
Cdd:TIGR02169  253 LEKLTEEISELEKRLEEIEQLLEELNKKIkdlgeeeQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAkleAEID 332

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   429 TLMSKLEDTRQRLVCSENRNRLLEAQVSEEQLAFADAQKKLEELDLQVKRLQKDLDSEKQAArEEAWAKVSALELEISAA 508
Cdd:TIGR02169  333 KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL-EKLKREINELKRELDRL 411

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 334184921   509 VRDLDVERQRHRGARERIMLRETQMRAFYSTTEEISALFAKQQEQLKTMQRTLEDED 565
Cdd:TIGR02169  412 QEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
FHA_RNF8 cd22663
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ...
 89-186 5.51e-07

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: 48.89  E-value: 5.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  89 NILLTSD-EHCLGRLPCHASYQV--ESNAISGNHCkVFRKpvtggdGDDVTVFMVD-TSTNGTFLNWERLTKNGPeVRVQ 164
Cdd:cd22663   14 VLLLEDGkEVTVGRGLGVTYQLVstCPLMISRNHC-VLKK------NDEGQWTIKDnKSLNGVWVNGERIEPLKP-YPLN 85

                         90       100
                 ....*....|....*....|..
gi 334184921 165 HGDIISLAVPPEHEKAFAFVYR 186
Cdd:cd22663   86 EGDLIQLGVPPENKEPAEYVFN 107
FHA_NBN cd22667
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ...
 71-173 5.92e-07

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: 48.86  E-value: 5.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  71 WGVLTAISSNARKRRqginiLLTSDEHCLGRLPCHASyQVESNAISGNHC--KVFRKPVTGGDGDDV-TVFMVDTSTNGT 147
Cdd:cd22667    1 WWLLSEQDGAGTSYY-----LLPGGEYTVGRKDCDII-IVDDSSISRKHAtlTVLHPEANLSDPDTRpELTLKDLSKYGT 74

                         90       100
                 ....*....|....*....|....*.
gi 334184921 148 FLNWERLtKNGPEVRVQHGDIISLAV 173
Cdd:cd22667   75 FVNGEKL-KGGSEVTLKDGDVITFGV 99
FHA_TCF19 cd22685
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ...
 90-188 1.16e-06

forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar proteins; TCF-19, also called transcription factor SC1, was identified as a putative trans-activating factor with expression beginning at the late G1-S boundary in dividing cells. It also functions as a novel islet factor necessary for proliferation and survival in the INS-1 beta cell line. It plays an important role in susceptibility to both Type 1 Diabetes Mellitus (T1DM) and Type 2 Diabetes Mellitus (T2DM); it has been suggested that it may positively impact beta cell mass under conditions of beta cell stress and increased insulin demand. TCF-19 contains an N-terminal fork head association domain (FHA), a proline rich region, and a C-terminal plant homeodomain (PHD) finger. The FHA domain may serve as a nuclear signaling domain or as a phosphoprotein binding domain. The proline rich region is a common characteristic of trans-activating factors. The PHD finger may allow TCF-19 to interact with chromatin via methylated histone H3.


Pssm-ID: 438737 [Multi-domain]  Cd Length: 130  Bit Score: 48.57  E-value: 1.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  90 ILLTSDEHCLGRLP----CHASYQVESNAISGNHCKVFRKPVTGGDgddVTVFMVDTSTNGTFLNWERLtKNGPEVRVQH 165
Cdd:cd22685   23 FRPDLCEYRIGRNPevcdVFLCSSQHPNLISREHAEIHAERDGNGN---WKVLIEDRSTNGTYVNDVRL-QDGQRRELSD 98

                         90       100       110
                 ....*....|....*....|....*....|..
gi 334184921 166 GDIISL---------AVPPEHEKAFAFVYREV 188
Cdd:cd22685   99 GDTITFghkngrrvkQWPYQKSSEFYFLFQKV 130
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 282-500 2.54e-06

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 50.92  E-value: 2.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 282 QEIKQiKESTAKSFHNELIELRDQLDTKQKELAQVNKLSAEQKNSIDELGERVSASLQTLSEANEVIQSQKASIAELKTG 361
Cdd:COG4942   34 QEIAE-LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 362 LDEERNQRREERETAIAELKAAIHRcqIEAQEELKRFSDAAMRHEREQQEVINKMKESEKEKSMQVETLMSKLEDTRQRL 441
Cdd:COG4942  113 LYRLGRQPPLALLLSPEDFLDAVRR--LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 334184921 442 VCSENRNRLLEAQVSEEQlafADAQKKLEELDLQVKRLQKDLDSEKQAAREEAWAKVSA 500
Cdd:COG4942  191 EALKAERQKLLARLEKEL---AELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
228-563 6.61e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 50.04  E-value: 6.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 228 LDDFKSLQRSN----TELRKQLEAQVLTIDTLRNESRSIVEHHESDYLSISTEISLHLQEIKQIKESTAKsFHNELIELR 303
Cdd:PRK02224 410 AEDFLEELREErdelREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEE-LEAELEDLE 488

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 304 DQLDTKQKELAQVNKLsAEQKNSIDELGERVSASLQTLSEANEVIQSQKASIAELKTGLDEERNQRREERETAiAELKAA 383
Cdd:PRK02224 489 EEVEEVEERLERAEDL-VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAA-AEAEEE 566

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 384 IHRCQIEAQE-ELKRfsdAAMRHEREQQEVINKMKESEKEKSMQVETLMSKLED-------TRQRLVCSENRNRLLEAQV 455
Cdd:PRK02224 567 AEEAREEVAElNSKL---AELKERIESLERIRTLLAAIADAEDEIERLREKREAlaelndeRRERLAEKRERKRELEAEF 643

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 456 SEEqlAFADAQKKLEELDLQVKRLQKDLDsEKQAAREEAWAKVSALELEISaavrdldvERQRHRGARERIMLRETQMRA 535
Cdd:PRK02224 644 DEA--RIEEAREDKERAEEYLEQVEEKLD-ELREERDDLQAEIGAVENELE--------ELEELRERREALENRVEALEA 712

                        330       340       350
                 ....*....|....*....|....*....|...
gi 334184921 536 FYSTTEEISALFAK-----QQEQLKTMQRTLED 563
Cdd:PRK02224 713 LYDEAEELESMYGDlraelRQRNVETLERMLNE 745
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
390-564 8.71e-06

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.91  E-value: 8.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  390 EAQEELKRFSDA--AMRHEREQQEVINKMKES-EKEKSMQVETLMSKLEDTRQRLVCSENRNRLLEAQVSEEQLAFADAQ 466
Cdd:COG4913   229 ALVEHFDDLERAheALEDAREQIELLEPIRELaERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLE 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  467 KKLEELDLQVKRLQKDLDSEKQAAREEAWAKVSALELEISAAVRDLDvERQRHRGARERimlretQMRAFYSTTEEISAL 546
Cdd:COG4913   309 AELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELE-ERERRRARLEA------LLAALGLPLPASAEE 381

                         170
                  ....*....|....*...
gi 334184921  547 FAKQQEQLKTMQRTLEDE 564
Cdd:COG4913   382 FAALRAEAAALLEALEEE 399
COG3456 COG3456
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ...
 73-171 1.08e-05

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: 48.99  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  73 VLTAISSNARKRRQGINILLTSDEHCLGRLP-CHASYQVESNAISGNHCKVfrkpvtggDGDDVTVFMVDTSTNGTFLN- 150
Cdd:COG3456    4 TLRIINSPDLESGSAASATFGRGGGTIGRSAdCDWVLPDPDRSVSRRHAEI--------RFRDGAFCLTDLSTNGTFLNg 75

                         90       100
                 ....*....|....*....|..
gi 334184921 151 -WERLTKNGPeVRVQHGDIISL 171
Cdd:COG3456   76 sDHPLGPGRP-VRLRDGDRLRI 96
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 304-522 1.31e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.61  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 304 DQLDTKQKELAQVNKLSAEQKNSIDELGERVSASLQTLSEANEVIQSQKASIAELKTGLDeERNQRREERETAIAELKAA 383
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA-ALEAELAELEKEIAELRAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 384 IHrcqiEAQEELKRFSDAAMRHERE-----------------QQEVINKMKESEKEKSMQVETLMSKLEDTRQRLVCSEN 446
Cdd:COG4942   99 LE----AQKEELAELLRALYRLGRQpplalllspedfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334184921 447 RNRLLEAQVSEEQLAFADAQKKLEELdlqVKRLQKDLDSEKQAAREEAwAKVSALELEISAAVRDLDVERQRHRGA 522
Cdd:COG4942  175 ELEALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQ-QEAEELEALIARLEAEAAAAAERTPAA 246
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
273-505 1.46e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.91  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 273 ISTEISLHLQEIKQIKEstaksFHNELIELRDQLDTKQKELAQVNK-LSAEQKNSIDELGERVSaSLQ-------TLSEA 344
Cdd:PRK03918 537 LKGEIKSLKKELEKLEE-----LKKKLAELEKKLDELEEELAELLKeLEELGFESVEELEERLK-ELEpfyneylELKDA 610

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 345 NEVIQSQKASIAELKTGLDEERNQrreeretaIAELKAAIHRCQIEAQEELKRFSdaamrhEREQQEVINKMKESEKE-- 422
Cdd:PRK03918 611 EKELEREEKELKKLEEELDKAFEE--------LAETEKRLEELRKELEELEKKYS------EEEYEELREEYLELSREla 676

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 423 -KSMQVETLMSKLEDTRQRLvcsENRNRLLEA--QVSEEQLAFADAQKKLEELDLQVKRLqkdldseKQAAREEAWAKVS 499
Cdd:PRK03918 677 gLRAELEELEKRREEIKKTL---EKLKEELEEreKAKKELEKLEKALERVEELREKVKKY-------KALLKERALSKVG 746


                 ....*.
gi 334184921 500 ALELEI 505
Cdd:PRK03918 747 EIASEI 752
PTZ00121 PTZ00121
MAEBL; Provisional
 301-701 7.01e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 7.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  301 ELRDQLDTKQKELAQvnklSAEQKNSIDELgeRVSASLQTLSEANEVIQSQKAS--------IAELKTGLDEERNQRREE 372
Cdd:PTZ00121 1526 EAKKAEEAKKADEAK----KAEEKKKADEL--KKAEELKKAEEKKKAEEAKKAEedknmalrKAEEAKKAEEARIEEVMK 1599

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  373 RETAIAELKAAIHRcqieaQEELKRFSDAAMRHEREQQEVINKMKESEKEKSMQVETLMSKLEDTRQRlVCSENRNRLLE 452
Cdd:PTZ00121 1600 LYEEEKKMKAEEAK-----KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK-AAEEAKKAEED 1673

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  453 AQVSEEQLAFADAQKKLEEldlQVKRLQKDLDSEKQAAREEAWAKVSALELEISAAVRDLDVER------QRHRGARERI 526
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKKAAE---ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEakkeaeEDKKKAEEAK 1750

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  527 MLRETQMRAFYSTTEEISALFAKQQEQLKTMQRTLEDEDNCDNTSLDIDLNPInrSPNRANTQ-GDKRATSHLNfaaras 605
Cdd:PTZ00121 1751 KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDI--FDNFANIIeGGKEGNLVIN------ 1822

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  606 SSTSGQRSTRNEVVDTS---CEDADATQKHDCEIMSQEGQNTQEAEYPSSDKVAKGGFGSDIEGIGTAPTSGTDPVGTEQ 682
Cdd:PTZ00121 1823 DSKEMEDSAIKEVADSKnmqLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREI 1902

                         410
                  ....*....|....*....
gi 334184921  683 VNETQSPGNDYERNDHLRK 701
Cdd:PTZ00121 1903 PNNNMAGKNNDIIDDKLDK 1921
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
296-535 8.62e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 8.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  296 HNELIELRDQLDTkqkeLAQvnklsaeqknsIDELGERVSASLQTLSEANEVIQSQKASIAELKTGLdeernqrreeRET 375
Cdd:COG4913   241 HEALEDAREQIEL----LEP-----------IRELAERYAAARERLAELEYLRAALRLWFAQRRLEL----------LEA 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  376 AIAELKAAIHRcqieAQEELKRFSDAAMRHEREQQEVINKMKESEKEKSMQVETLMSKLEDTRQRlvCSENRNRlLEAQV 455
Cdd:COG4913   296 ELEELRAELAR----LEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEE--RERRRAR-LEALL 368

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  456 SEEQLAFADAQKKLEELDLQVKRLQKDLDSEKQAAREEAWAKVSALElEISAAVRDLDVERQRHRGARERIMLRETQMRA 535
Cdd:COG4913   369 AALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR-DLRRELRELEAEIASLERRKSNIPARLLALRD 447
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
240-563 1.57e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 1.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 240 ELRKQLEAQVLTIDTLRNEsrsIVEHHESDYLSISTEISLHLQEIKQIKESTAKSfHNELIELRDQLDTKQKELAQV--N 317
Cdd:COG4717  160 ELEEELEELEAELAELQEE---LEELLEQLSLATEEELQDLAEELEELQQRLAEL-EEELEEAQEELEELEEELEQLenE 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 318 KLSAEQKNSIDE-------LGERVSASLQTLSEANEVIQSQK--ASIAELKTGLDEERNQRREERETAIAELKAAIHRCQ 388
Cdd:COG4717  236 LEAAALEERLKEarlllliAAALLALLGLGGSLLSLILTIAGvlFLVLGLLALLFLLLAREKASLGKEAEELQALPALEE 315

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 389 IEAQEELKRFSDAAMRHEREQQEVINKMKESEKEKSMQVEtlMSKLEDTRQRLVCSENRNRLLEAQ--VSEEQL-----A 461
Cdd:COG4717  316 LEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLRE--AEELEEELQLEELEQEIAALLAEAgvEDEEELraaleQ 393

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 462 FADAQKKLEELDLQVKRLQKDLDSEKQAAREEAWAKVSALELEISAAVRDLDVERQRHRGARERImlrETQMRAfYSTTE 541
Cdd:COG4717  394 AEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAEL---EAELEQ-LEEDG 469

                        330       340
                 ....*....|....*....|..
gi 334184921 542 EISALFAKQQEQLKTMQRTLED 563
Cdd:COG4717  470 ELAELLQELEELKAELRELAEE 491
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 229-526 1.71e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 229 DDFKSLQRSNTELRKQLEAQVLTIDTLRNESRSIVEHHESDYLSISTEISLHLQEIKQIKESTAksfhnELIELRDQLDT 308
Cdd:COG1196  281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE-----ELEEAEEELEE 355

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 309 KQKELAQVNKLSAEQKNSIDELGERVSASLQTLSEANEVIQSQKASIAELKTGLDEERNQRREERETAIAELKAAIHrcQ 388
Cdd:COG1196  356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE--L 433

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 389 IEAQEELKRFSDAAMRHEREQQEVINKMKESEKEKSMQVETLMSKLEDTRQRLVCSENRNRLLEAQVSEEQLAFADAQKK 468
Cdd:COG1196  434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 469 LEELD-------------------------LQVKRLQKDLDSEKQAAREEAWAK------VSALELEISAAVRDLDVERQ 517
Cdd:COG1196  514 LLLAGlrglagavavligveaayeaaleaaLAAALQNIVVEDDEVAAAAIEYLKaakagrATFLPLDKIRARAALAAALA 593


                 ....*....
gi 334184921 518 RHRGARERI 526
Cdd:COG1196  594 RGAIGAAVD 602
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 377-565 1.79e-04

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 43.35  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  377 IAELKAAIHRCQIEAQEeLKRFSDAAMRHEREQQEVINKMKESEKEKSMQVETLMSKLEDTRQRLVCSENRNRLLEAQVS 456
Cdd:pfam15619  13 IKELQNELAELQSKLEE-LRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQEKERDLERKLK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  457 EeqlafadAQKKLEELDLQVKRLQKdLDSEKQAA-REEAWAKVSALELEISAAVRDL-DVERQ--------RHRGARERI 526
Cdd:pfam15619  92 E-------KEAELLRLRDQLKRLEK-LSEDKNLAeREELQKKLEQLEAKLEDKDEKIqDLERKlelenksfRRQLAAEKK 163

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 334184921  527 MLRETQmrafysttEEISALfakqQEQLKTMQRTLEDED 565
Cdd:pfam15619 164 KHKEAQ--------EEVKIL----QEEIERLQQKLKEKE 190
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 239-488 2.21e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.01  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  239 TELRKQLEAQVLTIDTLRNESRSIVEHHESDYLSISTEISLHLQEIKQIKestaksfhNELIELRDQLDTKQKELAQVNK 318
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLK--------DEQNKIKKQLSEKQKELEQNNK 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  319 LSAEQKNSIDELGERVS-----ASLQTLSEANEVIQSQKASIAELKTGLDEERNqrreeretAIAELKAAIHrcQIEAQE 393
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISdlnnqKEQDWNKELKSELKNQEKKLEEIQNQISQNNK--------IISQLNEQIS--QLKKEL 351

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  394 ELKRFSDAAMRHE-REQQEVINKMKESEKEKSMQVETLMSKLEDTRQRLVCSENRNRLLEAQVSEeqlafadAQKKLEEL 472
Cdd:TIGR04523 352 TNSESENSEKQRElEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK-------LQQEKELL 424

                         250
                  ....*....|....*.
gi 334184921  473 DLQVKRLQKDLDSEKQ 488
Cdd:TIGR04523 425 EKEIERLKETIIKNNS 440
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 390-530 3.17e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 44.78  E-value: 3.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   390 EAQEELKRFSDAAMR-----------HEREQQEVINKMKESEKEKSMQVETLMSKLEDTR-QRLVCSENRNRL------L 451
Cdd:pfam01576  703 ELEDELQATEDAKLRlevnmqalkaqFERDLQARDEQGEEKRRQLVKQVRELEAELEDERkQRAQAVAAKKKLeldlkeL 782

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   452 EAQVSEEQLAFADAQKKLEELDLQVKRLQKDLDsEKQAAREEAWA-------KVSALELEISAAVRDLDV-ERQRHRGAR 523
Cdd:pfam01576  783 EAQIDAANKGREEAVKQLKKLQAQMKDLQRELE-EARASRDEILAqskesekKLKNLEAELLQLQEDLAAsERARRQAQQ 861


                   ....*..
gi 334184921   524 ERIMLRE 530
Cdd:pfam01576  862 ERDELAD 868
FHA_RAD53-like_rpt1 cd22689
first forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ...
 108-181 3.75e-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: 41.49  E-value: 3.75e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334184921 108 YQVESNAISGNHckvFRKPVTGGDGDDVTVFMVDTSTNGTFLNWERLTKNGPEVrVQHGDIISLAV-PPEHEKAF 181
Cdd:cd22689   57 YHLGNSRLSNKH---FQILLGESDPSDGNVLLNDISSNGTWLNGQRLEKNSNQL-LSQGDEITIGVgVTGDILSL 127
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 309-566 3.75e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 44.34  E-value: 3.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   309 KQKELAQVNKLSAE---QKNSIDELGERVSASLQTLSEANEVIQSQKASIAELKTGLDEERnqrreeretaiAELKAAIH 385
Cdd:pfam15921  456 KNESLEKVSSLTAQlesTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATN-----------AEITKLRS 524

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   386 RCQIEAQE--ELKRFSDaamrHEREQQEVINKMKESEKEKSMQVETLMSKLEDTRQrLVCSENRNRLlEAQVSEEQLafa 463
Cdd:pfam15921  525 RVDLKLQElqHLKNEGD----HLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQ-LVGQHGRTAG-AMQVEKAQL--- 595

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   464 daQKKLEELDLQVKRLqKDLDSEKQAAREEAWAKVSALELE----ISA------AVRDLDVERQR--HRGARERIMLR-- 529
Cdd:pfam15921  596 --EKEINDRRLELQEF-KILKDKKDAKIRELEARVSDLELEkvklVNAgserlrAVKDIKQERDQllNEVKTSRNELNsl 672

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 334184921   530 ----ETQMRAFYSTTEEISALFAKQQEQLKTMQRTLEDEDN 566
Cdd:pfam15921  673 sedyEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRN 713
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
285-508 4.31e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.26  E-value: 4.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 285 KQIKESTAKSFHNELIELRDQLDT---------KQKELAQVNKLSAEQ---------------KNSIDELGERVSASLQT 340
Cdd:PRK02224 194 AQIEEKEEKDLHERLNGLESELAEldeeieryeEQREQARETRDEADEvleeheerreeletlEAEIEDLRETIAETERE 273

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 341 LSEANEVIQSQKASIAELKTGLDEERNQR--REERETAIAELKAAIHRCQIEAQEELKRFSDAAMRHEREQQ---EVINK 415
Cdd:PRK02224 274 REELAEEVRDLRERLEELEEERDDLLAEAglDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAEslrEDADD 353

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 416 MKESEKEKSMQVETLMSKLEDTRQRLVCSENRNRLLEAQVSEEQLAFADAQKKLEELDlqvkrlqkDLDSEKQAAREEAW 495
Cdd:PRK02224 354 LEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE--------DFLEELREERDELR 425

                        250
                 ....*....|...
gi 334184921 496 AKVSALELEISAA 508
Cdd:PRK02224 426 EREAELEATLRTA 438
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 244-508 4.57e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 43.94  E-value: 4.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  244 QLEAQVLTIDTLRNESRSIVEHHESDYLSISTEISLHLQEIKQIKESTAKSfHNELIELRDQLDTKQK---ELAQVNKLS 320
Cdd:pfam05483 353 EFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNK-EVELEELKKILAEDEKlldEKKQFEKIA 431

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  321 AEQKNSIDELGERVSASLQTLSEANEVIQSQKAS-------IAELKTGLDEERNQRReeretaiaELKAAIHRCQIEAQE 393
Cdd:pfam05483 432 EELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSeehylkeVEDLKTELEKEKLKNI--------ELTAHCDKLLLENKE 503

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  394 ELKRFSDAAMRHeREQQEVINKMKESEKEKSMQVETLMSK-------LEDTRQRLV-------C----SENRNRLLEAQV 455
Cdd:pfam05483 504 LTQEASDMTLEL-KKHQEDIINCKKQEERMLKQIENLEEKemnlrdeLESVREEFIqkgdevkCkldkSEENARSIEYEV 582

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334184921  456 SEEQLAFADAQKKLEELDLQVKRLQK---DLDSEKQAAREEAWA----------KVSALELEISAA 508
Cdd:pfam05483 583 LKKEKQMKILENKCNNLKKQIENKNKnieELHQENKALKKKGSAenkqlnayeiKVNKLELELASA 648
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 428-565 5.03e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 5.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 428 ETLmSKLEDTRQRL-----VCSENRNRL--LEAQvSEEQLAFADAQKKLEELDLQVKRLQKDLDSEKQAAREEAWAKVSA 500
Cdd:COG1196  176 EAE-RKLEATEENLerledILGELERQLepLERQ-AEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEA 253

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334184921 501 LELEISAAVRDLDVERQRHRGARERIMLRETQMRA-FYSTTEEISALFAKQQEQLKTMQRTLEDED 565
Cdd:COG1196  254 ELEELEAELAELEAELEELRLELEELELELEEAQAeEYELLAELARLEQDIARLEERRRELEERLE 319
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 410-517 5.79e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.66  E-value: 5.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 410 QEVINKMKESEKEKSMQVETLMSKLEDTRQRLvcsENRNRLLEAQVSEeqlafadAQKKLEELDLQVKRLQKDLDSEKQA 489
Cdd:PRK00409 501 ENIIEEAKKLIGEDKEKLNELIASLEELEREL---EQKAEEAEALLKE-------AEKLKEELEEKKEKLQEEEDKLLEE 570

                         90       100
                 ....*....|....*....|....*...
gi 334184921 490 AREEAWAKVSALELEISAAVRDLDVERQ 517
Cdd:PRK00409 571 AEKEAQQAIKEAKKEADEIIKELRQLQK 598
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 379-566 6.27e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 6.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 379 ELKAAIHRCQIEAQeeLKRFSDAAMRHEREQQEvINKMKESEKEKSMQVETLMSKLEDTRQRLvcSENRNRLLEAQVSEE 458
Cdd:COG1196  217 ELKEELKELEAELL--LLKLRELEAELEELEAE-LEELEAELEELEAELAELEAELEELRLEL--EELELELEEAQAEEY 291

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 459 QL--AFADAQKKLEELDLQVKRLQKDLDSEKQAAREEAWAKVSALELEISAAVRDLDVERQRHRGARERIMLRETQMRAF 536
Cdd:COG1196  292 ELlaELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371

                        170       180       190
                 ....*....|....*....|....*....|
gi 334184921 537 YSTTEEISALFAKQQEQLKTMQRTLEDEDN 566
Cdd:COG1196  372 AELAEAEEELEELAEELLEALRAAAELAAQ 401
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
 99-154 6.88e-04

Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 38.31  E-value: 6.88e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 334184921    99 LGRLPCHASYQVESNAISGNHCKVFRKpvtggDGDDVTVFMVDtSTNGTFLNWERL 154
Cdd:smart00240   3 IGRSSEDCDIQLDGPSISRRHAVIVYD-----GGGRFYLIDLG-STNGTFVNGKRI 52
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 234-575 1.24e-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: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   234 LQRSNTELRKQLEAQV--LTIDTLRNESRSIVEHHESDYLSISTEISLHLQ----EIKQIKESTAKSFHN------ELIE 301
Cdd:pfam12128  417 LQALESELREQLEAGKleFNEEEYRLKSRLGELKLRLNQATATPELLLQLEnfdeRIERAREEQEAANAEverlqsELRQ 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   302 LRDQLDTKQKELAQVNKLSAEQKNSIDELGERVSASLQTLSE-ANEVIQSQKASIAEL-------KTGLDEERNQRREER 373
Cdd:pfam12128  497 ARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHfLRKEAPDWEQSIGKVispellhRTDLDPEVWDGSVGG 576

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   374 ETAIAELKAAIHRCQI----EAQEELKRFSDAAMRHEREQQEVINKMKESEKEKSMQVETLMSKLEDTRQRLvcSENRNR 449
Cdd:pfam12128  577 ELNLYGVKLDLKRIDVpewaASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTAL--KNARLD 654

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   450 LLEAQVSEEQLAFADAQKKLEELDLQVKRLQkDLDSEKQaareeawakvsALELEISAAVRDLDverqrhRGARERIMLR 529
Cdd:pfam12128  655 LRRLFDEKQSEKDKKNKALAERKDSANERLN-SLEAQLK-----------QLDKKHQAWLEEQK------EQKREARTEK 716

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 334184921   530 ETQMRAFYSTTE----EISALFAKQQEQLKTMQRTLEDEDNCDNTSLDID 575
Cdd:pfam12128  717 QAYWQVVEGALDaqlaLLKAAIAARRSGAKAELKALETWYKRDLASLGVD 766
FHA_SLMAP cd22679
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ...
 133-173 1.58e-03

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: 39.56  E-value: 1.58e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 334184921 133 DDVTVFMVDT-STNGTFLNWERLTKNGPEV---RVQHGDIISLAV 173
Cdd:cd22679   59 DDGKFYLQDTkSSNGTFVNNQRLSKGSEESeprELHSGDIVQFGV 103
VI_FHA TIGR03354
type VI secretion system FHA domain protein; Members of this protein family are FHA ...
 73-171 3.11e-03

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: 40.82  E-value: 3.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   73 VLTAISSNARKRRQGINILLTSDEHCLGRLP-CHASYQVESNAISGNHCKVfrkpvTGGDGddvTVFMVDTSTNGTFLNW 151
Cdd:TIGR03354   2 VLTVLNAHQLTPGIAAQKTFGTNGGTIGRSEdCDWVLPDPERHVSGRHARI-----RYRDG---AYLLTDLSTNGVFLNG 73

                          90       100
                  ....*....|....*....|..
gi 334184921  152 E--RLTKnGPEVRVQHGDIISL 171
Cdd:TIGR03354  74 SgsPLGR-GNPVRLEQGDRLRL 94
FHA_ArnA-like cd22680
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ...
 72-172 3.28e-03

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: 37.71  E-value: 3.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  72 GVLTAISSnarKRRQGINILLTSDEHCLGRLPcHASYQVESNAISGNHCKVFrkpVTGGdgddvTVFMVDT-STNGTFLN 150
Cdd:cd22680    1 LVLEILSS---PNLTGKKFPFDFSSVSIGRDP-ENVIVIPDPFVSRNHARIT---VDSN-----EIYIEDLgSTNGTFVN 68

                         90       100
                 ....*....|....*....|..
gi 334184921 151 WERLTKngPEVRVQHGDIISLA 172
Cdd:cd22680   69 DFKRIK--GPAKLHPNDIIKLG 88
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 279-486 4.00e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.91  E-value: 4.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 279 LHLQEIkqikestaksfHNELIELRDQLDTKQKELAQVNKLSAEQKNSIDELGERVSASLQTLSEANEVIQSQKASIAEL 358
Cdd:COG1579   10 LDLQEL-----------DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 359 KTGLDeernqrreeretaiaelkaaihrcQIEAQEELKrfsdaAMRHEREQQEV-INKMKESEKEKSMQVETLMSKLEDT 437
Cdd:COG1579   79 EEQLG------------------------NVRNNKEYE-----ALQKEIESLKRrISDLEDEILELMERIEELEEELAEL 129

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 334184921 438 RQRLvcsENRNRLLEAQVSEEQLAFADAQKKLEELDLQVKRLQKDLDSE 486
Cdd:COG1579  130 EAEL---AELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPE 175
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 327-562 4.01e-03

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 40.44  E-value: 4.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  327 IDELGERVSASLQTLSEANEVIQSQKASIAELKTGLdeerNQRREERETAIAELKAAIHRCQiEAQEELKRFSDAAMRHE 406
Cdd:pfam19220  22 LRSLKADFSQLIEPIEAILRELPQAKSRLLELEALL----AQERAAYGKLRRELAGLTRRLS-AAEGELEELVARLAKLE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  407 ---REQQEVINKMKESEKEKSMQVETLMSKL--EDTRQRLVCSENRNRLLEAQVSEEQLA-----FADAQKKLEELDLQV 476
Cdd:pfam19220  97 aalREAEAAKEELRIELRDKTAQAEALERQLaaETEQNRALEEENKALREEAQAAEKALQraegeLATARERLALLEQEN 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  477 KRLQKDLD-------------SEKQAAREEAWAKVSALELEISA-------AVRDLDVERQRHRGARERIMLRETQMRAF 536
Cdd:pfam19220 177 RRLQALSEeqaaelaeltrrlAELETQLDATRARLRALEGQLAAeqaererAEAQLEEAVEAHRAERASLRMKLEALTAR 256

                         250       260
                  ....*....|....*....|....*.
gi 334184921  537 YSTTEEISALFAKQQEQLKTMQRTLE 562
Cdd:pfam19220 257 AAATEQLLAEARNQLRDRDEAIRAAE 282
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 405-564 4.25e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 40.88  E-value: 4.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  405 HEREQQEVINKMKESEKEKSMQVETLMSKLEDTRQRLvcsENRNRLLEAQVS-----EEQLA-FADAQKKLEELDLQVKR 478
Cdd:pfam17380 276 HIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREV---ERRRKLEEAEKArqaemDRQAAiYAEQERMAMERERELER 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  479 LQKDldsEKQAAREEAWAKVSALELEISAAVRDLDVERQRH--------RGARERIMLRETQMRAFYSTTEEISALFAKQ 550
Cdd:pfam17380 353 IRQE---ERKRELERIRQEEIAMEISRMRELERLQMERQQKnervrqelEAARKVKILEEERQRKIQQQKVEMEQIRAEQ 429

                         170
                  ....*....|....
gi 334184921  551 QEQLKTMQRTLEDE 564
Cdd:pfam17380 430 EEARQREVRRLEEE 443
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 390-564 4.59e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.93  E-value: 4.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   390 EAQEELKRFSDAAMRHEREQQEVINKMKESEK-----------------EKSMQVETLMSKLEDTRQRLVCSENRNRLLE 452
Cdd:pfam01576  170 EEEEKAKSLSKLKNKHEAMISDLEERLKKEEKgrqelekakrklegestDLQEQIAELQAQIAELRAQLAKKEEELQAAL 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   453 AQVSEEQLAFADAQKKLEELDLQVKRLQKDLDSEKqAAREEAwakvsaleleisaavrdldvERQRhRGARERIMLRETQ 532
Cdd:pfam01576  250 ARLEEETAQKNNALKKIRELEAQISELQEDLESER-AARNKA--------------------EKQR-RDLGEELEALKTE 307

                          170       180       190
                   ....*....|....*....|....*....|..
gi 334184921   533 MRAFYSTTEEISALFAKQQEQLKTMQRTLEDE 564
Cdd:pfam01576  308 LEDTLDTTAAQQELRSKREQEVTELKKALEEE 339
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
410-526 5.36e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 40.61  E-value: 5.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 410 QEVINKMKESEKEKSMQVETLMS-----KLEDTRQRLVCSENRNRLLEAQVSEEQLAFADAQKKLEELDLQVKRLQKdld 484
Cdd:COG2433  379 EEALEELIEKELPEEEPEAEREKeheerELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARS--- 455

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 334184921 485 SEKQAAREEawAKVSALELEISAAVRDLDVERQRHRGARERI 526
Cdd:COG2433  456 EERREIRKD--REISRLDREIERLERELEEERERIEELKRKL 495
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 233-484 5.91e-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: 40.39  E-value: 5.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  233 SLQRSNTELRKQLEAQVLTIDTLRNESRS---IVEHHESDYLSISTEISLHLQEIKQIKestaksfhNELIELRDQLDTK 309
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEIKDLTNQDSVkelIIKNLDNTRESLETQLKVLSRSINKIK--------QNLEQKQKELKSK 494

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  310 QKELAQVNKLSAEQKNSIDELGERVSASLQTLSEANEVIQSQKASIAELKTGLDEERNQRREEretaiaELKAAIHRCQI 389
Cdd:TIGR04523 495 EKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKE------NLEKEIDEKNK 568

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  390 EAqEELKRFSDAAMRHEREQQEVINKMKESEKEKSMQVETLMSKLEDTRQRLVCSENRNRLLEAQVSeeqlafaDAQKKL 469
Cdd:TIGR04523 569 EI-EELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIK-------NIKSKK 640

                         250
                  ....*....|....*
gi 334184921  470 EELDLQVKRLQKDLD 484
Cdd:TIGR04523 641 NKLKQEVKQIKETIK 655
FHA_Kanadaptin cd22677
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ...
 97-169 6.18e-03

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: 37.15  E-value: 6.18e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334184921  97 HCLGRLP-CHasYQVESNAISGNHCKV-FRKPVTGGDGDdvtVFMVDT-STNGTFLNWERLTKNGPeVRVQHGDII 169
Cdd:cd22677   24 YVFGRLPgCD--VVLEHPSISRYHAVLqYRGDADDHDGG---FYLYDLgSTHGTFLNKQRIPPKQY-YRLRVGHVL 93
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 301-517 6.51e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.54  E-value: 6.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   301 ELRDQLDT----------KQKELAQVNKLSAEQKNS----IDELGERVSASLQTLSEANEVIQSQKASIAELKTGLDEER 366
Cdd:pfam01576  307 ELEDTLDTtaaqqelrskREQEVTELKKALEEETRSheaqLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESEN 386

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   367 NQRREERET-AIAELKAAIHRCQIEAQ-EELKRFSDAAMRHEREQQEVINKMKE---------SEKEK-----SMQVETL 430
Cdd:pfam01576  387 AELQAELRTlQQAKQDSEHKRKKLEGQlQELQARLSESERQRAELAEKLSKLQSelesvssllNEAEGkniklSKDVSSL 466

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921   431 MSKLED--------TRQRLVCS-------ENRNRL-------------LEAQVSEEQLAFADAQKKLEELDLQV------ 476
Cdd:pfam01576  467 ESQLQDtqellqeeTRQKLNLStrlrqleDERNSLqeqleeeeeakrnVERQLSTLQAQLSDMKKKLEEDAGTLealeeg 546

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 334184921   477 -KRLQKDLDS------EKQAAREEAWAKVSALELEISAAVRDLDVERQ 517
Cdd:pfam01576  547 kKRLQRELEAltqqleEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQ 594
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 302-558 6.96e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 40.06  E-value: 6.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  302 LRDQLDTKQKELAQV-NKLSAEQ----------KNSIDELG------ERVSASLQTLSEANEVIQSQKASIAELkTGLDE 364
Cdd:pfam05622 181 LRGQLETYKRQVQELhGKLSEESkkadklefeyKKLEEKLEalqkekERLIIERDTLRETNEELRCAQLQQAEL-SQADA 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  365 ERNQRREERETAIAELKAAihrcqiEAQEELKRfsdaaMRHE----REQQEvinkmkESEKEKSMQVETLmskLEDTRQR 440
Cdd:pfam05622 260 LLSPSSDPGDNLAAEIMPA------EIREKLIR-----LQHEnkmlRLGQE------GSYRERLTELQQL---LEDANRR 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921  441 LVCSENRNRL-------LEAQVSEEQLAFADA-----------------QKKLEELDLQVKRLQKDLDSEKQAAREEAWA 496
Cdd:pfam05622 320 KNELETQNRLanqrileLQQQVEELQKALQEQgskaedssllkqkleehLEKLHEAQSELQKKKEQIEELEPKQDSNLAQ 399

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334184921  497 KVSALELEISAAVRDLDVERQRHR----GARERImlRETQMRAFYSTTEEISALFAKQQEQLKTMQ 558
Cdd:pfam05622 400 KIDELQEALRKKDEDMKAMEERYKkyveKAKSVI--KTLDPKQNPASPPEIQALKNQLLEKDKKIE 463
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 450-561 8.03e-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: 39.75  E-value: 8.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 450 LLEAQVSEEQLAFADAQKKLEELDLQVKRLQKDLDsEKQAAREEAWAKVSALELEISAAVRDLDVERQRHRGARERImlR 529
Cdd:COG4942   10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELA-ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL--A 86

                         90       100       110
                 ....*....|....*....|....*....|..
gi 334184921 530 ETQMRAfysttEEISALFAKQQEQLKTMQRTL 561
Cdd:COG4942   87 ELEKEI-----AELRAELEAQKEELAELLRAL 113
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
240-435 8.90e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.12  E-value: 8.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 240 ELRKQLEAQVLTIDTLRNESRSIVEHHESDYLSISTEISLhLQEIKQIKES-----TAKSFHNELIELRDQLDTKQKELA 314
Cdd:COG1340   99 KELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKEL-VEKIKELEKElekakKALEKNEKLKELRAELKELRKEAE 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184921 315 QVNKLSAEQKNSIDELGERVSASLQTLSEANEVIQSQKASIAELKTGLDeernqrreeretaiaelkaAIHRCQIEAQEE 394
Cdd:COG1340  178 EIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKAD-------------------ELHEEIIELQKE 238

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 334184921 395 LKRFSDAAMRHEREQQEVinKMKESEKEKSMQVETLMSKLE 435
Cdd:COG1340  239 LRELRKELKKLRKKQRAL--KREKEKEELEEKAEEIFEKLK 277
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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