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Conserved domains on  [gi|1207192617|ref|XP_021329124|]
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epidermal growth factor receptor substrate 15-like 1 isoform X5 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 120-213 1.70e-39

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


:

Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 141.26  E-value: 1.70e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  120 WAVRPEEKSKFDGIFESLAP-VNGLLSGEKVKPVLINSKLPVDVLGKVWDLSDIDKDGHLDRDEFAVAMHLVYRALEKEP 198
Cdd:smart00027   2 WAISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYP 81

                           90
                   ....*....|....*
gi 1207192617  199 VPSVLPSSLIPPSKR 213
Cdd:smart00027  82 IPASLPPSLIPPSKR 96
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 270-366 1.01e-35

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


:

Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 130.48  E-value: 1.01e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  270 NWVVPVADRGRYDDIFLKTDTDLDGFVSGLEVKDIFMQSGLHQNLLAHIWALADTRQMGKLTREQFSLAMYLIQQKVSkG 349
Cdd:smart00027   1 PWAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLN-G 79

                           90
                   ....*....|....*..
gi 1207192617  350 LDPPQALTPDMIPPSER 366
Cdd:smart00027  80 YPIPASLPPSLIPPSKR 96
EH super family cl42943
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 11-101 2.10e-23

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


The actual alignment was detected with superfamily member smart00027:

Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 95.42  E-value: 2.10e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617   11 SSGNPVYENFYRQVDPGNTGRVGPTEAALFLKKSGLPDITLGKIWDLADPDGKGFLDKQGFYVALRLVACAQSGHDISIS 90
Cdd:smart00027   6 PEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIPAS 85

                           90
                   ....*....|.
gi 1207192617   91 SLNLPVPPPKF 101
Cdd:smart00027  86 LPPSLIPPSKR 96
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 418-604 1.68e-21

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: 100.78  E-value: 1.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 418 DISQEIAQLQSTLAFTHWDTLREKY-TLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQ 496
Cdd:COG1196   217 ELKEELKELEAELLLLKLRELEAELeELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 497 KAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKA 576
Cdd:COG1196   297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376

                         170       180
                  ....*....|....*....|....*...
gi 1207192617 577 TQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:COG1196   377 AEEELEELAEELLEALRAAAELAAQLEE 404
PTZ00395 super family cl33180
Sec24-related protein; Provisional
 657-774 2.02e-05

Sec24-related protein; Provisional


The actual alignment was detected with superfamily member PTZ00395:

Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 48.53  E-value: 2.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  657 HTDPFQSEDPFKTDPFKGDPFQNDPFSKPATTVPdPFGGDPFKETdpfrtssedffkkPSKPDPFTNADPfSKSATLPSK 736
Cdd:PTZ00395   419 NSNPGYNNAPNSNTPYNNPPNSNTPYSNPPNSNP-PYSNLPYSNT-------------PYSNAPLSNAPP-SSAKDHHSA 483

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207192617  737 SH----HFASNDPF--ISTSPKPKGQDFFGTLD----------PFGSSTFGSNS 774
Cdd:PTZ00395   484 YHaayqHRAANQPAanLPTANQPAANNFHGAAGnsvgnpfasrPFGSAPYGGNA 537
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 625-870 5.36e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.99  E-value: 5.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 625 EGFPEKENGGFGAMedPFKVKPTVFNSAPQEMHTDPFQSEDPFKTDPfKGDPFQNDPFS----KPATTVPDPFGGDPFKE 700
Cdd:pfam03154 296 QPFPLTPQSSQSQV--PPGPSPAAPGQSQQRIHTPPSQSQLQSQQPP-REQPLPPAPLSmphiKPPPTTPIPQLPNPQSH 372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 701 TDPFRTSSEDFFKKPSKPDPFTNADPFSKSATLPSKSHH------FASNDPFISTSPKPKGQDFFGTLDPFGSSTFGSNS 774
Cdd:pfam03154 373 KHPPHLSGPSPFQMNSNLPPPPALKPLSSLSTHHPPSAHppplqlMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSG 452

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 775 GFADFSQmskgfveDPFSRKQDMPALPPKKSIPPRPKPPSGKSTPVNVPGSGDPAKTSDPFQPFSADPVDPFQCKKGVGD 854
Cdd:pfam03154 453 LHQVPSQ-------SPFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIKEEALD 525

                         250
                  ....*....|....*.
gi 1207192617 855 pfSGKDPFAPSAPSKA 870
Cdd:pfam03154 526 --EAEEPESPPPPPRS 539
 
Name Accession Description Interval E-value
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 120-213 1.70e-39

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 141.26  E-value: 1.70e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  120 WAVRPEEKSKFDGIFESLAP-VNGLLSGEKVKPVLINSKLPVDVLGKVWDLSDIDKDGHLDRDEFAVAMHLVYRALEKEP 198
Cdd:smart00027   2 WAISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYP 81

                           90
                   ....*....|....*
gi 1207192617  199 VPSVLPSSLIPPSKR 213
Cdd:smart00027  82 IPASLPPSLIPPSKR 96
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 270-366 1.01e-35

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 130.48  E-value: 1.01e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  270 NWVVPVADRGRYDDIFLKTDTDLDGFVSGLEVKDIFMQSGLHQNLLAHIWALADTRQMGKLTREQFSLAMYLIQQKVSkG 349
Cdd:smart00027   1 PWAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLN-G 79

                           90
                   ....*....|....*..
gi 1207192617  350 LDPPQALTPDMIPPSER 366
Cdd:smart00027  80 YPIPASLPPSLIPPSKR 96
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
 124-213 1.91e-26

Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.


Pssm-ID: 289529  Cd Length: 104  Bit Score: 104.38  E-value: 1.91e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 124 PEEKSKFDGIFESLAPVNGLLSGEKVKPVLINSKLPVDVLGKVWDLSDIDKDGHLDRDEFAVAMHLVYRALEKE--PVPS 201
Cdd:pfam12763   6 EWEIKKYWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNiaDVPD 85

                          90
                  ....*....|..
gi 1207192617 202 VLPSSLIPPSKR 213
Cdd:pfam12763  86 ELPDWLVPGSKA 97
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 130-195 6.66e-25

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 98.45  E-value: 6.66e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207192617 130 FDGIFESLAPVN-GLLSGEKVKPVLINSKLPVDVLGKVWDLSDIDKDGHLDRDEFAVAMHLVYRALE 195
Cdd:cd00052     1 YDQIFRSLDPDGdGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 281-347 2.27e-24

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 96.91  E-value: 2.27e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207192617 281 YDDIFLKTDTDLDGFVSGLEVKDIFMQSGLHQNLLAHIWALADTRQMGKLTREQFSLAMYLIQQKVS 347
Cdd:cd00052     1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 11-101 2.10e-23

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 95.42  E-value: 2.10e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617   11 SSGNPVYENFYRQVDPGNTGRVGPTEAALFLKKSGLPDITLGKIWDLADPDGKGFLDKQGFYVALRLVACAQSGHDISIS 90
Cdd:smart00027   6 PEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIPAS 85

                           90
                   ....*....|.
gi 1207192617   91 SLNLPVPPPKF 101
Cdd:smart00027  86 LPPSLIPPSKR 96
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 17-83 4.52e-22

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 90.36  E-value: 4.52e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207192617  17 YENFYRQVDPGNTGRVGPTEAALFLKKSGLPDITLGKIWDLADPDGKGFLDKQGFYVALRLVACAQS 83
Cdd:cd00052     1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 418-604 1.68e-21

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 100.78  E-value: 1.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 418 DISQEIAQLQSTLAFTHWDTLREKY-TLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQ 496
Cdd:COG1196   217 ELKEELKELEAELLLLKLRELEAELeELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 497 KAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKA 576
Cdd:COG1196   297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376

                         170       180
                  ....*....|....*....|....*...
gi 1207192617 577 TQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:COG1196   377 AEEELEELAEELLEALRAAAELAAQLEE 404
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 414-611 3.62e-19

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: 93.58  E-value: 3.62e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  414 KELDDISQEIAQLQSTLAFTH--WDTLREK-YTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRL 490
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEkaLAELRKElEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  491 EEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETI 570
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1207192617  571 IKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLNG 611
Cdd:TIGR02168  837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
415-614 1.13e-10

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 65.45  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 415 ELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDREtsslqelEAQKQDAQDRLEEMD 494
Cdd:PRK02224  252 ELETLEAEIEDLRETIA----ETEREREELAEEVRDLRERLEELEEERDDLLAEAGLD-------DADAEAVEARREELE 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 495 QQKAKLEDMLNDVRQKCQEESQMISSLQTQIhsqeSDLQSQEEElgrakadlnrLQQEEAQLEQSLQAGRIQLETIIKSL 574
Cdd:PRK02224  321 DRDEELRDRLEECRVAAQAHNEEAESLREDA----DDLEERAEE----------LREEAAELESELEEAREAVEDRREEI 386

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1207192617 575 KATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLNGTHG 614
Cdd:PRK02224  387 EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRE 426
Filament pfam00038
Intermediate filament protein;
414-610 7.97e-10

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 61.09  E-value: 7.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEIAQLQSTL--AFTHWDTLREKYTLEQDIRETEEAirhkttEVQEMQNDLDRETSSLQELEAQKQDAQDRL- 490
Cdd:pfam00038  61 RQLDTLTVERARLQLELdnLRLAAEDFRQKYEDELNLRTSAEN------DLVGLRKDLDEATLARVDLEAKIESLKEELa 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 491 -------EEMDQQKAKLED-----------------MLNDVR-------QKCQEESQM-----ISSLQTQIHSQESDLQS 534
Cdd:pfam00038 135 flkknheEEVRELQAQVSDtqvnvemdaarkldltsALAEIRaqyeeiaAKNREEAEEwyqskLEELQQAAARNGDALRS 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 535 QEEELgrakADLNR-LQQEEAQLeQSLQAGRIQLETIIKSLKATQD-EINQARSKLS----QIQDSQHEISKNIEQYSST 608
Cdd:pfam00038 215 AKEEI----TELRRtIQSLEIEL-QSLKKQKASLERQLAETEERYElQLADYQELISeleaELQETRQEMARQLREYQEL 289


                  ..
gi 1207192617 609 LN 610
Cdd:pfam00038 290 LN 291
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 440-601 1.00e-07

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 53.60  E-value: 1.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 440 EKYTLEQDIRETEEAIRHKTTEVQEMQNDLDretssLQELEAQKQDAQDRLEEMDQQKAKLEDML---NDVRQKCQEESQ 516
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDD-----LESVEALLKKHEALEAELAAHEERVEALNelgEQLIEEGHPDAE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 517 MISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQ---EEAQLEQSLQAGRIQLETI------------IKSLKATQDEI 581
Cdd:cd00176    76 EIQERLEELNQRWEELRELAEERRQRLEEALDLQQffrDADDLEQWLEEKEAALASEdlgkdlesveelLKKHKELEEEL 155

                         170       180
                  ....*....|....*....|
gi 1207192617 582 NQARSKLSQIQDSQHEISKN 601
Cdd:cd00176   156 EAHEPRLKSLNELAEELLEE 175
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
 17-78 2.20e-07

Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.


Pssm-ID: 289529  Cd Length: 104  Bit Score: 50.06  E-value: 2.20e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207192617  17 YENFYRQVDPGNtGRVGPTEAALFLKKSGLPDITLGKIWDLADPDGKGFLDKQGFYVALRLV 78
Cdd:pfam12763  12 YWEIFSGLKPEN-NKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLI 72
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 476-608 4.28e-06

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 49.63  E-value: 4.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  476 LQELEAQKQDAQDRLEEMDQQKAKL---EDMLNDVRQKCQEESQMISSLQTQIHSQESDLQS-QEEELGRAKADLNRLQQ 551
Cdd:smart00787 139 MKLLEGLKEGLDENLEGLKEDYKLLmkeLELLNSIKPKLRDRKDALEEELRQLKQLEDELEDcDPTELDRAKEKLKKLLQ 218

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207192617  552 E-------EAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQD-SQHEISKNIEQYSST 608
Cdd:smart00787 219 EimikvkkLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGfTFKEIEKLKEQLKLL 283
PTZ00395 PTZ00395
Sec24-related protein; Provisional
 657-774 2.02e-05

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 48.53  E-value: 2.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  657 HTDPFQSEDPFKTDPFKGDPFQNDPFSKPATTVPdPFGGDPFKETdpfrtssedffkkPSKPDPFTNADPfSKSATLPSK 736
Cdd:PTZ00395   419 NSNPGYNNAPNSNTPYNNPPNSNTPYSNPPNSNP-PYSNLPYSNT-------------PYSNAPLSNAPP-SSAKDHHSA 483

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207192617  737 SH----HFASNDPF--ISTSPKPKGQDFFGTLD----------PFGSSTFGSNS 774
Cdd:PTZ00395   484 YHaayqHRAANQPAanLPTANQPAANNFHGAAGnsvgnpfasrPFGSAPYGGNA 537
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
 293-366 6.41e-05

Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.


Pssm-ID: 289529  Cd Length: 104  Bit Score: 42.75  E-value: 6.41e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207192617 293 DGFVSGLEVKDIFMQSGLHQNLLAHIWALADTRQMGKLTREQFSLAMYLIQQKVSKGL-DPPQALTPDMIPPSER 366
Cdd:pfam12763  23 NNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNIaDVPDELPDWLVPGSKA 97
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 625-870 5.36e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.99  E-value: 5.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 625 EGFPEKENGGFGAMedPFKVKPTVFNSAPQEMHTDPFQSEDPFKTDPfKGDPFQNDPFS----KPATTVPDPFGGDPFKE 700
Cdd:pfam03154 296 QPFPLTPQSSQSQV--PPGPSPAAPGQSQQRIHTPPSQSQLQSQQPP-REQPLPPAPLSmphiKPPPTTPIPQLPNPQSH 372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 701 TDPFRTSSEDFFKKPSKPDPFTNADPFSKSATLPSKSHH------FASNDPFISTSPKPKGQDFFGTLDPFGSSTFGSNS 774
Cdd:pfam03154 373 KHPPHLSGPSPFQMNSNLPPPPALKPLSSLSTHHPPSAHppplqlMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSG 452

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 775 GFADFSQmskgfveDPFSRKQDMPALPPKKSIPPRPKPPSGKSTPVNVPGSGDPAKTSDPFQPFSADPVDPFQCKKGVGD 854
Cdd:pfam03154 453 LHQVPSQ-------SPFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIKEEALD 525

                         250
                  ....*....|....*.
gi 1207192617 855 pfSGKDPFAPSAPSKA 870
Cdd:pfam03154 526 --EAEEPESPPPPPRS 539
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
141-188 7.84e-03

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.85  E-value: 7.84e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1207192617 141 NGLLSGEKVKPVLINSKLPVDVLGKVWDLSDIDKDGHLDRDEFAVAMH 188
Cdd:COG5126    83 DGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVR 130
 
Name Accession Description Interval E-value
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 120-213 1.70e-39

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 141.26  E-value: 1.70e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  120 WAVRPEEKSKFDGIFESLAP-VNGLLSGEKVKPVLINSKLPVDVLGKVWDLSDIDKDGHLDRDEFAVAMHLVYRALEKEP 198
Cdd:smart00027   2 WAISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYP 81

                           90
                   ....*....|....*
gi 1207192617  199 VPSVLPSSLIPPSKR 213
Cdd:smart00027  82 IPASLPPSLIPPSKR 96
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 270-366 1.01e-35

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 130.48  E-value: 1.01e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  270 NWVVPVADRGRYDDIFLKTDTDLDGFVSGLEVKDIFMQSGLHQNLLAHIWALADTRQMGKLTREQFSLAMYLIQQKVSkG 349
Cdd:smart00027   1 PWAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLN-G 79

                           90
                   ....*....|....*..
gi 1207192617  350 LDPPQALTPDMIPPSER 366
Cdd:smart00027  80 YPIPASLPPSLIPPSKR 96
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
 124-213 1.91e-26

Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.


Pssm-ID: 289529  Cd Length: 104  Bit Score: 104.38  E-value: 1.91e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 124 PEEKSKFDGIFESLAPVNGLLSGEKVKPVLINSKLPVDVLGKVWDLSDIDKDGHLDRDEFAVAMHLVYRALEKE--PVPS 201
Cdd:pfam12763   6 EWEIKKYWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNiaDVPD 85

                          90
                  ....*....|..
gi 1207192617 202 VLPSSLIPPSKR 213
Cdd:pfam12763  86 ELPDWLVPGSKA 97
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 130-195 6.66e-25

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 98.45  E-value: 6.66e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207192617 130 FDGIFESLAPVN-GLLSGEKVKPVLINSKLPVDVLGKVWDLSDIDKDGHLDRDEFAVAMHLVYRALE 195
Cdd:cd00052     1 YDQIFRSLDPDGdGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 281-347 2.27e-24

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 96.91  E-value: 2.27e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207192617 281 YDDIFLKTDTDLDGFVSGLEVKDIFMQSGLHQNLLAHIWALADTRQMGKLTREQFSLAMYLIQQKVS 347
Cdd:cd00052     1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 11-101 2.10e-23

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 95.42  E-value: 2.10e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617   11 SSGNPVYENFYRQVDPGNTGRVGPTEAALFLKKSGLPDITLGKIWDLADPDGKGFLDKQGFYVALRLVACAQSGHDISIS 90
Cdd:smart00027   6 PEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIPAS 85

                           90
                   ....*....|.
gi 1207192617   91 SLNLPVPPPKF 101
Cdd:smart00027  86 LPPSLIPPSKR 96
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 17-83 4.52e-22

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 90.36  E-value: 4.52e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207192617  17 YENFYRQVDPGNTGRVGPTEAALFLKKSGLPDITLGKIWDLADPDGKGFLDKQGFYVALRLVACAQS 83
Cdd:cd00052     1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 418-604 1.68e-21

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 100.78  E-value: 1.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 418 DISQEIAQLQSTLAFTHWDTLREKY-TLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQ 496
Cdd:COG1196   217 ELKEELKELEAELLLLKLRELEAELeELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 497 KAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKA 576
Cdd:COG1196   297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376

                         170       180
                  ....*....|....*....|....*...
gi 1207192617 577 TQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:COG1196   377 AEEELEELAEELLEALRAAAELAAQLEE 404
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
411-595 2.47e-19

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 91.12  E-value: 2.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 411 TGIKELDDISQEIAQLQSTLAfthwdtlrekyTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRL 490
Cdd:COG4372    35 KALFELDKLQEELEQLREELE-----------QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 491 EEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQagRIQLETI 570
Cdd:COG4372   104 ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ--ALSEAEA 181

                         170       180
                  ....*....|....*....|....*
gi 1207192617 571 IKSLKATQDEINQARSKLSQIQDSQ 595
Cdd:COG4372   182 EQALDELLKEANRNAEKEEELAEAE 206
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 414-611 3.62e-19

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: 93.58  E-value: 3.62e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  414 KELDDISQEIAQLQSTLAFTH--WDTLREK-YTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRL 490
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEkaLAELRKElEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  491 EEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETI 570
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1207192617  571 IKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLNG 611
Cdd:TIGR02168  837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 418-610 3.81e-18

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 90.12  E-value: 3.81e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  418 DISQEIAQLQSTLAFTHWDTLREKY-TLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQ 496
Cdd:TIGR02168  217 ELKAELRELELALLVLRLEELREELeELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  497 KAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKA 576
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1207192617  577 TQDEINQARSKLSQIQDSQHEISKNIEQYSSTLN 610
Cdd:TIGR02168  377 LEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 414-604 7.68e-18

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 88.84  E-value: 7.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM 493
Cdd:COG1196   267 AELEELRLELEELELELE----EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 494 DQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKS 573
Cdd:COG1196   343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1207192617 574 LKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:COG1196   423 LEELEEALAELEEEEEEEEEALEEAAEEEAE 453
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
448-606 2.87e-17

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 84.57  E-value: 2.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 448 IRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQkakledmLNDVRQKCQEESQMISSLQTQIHS 527
Cdd:COG4372    26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSE-------LEQLEEELEELNEQLQAAQAELAQ 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207192617 528 QESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYS 606
Cdd:COG4372    99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS 177
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 414-604 1.11e-16

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 85.37  E-value: 1.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM 493
Cdd:COG1196   239 AELEELEAELEELEAELE----ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 494 DQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKS 573
Cdd:COG1196   315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1207192617 574 LKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:COG1196   395 AAELAAQLEELEEAEEALLERLERLEEELEE 425
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 415-604 1.97e-16

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 84.22  E-value: 1.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 415 ELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMD 494
Cdd:COG1196   275 ELEELELELEEAQAEEY----ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 495 QQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSL 574
Cdd:COG1196   351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430

                         170       180       190
                  ....*....|....*....|....*....|
gi 1207192617 575 KATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:COG1196   431 AELEEEEEEEEEALEEAAEEEAELEEEEEA 460
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 414-604 4.61e-16

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: 80.96  E-value: 4.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEm 493
Cdd:COG4942    27 AELEQLQQEIAELEKELA----ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA- 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 494 dqQKAKLEDMLN-----------DVRQKCQEESQMISSLQ-------------TQIHSQESDLQSQEEELGRAKADLNRL 549
Cdd:COG4942   102 --QKEELAELLRalyrlgrqpplALLLSPEDFLDAVRRLQylkylaparreqaEELRADLAELAALRAELEAERAELEAL 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1207192617 550 QQEEAQLEQSLQAGRIQLETIIKSLKAtqdEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:COG4942   180 LAELEEERAALEALKAERQKLLARLEK---ELAELAAELAELQQEAEELEALIAR 231
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 385-604 1.56e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 81.52  E-value: 1.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 385 AALTEMRRAIMfKLWDSSSSVGSGEFTGIKELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQE 464
Cdd:COG1196   267 AELEELRLELE-ELELELEEAQAEEYELLAELARLEQDIARLEERRR----ELEERLEELEEELAELEEELEELEEELEE 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 465 MQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKA 544
Cdd:COG1196   342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 545 DLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:COG1196   422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
413-609 5.32e-15

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 79.43  E-value: 5.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 413 IKELDDISQEIAQLQSTLAftHWDTLREKY-TLEQDIRETEEAIRHKTTEVQEMQNDLDRET--SSLQELEAQKQDAQDR 489
Cdd:COG4717    70 LKELKELEEELKEAEEKEE--EYAELQEELeELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPER 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 490 LEEMDQQKAKLEDMLNDVRQKCQEesqmISSLQTQIHSQESDL-QSQEEELGRAKADLNRLQQEEAQLEQslqagriqle 568
Cdd:COG4717   148 LEELEERLEELRELEEELEELEAE----LAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEE---------- 213

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1207192617 569 tiikSLKATQDEINQARSKLSQIQDSQ--HEISKNIEQYSSTL 609
Cdd:COG4717   214 ----ELEEAQEELEELEEELEQLENELeaAALEERLKEARLLL 252
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 414-604 6.52e-15

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 79.72  E-value: 6.52e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  414 KELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM 493
Cdd:TIGR02168  239 EELEELQEELKEAEEELE----ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  494 DQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADL----NRLQQEEAQLEQsLQAGRIQLEt 569
Cdd:TIGR02168  315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELeeleSRLEELEEQLET-LRSKVAQLE- 392

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1207192617  570 iiKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:TIGR02168  393 --LQIASLNNEIERLEARLERLEDRRERLQQEIEE 425
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
443-632 7.90e-15

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 77.25  E-value: 7.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 443 TLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQ 522
Cdd:COG4372    28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 523 TQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIqdSQHEISKNI 602
Cdd:COG4372   108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL--SEAEAEQAL 185

                         170       180       190
                  ....*....|....*....|....*....|
gi 1207192617 603 EQYSSTLNGTHGGSMTNLADMSEGFPEKEN 632
Cdd:COG4372   186 DELLKEANRNAEKEEELAEAEKLIESLPRE 215
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 444-588 1.47e-14

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: 74.19  E-value: 1.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 444 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVR-----QKCQEEsqmI 518
Cdd:COG1579    22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeyEALQKE---I 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 519 SSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKL 588
Cdd:COG1579    99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 414-604 9.51e-14

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 75.86  E-value: 9.51e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  414 KELDDISQEIAQLQSTLAFTH--WDTLR-EKYTLEQDIRETEEA-------IRHKTTEVQEMQNDLDRETSSLQELEAQK 483
Cdd:TIGR02168  246 EELKEAEEELEELTAELQELEekLEELRlEVSELEEEIEELQKElyalaneISRLEQQKQILRERLANLERQLEELEAQL 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  484 QDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAG 563
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1207192617  564 RIQLETIIKSLKATQDEINQARSKLS--QIQDSQHEISKNIEQ 604
Cdd:TIGR02168  406 EARLERLEDRRERLQQEIEELLKKLEeaELKELQAELEELEEE 448
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 413-606 1.65e-13

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 75.10  E-value: 1.65e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  413 IKELDDISQEIAQLQSTLAFTHwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDREtssLQELEAQKQDAQDRLEE 492
Cdd:TIGR02169  694 QSELRRIENRLDELSQELSDAS-RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE---IENVKSELKELEARIEE 769

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  493 MDQQKAKLEDMLNDVRQKCQEESqmISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLE---QSLQAGRIQLET 569
Cdd:TIGR02169  770 LEEDLHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEkeiQELQEQRIDLKE 847

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1207192617  570 IIKSLKATQDEIN-QARSKLSQIQDSQHEISKNIEQYS 606
Cdd:TIGR02169  848 QIKSIEKEIENLNgKKEELEEELEELEAALRDLESRLG 885
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 406-610 4.20e-13

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 73.56  E-value: 4.20e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  406 GSGEFTGIKE-LDDISQEIAQLQSTLAFTH---WDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEA 481
Cdd:TIGR02169  285 GEEEQLRVKEkIGELEAEIASLERSIAEKErelEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE 364

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  482 QKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLq 561
Cdd:TIGR02169  365 ELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK- 443

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1207192617  562 agriqletiikslKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLN 610
Cdd:TIGR02169  444 -------------EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD 479
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
414-604 1.92e-12

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 71.48  E-value: 1.92e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  414 KELDDISQEIAQLQSTLAftHWDTLREKYTLEQDIRETEEAIRHKT--TEVQEMQNDLDRETSSLQELEAQKQDAQDRLE 491
Cdd:COG4913    242 EALEDAREQIELLEPIRE--LAERYAAARERLAELEYLRAALRLWFaqRRLELLEAELEELRAELARLEAELERLEARLD 319

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  492 EMDQQKAKLEdmlndvRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQ----L 567
Cdd:COG4913    320 ALREELDELE------AQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEaaalL 393

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1207192617  568 ETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:COG4913    394 EALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 414-602 2.67e-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: 71.24  E-value: 2.67e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  414 KELDDISQEIAQLQSTLAFThwdtLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQK-------QDA 486
Cdd:TIGR02168  719 KELEELSRQISALRKDLARL----EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIeeleaqiEQL 794

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  487 QDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQ 566
Cdd:TIGR02168  795 KEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE 874

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1207192617  567 LETIIKSLKATQDEINQARSKLSQIQDSQHEISKNI 602
Cdd:TIGR02168  875 LEALLNERASLEEALALLRSELEELSEELRELESKR 910
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 414-604 6.89e-12

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: 69.28  E-value: 6.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEIAQLQSTLAfthwdtlrekyTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM 493
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIIS-----------QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 494 DQQKakledmlNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAgriqLETIIKS 573
Cdd:TIGR04523 390 ESQI-------NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSV----KELIIKN 458

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1207192617 574 LKATQDEINQarsKLSQIQDSQHEISKNIEQ 604
Cdd:TIGR04523 459 LDNTRESLET---QLKVLSRSINKIKQNLEQ 486
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
414-604 1.91e-11

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 68.40  E-value: 1.91e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  414 KELDDISQEIAQLQSTLA-FTHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQ-DRLE 491
Cdd:COG4913    262 ERYAAARERLAELEYLRAaLRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLE 341

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  492 EMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEElgrAKADLNRLQQEEAQLEQSLQAGRIQLETII 571
Cdd:COG4913    342 QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE---AAALLEALEEELEALEEALAEAEAALRDLR 418

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1207192617  572 KSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:COG4913    419 RELRELEAEIASLERRKSNIPARLLALRDALAE 451
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
431-605 3.43e-11

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 67.25  E-value: 3.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  431 AFTHWDT--LREKYTLEQDireTEEAIRHKTTEVQEMQNDLdretsslQELEAQKQDAQDRLEEMDQQKAKLEDMLNDvr 508
Cdd:COG4913    589 RHEKDDRrrIRSRYVLGFD---NRAKLAALEAELAELEEEL-------AEAEERLEALEAELDALQERREALQRLAEY-- 656

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  509 qkcQEESQMISSLQTQIhsqeSDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKL 588
Cdd:COG4913    657 ---SWDEIDVASAEREI----AELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729

                          170
                   ....*....|....*..
gi 1207192617  589 SQIQDSQHEISKNIEQY 605
Cdd:COG4913    730 DELQDRLEAAEDLARLE 746
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
413-592 5.03e-11

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 66.58  E-value: 5.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 413 IKELDDISQEIAQLQSTLAfthwdTLREKY-TLEQDIRETEEAIR--HKTTEVQEMQNDLDRETSSLQELEAQKQDAQDR 489
Cdd:COG3206   218 LQQLSELESQLAEARAELA-----EAEARLaALRAQLGSGPDALPelLQSPVIQQLRAQLAELEAELAELSARYTPNHPD 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 490 LEEMDQQKAKLEDMLNdvrqkcQEESQMISSLQTQI---HSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQ 566
Cdd:COG3206   293 VIALRAQIAALRAQLQ------QEAQRILASLEAELealQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVAREL 366

                         170       180
                  ....*....|....*....|....*.
gi 1207192617 567 LETIIKSLKATQDEINQARSKLSQIQ 592
Cdd:COG3206   367 YESLLQRLEEARLAEALTVGNVRVID 392
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 414-604 6.55e-11

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 66.63  E-value: 6.55e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  414 KELDDISQEIAQLQSTLafthwDTLREKY-TLEQDIRETEEAIRHKTTE----VQEMQNDLDRETSSLQELEAQKQDAQd 488
Cdd:TIGR02169  244 RQLASLEEELEKLTEEI-----SELEKRLeEIEQLLEELNKKIKDLGEEeqlrVKEKIGELEAEIASLERSIAEKEREL- 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  489 rlEEMDQQKAKLEDMLNDVRQKcqeesqmISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLE 568
Cdd:TIGR02169  318 --EDAEERLAKLEAEIDKLLAE-------IEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK 388

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1207192617  569 TIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:TIGR02169  389 DYREKLEKLKREINELKRELDRLQEELQRLSEELAD 424
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 413-593 6.65e-11

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: 66.20  E-value: 6.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 413 IKELDDISQEIAQLQStlafthwdtlrEKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEE 492
Cdd:TIGR04523 376 KKENQSYKQEIKNLES-----------QINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 493 MDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQagriQLETIIK 572
Cdd:TIGR04523 445 LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK----DLTKKIS 520

                         170       180
                  ....*....|....*....|....*
gi 1207192617 573 SLKATQD----EINQARSKLSQIQD 593
Cdd:TIGR04523 521 SLKEKIEklesEKKEKESKISDLED 545
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 414-562 6.91e-11

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: 63.41  E-value: 6.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEIAQLQSTLAfthwdtlrekyTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQK--QDAQDRLE 491
Cdd:COG1579    31 AELAELEDELAALEARLE-----------AAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEALQKEIE 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207192617 492 EMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELgraKADLNRLQQEEAQLEQSLQA 562
Cdd:COG1579   100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL---DEELAELEAELEELEAEREE 167
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 444-603 8.97e-11

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: 65.81  E-value: 8.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 444 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQT 523
Cdd:TIGR04523 129 LEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKK 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 524 QIH------SQESDLQSQEEELgraKADLNRLQQEEAQLEQSLQAGRIQLET-------IIKSLKATQDEINQARSKLSQ 590
Cdd:TIGR04523 209 KIQknksleSQISELKKQNNQL---KDNIEKKQQEINEKTTEISNTQTQLNQlkdeqnkIKKQLSEKQKELEQNNKKIKE 285

                         170
                  ....*....|...
gi 1207192617 591 IQDSQHEISKNIE 603
Cdd:TIGR04523 286 LEKQLNQLKSEIS 298
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 414-595 9.04e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.11  E-value: 9.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM 493
Cdd:COG1196   323 EELAELEEELEELEEELE----ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 494 DQQKAKLEDMLNDVRQKCQEESQMISSLQTQIH---SQESDLQSQEEElgrAKADLNRLQQEEAQLEQSLQAGRIQLETI 570
Cdd:COG1196   399 AAQLEELEEAEEALLERLERLEEELEELEEALAeleEEEEEEEEALEE---AAEEEAELEEEEEALLELLAELLEEAALL 475

                         170       180
                  ....*....|....*....|....*
gi 1207192617 571 IKSLKATQDEINQARSKLSQIQDSQ 595
Cdd:COG1196   476 EAALAELLEELAEAAARLLLLLEAE 500
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
415-614 1.13e-10

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 65.45  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 415 ELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDREtsslqelEAQKQDAQDRLEEMD 494
Cdd:PRK02224  252 ELETLEAEIEDLRETIA----ETEREREELAEEVRDLRERLEELEEERDDLLAEAGLD-------DADAEAVEARREELE 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 495 QQKAKLEDMLNDVRQKCQEESQMISSLQTQIhsqeSDLQSQEEElgrakadlnrLQQEEAQLEQSLQAGRIQLETIIKSL 574
Cdd:PRK02224  321 DRDEELRDRLEECRVAAQAHNEEAESLREDA----DDLEERAEE----------LREEAAELESELEEAREAVEDRREEI 386

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1207192617 575 KATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLNGTHG 614
Cdd:PRK02224  387 EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRE 426
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
414-599 2.96e-10

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 64.27  E-value: 2.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEIAQLQSTLafthwdtlrEKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLE-- 491
Cdd:COG3206   182 EQLPELRKELEEAEAAL---------EEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGsg 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 492 --------------EMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEE-LGRAKADLNRLQQEEAQL 556
Cdd:COG3206   253 pdalpellqspviqQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRiLASLEAELEALQAREASL 332

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1207192617 557 EQSLQagriQLETIIKSLKATQDEINQ-------ARSKLSQIQDSQHEIS 599
Cdd:COG3206   333 QAQLA----QLEARLAELPELEAELRRlerevevARELYESLLQRLEEAR 378
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 466-604 3.36e-10

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: 62.86  E-value: 3.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 466 QNDLDRETSS-LQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKA 544
Cdd:COG4942    18 QADAAAEAEAeLEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 545 DLNRLQQEEAQL-------------------EQSLQAGRI---------QLETIIKSLKATQDEINQARSKLSQIQDSQH 596
Cdd:COG4942    98 ELEAQKEELAELlralyrlgrqpplalllspEDFLDAVRRlqylkylapARREQAEELRADLAELAALRAELEAERAELE 177


                  ....*...
gi 1207192617 597 EISKNIEQ 604
Cdd:COG4942   178 ALLAELEE 185
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 416-604 4.29e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.80  E-value: 4.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 416 LDDISQEI-AQL-----QSTLAfthwdtlrEKYtleQDIRETEEAIrhkttEVQEMQNDLDRETSSLQELEAQKQDAQDR 489
Cdd:COG1196   191 LEDILGELeRQLeplerQAEKA--------ERY---RELKEELKEL-----EAELLLLKLRELEAELEELEAELEELEAE 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 490 LEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKAdlnRLQQEEAQLEQSLQagriQLET 569
Cdd:COG1196   255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE---RRRELEERLEELEE----ELAE 327

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1207192617 570 IIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:COG1196   328 LEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 413-608 4.34e-10

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 62.54  E-value: 4.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 413 IKELDDISQEIAQLQSTLafthwDTLREKY--------TLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQE------ 478
Cdd:COG3883    29 QAELEAAQAELDALQAEL-----EELNEEYnelqaeleALQAEIDKLQAEIAEAEAEIEERREELGERARALYRsggsvs 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 479 -----LEAQK-QDAQDRLEEMDQQKAKLEDMLNDVRQKCQEesqmISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQE 552
Cdd:COG3883   104 yldvlLGSESfSDFLDRLSALSKIADADADLLEELKADKAE----LEAKKAELEAKLAELEALKAELEAAKAELEAQQAE 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207192617 553 EAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSST 608
Cdd:COG3883   180 QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
435-604 4.51e-10

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 63.78  E-value: 4.51e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  435 WDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEeMDQQKAKLEDmLNDVRQKCQEE 514
Cdd:COG4913    606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-VASAEREIAE-LEAELERLDAS 683

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  515 SQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDS 594
Cdd:COG4913    684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAV 763

                          170
                   ....*....|
gi 1207192617  595 QHEISKNIEQ 604
Cdd:COG4913    764 ERELRENLEE 773
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
410-564 5.26e-10

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 63.40  E-value: 5.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  410 FTGIKELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRhkTTEVQEMQNDLDRetssLQELEAQKQDAQDR 489
Cdd:COG4913    284 WFAQRRLELLEAELEELRAELA----RLEAELERLEARLDALREELD--ELEAQIRGNGGDR----LEQLEREIERLERE 353

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  490 LEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQ----EEELGRAKADLNRLQQEEAQLEQ---SLQA 562
Cdd:COG4913    354 LEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEElealEEALAEAEAALRDLRRELRELEAeiaSLER 433


                   ..
gi 1207192617  563 GR 564
Cdd:COG4913    434 RK 435
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 476-604 7.54e-10

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: 60.32  E-value: 7.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 476 LQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKA---------DL 546
Cdd:COG1579    12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEY 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207192617 547 NRLQQEEA-------QLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:COG1579    92 EALQKEIEslkrrisDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 445-595 7.77e-10

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 61.77  E-value: 7.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 445 EQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQ---KCQEE-SQMISS 520
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAeieERREElGERARA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 521 LQTQ------------------------------------IHSQESD---LQSQEEELGRAKADLNRLQQEEAQLEQSLQ 561
Cdd:COG3883    95 LYRSggsvsyldvllgsesfsdfldrlsalskiadadadlLEELKADkaeLEAKKAELEAKLAELEALKAELEAAKAELE 174

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1207192617 562 AGRIQLETIIKSLKATQDEINQARSKLSQIQDSQ 595
Cdd:COG3883   175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
Filament pfam00038
Intermediate filament protein;
414-610 7.97e-10

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 61.09  E-value: 7.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEIAQLQSTL--AFTHWDTLREKYTLEQDIRETEEAirhkttEVQEMQNDLDRETSSLQELEAQKQDAQDRL- 490
Cdd:pfam00038  61 RQLDTLTVERARLQLELdnLRLAAEDFRQKYEDELNLRTSAEN------DLVGLRKDLDEATLARVDLEAKIESLKEELa 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 491 -------EEMDQQKAKLED-----------------MLNDVR-------QKCQEESQM-----ISSLQTQIHSQESDLQS 534
Cdd:pfam00038 135 flkknheEEVRELQAQVSDtqvnvemdaarkldltsALAEIRaqyeeiaAKNREEAEEwyqskLEELQQAAARNGDALRS 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 535 QEEELgrakADLNR-LQQEEAQLeQSLQAGRIQLETIIKSLKATQD-EINQARSKLS----QIQDSQHEISKNIEQYSST 608
Cdd:pfam00038 215 AKEEI----TELRRtIQSLEIEL-QSLKKQKASLERQLAETEERYElQLADYQELISeleaELQETRQEMARQLREYQEL 289


                  ..
gi 1207192617 609 LN 610
Cdd:pfam00038 290 LN 291
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 481-610 1.28e-09

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: 61.32  E-value: 1.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 481 AQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSL 560
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207192617 561 QAGRIQLETIIKS-----------LKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLN 610
Cdd:COG4942   100 EAQKEELAELLRAlyrlgrqpplaLLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA 160
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
414-604 1.46e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 62.00  E-value: 1.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQnDLDRETSSLQE-------LEAQKQDA 486
Cdd:PRK03918  231 KELEELKEEIEELEKELE----SLEGSKRKLEEKIRELEERIEELKKEIEELE-EKVKELKELKEkaeeyikLSEFYEEY 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 487 QDRLEEMDQQKAKLEDMLNDVRQKCQEESQM------ISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEqSL 560
Cdd:PRK03918  306 LDELREIEKRLSRLEEEINGIEERIKELEEKeerleeLKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLT-GL 384

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1207192617 561 QAGRI--QLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:PRK03918  385 TPEKLekELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 414-605 1.80e-09

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 62.01  E-value: 1.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  414 KELDDISQEIAQLQSTLAfthwdTLREKYT-LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRL-- 490
Cdd:TIGR02169  716 RKIGEIEKEIEQLEQEEE-----KLKERLEeLEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLsh 790

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  491 ----------EEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQES---DLQSQEEELGRAKADLN---------- 547
Cdd:TIGR02169  791 sripeiqaelSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEqriDLKEQIKSIEKEIENLNgkkeeleeel 870

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207192617  548 -RLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQ-------ARSKLSQIQDSQHEISKNIEQY 605
Cdd:TIGR02169  871 eELEAALRDLESRLGDLKKERDELEAQLRELERKIEEleaqiekKRKRLSELKAKLEALEEELSEI 936
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 440-631 2.27e-09

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 59.77  E-value: 2.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 440 EKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQEleaQKQDAQDRLEEmdqQKAKLEDMLNDVRQKCQEESQMIS 519
Cdd:pfam09787  55 ERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSRE---QLQELEEQLAT---ERSARREAEAELERLQEELRYLEE 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 520 SLQTQIHSQESDLQSQEEELGRAKADLNRLQQ---EEAQLEQSLQagriQL-ETIIKS---LKATQDEINQARSKL---- 588
Cdd:pfam09787 129 ELRRSKATLQSRIKDREAEIEKLRNQLTSKSQsssSQSELENRLH----QLtETLIQKqtmLEALSTEKNSLVLQLerme 204

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1207192617 589 SQIQDSQHEISKNIeqySSTLNGTHGGSMTNLADMSEGFPEKE 631
Cdd:pfam09787 205 QQIKELQGEGSNGT---SINMEGISDGEGTRLRNVPGLFSESD 244
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
415-592 2.62e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 61.47  E-value: 2.62e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  415 ELDDISQEIAQLQSTLA-----FTHWDTLREKYTLEQDIRETEEAIRhkttEVQEMQNDLDRETSSLQELEAQKQDAQDR 489
Cdd:COG4913    625 ELAEAEERLEALEAELDalqerREALQRLAEYSWDEIDVASAEREIA----ELEAELERLDASSDDLAALEEQLEELEAE 700

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  490 LEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQagriqlet 569
Cdd:COG4913    701 LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLE-------- 772

                          170       180
                   ....*....|....*....|...
gi 1207192617  570 iiKSLKATQDEINQARSKLSQIQ 592
Cdd:COG4913    773 --ERIDALRARLNRAEEELERAM 793
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 414-595 2.80e-09

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 60.23  E-value: 2.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQE----MQND-------------------LD 470
Cdd:COG3883    44 AELEELNEEYNELQAELE----ALQAEIDKLQAEIAEAEAEIEERREELGEraraLYRSggsvsyldvllgsesfsdfLD 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 471 RETSSLQELEAQK---QDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLN 547
Cdd:COG3883   120 RLSALSKIADADAdllEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1207192617 548 RLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQ 595
Cdd:COG3883   200 ELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 422-600 2.98e-09

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 60.91  E-value: 2.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 422 EIAQLQSTLAFTHWDTLREKYTLEQDIRETEEAIrhkTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLE 501
Cdd:pfam05557  76 ELNRLKKKYLEALNKKLNEKESQLADAREVISCL---KNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAE 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 502 DMLNDVRQKCQEES---QMISSLQTQIHSQESDlqsqEEELGRAKADLNRLQQEEAQLEQsLQAGRIQLETIIKSLKATQ 578
Cdd:pfam05557 153 QLRQNLEKQQSSLAeaeQRIKELEFEIQSQEQD----SEIVKNSKSELARIPELEKELER-LREHNKHLNENIENKLLLK 227

                         170       180
                  ....*....|....*....|..
gi 1207192617 579 DEINQARSKLSQIQDSQHEISK 600
Cdd:pfam05557 228 EEVEDLKRKLEREEKYREEAAT 249
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
476-611 3.65e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 60.70  E-value: 3.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  476 LQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIhsqesDLQSQEEELGRAKADLNRLQQEEAQ 555
Cdd:COG4913    612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-----DVASAEREIAELEAELERLDASSDD 686

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207192617  556 LEQsLQAgriQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLNG 611
Cdd:COG4913    687 LAA-LEE---QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 414-597 4.39e-09

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 59.46  E-value: 4.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEIAQLQSTLAfthwdtlrekyTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM 493
Cdd:COG3883    23 KELSELQAELEAAQAELD-----------ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 494 --DQQKA-----KLEDMLNdvrqkcqeeSQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLE---QSLQAG 563
Cdd:COG3883    92 arALYRSggsvsYLDVLLG---------SESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEaklAELEAL 162

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1207192617 564 RIQLETIIKSLKATQDEINQARSKLSQIQDSQHE 597
Cdd:COG3883   163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEA 196
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 413-609 4.99e-09

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 60.37  E-value: 4.99e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  413 IKELDDISQEIAQLQSTLAfthwdtlREKYTLEQDiRETEEAIRHKTTEVQEM---QNDLDRETSSLQELEAQKQDAQDR 489
Cdd:TIGR00618  631 RLHLQQCSQELALKLTALH-------ALQLTLTQE-RVREHALSIRVLPKELLasrQLALQKMQSEKEQLTYWKEMLAQC 702

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  490 LEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQI-----------HSQESDLQSQEEELGRAK----ADLNRLQQEEa 554
Cdd:TIGR00618  703 QTLLRELETHIEEYDREFNEIENASSSLGSDLAAREdalnqslkelmHQARTVLKARTEAHFNNNeevtAALQTGAELS- 781

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207192617  555 QLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQD-SQHEISKNIEQYSSTL 609
Cdd:TIGR00618  782 HLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNlQCETLVQEEEQFLSRL 837
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 426-613 5.16e-09

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 60.47  E-value: 5.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  426 LQSTLAFTHWDTLRE---KY---TLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAK 499
Cdd:TIGR02169  620 FGDTLVVEDIEAARRlmgKYrmvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRR 699

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  500 LEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQagriqleTIIKSLKATQD 579
Cdd:TIGR02169  700 IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK-------ELEARIEELEE 772

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1207192617  580 EINQARSKLSQIQDS-QHEISKNIEQYSSTLNGTH 613
Cdd:TIGR02169  773 DLHKLEEALNDLEARlSHSRIPEIQAELSKLEEEV 807
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 444-604 5.89e-09

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: 59.01  E-value: 5.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 444 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKcqeesqmISSLQT 523
Cdd:COG4942    25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE-------IAELRA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 524 QIHSQESDLQ-------------------SQEE--ELGR--------AKADLNRLQQEEAQLEQsLQAGRIQLETIIKSL 574
Cdd:COG4942    98 ELEAQKEELAellralyrlgrqpplalllSPEDflDAVRrlqylkylAPARREQAEELRADLAE-LAALRAELEAERAEL 176

                         170       180       190
                  ....*....|....*....|....*....|
gi 1207192617 575 KATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:COG4942   177 EALLAELEEERAALEALKAERQKLLARLEK 206
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 414-609 6.23e-09

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 60.03  E-value: 6.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEIAQLQST------------LAFTHWDTLREKytLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEA 481
Cdd:TIGR04523 426 KEIERLKETIIKNNSEikdltnqdsvkeLIIKNLDNTRES--LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 482 QKQDAQDRLEEMDQQKAKLEdmlndvrQKCQEESQMISSLQTQIHSQESDLQSQEEELGRA--KADLNRLQQEEAQLEQS 559
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLK-------EKIEKLESEKKEKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQT 576

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1207192617 560 lqagriqletiIKSLKATQDEINQarsKLSQIQDSQHEISKNIEQYSSTL 609
Cdd:TIGR04523 577 -----------QKSLKKKQEEKQE---LIDQKEKEKKDLIKEIEEKEKKI 612
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 414-589 8.84e-09

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 59.14  E-value: 8.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEIAQLQSTLafthwdtLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQdrlEEM 493
Cdd:pfam07888 104 KELSASSEELSEEKDAL-------LAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEE---AER 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 494 DQQKAKLEDMLNDVRQKCQEESQMISSLQtqihSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQagriQLETIIKS 573
Cdd:pfam07888 174 KQLQAKLQQTEEELRSLSKEFQELRNSLA----QRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLE----ELRSLQER 245

                         170
                  ....*....|....*.
gi 1207192617 574 LKATQDEINQARSKLS 589
Cdd:pfam07888 246 LNASERKVEGLGEELS 261
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
441-610 9.99e-09

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 59.26  E-value: 9.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 441 KYTLEQDIRETEEAIRHKTTEVQEMQNDLD---------RETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKc 511
Cdd:COG3206   163 EQNLELRREEARKALEFLEEQLPELRKELEeaeaaleefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR- 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 512 qeesqmISSLQTQIHSQESDLQ--SQEEELGRAKADLNRLQQEEAQLEQSLQAG-------RIQLETIIKSLKATQDEI- 581
Cdd:COG3206   242 ------LAALRAQLGSGPDALPelLQSPVIQQLRAQLAELEAELAELSARYTPNhpdvialRAQIAALRAQLQQEAQRIl 315

                         170       180
                  ....*....|....*....|....*....
gi 1207192617 582 NQARSKLSQIQDSQHEISKNIEQYSSTLN 610
Cdd:COG3206   316 ASLEAELEALQAREASLQAQLAQLEARLA 344
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 414-603 1.01e-08

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 59.26  E-value: 1.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEIAQLQSTLafthwdtlrEKytLEQDIRETEEAIRHKTTEVQEMQNDLDREtsslqELEAQKQDAQDRLEEM 493
Cdd:TIGR04523 510 EKVKDLTKKISSLKEKI---------EK--LESEKKEKESKISDLEDELNKDDFELKKE-----NLEKEIDEKNKEIEEL 573

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 494 DQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSlqagriqLETIIKS 573
Cdd:TIGR04523 574 KQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSK-------KNKLKQE 646

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1207192617 574 LKATQDEINQARSKLSQI----QDSQHEISKNIE 603
Cdd:TIGR04523 647 VKQIKETIKEIRNKWPEIikkiKESKTKIDDIIE 680
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 445-643 1.19e-08

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 59.29  E-value: 1.19e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  445 EQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQD-------------RLEEMD----QQKAKLEDM---- 503
Cdd:TIGR00606  743 EKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVcltdvtimerfqmELKDVErkiaQQAAKLQGSdldr 822

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  504 -LNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQ-AGRI--QLETIIKSLKATQD 579
Cdd:TIGR00606  823 tVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQrRQQFeeQLVELSTEVQSLIR 902

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207192617  580 EINQARSKLSQIQDSQHEISKNIEQYSSTLNGTHGGSMTNLADMSEGFPEKenggFGAMEDPFK 643
Cdd:TIGR00606  903 EIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNI----HGYMKDIEN 962
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 468-610 1.26e-08

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 57.92  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 468 DLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELG-RAKA-- 544
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGeRARAly 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 545 --------------------------DLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDsqhEI 598
Cdd:COG3883    97 rsggsvsyldvllgsesfsdfldrlsALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA---EL 173

                         170
                  ....*....|..
gi 1207192617 599 SKNIEQYSSTLN 610
Cdd:COG3883   174 EAQQAEQEALLA 185
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 416-594 1.83e-08

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 57.98  E-value: 1.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 416 LDDISQEIAQLQSTLAFTHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQ 495
Cdd:pfam07888  36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 496 QKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLK 575
Cdd:pfam07888 116 EKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQ 195

                         170
                  ....*....|....*....
gi 1207192617 576 ATQDEINQARSKLSQIQDS 594
Cdd:pfam07888 196 ELRNSLAQRDTQVLQLQDT 214
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
414-612 1.93e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 58.51  E-value: 1.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEIAQLqstlafthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMqNDLDRETSS-----LQELEAQKQDaqD 488
Cdd:PRK02224  579 SKLAELKERIESL---------ERIRTLLAAIADAEDEIERLREKREALAEL-NDERRERLAekrerKRELEAEFDE--A 646

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 489 RLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSqeeelgrakadLNRLQQEEAQLEQSLQAgriqLE 568
Cdd:PRK02224  647 RIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEE-----------LEELRERREALENRVEA----LE 711

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1207192617 569 TIIKSLKATQDEINQARSKLSQiqdsqheisKNIEQYSSTLNGT 612
Cdd:PRK02224  712 ALYDEAEELESMYGDLRAELRQ---------RNVETLERMLNET 746
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
488-604 2.41e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 57.22  E-value: 2.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 488 DRLEEMDQqKAKLEdmLNDVRQKcqeESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQE----EAQLEQS---L 560
Cdd:COG4372     2 DRLGEKVG-KARLS--LFGLRPK---TGILIAALSEQLRKALFELDKLQEELEQLREELEQAREEleqlEEELEQArseL 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1207192617 561 QAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:COG4372    76 EQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 414-604 2.70e-08

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 57.56  E-value: 2.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEIAQLQSTLAfthwdtlrekytlEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM 493
Cdd:pfam06160 237 KEIQQLEEQLEENLALLE-------------NLELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHA 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 494 DQQKAKLEDMLNDVRQKCQ---EESQMISSLQTQIHSQESDLQSQEEELGRAKAD----LNRLQQEEAQLEQsLQAgriQ 566
Cdd:pfam06160 304 EEQNKELKEELERVQQSYTlneNELERVRGLEKQLEELEKRYDEIVERLEEKEVAyselQEELEEILEQLEE-IEE---E 379

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1207192617 567 LETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:pfam06160 380 QEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEK 417
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
415-561 3.57e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.47  E-value: 3.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 415 ELDDISQEIAQLQSTLAFTHWDTLREKYT-------LEQDIRETEEAIRHKTTEVQEMQNDLDRET--SSLQELEAQKQD 485
Cdd:COG4717   364 QLEELEQEIAALLAEAGVEDEEELRAALEqaeeyqeLKEELEELEEQLEELLGELEELLEALDEEEleEELEELEEELEE 443

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207192617 486 AQDRLEEMDQQKAKLEDMLNDVrqkcqEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQ 561
Cdd:COG4717   444 LEEELEELREELAELEAELEQL-----EEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
430-605 3.76e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.08  E-value: 3.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 430 LAFTHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDR-------ETSSLQELEAQKQDAQDRLEEMDQQKAKLE- 501
Cdd:COG4717   286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAlglppdlSPEELLELLDRIEELQELLREAEELEEELQl 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 502 ----------------DMLNDVRQKCQEESQMISsLQTQIHSQESDLQSQEEELGR--AKADLNRLQQEEAQLEQSLQAG 563
Cdd:COG4717   366 eeleqeiaallaeagvEDEEELRAALEQAEEYQE-LKEELEELEEQLEELLGELEEllEALDEEELEEELEELEEELEEL 444

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1207192617 564 RIQLETIIKSLKATQDEINQARS--KLSQIQDSQHEISKNIEQY 605
Cdd:COG4717   445 EEELEELREELAELEAELEQLEEdgELAELLQELEELKAELREL 488
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 446-592 3.84e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.37  E-value: 3.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  446 QDI-RETEEAIRH------KTTEVQEMQNDLdrETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMI 518
Cdd:TIGR02168  192 EDIlNELERQLKSlerqaeKAERYKELKAEL--RELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKL 269

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  519 SSLQTQIHSQESDLQSQEEELGRAKADLNRL-------QQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQI 591
Cdd:TIGR02168  270 EELRLEVSELEEEIEELQKELYALANEISRLeqqkqilRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349


                   .
gi 1207192617  592 Q 592
Cdd:TIGR02168  350 K 350
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 414-625 4.00e-08

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: 57.49  E-value: 4.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  414 KELDDISQEIAQLQSTLA-----FTHWDTLREKYtlEQDIRETEEAIRHKTTEVQEMQN---DLDRETSSLQEleaQKQD 485
Cdd:pfam01576  152 KERKLLEERISEFTSNLAeeeekAKSLSKLKNKH--EAMISDLEERLKKEEKGRQELEKakrKLEGESTDLQE---QIAE 226

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  486 AQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRI 565
Cdd:pfam01576  227 LQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKT 306

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207192617  566 QLETIIKSlKATQDEINQAR-SKLSQIQDSQHEISKNIEQYSSTLNGTHGGSMTNLADMSE 625
Cdd:pfam01576  307 ELEDTLDT-TAAQQELRSKReQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLE 366
PRK12704 PRK12704
phosphodiesterase; Provisional
 414-570 4.55e-08

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 56.71  E-value: 4.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEiAQLQstlAFTHWDTLREKytLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSL----QELEAQKQDAQDR 489
Cdd:PRK12704   49 KEAEAIKKE-ALLE---AKEEIHKLRNE--FEKELRERRNELQKLEKRLLQKEENLDRKLELLekreEELEKKEKELEQK 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 490 LEEMDQQKAKLEDMLNDVRQKCQEesqmISSLqTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLET 569
Cdd:PRK12704  123 QQELEKKEEELEELIEEQLQELER----ISGL-TAEEAKEILLEKVEEEARHEAAVLIKEIEEEAKEEADKKAKEILAQA 197


                  .
gi 1207192617 570 I 570
Cdd:PRK12704  198 I 198
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 421-640 6.06e-08

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: 56.72  E-value: 6.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  421 QEIAQLQSTLAfthwdtlREKYTLEQDIRETEEaiRHkTTEVQEMQNDLD---RETSSL----QELEAQKQDAQDRLE-- 491
Cdd:pfam01576  327 QEVTELKKALE-------EETRSHEAQLQEMRQ--KH-TQALEELTEQLEqakRNKANLekakQALESENAELQAELRtl 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  492 -----EMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGR-- 564
Cdd:pfam01576  397 qqakqDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQel 476

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  565 IQLETIIK-----SLKATQDEinqaRSKLSQIQDSQHEISKNIEQYSSTLNgthggsmTNLADMSEGFpEKENGGFGAME 639
Cdd:pfam01576  477 LQEETRQKlnlstRLRQLEDE----RNSLQEQLEEEEEAKRNVERQLSTLQ-------AQLSDMKKKL-EEDAGTLEALE 544


                   .
gi 1207192617  640 D 640
Cdd:pfam01576  545 E 545
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 414-591 6.33e-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: 56.99  E-value: 6.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  414 KELDDISQEIAQLQSTLAF---------THWDTLREKYTLEQDIRETEEAIRHKT-TEVQEMQNDLDRETSSLQELEAQK 483
Cdd:TIGR02168  838 RRLEDLEEQIEELSEDIESlaaeieeleELIEELESELEALLNERASLEEALALLrSELEELSEELRELESKRSELRREL 917

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  484 QDAQDRLEEMDQQKAKLEdmlndvrqkcqeesQMISSLQTQIHSQESD-LQSQEEELGRAKADLNRLQQEEAQLEQSLQA 562
Cdd:TIGR02168  918 EELREKLAQLELRLEGLE--------------VRIDNLQERLSEEYSLtLEEAEALENKIEDDEEEARRRLKRLENKIKE 983

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1207192617  563 -GRIQLETI--IKSLK------ATQDE-INQARSKLSQI 591
Cdd:TIGR02168  984 lGPVNLAAIeeYEELKerydflTAQKEdLTEAKETLEEA 1022
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
445-551 7.16e-08

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 56.40  E-value: 7.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 445 EQDIRETEEAIRHKTTEVQEMQNDLDRETSSL----QELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEE---SQM 517
Cdd:COG2433   387 EKELPEEEPEAEREKEHEERELTEEEEEIRRLeeqvERLEAEVEELEAELEEKDERIERLERELSEARSEERREirkDRE 466

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1207192617 518 ISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQ 551
Cdd:COG2433   467 ISRLDREIERLERELEEERERIEELKRKLERLKE 500
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
414-605 8.40e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 55.29  E-value: 8.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEIAQLQSTLAFTHwdtlREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDR---ETSSLQE-----------L 479
Cdd:COG4372    52 EELEQAREELEQLEEELEQAR----SELEQLEEELEELNEQLQAAQAELAQAQEELESlqeEAEELQEeleelqkerqdL 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 480 EAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKcqeesqmISSLQTQIHSQESDLQSQEEElgRAKADLNRLQQEEAQLEQS 559
Cdd:COG4372   128 EQQRKQLEAQIAELQSEIAEREEELKELEEQ-------LESLQEELAALEQELQALSEA--EAEQALDELLKEANRNAEK 198

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1207192617 560 LQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQY 605
Cdd:COG4372   199 EEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 414-553 9.34e-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: 56.23  E-value: 9.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  414 KELDDISQEIAQLQSTLAFTHW----------DTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQK 483
Cdd:TIGR02169  364 EELEDLRAELEEVDKEFAETRDelkdyrekleKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  484 QDAQDRLEEMDQQKAKLEDMLNDVRQKcqeesqmISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEE 553
Cdd:TIGR02169  444 EDKALEIKKQEWKLEQLAADLSKYEQE-------LYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 440-601 1.00e-07

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 53.60  E-value: 1.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 440 EKYTLEQDIRETEEAIRHKTTEVQEMQNDLDretssLQELEAQKQDAQDRLEEMDQQKAKLEDML---NDVRQKCQEESQ 516
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDD-----LESVEALLKKHEALEAELAAHEERVEALNelgEQLIEEGHPDAE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 517 MISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQ---EEAQLEQSLQAGRIQLETI------------IKSLKATQDEI 581
Cdd:cd00176    76 EIQERLEELNQRWEELRELAEERRQRLEEALDLQQffrDADDLEQWLEEKEAALASEdlgkdlesveelLKKHKELEEEL 155

                         170       180
                  ....*....|....*....|
gi 1207192617 582 NQARSKLSQIQDSQHEISKN 601
Cdd:cd00176   156 EAHEPRLKSLNELAEELLEE 175
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
409-592 1.02e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.84  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 409 EFTGIKE-LDDISQEIAQLQstlafthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRET-SSLQELEAQKQ-- 484
Cdd:PRK03918  526 EYEKLKEkLIKLKGEIKSLK--------KELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKel 597

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 485 -----------DAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIhsqeSDLQSQ--EEELGRAKADLNRLQQ 551
Cdd:PRK03918  598 epfyneylelkDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL----EELEKKysEEEYEELREEYLELSR 673

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1207192617 552 EEAQLEQSLQAGRIQLETIIKS---LKATQDEINQARSKLSQIQ 592
Cdd:PRK03918  674 ELAGLRAELEELEKRREEIKKTlekLKEELEEREKAKKELEKLE 717
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 415-609 1.06e-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: 56.23  E-value: 1.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  415 ELDDISQEIAQLQSTLAFTHWDTLREKYT-LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDR---- 489
Cdd:TIGR02169  773 DLHKLEEALNDLEARLSHSRIPEIQAELSkLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQiksi 852

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  490 ----------LEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQ-------QE 552
Cdd:TIGR02169  853 ekeienlngkKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKaklealeEE 932

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207192617  553 EAQLEQSLQAGR--IQLETIIKSLKATQDEINQARSKLSQIQdsqheiSKNIEQYSSTL 609
Cdd:TIGR02169  933 LSEIEDPKGEDEeiPEEELSLEDVQAELQRVEEEIRALEPVN------MLAIQEYEEVL 985
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 444-604 1.09e-07

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 55.90  E-value: 1.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 444 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLE----------EMDQQKAKLED----MLNDVRQ 509
Cdd:pfam05557  18 KKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAeaeealreqaELNRLKKKYLEalnkKLNEKES 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 510 KCQEESQMISSL-------QTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQagriQLETIIKSLKATQDEIN 582
Cdd:pfam05557  98 QLADAREVISCLknelselRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQ----NLEKQQSSLAEAEQRIK 173

                         170       180
                  ....*....|....*....|...
gi 1207192617 583 QARSKL-SQIQDSqhEISKNIEQ 604
Cdd:pfam05557 174 ELEFEIqSQEQDS--EIVKNSKS 194
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 421-593 1.55e-07

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 53.46  E-value: 1.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 421 QEIAQLQSTLAFthwdtLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSlQELEAQKQDAQDRLEEMDQQKAKL 500
Cdd:pfam12795  17 KLLQDLQQALSL-----LDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAK-AEAAPKEILASLSLEELEQRLLQT 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 501 EDMLNDVRQKCQEESQMISSLQTQIhsqeSDLQSQEEELGRAKADL-NRLQQEEAQLEQSLQAGRIQLETIIKSLKATQD 579
Cdd:pfam12795  91 SAQLQELQNQLAQLNSQLIELQTRP----ERAQQQLSEARQRLQQIrNRLNGPAPPGEPLSEAQRWALQAELAALKAQID 166

                         170
                  ....*....|....
gi 1207192617 580 EINQARSKLSQIQD 593
Cdd:pfam12795 167 MLEQELLSNNNRQD 180
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 415-596 1.91e-07

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 55.12  E-value: 1.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  415 ELDDISQEIA----QLQSTLAFTHwdtLREK---YTLEQDIRETEEAIRHKTTeVQEMQNDLDRETSSLQELEAQKQDAQ 487
Cdd:pfam15921  364 ERDQFSQESGnlddQLQKLLADLH---KREKelsLEKEQNKRLWDRDTGNSIT-IDHLRRELDDRNMEVQRLEALLKAMK 439

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  488 DRLE-EMDQQKAKLedmlndvrQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRiq 566
Cdd:pfam15921  440 SECQgQMERQMAAI--------QGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKE-- 509

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1207192617  567 letiiKSLKATQDEINQARSKLS-QIQDSQH 596
Cdd:pfam15921  510 -----RAIEATNAEITKLRSRVDlKLQELQH 535
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 481-610 1.96e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.06  E-value: 1.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  481 AQKQDAQDRLEEMDQQKAKLEDMLNDVRQKcqeesqmISSLQTQIHSQES--DLQSQEEELGRA--KADLNRLQQEEAQL 556
Cdd:TIGR02168  172 ERRKETERKLERTRENLDRLEDILNELERQ-------LKSLERQAEKAERykELKAELRELELAllVLRLEELREELEEL 244

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207192617  557 EQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLN 610
Cdd:TIGR02168  245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS 298
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 414-607 2.05e-07

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 55.03  E-value: 2.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEIAQLQSTLA--FTHWDTL-REKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQD---AQ 487
Cdd:TIGR04523 138 KNIDKFLTEIKKKEKELEklNNKYNDLkKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKnksLE 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 488 DRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIhsqeSDLQSQEEElgrakaDLNRLQQEEAQLEQS------LQ 561
Cdd:TIGR04523 218 SQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL----NQLKDEQNK------IKKQLSEKQKELEQNnkkikeLE 287

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1207192617 562 AGRIQLETIIKSLK--ATQDEINQARSKLS----QIQDSQHEISKNIEQYSS 607
Cdd:TIGR04523 288 KQLNQLKSEISDLNnqKEQDWNKELKSELKnqekKLEEIQNQISQNNKIISQ 339
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
 17-78 2.20e-07

Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.


Pssm-ID: 289529  Cd Length: 104  Bit Score: 50.06  E-value: 2.20e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207192617  17 YENFYRQVDPGNtGRVGPTEAALFLKKSGLPDITLGKIWDLADPDGKGFLDKQGFYVALRLV 78
Cdd:pfam12763  12 YWEIFSGLKPEN-NKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLI 72
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 504-601 2.37e-07

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 51.16  E-value: 2.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 504 LNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQ 583
Cdd:pfam11559  40 IYELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQR 119

                          90
                  ....*....|....*....
gi 1207192617 584 ARSKLSQIQDSQ-HEISKN 601
Cdd:pfam11559 120 LKNALQQIKTQFaHEVKKR 138
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 414-590 2.38e-07

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 54.97  E-value: 2.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  414 KELDDISQEIAQLQSTLA-FTHWDT-LREKYTLEQDIRET---EEAIRHKTTEVQEMQNDLDRETSSLQELEAQK----- 483
Cdd:TIGR00618  226 KELKHLREALQQTQQSHAyLTQKREaQEEQLKKQQLLKQLrarIEELRAQEAVLEETQERINRARKAAPLAAHIKavtqi 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  484 -QDAQDRLEEMDQQKAKLEDMLNDVR--QKCQEESQMISSLQTQIHSQESDLQSQ-------EEELGRAKADLNRLQQEE 553
Cdd:TIGR00618  306 eQQAQRIHTELQSKMRSRAKLLMKRAahVKQQSSIEEQRRLLQTLHSQEIHIRDAhevatsiREISCQQHTLTQHIHTLQ 385

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1207192617  554 AQLEQSLQAGRI--QLETIIKSLKATQDEINQARSKLSQ 590
Cdd:TIGR00618  386 QQKTTLTQKLQSlcKELDILQREQATIDTRTSAFRDLQG 424
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 391-609 2.39e-07

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: 54.73  E-value: 2.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 391 RRAIMFKLWDSSSSVGSGEFTGIKELDDISQEIAQL--QST--------LAF------THWDTLREKYTLE-QDIRETEE 453
Cdd:pfam05483 210 RLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLliQITekenkmkdLTFlleesrDKANQLEEKTKLQdENLKELIE 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 454 AIRHKTTEVQEMQNDLDRETSSLQELEAQKQDA-----------QDRLEEMDQQKA--------------KLEDMLNDVR 508
Cdd:pfam05483 290 KKDHLTKELEDIKMSLQRSMSTQKALEEDLQIAtkticqlteekEAQMEELNKAKAahsfvvtefeattcSLEELLRTEQ 369

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 509 QKCQEESQMISSLQTQIHSQESDLQS----------QEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQ 578
Cdd:pfam05483 370 QRLEKNEDQLKIITMELQKKSSELEEmtkfknnkevELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQARE 449

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1207192617 579 DEINQARSKLSQIQDSQHEISKNIEQYSSTL 609
Cdd:pfam05483 450 KEIHDLEIQLTAIKTSEEHYLKEVEDLKTEL 480
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 416-604 2.62e-07

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 54.46  E-value: 2.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 416 LDDISQEIAQLQST-------LAFTHWDTLREKYTL-EQDIRETEEAIRHKTTEVQEMQNDLDretssLQELEAQKQDAQ 487
Cdd:PRK04778  214 MEEIPELLKELQTElpdqlqeLKAGYRELVEEGYHLdHLDIEKEIQDLKEQIDENLALLEELD-----LDEAEEKNEEIQ 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 488 DRLEEMDQQ-----KAKledmlNDVRQKCQEESQMISslqtqiHSQEsdlqsQEEELgraKADLNRLQQ------EEAQL 556
Cdd:PRK04778  289 ERIDQLYDIlerevKAR-----KYVEKNSDTLPDFLE------HAKE-----QNKEL---KEEIDRVKQsytlneSELES 349

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1207192617 557 EQSLQAgriQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:PRK04778  350 VRQLEK---QLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEE 394
PRK11281 PRK11281
mechanosensitive channel MscK;
414-603 3.56e-07

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 54.15  E-value: 3.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  414 KELDDISQEIAQLQSTLAFTHWDTLrEKYTLEQdireTEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM 493
Cdd:PRK11281    94 AKLRQAQAELEALKDDNDEETRETL-STLSLRQ----LESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYAN 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  494 DQQKAKLEDMLNDV-----------RQKCQEESQMissLQTQIHSQESDLQ--SQEEELGRAKADLNRLQQeeAQLEQSL 560
Cdd:PRK11281   169 SQRLQQIRNLLKGGkvggkalrpsqRVLLQAEQAL---LNAQNDLQRKSLEgnTQLQDLLQKQRDYLTARI--QRLEHQL 243

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207192617  561 QAgriqLETII--KSLKATQDEINQARS--KLSQIQDS---QHEISKNIE 603
Cdd:PRK11281   244 QL----LQEAInsKRLTLSEKTVQEAQSqdEAARIQANplvAQELEINLQ 289
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 413-592 4.52e-07

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 51.92  E-value: 4.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 413 IKELDDISQEIAQLQSTL--AFTHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRL 490
Cdd:pfam12795  29 LDKIDASKQRAAAYQKALddAPAELRELRQELAALQAKAEAAPKEILASLSLEELEQRLLQTSAQLQELQNQLAQLNSQL 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 491 --------------EEMDQQKAKLEDMLN--DVRQKCQEESQM------ISSLQTQIHSQESDLQS--QEEELGRAKADL 546
Cdd:pfam12795 109 ielqtrperaqqqlSEARQRLQQIRNRLNgpAPPGEPLSEAQRwalqaeLAALKAQIDMLEQELLSnnNRQDLLKARRDL 188

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1207192617 547 --NRLQQEEAQLE--QSLQAGRIQLETiIKSLKATQDEINQARSKLSQIQ 592
Cdd:pfam12795 189 ltLRIQRLEQQLQalQELLNEKRLQEA-EQAVAQTEQLAEEAAGDHPLVQ 237
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 414-606 4.87e-07

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 53.32  E-value: 4.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEIAQLQST-------LAFTHWDTLREKYTLEQDirETEEairhkttEVQEMQNDLDRETSSLQELEAQkqDA 486
Cdd:pfam06160 193 ELMEDIPPLYEELKTElpdqleeLKEGYREMEEEGYALEHL--NVDK-------EIQQLEEQLEENLALLENLELD--EA 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 487 QDRLEEMDQQKAKLEDMLN---DVRQKCQEESQMISSLQTQIHSQESDLQsqeEELGRAKadLN-RLQQEEAQLEQSLQA 562
Cdd:pfam06160 262 EEALEEIEERIDQLYDLLEkevDAKKYVEKNLPEIEDYLEHAEEQNKELK---EELERVQ--QSyTLNENELERVRGLEK 336

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1207192617 563 griQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYS 606
Cdd:pfam06160 337 ---QLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIE 377
mukB PRK04863
chromosome partition protein MukB;
413-585 5.30e-07

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 53.81  E-value: 5.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  413 IKELDDISQEIAQLQSTLAF--THWDTLREKYTLEQDIRETEEAI---RHKTTEVQEMQNDLDRETSSLQELEAQK---- 483
Cdd:PRK04863   893 ADRVEEIREQLDEAEEAKRFvqQHGNALAQLEPIVSVLQSDPEQFeqlKQDYQQAQQTQRDAKQQAFALTEVVQRRahfs 972

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  484 -QDAQD--------------RLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELG-------- 540
Cdd:PRK04863   973 yEDAAEmlaknsdlneklrqRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQdlgvpads 1052

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207192617  541 ----RAKADLNRLQQE-------EAQLEQSLQAGRIQLETIIKSLKATQDEINQAR 585
Cdd:PRK04863  1053 gaeeRARARRDELHARlsanrsrRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMR 1108
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 467-609 6.03e-07

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 52.45  E-value: 6.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 467 NDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDM---LNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEElgrAK 543
Cdd:pfam09787  37 EGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLrteLQELEAQQQEEAESSREQLQELEEQLATERSARRE---AE 113

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207192617 544 ADLNRLQQEEAQLEQSLQAGRIQLETIIKSLkatQDEINQARSKL---SQIQDSQHEISKNIEQYSSTL 609
Cdd:pfam09787 114 AELERLQEELRYLEEELRRSKATLQSRIKDR---EAEIEKLRNQLtskSQSSSSQSELENRLHQLTETL 179
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 424-609 7.13e-07

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 53.43  E-value: 7.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  424 AQLQSTLafTHWDTLREKytlEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQ-------ELEAQKQDAQDRLEEMDQQ 496
Cdd:TIGR00618  549 HQLTSER--KQRASLKEQ---MQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQdlteklsEAEDMLACEQHALLRKLQP 623

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  497 KAKLEDMLNDVRQKCQEESQmissLQTQIHSQESDLQSQEEELGRAkadlnRLQQEEAQLEQSLQAGRIQLETIIKSLKA 576
Cdd:TIGR00618  624 EQDLQDVRLHLQQCSQELAL----KLTALHALQLTLTQERVREHAL-----SIRVLPKELLASRQLALQKMQSEKEQLTY 694

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1207192617  577 TQDEINQARSKLSQIQDSQHEISKNIEQYSSTL 609
Cdd:TIGR00618  695 WKEMLAQCQTLLRELETHIEEYDREFNEIENAS 727
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 432-604 8.38e-07

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 50.91  E-value: 8.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 432 FTHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQ-----------KQDAQDRLEEMDQQKAKL 500
Cdd:cd00176    12 LEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELgeqlieeghpdAEEIQERLEELNQRWEEL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 501 EDMLNDVRQKCQE------ESQMISSLQTQIHSQESDLQSQeeELGRAKADLNRLQQEEAQLEQSLQAgriqLETIIKSL 574
Cdd:cd00176    92 RELAEERRQRLEEaldlqqFFRDADDLEQWLEEKEAALASE--DLGKDLESVEELLKKHKELEEELEA----HEPRLKSL 165

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1207192617 575 KATQDEINQARSKLS--QIQDSQHEISKNIEQ 604
Cdd:cd00176   166 NELAEELLEEGHPDAdeEIEEKLEELNERWEE 197
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 417-637 8.54e-07

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 51.99  E-value: 8.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 417 DDISQEIAQLQSTLA-----FTHW--DTLREKYTLEQDIRE-TEEAIRHKTTEVQEMQNDLDR--ETSSLQELEAQKQDA 486
Cdd:cd22656    40 DKLSSDFDPLLDAYKsikdhCTDFkdDTYPSIVSLAGDIYNyAQNAGGTIDSYYAEILELIDDlaDATDDEELEEAKKTI 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 487 QDRLEEMD------QQKA-KLEDMLNDVRQKCQEESQMISSLQTQIHSQ----------------ESDLQSQEEELG-RA 542
Cdd:cd22656   120 KALLDDLLkeakkyQDKAaKVVDKLTDFENQTEKDQTALETLEKALKDLltdeggaiarkeikdlQKELEKLNEEYAaKL 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 543 KADLNRLQQEEAQLEQSLQAG-RIQ--LETIIKSLKATQDEINQARSKLSQIQDSQHEISknieqysstlngthgGSMTN 619
Cdd:cd22656   200 KAKIDELKALIADDEAKLAAAlRLIadLTAADTDLDNLLALIGPAIPALEKLQGAWQAIA---------------TDLDS 264

                         250
                  ....*....|....*...
gi 1207192617 620 LADMSEGFPEKENGGFGA 637
Cdd:cd22656   265 LKDLLEDDISKIPAAILA 282
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 420-598 9.82e-07

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 51.84  E-value: 9.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 420 SQEIAQLQSTLAFTHWDTLREKYTLEQDIRETEEAirhktteVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAK 499
Cdd:pfam13868   5 SDELRELNSKLLAAKCNKERDAQIAEKKRIKAEEK-------EEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 500 LEDMLNDVRQKCQE-------ESQMISSLQTQIhsQESDLQSQE----------EELGRAKADLNRLQQEEAQLEQsLQA 562
Cdd:pfam13868  78 LEEQIEEREQKRQEeyeeklqEREQMDEIVERI--QEEDQAEAEeklekqrqlrEEIDEFNEEQAEWKELEKEEER-EED 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1207192617 563 GRI-----QLETIIKSLKATQDEINQA--------RSKLSQIQDSQHEI 598
Cdd:pfam13868 155 ERIleylkEKAEREEEREAEREEIEEEkereiarlRAQQEKAQDEKAER 203
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 475-612 1.16e-06

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 50.76  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 475 SLQELEAQK-------------QDAQDRLEEMDQQKAKLEDmlndVRQKCQEESQMISSLQTQIHSQEsdlQSQEEELgr 541
Cdd:pfam12795   1 KLDELEKAKldeaakkkllqdlQQALSLLDKIDASKQRAAA----YQKALDDAPAELRELRQELAALQ---AKAEAAP-- 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207192617 542 aKADLNRLQQEeaQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLNGT 612
Cdd:pfam12795  72 -KEILASLSLE--ELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGP 139
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 414-610 1.21e-06

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 52.15  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEIAQLqstlafthWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQ--------ELEAQKQd 485
Cdd:PRK04778  282 EKNEEIQERIDQL--------YDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKqsytlnesELESVRQ- 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 486 AQDRLEEMDQQkakledmLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRI 565
Cdd:PRK04778  353 LEKQLESLEKQ-------YDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRN 425

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207192617 566 QLETII----KS------------LKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLN 610
Cdd:PRK04778  426 KLHEIKryleKSnlpglpedylemFFEVSDEIEALAEELEEKPINMEAVNRLLEEATEDVE 486
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
443-589 1.23e-06

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 50.21  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 443 TLEQDIRETEEAIrhkttevQEMQNDLDRETSSLQELEAQKQDAQDRLEEMdQQKAKL------EDMLNDVRQKCQEESQ 516
Cdd:COG1842    27 MLDQAIRDMEEDL-------VEARQALAQVIANQKRLERQLEELEAEAEKW-EEKARLalekgrEDLAREALERKAELEA 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207192617 517 MISSLQTQIhsqesdlQSQEEELGRAKADLNRLqqeEAQLEQsLQAGRIQLETIIKSLKATQdEINQARSKLS 589
Cdd:COG1842    99 QAEALEAQL-------AQLEEQVEKLKEALRQL---ESKLEE-LKAKKDTLKARAKAAKAQE-KVNEALSGID 159
STAT3_CCD cd16853
Coiled-coil domain of Signal Transducer and Activator of Transcription 3 (STAT3); This family ...
 446-592 1.32e-06

Coiled-coil domain of Signal Transducer and Activator of Transcription 3 (STAT3); This family consists of the coiled-coil (alpha) domain of the STAT3 proteins (Signal Transducer and Activator of Transcription 3, or Signal Transduction And Transcription 3). STAT3 continuously shuttles between nuclear and cytoplasmic compartments. The coiled-coil domain (CCD) of STAT3 appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the STAT3 CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 in the testis, and importin-alpha6 NLS adapters in most cells. STAT3 plays key roles in vertebrate development and mature tissue function including control of inflammation and immunity. Mutations in human STAT3, especially in the DNA-binding and SH2 domains, are associated with diseases such as autoimmunity, immunodeficiency and cancer. STAT3 regulation is tightly controlled since either inactivation or hyperactivation results in disease. STAT3 activation is stimulated by several cytokines and growth factors, via diverse receptors. For example, IL-6 receptors depend on the tyrosine kinases JAK1 or JAK2, which associate with the cytoplasmic tail of gp130, and results in STAT3 phosphorylation, dimerization, and translocation to the nucleus; this leads to further IL-6 production and up-regulation of anti-apoptotic genes, thus promoting various cellular processes required for cancer progression. Other activators of STAT3 include IL-10, IL-23, and LPS activation of Toll-like receptors TLR4 and TLR9. STAT3 is constitutively activated in numerous cancer types, including over 40% of breast cancers. It has been shown to play a significant role in promoting acute myeloid leukemia (AML) through three mechanisms: promoting proliferation and survival, preventing AML differentiation to functional dendritic cells (DCs), and blocking T-cell function through other pathways. STAT3 also regulates mitochondrion functions, as well as gene expression through epigenetic mechanisms; its activation is induced by overexpression of Bcl-2 via an increase in mitochondrial superoxide. Thus, many of the regulators and functions of JAK-STAT3 in tumors are important therapeutic targets for cancer treatment.


Pssm-ID: 341078 [Multi-domain]  Cd Length: 180  Bit Score: 49.61  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 446 QDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQI 525
Cdd:cd16853    11 QDVRKRVQDLEQKMKVVENLQDDFDFNYKTLKSQGDMQDLNGNNQSVTRQKMQQLEQMLTALDQMRRQIVSELAGLLSAM 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207192617 526 HSQESDLqsQEEELgrakADLNRLQQeEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQ 592
Cdd:cd16853    91 EYVQKNL--TDEEL----ADWKRRQQ-IACIGGPPNICLDRLENWITSLAESQLQTRQQIKKLEELQ 150
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 414-598 1.50e-06

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 51.76  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEIAQLQSTLAFThwdtlrekytleqDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM 493
Cdd:PRK04778  256 KEIQDLKEQIDENLALLEEL-------------DLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHA 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 494 DQQKAKLEDMLNDVRQKCQ---EESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETI 570
Cdd:PRK04778  323 KEQNKELKEEIDRVKQSYTlneSELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKL 402

                         170       180
                  ....*....|....*....|....*...
gi 1207192617 571 IKSLKATQDEINQARSKLSQIQDSQHEI 598
Cdd:PRK04778  403 SEMLQGLRKDELEAREKLERYRNKLHEI 430
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 414-604 1.75e-06

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: 52.10  E-value: 1.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  414 KELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETE----EAIRHKTT---EVQEMQNDLDRETSSLQE-------- 478
Cdd:pfam01576  384 SENAELQAELRTLQQAKQ----DSEHKRKKLEGQLQELQarlsESERQRAElaeKLSKLQSELESVSSLLNEaegknikl 459

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  479 ------LEAQKQDAQDRLEEMDQQKAK-------LEDMLNDVRQKCQEE-------SQMISSLQTQIhsqeSDLQSQ-EE 537
Cdd:pfam01576  460 skdvssLESQLQDTQELLQEETRQKLNlstrlrqLEDERNSLQEQLEEEeeakrnvERQLSTLQAQL----SDMKKKlEE 535

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  538 ELGRAKA---DLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQarskLSQIQDSQHEISKNIEQ 604
Cdd:pfam01576  536 DAGTLEAleeGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDD----LLVDLDHQRQLVSNLEK 601
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 414-657 1.79e-06

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 52.04  E-value: 1.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  414 KELDDISQEIAQLQST---LAFTHWDTLREKYTLEQDIR----------ETEEAIRHKTTEVQEMQNDLDRETSSLQELE 480
Cdd:pfam15921  458 ESLEKVSSLTAQLESTkemLRKVVEELTAKKMTLESSERtvsdltaslqEKERAIEATNAEITKLRSRVDLKLQELQHLK 537

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  481 AQK---QDAQ---------------------DRLEEMDQ--------------QKAKLEDMLNDVRQKCQEESQMISSLQ 522
Cdd:pfam15921  538 NEGdhlRNVQtecealklqmaekdkvieilrQQIENMTQlvgqhgrtagamqvEKAQLEKEINDRRLELQEFKILKDKKD 617

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  523 TQIHSQE---SDLQSQEEELGRAKADLNR----LQQEEAQLEQSLQAGRIQL-------ETIIKSLKATQDEINQARSKL 588
Cdd:pfam15921  618 AKIRELEarvSDLELEKVKLVNAGSERLRavkdIKQERDQLLNEVKTSRNELnslsedyEVLKRNFRNKSEEMETTTNKL 697

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207192617  589 S-QIQDSQHEisknIEQYSSTLN---GTHGGSMTNLADMSEGFPEKEnGGFGAMEDPFKVKPTVFNSAPQEMH 657
Cdd:pfam15921  698 KmQLKSAQSE----LEQTRNTLKsmeGSDGHAMKVAMGMQKQITAKR-GQIDALQSKIQFLEEAMTNANKEKH 765
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 444-567 1.89e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 51.30  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 444 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEemdQQKAKLEDMLNDVRQKCQEESQMISSLQt 523
Cdd:COG4942   144 LAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALE---ALKAERQKLLARLEKELAELAAELAELQ- 219

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1207192617 524 qihSQESDLQSQEEELGRAKAdlnrlQQEEAQLEQSLQAGRIQL 567
Cdd:COG4942   220 ---QEAEELEALIARLEAEAA-----AAAERTPAAGFAALKGKL 255
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 415-630 2.08e-06

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 51.76  E-value: 2.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  415 ELDDISQEIAQLQSTLAfthwdtlrEKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSL------------QELEAQ 482
Cdd:pfam12128  242 EFTKLQQEFNTLESAEL--------RLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLddqwkekrdelnGELSAA 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  483 KQD-AQDR--LEEMDQQKAKLEDmlNDVRQKCQEESQMiSSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQleqs 559
Cdd:pfam12128  314 DAAvAKDRseLEALEDQHGAFLD--ADIETAAADQEQL-PSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKE---- 386

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207192617  560 lqagriQLETIIKSLKATQDEINQARsklsqiqDSQH-EISKNIEQYSSTLNGTHGGSMTNLADMSEGFPEK 630
Cdd:pfam12128  387 ------QNNRDIAGIKDKLAKIREAR-------DRQLaVAEDDLQALESELREQLEAGKLEFNEEEYRLKSR 445
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 443-631 2.31e-06

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 51.66  E-value: 2.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  443 TLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQ-ELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSL 521
Cdd:pfam15921  296 SIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRsELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNL 375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  522 QTQIHSQESDLQSQEEELGRAKADLNRL-------------------------QQEEAQLEQSLQAGRIQLETIIKSLKA 576
Cdd:pfam15921  376 DDQLQKLLADLHKREKELSLEKEQNKRLwdrdtgnsitidhlrrelddrnmevQRLEALLKAMKSECQGQMERQMAAIQG 455

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1207192617  577 TQDEINQARSKLSQIQDSQHEISKNIEQYSSTlNGTHGGSMTNLADMSEGFPEKE 631
Cdd:pfam15921  456 KNESLEKVSSLTAQLESTKEMLRKVVEELTAK-KMTLESSERTVSDLTASLQEKE 509
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 416-623 2.37e-06

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 51.66  E-value: 2.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  416 LDDISQEIAQLQSTLAFTHWDTLREKYTLEQDIRETEeairhktTEVQEMQNDLD-------RETSSLQELEAQKQDAqd 488
Cdd:pfam15921   80 LEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQ-------TKLQEMQMERDamadirrRESQSQEDLRNQLQNT-- 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  489 rLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQ--------------EEA 554
Cdd:pfam15921  151 -VHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTmhfrslgsaiskilREL 229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  555 QLEQSLQAGRI-----QLETiIKS---------LKATQDEINQ------------------ARSKLSQIQdSQHEIsknI 602
Cdd:pfam15921  230 DTEISYLKGRIfpvedQLEA-LKSesqnkiellLQQHQDRIEQliseheveitgltekassARSQANSIQ-SQLEI---I 304

                          250       260
                   ....*....|....*....|.
gi 1207192617  603 EQYSSTLNGTHggsMTNLADM 623
Cdd:pfam15921  305 QEQARNQNSMY---MRQLSDL 322
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 532-604 2.46e-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: 2.46e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207192617 532 LQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:COG4942    15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 418-625 2.60e-06

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 51.26  E-value: 2.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 418 DISQEIAQLqsTLAFTHWDTLREKYTLEQ--DIRETEEAIRHKTTEVQEMQNDLDRETSSL----QELEAQKQD------ 485
Cdd:pfam05483 187 DLNNNIEKM--ILAFEELRVQAENARLEMhfKLKEDHEKIQHLEEEYKKEINDKEKQVSLLliqiTEKENKMKDltflle 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 486 -AQDRLEEMdQQKAKLEDmlNDVRQKCQEESQMISSLQTQIHSQESDLQSQ---EEELGRAKADLNRLQQE-EAQLEQSL 560
Cdd:pfam05483 265 eSRDKANQL-EEKTKLQD--ENLKELIEKKDHLTKELEDIKMSLQRSMSTQkalEEDLQIATKTICQLTEEkEAQMEELN 341

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207192617 561 QAgRIQLETIIKSLKAT----QDEINQARSKLSQIQDSQHEISKNIEQYSSTLNgthggSMTNLADMSE 625
Cdd:pfam05483 342 KA-KAAHSFVVTEFEATtcslEELLRTEQQRLEKNEDQLKIITMELQKKSSELE-----EMTKFKNNKE 404
ATG17_like pfam04108
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ...
 372-593 2.81e-06

Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.


Pssm-ID: 427715 [Multi-domain]  Cd Length: 360  Bit Score: 50.46  E-value: 2.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 372 SLSGYMTPVGSDMAALTEMRRAImfklwDSSSSVGSGEFTGIKELDDISQEIAQ-LQStlafthwdtlrekytLEQDIRE 450
Cdd:pfam04108 134 SLDSDLKRFDDDLRDLQKELESL-----SSPSESISLIPTLLKELESLEEEMASlLES---------------LTNHYDQ 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 451 TEEAIRHKTTEVQEMQNDLDRETsslQELEAQKQDAQDRLEEMDQQKAKLE---DMLNDVRQKCQEESQMISSLQTQIHS 527
Cdd:pfam04108 194 CVTAVKLTEGGRAEMLEVLENDA---RELDDVVPELQDRLDEMENNYERLQkllEQKNSLIDELLSALQLIAEIQSRLPE 270

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207192617 528 QESDLQSQEEELGRAKAdlnRLQQEEAQLEQsLQAGRIQLETIIKSL-------KATQDEI----NQARSKLSQIQD 593
Cdd:pfam04108 271 YLAALKEFEERWEEEKE---TIEDYLSELED-LREFYEGFPSAYGSLlleverrREWAEKMkkilRKLAEELDRLQE 343
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 439-609 3.05e-06

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 51.12  E-value: 3.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  439 REKYTLEQDIRETEEaIRHKTTEVQEMQNDLDRETSSLQ-ELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQM 517
Cdd:TIGR00618  163 KEKKELLMNLFPLDQ-YTQLALMEFAKKKSLHGKAELLTlRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQS 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  518 ISSLQTQIHSQESDLQSQEEelgrakadlnrLQQEEAQLEqslqagriQLETIIKSLKATQDEINQARSKLSQIQDSQH- 596
Cdd:TIGR00618  242 HAYLTQKREAQEEQLKKQQL-----------LKQLRARIE--------ELRAQEAVLEETQERINRARKAAPLAAHIKAv 302

                          170
                   ....*....|....
gi 1207192617  597 -EISKNIEQYSSTL 609
Cdd:TIGR00618  303 tQIEQQAQRIHTEL 316
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 436-610 3.17e-06

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 51.59  E-value: 3.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  436 DTLREKYTLEQDIreTEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQ------ 509
Cdd:TIGR01612 1621 DCLKETESIEKKI--SSFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQhkknye 1698

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  510 -----KCQE----ESQMISSLQTQIHSQESDLQSQ-----------EEELGRAKADLNRLQQEEAQLeQSLQAGriQLET 569
Cdd:TIGR01612 1699 igiieKIKEiaiaNKEEIESIKELIEPTIENLISSfntndlegidpNEKLEEYNTEIGDIYEEFIEL-YNIIAG--CLET 1775

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1207192617  570 IIKSlKATQDEINQARSklsqiqDSQHEISKNIE---QYSSTLN 610
Cdd:TIGR01612 1776 VSKE-PITYDEIKNTRI------NAQNEFLKIIEiekKSKSYLD 1812
PRK12704 PRK12704
phosphodiesterase; Provisional
 441-605 3.23e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 50.93  E-value: 3.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 441 KYTLEQDIRETEEAIRHKtteVQEMQNDLDrETSSLQELEAQkqdaqdrlEEMDQQKAKLEdmlNDVRQKCQEesqmISS 520
Cdd:PRK12704   26 KKIAEAKIKEAEEEAKRI---LEEAKKEAE-AIKKEALLEAK--------EEIHKLRNEFE---KELRERRNE----LQK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 521 LQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKA--------TQDEinqARSKLSQ-- 590
Cdd:PRK12704   87 LEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQelerisglTAEE---AKEILLEkv 163

                         170
                  ....*....|....*
gi 1207192617 591 IQDSQHEISKNIEQY 605
Cdd:PRK12704  164 EEEARHEAAVLIKEI 178
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
413-605 3.83e-06

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 49.91  E-value: 3.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 413 IKELDDISQEIAQLQSTLafthwDTLREKytleqdIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEE 492
Cdd:COG1340    28 KEKRDELNEELKELAEKR-----DELNAQ------VKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 493 MDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQE------SDLQSQEEELGRAKaDLNRLQQEEAQLEQSLQAGRIQ 566
Cdd:COG1340    97 LRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEeekelvEKIKELEKELEKAK-KALEKNEKLKELRAELKELRKE 175

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1207192617 567 LETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQY 605
Cdd:COG1340   176 AEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADEL 214
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 409-594 4.17e-06

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 48.36  E-value: 4.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 409 EFTGIKE---------LDDISQ---EIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDL---DRET 473
Cdd:pfam13851   9 AFNEIKNyynditrnnLELIKSlkeEIAELKKKEE----RNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLenyEKDK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 474 SSLQELEAQKQDAQDRL-------EEMDQQKAKLEDMLNDVRQKCQeesQMISSLQtqihsQESDLQSQEEElgrakadl 546
Cdd:pfam13851  85 QSLKNLKARLKVLEKELkdlkwehEVLEQRFEKVERERDELYDKFE---AAIQDVQ-----QKTGLKNLLLE-------- 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1207192617 547 NRLQQEEAQLEQSlqagRIQLETIIKSLKATQDEINQARSKLSQIQDS 594
Cdd:pfam13851 149 KKLQALGETLEKK----EAQLNEVLAAANLDPDALQAVTEKLEDVLES 192
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 476-608 4.28e-06

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 49.63  E-value: 4.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  476 LQELEAQKQDAQDRLEEMDQQKAKL---EDMLNDVRQKCQEESQMISSLQTQIHSQESDLQS-QEEELGRAKADLNRLQQ 551
Cdd:smart00787 139 MKLLEGLKEGLDENLEGLKEDYKLLmkeLELLNSIKPKLRDRKDALEEELRQLKQLEDELEDcDPTELDRAKEKLKKLLQ 218

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207192617  552 E-------EAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQD-SQHEISKNIEQYSST 608
Cdd:smart00787 219 EimikvkkLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGfTFKEIEKLKEQLKLL 283
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 414-610 5.48e-06

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 50.43  E-value: 5.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  414 KELDDISQEIAQLQSTLAFTHWDTLREKYTLEQDIRETEEAIRHKTT-------EVQEMQNDLDRETSSLQELEAQKQDA 486
Cdd:TIGR00606  888 EQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETsnkkaqdKVNDIKEKVKNIHGYMKDIENKIQDG 967

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  487 QDR---------------LEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQI--HSQESDLQSQEEELGRAKADLNRL 549
Cdd:TIGR00606  968 KDDylkqketelntvnaqLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLtlRKRENELKEVEEELKQHLKEMGQM 1047

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  550 Q-----QEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLS--QIQDSQ-------------HEISKNIEQYSSTL 609
Cdd:TIGR00606 1048 QvlqmkQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRepQFRDAEekyremmivmrttELVNKDLDIYYKTL 1127


                   .
gi 1207192617  610 N 610
Cdd:TIGR00606 1128 D 1128
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 440-593 6.96e-06

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 49.15  E-value: 6.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 440 EKYTLEQDIRETEEAIrhkttEVQEMQNDLDREtssLQELEAQKQDAQDRLEEMDQQKAKL----------EDMLNDVRQ 509
Cdd:pfam13868 158 LEYLKEKAEREEEREA-----EREEIEEEKERE---IARLRAQQEKAQDEKAERDELRAKLyqeeqerkerQKEREEAEK 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 510 KCQEESQMISSLQTQIHSQEsdlQSQEEELGRAKADLNRL---QQEEAQLEQSLQAGRIQLetiiksLKATQDEInqars 586
Cdd:pfam13868 230 KARQRQELQQAREEQIELKE---RRLAEEAEREEEEFERMlrkQAEDEEIEQEEAEKRRMK------RLEHRREL----- 295


                  ....*..
gi 1207192617 587 kLSQIQD 593
Cdd:pfam13868 296 -EKQIEE 301
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
414-604 7.22e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.06  E-value: 7.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTT--EVQEMQNDLdrETSSLQELEAQKQDAQ---- 487
Cdd:PRK03918  459 AELKRIEKELKEIEEKER----KLRKELRELEKVLKKESELIKLKELaeQLKELEEKL--KKYNLEELEKKAEEYEklke 532

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 488 -------------DRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEA 554
Cdd:PRK03918  533 kliklkgeikslkKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEK 612

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1207192617 555 QLEQSLqagriqletiiKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:PRK03918  613 ELEREE-----------KELKKLEEELDKAFEELAETEKRLEELRKELEE 651
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 443-589 7.35e-06

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 48.14  E-value: 7.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 443 TLEQDIRETEEAIRhkttevqEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDmlndvrqKCQE-----ESQM 517
Cdd:pfam04012  19 KAEDPEKMLEQAIR-------DMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEE-------KAQAaltkgNEEL 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207192617 518 ISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKA--TQDEINQARSKLS 589
Cdd:pfam04012  85 AREALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAakAQEAVQTSLGSLS 158
HBM pfam16591
Helical bimodular sensor domain; The HBM sensor domain has been identified primarily in ...
 421-604 8.80e-06

Helical bimodular sensor domain; The HBM sensor domain has been identified primarily in bacterial chemoreceptors but is also present on histidine kinases. characteriztic features of this domain are its size of approximately 250 amino acids and its location in the bacterial periplasm. The McpS chemoreceptor of Pseudomonas putida KT2440 was found to possess an HBM sensor domain and its 3D structure in complex with physiologically relevant ligands has been reported. This domain is composed of 2 long and 4 short helices that form two modules each composed of a 4-helix bundle. The McpS chemoreceptor mediates chemotaxis towards a number of organic acids. Both modules of the McpS HBM domain contain a ligand binding site. Chemo-attractants binds to each of these sites and their binding was shown to trigger a chemotactic response. This domain is primarily found in different proteobacteria but also in archaea. Interestingly, amino acids in both ligand binding sites showed a high degree of conservation suggesting that members of this family sense similar ligands. This domain recognizes Multiple TCA cycle intermediates, citrate and alpha-ketoglutarate (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 435446 [Multi-domain]  Cd Length: 246  Bit Score: 48.16  E-value: 8.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 421 QEIAQLQSTLafTHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSS------LQELEAQKQDAQDRLEEMD 494
Cdd:pfam16591   9 TDISQLNDTL--TDLRIARLQYMLSNGDATAAQAVQKKLDELKQQLQQLKTTFTSpenvrlLQEQLQLIQAYRKSFNELR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 495 QQKAKLEDMLNDVRQKCQEESQMISSLQTQI----------------------HSQ--------------ESDLQSQEEE 538
Cdd:pfam16591  87 AAYESRNASRQVMDSAAERALEAIDQLEAEVlqtpeadsrraaqyqaiselkrQVQmaryqvrgytftpnEDSEQAAYQQ 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207192617 539 LGRAKADLNRLQQEEA--------QLEQSLQAGRIQLETiiksLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:pfam16591 167 LDAALASLDQLRQALAgdpgaalqQLTSALQGYRDALDT----FKAAVAAIEQARQEMTSQGDEIVRISDELYQ 236
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 414-563 9.43e-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: 48.99  E-value: 9.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAI-------------------------------------- 455
Cdd:COG4942    69 RRIRALEQELAALEAELA----ELEKEIAELRAELEAQKEELaellralyrlgrqpplalllspedfldavrrlqylkyl 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 456 -RHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLndvrqkcQEESQMISSLQTQIHSQESDLQS 534
Cdd:COG4942   145 aPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK-------AERQKLLARLEKELAELAAELAE 217

                         170       180
                  ....*....|....*....|....*....
gi 1207192617 535 QEEELGRAKADLNRLQQEEAQLEQSLQAG 563
Cdd:COG4942   218 LQQEAEELEALIARLEAEAAAAAERTPAA 246
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 444-583 9.80e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 9.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 444 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQT 523
Cdd:COG1196   674 LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAL 753

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 524 QIHSQESDLQSQEEELGRAKADLNRL------------QQEE------AQLEQsLQAGRIQLETIIKSL--------KAT 577
Cdd:COG1196   754 EELPEPPDLEELERELERLEREIEALgpvnllaieeyeELEErydflsEQRED-LEEARETLEEAIEEIdretrerfLET 832


                  ....*.
gi 1207192617 578 QDEINQ 583
Cdd:COG1196   833 FDAVNE 838
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 414-602 1.12e-05

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 49.33  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEIAQLQSTLAFTHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAqkqdaqdrleem 493
Cdd:pfam05483 425 KQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTA------------ 492

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 494 DQQKAKLEDmlndvRQKCQEESQMISSLQtqihSQESDLQSQEEELGRAKADLNRLQQEEAQLeqslqagRIQLETIIKS 573
Cdd:pfam05483 493 HCDKLLLEN-----KELTQEASDMTLELK----KHQEDIINCKKQEERMLKQIENLEEKEMNL-------RDELESVREE 556

                         170       180
                  ....*....|....*....|....*....
gi 1207192617 574 LKATQDEInqaRSKLSQIQDSQHEISKNI 602
Cdd:pfam05483 557 FIQKGDEV---KCKLDKSEENARSIEYEV 582
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 416-585 1.14e-05

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 49.57  E-value: 1.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  416 LDDISQEIAQLQSTLAFT--HWDTLRE----KYTLEQDiRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQK-----Q 484
Cdd:COG3096    895 LEELREELDAAQEAQAFIqqHGKALAQleplVAVLQSD-PEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRphfsyE 973

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  485 DAQDRLEE----MDQQKAKLEDM----------LNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELG---------- 540
Cdd:COG3096    974 DAVGLLGEnsdlNEKLRARLEQAeearreareqLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEelgvqadaea 1053

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207192617  541 --RAKADLNRLQQE-------EAQLEQSLQAGRIQLETIIKSLKATQDEINQAR 585
Cdd:COG3096   1054 eeRARIRRDELHEElsqnrsrRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQER 1107
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 440-587 1.18e-05

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: 49.40  E-value: 1.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  440 EKYTLEQDIRETEEAI------------RHKTTE--VQEMQNDLDRE---TSSLQEL----EAQKQDAQDRL-------E 491
Cdd:pfam01576  125 EKVTTEAKIKKLEEDIllledqnsklskERKLLEerISEFTSNLAEEeekAKSLSKLknkhEAMISDLEERLkkeekgrQ 204

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  492 EMDQQKAKLEDMLNDVRQKcqeesqmISSLQTQIHSQESDLQSQEEELgraKADLNRLQQEEAQLEQSLQAGRiQLETII 571
Cdd:pfam01576  205 ELEKAKRKLEGESTDLQEQ-------IAELQAQIAELRAQLAKKEEEL---QAALARLEEETAQKNNALKKIR-ELEAQI 273

                          170
                   ....*....|....*.
gi 1207192617  572 KSLKATQDEINQARSK 587
Cdd:pfam01576  274 SELQEDLESERAARNK 289
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 431-605 1.24e-05

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 49.20  E-value: 1.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  431 AFTHWDTLREKYTLEQDIRETE-EAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQD-------RLEEMDQQKA---- 498
Cdd:TIGR00618  301 AVTQIEQQAQRIHTELQSKMRSrAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDahevatsIREISCQQHTltqh 380

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  499 --KLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEElgraKADLNRLQ-QEEAQLEQSLQAgRIQLETIIKSLK 575
Cdd:TIGR00618  381 ihTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDL----QGQLAHAKkQQELQQRYAELC-AAAITCTAQCEK 455

                          170       180       190
                   ....*....|....*....|....*....|
gi 1207192617  576 ATQDEINQARSKLsqiqDSQHEISKNIEQY 605
Cdd:TIGR00618  456 LEKIHLQESAQSL----KEREQQLQTKEQI 481
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 486-608 1.24e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 48.67  E-value: 1.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 486 AQDRLEEMDQQKAKLEDMLNDVRQKcqeesqmISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRI 565
Cdd:COG3883    14 ADPQIQAKQKELSELQAELEAAQAE-------LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207192617 566 QLETIIKSL----------------KATQDEINQArSKLSQIQDSQHEIsknIEQYSST 608
Cdd:COG3883    87 ELGERARALyrsggsvsyldvllgsESFSDFLDRL-SALSKIADADADL---LEELKAD 141
PRK11637 PRK11637
AmiB activator; Provisional
 415-594 1.31e-05

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 48.54  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 415 ELDDISQEIA----------QLQSTLAfthwDTLREKytlEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQkQ 484
Cdd:PRK11637   48 QLKSIQQDIAakeksvrqqqQQRASLL----AQLKKQ---EEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQ-Q 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 485 DAQDRL--EEMDQ-----QKAKLEDM------------------LNDVRQKCQEE-SQMISSLQTQIHSQEsDLQSQEEE 538
Cdd:PRK11637  120 AAQERLlaAQLDAafrqgEHTGLQLIlsgeesqrgerilayfgyLNQARQETIAElKQTREELAAQKAELE-EKQSQQKT 198

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207192617 539 LgrakadLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDS 594
Cdd:PRK11637  199 L------LYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDS 248
DUF4201 pfam13870
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ...
 414-604 1.51e-05

Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. The function is not known.


Pssm-ID: 464008 [Multi-domain]  Cd Length: 177  Bit Score: 46.44  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEIAQLQSTLAFTHwDTLREKYTLEQDIRETE-EAIRhktTEVQEMQNdldretsslqELEAQKQDaqdrLEE 492
Cdd:pfam13870   6 NELSKLRLELITLKHTLAKIQ-EKLEQKEELGEGLTMIDfLQLQ---IENQALNE----------KIEERNKE----LKR 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 493 MDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQslQAGRIQLETIIK 572
Cdd:pfam13870  68 LKLKVTNTVHALTHLKEKLHFLSAELSRLKKELRERQELLAKLRKELYRVKLERDKLRKQNKKLRQ--QGGLLHVPALLH 145

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1207192617 573 SLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:pfam13870 146 DYDKTKAEVEEKRKSVKKLRRKVKILEMRIKE 177
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 411-598 1.52e-05

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 48.27  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 411 TGIKELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRE--TEEAIRHKTTEVQEMQNDLD---RETSSLQE-LEAQKQ 484
Cdd:pfam15905 112 AAVREKTSLSASVASLEKQLL----ELTRVNELLKAKFSEdgTQKKMSSLSMELMKLRNKLEakmKEVMAKQEgMEGKLQ 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 485 DAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQ---TQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQ 561
Cdd:pfam15905 188 VTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLeyiTELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLE 267

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1207192617 562 AGRIQLETIIKSL--------KATQDEINQARSK----LSQIQDSQHEI 598
Cdd:pfam15905 268 EKEQELSKQIKDLnekcklleSEKEELLREYEEKeqtlNAELEELKEKL 316
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 417-594 1.53e-05

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 48.68  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 417 DDISQEIAQLQSTLAFThwDTLREKYTLEQD----IRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEE 492
Cdd:PRK04778  317 DFLEHAKEQNKELKEEI--DRVKQSYTLNESelesVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEE 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 493 MDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHS-----QESDLQSQEEELgraKADLNRLQQEEAQLEQSLQAGRIQL 567
Cdd:PRK04778  395 IEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEikrylEKSNLPGLPEDY---LEMFFEVSDEIEALAEELEEKPINM 471

                         170       180
                  ....*....|....*....|....*..
gi 1207192617 568 ETIIKSLKATQDEINQARSKLSQIQDS 594
Cdd:PRK04778  472 EAVNRLLEEATEDVETLEEETEELVEN 498
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 414-552 1.80e-05

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 47.70  E-value: 1.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  414 KELDDISQEIAQLQSTLafthwDTLREKY-TLEQDIRETEEAirhkTTEVQEM-QNDLDRETSSLQELEAQKQDAQDRLE 491
Cdd:smart00787 158 EDYKLLMKELELLNSIK-----PKLRDRKdALEEELRQLKQL----EDELEDCdPTELDRAKEKLKKLLQEIMIKVKKLE 228

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207192617  492 EMDQQKAKLEDMLNDVRQKCQEesqmissLQTQIHSQESDL-QSQ---EEELGRAKADLNRLQQE 552
Cdd:smart00787 229 ELEEELQELESKIEDLTNKKSE-------LNTEIAEAEKKLeQCRgftFKEIEKLKEQLKLLQSL 286
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
413-587 1.87e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.52  E-value: 1.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 413 IKELDDISQEIAQLQ-STLAFTHWDTLREKYTLE-QDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRL 490
Cdd:PRK03918  275 IEELEEKVKELKELKeKAEEYIKLSEFYEEYLDElREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 491 EEMdQQKAKLedmLNDVRQKcQEESQMISSLQTqIHSQEsDLQSQEEELGRAKadlnrlqqEEAQLEQSLQAGRI-QLET 569
Cdd:PRK03918  355 EEL-EERHEL---YEEAKAK-KEELERLKKRLT-GLTPE-KLEKELEELEKAK--------EEIEEEISKITARIgELKK 419

                         170
                  ....*....|....*...
gi 1207192617 570 IIKSLKATQDEINQARSK 587
Cdd:PRK03918  420 EIKELKKAIEELKKAKGK 437
PTZ00395 PTZ00395
Sec24-related protein; Provisional
 657-774 2.02e-05

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 48.53  E-value: 2.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  657 HTDPFQSEDPFKTDPFKGDPFQNDPFSKPATTVPdPFGGDPFKETdpfrtssedffkkPSKPDPFTNADPfSKSATLPSK 736
Cdd:PTZ00395   419 NSNPGYNNAPNSNTPYNNPPNSNTPYSNPPNSNP-PYSNLPYSNT-------------PYSNAPLSNAPP-SSAKDHHSA 483

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207192617  737 SH----HFASNDPF--ISTSPKPKGQDFFGTLD----------PFGSSTFGSNS 774
Cdd:PTZ00395   484 YHaayqHRAANQPAanLPTANQPAANNFHGAAGnsvgnpfasrPFGSAPYGGNA 537
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 437-591 2.05e-05

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 48.80  E-value: 2.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  437 TLREKYT-LEQDIRETEEAIRhkttEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAkledmlndvrqKCQEEs 515
Cdd:COG3096    516 QLRAQLAeLEQRLRQQQNAER----LLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAA-----------EAVEQ- 579

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  516 qmisslQTQIHSQESDLQSQEEELGR-------AKADLNRLQ-QEEAQLE--QSLQAGRIQLETIIKSLKATQDEINQAR 585
Cdd:COG3096    580 ------RSELRQQLEQLRARIKELAArapawlaAQDALERLReQSGEALAdsQEVTAAMQQLLEREREATVERDELAARK 653


                   ....*..
gi 1207192617  586 SKL-SQI 591
Cdd:COG3096    654 QALeSQI 660
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 438-625 2.09e-05

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 48.50  E-value: 2.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  438 LREKYTLEQDIRETEEAI----RHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQE 513
Cdd:TIGR00606  222 IRDQITSKEAQLESSREIvksyENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDE 301

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  514 EsqmissLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQ------------SLQAGRIQLETIIKSLKATQdei 581
Cdd:TIGR00606  302 Q------LNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQektellveqgrlQLQADRHQEHIRARDSLIQS--- 372

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1207192617  582 NQARSKLSQIQ---DSQHEISKNIEQYSSTLNGTHGGSMTNLADMSE 625
Cdd:TIGR00606  373 LATRLELDGFErgpFSERQIKNFHTLVIERQEDEAKTAAQLCADLQS 419
Tektin pfam03148
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
 413-603 2.30e-05

Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.


Pssm-ID: 460827 [Multi-domain]  Cd Length: 383  Bit Score: 47.93  E-value: 2.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 413 IKELDDISQEIAQLQSTLAFThWDTLRE----KYTLEQDIRETEEAIrHKTTEVQEMQND------------LDRETSSL 476
Cdd:pfam03148 122 LKEVELIEGIQELLQRTLEQA-WEQLRLlraaRHKLEKDLSDKKEAL-EIDEKCLSLNNTspnisykpgptrIPPNSSTP 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 477 QE---------LEAQK--QDAQDRLEEMDQQkakLEDMLNDV-----------RQKCQEESQMISSLQTQ-------IHS 527
Cdd:pfam03148 200 EEwekftqdniERAEKerAASAQLRELIDSI---LEQTANDLraqadavnfalRKRIEETEDAKNKLEWQlkktlqeIAE 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 528 QESDLQSQEEELGRAKADL--------NRLQ-------QEEAQ--LEQSLQagriQLETIIKSLkatQDEINQARSKLSQ 590
Cdd:pfam03148 277 LEKNIEALEKAIRDKEAPLklaqtrleNRTYrpnvelcRDEAQygLVDEVK----ELEETIEAL---KQKLAEAEASLQA 349

                         250
                  ....*....|...
gi 1207192617 591 IQDSQHEISKNIE 603
Cdd:pfam03148 350 LERTRLRLEEDIA 362
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 444-604 2.88e-05

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: 48.25  E-value: 2.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  444 LEQDIRETEEAIRHKTTE-------VQEMQNDLDRETSSLQELEAQKQDAQDRLEEM--------DQQ------KAKLED 502
Cdd:pfam01576   80 LESRLEEEEERSQQLQNEkkkmqqhIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLeedillleDQNsklskeRKLLEE 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  503 MLNDVRQKCQEESQMISSLQTQIHSQE---SDLQ---SQEE----ELGRAK----ADLNRLQQEEAQLEQSLQAGRIQLE 568
Cdd:pfam01576  160 RISEFTSNLAEEEEKAKSLSKLKNKHEamiSDLEerlKKEEkgrqELEKAKrkleGESTDLQEQIAELQAQIAELRAQLA 239

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1207192617  569 TIIKSLKATQDEI-------NQARSKLSQIQDSQHEISKNIEQ 604
Cdd:pfam01576  240 KKEEELQAALARLeeetaqkNNALKKIRELEAQISELQEDLES 282
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 417-592 3.07e-05

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 47.81  E-value: 3.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 417 DDISQEIAQLQSTLAfTHWDtlrEKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRL----EE 492
Cdd:pfam05557 279 EDLSRRIEQLQQREI-VLKE---ENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVllltKE 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 493 MDQQKAKLEDMLNDV---------RQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKadlnrlqQEEAQLEQSLQAG 563
Cdd:pfam05557 355 RDGYRAILESYDKELtmsnyspqlLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYK-------QQAQTLERELQAL 427

                         170       180
                  ....*....|....*....|....*....
gi 1207192617 564 RIQLETiiKSLKATQDEINQARSKLSQIQ 592
Cdd:pfam05557 428 RQQESL--ADPSYSKEEVDSLRRKLETLE 454
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 446-561 3.41e-05

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 44.10  E-value: 3.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 446 QDIRETEEAIRHKTTEVQEMQNDLDREtssLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLqtqi 525
Cdd:pfam13863   6 REMFLVQLALDAKREEIERLEELLKQR---EEELEKKEQELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEK---- 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1207192617 526 hsqesdlqsqEEELGRAKADLNRLQQEEAQLEQSLQ 561
Cdd:pfam13863  79 ----------EKEIKKLTAQIEELKSEISKLEEKLE 104
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 416-591 3.52e-05

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 48.02  E-value: 3.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  416 LDDISQEIAQLQSTLAFTHW---DTLREKY-TLEQDIRETEEAIRH------KTTEVQEMQNDLDRETSSLQELEAQKQD 485
Cdd:COG3096    866 LDQLKEQLQLLNKLLPQANLladETLADRLeELREELDAAQEAQAFiqqhgkALAQLEPLVAVLQSDPEQFEQLQADYLQ 945

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  486 AQDRLEEMDQQKakleDMLNDVRQKC-----QEESQMI---SSLQTQIHSQesdLQSQEEElgRAKADlNRLQQEEAQLE 557
Cdd:COG3096    946 AKEQQRRLKQQI----FALSEVVQRRphfsyEDAVGLLgenSDLNEKLRAR---LEQAEEA--RREAR-EQLRQAQAQYS 1015

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1207192617  558 QSLQAgRIQLETiikSLKATQDEINQARSKLSQI 591
Cdd:COG3096   1016 QYNQV-LASLKS---SRDAKQQTLQELEQELEEL 1045
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 526-610 3.91e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.07  E-value: 3.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 526 HSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQY 605
Cdd:COG4942    16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95


                  ....*
gi 1207192617 606 SSTLN 610
Cdd:COG4942    96 RAELE 100
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 413-632 4.04e-05

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 47.44  E-value: 4.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 413 IKELDDISQEIAQLQSTLAFTHWD-----TLRE---KYTLEQDI----RETEEAIRHKTTE-VQEMQNDLDRETSSLQEL 479
Cdd:pfam07111 189 AKQLAEAQKEAELLRKQLSKTQEEleaqvTLVEslrKYVGEQVPpevhSQTWELERQELLDtMQHLQEDRADLQATVELL 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 480 EAQKQDAQDRL----EEMDQQKAKLEDMLNDVRQKCQE----ESQMISSLQTQIHSQESDLQSQEEELGRAKADLNR--- 548
Cdd:pfam07111 269 QVRVQSLTHMLalqeEELTRKIQPSDSLEPEFPKKCRSllnrWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEqvt 348

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 549 -LQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQA----RSKLSQIQDSQHEISKNIEQYSSTLNGTHgGSMTNLADM 623
Cdd:pfam07111 349 sQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAqearRRQQQQTASAEEQLKFVVNAMSSTQIWLE-TTMTRVEQA 427


                  ....*....
gi 1207192617 624 SEGFPEKEN 632
Cdd:pfam07111 428 VARIPSLSN 436
CENP-H pfam05837
Centromere protein H (CENP-H); This family consists of several eukaryotic centromere protein H ...
 413-511 4.13e-05

Centromere protein H (CENP-H); This family consists of several eukaryotic centromere protein H (CENP-H) sequences. Macromolecular centromere-kinetochore complex plays a critical role in sister chromatid separation, but its complete protein composition as well as its precise dynamic function during mitosis has not yet been clearly determined. CENP-H contains a coiled-coil structure and a nuclear localization signal. CENP-H is specifically and constitutively localized in kinetochores throughout the cell cycle. CENP-H may play a role in kinetochore organization and function throughout the cell cycle. This the C-terminus of the region, which is conserved from fungi to humans.


Pssm-ID: 461756 [Multi-domain]  Cd Length: 114  Bit Score: 43.73  E-value: 4.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 413 IKELDDISQEIAQLQSTlaftHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMqndldretsslqeleAQKQDAQDRLEE 492
Cdd:pfam05837   5 INRRDELSSAILKLSSE----LRELQEELTEVEKENLRLKRKNRELAAELLEL---------------AKEKESRREDPK 65

                          90
                  ....*....|....*....
gi 1207192617 493 MDQQKAKLEDMLNDVRQKC 511
Cdd:pfam05837  66 LRAQLEKLEAELKKSRRRW 84
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
 401-593 4.32e-05

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe Cdc15, and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Schizosaccharomyces pombe Cdc15 and Imp2, and similar proteins. These proteins contain an N-terminal F-BAR domain and a C-terminal SH3 domain. S. pombe Cdc15 and Imp2 play both distinct and overlapping roles in the maintenance and strengthening of the contractile ring at the division site, which is required in cell division. Cdc15 is a component of the actomyosin ring and is required in normal cytokinesis. Imp2 colocalizes with the medial ring during septation and is required for normal septation. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153335 [Multi-domain]  Cd Length: 236  Bit Score: 45.76  E-value: 4.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 401 SSSSVGSGEFTGIKElddisqeiaqlqstlAFthwDTLREkytleqdirETEEAIRHKTTEVQEMQNDL-DRETSSLQEL 479
Cdd:cd07651    46 SRKSLGGSEEGGLKN---------------SL---DTLRL---------ETESMAKSHLKFAKQIRQDLeEKLAAFASSY 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 480 EAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQtqihSQESDLQSQEEELGRAKadLNRLQqeeaqleQS 559
Cdd:cd07651    99 TQKRKKIQSHMEKLLKKKQDQEKYLEKAREKYEADCSKINSYT----LQSQLTWGKELEKNNAK--LNKAQ-------SS 165

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1207192617 560 LQAGRIQLETIIKSLKATQDEINQA-RSKLSQIQD 593
Cdd:cd07651   166 INSSRRDYQNAVKALRELNEIWNREwKAALDDFQD 200
DUF4795 pfam16043
Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. ...
 436-588 4.36e-05

Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 285 and 978 amino acids in length.


Pssm-ID: 464990 [Multi-domain]  Cd Length: 181  Bit Score: 44.99  E-value: 4.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 436 DTLREKYTLEQ----DIRETEEAIRHKTtevQEMQNDLDRETSSLQELEAQKQDaQDRLEEMDQQKAKLEDMLNDVR--- 508
Cdd:pfam16043  10 DQLQALILDLQeeleKLSETTSELSERL---QQRQKHLEALYQQIEKLEKVKAD-KEVVEEELDEKADKEALASKVSrdq 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 509 --QKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQslqagriqletIIKSLKATQDEINQARS 586
Cdd:pfam16043  86 fdETLEELNQMLQELLDKLEGQEDAWKKALETLSEELDTKLDRLELDPLKEL-----------LERRIKALQKLLQEGSE 154


                  ..
gi 1207192617 587 KL 588
Cdd:pfam16043 155 EL 156
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 444-547 4.47e-05

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 45.79  E-value: 4.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 444 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQT 523
Cdd:pfam00261 125 VEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEK 204

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1207192617 524 QIHSQESDLQSQEE-------ELGRAKADLN 547
Cdd:pfam00261 205 EVDRLEDELEAEKEkykaiseELDQTLAELN 235
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 438-596 4.50e-05

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 47.64  E-value: 4.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  438 LRE-KYTLEQdIRET---EEAIRHKTTEVQEM--------QNDLDRETSSLQELE-----AQKQ--DAQDRLEEMDQQKA 498
Cdd:COG3096    238 LREnRMTLEA-IRVTqsdRDLFKHLITEATNYvaadymrhANERRELSERALELRrelfgARRQlaEEQYRLVEMARELE 316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  499 KLEDMLNDVRQKCQEESQMISSLQTQIHSQESdLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLEtiikslkATQ 578
Cdd:COG3096    317 ELSARESDLEQDYQAASDHLNLVQTALRQQEK-IERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLE-------AAE 388

                          170       180
                   ....*....|....*....|.
gi 1207192617  579 DEINQARSKLSQIQ---DSQH 596
Cdd:COG3096    389 EEVDSLKSQLADYQqalDVQQ 409
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 472-609 5.33e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.37  E-value: 5.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  472 ETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQ---KCQEE----------------------SQMISSLQTQIH 526
Cdd:TIGR02169  161 EIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQqleRLRRErekaeryqallkekreyegyelLKEKEALERQKE 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  527 SQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQ--AGRI---------QLETIIKSLKAtqdEINQARS----KLSQI 591
Cdd:TIGR02169  241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEelNKKIkdlgeeeqlRVKEKIGELEA---EIASLERsiaeKEREL 317

                          170
                   ....*....|....*...
gi 1207192617  592 QDSQHEISKNIEQYSSTL 609
Cdd:TIGR02169  318 EDAEERLAKLEAEIDKLL 335
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 436-585 5.57e-05

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 46.87  E-value: 5.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 436 DTLREKYTlEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEaqkQDAQDRLEEMDQQKAKLEDmlndvRQKCQEES 515
Cdd:pfam15709 336 DRLRAERA-EMRRLEVERKRREQEEQRRLQQEQLERAEKMREELE---LEQQRRFEEIRLRKQRLEE-----ERQRQEEE 406

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 516 QMISSLQTQIHSQESDLQSQE--------------EELGRAKADLNRLQQEEAQL--EQSLQAGRIQlETIIKSLKATQD 579
Cdd:pfam15709 407 ERKQRLQLQAAQERARQQQEEfrrklqelqrkkqqEEAERAEAEKQRQKELEMQLaeEQKRLMEMAE-EERLEYQRQKQE 485


                  ....*.
gi 1207192617 580 EINQAR 585
Cdd:pfam15709 486 AEEKAR 491
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 439-592 5.93e-05

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 43.78  E-value: 5.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 439 REKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQEleaqkqdAQDRLE-EMdQQKAKLEDMLNDVRQKCQEESQM 517
Cdd:pfam07926   1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIARE-------AQQNYErEL-VLHAEDIKALQALREELNELKAE 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207192617 518 ISSLQTQIHSQESDLQSQEEELgrakadlnrlQQEEAQLEQSLqagriqletiiKSLKATQDEIN-QARSKLSQIQ 592
Cdd:pfam07926  73 IAELKAEAESAKAELEESEESW----------EEQKKELEKEL-----------SELEKRIEDLNeQNKLLHDQLE 127
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
 293-366 6.41e-05

Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.


Pssm-ID: 289529  Cd Length: 104  Bit Score: 42.75  E-value: 6.41e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207192617 293 DGFVSGLEVKDIFMQSGLHQNLLAHIWALADTRQMGKLTREQFSLAMYLIQQKVSKGL-DPPQALTPDMIPPSER 366
Cdd:pfam12763  23 NNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNIaDVPDELPDWLVPGSKA 97
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 415-593 6.62e-05

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 45.79  E-value: 6.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 415 ELDDISQEIAQLQSTLAFThwDTLREKYTLEQDIRETEEA----IRHKTTE-----------VQEMQNDLDRETSSLQEL 479
Cdd:pfam04849 109 QLGSAREEILQLRHELSKK--DDLLQIYSNDAEESETESScstpLRRNESFsslhgcvqldaLQEKLRGLEEENLKLRSE 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 480 EAQKQDAQDRLEEMDQQkakledMLNDVRQKCQEESQMISSLqtqihsqesdlqsqEEELGRaKADLNRLQQEE-----A 554
Cdd:pfam04849 187 ASHLKTETDTYEEKEQQ------LMSDCVEQLSEANQQMAEL--------------SEELAR-KMEENLRQQEEitsllA 245

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1207192617 555 Q---LEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQD 593
Cdd:pfam04849 246 QivdLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQD 287
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 440-606 7.24e-05

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 46.89  E-value: 7.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  440 EKYTLEQDIRETEEAIRHKTtEVQEMQNDLDRETSSLQELEAQK---QDAQDRLEEMDQQKAKLEDMLNDVRQKCQEEsq 516
Cdd:TIGR00618  544 EEDVYHQLTSERKQRASLKE-QMQEIQQSFSILTQCDNRSKEDIpnlQNITVRLQDLTEKLSEAEDMLACEQHALLRK-- 620

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  517 missLQTQIHSQESDLQSQ--EEELGRAKADLNRLQQEEAQLEQSLQAGRIQ------LETIIKSLKATQDEINQA---R 585
Cdd:TIGR00618  621 ----LQPEQDLQDVRLHLQqcSQELALKLTALHALQLTLTQERVREHALSIRvlpkelLASRQLALQKMQSEKEQLtywK 696

                          170       180
                   ....*....|....*....|.
gi 1207192617  586 SKLSQIQDSQHEISKNIEQYS 606
Cdd:TIGR00618  697 EMLAQCQTLLRELETHIEEYD 717
PRK01156 PRK01156
chromosome segregation protein; Provisional
 413-604 7.33e-05

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 46.82  E-value: 7.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 413 IKELDDISQEIAQLQSTlaftHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLD---RETSSLQELEAQKQDAQDR 489
Cdd:PRK01156  196 NLELENIKKQIADDEKS----HSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDmknRYESEIKTAESDLSMELEK 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 490 LEEMDQQKAKLEDMLNDVRQKCQEEsqmISSLQTQIhsqeSDLQSQEEELGRAKADLNRLQQEEAQLEQsLQAGRIQLEt 569
Cdd:PRK01156  272 NNYYKELEERHMKIINDPVYKNRNY---INDYFKYK----NDIENKKQILSNIDAEINKYHAIIKKLSV-LQKDYNDYI- 342

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1207192617 570 iikSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:PRK01156  343 ---KKKSRYDDLNNQILELEGYEMDYNSYLKSIES 374
YscO pfam07321
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ...
 475-592 7.95e-05

Type III secretion protein YscO; This family contains the bacterial type III secretion protein YscO, which is approximately 150 residues long. YscO has been shown to be required for high-level expression and secretion of the anti-host proteins V antigen and Yops in Yersinia pestis.


Pssm-ID: 399954 [Multi-domain]  Cd Length: 148  Bit Score: 43.54  E-value: 7.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 475 SLQELEAQKQ--DAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQ-MISSLQTQIHSQEsdlqsqeeELGRAKADLNRLQQ 551
Cdd:pfam07321   9 HLREDRAEKAvkRQEQALAAARAAHQQAQASLQDYRAWRPQEEQrLYAEIQGKLVLLK--------ELEKVKQQVALLRE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1207192617 552 EEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQ 592
Cdd:pfam07321  81 NEADLEKQVAEARQQLEAEREALRQARQALAEARRAVEKFA 121
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
444-605 8.51e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.57  E-value: 8.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 444 LEQDIRETEEAIRHKTteVQEMQNDLDRETSSLQELEAQKQDAQDRLEEmdqqkakLEDMLNDVRQKCQEES---QMISS 520
Cdd:PRK02224  192 LKAQIEEKEEKDLHER--LNGLESELAELDEEIERYEEQREQARETRDE-------ADEVLEEHEERREELEtleAEIED 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 521 LQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISK 600
Cdd:PRK02224  263 LRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNE 342


                  ....*
gi 1207192617 601 NIEQY 605
Cdd:PRK02224  343 EAESL 347
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 439-598 1.01e-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: 46.32  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  439 REKYT--------LE--QDIR-ETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDV 507
Cdd:pfam01576  632 REKETralslaraLEeaLEAKeELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQAT 711

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  508 RQ-KCQEESQMiSSLQTQIhsqESDLQSQEEELGRAKADLNR-LQQEEAQLE----QSLQA--GRIQLETIIKSLKATQD 579
Cdd:pfam01576  712 EDaKLRLEVNM-QALKAQF---ERDLQARDEQGEEKRRQLVKqVRELEAELEderkQRAQAvaAKKKLELDLKELEAQID 787

                          170       180
                   ....*....|....*....|....*..
gi 1207192617  580 EINQARS-------KL-SQIQDSQHEI 598
Cdd:pfam01576  788 AANKGREeavkqlkKLqAQMKDLQREL 814
PRK01156 PRK01156
chromosome segregation protein; Provisional
 415-625 1.12e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 46.05  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 415 ELDDISQEIAQLQStlafthwdtlREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDREtSSLQELEAQKQDAQDRLEEMD 494
Cdd:PRK01156  491 EVKDIDEKIVDLKK----------RKEYLESEEINKSINEYNKIESARADLEDIKIKI-NELKDKHDKYEEIKNRYKSLK 559

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 495 QQ--KAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLN--------RLQQEEAQLE---QSLQ 561
Cdd:PRK01156  560 LEdlDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKsyidksirEIENEANNLNnkyNEIQ 639

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207192617 562 AGRIQLETIIKSLKATQDEInqarSKLSQIQDSQHEISKNIEQYSSTLNGTHGGSMTNLADMSE 625
Cdd:PRK01156  640 ENKILIEKLRGKIDNYKKQI----AEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRAR 699
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 443-587 1.15e-04

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 45.40  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 443 TLEQDIRETEEAIRHKTTEVqemqNDLDRETSSLQELEAQ-KQDAQDRLEEMDQQKAKLEDML-----NDVRQkcQEEsq 516
Cdd:pfam04849 168 ALQEKLRGLEEENLKLRSEA----SHLKTETDTYEEKEQQlMSDCVEQLSEANQQMAELSEELarkmeENLRQ--QEE-- 239

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207192617 517 mISSLQTQIhsqeSDLQSQEEELGRAKADLNR-LQQE---EAQLEQSLQAGRIQLETIIKSLKATQDEINQARSK 587
Cdd:pfam04849 240 -ITSLLAQI----VDLQHKCKELGIENEELQQhLQASkeaQRQLTSELQELQDRYAECLGMLHEAQEELKELRKK 309
mukB PRK04863
chromosome partition protein MukB;
443-590 1.16e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 46.10  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  443 TLEQDIRETEEAIRhkttEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQ 522
Cdd:PRK04863   524 ELEQRLRQQQRAER----LLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLA 599

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207192617  523 TQ----IHSQE--SDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKAtqdEInqarSKLSQ 590
Cdd:PRK04863   600 ARapawLAAQDalARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDE---EI----ERLSQ 666
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 481-609 1.17e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 481 AQKQDAQDRLEEMDQQKAKLEDMLNDVrqkcqeESQmISSLQTQ---------IHSQESDLQSQEeelgrAKADLNRLQQ 551
Cdd:COG1196   172 ERKEEAERKLEATEENLERLEDILGEL------ERQ-LEPLERQaekaeryreLKEELKELEAEL-----LLLKLRELEA 239

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207192617 552 EEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTL 609
Cdd:COG1196   240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 451-594 1.21e-04

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 43.79  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 451 TEEAIRHKTTEVQEMQNDLDretsslQELEAQKQDAQDRLEEMDQQ--------KAKLEDMLNDVRQKCQEESQmisSLQ 522
Cdd:pfam01442  24 AQELVDRLEKETEALRERLQ------KDLEEVRAKLEPYLEELQAKlgqnveelRQRLEPYTEELRKRLNADAE---ELQ 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207192617 523 TQIHSQESDLQSQ-EEELGRAKADLN-RLQQEEAQLEQSLQAGRIQLETIIKSLKAtqdeinQARSKLSQIQDS 594
Cdd:pfam01442  95 EKLAPYGEELRERlEQNVDALRARLApYAEELRQKLAERLEELKESLAPYAEEVQA------QLSQRLQELREK 162
bMERB_dom pfam12130
Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact ...
 476-595 1.27e-04

Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact specifically with GTP-bound Rab proteins and mediate their versatile roles in membrane trafficking, including budding of vesicles from a donor membrane, directed transport through the cell and finally tethering and fusion with a target membrane. The 'bivalent Mical/EHBP Rab binding' (bMERB) domain is a Rab effector domain that is present in proteins of the Mical and EHBP families, both known to act in endosomal trafficking. The bMERB domain displays a preference for Rab8 family proteins (Rab8, 10, 13 and 15) and at least some of the bMERB domains contain two separate binding sites for Rab-proteins, allowing Micals and EHBPs to bind two Rabs simultaneously. The strong similarity between the two binding sites within one bMRB domain strongly suggests an evolutionarily development via duplication of a common ancestor supersecondary structure element. The bMERB domain has a completely alpha-helical fold consisting of a central helix and N- and C-terminal helices folding back on this central helix.


Pssm-ID: 463467 [Multi-domain]  Cd Length: 131  Bit Score: 42.89  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 476 LQELEAQkqdaqdrLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIH------SQESDLQSQEEELgrakadlnRL 549
Cdd:pfam12130   2 LEEIEER-------QRELEERGVELEKALRGEMSGDEEEEQLLQEWFKLVNeknalvRRESELMYLAKEQ--------DL 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1207192617 550 QQEEAQLEQSLQAgRIQLETIIKS---LKATQD------EINQARSKLSQIQDSQ 595
Cdd:pfam12130  67 EERQARLEQELRE-LMSKPDWLKTeedKQREEElleelvEIVEQRDALVDSLEED 120
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
413-605 1.29e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 413 IKELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEmqndLDRETSSLQELEAQKQDAQDRLEE 492
Cdd:PRK03918  185 IKRTENIEELIKEKEKELE----EVLREINEISSELPELREELEKLEKEVKE----LEELKEEIEELEKELESLEGSKRK 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 493 MDQQKAKLEDMLNDVRQKCQEESQMISSLqTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAgriqLETIIK 572
Cdd:PRK03918  257 LEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING----IEERIK 331

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1207192617 573 SLKATQDEINQARSKLSQIQDSQHEISKNIEQY 605
Cdd:PRK03918  332 ELEEKEERLEELKKKLKELEKRLEELEERHELY 364
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
435-606 1.32e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 44.90  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 435 WDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEE 514
Cdd:COG1340    11 EELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNEL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 515 SQMISSLQTQIhsqesdlqsqeEELGRAKADLNRLQQEEAQLEQSLQ------------AGRI-QLETIIKSLKA---TQ 578
Cdd:COG1340    91 REELDELRKEL-----------AELNKAGGSIDKLRKEIERLEWRQQtevlspeeekelVEKIkELEKELEKAKKaleKN 159

                         170       180
                  ....*....|....*....|....*...
gi 1207192617 579 DEINQARSKLSQIQDSQHEISKNIEQYS 606
Cdd:COG1340   160 EKLKELRAELKELRKEAEEIHKKIKELA 187
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 421-604 1.37e-04

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 45.41  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 421 QEIAQLQsTLAFTHWDTLREKytlEQDIRETEEAIR-----------------HKTTEVQEMQNDLDRETSSLQELE--- 480
Cdd:pfam15558  21 QRMRELQ-QQAALAWEELRRR---DQKRQETLERERrlllqqsqeqwqaekeqRKARLGREERRRADRREKQVIEKEsrw 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 481 ---AQKQDAQdRLEEMdqQKAKLEDMLndvRQKCQEESqmisslqtqihsqesdLQSQEEELgRAKADLNRLQQ----EE 553
Cdd:pfam15558  97 reqAEDQENQ-RQEKL--ERARQEAEQ---RKQCQEQR----------------LKEKEEEL-QALREQNSLQLqerlEE 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1207192617 554 AQLEQSLQAGRIQLETIIKSLKatqDEIN-QARSKL--SQIQDSQHEISKNIEQ 604
Cdd:pfam15558 154 ACHKRQLKEREEQKKVQENNLS---ELLNhQARKVLvdCQAKAEELLRRLSLEQ 204
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 422-595 1.37e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.88  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 422 EIAQLQSTLAFTHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLE 501
Cdd:pfam17380 399 EAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLE 478

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 502 dmlndvRQKCQEESQMISSLQTQIHSQESDLQSQ---EEELGR--------------AKADLNRLQQEEAQLEQSLQA-G 563
Cdd:pfam17380 479 ------LEKEKRDRKRAEEQRRKILEKELEERKQamiEEERKRkllekemeerqkaiYEEERRREAEEERRKQQEMEErR 552

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1207192617 564 RIQLETIIKSLKATQ-DEINQARSKLSQIQDSQ 595
Cdd:pfam17380 553 RIQEQMRKATEERSRlEAMEREREMMRQIVESE 585
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
463-611 1.53e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 1.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 463 QEMQNDLDRETSSLQELEAQKQDAQDRLEEmdqQKAKLEDMLNDVRQkcqeesqmISSLQTQIHSQESDLQSQEEELGRA 542
Cdd:PRK03918  168 GEVIKEIKRRIERLEKFIKRTENIEELIKE---KEKELEEVLREINE--------ISSELPELREELEKLEKEVKELEEL 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 543 KADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSK--------------------LSQIQDSQHEISKNI 602
Cdd:PRK03918  237 KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkelkelkekaeeyiklsefYEEYLDELREIEKRL 316


                  ....*....
gi 1207192617 603 EQYSSTLNG 611
Cdd:PRK03918  317 SRLEEEING 325
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 516-610 1.62e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 45.59  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 516 QMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLE----TIIKSLKATQDEI---------- 581
Cdd:PRK00409  520 ELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEkeaqQAIKEAKKEADEIikelrqlqkg 599

                          90       100
                  ....*....|....*....|....*....
gi 1207192617 582 NQARSKLSQIQDSQHEISKNIEQYSSTLN 610
Cdd:PRK00409  600 GYASVKAHELIEARKRLNKANEKKEKKKK 628
PRK11281 PRK11281
mechanosensitive channel MscK;
440-592 1.76e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 45.67  E-value: 1.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  440 EKYTLEQDIRETeeairhkttevQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKcQEESQMIS 519
Cdd:PRK11281    57 EDKLVQQDLEQT-----------LALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRE-TLSTLSLR 124

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207192617  520 SLQTQIHSQESDLQSQEEELGRAKADL--NRLQQEEAQLEQSLQAGRIQ-LETIIKSLKATQDEINQARSKLSQIQ 592
Cdd:PRK11281   125 QLESRLAQTLDQLQNAQNDLAEYNSQLvsLQTQPERAQAALYANSQRLQqIRNLLKGGKVGGKALRPSQRVLLQAE 200
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 468-553 1.92e-04

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 45.46  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 468 DLDREtssLQELEAQKQDA--------QDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQT------QIHSQESDLQ 533
Cdd:COG0542   415 ELERR---LEQLEIEKEALkkeqdeasFERLAELRDELAELEEELEALKARWEAEKELIEEIQElkeeleQRYGKIPELE 491

                          90       100
                  ....*....|....*....|
gi 1207192617 534 SQEEELGRAKADLNRLQQEE 553
Cdd:COG0542   492 KELAELEEELAELAPLLREE 511
COG5325 COG5325
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion];
413-610 2.04e-04

t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion];


Pssm-ID: 227635 [Multi-domain]  Cd Length: 283  Bit Score: 44.45  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 413 IKELDDISQEIAQLQSTLAfthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNdldretsslqeleAQKQDAQDRLEE 492
Cdd:COG5325    76 EDEIDELSKKVNQDLQRCE----KILKTKYKNLQSSFLQSKLLRDLNTECMEGQR-------------IQQKSAQFRKYQ 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 493 MDQQKaKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEeLGRAKADLNRLQQEEAQLEQSLQagriQLETIIK 572
Cdd:COG5325   139 VLQAK-FLRNKNNDQHPLEEEEDEESLSSLGSQQTLQQQGLSNEE-LEYQQILITERDEEIKNLARGIY----ELNEIFR 212

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1207192617 573 SLkatQDEINQarsklsqiqdsQHEISKNIEQYSSTLN 610
Cdd:COG5325   213 DL---GSLVGE-----------QGELVDRIDFNIENTS 236
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 414-588 2.19e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 44.52  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEIAQLQSTLAftHWDTLREKYTLEqdirETEEAIRHKttEVQEMQNDLDRETSSLQELEAQKQDAQDRL-EE 492
Cdd:pfam13868 184 REIARLRAQQEKAQDEKA--ERDELRAKLYQE----EQERKERQK--EREEAEKKARQRQELQQAREEQIELKERRLaEE 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 493 MDQQKAKLEDMLNDVRQKC---QEESQMISSLQTQiHSQEsdLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRiqlet 569
Cdd:pfam13868 256 AEREEEEFERMLRKQAEDEeieQEEAEKRRMKRLE-HRRE--LEKQIEEREEQRAAEREEELEEGERLREEEAER----- 327

                         170
                  ....*....|....*....
gi 1207192617 570 iikslkatQDEINQARSKL 588
Cdd:pfam13868 328 --------RERIEEERQKK 338
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 413-613 2.23e-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: 2.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 413 IKELDDISQEIAQLQSTLAFTHwDTLREKytlEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEE 492
Cdd:TIGR04523  39 EKKLKTIKNELKNKEKELKNLD-KNLNKD---EEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKN 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 493 MDQQKAKLEDMLNDVRQKCQE---------------ESQMISS------LQTQIHSQESDLQSQEEELGRAKADLNRLQQ 551
Cdd:TIGR04523 115 DKEQKNKLEVELNKLEKQKKEnkknidkflteikkkEKELEKLnnkyndLKKQKEELENELNLLEKEKLNIQKNIDKIKN 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207192617 552 EEAQLEQSLqagrIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLNGTH 613
Cdd:TIGR04523 195 KLLKLELLL----SNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQ 252
46 PHA02562
endonuclease subunit; Provisional
 461-610 2.61e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 44.62  E-value: 2.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 461 EVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM-DQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEeel 539
Cdd:PHA02562  178 ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKnGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPS--- 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 540 grakADLNRLQQEEAQLEQSLQagriQLETIIK-------------SLKATQDEINQARSKLSQIQDSQHEISKNIEQYS 606
Cdd:PHA02562  255 ----AALNKLNTAAAKIKSKIE----QFQKVIKmyekggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDELE 326


                  ....
gi 1207192617 607 STLN 610
Cdd:PHA02562  327 EIMD 330
Gp58 pfam07902
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage ...
 406-626 2.64e-04

gp58-like protein; Sequences found in this family are derived from a number of bacteriophage and prophage proteins. They are similar to gp58, a minor structural protein of Lactococcus delbrueckii bacteriophage LL-H.


Pssm-ID: 369586 [Multi-domain]  Cd Length: 594  Bit Score: 44.56  E-value: 2.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 406 GSGEFTGI--------KELDDISQEI-----AQLQSTLAFTHWDTLREKY--TLEQDIRETEEAIRHKTTEVQEMQNDLD 470
Cdd:pfam07902  69 GSGESTGLfksleemlSQLKELNLELtdtknSNLWSKIKLNNNGMLREYHndTIKTEIVESAEGIATRISEDTDKKLALI 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 471 RETssLQELEAQKQDAQDRLEEMDQQ-----KAKLE----DMLNDVRQKCQEESQMISSLQTQIHSQESDLQSqeeelGR 541
Cdd:pfam07902 149 NET--ISGIRREYQDADRQLSSSYQAgieglKATMAsdkiGLQAEIQASAQGLSQRYDNEIRKLSAKITTTSS-----GT 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 542 AKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQD----EINQ-------ARSKLSQIQDSQHEISKNIEQYSSTLN 610
Cdd:pfam07902 222 TEAYESKLDDLRAEFTRSNQGMRTELESKISGLQSTQQstayQISQeisnregAVSRVQQDLDSYQRRLQDAEKNYSSLT 301

                         250
                  ....*....|....*.
gi 1207192617 611 GTHGGSMTNLADMSEG 626
Cdd:pfam07902 302 QTVKGLQSTVSDPNSK 317
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 414-594 2.71e-04

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 44.46  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEIAQLQSTLAFTHWDTlrekytleQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM 493
Cdd:pfam06160 305 EQNKELKEELERVQQSYTLNENEL--------ERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEI 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 494 DQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHS-----QESDL----QSQEEELGRAKADLNRLQQeeaQLEQSlqagR 564
Cdd:pfam06160 377 EEEQEEFKESLQSLRKDELEAREKLDEFKLELREikrlvEKSNLpglpESYLDYFFDVSDEIEDLAD---ELNEV----P 449

                         170       180       190
                  ....*....|....*....|....*....|
gi 1207192617 565 IQLETIIKSLKATQDEINQARSKLSQIQDS 594
Cdd:pfam06160 450 LNMDEVNRLLDEAQDDVDTLYEKTEELIDN 479
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
 443-593 2.87e-04

Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.


Pssm-ID: 310534 [Multi-domain]  Cd Length: 258  Bit Score: 43.56  E-value: 2.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 443 TLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKL--EDMLNDVRQkCQEESQMISS 520
Cdd:pfam06008  51 SLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLgeNDFALPSSD-LSRMLAEAQR 129

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207192617 521 LQTQIHSQE--SDLQSQEEELGRAKADLNRLQqeeaQLEQSLQAgriQLETIiksLKATQDEINQARSKLSQIQD 593
Cdd:pfam06008 130 MLGEIRSRDfgTQLQNAEAELKAAQDLLSRIQ----TWFQSPQE---ENKAL---ANALRDSLAEYEAKLSDLRE 194
PRK01156 PRK01156
chromosome segregation protein; Provisional
 410-600 3.03e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 44.89  E-value: 3.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 410 FTGIKELDD-ISQEIAQLQSTLA-FTHWDTLREKYTLEQDIRETEEA----IRHKTTEVQEMQNDLDRETSSLQELEAQK 483
Cdd:PRK01156  134 FVGQGEMDSlISGDPAQRKKILDeILEINSLERNYDKLKDVIDMLRAeisnIDYLEEKLKSSNLELENIKKQIADDEKSH 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 484 QDAQ---DRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKA---DLNRLQQEEAQLE 557
Cdd:PRK01156  214 SITLkeiERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKEleeRHMKIINDPVYKN 293

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1207192617 558 Q-------SLQAGRIQLETIIKSLKATQDEINQARSKLSQIQD--SQHEISK 600
Cdd:PRK01156  294 RnyindyfKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKdyNDYIKKK 345
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 414-605 3.55e-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: 44.40  E-value: 3.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  414 KELDDISQEIAQLQSTLAFTHwdtlREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEem 493
Cdd:pfam01576  833 KKLKNLEAELLQLQEDLAASE----RARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTE-- 906

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  494 dqqkakledMLNDVRQKCQeesQMISSLQTQIHSQESDLQSQE---EELGRAKADLN-RLQQEE-----------AQLEQ 558
Cdd:pfam01576  907 ---------LLNDRLRKST---LQVEQLTTELAAERSTSQKSEsarQQLERQNKELKaKLQEMEgtvkskfkssiAALEA 974

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1207192617  559 SLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQY 605
Cdd:pfam01576  975 KIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQY 1021
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 436-588 3.77e-04

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 44.44  E-value: 3.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  436 DTLREKYTLEQDIR-----ETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQ----DRLEEMDQQKAKLEDMLND 506
Cdd:pfam12128  707 EQKREARTEKQAYWqvvegALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLgvdpDVIAKLKREIRTLERKIER 786

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  507 VRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAkadLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARS 586
Cdd:pfam12128  787 IAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERA---ISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLR 863


                   ..
gi 1207192617  587 KL 588
Cdd:pfam12128  864 GL 865
COG5022 COG5022
Myosin heavy chain [General function prediction only];
437-601 4.09e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 44.30  E-value: 4.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  437 TLREKYTLEQDIRET-------EEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQD---RLEEMDQQKAKLEDMLND 506
Cdd:COG5022    831 KLRETEEVEFSLKAEvliqkfgRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIdvkSISSLKLVNLELESEIIE 910

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  507 VRQKCQ----EESQMISSLQT--QIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQagriQLETIIKSLKATQDE 580
Cdd:COG5022    911 LKKSLSsdliENLEFKTELIArlKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETSE----EYEDLLKKSTILVRE 986

                          170       180
                   ....*....|....*....|.
gi 1207192617  581 INQARSKLSQIQDSQHEISKN 601
Cdd:COG5022    987 GNKANSELKNFKKELAELSKQ 1007
CHASE3 COG5278
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
442-597 4.16e-04

Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];


Pssm-ID: 444089 [Multi-domain]  Cd Length: 530  Bit Score: 44.13  E-value: 4.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 442 YTLEQDIRETEEAIRH---KTTEVQEMQNDL-DRET-----------SSLQELEAQKQDAQDRLEEMDQ-------QKAK 499
Cdd:COG5278    29 YLSLNRLREASEWVEHtyeVLRALEELLSALlDAETgqrgylltgdeSFLEPYEEARAEIDELLAELRSltadnpeQQAR 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 500 LEDMLNDVRQKCQEESQMISSLQTQIHSQESDLqsqeEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQD 579
Cdd:COG5278   109 LDELEALIDQWLAELEQVIALRRAGGLEAALAL----VRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAA 184

                         170
                  ....*....|....*...
gi 1207192617 580 EINQARSKLSQIQDSQHE 597
Cdd:COG5278   185 LLALAELLLLALARALAA 202
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
415-604 4.70e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.26  E-value: 4.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 415 ELDDISQEIAQLQSTL---------AFTHWDTLREKY-TLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQ 484
Cdd:PRK02224  315 RREELEDRDEELRDRLeecrvaaqaHNEEAESLREDAdDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 485 DAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKA-----------DLNRLQQEE 553
Cdd:PRK02224  395 ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCpecgqpvegspHVETIEEDR 474

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1207192617 554 AQLEqSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQhEISKNIEQ 604
Cdd:PRK02224  475 ERVE-ELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLE-ERREDLEE 523
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 449-591 4.75e-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: 4.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 449 RETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQkcQEESQMISSLQTQIHSQ 528
Cdd:COG1196   668 RELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEE--QLEAEREELLEELLEEE 745

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207192617 529 ESDLQSQEEELGRAkADLNRLQQEEAQLEQSLQA-GRI---------QLETIIKSLKATQDEINQARSKLSQI 591
Cdd:COG1196   746 ELLEEEALEELPEP-PDLEELERELERLEREIEAlGPVnllaieeyeELEERYDFLSEQREDLEEARETLEEA 817
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 458-572 4.76e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 41.41  E-value: 4.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 458 KTTEVQEMQNDLDRETSSLQ-ELEAQKQDAQDRLEEMDQQKAKLEDMLNDvrqkcqeesqmisslqtqihsQESDLQSQE 536
Cdd:pfam03938  13 ESPEGKAAQAQLEKKFKKRQaELEAKQKELQKLYEELQKDGALLEEEREE---------------------KEQELQKKE 71

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1207192617 537 EELGRAKADLNR-LQQEEAQLEQSLQAgriQLETIIK 572
Cdd:pfam03938  72 QELQQLQQKAQQeLQKKQQELLQPIQD---KINKAIK 105
46 PHA02562
endonuclease subunit; Provisional
 416-599 4.76e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.85  E-value: 4.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 416 LDDISQEIAQLQSTLA-FTHWDTLREKY----TLEQDIRETEEAIRHKTTEVQEMQNDLDREtsslqeleaqkQDAQDRL 490
Cdd:PHA02562  257 LNKLNTAAAKIKSKIEqFQKVIKMYEKGgvcpTCTQQISEGPDRITKIKDKLKELQHSLEKL-----------DTAIDEL 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 491 EEmdqqkakLEDMLNDVRQKCQEesqmissLQTQIHSQESDLQSQEEELGRAKADLNRlqqeeaqleqsLQAGRIQLETI 570
Cdd:PHA02562  326 EE-------IMDEFNEQSKKLLE-------LKNKISTNKQSLITLVDKAKKVKAAIEE-----------LQAEFVDNAEE 380

                         170       180
                  ....*....|....*....|....*....
gi 1207192617 571 IKSLKATQDEINQARSKLSQIQDSQHEIS 599
Cdd:PHA02562  381 LAKLQDELDKIVKTKSELVKEKYHRGIVT 409
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 414-560 4.99e-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: 44.01  E-value: 4.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  414 KELDDISQEIAQLqstlafthwdtLREKYTLEQDIR-ETE-----EAIR----HKTTEVQEMqndldretssLQELEAQK 483
Cdd:pfam01576   26 SELKELEKKHQQL-----------CEEKNALQEQLQaETElcaeaEEMRarlaARKQELEEI----------LHELESRL 84

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207192617  484 QDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSL 560
Cdd:pfam01576   85 EEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERI 161
PTZ00121 PTZ00121
MAEBL; Provisional
 413-580 5.12e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 5.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  413 IKELDDISQEIAQLQSTLAfthwdtlREKYTLEQdIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEE 492
Cdd:PTZ00121  1625 LKKAEEEKKKVEQLKKKEA-------EEKKKAEE-LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  493 MDQQKAKLEdmlnDVRQKCQEESQMISSLQT----------QIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQA 562
Cdd:PTZ00121  1697 EAEEAKKAE----ELKKKEAEEKKKAEELKKaeeenkikaeEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772

                          170
                   ....*....|....*...
gi 1207192617  563 GRIQLETIIKSLKATQDE 580
Cdd:PTZ00121  1773 IRKEKEAVIEEELDEEDE 1790
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
449-592 5.23e-04

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 43.71  E-value: 5.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 449 RETEEAIR--HKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLE-EMDQQKAKLEDMLNDVRQKCQEESQMisslQTQI 525
Cdd:COG2268   210 RETEIAIAqaNREAEEAELEQEREIETARIAEAEAELAKKKAEERrEAETARAEAEAAYEIAEANAEREVQR----QLEI 285

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207192617 526 HSQESD--LQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKAT---QDEINQARSKLSQIQ 592
Cdd:COG2268   286 AEREREieLQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEaegKRALAEAWNKLGDAA 357
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 402-584 5.25e-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: 44.01  E-value: 5.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  402 SSSVGSGEFTGIKELDDISQEIAQLQSTLAFTHWDTlREKYTLEQDIRETEE---AIRHKTTEVQEMQNDLDRETSSLQe 478
Cdd:pfam01576  446 SSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEET-RQKLNLSTRLRQLEDernSLQEQLEEEEEAKRNVERQLSTLQ- 523

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  479 leAQKQDAQDRLEEM-------DQQKAKLEDMLNDVRQKCQEESqmisslqtqihsqesdlqSQEEELGRAKadlNRLQQ 551
Cdd:pfam01576  524 --AQLSDMKKKLEEDagtlealEEGKKRLQRELEALTQQLEEKA------------------AAYDKLEKTK---NRLQQ 580

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1207192617  552 EEAQLEQSLQAGRiqleTIIKSLKATQDEINQA 584
Cdd:pfam01576  581 ELDDLLVDLDHQR----QLVSNLEKKQKKFDQM 609
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 625-870 5.36e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.99  E-value: 5.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 625 EGFPEKENGGFGAMedPFKVKPTVFNSAPQEMHTDPFQSEDPFKTDPfKGDPFQNDPFS----KPATTVPDPFGGDPFKE 700
Cdd:pfam03154 296 QPFPLTPQSSQSQV--PPGPSPAAPGQSQQRIHTPPSQSQLQSQQPP-REQPLPPAPLSmphiKPPPTTPIPQLPNPQSH 372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 701 TDPFRTSSEDFFKKPSKPDPFTNADPFSKSATLPSKSHH------FASNDPFISTSPKPKGQDFFGTLDPFGSSTFGSNS 774
Cdd:pfam03154 373 KHPPHLSGPSPFQMNSNLPPPPALKPLSSLSTHHPPSAHppplqlMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSG 452

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 775 GFADFSQmskgfveDPFSRKQDMPALPPKKSIPPRPKPPSGKSTPVNVPGSGDPAKTSDPFQPFSADPVDPFQCKKGVGD 854
Cdd:pfam03154 453 LHQVPSQ-------SPFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIKEEALD 525

                         250
                  ....*....|....*.
gi 1207192617 855 pfSGKDPFAPSAPSKA 870
Cdd:pfam03154 526 --EAEEPESPPPPPRS 539
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 444-610 5.45e-04

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 43.89  E-value: 5.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  444 LEQDIRETEEAIRHKTTEVQEMQ--NDLDRET----SSLQELEAQKQDAQDRLEEMD-------QQKAKLEDMLNDVRQK 510
Cdd:PRK10929    80 LSAELRQQLNNERDEPRSVPPNMstDALEQEIlqvsSQLLEKSRQAQQEQDRAREISdslsqlpQQQTEARRQLNEIERR 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  511 CQ---------EESQMiSSLQTQIHSQESDLQSQE---------EELGRAKADLnrLQQEEAQLEQSLQAGRIQL----- 567
Cdd:PRK10929   160 LQtlgtpntplAQAQL-TALQAESAALKALVDELElaqlsannrQELARLRSEL--AKKRSQQLDAYLQALRNQLnsqrq 236

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207192617  568 ---------------------ETIIKSLKATQD---EINQARSKLSQIQDSQHEISKNIEQYSSTLN 610
Cdd:PRK10929   237 reaeralestellaeqsgdlpKSIVAQFKINRElsqALNQQAQRMDLIASQQRQAASQTLQVRQALN 303
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
500-610 6.13e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 6.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 500 LEDMLndvRQKCQEESQMISSLQ--------TQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQsLQAGRIQLETII 571
Cdd:COG4717    43 IRAML---LERLEKEADELFKPQgrkpelnlKELKELEEELKEAEEKEEEYAELQEELEELEEELEE-LEAELEELREEL 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1207192617 572 KSLKATQD------EINQARSKLSQIQDSQHEISKNIEQYSSTLN 610
Cdd:COG4717   119 EKLEKLLQllplyqELEALEAELAELPERLEELEERLEELRELEE 163
PRK12704 PRK12704
phosphodiesterase; Provisional
 471-607 7.01e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.23  E-value: 7.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 471 RETSSLQELEAQKQDAQDRLEEmdqqkAKLEdmLNDVRQKCQEESQ-MISSLQTQIhsqESDLQSQEEELGRAKadlNRL 549
Cdd:PRK12704   25 RKKIAEAKIKEAEEEAKRILEE-----AKKE--AEAIKKEALLEAKeEIHKLRNEF---EKELRERRNELQKLE---KRL 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207192617 550 QQEEAQLE---QSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSS 607
Cdd:PRK12704   92 LQKEENLDrklELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTA 152
IFT57 pfam10498
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles ...
 415-610 7.43e-04

Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles found at the periphery of cells of diverse organizms. Intra-flagellar transport (IFT) is required for the assembly and maintenance of eukaryotic cilia and flagella, and consists of the bidirectional movement of large protein particles between the base and the distal tip of the organelle. IFT particles contain multiple copies of two distinct protein complexes, A and B, which contain at least 6 and 11 protein subunits. IFT57 is part of complex B but is not, however, required for the core subunits to stay associated. This protein is known as Huntington-interacting protein-1 in humans.


Pssm-ID: 463118 [Multi-domain]  Cd Length: 360  Bit Score: 43.02  E-value: 7.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 415 ELDDISQEIAQLQSTLAF--THWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQ-ELEAQKQDAQDRLE 491
Cdd:pfam10498 146 TLEKVEEEMLIEGDDFKEddEDEDLYNESTKGEEAESSKPREIIESNVDAAEWKLELERVLPQLKvTIKADAKDWRAHLE 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 492 EMDQQKAKLEDMLNDVRQKcqeesqmisslqtqihsqesdLQSQEEELGRAkadLNRLQQEEAQLEQslqagriQLETII 571
Cdd:pfam10498 226 QMKQHKKSIEESLPDTKSQ---------------------LDKLHTDISKT---LEKIESREKYINS-------QLEPLI 274

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1207192617 572 KSLKATQDEinqarskLSQIQDSQHEISKNIEQYSSTLN 610
Cdd:pfam10498 275 QEYREAQDE-------LSEVQEKYKQLSEGVTERTRELA 306
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 438-604 7.73e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.42  E-value: 7.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  438 LREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEA-------QKQDAQDRLEEMDQQKAKLEDMLNDVRQK 510
Cdd:TIGR00618  437 QRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQihlqetrKKAVVLARLLELQEEPCPLCGSCIHPNPA 516

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  511 -------------CQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKAT 577
Cdd:TIGR00618  517 rqdidnpgpltrrMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRL 596

                          170       180
                   ....*....|....*....|....*....
gi 1207192617  578 QDEIN-QARSKLSQIQDSQ-HEISKNIEQ 604
Cdd:TIGR00618  597 QDLTEkLSEAEDMLACEQHaLLRKLQPEQ 625
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 415-613 7.80e-04

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 43.50  E-value: 7.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  415 ELDDISQEIAQLQSTlafthwdtlrekytleqdIRETEEAIRHktteVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMD 494
Cdd:TIGR00606  837 ELDTVVSKIELNRKL------------------IQDQQEQIQH----LKSKTNELKSEKLQIGTNLQRRQQFEEQLVELS 894

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  495 QQKAKLEDMLNDVRQKCQEESQMISSLQTQ----IHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRiqleti 570
Cdd:TIGR00606  895 TEVQSLIREIKDAKEQDSPLETFLEKDQQEkeelISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGK------ 968

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1207192617  571 IKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLNGTH 613
Cdd:TIGR00606  969 DDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQK 1011
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 447-607 8.27e-04

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 43.27  E-value: 8.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 447 DIRETEEAIRHKTTEVQEMQNDLDRETSSLQELE----AQKQDaqdrLEEMDQQKAKLEDMLN------DVRQKCQEESQ 516
Cdd:pfam10174 110 TPELTEENFRRLQSEHERQAKELFLLRKTLEEMElrieTQKQT----LGARDESIKKLLEMLQskglpkKSGEEDWERTR 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 517 MISSLQTQIHSQESDLQSQEEELGRAKADL---NRLQQEEAQ---LEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQ 590
Cdd:pfam10174 186 RIAEAEMQLGHLEVLLDQKEKENIHLREELhrrNQLQPDPAKtkaLQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLL 265

                         170
                  ....*....|....*..
gi 1207192617 591 IQDSQHEISKNIEQYSS 607
Cdd:pfam10174 266 HTEDREEEIKQMEVYKS 282
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 371-611 8.44e-04

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 43.29  E-value: 8.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  371 PSLSGYMTPVGSDMAALTEMRRAIMFKLWDSSSSVGS---GEFTGIKELDDISQEIAQLQSTLAFTHWDTLRE--KYTLE 445
Cdd:pfam12128  350 PSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEqnnRDIAGIKDKLAKIREARDRQLAVAEDDLQALESelREQLE 429

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  446 QDIRE-TEEAIRHKT-----------------TEVQEMQND--LDRETSSLQELEAQKQDAQDRLEEM----DQQKAKLE 501
Cdd:pfam12128  430 AGKLEfNEEEYRLKSrlgelklrlnqatatpeLLLQLENFDerIERAREEQEAANAEVERLQSELRQArkrrDQASEALR 509

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  502 DM---LNDVRQKCQE-ESQMISSLQTQIHSQESDLQSQEEELGR--AKADLNR------LQQEEAQLEQSLQAGRIQLET 569
Cdd:pfam12128  510 QAsrrLEERQSALDElELQLFPQAGTLLHFLRKEAPDWEQSIGKviSPELLHRtdldpeVWDGSVGGELNLYGVKLDLKR 589

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1207192617  570 I-IKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLNG 611
Cdd:pfam12128  590 IdVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANG 632
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 409-591 9.08e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.03  E-value: 9.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  409 EFTGIKELDDISQEIAQ----LQSTLAFthwdtlrEKYTLEQDIRETEEAIRHKTTE-VQEMQNDLDRETSSLQ---ELE 480
Cdd:TIGR00618  709 LETHIEEYDREFNEIENasssLGSDLAA-------REDALNQSLKELMHQARTVLKArTEAHFNNNEEVTAALQtgaELS 781

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  481 AQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSL 560
Cdd:TIGR00618  782 HLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQL 861

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1207192617  561 QagriQLETIIKSLKATQDEINQARSKLSQI 591
Cdd:TIGR00618  862 A----QLTQEQAKIIQLSDKLNGINQIKIQF 888
YscO-like pfam16789
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ...
 414-584 9.26e-04

YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. The family includes Chlamydia trachomatis CT670 which is found in a type III secretion gene cluster. CT670 interacts with CT671, a putative YscP homolog and CT670 and CT671 may form a chaperone-effector pair.


Pssm-ID: 435583 [Multi-domain]  Cd Length: 160  Bit Score: 40.97  E-value: 9.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEIAQLQSTLAfthwdtlREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSlqeleaqkqdaqDRLEEM 493
Cdd:pfam16789  14 KRVEEAEKVVKDKKRALE-------KEKEKLAELEAERDKVRKHKKAKMQQLRDEMDRGTTS------------DKILQM 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 494 DQQKAKLEDMLNDVRQKCQEESQmisslqtQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIiks 573
Cdd:pfam16789  75 KRYIKVVKERLKQEEKKVQDQKE-------QVRTAARNLEIAREELKKKRQEVEKLEKHKKEWVKEMKKEEEDQEER--- 144

                         170
                  ....*....|.
gi 1207192617 574 lkaTQDEINQA 584
Cdd:pfam16789 145 ---EQDEIGSA 152
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
416-604 9.28e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 9.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 416 LDDISQEIAQLQSTLAfthwdTLREKY-TLEQDIrETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMD 494
Cdd:PRK02224  470 IEEDRERVEELEAELE-----DLEEEVeEVEERL-ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELR 543

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 495 QQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAkADLNRLQQEEAQLEQSLQAGRIQLETI---- 570
Cdd:PRK02224  544 ERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREALaeln 622

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1207192617 571 -------------IKSLKATQDE--INQARSKLSQIQDSQHEISKNIEQ 604
Cdd:PRK02224  623 derrerlaekrerKRELEAEFDEarIEEAREDKERAEEYLEQVEEKLDE 671
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 448-590 9.55e-04

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 40.76  E-value: 9.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 448 IRETEEAIRHKT---TEVQEMQNDLDRETSSLQELEAQKQDAQdrlEEMDQQKAKLedmlndvrqkcqeesqmiSSLQTQ 524
Cdd:pfam11559  44 LQQRDRDLEFREslnETIRTLEAEIERLQSKIERLKTQLEDLE---RELALLQAKE------------------RQLEKK 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207192617 525 IHSQESDLQSQEEELGRAKadlNRLQQEEAQLEQslqagriqletiikSLKATQDEINQARSKLSQ 590
Cdd:pfam11559 103 LKTLEQKLKNEKEELQRLK---NALQQIKTQFAH--------------EVKKRDREIEKLKERLAQ 151
PRK13735 PRK13735
conjugal transfer mating pair stabilization protein TraG; Provisional
 477-580 9.63e-04

conjugal transfer mating pair stabilization protein TraG; Provisional


Pssm-ID: 184287 [Multi-domain]  Cd Length: 942  Bit Score: 43.20  E-value: 9.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 477 QELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEEL-----GRAKADLNRLQQ 551
Cdd:PRK13735  833 QDIIADHQGHQAIIEQRTQDSGIRNDVKHQVDNMVTEYEGNIGDTQNSIRGEENTVKGQYSELqnhhkTEALSQNNKYNE 912

                          90       100
                  ....*....|....*....|....*....
gi 1207192617 552 EEAqlEQSLQAGRIQLETIIKSLKATQDE 580
Cdd:PRK13735  913 EKS--AQERMPGADSPEELMKRAKEYQDK 939
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
416-600 9.66e-04

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 42.75  E-value: 9.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 416 LDDISQEIAQLQStlafthwdtLREKYtleQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAqkqdAQ---DRLEE 492
Cdd:COG0497   147 LDAFAGLEELLEE---------YREAY---RAWRALKKELEELRADEAERARELDLLRFQLEELEA----AAlqpGEEEE 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 493 MDQQKAKLEDMlNDVRQKCQEESQMISSLQTQIHSQesdlqsqeeeLGRAKADLNRLQQEEAQLE---QSLQAGRIQLET 569
Cdd:COG0497   211 LEEERRRLSNA-EKLREALQEALEALSGGEGGALDL----------LGQALRALERLAEYDPSLAelaERLESALIELEE 279

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1207192617 570 IIKSLKATQD--EINQARskLSQIQDSQHEISK 600
Cdd:COG0497   280 AASELRRYLDslEFDPER--LEEVEERLALLRR 310
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 457-606 9.94e-04

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 39.86  E-value: 9.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 457 HKTTEVQEMQndldretsslQELEAQKQDAQDRLEEMDQQKAKLEDMlndvRQKCQEESQMISSLqtqihsqesdlqsqe 536
Cdd:pfam13863   3 EKKREMFLVQ----------LALDAKREEIERLEELLKQREEELEKK----EQELKEDLIKFDKF--------------- 53

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 537 eelgrakadlnrLQQEEAQLEQSLQagRIQLETIIKSLKatQDEINQARSKLSQIQDSQHEISKNIEQYS 606
Cdd:pfam13863  54 ------------LKENDAKRRRALK--KAEEETKLKKEK--EKEIKKLTAQIEELKSEISKLEEKLEEYK 107
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 452-609 1.03e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.85  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  452 EEAIRHKTTE---VQEMQNDLDRETSSL----QELEAQKQDAQDRL----------EEM----DQQKAKLEDMLNDVRQK 510
Cdd:pfam01576    4 EEEMQAKEEElqkVKERQQKAESELKELekkhQQLCEEKNALQEQLqaetelcaeaEEMrarlAARKQELEEILHELESR 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  511 CQEESQMISSLQTQIHSQESDLQSQEEELgrakadlnrlqQEEAQLEQSLQAGRIQLETIIKSLkatQDEINQARSKLSQ 590
Cdd:pfam01576   84 LEEEEERSQQLQNEKKKMQQHIQDLEEQL-----------DEEEAARQKLQLEKVTTEAKIKKL---EEDILLLEDQNSK 149

                          170
                   ....*....|....*....
gi 1207192617  591 IQDSQHEISKNIEQYSSTL 609
Cdd:pfam01576  150 LSKERKLLEERISEFTSNL 168
mukB PRK04863
chromosome partition protein MukB;
438-597 1.06e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.02  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  438 LREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRL----EEMDQQKaKLEDMLNDVRQKCQ- 512
Cdd:PRK04863   285 LEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLnlvqTALRQQE-KIERYQADLEELEEr 363

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  513 -EESQMISSLQT-QIHSQESDLQSQEEELGRAK---ADLNR---LQQEEA-QLEQSLQA-GRIQ------------LETI 570
Cdd:PRK04863   364 lEEQNEVVEEADeQQEENEARAEAAEEEVDELKsqlADYQQaldVQQTRAiQYQQAVQAlERAKqlcglpdltadnAEDW 443

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1207192617  571 IKSLKATQDEI----NQARSKLSQIQD--SQHE 597
Cdd:PRK04863   444 LEEFQAKEQEAteelLSLEQKLSVAQAahSQFE 476
46 PHA02562
endonuclease subunit; Provisional
 432-620 1.06e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 42.69  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 432 FTHWDTLREKYtleqdIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEM-DQQKAKLEDMLNDVRQk 510
Cdd:PHA02562  165 LSEMDKLNKDK-----IRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKyDELVEEAKTIKAEIEE- 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 511 CQEEsqmISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLE---------QSLQAGRIQLETIIKSLKATQ--- 578
Cdd:PHA02562  239 LTDE---LLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEkggvcptctQQISEGPDRITKIKDKLKELQhsl 315

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1207192617 579 DEINQARSKLSQIQDSQHEISKNIEQYSSTLNgTHGGSMTNL 620
Cdd:PHA02562  316 EKLDTAIDELEEIMDEFNEQSKKLLELKNKIS-TNKQSLITL 356
46 PHA02562
endonuclease subunit; Provisional
 415-607 1.07e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 42.69  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 415 ELDDISQEIAQLQSTLAfthwdtLREKYTLEQDIRETEEairhktteVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMD 494
Cdd:PHA02562  182 QIQTLDMKIDHIQQQIK------TYNKNIEEQRKKNGEN--------IARKQNKYDELVEEAKTIKAEIEELTDELLNLV 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 495 QQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQE---------SDLQSQEEELGRAKADLNRLQQEEAQLE---QSLQA 562
Cdd:PHA02562  248 MDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEkggvcptctQQISEGPDRITKIKDKLKELQHSLEKLDtaiDELEE 327

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1207192617 563 GRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSS 607
Cdd:PHA02562  328 IMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQA 372
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 414-597 1.13e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 42.89  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEIAQLQStlAFTHWDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAqdrleem 493
Cdd:pfam10174 528 QKKEECSKLENQLKK--AHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDK------- 598

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 494 DQQKAKLEDMlndVRQKCQEESQMISSLQtqiHSQesdlqsQEEELGRAKADLNRLQQEEAQLEQSLQagrIQLETIIKS 573
Cdd:pfam10174 599 DKKIAELESL---TLRQMKEQNKKVANIK---HGQ------QEMKKKGAQLLEEARRREDNLADNSQQ---LQLEELMGA 663

                         170       180
                  ....*....|....*....|....
gi 1207192617 574 LKATQDEINQARSKLSQIQDSQHE 597
Cdd:pfam10174 664 LEKTRQELDATKARLSSTQQSLAE 687
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
 415-598 1.18e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 42.87  E-value: 1.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  415 ELDDISQEIAQLQSTLafthwDTLREKYTLE--------QDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKqDA 486
Cdd:PRK10246   683 ELTALQNRIQQLTPLL-----ETLPQSDDLPhseetvalDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQF-DT 756

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  487 QDRLEEMDQQKAKLEDMLND--------VRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQ 558
Cdd:PRK10246   757 ALQASVFDDQQAFLAALLDEetltqleqLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQ 836

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1207192617  559 SLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEI 598
Cdd:PRK10246   837 QLRENTTRQGEIRQQLKQDADNRQQQQALMQQIAQATQQV 876
COG5283 COG5283
Phage-related tail protein [Mobilome: prophages, transposons];
508-607 1.29e-03

Phage-related tail protein [Mobilome: prophages, transposons];


Pssm-ID: 444094 [Multi-domain]  Cd Length: 747  Bit Score: 42.53  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 508 RQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQL--------------ETIIKS 573
Cdd:COG5283    13 KSALESAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALdqagidtrqlsaaqRRLRSS 92

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1207192617 574 LKATQDEINQARSKLSQIQDSQHEISKNIEQYSS 607
Cdd:COG5283    93 LEQTNRQLERQQQRLARLGARQDRLKAARARLQR 126
BBP1_C pfam15272
Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole ...
 459-610 1.52e-03

Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole body component, carries coiled-coils that are necessary for the localization of BBP1 to the spindle pole body (SPB). Although not a membrane protein itself, BBP1 binds to Mps2 as well as to Spc29 and the half-bridge protein Kar1, thus providing a model for how the SPB core is tethered within the nuclear envelope and to the half-bridge


Pssm-ID: 405864 [Multi-domain]  Cd Length: 183  Bit Score: 40.45  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 459 TTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQ-KAKLEDM----LNDVRQ-------------KCQEESQMISS 520
Cdd:pfam15272   3 TSEYLELLDKLDKNNRALHLLNKDVRERDEHYQLQETSyKKKYLQTrnelINELKQskklydnyyklysKYQQLKKISNE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 521 ---LQTQIHSQESDLQSQEEELGRAKADLN-RLQQEEAQ---LEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQD 593
Cdd:pfam15272  83 sldLQSTITNLESQLVDQAIDKDREIHNLNeKILSLELRnqeLETKREIDKMKYESRIDELERQLKEQEYPNVSSSSPYF 162

                         170
                  ....*....|....*..
gi 1207192617 594 SQHEISKNIEQYSSTLN 610
Cdd:pfam15272 163 STSSYRDSSELFSTDYN 179
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 414-546 1.55e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  414 KELDDISQEIAQLQSTLAfthwdTLREKYT-----LEQDIRETEEAIRHKT-TEVQEMQNDLDRETSSLQELEAQKQDAQ 487
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIE-----RLEARLErledrRERLQQEIEELLKKLEeAELKELQAELEELEEELEELQEELERLE 460

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207192617  488 DRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQtqihsqesDLQSQEEELGRAKADL 546
Cdd:TIGR02168  461 EALEELREELEEAEQALDAAERELAQLQARLDSLE--------RLQENLEGFSEGVKAL 511
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 461-614 1.56e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 42.34  E-value: 1.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  461 EVQEMQNDLDRETSSlqeleaqkqdAQDRLEEMDQQKAKLEdmlndvrqkcQEESQMIsslqTQIHSQESDLQSQEEELG 540
Cdd:TIGR00606  692 ELQEFISDLQSKLRL----------APDKLKSTESELKKKE----------KRRDEML----GLAPGRQSIIDLKEKEIP 747

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207192617  541 RAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQArSKLSQIQDSQHEISKNIEQYSSTLNGTHG 614
Cdd:TIGR00606  748 ELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDV-TIMERFQMELKDVERKIAQQAAKLQGSDL 820
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 445-603 1.62e-03

Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".


Pssm-ID: 461718 [Multi-domain]  Cd Length: 562  Bit Score: 42.32  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 445 EQDIRETEEAIRHKTTEVQEMQNDLDRETSslqELEAQKQDAQDRLEEMDQQKAKLEDMlndvRQKCQEESQMISSLQTQ 524
Cdd:pfam05701 285 KKTSTSIQAALASAKKELEEVKANIEKAKD---EVNCLRVAAASLRSELEKEKAELASL----RQREGMASIAVSSLEAE 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 525 IHSQESDL---QSQEEELGRAKADLNRLQQEEAQ-LEQSLQAGRIQLETIIKSlkatQDEINQARSKLSQIQDSQHEISK 600
Cdd:pfam05701 358 LNRTKSEIalvQAKEKEAREKMVELPKQLQQAAQeAEEAKSLAQAAREELRKA----KEEAEQAKAAASTVESRLEAVLK 433


                  ...
gi 1207192617 601 NIE 603
Cdd:pfam05701 434 EIE 436
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 452-567 1.83e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 39.13  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 452 EEAIRHKttevQEMQndlDRetssLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVR-------QKCQEESQMISSLQTQ 524
Cdd:pfam20492   2 EEAEREK----QELE---ER----LKQYEEETKKAQEELEESEETAEELEEERRQAEeeaerleQKRQEAEEEKERLEES 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1207192617 525 IHSQESDLQSQEEELGRAKADLNRLQQE------EA-QLEQSLQAGRIQL 567
Cdd:pfam20492  71 AEMEAEEKEQLEAELAEAQEEIARLEEEverkeeEArRLQEELEEAREEE 120
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 415-588 1.91e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.08  E-value: 1.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  415 ELDDISQEIAQLQSTLAFThwdtLREKYTLEQDIRETEEAI--------------RHKTTEVQEMQNDLDRETSSLQ--- 477
Cdd:pfam01576  862 ERDELADEIASGASGKSAL----QDEKRRLEARIAQLEEELeeeqsntellndrlRKSTLQVEQLTTELAAERSTSQkse 937

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  478 ----ELEAQKQDAQDRLEEMDQQ------------KAKLEDMLNDVRQKCQEESQMISSL-QTQIHSQESDLQSQEEelg 540
Cdd:pfam01576  938 sarqQLERQNKELKAKLQEMEGTvkskfkssiaalEAKIAQLEEQLEQESRERQAANKLVrRTEKKLKEVLLQVEDE--- 1014

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207192617  541 RAKAD---------LNRLQQEEAQLE------QSLQAGR--IQ--LETIIKSLKATQDEINQARSKL 588
Cdd:pfam01576 1015 RRHADqykdqaekgNSRMKQLKRQLEeaeeeaSRANAARrkLQreLDDATESNESMNREVSTLKSKL 1081
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
415-546 2.08e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 2.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  415 ELDDISQEIAQLQSTLafthwDTLREKY---------TLEQDIRETEEAIRHKTTEVQEMQNDLDR----ETSSLQELEA 481
Cdd:COG4913    310 ELERLEARLDALREEL-----DELEAQIrgnggdrleQLEREIERLERELEERERRRARLEALLAAlglpLPASAEEFAA 384

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207192617  482 QKQDAQDRLEEMD-------QQKAKLEDMLNDVRQKCQEESQMISSLQTQ---IHSQESDLQSQ-EEELGRAKADL 546
Cdd:COG4913    385 LRAEAAALLEALEeelealeEALAEAEAALRDLRRELRELEAEIASLERRksnIPARLLALRDAlAEALGLDEAEL 460
CENP-Q pfam13094
CENP-Q, a CENPA-CAD centromere complex subunit; CENP-Q is one of the components that assembles ...
 438-562 2.11e-03

CENP-Q, a CENPA-CAD centromere complex subunit; CENP-Q is one of the components that assembles onto the CENPA-nucleosome distal (CAD) centromere. The centromere, which is the basic element of chromosome inheritance, is epigenetically determined in mammals. CENP-A, the centromere-specific histone H3 variant, assembles an array of nucleosomes and it is this that seems to be the prime candidate for specifying centromere identity. CENPA nucleosomes directly recruit a proximal CENPA-nucleosome-associated complex (NAC) comprised of CENP-M, CENP-N and CENP-T, CENP-U(50), CENP-C and CENP-H. Assembly of the CENPA NAC at centromeres is dependent on CENP-M, CENP-N and CENP-T. Additionally, there are seven other subunits which make up the CENPA-nucleosome distal (CAD) centromere, CENP-K, CENP-L, CENP-O, CENP-P, CENP-Q, CENP-R and CENP-S, also assembling on the CENP-A NAC. Fta7 is the equivalent component of the fission yeast Sim4 complex.


Pssm-ID: 432970 [Multi-domain]  Cd Length: 159  Bit Score: 39.96  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 438 LREKYTLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQM 517
Cdd:pfam13094  25 LDRNKALEAQLSAELHSLELLEEEIEKEEALLESDEEYLEELEKNAKAEARERKEKLKKEHPLLQEDDSGVLSLPELSSD 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1207192617 518 ISSLQTQIHSQESDLQSQEEELGRA-KADLNRLQQEEAQLEQSLQA 562
Cdd:pfam13094 105 LGLGDTDFSLFDPTLDEELLPLLEQlQKHLESMQGNLAQLEGLNEA 150
SPEC smart00150
Spectrin repeats;
442-538 2.24e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 38.46  E-value: 2.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  442 YTLEQDIRETEEAIRHKttEVQEMQNDLdreTSSLQELEAQKQDAQDRLEEMDQQKAKLEDML---NDVRQKCQEESQMI 518
Cdd:smart00150   1 QQFLRDADELEAWLEEK--EQLLASEDL---GKDLESVEALLKKHEAFEAELEAHEERVEALNelgEQLIEEGHPDAEEI 75

                           90       100
                   ....*....|....*....|
gi 1207192617  519 SSLQTQIHSQESDLQSQEEE 538
Cdd:smart00150  76 EERLEELNERWEELKELAEE 95
Lipase_chap pfam03280
Proteobacterial lipase chaperone protein;
435-539 2.38e-03

Proteobacterial lipase chaperone protein;


Pssm-ID: 427230 [Multi-domain]  Cd Length: 185  Bit Score: 39.99  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 435 WDTLREKytLEQDIRETEEAiRHKTTEVQEMQNDLDRETSSLQELEAQKQ-----DAQDRLEEMDQQ----KAKLEDMLn 505
Cdd:pfam03280  84 LAALRAQ--LPEDLRAAREA-QQRLQELAARTAQLQKAGASPQQLRQARAqlvgpEAAQRLAALDQQraawQQRLDDYL- 159

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1207192617 506 dvrqkcQEESQMisslqTQIHSQESDLQSQEEEL 539
Cdd:pfam03280 160 ------AERQQI-----NAAGLSEQERQAAIAQL 182
PTZ00491 PTZ00491
major vault protein; Provisional
 459-587 2.40e-03

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 41.93  E-value: 2.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 459 TTEVQEMQndldretsSLQELEAQKQDAQDRLEemdQQKakledMLNDVrqkcQEESQMISSLQTQIHSQ--ESDLQSQE 536
Cdd:PTZ00491  660 TTKSQEAA--------ARHQAELLEQEARGRLE---RQK-----MHDKA----KAEEQRTKLLELQAESAavESSGQSRA 719

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1207192617 537 EELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQD-EINQARSK 587
Cdd:PTZ00491  720 EALAEAEARLIEAEAEVEQAELRAKALRIEAEAELEKLRKRQElELEYEQAQ 771
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 482-584 2.66e-03

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 39.82  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 482 QKQDAQDRLE-EMDQQKAKLEDMLNDVR---QKCQEESQMISslqtqihsqESDLQSQEEELGRAKADLNRLQQEeaqLE 557
Cdd:COG2825    40 EGKAAQKKLEkEFKKRQAELQKLEKELQalqEKLQKEAATLS---------EEERQKKERELQKKQQELQRKQQE---AQ 107

                          90       100
                  ....*....|....*....|....*..
gi 1207192617 558 QSLQAGRIQLetiiksLKATQDEINQA 584
Cdd:COG2825   108 QDLQKRQQEL------LQPILEKIQKA 128
Zwint pfam15556
ZW10 interactor; This family of proteins is found in eukaryotes. Proteins in this family are ...
 414-561 2.83e-03

ZW10 interactor; This family of proteins is found in eukaryotes. Proteins in this family are typically between 127 and 281 amino acids in length.


Pssm-ID: 464766 [Multi-domain]  Cd Length: 252  Bit Score: 40.73  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEIAQLQSTLAFT-HWDTLREKYtleqdiRETEEAIRHKTTEVQEMQNDLDRETSSLQE----LEAQKQDAQD 488
Cdd:pfam15556  46 QGLDPLASEDTSRQKAIAAKeQWKELKATY------QEHVEAITSALTQALPKMEEAQRKRAQLQEaleqLQAKKQMAME 119

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207192617 489 RLEEMDQQkakledmlndvRQKCQEES-QMISSLQTQIHSQESDLQsqeEELGRAKADLNRLQQEEAQLEQSLQ 561
Cdd:pfam15556 120 KLRTAQKQ-----------WQLQQEKHlQHLAEVSAEVRERQTGTQ---QELERLYQELGTLKQQAGQERDKLQ 179
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
 461-592 3.13e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 41.32  E-value: 3.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  461 EVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEEsQMISSLQtqihSQESDLQS------ 534
Cdd:PRK10246   434 QIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKTICEQE-ARIKDLE----AQRAQLQAgqpcpl 508

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  535 ------------QEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKatQDEiNQARSKLSQIQ 592
Cdd:PRK10246   509 cgstshpaveayQALEPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQ--RDE-SEAQSLRQEEQ 575
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 436-645 3.23e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 41.35  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 436 DTLREKY-TLEQDIRETEEAIrhktTEVQEMQNDLDRETSSLQE-LEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQE 513
Cdd:pfam10174 418 AGLKERVkSLQTDSSNTDTAL----TTLEEALSEKERIIERLKEqREREDRERLEELESLKKENKDLKEKVSALQPELTE 493

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 514 ESQMISSLQTQIHSQESD-------LQSQEEELGRAKADLNRLQ---QEEAQLEQSLQAG-----RIQ-LETIIKSLK-- 575
Cdd:pfam10174 494 KESSLIDLKEHASSLASSglkkdskLKSLEIAVEQKKEECSKLEnqlKKAHNAEEAVRTNpeindRIRlLEQEVARYKee 573

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207192617 576 --ATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLNGTHGGSMTNLADMSEGFPEKENGGFGAMEDPFKVK 645
Cdd:pfam10174 574 sgKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRRE 645
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 438-575 3.32e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 40.64  E-value: 3.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 438 LREKYTLEQDIRETEEAIRHKTTEVQEMQndlDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEEsqm 517
Cdd:cd16269   176 LQSKEAEAEAILQADQALTEKEKEIEAER---AKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEE--- 249

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207192617 518 isslqtqihsqesdLQSQEEELGRAKAdlNRLQQEEAQLEQSLQAGRIQLETIIKSLK 575
Cdd:cd16269   250 --------------RENLLKEQERALE--SKLKEQEALLEEGFKEQAELLQEEIRSLK 291
KpsE COG3524
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
417-569 3.57e-03

Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442746 [Multi-domain]  Cd Length: 370  Bit Score: 40.60  E-value: 3.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 417 DDISQEIAQlqstlafthwDTLRekyTLEQDIRETEEAIRHKTTEVQEMQN-----DLDRETSSLQ----ELEAQKQDAQ 487
Cdd:COG3524   168 NQLSERARE----------DAVR---FAEEEVERAEERLRDAREALLAFRNrngilDPEATAEALLqliaTLEGQLAELE 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 488 drleemdQQKAKLEDMLND----VRQKcqeESQmISSLQTQIHSQESDL--QSQEEELGRAKADLNRLQQEEAQLEQSLQ 561
Cdd:COG3524   235 -------AELAALRSYLSPnspqVRQL---RRR-IAALEKQIAAERARLtgASGGDSLASLLAEYERLELEREFAEKAYT 303


                  ....*...
gi 1207192617 562 AGRIQLET 569
Cdd:COG3524   304 SALAALEQ 311
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 420-639 3.87e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 41.10  E-value: 3.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 420 SQEIAQLQSTLA---FTHWDTLREkYTLEQDIR---ETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQ-KQDAQDRLEE 492
Cdd:COG5185   277 SKRLNENANNLIkqfENTKEKIAE-YTKSIDIKkatESLEEQLAAAEAEQELEESKRETETGIQNLTAEiEQGQESLTEN 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 493 MDQQKAKLEDMLNDVR-----QKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKAD-LNRLQQEEAQLEQSLQAGRIQ 566
Cdd:COG5185   356 LEAIKEEIENIVGEVElskssEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDtLKAADRQIEELQRQIEQATSS 435

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207192617 567 LETIIKSLKATQDEINQAR-----SKLSQIQDSQHEISKNIEQYSSTLNGTHggsmTNLADMSEGFPEKENGGFGAME 639
Cdd:COG5185   436 NEEVSKLLNELISELNKVMreadeESQSRLEEAYDEINRSVRSKKEDLNEEL----TQIESRVSTLKATLEKLRAKLE 509
Mod_r pfam07200
Modifier of rudimentary (Mod(r)) protein; This family represents a conserved region ...
 446-577 3.88e-03

Modifier of rudimentary (Mod(r)) protein; This family represents a conserved region approximately 150 residues long within a number of eukaryotic proteins that show homology with Drosophila melanogaster Modifier of rudimentary (Mod(r)) proteins. The N-terminal half of Mod(r) proteins is acidic, whereas the C-terminal half is basic, and both of these regions are represented in this family. Members of this family include the Vps37 subunit of the endosomal sorting complex ESCRT-I, a complex involved in recruiting transport machinery for protein sorting at the multivesicular body (MVB). The yeast ESCRT-I complex consists of three proteins (Vps23, Vps28 and Vps37). The mammalian homolog of Vps37 interacts with Tsg101 (Pfam: PF05743) through its mod(r) domain and its function is essential for lysosomal sorting of EGF receptors.


Pssm-ID: 462117 [Multi-domain]  Cd Length: 146  Bit Score: 38.75  E-value: 3.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 446 QDIRETEEAIR---HKTTEVQEMQNDLDRETSSLQELeaqkqdAQDRLEemdqqkakLEDMLNDVRQKCQEESQMISSLQ 522
Cdd:pfam07200   9 QELLNDEDKLDafvHSLPQVKALQAEKEELLAENESL------AEENLS--------LEPELEELRSQLQELLEELKALK 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207192617 523 TQIHSQESDLQSQEEELGRAkADLNRLQ-----QEEA--QLEQSLQAGRIQLETIIKSLKAT 577
Cdd:pfam07200  75 SEYEEKEQELDELLSKFSPD-ALLARLQaaaaeAEEEseALAESFLEGEIDLDEFLKQFKEK 135
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 436-593 3.89e-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: 40.83  E-value: 3.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 436 DTLREKYTLEQDIRETEeairHKTTEVQEMQNDLDRETSSLQELEAQKQD--------------AQDRLEEMDQQKAKLE 501
Cdd:pfam05622   4 EAQEEKDELAQRCHELD----QQVSLLQEEKNSLQQENKKLQERLDQLESgddsgtpggkkyllLQKQLEQLQEENFRLE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 502 DMLNDVRQKCQEesqmissLQTQIhsqeSDLQSQEEELGRAKADLNRLQQEEAQLEQSlqAGRI-QLETIIKSLKATQDE 580
Cdd:pfam05622  80 TARDDYRIKCEE-------LEKEV----LELQHRNEELTSLAEEAQALKDEMDILRES--SDKVkKLEATVETYKKKLED 146

                         170
                  ....*....|...
gi 1207192617 581 INQARSKLSQIQD 593
Cdd:pfam05622 147 LGDLRRQVKLLEE 159
mukB PRK04863
chromosome partition protein MukB;
462-608 3.99e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.10  E-value: 3.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  462 VQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDV---------RQKCQE------ESQMISSLQTQIH 526
Cdd:PRK04863   444 LEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVsrseawdvaRELLRRlreqrhLAEQLQQLRMRLS 523

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  527 SQESDLQSQeEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDsqhEISKNIEQYS 606
Cdd:PRK04863   524 ELEQRLRQQ-QRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLE---QLQARIQRLA 599


                   ..
gi 1207192617  607 ST 608
Cdd:PRK04863   600 AR 601
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
 447-565 4.08e-03

Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.


Pssm-ID: 405647 [Multi-domain]  Cd Length: 206  Bit Score: 39.75  E-value: 4.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 447 DIRETEEAIRHKTTEVQEMQNDL-DRETSSLQELEAQKQDAQDR-------LEEMDQQKAKLEDMLndvRQKCQEESQmI 518
Cdd:pfam14988   1 ENKFFLEYLAKKTEEKQKKIEKLwNQYVQECEEIERRRQELASRytqqtaeLQTQLLQKEKEQASL---KKELQALRP-F 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1207192617 519 SSLQTQihsQESDLQSQEEELGRAKADLN--------RLQQEEAQLEQSLQAGRI 565
Cdd:pfam14988  77 AKLKES---QEREIQDLEEEKEKVRAETAekdreahlQFLKEKALLEKQLQELRI 128
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 413-614 4.14e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 41.19  E-value: 4.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  413 IKELDDISQEIaQLQSTLafthwDTLREKYTLEQDIRETEEAIRHKTTEVQEMQNDLdreTSSLQELEAQKQDAQDRLEE 492
Cdd:TIGR00606  363 IRARDSLIQSL-ATRLEL-----DGFERGPFSERQIKNFHTLVIERQEDEAKTAAQL---CADLQSKERLKQEQADEIRD 433

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  493 MDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQE---EAQL--EQSLQAGRIQL 567
Cdd:TIGR00606  434 EKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNsltETLKkeVKSLQNEKADL 513

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207192617  568 ETIIKSLKATQDEINQARSKLSQIQ-------DSQHEISKNIEQYSSTLNGTHG 614
Cdd:TIGR00606  514 DRKLRKLDQEMEQLNHHTTTRTQMEmltkdkmDKDEQIRKIKSRHSDELTSLLG 567
PRK09039 PRK09039
peptidoglycan -binding protein;
444-593 4.41e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 40.33  E-value: 4.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 444 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNdvrqkcqEESQMISSLQT 523
Cdd:PRK09039   44 LSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLA-------ELAGAGAAAEG 116

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 524 QIHSQESDLQSQEEELGRAKADLNRLQQeeaQLEqslqAGRIQLETIIKSLKATQDEInqaRSKLSQIQD 593
Cdd:PRK09039  117 RAGELAQELDSEKQVSARALAQVELLNQ---QIA----ALRRQLAALEAALDASEKRD---RESQAKIAD 176
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 444-518 4.50e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 38.33  E-value: 4.50e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207192617  444 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQelEAQKQDAQDRLEEMDQQ-KAKLEDMLNDVRQKCQEESQMI 518
Cdd:smart00935  23 LEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS--EAAREKKEKELQKKVQEfQRKQQKLQQDLQKRQQEELQKI 96
ING_ING3_Yng2p cd16858
Inhibitor of growth (ING) domain of inhibitor of growth protein 3 (ING3), Yng2p and similar ...
 444-526 4.58e-03

Inhibitor of growth (ING) domain of inhibitor of growth protein 3 (ING3), Yng2p and similar proteins; ING3, also termed p47ING3, is a member of the inhibitor of growth (ING) family of type II tumor suppressors. It is ubiquitously expressed and has been implicated in transcription modulation, cell cycle control, and the induction of apoptosis. It is an important subunit of human NuA4 histone acetyltransferase complex, which regulates the acetylation of histones H2A and H4. Moreover, ING3 promotes ultraviolet (UV)-induced apoptosis through the Fas/caspase-8-dependent pathway in melanoma cells. It physically interacts with subunits of E3 ligase Skp1-Cullin-F-boxprotein complex (SCF complex) and is degraded by the SCF (F-box protein S-phase kinase-associated protein 2, Skp2)-mediated ubiquitin-proteasome system. It also acts as a suppression factor during tumorigenesis and progression of hepatocellular carcinoma (HCC). Yeast chromatin modification-related protein Yng2p, also termed ESA1-associated factor 4 or ING1 homolog 2, is a subunit of the NuA4 histone acetyltransferase (HAT) complex. It plays a critical role in intra-S-phase DNA damage response. Members of this family contain an N-terminal leucine zipper-like (LZL) motif-containing ING domain, and a well-characterized C-terminal plant homeodomain (PHD)-type zinc-finger domain.


Pssm-ID: 341091  Cd Length: 92  Bit Score: 37.18  E-value: 4.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 444 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELeAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQT 523
Cdd:cd16858     4 LPSELRHLLTEIREKDLQVQELLDRIQQRDAKLFKH-IKKNGSLTPNPKEEELYEKIREDYDKALELADEKVELANRLLD 82


                  ...
gi 1207192617 524 QIH 526
Cdd:cd16858    83 LVD 85
ClyA-like cd21116
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ...
 463-592 5.16e-03

family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).


Pssm-ID: 439149 [Multi-domain]  Cd Length: 224  Bit Score: 39.32  E-value: 5.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 463 QEMQNDLDRETSSLQEleaQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRA 542
Cdd:cd21116    76 PDLIELADNLIKGDQG---AKQQLLQGLEALQSQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDATKAQAQVAVLNAL 152

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1207192617 543 KADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQ 592
Cdd:cd21116   153 KNQLNSLAEQIDAAIDALEKLSNDWQTLDSDIKELITDLEDAESSIDAAF 202
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 452-603 5.50e-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: 5.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  452 EEAIRHKTTEVQEMQNDLDRETSS--------------LQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQM 517
Cdd:pfam01576  741 EEKRRQLVKQVRELEAELEDERKQraqavaakkkleldLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARAS 820

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  518 ISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSlqagRIQL-ETIIKSLK---ATQDEINQARSKLSQIQD 593
Cdd:pfam01576  821 RDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQE----RDELaDEIASGASgksALQDEKRRLEARIAQLEE 896

                          170
                   ....*....|
gi 1207192617  594 SQHEISKNIE 603
Cdd:pfam01576  897 ELEEEQSNTE 906
ALIX_LYPXL_bnd pfam13949
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ...
 436-604 5.52e-03

ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV p9Gag to this domain is necessary for viral budding.This domain is generally central between an N-terminal Bro1 domain, pfam03097 and a C-terminal proline-rich domain. The retroviruses thus used this domain to hijack the ESCRT system of the cell.


Pssm-ID: 464053 [Multi-domain]  Cd Length: 294  Bit Score: 39.91  E-value: 5.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 436 DTLREKY--------------TLEQDIRETEEAIRHKTT-------EVQEMQNDLDRETSSLQELEAQ--KQDAQDRLEE 492
Cdd:pfam13949  55 EQLRAKYgtrwtrppsseltaTLRAEIRKYREILEQASEsdsqvrsKFREHEEDLELLSGPDEDLEAFlpSSRRAKNSPS 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 493 MDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIH------------------SQESDLqsQEEELGRAKADLNRLQQ--- 551
Cdd:pfam13949 135 VEEQVAKLRELLNKLNELKREREQLLKDLKEKARnddispklllekarliapNQEEQL--FEEELEKYDPLQNRLEQnlh 212

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1207192617 552 EEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQ 604
Cdd:pfam13949 213 KQEELLKEITEANNEFLQDKRVDSEKQRQREEALQKLENAYDKYKELVSNLQE 265
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 463-555 5.64e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 40.71  E-value: 5.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  463 QEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRA 542
Cdd:PRK11448   145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEITDQ 224

                           90
                   ....*....|...
gi 1207192617  543 KAdlNRLQQEEAQ 555
Cdd:PRK11448   225 AA--KRLELSEEE 235
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 413-604 5.65e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 40.20  E-value: 5.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 413 IKELDDISQEIAQL----------------QSTLAFTHWdtlREKYT---------LEQDIRETEEAIRhkTTEVQEMQN 467
Cdd:PRK04778   31 IDELEERKQELENLpvndelekvkklnltgQSEEKFEEW---RQKWDeivtnslpdIEEQLFEAEELND--KFRFRKAKH 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 468 DLDRETSSLQELEAQKQDAQDRLEEMDQQKAK-------LEDMLNDVRQKCQEESQM----ISSLQTQIHSQESDLQSQE 536
Cdd:PRK04778  106 EINEIESLLDLIEEDIEQILEELQELLESEEKnreeveqLKDLYRELRKSLLANRFSfgpaLDELEKQLENLEEEFSQFV 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 537 E--ELG---RAKADLNRLQQEEAQLEQSLQagriQLETIIKSLKAT-QDEINQARS---KL-------------SQIQDS 594
Cdd:PRK04778  186 EltESGdyvEAREILDQLEEELAALEQIME----EIPELLKELQTElPDQLQELKAgyrELveegyhldhldieKEIQDL 261

                         250
                  ....*....|
gi 1207192617 595 QHEISKNIEQ 604
Cdd:PRK04778  262 KEQIDENLAL 271
KpsE COG3524
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
472-605 5.76e-03

Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442746 [Multi-domain]  Cd Length: 370  Bit Score: 40.22  E-value: 5.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 472 ETSSLQELEAQKQDAQD--RLEEMDQQKAklEDMLNDVRQKCQEEsqmisslqtQIHSQESDLQSQEEELGRAKADLNRL 549
Cdd:COG3524   135 STSGIITLEVRAFDPEDaqAIAEALLAES--EELVNQLSERARED---------AVRFAEEEVERAEERLRDAREALLAF 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 550 QQEE----------------AQLEQSLQAGRIQLETI----------IKSLK----ATQDEINQARSKLSQiQDSQHEIS 599
Cdd:COG3524   204 RNRNgildpeataeallqliATLEGQLAELEAELAALrsylspnspqVRQLRrriaALEKQIAAERARLTG-ASGGDSLA 282


                  ....*.
gi 1207192617 600 KNIEQY 605
Cdd:COG3524   283 SLLAEY 288
DivIC pfam04977
Septum formation initiator; DivIC from B. subtilis is necessary for both vegetative and ...
 527-588 5.85e-03

Septum formation initiator; DivIC from B. subtilis is necessary for both vegetative and sporulation septum formation. These proteins are mainly composed of an amino terminal coiled-coil.


Pssm-ID: 428231 [Multi-domain]  Cd Length: 69  Bit Score: 36.43  E-value: 5.85e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207192617 527 SQESDLQSQEEELGRAKADLNRLQQEEAQLEQSlqagriqletiIKSLKATQDEI-NQARSKL 588
Cdd:pfam04977   3 NGLLTYYQLKQEIAQLQAEIAKLKQENEELEAE-----------IKDLKSDPDYIeERARSEL 54
46 PHA02562
endonuclease subunit; Provisional
 436-600 6.00e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.38  E-value: 6.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 436 DTLREKY-TLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEemdqQKAKLEDMLND------VR 508
Cdd:PHA02562  216 ARKQNKYdELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIE----QFQKVIKMYEKggvcptCT 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 509 QKCQEESQMISSLQTQIHS---QESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQA- 584
Cdd:PHA02562  292 QQISEGPDRITKIKDKLKElqhSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELq 371

                         170       180
                  ....*....|....*....|..
gi 1207192617 585 ------RSKLSQIQDSQHEISK 600
Cdd:PHA02562  372 aefvdnAEELAKLQDELDKIVK 393
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 414-625 6.27e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 40.19  E-value: 6.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 414 KELDDISQEIAQLQSTLafthwDTLREKYT-LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEE 492
Cdd:pfam10174 296 QELSKKESELLALQTKL-----ETLTNQNSdCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQD 370

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 493 MDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEE-------AQLEQSLQagri 565
Cdd:pfam10174 371 LTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSsntdtalTTLEEALS---- 446

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 566 QLETIIKSLKATQDEINQARskLSQIQDSQHEIsKNIEQYSSTLNGTHGGSMTNLADMSE 625
Cdd:pfam10174 447 EKERIIERLKEQREREDRER--LEELESLKKEN-KDLKEKVSALQPELTEKESSLIDLKE 503
HAUS-augmin3 pfam14932
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found ...
 444-601 6.41e-03

HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found from Drosophila to humans. The HAUS-augmin complex is made up of eight subunits. The augmin complex interacts with gamma-TuRC, and attenuation of this interaction severely impairs spindle MT generation. Furthermore, we provide evidence that human augmin plays critical and non-redundant roles in the kinetochore-MT attachment and also central spindle formation during anaphase in human cells.The HAUS complex is required for mitotic spindle assembly and for maintenance of centrosome integrity.


Pssm-ID: 464384 [Multi-domain]  Cd Length: 261  Bit Score: 39.61  E-value: 6.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 444 LEQDIRETEEAIRHKTTEVQEMQ----------NDLDRETSSLQ----ELEAQKQDAQDRLEEMDQQKAKLEDMLNDVRQ 509
Cdd:pfam14932  72 LEESLEEIREATEDLEAELQELQktkqlkinrlNKLQAQASSLSqglrALVAEEEEAAKQLEELQEELAALNAKTNNVLQ 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 510 KCQEESQMISSLQTQIH-----SQeSDLQ---SQEEELGRAkadLNRLQQEeaQLEQSLQA-------GRIQLETIIKSL 574
Cdd:pfam14932 152 SLQSEVKELASFFSASEppvflSQ-LPLEpylLQEEQFTKY---LTLYTKK--QFFQGISElvefsneERFQLLDLSDCS 225

                         170       180
                  ....*....|....*....|....*....
gi 1207192617 575 KATQDE--INQARSKLSQIQdSQHEISKN 601
Cdd:pfam14932 226 ERDSDEvdVEHRRSELARLQ-SAYICAQL 253
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 527-593 6.72e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 36.77  E-value: 6.72e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207192617 527 SQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQD 593
Cdd:cd22887     1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQE 67
ClyA-like cd21116
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ...
 444-591 6.77e-03

family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).


Pssm-ID: 439149 [Multi-domain]  Cd Length: 224  Bit Score: 39.32  E-value: 6.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 444 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQkakledmLNDVRQKCQEESQMISSLQT 523
Cdd:cd21116    82 ADNLIKGDQGAKQQLLQGLEALQSQVTKKQTSVTSFINELTTFKNDLDDDSRN-------LQTDATKAQAQVAVLNALKN 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 524 QIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGR--IQLETIIKSLKATQDEINQARSKLSQI 591
Cdd:cd21116   155 QLNSLAEQIDAAIDALEKLSNDWQTLDSDIKELITDLEDAEssIDAAFLQADLKAAKADWNQLYEQAKSL 224
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 482-585 7.22e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 37.94  E-value: 7.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 482 QKQDAQDRLEEM-DQQKAKLEDMLNDVRQkcqeesqMISSLQTQIHSQESDLQSQEEELGRAKADLNRLQQEeaqLEQSL 560
Cdd:pfam03938  16 EGKAAQAQLEKKfKKRQAELEAKQKELQK-------LYEELQKDGALLEEEREEKEQELQKKEQELQQLQQK---AQQEL 85

                          90       100
                  ....*....|....*....|....*.
gi 1207192617 561 QAGRIQL-ETIIKSLKATQDEINQAR 585
Cdd:pfam03938  86 QKKQQELlQPIQDKINKAIKEVAKEK 111
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 478-593 7.60e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 37.21  E-value: 7.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 478 ELEAQKQDAQDRLEEMDQQKAKledmlndvRQKCQEESQ-MISSLqtqihsqesdlqsqEEELGRAKADLNRLQQEEAQL 556
Cdd:pfam20492   3 EAEREKQELEERLKQYEEETKK--------AQEELEESEeTAEEL--------------EEERRQAEEEAERLEQKRQEA 60

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1207192617 557 EQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQD 593
Cdd:pfam20492  61 EEEKERLEESAEMEAEEKEQLEAELAEAQEEIARLEE 97
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 521-592 7.76e-03

Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];


Pssm-ID: 440606 [Multi-domain]  Cd Length: 324  Bit Score: 39.54  E-value: 7.76e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207192617 521 LQTQIHSQESDLQSQEEELGRAKADLNRLQqeeaQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQ 592
Cdd:COG0845    59 LQAALAQAQAQLAAAQAQLELAKAELERYK----ALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQAR 126
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 487-609 7.80e-03

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 38.40  E-value: 7.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 487 QDRLEEMDQQKAKLEDMLNDVRQKcqeesqmissLQTQIhSQESDLQSQE--EELGRAKADLN-RLQQEEAQLEQSLQAG 563
Cdd:pfam01442   3 EDSLDELSTYAEELQEQLGPVAQE----------LVDRL-EKETEALRERlqKDLEEVRAKLEpYLEELQAKLGQNVEEL 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1207192617 564 RIQLETIIKSLKATQD-EINQARSKLSQ-IQDSQHEISKNIEQYSSTL 609
Cdd:pfam01442  72 RQRLEPYTEELRKRLNaDAEELQEKLAPyGEELRERLEQNVDALRARL 119
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
141-188 7.84e-03

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.85  E-value: 7.84e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1207192617 141 NGLLSGEKVKPVLINSKLPVDVLGKVWDLSDIDKDGHLDRDEFAVAMH 188
Cdd:COG5126    83 DGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVR 130
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 523-601 7.88e-03

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 39.71  E-value: 7.88e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207192617 523 TQIHSQESDLQSQEEELGRAKADLNRLQQEEAQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKN 601
Cdd:TIGR04320 247 TPIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTAQNNLATAQA 325
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 413-515 8.07e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 39.23  E-value: 8.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  413 IKELDDISQEIAQLQSTLAfthwDTLREKYT-LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLE 491
Cdd:smart00787 188 LRQLKQLEDELEDCDPTEL----DRAKEKLKkLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLE 263

                           90       100
                   ....*....|....*....|....
gi 1207192617  492 EMDQQKAKLEDMLNDVRQKCQEES 515
Cdd:smart00787 264 QCRGFTFKEIEKLKEQLKLLQSLT 287
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 444-525 8.49e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 37.56  E-value: 8.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 444 LEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDA-QDRLEEMDQQKAKLEDMLNdvrqkcQEESQMISSLQ 522
Cdd:pfam03938  24 LEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQElQKKEQELQQLQQKAQQELQ------KKQQELLQPIQ 97


                  ...
gi 1207192617 523 TQI 525
Cdd:pfam03938  98 DKI 100
mukB PRK04863
chromosome partition protein MukB;
468-593 8.61e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.94  E-value: 8.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617  468 DLDRETSSLQELEAQKQDAQDRLEEMDQ---QKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEEELGRAKA 544
Cdd:PRK04863   500 ELLRRLREQRHLAEQLQQLRMRLSELEQrlrQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARE 579

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1207192617  545 DLNRLQQEEAQLEQSlqagriqletiIKSLKATQDEINQARSKLSQIQD 593
Cdd:PRK04863   580 RRMALRQQLEQLQAR-----------IQRLAARAPAWLAAQDALARLRE 617
PRK00106 PRK00106
ribonuclease Y;
461-598 8.87e-03

ribonuclease Y;


Pssm-ID: 178867 [Multi-domain]  Cd Length: 535  Bit Score: 39.85  E-value: 8.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207192617 461 EVQEMQNDLDRETSSLQE---LEAqKQDAQDRLEEMDQQKAKLEDMLNDVRQKCQEESQMISSLQTQIHSQESDLQSQEE 537
Cdd:PRK00106   54 DAEHIKKTAKRESKALKKellLEA-KEEARKYREEIEQEFKSERQELKQIESRLTERATSLDRKDENLSSKEKTLESKEQ 132

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207192617 538 ELGRAKADLNRLQQEEAQLEQSLQA--GRIQLETI--IKSLKATQDEINQARSKLSQIQDSQHEI 598
Cdd:PRK00106  133 SLTDKSKHIDEREEQVEKLEEQKKAelERVAALSQaeAREIILAETENKLTHEIATRIREAEREV 197
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 443-514 8.93e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 36.39  E-value: 8.93e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207192617 443 TLEQDIRETEEAIRHKTTEVQEMQNDLDRETSSLQELEAQKQDAQDRLEEMDQQKAKLEDMLndvrQKCQEE 514
Cdd:cd22887     1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKL----RKLQEE 68
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
537-610 9.22e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.50  E-value: 9.22e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207192617 537 EELGRAKADLNRLQQEE----AQLEQSLQAGRIQLETIIKSLKATQDEINQARSKLSQIQDSQHEISKNIEQYSSTLN 610
Cdd:COG4372     6 EKVGKARLSLFGLRPKTgiliAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
 
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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