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Conserved domains on  [gi|15221012|ref|NP_175226|]
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filament-like protein (DUF869) [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
132-957 0e+00

Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.


:

Pssm-ID: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 998.03  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    132 KEALVKQHSKVAEDAVSGWEKADAEALALKNTLESVTLSKLTAEDRAAHLDGALKECMRQIRNLKKDHEVKLHDVALSKT 211
Cdd:pfam05911    1 KDDLVKQHAKVAEEAVSGWEKAEAEALALKQQLESVTLQKLTAEERAAHLDGALKECMQQLRNVKEEQEQKIHDVVLKKT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    212 KQIEKMTMEFEKRMCDYEQELLRSAADSDALSRTLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSLKYEVHVV 291
Cdd:pfam05911   81 KEWEKIKAELEAKLVETEQELLRAAAENDALSRSLQERENLLMKLSEEKSQAEAEIEALKSRLESCEKEINSLKYELHVL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    292 SKELEIRNEEKNMCIRSAESANKQHLEGVKKIAKLEAECQRLRSLVRKKLPGPAALAQMKLEVENLGRDSGDARQKRSPV 371
Cdd:pfam05911  161 SKELEIRNEEKNMSRRSADAAHKQHLESVKKIAKLEAECQRLRGLVRKKLPGPAALAQMKLEVEMLGRDSGETRLRRSPV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    372 KVSSPCKSPggysstGSEFSLDNAQKFQKENEFLTERLLAMEEETKMLKEALAKRNSELLESRNLCAQSTSKLQSLEAQL 451
Cdd:pfam05911  241 KNSSPHLSP------DPDFSEDSLQTPHKENEFLTERLLAMEEETKMLKEALAKRNSELQASRNMCAKTASKLSQLEAQL 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    452 QQNNSQKSSLEVCPNLNTSNPSSSISV-SEDGNDDSGSCSGSLST---NPSQQIKKEKDMAALERVESVNSHVELMDDFL 527
Cdd:pfam05911  315 EELNQGQVSMELASSQNPASNPPSLTSmSEDGSDDEVSCAESWASaliSELEHFKKEKPKTKSSCKSVGNSDLELMDDFL 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    528 EMEKLACLPNLSSSNGSIDSKDGSGDQK----------SEMVILDAHTDLEDSDRGSPAVMKFRSRLSKVLESVSPDADI 597
Cdd:pfam05911  395 EMEKLACLSNDKPSNGSHSSSKSSNNKKgeesdsekdsSESTGKELVPVSSKDISLGKSLSWLQSRISVILESHVTQKSI 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    598 QKIVGDIKCILQDVNACMDQEKPSEVHVHPEE----VSDLCPEQNLV---------EDCHLAEQKLQSIHQDLKNAVSRI 664
Cdd:pfam05911  475 GKILEDIRCALQDINDSLPEADSCLSSGHPSTdascDYITCKENSSVvekegsvsgDDKSSEETSKQSIQQDLSKAISKI 554
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    665 HDFVLLLRNEVKAGQDTSIEGNDFVELIEGFSVTFNHVLSGDKSLDDFVSNLANVFNEAMERKVSFRGLASSEVETLSPD 744
Cdd:pfam05911  555 IDFVEGLSKEALDDQDTSSDSSELSEVLQQFSATCNDVLSGKADLEDFVLELSHILDWISNHCFSLLDVSSMEDEIKKHD 634
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    745 CIDKVALPESKVVDKDSSqeIYQNGCVHNEPGVPCDENRVSGY------ESDSKLQEIEELRSEKEKMAVD-------IE 811
Cdd:pfam05911  635 CIDKVTLSENKVAQVDNG--CSEIDNLSSDPEIPSDGPLVSGSndlkteENKRLKEEFEQLKSEKENLEVElasctenLE 712
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    812 GLKCQLQESEQLLADIRSQFDSAQRSNRLADTQLRCMTESYRSLESRAADLEIDVNQLKEKIQKLENELEDEKCNHQEAI 891
Cdd:pfam05911  713 STKSQLQESEQLIAELRSELASLKESNSLAETQLKCMAESYEDLETRLTELEAELNELRQKFEALEVELEEEKNCHEELE 792
                          810       820       830       840       850       860
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15221012    892 LRCHELEEHIQRHRNTSLVAEDDEEADIKSKQERELSAAAEKLAECQETIFVLGKQLKSFR-PQPEQ 957
Cdd:pfam05911  793 AKCLELQEQLERNEKKESSNCDADQEDKKLQQEKEITAASEKLAECQETILNLGKQLKALAsPQDAS 859
Phage_GP20 super family cl37747
Phage minor structural protein GP20; This family consists of several phage minor structural ...
57-200 6.86e-03

Phage minor structural protein GP20; This family consists of several phage minor structural protein GP20 sequences of around 180 residues in length. The function of this family is unknown.


The actual alignment was detected with superfamily member pfam06810:

Pssm-ID: 429131 [Multi-domain]  Cd Length: 149  Bit Score: 38.11  E-value: 6.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012     57 EQIKSYDVQIKGYDV---QVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEqvqkLNEDVEDLNEKLSVANEEIVTKE 133
Cdd:pfam06810    1 EQADKVMEAENGKDIpkaKFDEVNTERDTLKEQLATRDKQLKDLKKVAKDNEE----LQKQIDELQAKNKDAEADYEAKI 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15221012    134 ALVKQHSKVaEDAVSGWEKADAEALALKNTLESVTLSKltaedraahlDGALKECMRQIRNLKKDHE 200
Cdd:pfam06810   77 ADLKFDNAI-KLALKGAKAKNEKAVKALLDKDKLKLKD----------DGTLIGLDEQIEGLKESDK 132
 
Name Accession Description Interval E-value
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
132-957 0e+00

Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.


Pssm-ID: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 998.03  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    132 KEALVKQHSKVAEDAVSGWEKADAEALALKNTLESVTLSKLTAEDRAAHLDGALKECMRQIRNLKKDHEVKLHDVALSKT 211
Cdd:pfam05911    1 KDDLVKQHAKVAEEAVSGWEKAEAEALALKQQLESVTLQKLTAEERAAHLDGALKECMQQLRNVKEEQEQKIHDVVLKKT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    212 KQIEKMTMEFEKRMCDYEQELLRSAADSDALSRTLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSLKYEVHVV 291
Cdd:pfam05911   81 KEWEKIKAELEAKLVETEQELLRAAAENDALSRSLQERENLLMKLSEEKSQAEAEIEALKSRLESCEKEINSLKYELHVL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    292 SKELEIRNEEKNMCIRSAESANKQHLEGVKKIAKLEAECQRLRSLVRKKLPGPAALAQMKLEVENLGRDSGDARQKRSPV 371
Cdd:pfam05911  161 SKELEIRNEEKNMSRRSADAAHKQHLESVKKIAKLEAECQRLRGLVRKKLPGPAALAQMKLEVEMLGRDSGETRLRRSPV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    372 KVSSPCKSPggysstGSEFSLDNAQKFQKENEFLTERLLAMEEETKMLKEALAKRNSELLESRNLCAQSTSKLQSLEAQL 451
Cdd:pfam05911  241 KNSSPHLSP------DPDFSEDSLQTPHKENEFLTERLLAMEEETKMLKEALAKRNSELQASRNMCAKTASKLSQLEAQL 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    452 QQNNSQKSSLEVCPNLNTSNPSSSISV-SEDGNDDSGSCSGSLST---NPSQQIKKEKDMAALERVESVNSHVELMDDFL 527
Cdd:pfam05911  315 EELNQGQVSMELASSQNPASNPPSLTSmSEDGSDDEVSCAESWASaliSELEHFKKEKPKTKSSCKSVGNSDLELMDDFL 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    528 EMEKLACLPNLSSSNGSIDSKDGSGDQK----------SEMVILDAHTDLEDSDRGSPAVMKFRSRLSKVLESVSPDADI 597
Cdd:pfam05911  395 EMEKLACLSNDKPSNGSHSSSKSSNNKKgeesdsekdsSESTGKELVPVSSKDISLGKSLSWLQSRISVILESHVTQKSI 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    598 QKIVGDIKCILQDVNACMDQEKPSEVHVHPEE----VSDLCPEQNLV---------EDCHLAEQKLQSIHQDLKNAVSRI 664
Cdd:pfam05911  475 GKILEDIRCALQDINDSLPEADSCLSSGHPSTdascDYITCKENSSVvekegsvsgDDKSSEETSKQSIQQDLSKAISKI 554
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    665 HDFVLLLRNEVKAGQDTSIEGNDFVELIEGFSVTFNHVLSGDKSLDDFVSNLANVFNEAMERKVSFRGLASSEVETLSPD 744
Cdd:pfam05911  555 IDFVEGLSKEALDDQDTSSDSSELSEVLQQFSATCNDVLSGKADLEDFVLELSHILDWISNHCFSLLDVSSMEDEIKKHD 634
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    745 CIDKVALPESKVVDKDSSqeIYQNGCVHNEPGVPCDENRVSGY------ESDSKLQEIEELRSEKEKMAVD-------IE 811
Cdd:pfam05911  635 CIDKVTLSENKVAQVDNG--CSEIDNLSSDPEIPSDGPLVSGSndlkteENKRLKEEFEQLKSEKENLEVElasctenLE 712
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    812 GLKCQLQESEQLLADIRSQFDSAQRSNRLADTQLRCMTESYRSLESRAADLEIDVNQLKEKIQKLENELEDEKCNHQEAI 891
Cdd:pfam05911  713 STKSQLQESEQLIAELRSELASLKESNSLAETQLKCMAESYEDLETRLTELEAELNELRQKFEALEVELEEEKNCHEELE 792
                          810       820       830       840       850       860
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15221012    892 LRCHELEEHIQRHRNTSLVAEDDEEADIKSKQERELSAAAEKLAECQETIFVLGKQLKSFR-PQPEQ 957
Cdd:pfam05911  793 AKCLELQEQLERNEKKESSNCDADQEDKKLQQEKEITAASEKLAECQETILNLGKQLKALAsPQDAS 859
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
150-953 3.67e-11

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 67.77  E-value: 3.67e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    150 WEKADAEALALKNTLESVTLSKLTAEDRAAHLDGALKECMRQIRNLKKDHEVKLHDVaLSKTKQIEKMTMEFEKrmcdYE 229
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL-YALANEISRLEQQKQI----LR 308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    230 QELLRSAADSDALSRTLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSLKYEVhvvsKELEIRNEEKNMCIRSA 309
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL----EELESRLEELEEQLETL 384
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    310 ESANKQHLEgvkKIAKLEAECQRLRSLvrkklpgpaaLAQMKLEVENLGRDSGDARQKRSPVKVSspckspggysstgsE 389
Cdd:TIGR02168  385 RSKVAQLEL---QIASLNNEIERLEAR----------LERLEDRRERLQQEIEELLKKLEEAELK--------------E 437
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    390 FSLDNAQKfQKENEFLTERLLAMEEETKMLKEALAKRNSELLESRNLCAQSTSKLQSLEAQlqQNNSQKSSLEVCPNLNt 469
Cdd:TIGR02168  438 LQAELEEL-EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL--QENLEGFSEGVKALLK- 513
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    470 snpsssisVSEDGNDDSGSCSGSLSTnpsqqikKEKDMAALERVESvnshvELMDDflemeklACLPNLSSSNGSIDSKD 549
Cdd:TIGR02168  514 --------NQSGLSGILGVLSELISV-------DEGYEAAIEAALG-----GRLQA-------VVVENLNAAKKAIAFLK 566
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    550 GSGDQKSEMVILDAHTDLEDSDRGSPAVMKFRSRLSKVLESVSPDADIQKIV----GDIKCI--LQDVNACMDQEKPSEV 623
Cdd:TIGR02168  567 QNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALsyllGGVLVVddLDNALELAKKLRPGYR 646
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    624 HVHPE-----------------EVSDLCPEQ---NLVEDCHLAEQKLQSIHQDLKNAVSRIHDFVLLLRNEVKAGQDTSI 683
Cdd:TIGR02168  647 IVTLDgdlvrpggvitggsaktNSSILERRReieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR 726
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    684 EGNDFVELIEGFSVTFNHVLSGDKSLDDFVSNLANVFNEAMERKVSFRGL---ASSEVETLSPDCIDKVALPESKVVDKD 760
Cdd:TIGR02168  727 QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEElaeAEAEIEELEAQIEQLKEELKALREALD 806
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    761 SSQEIYQ--NGCVHNEpgvpcdENRVSGYESD--SKLQEIEELRSEKEKMAVDIEGLKCQLQESEQLLADIRSQFDSAQR 836
Cdd:TIGR02168  807 ELRAELTllNEEAANL------RERLESLERRiaATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN 880
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    837 SNRLADTQLRCMTESYRSLESRAADLEIDVNQLKEKIQKLENELEDEKCNHQEAILRCHELEEHIqrhrntSLVAEDDEE 916
Cdd:TIGR02168  881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL------SEEYSLTLE 954
                          810       820       830
                   ....*....|....*....|....*....|....*..
gi 15221012    917 ADIKSKQERELSaaaekLAECQETIFVLGKQLKSFRP 953
Cdd:TIGR02168  955 EAEALENKIEDD-----EEEARRRLKRLENKIKELGP 986
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
55-284 3.45e-08

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 56.70  E-value: 3.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012   55 LEEQIKSYDVQIKGYDVQVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANEEIVTKEA 134
Cdd:COG4942   25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  135 LVKQHSKVAEDAvsgwEKADAEALALKNTlesvtlSKLTAEDRAAHLDGALKECMRQIRNLKKDhevklhdvalskTKQI 214
Cdd:COG4942  105 ELAELLRALYRL----GRQPPLALLLSPE------DFLDAVRRLQYLKYLAPARREQAEELRAD------------LAEL 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  215 EKMTMEFEKRMCDYEQELLRSAADSDALSRTLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSL 284
Cdd:COG4942  163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
46 PHA02562
endonuclease subunit; Provisional
54-301 6.77e-06

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 50.01  E-value: 6.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    54 GLEEQIKSYDVQIKGYDVQVKTYENQVESYEEQVKdfeEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANEEIvtke 133
Cdd:PHA02562  178 ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNG---ENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDI---- 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012   134 alvkqhskvaEDAVSGWEKADAEALALKNTLESvtlskLTAEDRAAHLDGALKECMRQIrnlkKDHEVKLHDVAlSKTKQ 213
Cdd:PHA02562  251 ----------EDPSAALNKLNTAAAKIKSKIEQ-----FQKVIKMYEKGGVCPTCTQQI----SEGPDRITKIK-DKLKE 310
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012   214 IEKmtmEFEKRMCDYEQellrsaadsdalsrtLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSLKYEVHVVSK 293
Cdd:PHA02562  311 LQH---SLEKLDTAIDE---------------LEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQA 372

                  ....*...
gi 15221012   294 ELEIRNEE 301
Cdd:PHA02562  373 EFVDNAEE 380
Phage_GP20 pfam06810
Phage minor structural protein GP20; This family consists of several phage minor structural ...
57-200 6.86e-03

Phage minor structural protein GP20; This family consists of several phage minor structural protein GP20 sequences of around 180 residues in length. The function of this family is unknown.


Pssm-ID: 429131 [Multi-domain]  Cd Length: 149  Bit Score: 38.11  E-value: 6.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012     57 EQIKSYDVQIKGYDV---QVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEqvqkLNEDVEDLNEKLSVANEEIVTKE 133
Cdd:pfam06810    1 EQADKVMEAENGKDIpkaKFDEVNTERDTLKEQLATRDKQLKDLKKVAKDNEE----LQKQIDELQAKNKDAEADYEAKI 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15221012    134 ALVKQHSKVaEDAVSGWEKADAEALALKNTLESVTLSKltaedraahlDGALKECMRQIRNLKKDHE 200
Cdd:pfam06810   77 ADLKFDNAI-KLALKGAKAKNEKAVKALLDKDKLKLKD----------DGTLIGLDEQIEGLKESDK 132
 
Name Accession Description Interval E-value
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
132-957 0e+00

Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.


Pssm-ID: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 998.03  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    132 KEALVKQHSKVAEDAVSGWEKADAEALALKNTLESVTLSKLTAEDRAAHLDGALKECMRQIRNLKKDHEVKLHDVALSKT 211
Cdd:pfam05911    1 KDDLVKQHAKVAEEAVSGWEKAEAEALALKQQLESVTLQKLTAEERAAHLDGALKECMQQLRNVKEEQEQKIHDVVLKKT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    212 KQIEKMTMEFEKRMCDYEQELLRSAADSDALSRTLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSLKYEVHVV 291
Cdd:pfam05911   81 KEWEKIKAELEAKLVETEQELLRAAAENDALSRSLQERENLLMKLSEEKSQAEAEIEALKSRLESCEKEINSLKYELHVL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    292 SKELEIRNEEKNMCIRSAESANKQHLEGVKKIAKLEAECQRLRSLVRKKLPGPAALAQMKLEVENLGRDSGDARQKRSPV 371
Cdd:pfam05911  161 SKELEIRNEEKNMSRRSADAAHKQHLESVKKIAKLEAECQRLRGLVRKKLPGPAALAQMKLEVEMLGRDSGETRLRRSPV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    372 KVSSPCKSPggysstGSEFSLDNAQKFQKENEFLTERLLAMEEETKMLKEALAKRNSELLESRNLCAQSTSKLQSLEAQL 451
Cdd:pfam05911  241 KNSSPHLSP------DPDFSEDSLQTPHKENEFLTERLLAMEEETKMLKEALAKRNSELQASRNMCAKTASKLSQLEAQL 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    452 QQNNSQKSSLEVCPNLNTSNPSSSISV-SEDGNDDSGSCSGSLST---NPSQQIKKEKDMAALERVESVNSHVELMDDFL 527
Cdd:pfam05911  315 EELNQGQVSMELASSQNPASNPPSLTSmSEDGSDDEVSCAESWASaliSELEHFKKEKPKTKSSCKSVGNSDLELMDDFL 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    528 EMEKLACLPNLSSSNGSIDSKDGSGDQK----------SEMVILDAHTDLEDSDRGSPAVMKFRSRLSKVLESVSPDADI 597
Cdd:pfam05911  395 EMEKLACLSNDKPSNGSHSSSKSSNNKKgeesdsekdsSESTGKELVPVSSKDISLGKSLSWLQSRISVILESHVTQKSI 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    598 QKIVGDIKCILQDVNACMDQEKPSEVHVHPEE----VSDLCPEQNLV---------EDCHLAEQKLQSIHQDLKNAVSRI 664
Cdd:pfam05911  475 GKILEDIRCALQDINDSLPEADSCLSSGHPSTdascDYITCKENSSVvekegsvsgDDKSSEETSKQSIQQDLSKAISKI 554
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    665 HDFVLLLRNEVKAGQDTSIEGNDFVELIEGFSVTFNHVLSGDKSLDDFVSNLANVFNEAMERKVSFRGLASSEVETLSPD 744
Cdd:pfam05911  555 IDFVEGLSKEALDDQDTSSDSSELSEVLQQFSATCNDVLSGKADLEDFVLELSHILDWISNHCFSLLDVSSMEDEIKKHD 634
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    745 CIDKVALPESKVVDKDSSqeIYQNGCVHNEPGVPCDENRVSGY------ESDSKLQEIEELRSEKEKMAVD-------IE 811
Cdd:pfam05911  635 CIDKVTLSENKVAQVDNG--CSEIDNLSSDPEIPSDGPLVSGSndlkteENKRLKEEFEQLKSEKENLEVElasctenLE 712
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    812 GLKCQLQESEQLLADIRSQFDSAQRSNRLADTQLRCMTESYRSLESRAADLEIDVNQLKEKIQKLENELEDEKCNHQEAI 891
Cdd:pfam05911  713 STKSQLQESEQLIAELRSELASLKESNSLAETQLKCMAESYEDLETRLTELEAELNELRQKFEALEVELEEEKNCHEELE 792
                          810       820       830       840       850       860
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15221012    892 LRCHELEEHIQRHRNTSLVAEDDEEADIKSKQERELSAAAEKLAECQETIFVLGKQLKSFR-PQPEQ 957
Cdd:pfam05911  793 AKCLELQEQLERNEKKESSNCDADQEDKKLQQEKEITAASEKLAECQETILNLGKQLKALAsPQDAS 859
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
150-953 3.67e-11

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 67.77  E-value: 3.67e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    150 WEKADAEALALKNTLESVTLSKLTAEDRAAHLDGALKECMRQIRNLKKDHEVKLHDVaLSKTKQIEKMTMEFEKrmcdYE 229
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL-YALANEISRLEQQKQI----LR 308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    230 QELLRSAADSDALSRTLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSLKYEVhvvsKELEIRNEEKNMCIRSA 309
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL----EELESRLEELEEQLETL 384
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    310 ESANKQHLEgvkKIAKLEAECQRLRSLvrkklpgpaaLAQMKLEVENLGRDSGDARQKRSPVKVSspckspggysstgsE 389
Cdd:TIGR02168  385 RSKVAQLEL---QIASLNNEIERLEAR----------LERLEDRRERLQQEIEELLKKLEEAELK--------------E 437
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    390 FSLDNAQKfQKENEFLTERLLAMEEETKMLKEALAKRNSELLESRNLCAQSTSKLQSLEAQlqQNNSQKSSLEVCPNLNt 469
Cdd:TIGR02168  438 LQAELEEL-EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL--QENLEGFSEGVKALLK- 513
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    470 snpsssisVSEDGNDDSGSCSGSLSTnpsqqikKEKDMAALERVESvnshvELMDDflemeklACLPNLSSSNGSIDSKD 549
Cdd:TIGR02168  514 --------NQSGLSGILGVLSELISV-------DEGYEAAIEAALG-----GRLQA-------VVVENLNAAKKAIAFLK 566
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    550 GSGDQKSEMVILDAHTDLEDSDRGSPAVMKFRSRLSKVLESVSPDADIQKIV----GDIKCI--LQDVNACMDQEKPSEV 623
Cdd:TIGR02168  567 QNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALsyllGGVLVVddLDNALELAKKLRPGYR 646
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    624 HVHPE-----------------EVSDLCPEQ---NLVEDCHLAEQKLQSIHQDLKNAVSRIHDFVLLLRNEVKAGQDTSI 683
Cdd:TIGR02168  647 IVTLDgdlvrpggvitggsaktNSSILERRReieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR 726
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    684 EGNDFVELIEGFSVTFNHVLSGDKSLDDFVSNLANVFNEAMERKVSFRGL---ASSEVETLSPDCIDKVALPESKVVDKD 760
Cdd:TIGR02168  727 QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEElaeAEAEIEELEAQIEQLKEELKALREALD 806
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    761 SSQEIYQ--NGCVHNEpgvpcdENRVSGYESD--SKLQEIEELRSEKEKMAVDIEGLKCQLQESEQLLADIRSQFDSAQR 836
Cdd:TIGR02168  807 ELRAELTllNEEAANL------RERLESLERRiaATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN 880
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    837 SNRLADTQLRCMTESYRSLESRAADLEIDVNQLKEKIQKLENELEDEKCNHQEAILRCHELEEHIqrhrntSLVAEDDEE 916
Cdd:TIGR02168  881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL------SEEYSLTLE 954
                          810       820       830
                   ....*....|....*....|....*....|....*..
gi 15221012    917 ADIKSKQERELSaaaekLAECQETIFVLGKQLKSFRP 953
Cdd:TIGR02168  955 EAEALENKIEDD-----EEEARRRLKRLENKIKELGP 986
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
84-357 1.82e-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: 58.91  E-value: 1.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012     84 EEQVKDFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANEEIVTKEALVKQHSKVAEDAVSGWEKADAEALALKNT 163
Cdd:TIGR02168  683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    164 LESvtlskltAEDRAAHLDGALKECMRQIRNLKKDHEvklhdVALSKTKQIEKMTMEFEKRMCDYEQELLRSAADSDALS 243
Cdd:TIGR02168  763 IEE-------LEERLEEAEEELAEAEAEIEELEAQIE-----QLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    244 RTLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSLKYEVHVVSKELEIRNEEKNMCIRSAESANKQHLEGVKKI 323
Cdd:TIGR02168  831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 15221012    324 AKLEAECQRLR-SLVRKKLpgpaALAQMKLEVENL 357
Cdd:TIGR02168  911 SELRRELEELReKLAQLEL----RLEGLEVRIDNL 941
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
55-284 3.45e-08

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 56.70  E-value: 3.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012   55 LEEQIKSYDVQIKGYDVQVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANEEIVTKEA 134
Cdd:COG4942   25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  135 LVKQHSKVAEDAvsgwEKADAEALALKNTlesvtlSKLTAEDRAAHLDGALKECMRQIRNLKKDhevklhdvalskTKQI 214
Cdd:COG4942  105 ELAELLRALYRL----GRQPPLALLLSPE------DFLDAVRRLQYLKYLAPARREQAEELRAD------------LAEL 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  215 EKMTMEFEKRMCDYEQELLRSAADSDALSRTLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSL 284
Cdd:COG4942  163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
794-959 7.08e-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: 7.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    794 QEIEELRSEKEKMAVDIEGLKCQLQESEQLLADIRSQFDSAQRSNRLADTQLRCMTESYRSLESRAADLEIDVNQLKEKI 873
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    874 QKLENELEDEKCNHQEAILRCHELEEHIQR-----HRNTSLVAEDDEEADIKSKQERELSAAA----EKLAECQETIFVL 944
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEIEEleaqiEQLKEELKALREALDELRAELTLLNEEAanlrERLESLERRIAAT 836
                          170
                   ....*....|....*
gi 15221012    945 GKQLKSFRPQPEQMR 959
Cdd:TIGR02168  837 ERRLEDLEEQIEELS 851
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
55-374 2.53e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 2.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012   55 LEEQIKSYDVQIKGYdvqvktyenQVESYEEQVKDFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANEEIVTKEA 134
Cdd:COG1196  218 LKEELKELEAELLLL---------KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA 288
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  135 LVKQHSKVAEDAVSGWEKADAEALALKNTLESVTLSKLTAEDRAAHLDGALKECMRQIRNLKKDHEVKLHDVALSKTKQI 214
Cdd:COG1196  289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  215 EKmtmefEKRMCDYEQELLRSAADSDALSRTLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSLKYEVHVVSKE 294
Cdd:COG1196  369 EA-----EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  295 LEIRNEEKNMCIRSAESANKQHLEGVKKIAKLEAECQRLRSLVRKKLPGPAALAQMKLEVENLGRDSGDARQKRSPVKVS 374
Cdd:COG1196  444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
55-366 2.95e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 2.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012   55 LEEQIKSYDVQIKGYDVQVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEQVQKL-------NEDVEDLNEKLSVANE 127
Cdd:COG1196  244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLeqdiarlEERRRELEERLEELEE 323
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  128 EIVTKEALVKQHSKVAEDAVSGWEKADAEALALKNTLESVTLSKLTAEDRAAHLDGALKECMRQIRNLKKDHEvklhdVA 207
Cdd:COG1196  324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA-----EL 398
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  208 LSKTKQIEKMTMEFEKRMCDYEQELLRSAADSDALSRTLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSLKYE 287
Cdd:COG1196  399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  288 VHVVSKELEIRNEEKNMcIRSAESANKQHLEGVKKIAKLEAECQRLRSL-----VRKKLPGPAALAQMKLEVENLGRDSG 362
Cdd:COG1196  479 LAELLEELAEAAARLLL-LLEAEADYEGFLEGVKAALLLAGLRGLAGAVavligVEAAYEAALEAALAAALQNIVVEDDE 557

                 ....
gi 15221012  363 DARQ 366
Cdd:COG1196  558 VAAA 561
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
70-267 4.89e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 53.30  E-value: 4.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012   70 DVQVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANEEIVTKEALVKQHSKVAEDAVSG 149
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  150 WEKADAEALALKNTLESVT----LSKLTAEDRAAHLDGALkecMRQIRNLKKDHEVKLHDVAlSKTKQIEKMTMEFEKRM 225
Cdd:COG3883   95 LYRSGGSVSYLDVLLGSESfsdfLDRLSALSKIADADADL---LEELKADKAELEAKKAELE-AKLAELEALKAELEAAK 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 15221012  226 CDYEQELLRSAADSDALSRTLQERSNMLVKVSEEKSRADAEI 267
Cdd:COG3883  171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
55-334 1.79e-06

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: 52.37  E-value: 1.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012     55 LEEQIKSYDVQIKGYDVQVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANEEIVTKEA 134
Cdd:TIGR02168  710 LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEA 789
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    135 LVKQHSkvaedavSGWEKADAEALALKNTLESVTLSKLTAEDRAAHLDGALKECMRQIRNLKKDHEVKLHDVAL------ 208
Cdd:TIGR02168  790 QIEQLK-------EELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESlaaeie 862
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    209 SKTKQIEKMTMEFE---KRMCDYEQELLRSAADSDALSRTLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSLk 285
Cdd:TIGR02168  863 ELEELIEELESELEallNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL- 941
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 15221012    286 yevhvvskeLEIRNEEKNMcirSAESANKQHLEGVKKIAKLEAECQRLR 334
Cdd:TIGR02168  942 ---------QERLSEEYSL---TLEEAEALENKIEDDEEEARRRLKRLE 978
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
788-941 2.26e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 2.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  788 ESDSKLQEIEELRSEKEKMAVDIEGLKCQLQESEQLLADIRSQFDSAQRSNRLADTQLRCMTESYRSLESRAADLEIDVN 867
Cdd:COG1196  240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15221012  868 QLKEKIQKLENELEDEKCNHQEAILRCHELE---EHIQRHRNTSLVAEDDEEADIKSKQERELSAAAEKLAECQETI 941
Cdd:COG1196  320 ELEEELAELEEELEELEEELEELEEELEEAEeelEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
56-340 4.09e-06

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: 51.22  E-value: 4.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012     56 EEQIKSYDVQIKGYDVQVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANEEIVtkeal 135
Cdd:TIGR02169  208 EKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIK----- 282
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    136 vkqhskvaedavsgwEKADAEALALKNTLESVTLSKLTAEDRAAHLDGALKECMRQIRNLkkdhEVKLHDVaLSKTKQIE 215
Cdd:TIGR02169  283 ---------------DLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKL----EAEIDKL-LAEIEELE 342
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    216 KMTMEFEKRMCDYEQELLRSAADSDALSRTLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSLKYEvhvvSKEL 295
Cdd:TIGR02169  343 REIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE----LQRL 418
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 15221012    296 EIRNEEKNMCIRSAESANKQHLEGVK-KIAKLEAECQRLRSLVRKK 340
Cdd:TIGR02169  419 SEELADLNAAIAGIEAKINELEEEKEdKALEIKKQEWKLEQLAADL 464
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
55-282 4.89e-06

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: 50.84  E-value: 4.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012     55 LEEQIKSYDVQIKGYDVQVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANEEIVTKEA 134
Cdd:TIGR02169  292 VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRA 371
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    135 LVKQHSKVAEDAVSGWEKADAEALALKNTLESVTLSKLTAEDRAAHLDGALKECMRQIRNLKKDHEvKLHDVALSKTKQI 214
Cdd:TIGR02169  372 ELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKIN-ELEEEKEDKALEI 450
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15221012    215 EKMTMEFE---KRMCDYEQELLRSAADSDALSRTLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIK 282
Cdd:TIGR02169  451 KKQEWKLEqlaADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
46 PHA02562
endonuclease subunit; Provisional
54-301 6.77e-06

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 50.01  E-value: 6.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    54 GLEEQIKSYDVQIKGYDVQVKTYENQVESYEEQVKdfeEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANEEIvtke 133
Cdd:PHA02562  178 ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNG---ENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDI---- 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012   134 alvkqhskvaEDAVSGWEKADAEALALKNTLESvtlskLTAEDRAAHLDGALKECMRQIrnlkKDHEVKLHDVAlSKTKQ 213
Cdd:PHA02562  251 ----------EDPSAALNKLNTAAAKIKSKIEQ-----FQKVIKMYEKGGVCPTCTQQI----SEGPDRITKIK-DKLKE 310
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012   214 IEKmtmEFEKRMCDYEQellrsaadsdalsrtLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSLKYEVHVVSK 293
Cdd:PHA02562  311 LQH---SLEKLDTAIDE---------------LEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQA 372

                  ....*...
gi 15221012   294 ELEIRNEE 301
Cdd:PHA02562  373 EFVDNAEE 380
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
55-285 2.27e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.51  E-value: 2.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012     55 LEEQIKSYDVQIKGYDVQVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANEEIVTKEA 134
Cdd:TIGR02168  293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    135 LVKQHSKVAEDAVSGWEKADAEALALKNTLESvtlskltAEDRAAHLDGALKECMRQIR-NLKKDHEVKLHDVAlSKTKQ 213
Cdd:TIGR02168  373 RLEELEEQLETLRSKVAQLELQIASLNNEIER-------LEARLERLEDRRERLQQEIEeLLKKLEEAELKELQ-AELEE 444
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15221012    214 IEKMTMEFEKRMCDYEQELLRSAADSDALSRTLQERSNmlvKVSEEKSRADAeIETLKSNLEMCEREIKSLK 285
Cdd:TIGR02168  445 LEEELEELQEELERLEEALEELREELEEAEQALDAAER---ELAQLQARLDS-LERLQENLEGFSEGVKALL 512
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
72-329 3.73e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.14  E-value: 3.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012     72 QVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANEEIVTKEAlvkqhSKVaEDAVSGWE 151
Cdd:TIGR02169  738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAEL-----SKL-EEEVSRIE 811
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    152 KADAEalaLKNTLESVTLSKLTAEDRAAHLDGALKECMRQIRNLKKDHEVKLHDVA--LSKTKQIEKMTMEFEKRMCDYE 229
Cdd:TIGR02169  812 ARLRE---IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEelEEELEELEAALRDLESRLGDLK 888
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    230 QELLRSAADSDALSRTLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSLKYEVHVV-----------SKELEIR 298
Cdd:TIGR02169  889 KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElsledvqaelqRVEEEIR 968
                          250       260       270
                   ....*....|....*....|....*....|...
gi 15221012    299 N-EEKNM-CIRSAESANKQHLEGVKKIAKLEAE 329
Cdd:TIGR02169  969 AlEPVNMlAIQEYEEVLKRLDELKEKRAKLEEE 1001
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
788-966 5.16e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 5.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    788 ESDSKLQEIEELRSEKEKMAVDIEGLKCQLQESEQLLADIRSQFDSAQRSNRLADTQLRCMTESYRSLESRAADLEIDVN 867
Cdd:TIGR02168  261 ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELA 340
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    868 QLKEKIQKLENELEDEKCNH-------QEAILRCHELEEHIQRHRNtSLVAEDDEEADIKSKQER---ELSAAAEKLAEC 937
Cdd:TIGR02168  341 ELEEKLEELKEELESLEAELeeleaelEELESRLEELEEQLETLRS-KVAQLELQIASLNNEIERleaRLERLEDRRERL 419
                          170       180
                   ....*....|....*....|....*....
gi 15221012    938 QETIFVLGKQLKSFRPQPEQMRSPQTRNE 966
Cdd:TIGR02168  420 QQEIEELLKKLEEAELKELQAELEELEEE 448
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
103-337 2.07e-04

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: 45.44  E-value: 2.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    103 EYEEQVQKLNEDVEDLNEKLSVANEEIVTKEALVKQHSKVAEDAV-------SGWEKADAEALALKNTLE------SVTL 169
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASrkigeieKEIEQLEQEEEKLKERLEeleedlSSLE 750
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    170 SKLTAEDRA-AHLDGALKECMRQIRNLKKDHEVKLHDVALSKTKQI-------EKMTMEFEKRMCDYEQELLRSAADSDA 241
Cdd:TIGR02169  751 QEIENVKSElKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIqaelsklEEEVSRIEARLREIEQKLNRLTLEKEY 830
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    242 LSRTLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSLKYEVHVVSKEL-EIRNEEKNMcirsaesanKQHLEGV 320
Cdd:TIGR02169  831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLgDLKKERDEL---------EAQLREL 901
                          250
                   ....*....|....*...
gi 15221012    321 K-KIAKLEAECQRLRSLV 337
Cdd:TIGR02169  902 ErKIEELEAQIEKKRKRL 919
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
794-941 2.21e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 2.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  794 QEIEELRSEKEKMAVDIEGLKCQLQESEQLLADIRSQFDSAQRSNRLADTQ------------LRCMTESYRSLESRAAD 861
Cdd:COG4913  624 EELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEaelerldassddLAALEEQLEELEAELEE 703
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  862 LEIDVNQLKEKIQKLENELEDEKCNHQEAILRCHELEEHIQRHRNTSL------VAEDDEEADIKSKQERELSAAAEKLA 935
Cdd:COG4913  704 LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLeerfaaALGDAVERELRENLEERIDALRARLN 783

                 ....*.
gi 15221012  936 ECQETI 941
Cdd:COG4913  784 RAEEEL 789
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
55-325 2.48e-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: 2.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012     55 LEEQIKSYDVQIKGYDVQVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANEEIVTKEA 134
Cdd:TIGR04523  375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL 454
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    135 LVKQHSKVAEDAVSGWEKADAEALALKNTLESVT---------LSKLTAEDRaaHLDGALKECMRQIRNLKKDHEvKLHD 205
Cdd:TIGR04523  455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQkelkskekeLKKLNEEKK--ELEEKVKDLTKKISSLKEKIE-KLES 531
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    206 VALSKTKQIEKMTMEFEKRMCDYEQELLRSAADS--DALSRTLQERSNMLVKVSEEKSRAD---AEIETLKSNLEMCERE 280
Cdd:TIGR04523  532 EKKEKESKISDLEDELNKDDFELKKENLEKEIDEknKEIEELKQTQKSLKKKQEEKQELIDqkeKEKKDLIKEIEEKEKK 611
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 15221012    281 IKSLKYEVHVVSKELEIRNEEKnMCIRSAESANKQHLEGVKKIAK 325
Cdd:TIGR04523  612 ISSLEKELEKAKKENEKLSSII-KNIKSKKNKLKQEVKQIKETIK 655
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
798-941 2.82e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 2.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  798 ELRSEKEKmaVDIEGLKCQLQESEQLLADIRSQFDSAQRSNRLADTQLRCMTESYRSLESRAADLEIDVNQLKEKIQKLE 877
Cdd:COG1196  217 ELKEELKE--LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15221012  878 NELEDEKCNHQEAILRCHELEEHIQR--HRNTSLVAEDDEEADIKSKQERELSAAAEKLAECQETI 941
Cdd:COG1196  295 AELARLEQDIARLEERRRELEERLEEleEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
34-462 3.01e-04

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 45.11  E-value: 3.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012     34 EAIKKPKYVQISVEQYTHFTGLEEQIKSYDVQIKGYDVQVKTYENQVESYEEQVKDFEEQI----DAYDEKVHEYEEQVQ 109
Cdd:pfam15921  248 EALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQArnqnSMYMRQLSDLESTVS 327
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    110 KLNED-----------VEDLNEKLSVANEEIV---TKEALVKQHSKVAEDAVS-------------GWEKADAEALALKN 162
Cdd:pfam15921  328 QLRSElreakrmyedkIEELEKQLVLANSELTearTERDQFSQESGNLDDQLQklladlhkrekelSLEKEQNKRLWDRD 407
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    163 TLESVTLSKLTAE--DR---AAHLDGALK----ECM----RQIRNLKKDHEvKLHDVAlSKTKQIEKmTMEFEKRMCdye 229
Cdd:pfam15921  408 TGNSITIDHLRREldDRnmeVQRLEALLKamksECQgqmeRQMAAIQGKNE-SLEKVS-SLTAQLES-TKEMLRKVV--- 481
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    230 QELLRSAADSDALSRTLQERSNMLvkvsEEKSRA----DAEIETLKSNLEMCEREIKSLKYE------VHVVSKELEIRN 299
Cdd:pfam15921  482 EELTAKKMTLESSERTVSDLTASL----QEKERAieatNAEITKLRSRVDLKLQELQHLKNEgdhlrnVQTECEALKLQM 557
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    300 EEKNMCIRSAesanKQHLEGVKKIAKLEAECQRLRSLVRKKLPGPAALAQMKLEVENLGRDSGDARQKRSPVKVSSPCKS 379
Cdd:pfam15921  558 AEKDKVIEIL----RQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELE 633
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    380 PGGYSSTGSEfSLDNAQKFQKE-----NEFLTER--LLAMEEETKMLKEALAKRNSELLESRNlcaQSTSKLQSLEAQLQ 452
Cdd:pfam15921  634 KVKLVNAGSE-RLRAVKDIKQErdqllNEVKTSRneLNSLSEDYEVLKRNFRNKSEEMETTTN---KLKMQLKSAQSELE 709
                          490
                   ....*....|
gi 15221012    453 QNNSQKSSLE 462
Cdd:pfam15921  710 QTRNTLKSME 719
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
794-884 3.85e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.98  E-value: 3.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  794 QEIEELRSEKEKmavdiegLKCQLQESEQLLADIRSQFDSAQRSNRLADTQLRCMTESYRSLESRAADLEIDVNQLKEKI 873
Cdd:COG4942   20 DAAAEAEAELEQ-------LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
                         90
                 ....*....|.
gi 15221012  874 QKLENELEDEK 884
Cdd:COG4942   93 AELRAELEAQK 103
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
33-463 4.53e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 4.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    33 KEAIKKPKYVQISVEQYTHFTGLEEQIKSYDVQIKgydVQVKTYENQVESYEEQVKDFEEQidayDEKVHEYEEQVQKLN 112
Cdd:PRK03918  279 EEKVKELKELKEKAEEYIKLSEFYEEYLDELREIE---KRLSRLEEEINGIEERIKELEEK----EERLEELKKKLKELE 351
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012   113 EDVEDLNEKLSVANEEIVTKEALVKQHSKVAEDAVsgwEKADAEALALKNTLESVTLSKLTAEDRAAHLDGALKECMRQI 192
Cdd:PRK03918  352 KRLEELEERHELYEEAKAKKEELERLKKRLTGLTP---EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012   193 RNLKK--------------DHEVKLHDVALSKTKQIEKMTMEFEKRMCDYEQELLRSAADSDALSRTLQERS-------- 250
Cdd:PRK03918  429 EELKKakgkcpvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaeqlkel 508
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012   251 -NMLVKVSEEKSRADA-EIETLKSNLEMCEREIKSLKYEVHVVsKELEIRNEEKNMCIRSAESANKQHL-----EGVKKI 323
Cdd:PRK03918  509 eEKLKKYNLEELEKKAeEYEKLKEKLIKLKGEIKSLKKELEKL-EELKKKLAELEKKLDELEEELAELLkeleeLGFESV 587
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012   324 AKLEAECQRLRSLVRKKL---PGPAALAQMKLEVENLGRDSGDARQKRSPVKvsspckspggysstgSEFSLDNAQKFQK 400
Cdd:PRK03918  588 EELEERLKELEPFYNEYLelkDAEKELEREEKELKKLEEELDKAFEELAETE---------------KRLEELRKELEEL 652
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15221012   401 ENEFLTERLLAMEEETKMLKEALAKRNSELLESRNLCAQSTSKLQSLEAQLQQNNSQKSSLEV 463
Cdd:PRK03918  653 EKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
54-451 5.06e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 5.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    54 GLEEQIKSYD---VQIKGYDVQVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEQVQKLNE--DVEDLNEKLSVANEE 128
Cdd:PRK03918  225 KLEKEVKELEelkEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEKAEEYIKLSEFYEE 304
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012   129 IVTKEALVKQHSKVAEDAVSGWEKADAEALALKNTLESvtlskltaedraahLDGALKECMRQIRNLKKDHEvkLHDVAL 208
Cdd:PRK03918  305 YLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE--------------LKKKLKELEKRLEELEERHE--LYEEAK 368
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012   209 SKTKQIEKMtmefEKRMCDYEQELLrsAADSDALSRTLQERSNMLVKVSEEKSRADAEIETLKSNLEmcerEIKSLKYEV 288
Cdd:PRK03918  369 AKKEELERL----KKRLTGLTPEKL--EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE----ELKKAKGKC 438
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012   289 HVVSKELEirNEEKNMCIRSAESANKQHLEGVKKIAKLEAECQRLRSLVRKKLPGPAALAQMKLEVENLgrdsgdaRQKR 368
Cdd:PRK03918  439 PVCGRELT--EEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQL-------KELE 509
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012   369 SPVKvsspckspggysstgsEFSLDNAQKFQKENEFLTERLLAMEEETKMLKEALAKRnsELLESRNlcAQSTSKLQSLE 448
Cdd:PRK03918  510 EKLK----------------KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL--EELKKKL--AELEKKLDELE 569

                  ...
gi 15221012   449 AQL 451
Cdd:PRK03918  570 EEL 572
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
74-335 7.23e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 7.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    74 KTYENQVESYEEQVK---DFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANEEivtKEALVKQHSKVAEdavsgw 150
Cdd:PRK03918  172 KEIKRRIERLEKFIKrteNIEELIKEKEKELEEVLREINEISSELPELREELEKLEKE---VKELEELKEEIEE------ 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012   151 ekADAEALALKNTLESVTLSKLTAEDRAAHLDGALKECMRQIRNLKKDHEVKLHDVALSKTK-QIEKMTMEFEKRMCDYE 229
Cdd:PRK03918  243 --LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYeEYLDELREIEKRLSRLE 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012   230 QELlrsaadsDALSRTLQERSNM---LVKVSEEKSRADAEIETLKSNLEMCErEIKSLKYEVHVVSKELEIRNEEKnmCI 306
Cdd:PRK03918  321 EEI-------NGIEERIKELEEKeerLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPEK--LE 390
                         250       260
                  ....*....|....*....|....*....
gi 15221012   307 RSAESANKQHLEGVKKIAKLEAECQRLRS 335
Cdd:PRK03918  391 KELEELEKAKEEIEEEISKITARIGELKK 419
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
780-906 1.19e-03

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


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 42.05  E-value: 1.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    780 DENRVSGYESDSKLQEIEELRSEKEKMAVDIEGLKCQLQESEqllADIRSQFDSAQRSNRLADTQLrcmtesyRSLESRA 859
Cdd:pfam09787   40 DSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELE---AQQQEEAESSREQLQELEEQL-------ATERSAR 109
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 15221012    860 ADLEIDVNQLKEKIQKLENELEDEKCNHQEailRCHELEEHIQRHRN 906
Cdd:pfam09787  110 REAEAELERLQEELRYLEEELRRSKATLQS---RIKDREAEIEKLRN 153
V_ATPase_I pfam01496
V-type ATPase 116kDa subunit family; This family consists of the 116kDa V-type ATPase ...
855-945 1.40e-03

V-type ATPase 116kDa subunit family; This family consists of the 116kDa V-type ATPase (vacuolar (H+)-ATPases) subunits, as well as V-type ATP synthase subunit i. The V-type ATPases family are proton pumps that acidify intracellular compartments in eukaryotic cells for example yeast central vacuoles, clathrin-coated and synaptic vesicles. They have important roles in membrane trafficking processes. The 116kDa subunit (subunit a) in the V-type ATPase is part of the V0 functional domain responsible for proton transport. The a subunit is a transmembrane glycoprotein with multiple putative transmembrane helices it has a hydrophilic amino terminal and a hydrophobic carboxy terminal. It has roles in proton transport and assembly of the V-type ATPase complex. This subunit is encoded by two homologous gene in yeast VPH1 and STV1.


Pssm-ID: 460232 [Multi-domain]  Cd Length: 748  Bit Score: 42.85  E-value: 1.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    855 LESRAADLEIDVNQLKEKIQKLENELEDEKCNHQEAILRCHELEEHIQRHRNTS-LVAEDDEEADIKSKQERELSAAAEK 933
Cdd:pfam01496   60 LETPEAPSPREIDELEEKLEKLENELRELNENYETLKRNYNELTELRHVLRKAQeFFDRASGEQEEIRAASSDQEEDNAL 139
                           90
                   ....*....|..
gi 15221012    934 LAECQETIFVLG 945
Cdd:pfam01496  140 LLDDVELGFVAG 151
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
792-939 1.40e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  792 KLQEIEELRsEKEKMAVDIEGLKCQLQESEQLLADIRSQFDSAQRSNRLADTQLRCMTESYRSLESRAADLEIDVNQLKE 871
Cdd:COG1196  217 ELKEELKEL-EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  872 KIQKLENELEDEKCNHQEAILRCHELEEHIQR--HRNTSLVAEDDEEADIKSKQERELSAAAEKLAECQE 939
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAEleEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
56-269 1.69e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012   56 EEQIKSYDVQIKGYDVQVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANEEIvtKEAL 135
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL--GERA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  136 VKQ--------------HSKVAEDAVSGWEKADAEALALKNTLESVTLSKLTAEDRAAHLDGALKEcmrqIRNLKKDHEV 201
Cdd:COG3883   93 RALyrsggsvsyldvllGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE----LEALKAELEA 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15221012  202 KLHDVAlSKTKQIEKMTMEFEKRMCDYEQELLRSAADSDALSRTLQERSNMLVKVSEEKSRADAEIET 269
Cdd:COG3883  169 AKAELE-AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
55-282 1.78e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012   55 LEEQIKSYDVQIKGYDVQVKTYENQVESYEEQVKDFEEQID--AYDEKVHEYEEQVQKL---NEDVEDLNEKLSVANEEI 129
Cdd:COG4913  622 LEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvaSAEREIAELEAELERLdasSDDLAALEEQLEELEAEL 701
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  130 VT----KEALVKQHSKVA---EDAVSGWEKADAEALALKNTLESVTLSKLTAEDRAAHLDGALKECMRQIRNLKKDHEVK 202
Cdd:COG4913  702 EEleeeLDELKGEIGRLEkelEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRAR 781
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  203 LHDvalsKTKQIEKMTMEFEKRMCDYEQEL---LRSAADSDALSRTLQERSnmLVKVSEE-----KSRADAEIETLKSNL 274
Cdd:COG4913  782 LNR----AEEELERAMRAFNREWPAETADLdadLESLPEYLALLDRLEEDG--LPEYEERfkellNENSIEFVADLLSKL 855

                 ....*...
gi 15221012  275 EMCEREIK 282
Cdd:COG4913  856 RRAIREIK 863
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
788-956 2.05e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 2.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  788 ESDSKLQEIEELRSEKEKMAVDIEGLKCQLQESEQLLADIRSQFDSAQRSNRLADTQLRCMTESYRSLESRAADLEIDVN 867
Cdd:COG4372   46 ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  868 QLKEKIQKLENELEDEKCNHQEAILRCHELEEHIQRHRNTSLVAEDDEEADIKSKQERELSAAAEKLAECQETIFVLGKQ 947
Cdd:COG4372  126 DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEA 205

                 ....*....
gi 15221012  948 LKSFRPQPE 956
Cdd:COG4372  206 EKLIESLPR 214
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
792-956 2.31e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 2.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  792 KLQEIEELRSEKEKMAVDIEGLKCQLQESEQLLADIRSQFDSAQRSNRLADTQLRC--MTESYRSLESRAADLEIDVNQL 869
Cdd:COG4717   72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELPERLEEL 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  870 KEKIQKLEnELEDEKCNHQEAIlrcHELEEHIQRHRNTSLVAEDDEEADIK---SKQERELSAAAEKLAECQETIFVLGK 946
Cdd:COG4717  152 EERLEELR-ELEEELEELEAEL---AELQEELEELLEQLSLATEEELQDLAeelEELQQRLAELEEELEEAQEELEELEE 227
                        170
                 ....*....|
gi 15221012  947 QLKSFRPQPE 956
Cdd:COG4717  228 ELEQLENELE 237
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
55-325 2.65e-03

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


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 41.59  E-value: 2.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012     55 LEEQIKSYDVQIKGYDVQVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANEEIVTKEA 134
Cdd:pfam19220  123 LERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELET 202
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    135 LVKQHSK---------VAEDAVSGWEKA--DAEALALKNTLESVTLSKLTAEDRAAHLDGALKECMRQIRNlkKDHEVKL 203
Cdd:pfam19220  203 QLDATRArlralegqlAAEQAERERAEAqlEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRD--RDEAIRA 280
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    204 HDVALSKTkQIEKMTmeFEKRMCDYEQELLRSA---ADSDALSRTLQERSNMLVKVSEEKSRADAEIETLKSNLEmcERe 280
Cdd:pfam19220  281 AERRLKEA-SIERDT--LERRLAGLEADLERRTqqfQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLS--DR- 354
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 15221012    281 IKSLKYEVHVVSKELEIRNEEKNMCIRsAESANKQHLEGVKKIAK 325
Cdd:pfam19220  355 IAELTKRFEVERAALEQANRRLKEELQ-RERAERALAQGALEIAR 398
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
794-941 3.32e-03

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: 41.59  E-value: 3.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    794 QEIEELRSEKEKMAVDIEGLKCQLQESEQLLADIRSQFDSAQRsnrladtQLRCMTESYRSLESRAADLEIDVNQLKEKI 873
Cdd:TIGR02169  854 KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA-------QLRELERKIEELEAQIEKKRKRLSELKAKL 926
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    874 QKLENEL--------EDEKCNHQEAIL-----RCHELEEHIQRHRNTSLVAEDDEEadIKSKQERELSAAAEKLAECQET 940
Cdd:TIGR02169  927 EALEEELseiedpkgEDEEIPEEELSLedvqaELQRVEEEIRALEPVNMLAIQEYE--EVLKRLDELKEKRAKLEEERKA 1004

                   .
gi 15221012    941 I 941
Cdd:TIGR02169 1005 I 1005
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
85-275 4.34e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 4.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012   85 EQVKDFEEQIDAYDEKVHEYEEQVQKLNEdvedLNEKLSVANEEIVTKEALVKQHSKV--AEDAVSGWEKADAEALALKN 162
Cdd:COG4717   71 KELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELREELEKLEKLlqLLPLYQELEALEAELAELPE 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  163 TLESvtlskltAEDRAAhldgALKECMRQIRNLKKDHEVKLhdvalsktkqiEKMTMEFEKRMCDYEQELLRSAADSDAL 242
Cdd:COG4717  147 RLEE-------LEERLE----ELRELEEELEELEAELAELQ-----------EELEELLEQLSLATEEELQDLAEELEEL 204
                        170       180       190
                 ....*....|....*....|....*....|...
gi 15221012  243 SRTLQERSNMLVKVSEEKSRADAEIETLKSNLE 275
Cdd:COG4717  205 QQRLAELEEELEEAQEELEELEEELEQLENELE 237
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
71-369 4.37e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 4.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    71 VQVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANEEIVTKEALVKQHSKVAEDAVSGW 150
Cdd:PRK02224  335 VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL 414
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012   151 EKADAEALALKNTLESVTLSKLTAEDR---AAHLDGALK--ECMRQIRnlkkdhEVKLHDVALSKTKQIEKMTMEFEkrm 225
Cdd:PRK02224  415 EELREERDELREREAELEATLRTARERveeAEALLEAGKcpECGQPVE------GSPHVETIEEDRERVEELEAELE--- 485
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012   226 cDYEQELLRSAADSDALSrTLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSLKYEVhvvsKELEIRNEEKNmc 305
Cdd:PRK02224  486 -DLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERA----AELEAEAEEKR-- 557
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15221012   306 irsaESANKQHLEGVKKIAKLeAECQRLRSLVRKKLPGPAALAQMKLEVENLGRDSGDARQKRS 369
Cdd:PRK02224  558 ----EAAAEAEEEAEEAREEV-AELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKRE 616
DUF724 pfam05266
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ...
213-291 4.97e-03

Protein of unknown function (DUF724); This family contains several uncharacterized proteins found in Arabidopsis thaliana and other plants. This region is often found associated with Agenet domains and may contain coiled-coil.


Pssm-ID: 428400 [Multi-domain]  Cd Length: 188  Bit Score: 39.18  E-value: 4.97e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15221012    213 QIEKMTMEFEKRMCDYEQELLRSAADSDALSRTLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSLKYEVHVV 291
Cdd:pfam05266  106 KLLEELKKLEKKIAEEESEKRKLEEEIDELEKKILELERQLALAKEKKEAADKEIARLKSEAEKLEQEIQDVELEFEAT 184
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
81-444 6.25e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 40.80  E-value: 6.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    81 ESYEEQVKDFEEQ-IDAYdEKVHEYeeQVQKLNEDVEDLNEKLS----VANEEIV----TKEALVKQHSKVAEDAVSGWE 151
Cdd:PTZ00108  976 SDALDILKEFYLVrLDLY-KKRKEY--LLGKLERELARLSNKVRfikhVINGELVitnaKKKDLVKELKKLGYVRFKDII 1052
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012   152 KADAEALALKNTLESVTLSKLTAEDRAAHLDGAL--------------KEcmrQIRNLKKDHEVKLHDVALSKTKQIEKM 217
Cdd:PTZ00108 1053 KKKSEKITAEEEEGAEEDDEADDEDDEEELGAAVsydyllsmpiwsltKE---KVEKLNAELEKKEKELEKLKNTTPKDM 1129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012   218 TME----FEKRMCDYEQELLRSAADsdalSRTLQERSNMLVKVSEEKSRADAEiETLKSNLEMCEREIKSLKYEVHVVSK 293
Cdd:PTZ00108 1130 WLEdldkFEEALEEQEEVEEKEIAK----EQRLKSKTKGKASKLRKPKLKKKE-KKKKKSSADKSKKASVVGNSKRVDSD 1204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012   294 ELeIRNEEKNMCIRSAESANKQHLEGVKKIAKLEAECQRLRSLVRKKLPGPAALAQMKLEVENLGRDSGDARQKRSPVKV 373
Cdd:PTZ00108 1205 EK-RKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQY 1283
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15221012   374 SS--PCKSPGGYSSTGSEFSLDNAQKFQKeneFLTERLLAMEEETKMLKEALAKRNSELLESRNLCAQSTSKL 444
Cdd:PTZ00108 1284 SPppPSKRPDGESNGGSKPSSPTKKKVKK---RLEGSLAALKKKKKSEKKTARKKKSKTRVKQASASQSSRLL 1353
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
794-936 6.46e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 6.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  794 QEIEELRSEKEKMAVDIEGLKCQLQESEQLLADIRSQFDSAQRSNRLADTQLRCMTESYRSLESRAADLEIDVNQLKEKI 873
Cdd:COG1196  281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15221012  874 QKLENELEDEKCNHQEAILRCHELEEHIQRHRNTSLVAEDDE------EADIKSKQERELSAAAEKLAE 936
Cdd:COG1196  361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLeeleeaEEALLERLERLEEELEELEEA 429
Phage_GP20 pfam06810
Phage minor structural protein GP20; This family consists of several phage minor structural ...
57-200 6.86e-03

Phage minor structural protein GP20; This family consists of several phage minor structural protein GP20 sequences of around 180 residues in length. The function of this family is unknown.


Pssm-ID: 429131 [Multi-domain]  Cd Length: 149  Bit Score: 38.11  E-value: 6.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012     57 EQIKSYDVQIKGYDV---QVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEqvqkLNEDVEDLNEKLSVANEEIVTKE 133
Cdd:pfam06810    1 EQADKVMEAENGKDIpkaKFDEVNTERDTLKEQLATRDKQLKDLKKVAKDNEE----LQKQIDELQAKNKDAEADYEAKI 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15221012    134 ALVKQHSKVaEDAVSGWEKADAEALALKNTLESVTLSKltaedraahlDGALKECMRQIRNLKKDHE 200
Cdd:pfam06810   77 ADLKFDNAI-KLALKGAKAKNEKAVKALLDKDKLKLKD----------DGTLIGLDEQIEGLKESDK 132
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
112-362 6.98e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 6.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  112 NEDVEDLNEKLSVANEEIVTKEALVKQHSKVAEDAVSGWEKADAEALALKNTLEsvtlsklTAEDRAAHLDGALKECMRQ 191
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIR-------ALEQELAALEAELAELEKE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  192 IRNLKKDHEVKLHDVA-----LSKTKQIEKMTMEFEKrmcDYEQELLRSAADSDALSRTLQERSNMLVKVSEEksradae 266
Cdd:COG4942   92 IAELRAELEAQKEELAellraLYRLGRQPPLALLLSP---EDFLDAVRRLQYLKYLAPARREQAEELRADLAE------- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  267 IETLKSNLEMCEREIKSLKYEVHVVSKELEIRNEEKNMCIRSAESANKQHLegvKKIAKLEAECQRLRSLVrKKLPGPAA 346
Cdd:COG4942  162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA---AELAELQQEAEELEALI-ARLEAEAA 237
                        250
                 ....*....|....*.
gi 15221012  347 LAQMKLEVENLGRDSG 362
Cdd:COG4942  238 AAAERTPAAGFAALKG 253
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
84-275 8.17e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 8.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012   84 EEQVKDFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLSVANeeivtkealvkQHSKVAEDAVSgWEKADAEALALKNT 163
Cdd:COG4913  609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ-----------RLAEYSWDEID-VASAEREIAELEAE 676
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  164 LESVTLSKL---TAEDRAAHLDGALKECMRQIRNLKKD---HEVKLHDvALSKTKQIEKMTMEFEKRMCDYEQELL---R 234
Cdd:COG4913  677 LERLDASSDdlaALEEQLEELEAELEELEEELDELKGEigrLEKELEQ-AEEELDELQDRLEAAEDLARLELRALLeerF 755
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 15221012  235 SAADSDALSRTLQERsnmlvkVSEEKSRADAEIETLKSNLE 275
Cdd:COG4913  756 AAALGDAVERELREN------LEERIDALRARLNRAEEELE 790
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
791-936 8.22e-03

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: 40.44  E-value: 8.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012    791 SKLQEIEELRSEKEKMAVDIEGLKCQLQESEQLLADIRSQFDSAQRSNRLADTQLRCMTESYRSLESRAADLEidvnqlk 870
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELE------- 743
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15221012    871 EKIQKLENELEDEKCNHQEAILRCHELEEHIQRHRNtslvAEDDEEADIKSKQERELSAAAEKLAE 936
Cdd:TIGR02169  744 EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEE----ALNDLEARLSHSRIPEIQAELSKLEE 805
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
55-303 8.62e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.51  E-value: 8.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012   55 LEEQIKSYDVQIKGYDVQVKTYENQVESYEEQVKDFEEQIDAYDEKVHEYEEQVQKLNEDVEDLNEKLS-------VANE 127
Cdd:COG1340    6 LSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKelkeerdELNE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  128 EIVT-KEALVKQHSKVAEDAVSGWEKADAEAL--ALKNTLESVTLSKltAEDRAahLDGALKECMRQIRNLKKDHEVKlh 204
Cdd:COG1340   86 KLNElREELDELRKELAELNKAGGSIDKLRKEieRLEWRQQTEVLSP--EEEKE--LVEKIKELEKELEKAKKALEKN-- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221012  205 dvalSKTKQIEKMTMEFEKRMCDYEQELLRSAADSDALSRTLQERSNMLVKVSEEKSRADAEIETLKSNLEMCEREIKSL 284
Cdd:COG1340  160 ----EKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIEL 235
                        250
                 ....*....|....*....
gi 15221012  285 KYEVHVVSKELEIRNEEKN 303
Cdd:COG1340  236 QKELRELRKELKKLRKKQR 254
 
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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