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Conserved domains on  [gi|1958792183|ref|XP_038936054|]
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zinc finger C3H1 domain-containing protein isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1369-1700 3.18e-10

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 63.21  E-value: 3.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1369 WLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCETAVEYAPDYQsfctFLHL 1448
Cdd:COG2956     11 WYFKGLNYLLNGQ------PDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRA----EALL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1449 E---STFEEKDYvcERMVEFLMGAAKRETSDIlsfqllEALLFRVQLHIFTGRCQSALAILQNALKLANDAIVAEYLrte 1525
Cdd:COG2956     81 ElaqDYLKAGLL--DRAEELLEKLLELDPDDA------EALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCE--- 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1526 drclawLAYIHLiefnslpsklydpsnanpsrivntepfvmpwqaAQDvktNPDLLLAVFEDAVKACTDealtsgertev 1605
Cdd:COG2956    150 ------LAELYL---------------------------------EQG---DYDEAIEALEKALKLDPD----------- 176

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1606 CLPLYTNMMALHQLLERDEEAVELCKSLLESCPTNCQLLETLAALYLKTDCYDKARWVWLTAFENNPQNAEIFYhLCKFF 1685
Cdd:COG2956    177 CARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLA-LADLL 255

                          330
                   ....*....|....*
gi 1958792183 1686 ILQNGGDKLLPLLRQ 1700
Cdd:COG2956    256 ERKEGLEAALALLER 270
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 828-1002 5.99e-06

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


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 50.92  E-value: 5.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  828 TKQVADAEAKLKKHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKLTEQLQAAEKILSVNRMFLKKLQEQIHRVQQR 907
Cdd:COG4942     19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  908 VTIKKaltlkygEELARAKAVASKeLGKRKLEQDRLGPN------KMMRLDNSpVSSPRKHSAELIAMEKRRLQKLEYEY 981
Cdd:COG4942     99 LEAQK-------EELAELLRALYR-LGRQPPLALLLSPEdfldavRRLQYLKY-LAPARREQAEELRADLAELAALRAEL 169

                          170       180
                   ....*....|....*....|.
gi 1958792183  982 ALKIQKLKEARALKAKEQQNL 1002
Cdd:COG4942    170 EAERAELEALLAELEEERAAL 190
zf-C3H1 pfam10650
Putative zinc-finger domain; This domain is conserved in fungi and might be a zinc-finger ...
 1190-1209 1.03e-05

Putative zinc-finger domain; This domain is conserved in fungi and might be a zinc-finger domain as it contains three conserved Cs and an H in the C-x8-C-x5-C-x3-H conformation typical of a zinc-finger.


:

Pssm-ID: 431418  Cd Length: 22  Bit Score: 43.72  E-value: 1.03e-05
                           10        20
                   ....*....|....*....|.
gi 1958792183 1190 FCRFDLAG-TCNDDDCQWQHV 1209
Cdd:pfam10650    1 LCPYELAGgVCNDPSCEFQHF 21
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 744-1139 1.15e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member pfam02463:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1161  Bit Score: 47.27  E-value: 1.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  744 KEARRTAEQASKPKVPPKSEKENDPLRTPEALPEEKKIEYRLLKEEIA------NREKQRLIKSDQLKTSSSSPANSDVE 817
Cdd:pfam02463  242 LQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKllakeeEELKSELLKLERRKVDDEEKLKESEK 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  818 MDG--IGRIAMVTKQVADAEAKLKKHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKLTEQLQAAEKILSVNRMF-- 893
Cdd:pfam02463  322 EKKkaEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELks 401

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  894 --LKKLQEQIHRVQQRVTIKKALTLKYGEELARAKAVASKELGKRKLEQDRLGPNKMMRLDNSPVSSPRKHSAELIAMEK 971
Cdd:pfam02463  402 eeEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVK 481

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  972 RRLQKLEyeyALKIQKLKEARalkAKEQQNLVPVVEEEPEFSLPQPSLHDLTQDKLTlDTEENDADDEVLSGSNRERRRS 1051
Cdd:pfam02463  482 LQEQLEL---LLSRQKLEERS---QKESKARSGLKVLLALIKDGVGGRIISAHGRLG-DLGVAVENYKVAISTAVIVEVS 554

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1052 FLESNSFTKPNLKHTDTPNKecVNKLSKSTVEKPELFLGLKIGELQKLYSKADSLKQLILKTTTGITENILHGQEISVDV 1131
Cdd:pfam02463  555 ATADEVEERQKLVRALTELP--LGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDT 632


                   ....*...
gi 1958792183 1132 DFVTAQSK 1139
Cdd:pfam02463  633 ELTKLKES 640
 
Name Accession Description Interval E-value
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1369-1700 3.18e-10

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 63.21  E-value: 3.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1369 WLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCETAVEYAPDYQsfctFLHL 1448
Cdd:COG2956     11 WYFKGLNYLLNGQ------PDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRA----EALL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1449 E---STFEEKDYvcERMVEFLMGAAKRETSDIlsfqllEALLFRVQLHIFTGRCQSALAILQNALKLANDAIVAEYLrte 1525
Cdd:COG2956     81 ElaqDYLKAGLL--DRAEELLEKLLELDPDDA------EALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCE--- 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1526 drclawLAYIHLiefnslpsklydpsnanpsrivntepfvmpwqaAQDvktNPDLLLAVFEDAVKACTDealtsgertev 1605
Cdd:COG2956    150 ------LAELYL---------------------------------EQG---DYDEAIEALEKALKLDPD----------- 176

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1606 CLPLYTNMMALHQLLERDEEAVELCKSLLESCPTNCQLLETLAALYLKTDCYDKARWVWLTAFENNPQNAEIFYhLCKFF 1685
Cdd:COG2956    177 CARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLA-LADLL 255

                          330
                   ....*....|....*
gi 1958792183 1686 ILQNGGDKLLPLLRQ 1700
Cdd:COG2956    256 ERKEGLEAALALLER 270
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 828-1002 5.99e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 50.92  E-value: 5.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  828 TKQVADAEAKLKKHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKLTEQLQAAEKILSVNRMFLKKLQEQIHRVQQR 907
Cdd:COG4942     19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  908 VTIKKaltlkygEELARAKAVASKeLGKRKLEQDRLGPN------KMMRLDNSpVSSPRKHSAELIAMEKRRLQKLEYEY 981
Cdd:COG4942     99 LEAQK-------EELAELLRALYR-LGRQPPLALLLSPEdfldavRRLQYLKY-LAPARREQAEELRADLAELAALRAEL 169

                          170       180
                   ....*....|....*....|.
gi 1958792183  982 ALKIQKLKEARALKAKEQQNL 1002
Cdd:COG4942    170 EAERAELEALLAELEEERAAL 190
zf-C3H1 pfam10650
Putative zinc-finger domain; This domain is conserved in fungi and might be a zinc-finger ...
 1190-1209 1.03e-05

Putative zinc-finger domain; This domain is conserved in fungi and might be a zinc-finger domain as it contains three conserved Cs and an H in the C-x8-C-x5-C-x3-H conformation typical of a zinc-finger.


Pssm-ID: 431418  Cd Length: 22  Bit Score: 43.72  E-value: 1.03e-05
                           10        20
                   ....*....|....*....|.
gi 1958792183 1190 FCRFDLAG-TCNDDDCQWQHV 1209
Cdd:pfam10650    1 LCPYELAGgVCNDPSCEFQHF 21
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 739-1011 1.10e-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: 50.83  E-value: 1.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  739 LESMIKEARRTAEQASKpkvppKSEKENDPLRTPEALPEEKKIEYRLLKEEIANREKQRLIKSDQLKTSSSSPANSDVEM 818
Cdd:TIGR02168  710 LEEELEQLRKELEELSR-----QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  819 --------DGIGRIAMVTKQVADAEAKLKKHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKLTEQLQAAEKILSVN 890
Cdd:TIGR02168  785 eeleaqieQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  891 RMFLKKLQEQIHRVQQRVtikkaltlkygEELARAKAVASKELGKRKLEQDRLGpNKMMRLDNSpvsspRKHSAELIAME 970
Cdd:TIGR02168  865 EELIEELESELEALLNER-----------ASLEEALALLRSELEELSEELRELE-SKRSELRRE-----LEELREKLAQL 927

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1958792183  971 KRRLQKLEYEYALKIQKLKEARALKAKEQQNLVPVVEEEPE 1011
Cdd:TIGR02168  928 ELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEE 968
PTZ00121 PTZ00121
MAEBL; Provisional
 745-1046 1.21e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 1.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  745 EARRTAEQASKpkvppKSEKENDPLRTPEalpEEKKIEYRLLKEEIANREKQRLIKSDQLKTSSSSPANSDvemdgigri 824
Cdd:PTZ00121  1561 EEKKKAEEAKK-----AEEDKNMALRKAE---EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE--------- 1623

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  825 amvtkQVADAEAKLKKHKILLIKDEsvlknlvlQEAKKKESVRNAE--AKITKLTEQLQAAEKilsvnrmflKKLQEQIH 902
Cdd:PTZ00121  1624 -----ELKKAEEEKKKVEQLKKKEA--------EEKKKAEELKKAEeeNKIKAAEEAKKAEED---------KKKAEEAK 1681

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  903 RVQQRVTIKKALTLKYGEELARAKAVASKEL-GKRKLEQDRlgpnKMMRLDNSPVSSPRKHSAEliamEKRRLQ--KLEY 979
Cdd:PTZ00121  1682 KAEEDEKKAAEALKKEAEEAKKAEELKKKEAeEKKKAEELK----KAEEENKIKAEEAKKEAEE----DKKKAEeaKKDE 1753

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958792183  980 EYALKIQKLKEARALKAKE-QQNLVPVVEEEPEfslPQPSLHDLTQDKLTLDTEENDADdeVLSGSNR 1046
Cdd:PTZ00121  1754 EEKKKIAHLKKEEEKKAEEiRKEKEAVIEEELD---EEDEKRRMEVDKKIKDIFDNFAN--IIEGGKE 1816
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 738-1032 5.99e-05

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 47.97  E-value: 5.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  738 GLESMIKEARRTAEQaSKPKVPPKSEKENDPLRTPEALPEEKKIeyrLLKEEIANREKQRLIKSDqLKTSSSSPANSDVE 817
Cdd:pfam07888   77 ELESRVAELKEELRQ-SREKHEELEEKYKELSASSEELSEEKDA---LLAQRAAHEARIRELEED-IKTLTQRVLERETE 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  818 MDGIG-RIAMVTKQVADAEAKLKKHKILLIKDESVLKNLV--LQEAKKKESVRNAEA-----KITKLTEQLQAAEKILSV 889
Cdd:pfam07888  152 LERMKeRAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSkeFQELRNSLAQRDTQVlqlqdTITTLTQKLTTAHRKEAE 231

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  890 NRMFLKKL---QEQIHRVQQRVTIkkaltlkYGEELAraKAVASKELGKRKLEQDRLGPNKM----------MRLDNSPV 956
Cdd:pfam07888  232 NEALLEELrslQERLNASERKVEG-------LGEELS--SMAAQRDRTQAELHQARLQAAQLtlqladaslaLREGRARW 302

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  957 SSPRKHSAELIAMEKRRLQKLEYEYALKIQKLKEARALKAK--------EQQNLVPVVEEEPEFSLPQPSLHDLTQDKLT 1028
Cdd:pfam07888  303 AQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKlevelgreKDCNRVQLSESRRELQELKASLRVAQKEKEQ 382


                   ....
gi 1958792183 1029 LDTE 1032
Cdd:pfam07888  383 LQAE 386
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 744-1139 1.15e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 47.27  E-value: 1.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  744 KEARRTAEQASKPKVPPKSEKENDPLRTPEALPEEKKIEYRLLKEEIA------NREKQRLIKSDQLKTSSSSPANSDVE 817
Cdd:pfam02463  242 LQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKllakeeEELKSELLKLERRKVDDEEKLKESEK 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  818 MDG--IGRIAMVTKQVADAEAKLKKHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKLTEQLQAAEKILSVNRMF-- 893
Cdd:pfam02463  322 EKKkaEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELks 401

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  894 --LKKLQEQIHRVQQRVTIKKALTLKYGEELARAKAVASKELGKRKLEQDRLGPNKMMRLDNSPVSSPRKHSAELIAMEK 971
Cdd:pfam02463  402 eeEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVK 481

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  972 RRLQKLEyeyALKIQKLKEARalkAKEQQNLVPVVEEEPEFSLPQPSLHDLTQDKLTlDTEENDADDEVLSGSNRERRRS 1051
Cdd:pfam02463  482 LQEQLEL---LLSRQKLEERS---QKESKARSGLKVLLALIKDGVGGRIISAHGRLG-DLGVAVENYKVAISTAVIVEVS 554

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1052 FLESNSFTKPNLKHTDTPNKecVNKLSKSTVEKPELFLGLKIGELQKLYSKADSLKQLILKTTTGITENILHGQEISVDV 1131
Cdd:pfam02463  555 ATADEVEERQKLVRALTELP--LGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDT 632


                   ....*...
gi 1958792183 1132 DFVTAQSK 1139
Cdd:pfam02463  633 ELTKLKES 640
TPR_19 pfam14559
Tetratricopeptide repeat;
1352-1409 5.72e-03

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 37.18  E-value: 5.72e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958792183 1352 IANLEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIW 1409
Cdd:pfam14559    8 LELLEQALAEDPDNAEARLGLAEALLALGR------LDEAEALLAALPAADPDDPRYA 59
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 1619-1672 7.53e-03

Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 (ACL4) acts as a chaperone for the L4 ribosomal subunit, encoded by RPL4A and RPL4B, and is required for hierarchical ribosome assembly. It is required for the soluble expression of newly synthesized RPL4 and for the protection of RPL4 from the Tom1-dependent cellular degradation machinery. ACL4 shields ribosomal protein L4 until timely release and insertion into the pre-ribosome is possible, once ribosomal protein L18 is present.


Pssm-ID: 467942 [Multi-domain]  Cd Length: 306  Bit Score: 40.69  E-value: 7.53e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958792183 1619 LLERD--EEAVELCKSLLESCPTNCQLLETLAALYLKTDCYDKARWVWLTAFENNP 1672
Cdd:cd24142     10 LLDQGnfELALKFLQRALELEPNNVEALELLGEILLELGDVEEAREVLLRAIELDP 65
 
Name Accession Description Interval E-value
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1369-1700 3.18e-10

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 63.21  E-value: 3.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1369 WLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCETAVEYAPDYQsfctFLHL 1448
Cdd:COG2956     11 WYFKGLNYLLNGQ------PDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRA----EALL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1449 E---STFEEKDYvcERMVEFLMGAAKRETSDIlsfqllEALLFRVQLHIFTGRCQSALAILQNALKLANDAIVAEYLrte 1525
Cdd:COG2956     81 ElaqDYLKAGLL--DRAEELLEKLLELDPDDA------EALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCE--- 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1526 drclawLAYIHLiefnslpsklydpsnanpsrivntepfvmpwqaAQDvktNPDLLLAVFEDAVKACTDealtsgertev 1605
Cdd:COG2956    150 ------LAELYL---------------------------------EQG---DYDEAIEALEKALKLDPD----------- 176

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1606 CLPLYTNMMALHQLLERDEEAVELCKSLLESCPTNCQLLETLAALYLKTDCYDKARWVWLTAFENNPQNAEIFYhLCKFF 1685
Cdd:COG2956    177 CARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLA-LADLL 255

                          330
                   ....*....|....*
gi 1958792183 1686 ILQNGGDKLLPLLRQ 1700
Cdd:COG2956    256 ERKEGLEAALALLER 270
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 1352-1438 5.23e-10

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 59.25  E-value: 5.23e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1352 IANLEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCET 1431
Cdd:COG4235      3 IARLRQALAANPNDAEGWLLLGRAYLRLGR------YDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLER 76


                   ....*..
gi 1958792183 1432 AVEYAPD 1438
Cdd:COG4235     77 ALALDPD 83
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 1615-1700 1.97e-06

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 49.57  E-value: 1.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1615 ALHQLLERDEEAVELCKSLLESCPTNCQLLETLAALYLKTDCYDKARWVWLTAFENNPQNAEIFYHLCKFFILQNGGDKL 1694
Cdd:COG5010     62 NLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEA 141


                   ....*.
gi 1958792183 1695 LPLLRQ 1700
Cdd:COG5010    142 KAALQR 147
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
1352-1537 4.07e-06

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 50.39  E-value: 4.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1352 IANLEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCET 1431
Cdd:COG0457     62 LADYEQALELDPDDAEALNNLGLALQALGR------YEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYER 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1432 AVEYAPD----YQSFCTFLHLESTFEEKDYVCERMVEFLMGAAKRETSDILSFQLLEALLFRVQLHIFTGRCQSALAILQ 1507
Cdd:COG0457    136 ALELDPDdadaLYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILT 215

                          170       180       190
                   ....*....|....*....|....*....|
gi 1958792183 1508 NALKLANDAIVAEYLRTEDRCLAWLAYIHL 1537
Cdd:COG0457    216 LAALAELLLLALALLLALRLAALALYQYRA 245
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 828-1002 5.99e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 50.92  E-value: 5.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  828 TKQVADAEAKLKKHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKLTEQLQAAEKILSVNRMFLKKLQEQIHRVQQR 907
Cdd:COG4942     19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  908 VTIKKaltlkygEELARAKAVASKeLGKRKLEQDRLGPN------KMMRLDNSpVSSPRKHSAELIAMEKRRLQKLEYEY 981
Cdd:COG4942     99 LEAQK-------EELAELLRALYR-LGRQPPLALLLSPEdfldavRRLQYLKY-LAPARREQAEELRADLAELAALRAEL 169

                          170       180
                   ....*....|....*....|.
gi 1958792183  982 ALKIQKLKEARALKAKEQQNL 1002
Cdd:COG4942    170 EAERAELEALLAELEEERAAL 190
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1352-1522 7.69e-06

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 49.73  E-value: 7.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1352 IANLEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCET 1431
Cdd:COG2956     96 EELLEKLLELDPDDAEALRLLAEIYEQEGD------WEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEK 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1432 AVEYAPDYQSfcTFLHLEST-FEEKDYvcERMVEFLMGAAKRETSDilsfqlLEALLFRVQLHIFTGRCQSALAILQNAL 1510
Cdd:COG2956    170 ALKLDPDCAR--ALLLLAELyLEQGDY--EEAIAALERALEQDPDY------LPALPRLAELYEKLGDPEEALELLRKAL 239

                          170
                   ....*....|..
gi 1958792183 1511 KLANDAIVAEYL 1522
Cdd:COG2956    240 ELDPSDDLLLAL 251
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 1352-1439 9.10e-06

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 47.11  E-value: 9.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1352 IANLEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCET 1431
Cdd:COG4783     58 IVLLHEALELDPDEPEARLNLGLALLKAGD------YDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEK 131


                   ....*...
gi 1958792183 1432 AVEYAPDY 1439
Cdd:COG4783    132 ALELDPDD 139
zf-C3H1 pfam10650
Putative zinc-finger domain; This domain is conserved in fungi and might be a zinc-finger ...
 1190-1209 1.03e-05

Putative zinc-finger domain; This domain is conserved in fungi and might be a zinc-finger domain as it contains three conserved Cs and an H in the C-x8-C-x5-C-x3-H conformation typical of a zinc-finger.


Pssm-ID: 431418  Cd Length: 22  Bit Score: 43.72  E-value: 1.03e-05
                           10        20
                   ....*....|....*....|.
gi 1958792183 1190 FCRFDLAG-TCNDDDCQWQHV 1209
Cdd:pfam10650    1 LCPYELAGgVCNDPSCEFQHF 21
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 739-1011 1.10e-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: 50.83  E-value: 1.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  739 LESMIKEARRTAEQASKpkvppKSEKENDPLRTPEALPEEKKIEYRLLKEEIANREKQRLIKSDQLKTSSSSPANSDVEM 818
Cdd:TIGR02168  710 LEEELEQLRKELEELSR-----QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  819 --------DGIGRIAMVTKQVADAEAKLKKHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKLTEQLQAAEKILSVN 890
Cdd:TIGR02168  785 eeleaqieQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  891 RMFLKKLQEQIHRVQQRVtikkaltlkygEELARAKAVASKELGKRKLEQDRLGpNKMMRLDNSpvsspRKHSAELIAME 970
Cdd:TIGR02168  865 EELIEELESELEALLNER-----------ASLEEALALLRSELEELSEELRELE-SKRSELRRE-----LEELREKLAQL 927

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1958792183  971 KRRLQKLEYEYALKIQKLKEARALKAKEQQNLVPVVEEEPE 1011
Cdd:TIGR02168  928 ELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEE 968
PTZ00121 PTZ00121
MAEBL; Provisional
 745-1046 1.21e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 1.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  745 EARRTAEQASKpkvppKSEKENDPLRTPEalpEEKKIEYRLLKEEIANREKQRLIKSDQLKTSSSSPANSDvemdgigri 824
Cdd:PTZ00121  1561 EEKKKAEEAKK-----AEEDKNMALRKAE---EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE--------- 1623

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  825 amvtkQVADAEAKLKKHKILLIKDEsvlknlvlQEAKKKESVRNAE--AKITKLTEQLQAAEKilsvnrmflKKLQEQIH 902
Cdd:PTZ00121  1624 -----ELKKAEEEKKKVEQLKKKEA--------EEKKKAEELKKAEeeNKIKAAEEAKKAEED---------KKKAEEAK 1681

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  903 RVQQRVTIKKALTLKYGEELARAKAVASKEL-GKRKLEQDRlgpnKMMRLDNSPVSSPRKHSAEliamEKRRLQ--KLEY 979
Cdd:PTZ00121  1682 KAEEDEKKAAEALKKEAEEAKKAEELKKKEAeEKKKAEELK----KAEEENKIKAEEAKKEAEE----DKKKAEeaKKDE 1753

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958792183  980 EYALKIQKLKEARALKAKE-QQNLVPVVEEEPEfslPQPSLHDLTQDKLTLDTEENDADdeVLSGSNR 1046
Cdd:PTZ00121  1754 EEKKKIAHLKKEEEKKAEEiRKEKEAVIEEELD---EEDEKRRMEVDKKIKDIFDNFAN--IIEGGKE 1816
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 834-1050 2.59e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 2.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  834 AEAKLKKHKILLIKDESVLKNLVLQEAKKKEsvrnAEAKITKLTEQLQAAEKILSVNRMFLKKLQEQIHRVQQRVTIKKA 913
Cdd:COG1196    220 EELKELEAELLLLKLRELEAELEELEAELEE----LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  914 LTLKYGEELARAKAvASKELGKRKLEQDRLGPNKMMRLDNspvssprkHSAELIAMEKrRLQKLEYEYALKIQKLKEARA 993
Cdd:COG1196    296 ELARLEQDIARLEE-RRRELEERLEELEEELAELEEELEE--------LEEELEELEE-ELEEAEEELEEAEAELAEAEE 365

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958792183  994 LKAKEQQNLVPVVEEepefslpqpsLHDLTQDKLTLDTEENDADDEVLSGSNRERRR 1050
Cdd:COG1196    366 ALLEAEAELAEAEEE----------LEELAEELLEALRAAAELAAQLEELEEAEEAL 412
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 1352-1439 3.49e-05

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 45.57  E-value: 3.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1352 IANLEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCET 1431
Cdd:COG4783     24 EALLEKALELDPDNPEAFALLGEILLQLGD------LDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEK 97


                   ....*...
gi 1958792183 1432 AVEYAPDY 1439
Cdd:COG4783     98 ALKLDPEH 105
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 1352-1437 3.67e-05

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 46.11  E-value: 3.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1352 IANLEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCET 1431
Cdd:COG5010     74 LALLEQALQLDPNNPELYYNLALLYSRSGD------KDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQR 147


                   ....*.
gi 1958792183 1432 AVEYAP 1437
Cdd:COG5010    148 ALGTSP 153
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 1352-1439 4.60e-05

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 48.45  E-value: 4.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1352 IANLEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCET 1431
Cdd:COG3914     98 LALYRRALALNPDNAEALFNLGNLLLALGR------LEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRR 171


                   ....*...
gi 1958792183 1432 AVEYAPDY 1439
Cdd:COG3914    172 ALELDPDN 179
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 738-1032 5.99e-05

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 47.97  E-value: 5.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  738 GLESMIKEARRTAEQaSKPKVPPKSEKENDPLRTPEALPEEKKIeyrLLKEEIANREKQRLIKSDqLKTSSSSPANSDVE 817
Cdd:pfam07888   77 ELESRVAELKEELRQ-SREKHEELEEKYKELSASSEELSEEKDA---LLAQRAAHEARIRELEED-IKTLTQRVLERETE 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  818 MDGIG-RIAMVTKQVADAEAKLKKHKILLIKDESVLKNLV--LQEAKKKESVRNAEA-----KITKLTEQLQAAEKILSV 889
Cdd:pfam07888  152 LERMKeRAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSkeFQELRNSLAQRDTQVlqlqdTITTLTQKLTTAHRKEAE 231

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  890 NRMFLKKL---QEQIHRVQQRVTIkkaltlkYGEELAraKAVASKELGKRKLEQDRLGPNKM----------MRLDNSPV 956
Cdd:pfam07888  232 NEALLEELrslQERLNASERKVEG-------LGEELS--SMAAQRDRTQAELHQARLQAAQLtlqladaslaLREGRARW 302

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  957 SSPRKHSAELIAMEKRRLQKLEYEYALKIQKLKEARALKAK--------EQQNLVPVVEEEPEFSLPQPSLHDLTQDKLT 1028
Cdd:pfam07888  303 AQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKlevelgreKDCNRVQLSESRRELQELKASLRVAQKEKEQ 382


                   ....
gi 1958792183 1029 LDTE 1032
Cdd:pfam07888  383 LQAE 386
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1574-1702 6.00e-05

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 47.03  E-value: 6.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1574 VKTNPDLLLAVFE-----------DAVKACTDEALTSGERTEvclPLYTNMMALHQLLERDEEAVELCKSLLESCPTNCQ 1642
Cdd:COG2956     69 LERDPDRAEALLElaqdylkagllDRAEELLEKLLELDPDDA---EALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAH 145

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1643 LLETLAALYLKTDCYDKARWVWLTAFENNPQNAEIFYHLCKFFILQNGGDKLLPLLRQFI 1702
Cdd:COG2956    146 AYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERAL 205
PTZ00121 PTZ00121
MAEBL; Provisional
 744-1081 8.26e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 8.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  744 KEARRTAEQASKPKVPPKSEKENDPLRTPEALPEEKKIEYRLLKEEIANREKQRliKSDQLKTSSSSPANSDVEMDGIGR 823
Cdd:PTZ00121  1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK--KADELKKAEELKKAEEKKKAEEAK 1570

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  824 IAMVTKQVADAEAKL-----KKHKILLIKDESVLKNLVLQEAKKKEsvrnaEAKITklTEQLQAAEKILSVNRMFLKKLQ 898
Cdd:PTZ00121  1571 KAEEDKNMALRKAEEakkaeEARIEEVMKLYEEEKKMKAEEAKKAE-----EAKIK--AEELKKAEEEKKKVEQLKKKEA 1643

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  899 EQihrvqqrvtIKKALTLKYGEELARAKavasKELGKRKLEQDRLGPNKMMRLDNSpvsspRKHSAELIAMEKRRLQKLE 978
Cdd:PTZ00121  1644 EE---------KKKAEELKKAEEENKIK----AAEEAKKAEEDKKKAEEAKKAEED-----EKKAAEALKKEAEEAKKAE 1705

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  979 YEYALKIQKLKEARALKAKEQQNLVPVVEEEPEFSLPQPSLHDLTQDKltldtEENDADDEVLSGSNRERRRSFLESNSF 1058
Cdd:PTZ00121  1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE-----EEKKKIAHLKKEEEKKAEEIRKEKEAV 1780

                          330       340
                   ....*....|....*....|...
gi 1958792183 1059 TKPNLKHTDTPNKECVNKLSKST 1081
Cdd:PTZ00121  1781 IEEELDEEDEKRRMEVDKKIKDI 1803
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1577-1702 8.28e-05

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 46.65  E-value: 8.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1577 NPDLLLAVFEDAVKACTDEAltsgertevclPLYTNMMALHQLLERDEEAVELCKSLLESCPTNCQLLETLAALYLKTDC 1656
Cdd:COG2956     23 QPDKAIDLLEEALELDPETV-----------EAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGL 91

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958792183 1657 YDKARWVWLTAFENNPQNAEIFYHLCKFFILQNGGDKLLPLLRQFI 1702
Cdd:COG2956     92 LDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLL 137
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 744-1139 1.15e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 47.27  E-value: 1.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  744 KEARRTAEQASKPKVPPKSEKENDPLRTPEALPEEKKIEYRLLKEEIA------NREKQRLIKSDQLKTSSSSPANSDVE 817
Cdd:pfam02463  242 LQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKllakeeEELKSELLKLERRKVDDEEKLKESEK 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  818 MDG--IGRIAMVTKQVADAEAKLKKHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKLTEQLQAAEKILSVNRMF-- 893
Cdd:pfam02463  322 EKKkaEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELks 401

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  894 --LKKLQEQIHRVQQRVTIKKALTLKYGEELARAKAVASKELGKRKLEQDRLGPNKMMRLDNSPVSSPRKHSAELIAMEK 971
Cdd:pfam02463  402 eeEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVK 481

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  972 RRLQKLEyeyALKIQKLKEARalkAKEQQNLVPVVEEEPEFSLPQPSLHDLTQDKLTlDTEENDADDEVLSGSNRERRRS 1051
Cdd:pfam02463  482 LQEQLEL---LLSRQKLEERS---QKESKARSGLKVLLALIKDGVGGRIISAHGRLG-DLGVAVENYKVAISTAVIVEVS 554

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1052 FLESNSFTKPNLKHTDTPNKecVNKLSKSTVEKPELFLGLKIGELQKLYSKADSLKQLILKTTTGITENILHGQEISVDV 1131
Cdd:pfam02463  555 ATADEVEERQKLVRALTELP--LGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDT 632


                   ....*...
gi 1958792183 1132 DFVTAQSK 1139
Cdd:pfam02463  633 ELTKLKES 640
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
1610-1681 1.22e-04

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 45.77  E-value: 1.22e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958792183 1610 YTNMMALHQLLERDEEAVELCKSLLESCPTNCQLLETLAALYLKTDCYDKARWVWLTAFENNPQNAEIFYHL 1681
Cdd:COG0457     45 LYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNL 116
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
1352-1438 1.62e-04

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 42.46  E-value: 1.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1352 IANLEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNvLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCET 1431
Cdd:COG3063     12 EEYYEKALELDPDNADALNNLGLLLLEQGR------YDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLER 84


                   ....*..
gi 1958792183 1432 AVEYAPD 1438
Cdd:COG3063     85 ALELDPS 91
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 1498-1702 1.84e-04

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 46.52  E-value: 1.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1498 RCQSALAILQNALKLANDAIVAEYLRTEDRCLAWLAYIHLIEFNSLPSKLYDPSNANPSRIVNTEPFVMPWQAAQDVKTN 1577
Cdd:COG3914      5 ALLALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELA 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1578 PDLLLAV--FEDAVKACtDEALtsgERTEVCLPLYTNMMALHQLLERDEEAVELCKSLLESCPTNCQLLETLAALYLKTD 1655
Cdd:COG3914     85 ALLLQALgrYEEALALY-RRAL---ALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLG 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1958792183 1656 CYDKARWVWLTAFENNPQNAEIFYHLCKFFILQNGGDKLLPLLRQFI 1702
Cdd:COG3914    161 RLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRAL 207
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
1352-1539 2.12e-04

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 45.00  E-value: 2.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1352 IANLEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCET 1431
Cdd:COG0457     28 IEDYEKALELDPDDAEALYNLGLAYLRLGR------YEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDK 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1432 AVEYAPDYQSfcTFLHLESTFEE-KDYvcERMVEFLMGAAKRETSDIlsfqllEALLFRVQLHIFTGRCQSALAILQNAL 1510
Cdd:COG0457    102 ALELDPDDAE--ALYNLGLALLElGRY--DEAIEAYERALELDPDDA------DALYNLGIALEKLGRYEEALELLEKLE 171

                          170       180
                   ....*....|....*....|....*....
gi 1958792183 1511 KLANDAIVAEYLRTEDRCLAWLAYIHLIE 1539
Cdd:COG0457    172 AAALAALLAAALGEAALALAAAEVLLALL 200
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 1606-1702 3.32e-04

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 42.87  E-value: 3.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1606 CLPLYTNMMALHQLLERDEEAVELCKSLLESCPTNCQLLETLAALYLKTDCYDKARWVWLTAFENNPQNAEIFYHLCKFF 1685
Cdd:COG4783      3 CAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLAL 82

                           90
                   ....*....|....*..
gi 1958792183 1686 ILQNGGDKLLPLLRQFI 1702
Cdd:COG4783     83 LKAGDYDEALALLEKAL 99
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1613-1725 3.39e-04

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 44.72  E-value: 3.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1613 MMALHQLLERD-EEAVELCKSLLESCPTNCQLLETLAALYLKTDCYDKARWVWLTAFENNPQNAEIFYHLCKFFILQNGG 1691
Cdd:COG2956     13 FKGLNYLLNGQpDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLL 92

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1958792183 1692 DKLLPLLRQFIGsffkpgfEKYSNVDLFRYLLNI 1725
Cdd:COG2956     93 DRAEELLEKLLE-------LDPDDAEALRLLAEI 119
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
1610-1700 4.13e-04

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 44.23  E-value: 4.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1610 YTNMMALHQLLERDEEAVELCKSLLESCPTNCQLLETLAALYLKTDCYDKARWVWLTAFENNPQNAEIFYHLCKFFILQN 1689
Cdd:COG0457     79 LNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLG 158

                           90
                   ....*....|.
gi 1958792183 1690 GGDKLLPLLRQ 1700
Cdd:COG0457    159 RYEEALELLEK 169
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 739-999 4.36e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 45.35  E-value: 4.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  739 LESMIKEARRTAEQASKPKVPPKSEKENDPLRTPEALPEEKKIEYRLLKEEIANREKQRLIK------SDQLKTSSSSPA 812
Cdd:pfam02463  752 EEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEaelleeEQLLIEQEEKIK 831

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  813 NSDVEMDGIGRIAMVTKQVADAEAKLKKHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKLTEQLQAAEKILSVNRM 892
Cdd:pfam02463  832 EEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNL 911

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  893 flkkLQEQIHRVQQRVTIKKALTLKYGEELARAKAVASKElgKRKLEQDRLGPNKMMRLDNSPVSSPRKHSAELIaMEKR 972
Cdd:pfam02463  912 ----LEEKENEIEERIKEEAEILLKYEEEPEELLLEEADE--KEKEENNKEEEEERNKRLLLAKEELGKVNLMAI-EEFE 984

                          250       260
                   ....*....|....*....|....*..
gi 1958792183  973 RLQKLEYEYALKIQKLKEARALKAKEQ 999
Cdd:pfam02463  985 EKEERYNKDELEKERLEEEKKKLIRAI 1011
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
1362-1523 6.08e-04

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 43.84  E-value: 6.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1362 NPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCETAVEYAPDYQS 1441
Cdd:COG0457      4 DPDDAEAYNNLGLAYRRLGR------YEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1442 fcTFLHLESTFEE-KDYvcERMVEFLMGAAKRETSDIlsfqllEALLFRVQLHIFTGRCQSALAILQNALKLANDAIVAE 1520
Cdd:COG0457     78 --ALNNLGLALQAlGRY--EEALEDYDKALELDPDDA------EALYNLGLALLELGRYDEAIEAYERALELDPDDADAL 147


                   ...
gi 1958792183 1521 YLR 1523
Cdd:COG0457    148 YNL 150
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 778-1000 7.59e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 7.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  778 EKKIEYRLLKEEIANREKQRLIKSDQLKTSssspansdvemdgigRIAMVTKQVADAEAKLKKHKILLIKDESVLKNLVL 857
Cdd:COG1196    210 EKAERYRELKEELKELEAELLLLKLRELEA---------------ELEELEAELEELEAELEELEAELAELEAELEELRL 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  858 QEAKKKESVRNAEAKITKLTEQLQAAEKILSVNRMFLKKLQEQIHRVQQRVTIKKALTLKYGEELARAKAVASKELGKRK 937
Cdd:COG1196    275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958792183  938 LEQDRLgpnkmmrldnspvsspRKHSAELIAMEKRRLQKLEYEYALKIQKLKEARALKAKEQQ 1000
Cdd:COG1196    355 EAEAEL----------------AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
PTZ00121 PTZ00121
MAEBL; Provisional
 745-1009 1.08e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  745 EARRTAEQASKPKVPPKSEKENdplRTPEALPEEKKIEYRLLKEEIANRekqrliKSDQLKTSSSSPANSDVEMDGIGRI 824
Cdd:PTZ00121  1333 AAKKKAEEAKKAAEAAKAEAEA---AADEAEAAEEKAEAAEKKKEEAKK------KADAAKKKAEEKKKADEAKKKAEED 1403

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  825 AMVTKQVADAEAKLKKHKILLIKDESVLKnlvLQEAKKK-ESVRNAEAKITKLTEQLQAAEKILSVNRMflKKLQEQIHR 903
Cdd:PTZ00121  1404 KKKADELKKAAAAKKKADEAKKKAEEKKK---ADEAKKKaEEAKKADEAKKKAEEAKKAEEAKKKAEEA--KKADEAKKK 1478

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  904 VQQRvtiKKALTLKYGEELARAKA--VASKELGKRKLEQDRLGPNKMMRLDNSPVSSPRKHSAELIAMEKRRLQKL---- 977
Cdd:PTZ00121  1479 AEEA---KKADEAKKKAEEAKKKAdeAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELkkae 1555

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1958792183  978 EYEYALKIQKLKEARalKAKEQQNLVPVVEEE 1009
Cdd:PTZ00121  1556 ELKKAEEKKKAEEAK--KAEEDKNMALRKAEE 1585
PTZ00121 PTZ00121
MAEBL; Provisional
 743-1011 1.31e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  743 IKEARRTAEQASKPKVPPKSEKENDplRTPEALpeEKKIEYRLLKEEIANREKQRliKSDQLKTSSSSPANSDVEMDGIG 822
Cdd:PTZ00121  1304 ADEAKKKAEEAKKADEAKKKAEEAK--KKADAA--KKKAEEAKKAAEAAKAEAEA--AADEAEAAEEKAEAAEKKKEEAK 1377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  823 RIAMVTKQVADA-----EAKLK----KHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKLTEQLQAAEkilsvnrmf 893
Cdd:PTZ00121  1378 KKADAAKKKAEEkkkadEAKKKaeedKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADE--------- 1448

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  894 LKKLQEQIHRVQQrvTIKKALTLKYGEELARAKAVASK--------ELGKRKLEQDRLGPNKMMRLDNSPVSSPRKHSAE 965
Cdd:PTZ00121  1449 AKKKAEEAKKAEE--AKKKAEEAKKADEAKKKAEEAKKadeakkkaEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1958792183  966 L-IAMEKRRLQKL-EYEYALKIQKLKEARALKAKEQQNLVPVVEEEPE 1011
Cdd:PTZ00121  1527 AkKAEEAKKADEAkKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEE 1574
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
1616-1702 1.43e-03

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 39.77  E-value: 1.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1616 LHQLLERDEEAVELCKSLLESCPTNCQLLETLAALYLKTDCYDKARwVWLTAFENNPQNAEIFYHLCKFFILQNGGDKLL 1695
Cdd:COG3063      1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAI-ALEKALKLDPNNAEALLNLAELLLELGDYDEAL 79


                   ....*..
gi 1958792183 1696 PLLRQFI 1702
Cdd:COG3063     80 AYLERAL 86
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 1366-1515 2.00e-03

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 40.56  E-value: 2.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1366 VQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCETAVEYAPDYQSFCTF 1445
Cdd:COG4783      4 AEALYALAQALLLAGD------YDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLN 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1446 LhLESTFEEKDYvcERMVEFLMGAAKRETSDILSFQLLEALLFRvqlhifTGRCQSALAILQNALKLAND 1515
Cdd:COG4783     78 L-GLALLKAGDY--DEALALLEKALKLDPEHPEAYLRLARAYRA------LGRPDEAIAALEKALELDPD 138
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 1353-1539 2.24e-03

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 43.06  E-value: 2.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1353 ANLEASVLENPSHVQLWLKLAYKYLNQNEglcseSLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKEEVQEMCETA 1432
Cdd:COG3914     64 AGEAAAAAAALLLLAALLELAALLLQALG-----RYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRA 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1433 VEYAPDYQSFCTFLhLESTFEEKDYvcERMVEFLMGAAKRETSDILSFQLLEALLFRvqlhifTGRCQSALAILQNALKL 1512
Cdd:COG3914    139 LALNPDFAEAYLNL-GEALRRLGRL--EEAIAALRRALELDPDNAEALNNLGNALQD------LGRLEEAIAAYRRALEL 209

                          170       180
                   ....*....|....*....|....*....
gi 1958792183 1513 A--NDAIVAEYLRTEDRCLAWLAYIHLIE 1539
Cdd:COG3914    210 DpdNADAHSNLLFALRQACDWEVYDRFEE 238
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 1620-1681 2.61e-03

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 40.18  E-value: 2.61e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958792183 1620 LERDEEAVELCKSLLESCPTNCQLLETLAALYLKTDCYDKARWVWLTAFENNPQNAEIFYHL 1681
Cdd:COG4783     51 LGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRL 112
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 1509-1672 3.10e-03

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 40.33  E-value: 3.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1509 ALKLANDAIVAEYLRTEDRCLAWLAYIHLIEFNSLPSKLYDPSNANPSRIVNTEPFVMPWQAAQDVKTNPDLLLAVFEDA 1588
Cdd:COG5010      1 ARALEGFDRLPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1589 VKACTDEAltsgertevclPLYTNMMALHQLLERDEEAVELCKSLLESCPTNCQLLETLAALYLKTDCYDKARWVWLTAF 1668
Cdd:COG5010     81 LQLDPNNP-----------ELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRAL 149


                   ....
gi 1958792183 1669 ENNP 1672
Cdd:COG5010    150 GTSP 153
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
1610-1681 3.33e-03

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 41.53  E-value: 3.33e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958792183 1610 YTNMMALHQLLERDEEAVELCKSLLESCPTNCQLLETLAALYLKTDCYDKARWVWLTAFENNPQNAEIFYHL 1681
Cdd:COG0457     11 YNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNL 82
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 821-1000 3.36e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 42.65  E-value: 3.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  821 IGRIAMVTKQVADAEAKLKKHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKLTEQLQAAEKILSVNRMF------- 893
Cdd:TIGR00618  299 IKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREIScqqhtlt 378

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  894 --LKKLQEQIHRVQQRVTIKKALTLKYGEELARAKAVASKElgkRKLEQDRLGPNKMMRLDNSPVSSPRKHSAELIA--- 968
Cdd:TIGR00618  379 qhIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAF---RDLQGQLAHAKKQQELQQRYAELCAAAITCTAQcek 455

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1958792183  969 MEKRRLQKLEYEYALKIQKLKEARALKAKEQQ 1000
Cdd:TIGR00618  456 LEKIHLQESAQSLKEREQQLQTKEQIHLQETR 487
TPR_19 pfam14559
Tetratricopeptide repeat;
1352-1409 5.72e-03

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 37.18  E-value: 5.72e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958792183 1352 IANLEASVLENPSHVQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIW 1409
Cdd:pfam14559    8 LELLEQALAEDPDNAEARLGLAEALLALGR------LDEAEALLAALPAADPDDPRYA 59
TPR_14 pfam13428
Tetratricopeptide repeat;
1366-1415 6.01e-03

Tetratricopeptide repeat;


Pssm-ID: 463874 [Multi-domain]  Cd Length: 44  Bit Score: 36.63  E-value: 6.01e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1366 VQLWLKLAYKYLNQNEglcsesLDSALNVLARALENNKDNPEIWCHYLRL 1415
Cdd:pfam13428    1 PEALLALARALLALGD------PDEALALLERALALDPDDPEAWLALAQL 44
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 1569-1676 6.22e-03

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 38.83  E-value: 6.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183 1569 QAAQDVKTNPD-----LLLAV-------FEDAVKACtDEALT-SGERTEVclplYTNMMALHQLLERDEEAVELCKSLLE 1635
Cdd:COG4235      5 RLRQALAANPNdaegwLLLGRaylrlgrYDEALAAY-EKALRlDPDNADA----LLDLAEALLAAGDTEEAEELLERALA 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1958792183 1636 SCPTNCQLLETLAALYLKTDCYDKARWVWLTAFENNPQNAE 1676
Cdd:COG4235     80 LDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPADAP 120
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 1619-1672 7.53e-03

Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 (ACL4) acts as a chaperone for the L4 ribosomal subunit, encoded by RPL4A and RPL4B, and is required for hierarchical ribosome assembly. It is required for the soluble expression of newly synthesized RPL4 and for the protection of RPL4 from the Tom1-dependent cellular degradation machinery. ACL4 shields ribosomal protein L4 until timely release and insertion into the pre-ribosome is possible, once ribosomal protein L18 is present.


Pssm-ID: 467942 [Multi-domain]  Cd Length: 306  Bit Score: 40.69  E-value: 7.53e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958792183 1619 LLERD--EEAVELCKSLLESCPTNCQLLETLAALYLKTDCYDKARWVWLTAFENNP 1672
Cdd:cd24142     10 LLDQGnfELALKFLQRALELEPNNVEALELLGEILLELGDVEEAREVLLRAIELDP 65
PRK12704 PRK12704
phosphodiesterase; Provisional
 740-927 8.17e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 8.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  740 ESMIKEARRTAEQASKpkvppksekendplrtpEALPEEKKiEYRLLKEEIANREKQRLIKSDQLKtsssspansdvemd 819
Cdd:PRK12704    41 KRILEEAKKEAEAIKK-----------------EALLEAKE-EIHKLRNEFEKELRERRNELQKLE-------------- 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  820 gigriamvtKQVADAEAKLKKHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKL-TEQLQAAEKILSVNR-----MF 893
Cdd:PRK12704    89 ---------KRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELiEEQLQELERISGLTAeeakeIL 159

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1958792183  894 LKKLQEQIhRVQQRVTIKKAltlkygEELARAKA 927
Cdd:PRK12704   160 LEKVEEEA-RHEAAVLIKEI------EEEAKEEA 186
PTZ00121 PTZ00121
MAEBL; Provisional
 744-956 8.93e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 8.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  744 KEARRTAEQASKPKVPPKSEKENDPLRTPEALPEEKKIEyrllKEEIANREKQRLIKSDQLKTSSSSPANSdvemdgigr 823
Cdd:PTZ00121  1610 EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK----AEELKKAEEENKIKAAEEAKKAEEDKKK--------- 1676

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  824 iamvTKQVADAEAKLKKHKILLIKDEsvlknlvlQEAKKKESVRNAEAKITKLTEQLQAAEKILSVNRMFLKKLQEQIHR 903
Cdd:PTZ00121  1677 ----AEEAKKAEEDEKKAAEALKKEA--------EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK 1744

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958792183  904 V----------QQRVTIKKALTLKYGEELARAKAVASKELGKRKLEQDRLGPNKMMR--LDNSPV 956
Cdd:PTZ00121  1745 KaeeakkdeeeKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKdiFDNFAN 1809
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 836-994 9.57e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.11  E-value: 9.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  836 AKLKKHKILLIKDESVLKNLVLQEAKKKESVRNAEAKITKLTE-QLQAAEKILSVNRMFLKKLQEQIHRVQQRVT----- 909
Cdd:TIGR00618  559 ASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEkLSEAEDMLACEQHALLRKLQPEQDLQDVRLHlqqcs 638

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792183  910 --IKKALTLKYGEELA------RAKAVASKELGKRKLEQDRLGPNKM--------------------MRLDNSPVSSPRK 961
Cdd:TIGR00618  639 qeLALKLTALHALQLTltqervREHALSIRVLPKELLASRQLALQKMqsekeqltywkemlaqcqtlLRELETHIEEYDR 718

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1958792183  962 HSAELIAMEKRRLQKLEYEYALKIQKLKEARAL 994
Cdd:TIGR00618  719 EFNEIENASSSLGSDLAAREDALNQSLKELMHQ 751
 
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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