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Conserved domains on  [gi|87116683|ref|NP_659419|]
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zinc finger C3H1 domain-containing protein [Homo sapiens]

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 ...
 1364-1695 5.62e-11

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: 65.52  E-value: 5.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1364 WLKLAYKYLNQNEgecsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKDEVQEMCETAVEYAPdyQSFWTFLHL 1443
Cdd:COG2956   11 WYFKGLNYLLNGQ------PDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDP--DRAEALLEL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1444 -ESTFEEKDYvcERMLEFLMGAAKQETSNIlsfqllEALLFRVQLHIFTGRCQSALAILQNALKSANDGIVAEYLktsdr 1522
Cdd:COG2956   83 aQDYLKAGLL--DRAEELLEKLLELDPDDA------EALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCE----- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1523 clawLAYIHLIefnilpskfydpsndnpsrivntesfvmpwqavqdvKTNPDMLLAVFEDAVKACtdeslaveeriEACL 1602
Cdd:COG2956  150 ----LAELYLE------------------------------------QGDYDEAIEALEKALKLD-----------PDCA 178

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1603 PLYTNMIALHQLLERYEAAMELCKSLLESCPINCQLLEALVALYLQTNQHDKARAVWLTAFEKNPQNAEVFYhMCKFFIL 1682
Cdd:COG2956  179 RALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLA-LADLLER 257

                        330
                 ....*....|...
gi 87116683 1683 QNRGDNLLPFLRK 1695
Cdd:COG2956  258 KEGLEAALALLER 270
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 823-998 1.70e-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: 52.46  E-value: 1.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683  823 TKQVTDAESKLKKHRILLMKDESVLKNLVQQEAKKKESVRNAEAKITKLTEQLQATEKILNVNRMFLKKLQEQIHRVQQR 902
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683  903 VTIKKALtlkYGEELARAKAVASKEIGKRKLEQDRFGPNKMMRLDSSPVSSPRKHSAELIAMEKRRLQKLEYEYALKIQK 982
Cdd:COG4942   99 LEAQKEE---LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175

                        170
                 ....*....|....*.
gi 87116683  983 LKEARALKAKEQQNIS 998
Cdd:COG4942  176 LEALLAELEEERAALE 191
zf-C3H1 pfam10650
Putative zinc-finger domain; This domain is conserved in fungi and might be a zinc-finger ...
 1185-1204 5.27e-06

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: 44.49  E-value: 5.27e-06
                           10        20
                   ....*....|....*....|.
gi 87116683   1185 FCRFDLTG-TCNDDDCQWQHI 1204
Cdd:pfam10650    1 LCPYELAGgVCNDPSCEFQHF 21
Granin super family cl27033
Granin (chromogranin or secretogranin);
220-438 6.30e-05

Granin (chromogranin or secretogranin);


The actual alignment was detected with superfamily member pfam01271:

Pssm-ID: 279595 [Multi-domain]  Cd Length: 584  Bit Score: 48.10  E-value: 6.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    220 CVEETFEDLLLKYKQIQLELECINKDEKL------ALSSKEENVQEDPKTLnfEDQTSTDNVSITKDSSKEVAPEEKTQV 293
Cdd:pfam01271   11 CIIEVLSNALSKSSPPPITPECLEVLKKGrkriksEERSENYNPYFEVRLL--RDLADQSEASHLSSRSRDGLSDEDMQI 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    294 KTfqafelKPLRQKLTLPGDKNRLKKVKDGAKPLSLKSDTTDSSQGLQDKEQNLT--RRISTSDILSEKKLGEDEEELSE 371
Cdd:pfam01271   89 IT------EALRQAENEPGGHSRENQPYALQVEKEFKTDHSDDYETQQWEEEKLKhmRFPLRYEENSEEKHSEREGELSE 162

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 87116683    372 LQLrllalqsaskkwqQKEQQVMKESKEKLTKTKTVQQKVKTStKTHSAKKVSTTAKQALRKQQTKA 438
Cdd:pfam01271  163 VFE-------------NPRSQATLKKVFEEVSRLDTPSKQKRE-KSDEREKSSQESGEDTYRQENIP 215
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 244-1119 3.67e-03

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: 42.65  E-value: 3.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    244 KDEKLALSSKEENVQEDPKTLNFEDQTSTDNVSITKDSSKEVAPEEKTQVKTFQAFELKPLRQKLTLPGDKNRLKKvkdg 323
Cdd:pfam02463  168 KRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ---- 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    324 aKPLSLKSDTTDSSQGLQDKEQNLTRRISTSDILSEKKLGEDEEELSEL---------QLRLLALQSASKKWQQKEQQVM 394
Cdd:pfam02463  244 -ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLakeeeelksELLKLERRKVDDEEKLKESEKE 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    395 KESKEK-LTKTKTVQQKVKTSTKTHSAKKVS-TTAKQALRKQQTKAWKKLQQQKEQERQKEEDQRKQAEEEERRKREEEI 472
Cdd:pfam02463  323 KKKAEKeLKKEKEEIEELEKELKELEIKREAeEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE 402

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    473 RKIRDLSNQEEQYNRFM-KLVGGKRRSRSKSSDPDLRRSLDKQPTDSGGGIYQYDNYEEVAMDTDSETSSPAPSpvqppf 551
Cdd:pfam02463  403 EEKEAQLLLELARQLEDlLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKE------ 476

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    552 fSECSLGYFSPAPSLSLPPPPQVSSLPPLSQPYVEGLCVSLEPLPPLPPLPPLPPEDPEQPPKPPFADEEEEEEMLLREE 631
Cdd:pfam02463  477 -TQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSA 555

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    632 LLKSLANKRAFKPEETSSNSDPPSPPVLNNSHPVPRSNLSIVSINtvsqPRIQNPKFHRGPRLPRTVISLPKHKSVVVTL 711
Cdd:pfam02463  556 TADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEID----PILNLAQLDKATLEADEDDKRAKVVEGILKD 631

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    712 NDSDDSESDGEASKSTNSVFGGLESMIKEARRTAEQASKPKVPPKSEKENDPLRTPEALPEEKKIEyRLLKEEIANREKQ 791
Cdd:pfam02463  632 TELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRR-QLEIKKKEQREKE 710

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    792 RLIKSDQLKTSSSSPANSDVEIDGIGRIAMVTKQVTDAESKLKKHRILLMKDESVLKNLVQQEAKKKESVRNAE--AKIT 869
Cdd:pfam02463  711 ELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEklKVEE 790

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    870 KLTEQLQATEKILNVNRMFLKKLQEQIHRVQQRVTIKKALTLKYGEELArAKAVASKEIGKRKLEQDRFGPNKMMRLDSS 949
Cdd:pfam02463  791 EKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELA-LELKEEQKLEKLAEEELERLEEEITKEELL 869

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    950 PVSSPRKHSAELIAMEKRRLQKLEYEYALKIQKLKEARalkAKEQQNISPVVEEEPEFSLPQPSLHDLTQDKLTLDTEEN 1029
Cdd:pfam02463  870 QELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQ---KLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEAD 946

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683   1030 DVDDEILSGSSRERRRSFLESNYFTKPNLKhtdtankeciNKLNKNTVEKPELFLGLKIgELQKLYSKADSLKQLILKTT 1109
Cdd:pfam02463  947 EKEKEENNKEEEEERNKRLLLAKEELGKVN----------LMAIEEFEEKEERYNKDEL-EKERLEEEKKKLIRAIIEET 1015

                          890
                   ....*....|
gi 87116683   1110 TGITEKVLHG 1119
Cdd:pfam02463 1016 CQRLKEFLEL 1025
 
Name Accession Description Interval E-value
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1364-1695 5.62e-11

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: 65.52  E-value: 5.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1364 WLKLAYKYLNQNEgecsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKDEVQEMCETAVEYAPdyQSFWTFLHL 1443
Cdd:COG2956   11 WYFKGLNYLLNGQ------PDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDP--DRAEALLEL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1444 -ESTFEEKDYvcERMLEFLMGAAKQETSNIlsfqllEALLFRVQLHIFTGRCQSALAILQNALKSANDGIVAEYLktsdr 1522
Cdd:COG2956   83 aQDYLKAGLL--DRAEELLEKLLELDPDDA------EALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCE----- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1523 clawLAYIHLIefnilpskfydpsndnpsrivntesfvmpwqavqdvKTNPDMLLAVFEDAVKACtdeslaveeriEACL 1602
Cdd:COG2956  150 ----LAELYLE------------------------------------QGDYDEAIEALEKALKLD-----------PDCA 178

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1603 PLYTNMIALHQLLERYEAAMELCKSLLESCPINCQLLEALVALYLQTNQHDKARAVWLTAFEKNPQNAEVFYhMCKFFIL 1682
Cdd:COG2956  179 RALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLA-LADLLER 257

                        330
                 ....*....|...
gi 87116683 1683 QNRGDNLLPFLRK 1695
Cdd:COG2956  258 KEGLEAALALLER 270
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 823-998 1.70e-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: 52.46  E-value: 1.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683  823 TKQVTDAESKLKKHRILLMKDESVLKNLVQQEAKKKESVRNAEAKITKLTEQLQATEKILNVNRMFLKKLQEQIHRVQQR 902
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683  903 VTIKKALtlkYGEELARAKAVASKEIGKRKLEQDRFGPNKMMRLDSSPVSSPRKHSAELIAMEKRRLQKLEYEYALKIQK 982
Cdd:COG4942   99 LEAQKEE---LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175

                        170
                 ....*....|....*.
gi 87116683  983 LKEARALKAKEQQNIS 998
Cdd:COG4942  176 LEALLAELEEERAALE 191
zf-C3H1 pfam10650
Putative zinc-finger domain; This domain is conserved in fungi and might be a zinc-finger ...
 1185-1204 5.27e-06

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: 44.49  E-value: 5.27e-06
                           10        20
                   ....*....|....*....|.
gi 87116683   1185 FCRFDLTG-TCNDDDCQWQHI 1204
Cdd:pfam10650    1 LCPYELAGgVCNDPSCEFQHF 21
PTZ00121 PTZ00121
MAEBL; Provisional
 740-1029 3.99e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 3.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683   740 EARRTAEQASKpkvppKSEKENDPLRTPEalpEEKKIEYRLLKEEIANREKQRLIKSDQLKTSSSSPANSDveidgigri 819
Cdd:PTZ00121 1561 EEKKKAEEAKK-----AEEDKNMALRKAE---EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE--------- 1623

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683   820 amvtkQVTDAESKLKKHRILLMKDEsvlknlvqQEAKKKESVRNAE--AKITKLTEQLQATEKilnvnrmflKKLQEQIH 897
Cdd:PTZ00121 1624 -----ELKKAEEEKKKVEQLKKKEA--------EEKKKAEELKKAEeeNKIKAAEEAKKAEED---------KKKAEEAK 1681

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683   898 RVQQRVTIKKALTLKYGEELARAKAVASKEI-GKRKLEQDRfgpnKMMRLDSSPVSSPRKHSAEliamEKRRLQ--KLEY 974
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEEAKKAEELKKKEAeEKKKAEELK----KAEEENKIKAEEAKKEAEE----DKKKAEeaKKDE 1753

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 87116683   975 EYALKIQKLKEARALKAKE-QQNISPVVEEEPEfslPQPSLHDLTQDKLTLDTEEN 1029
Cdd:PTZ00121 1754 EEKKKIAHLKKEEEKKAEEiRKEKEAVIEEELD---EEDEKRRMEVDKKIKDIFDN 1806
Granin pfam01271
Granin (chromogranin or secretogranin);
220-438 6.30e-05

Granin (chromogranin or secretogranin);


Pssm-ID: 279595 [Multi-domain]  Cd Length: 584  Bit Score: 48.10  E-value: 6.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    220 CVEETFEDLLLKYKQIQLELECINKDEKL------ALSSKEENVQEDPKTLnfEDQTSTDNVSITKDSSKEVAPEEKTQV 293
Cdd:pfam01271   11 CIIEVLSNALSKSSPPPITPECLEVLKKGrkriksEERSENYNPYFEVRLL--RDLADQSEASHLSSRSRDGLSDEDMQI 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    294 KTfqafelKPLRQKLTLPGDKNRLKKVKDGAKPLSLKSDTTDSSQGLQDKEQNLT--RRISTSDILSEKKLGEDEEELSE 371
Cdd:pfam01271   89 IT------EALRQAENEPGGHSRENQPYALQVEKEFKTDHSDDYETQQWEEEKLKhmRFPLRYEENSEEKHSEREGELSE 162

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 87116683    372 LQLrllalqsaskkwqQKEQQVMKESKEKLTKTKTVQQKVKTStKTHSAKKVSTTAKQALRKQQTKA 438
Cdd:pfam01271  163 VFE-------------NPRSQATLKKVFEEVSRLDTPSKQKRE-KSDEREKSSQESGEDTYRQENIP 215
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 734-1006 1.85e-04

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: 46.59  E-value: 1.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    734 LESMIKEARRTAEQASKpkvppKSEKENDPLRTPEALPEEKKIEYRLLKEEIANREKQRLIKSDQLKTSSSSPANSDVEI 813
Cdd:TIGR02168  710 LEEELEQLRKELEELSR-----QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    814 --------DGIGRIAMVTKQVTDAESKLKKHRILLMKDESVLKNLVQQEAKKKESVRNAEAKITKLTEQLQATEKILNVN 885
Cdd:TIGR02168  785 eeleaqieQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    886 RMFLKKLQEQIhrvqqrvtiKKALTLKYGEELARAKAVASKEIGKRKLEQDRfgpNKMMRLDSSpvsspRKHSAELIAME 965
Cdd:TIGR02168  865 EELIEELESEL---------EALLNERASLEEALALLRSELEELSEELRELE---SKRSELRRE-----LEELREKLAQL 927

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 87116683    966 KRRLQKLEYEYALKIQKLKEARALKAKEQQNISPVVEEEPE 1006
Cdd:TIGR02168  928 ELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEE 968
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 1617-1667 6.77e-04

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: 43.77  E-value: 6.77e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 87116683 1617 RYEAAMELCKSLLESCPINCQLLEALVALYLQTNQHDKARAVWLTAFEKNP 1667
Cdd:cd24142   15 NFELALKFLQRALELEPNNVEALELLGEILLELGDVEEAREVLLRAIELDP 65
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 757-973 2.21e-03

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 42.89  E-value: 2.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    757 SEKEndplRTPEALPEEKKIEYRLLKEEIANREKQ-----------RLIKSDQ------LKTSSSSPANSDVEIDGIGR- 818
Cdd:pfam10174  446 SEKE----RIIERLKEQREREDRERLEELESLKKEnkdlkekvsalQPELTEKesslidLKEHASSLASSGLKKDSKLKs 521

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    819 --IAMVTK--QVTDAESKLKK-HRILL---MKDESV--LKNLVQQEAKKKESVRNAEAKITKLTEQLQATE--------K 880
Cdd:pfam10174  522 leIAVEQKkeECSKLENQLKKaHNAEEavrTNPEINdrIRLLEQEVARYKEESGKAQAEVERLLGILREVEnekndkdkK 601

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    881 ILNVNRMFLKKLQEQihrvqqrvtIKKALTLKYGEELARAKAVASKEIGKRkleqdrfgpnkmmRLDSSPVSSPRKHSAE 960
Cdd:pfam10174  602 IAELESLTLRQMKEQ---------NKKVANIKHGQQEMKKKGAQLLEEARR-------------REDNLADNSQQLQLEE 659

                          250
                   ....*....|....
gi 87116683    961 LI-AMEKRRlQKLE 973
Cdd:pfam10174  660 LMgALEKTR-QELD 672
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 244-1119 3.67e-03

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: 42.65  E-value: 3.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    244 KDEKLALSSKEENVQEDPKTLNFEDQTSTDNVSITKDSSKEVAPEEKTQVKTFQAFELKPLRQKLTLPGDKNRLKKvkdg 323
Cdd:pfam02463  168 KRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ---- 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    324 aKPLSLKSDTTDSSQGLQDKEQNLTRRISTSDILSEKKLGEDEEELSEL---------QLRLLALQSASKKWQQKEQQVM 394
Cdd:pfam02463  244 -ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLakeeeelksELLKLERRKVDDEEKLKESEKE 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    395 KESKEK-LTKTKTVQQKVKTSTKTHSAKKVS-TTAKQALRKQQTKAWKKLQQQKEQERQKEEDQRKQAEEEERRKREEEI 472
Cdd:pfam02463  323 KKKAEKeLKKEKEEIEELEKELKELEIKREAeEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE 402

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    473 RKIRDLSNQEEQYNRFM-KLVGGKRRSRSKSSDPDLRRSLDKQPTDSGGGIYQYDNYEEVAMDTDSETSSPAPSpvqppf 551
Cdd:pfam02463  403 EEKEAQLLLELARQLEDlLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKE------ 476

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    552 fSECSLGYFSPAPSLSLPPPPQVSSLPPLSQPYVEGLCVSLEPLPPLPPLPPLPPEDPEQPPKPPFADEEEEEEMLLREE 631
Cdd:pfam02463  477 -TQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSA 555

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    632 LLKSLANKRAFKPEETSSNSDPPSPPVLNNSHPVPRSNLSIVSINtvsqPRIQNPKFHRGPRLPRTVISLPKHKSVVVTL 711
Cdd:pfam02463  556 TADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEID----PILNLAQLDKATLEADEDDKRAKVVEGILKD 631

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    712 NDSDDSESDGEASKSTNSVFGGLESMIKEARRTAEQASKPKVPPKSEKENDPLRTPEALPEEKKIEyRLLKEEIANREKQ 791
Cdd:pfam02463  632 TELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRR-QLEIKKKEQREKE 710

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    792 RLIKSDQLKTSSSSPANSDVEIDGIGRIAMVTKQVTDAESKLKKHRILLMKDESVLKNLVQQEAKKKESVRNAE--AKIT 869
Cdd:pfam02463  711 ELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEklKVEE 790

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    870 KLTEQLQATEKILNVNRMFLKKLQEQIHRVQQRVTIKKALTLKYGEELArAKAVASKEIGKRKLEQDRFGPNKMMRLDSS 949
Cdd:pfam02463  791 EKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELA-LELKEEQKLEKLAEEELERLEEEITKEELL 869

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    950 PVSSPRKHSAELIAMEKRRLQKLEYEYALKIQKLKEARalkAKEQQNISPVVEEEPEFSLPQPSLHDLTQDKLTLDTEEN 1029
Cdd:pfam02463  870 QELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQ---KLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEAD 946

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683   1030 DVDDEILSGSSRERRRSFLESNYFTKPNLKhtdtankeciNKLNKNTVEKPELFLGLKIgELQKLYSKADSLKQLILKTT 1109
Cdd:pfam02463  947 EKEKEENNKEEEEERNKRLLLAKEELGKVN----------LMAIEEFEEKEERYNKDEL-EKERLEEEKKKLIRAIIEET 1015

                          890
                   ....*....|
gi 87116683   1110 TGITEKVLHG 1119
Cdd:pfam02463 1016 CQRLKEFLEL 1025
TPR_14 pfam13428
Tetratricopeptide repeat;
1361-1410 3.73e-03

Tetratricopeptide repeat;


Pssm-ID: 463874 [Multi-domain]  Cd Length: 44  Bit Score: 37.02  E-value: 3.73e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 87116683   1361 VQLWLKLAYKYLNQNEgecsesLDSALNVLARALENNKDNPEIWCHYLRL 1410
Cdd:pfam13428    1 PEALLALARALLALGD------PDEALALLERALALDPDDPEAWLALAQL 44
 
Name Accession Description Interval E-value
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1364-1695 5.62e-11

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: 65.52  E-value: 5.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1364 WLKLAYKYLNQNEgecsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKDEVQEMCETAVEYAPdyQSFWTFLHL 1443
Cdd:COG2956   11 WYFKGLNYLLNGQ------PDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDP--DRAEALLEL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1444 -ESTFEEKDYvcERMLEFLMGAAKQETSNIlsfqllEALLFRVQLHIFTGRCQSALAILQNALKSANDGIVAEYLktsdr 1522
Cdd:COG2956   83 aQDYLKAGLL--DRAEELLEKLLELDPDDA------EALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCE----- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1523 clawLAYIHLIefnilpskfydpsndnpsrivntesfvmpwqavqdvKTNPDMLLAVFEDAVKACtdeslaveeriEACL 1602
Cdd:COG2956  150 ----LAELYLE------------------------------------QGDYDEAIEALEKALKLD-----------PDCA 178

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1603 PLYTNMIALHQLLERYEAAMELCKSLLESCPINCQLLEALVALYLQTNQHDKARAVWLTAFEKNPQNAEVFYhMCKFFIL 1682
Cdd:COG2956  179 RALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLA-LADLLER 257

                        330
                 ....*....|...
gi 87116683 1683 QNRGDNLLPFLRK 1695
Cdd:COG2956  258 KEGLEAALALLER 270
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 1347-1441 7.11e-11

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: 61.56  E-value: 7.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1347 IANLEASVLENPSHVQLWLKLAYKYLNQNEgecsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKDEVQEMCET 1426
Cdd:COG4235    3 IARLRQALAANPNDAEGWLLLGRAYLRLGR------YDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLER 76

                         90
                 ....*....|....*
gi 87116683 1427 AVEYAPDYQSFWTFL 1441
Cdd:COG4235   77 ALALDPDNPEALYLL 91
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1347-1666 1.65e-08

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: 57.82  E-value: 1.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1347 IANLEASVLENPSHVQLWLKLAYKYLNQNEgecsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKDEVQEMCET 1426
Cdd:COG2956   28 IDLLEEALELDPETVEAHLALGNLYRRRGE------YDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1427 AVEYAPDYQSFWTFLhLESTFEEKDYvcERMLEFLMGAAKQETSNIlsfqllEALLFRVQLHIFTGRCQSALAILQNALK 1506
Cdd:COG2956  102 LLELDPDDAEALRLL-AEIYEQEGDW--EKAIEVLERLLKLGPENA------HAYCELAELYLEQGDYDEAIEALEKALK 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1507 SANDGIVAEYLktsdrclawLAYIHLIEFNilpskfydpsndnpsrivntesfvmpwqavqdvktnpdmllavFEDAVKA 1586
Cdd:COG2956  173 LDPDCARALLL---------LAELYLEQGD-------------------------------------------YEEAIAA 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1587 CtdesLAVEERIEACLPLYTNMIALHQLLERYEAAMELCKSLLESCPINCQLLeALVALYLQTNQHDKARAVWLTAFEKN 1666
Cdd:COG2956  201 L----ERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLL-ALADLLERKEGLEAALALLERQLRRH 275
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 1599-1698 1.71e-07

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: 52.12  E-value: 1.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1599 EACLPLYTNMIALHQLLERYEAAMELCKSLLESCPINCQLLEALVALYLQTNQHDKARAVWLTAFEKNPQNAEVFYHMCK 1678
Cdd:COG4783    1 AACAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGL 80

                         90       100
                 ....*....|....*....|
gi 87116683 1679 FFILQNRGDNLLPFLRKFIA 1698
Cdd:COG4783   81 ALLKAGDYDEALALLEKALK 100
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1605-1698 7.29e-07

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: 52.81  E-value: 7.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1605 YTNMIALHQLLERYEAAMELCKSLLESCPINCQLLEALVALYLQTNQHDKARAVWLTAFEKNPQNAEVFYHMCKFFILQN 1684
Cdd:COG2956  113 LRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQG 192

                         90
                 ....*....|....
gi 87116683 1685 RGDNLLPFLRKFIA 1698
Cdd:COG2956  193 DYEEAIAALERALE 206
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1572-1698 1.35e-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: 52.04  E-value: 1.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1572 NPDMLLAVFEDAVKACTDEslaveerieacLPLYTNMIALHQLLERYEAAMELCKSLLESCPINCQLLEALVALYLQTNQ 1651
Cdd:COG2956   23 QPDKAIDLLEEALELDPET-----------VEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGL 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 87116683 1652 HDKARAVWLTAFEKNPQNAEVFYHMCKFFILQNRGDNLLPFLRKFIA 1698
Cdd:COG2956   92 LDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLK 138
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 1563-1699 1.60e-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: 49.96  E-value: 1.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1563 WQAVQDVKTNPDMLLAVFEDAVKACTDESLAVEERIEACLPLYTNMIALHQLLERYEAAMELCKSLLESCPINCQLLEAL 1642
Cdd:COG5010   15 LLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNL 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 87116683 1643 VALYLQTNQHDKARAVWLTAFEKNPQNAEVFYHMCKFFILQNRGDNLLPFLRKFIAS 1699
Cdd:COG5010   95 ALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGT 151
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 823-998 1.70e-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: 52.46  E-value: 1.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683  823 TKQVTDAESKLKKHRILLMKDESVLKNLVQQEAKKKESVRNAEAKITKLTEQLQATEKILNVNRMFLKKLQEQIHRVQQR 902
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683  903 VTIKKALtlkYGEELARAKAVASKEIGKRKLEQDRFGPNKMMRLDSSPVSSPRKHSAELIAMEKRRLQKLEYEYALKIQK 982
Cdd:COG4942   99 LEAQKEE---LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175

                        170
                 ....*....|....*.
gi 87116683  983 LKEARALKAKEQQNIS 998
Cdd:COG4942  176 LEALLAELEEERAALE 191
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
1580-1718 1.70e-06

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 51.55  E-value: 1.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1580 FEDAVKACtDESLAVEERIeacLPLYTNMIALHQLLERYEAAMELCKSLLESCPINCQLLEALVALYLQTNQHDKARAVW 1659
Cdd:COG0457   24 YEEAIEDY-EKALELDPDD---AEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDY 99

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1660 LTAFEKNPQNAEVFYHMCKFFILQNRGDNLLPFLRKFIAsfFKPGFEK-YNNLDLFRYLL 1718
Cdd:COG0457  100 DKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALE--LDPDDADaLYNLGIALEKL 157
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 1336-1434 1.99e-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: 49.03  E-value: 1.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1336 DVRYFTNETDD-IANLEASVLENPSHVQLWLKLAYKYLNQNEgecsesLDSALNVLARALENNKDNPEIWCHYLRLFSKR 1414
Cdd:COG4783   46 EILLQLGDLDEaIVLLHEALELDPDEPEARLNLGLALLKAGD------YDEALALLEKALKLDPEHPEAYLRLARAYRAL 119

                         90       100
                 ....*....|....*....|
gi 87116683 1415 GTKDEVQEMCETAVEYAPDY 1434
Cdd:COG4783  120 GRPDEAIAALEKALELDPDD 139
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
1347-1441 3.95e-06

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 50.39  E-value: 3.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1347 IANLEASVLENPSHVQLWLKLAYKYLNQNEgecsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKDEVQEMCET 1426
Cdd:COG0457   62 LADYEQALELDPDDAEALNNLGLALQALGR------YEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYER 135

                         90
                 ....*....|....*
gi 87116683 1427 AVEYAPDYQSFWTFL 1441
Cdd:COG0457  136 ALELDPDDADALYNL 150
zf-C3H1 pfam10650
Putative zinc-finger domain; This domain is conserved in fungi and might be a zinc-finger ...
 1185-1204 5.27e-06

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: 44.49  E-value: 5.27e-06
                           10        20
                   ....*....|....*....|.
gi 87116683   1185 FCRFDLTG-TCNDDDCQWQHI 1204
Cdd:pfam10650    1 LCPYELAGgVCNDPSCEFQHF 21
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 1347-1441 7.85e-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: 47.49  E-value: 7.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1347 IANLEASVLENPSHVQLWLKLAYKYLNQNEgecsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKDEVQEMCET 1426
Cdd:COG4783   24 EALLEKALELDPDNPEAFALLGEILLQLGD------LDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEK 97

                         90
                 ....*....|....*
gi 87116683 1427 AVEYAPDYQSFWTFL 1441
Cdd:COG4783   98 ALKLDPEHPEAYLRL 112
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 1580-1687 8.09e-06

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 50.76  E-value: 8.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1580 FEDAVkACTDESLAVE-ERIEACLplytNMIALHQLLERYEAAMELCKSLLESCPINCQLLEALVALYLQTNQHDKARAV 1658
Cdd:COG3914  128 LEEAL-AALRRALALNpDFAEAYL----NLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAA 202

                         90       100
                 ....*....|....*....|....*....
gi 87116683 1659 WLTAFEKNPQNAEVFYHMCkfFILQNRGD 1687
Cdd:COG3914  203 YRRALELDPDNADAHSNLL--FALRQACD 229
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 1347-1432 1.97e-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: 46.88  E-value: 1.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1347 IANLEASVLENPSHVQLWLKLAYKYLNQNEgecsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKDEVQEMCET 1426
Cdd:COG5010   74 LALLEQALQLDPNNPELYYNLALLYSRSGD------KDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQR 147


                 ....*.
gi 87116683 1427 AVEYAP 1432
Cdd:COG5010  148 ALGTSP 153
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1610-1720 2.25e-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: 48.19  E-value: 2.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1610 ALHQLL-ERYEAAMELCKSLLESCPINCQLLEALVALYLQTNQHDKARAVWLTAFEKNPQNAEVFYHMCKFFILQNRGDN 1688
Cdd:COG2956   15 GLNYLLnGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDR 94

                         90       100       110
                 ....*....|....*....|....*....|..
gi 87116683 1689 LLPFLRKFIAsffkpgfEKYNNLDLFRYLLNI 1720
Cdd:COG2956   95 AEELLEKLLE-------LDPDDAEALRLLAEI 119
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 1347-1438 2.66e-05

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 49.22  E-value: 2.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1347 IANLEASVLENPSHVQLWLKLAYKYLNQNEgecsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKDEVQEMCET 1426
Cdd:COG3914   98 LALYRRALALNPDNAEALFNLGNLLLALGR------LEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRR 171

                         90
                 ....*....|..
gi 87116683 1427 AVEYAPDYQSFW 1438
Cdd:COG3914  172 ALELDPDNAEAL 183
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
1347-1534 3.88e-05

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 47.31  E-value: 3.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1347 IANLEASVLENPSHVQLWLKLAYKYLNQNEgecsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKDEVQEMCET 1426
Cdd:COG0457   28 IEDYEKALELDPDDAEALYNLGLAYLRLGR------YEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1427 AVEYAPDYQSFWTFLHLeSTFEEKDYvcERMLEFLMGAAKQETSNIlsfqllEALLFRVQLHIFTGRCQSALAILQNALK 1506
Cdd:COG0457  102 ALELDPDDAEALYNLGL-ALLELGRY--DEAIEAYERALELDPDDA------DALYNLGIALEKLGRYEEALELLEKLEA 172

                        170       180
                 ....*....|....*....|....*...
gi 87116683 1507 SANDGIVAEYLKTSDRCLAWLAYIHLIE 1534
Cdd:COG0457  173 AALAALLAAALGEAALALAAAEVLLALL 200
PTZ00121 PTZ00121
MAEBL; Provisional
 740-1029 3.99e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 3.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683   740 EARRTAEQASKpkvppKSEKENDPLRTPEalpEEKKIEYRLLKEEIANREKQRLIKSDQLKTSSSSPANSDveidgigri 819
Cdd:PTZ00121 1561 EEKKKAEEAKK-----AEEDKNMALRKAE---EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE--------- 1623

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683   820 amvtkQVTDAESKLKKHRILLMKDEsvlknlvqQEAKKKESVRNAE--AKITKLTEQLQATEKilnvnrmflKKLQEQIH 897
Cdd:PTZ00121 1624 -----ELKKAEEEKKKVEQLKKKEA--------EEKKKAEELKKAEeeNKIKAAEEAKKAEED---------KKKAEEAK 1681

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683   898 RVQQRVTIKKALTLKYGEELARAKAVASKEI-GKRKLEQDRfgpnKMMRLDSSPVSSPRKHSAEliamEKRRLQ--KLEY 974
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEEAKKAEELKKKEAeEKKKAEELK----KAEEENKIKAEEAKKEAEE----DKKKAEeaKKDE 1753

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 87116683   975 EYALKIQKLKEARALKAKE-QQNISPVVEEEPEfslPQPSLHDLTQDKLTLDTEEN 1029
Cdd:PTZ00121 1754 EEKKKIAHLKKEEEKKAEEiRKEKEAVIEEELD---EEDEKRRMEVDKKIKDIFDN 1806
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
1611-1698 4.92e-05

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 44.01  E-value: 4.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1611 LHQLLERYEAAMELCKSLLESCPINCQLLEALVALYLQTNQHDKARAvWLTAFEKNPQNAEVFYHMCKFFILQNRGDNLL 1690
Cdd:COG3063    1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEAL 79


                 ....*...
gi 87116683 1691 PFLRKFIA 1698
Cdd:COG3063   80 AYLERALE 87
Granin pfam01271
Granin (chromogranin or secretogranin);
220-438 6.30e-05

Granin (chromogranin or secretogranin);


Pssm-ID: 279595 [Multi-domain]  Cd Length: 584  Bit Score: 48.10  E-value: 6.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    220 CVEETFEDLLLKYKQIQLELECINKDEKL------ALSSKEENVQEDPKTLnfEDQTSTDNVSITKDSSKEVAPEEKTQV 293
Cdd:pfam01271   11 CIIEVLSNALSKSSPPPITPECLEVLKKGrkriksEERSENYNPYFEVRLL--RDLADQSEASHLSSRSRDGLSDEDMQI 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    294 KTfqafelKPLRQKLTLPGDKNRLKKVKDGAKPLSLKSDTTDSSQGLQDKEQNLT--RRISTSDILSEKKLGEDEEELSE 371
Cdd:pfam01271   89 IT------EALRQAENEPGGHSRENQPYALQVEKEFKTDHSDDYETQQWEEEKLKhmRFPLRYEENSEEKHSEREGELSE 162

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 87116683    372 LQLrllalqsaskkwqQKEQQVMKESKEKLTKTKTVQQKVKTStKTHSAKKVSTTAKQALRKQQTKA 438
Cdd:pfam01271  163 VFE-------------NPRSQATLKKVFEEVSRLDTPSKQKRE-KSDEREKSSQESGEDTYRQENIP 215
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
1580-1695 9.34e-05

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 46.15  E-value: 9.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1580 FEDAVKACtDESLAVE-ERIEAclplYTNMIALHQLLERYEAAMELCKSLLESCPINCQLLEALVALYLQTNQHDKARAV 1658
Cdd:COG0457   58 YEEALADY-EQALELDpDDAEA----LNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEA 132

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 87116683 1659 WLTAFEKNPQNAEVFYHMCKFFILQNRGDNLLPFLRK 1695
Cdd:COG0457  133 YERALELDPDDADALYNLGIALEKLGRYEEALELLEK 169
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
1347-1433 1.16e-04

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 42.85  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1347 IANLEASVLENPSHVQLWLKLAYKYLNQNEgecsesLDSALNvLARALENNKDNPEIWCHYLRLFSKRGTKDEVQEMCET 1426
Cdd:COG3063   12 EEYYEKALELDPDNADALNNLGLLLLEQGR------YDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLER 84


                 ....*..
gi 87116683 1427 AVEYAPD 1433
Cdd:COG3063   85 ALELDPS 91
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1611-1698 1.43e-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: 45.88  E-value: 1.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1611 LHQLLERYEAAMELCKSLLESCPINCQLLEALVALYLQTNQHDKARAVWLTAFEKNPQNAEVFYHMCKFFILQNRGDNLL 1690
Cdd:COG2956   85 DYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAI 164


                 ....*...
gi 87116683 1691 PFLRKFIA 1698
Cdd:COG2956  165 EALEKALK 172
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 1361-1510 1.46e-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: 43.64  E-value: 1.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1361 VQLWLKLAYKYLNQNEgecsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKDEVQEMCETAVEYAPDYQSFWTF 1440
Cdd:COG4783    4 AEALYALAQALLLAGD------YDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLN 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1441 LhLESTFEEKDYvcERMLEFLMGAAKQETSNILSFQLLEALLFRvqlhifTGRCQSALAILQNALKSAND 1510
Cdd:COG4783   78 L-GLALLKAGDY--DEALALLEKALKLDPEHPEAYLRLARAYRA------LGRPDEAIAALEKALELDPD 138
PTZ00121 PTZ00121
MAEBL; Provisional
 739-1006 1.70e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683   739 KEARRTAEQASKPKVPPKSEKENDPLRTPEALPEEKKIEYRLLKEEIANREKQRliKSDQLKTSSSSPANSDVEIDGIGR 818
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK--KADELKKAEELKKAEEKKKAEEAK 1570

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683   819 IA-----MVTKQVTDAESKLKKHRILLMKDESVLKNLVQQEAKKKESVRNAEAKITKLTEQLQATEKILNVNRMFLKKlQ 893
Cdd:PTZ00121 1571 KAeedknMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK-A 1649

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683   894 EQIHRVQQRVTIKKA-LTLKYGEELARAKAVASKEIGKRKLEQDRfgpnKMMRLDSSPVSSPRKHSAEliamEKRRLQKL 972
Cdd:PTZ00121 1650 EELKKAEEENKIKAAeEAKKAEEDKKKAEEAKKAEEDEKKAAEAL----KKEAEEAKKAEELKKKEAE----EKKKAEEL 1721

                         250       260       270
                  ....*....|....*....|....*....|....
gi 87116683   973 EYEYALKIQKLKEARALKAKEQQNISPVVEEEPE 1006
Cdd:PTZ00121 1722 KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 734-1006 1.85e-04

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: 46.59  E-value: 1.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    734 LESMIKEARRTAEQASKpkvppKSEKENDPLRTPEALPEEKKIEYRLLKEEIANREKQRLIKSDQLKTSSSSPANSDVEI 813
Cdd:TIGR02168  710 LEEELEQLRKELEELSR-----QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    814 --------DGIGRIAMVTKQVTDAESKLKKHRILLMKDESVLKNLVQQEAKKKESVRNAEAKITKLTEQLQATEKILNVN 885
Cdd:TIGR02168  785 eeleaqieQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    886 RMFLKKLQEQIhrvqqrvtiKKALTLKYGEELARAKAVASKEIGKRKLEQDRfgpNKMMRLDSSpvsspRKHSAELIAME 965
Cdd:TIGR02168  865 EELIEELESEL---------EALLNERASLEEALALLRSELEELSEELRELE---SKRSELRRE-----LEELREKLAQL 927

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 87116683    966 KRRLQKLEYEYALKIQKLKEARALKAKEQQNISPVVEEEPE 1006
Cdd:TIGR02168  928 ELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEE 968
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
1605-1687 2.11e-04

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 45.00  E-value: 2.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1605 YTNMIALHQLLERYEAAMELCKSLLESCPINCQLLEALVALYLQTNQHDKARAVWLTAFEKNPQNAEVFYHMCkfFILQN 1684
Cdd:COG0457   11 YNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLG--LALQA 88


                 ...
gi 87116683 1685 RGD 1687
Cdd:COG0457   89 LGR 91
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 1590-1698 2.43e-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: 43.26  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1590 ESLAVEERIEACLPLY--------TNMIALHQL------LERYEAAMELCKSLLESCPINCQLLEALVALYLQTNQHDKA 1655
Cdd:COG4783   12 QALLLAGDYDEAEALLekaleldpDNPEAFALLgeillqLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEA 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 87116683 1656 RAVWLTAFEKNPQNAEVFYHMCKFFILQNRGDNLLPFLRKFIA 1698
Cdd:COG4783   92 LALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALE 134
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 829-1004 3.14e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 3.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683  829 AESKLKKHRILLMKDESVLKNLVQQEAKKKEsvrnAEAKITKLTEQLQATEKILNVNRMFLKKLQEQIHRVQQRVTIKKA 908
Cdd:COG1196  220 EELKELEAELLLLKLRELEAELEELEAELEE----LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683  909 LTLKYGEELARAKAvASKEIGKRKLEQDRFGPNKMMRLDsspvssprKHSAELIAMEKrRLQKLEYEYALKIQKLKEARA 988
Cdd:COG1196  296 ELARLEQDIARLEE-RRRELEERLEELEEELAELEEELE--------ELEEELEELEE-ELEEAEEELEEAEAELAEAEE 365

                        170
                 ....*....|....*.
gi 87116683  989 LKAKEQQNISPVVEEE 1004
Cdd:COG1196  366 ALLEAEAELAEAEEEL 381
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
1357-1516 5.79e-04

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 43.84  E-value: 5.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1357 NPSHVQLWLKLAYKYLNQNEgecsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKDEVQEMCETAVEYAPDYqs 1436
Cdd:COG0457    4 DPDDAEAYNNLGLAYRRLGR------YEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDD-- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1437 FWTFLHLESTFEE-KDYvcERMLEFLMGAAKQETSNIlsfqllEALLFRVQLHIFTGRCQSALAILQNALKSANDGIVAE 1515
Cdd:COG0457   76 AEALNNLGLALQAlGRY--EEALEDYDKALELDPDDA------EALYNLGLALLELGRYDEAIEAYERALELDPDDADAL 147


                 .
gi 87116683 1516 Y 1516
Cdd:COG0457  148 Y 148
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 1617-1667 6.77e-04

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: 43.77  E-value: 6.77e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 87116683 1617 RYEAAMELCKSLLESCPINCQLLEALVALYLQTNQHDKARAVWLTAFEKNP 1667
Cdd:cd24142   15 NFELALKFLQRALELEPNNVEALELLGEILLELGDVEEAREVLLRAIELDP 65
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 1567-1671 1.78e-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: 40.37  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1567 QDVKTNPD-----MLLAV-------FEDAVKACtDESLAVE-ERIEAclplYTNMIALHQLLERYEAAMELCKSLLESCP 1633
Cdd:COG4235    8 QALAANPNdaegwLLLGRaylrlgrYDEALAAY-EKALRLDpDNADA----LLDLAEALLAAGDTEEAEELLERALALDP 82

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 87116683 1634 INCQLLEALVALYLQTNQHDKARAVWLTAFEKNPQNAE 1671
Cdd:COG4235   83 DNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPADAP 120
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 781-1036 2.05e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.09  E-value: 2.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    781 LKEEIANREKQRLIKSDQLktsssspANSDVEIDGIGR-IAMVTKQVTDAESKLKKHRILLMKDESVLKNLVQQEAKKKE 859
Cdd:TIGR04523  312 LKSELKNQEKKLEEIQNQI-------SQNNKIISQLNEqISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQ 384

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    860 SVRNAEAKITKLTEQLQATEKILNVNRMFLKKLQEQIHRVQQRVTIKKALTLKYGEELAR-AKAVASKEIGKRKLEQDRF 938
Cdd:TIGR04523  385 EIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDlTNQDSVKELIIKNLDNTRE 464

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    939 GPNKMMRLDSSpvssprkhsaeLIAMEKRRLQKLEYEYALKIQKLKEARALKAKEQQNISPVVEEEPEFSLPQpslHDLT 1018
Cdd:TIGR04523  465 SLETQLKVLSR-----------SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKI---EKLE 530

                          250
                   ....*....|....*...
gi 87116683   1019 QDKLTLDTEENDVDDEIL 1036
Cdd:TIGR04523  531 SEKKEKESKISDLEDELN 548
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 757-973 2.21e-03

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 42.89  E-value: 2.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    757 SEKEndplRTPEALPEEKKIEYRLLKEEIANREKQ-----------RLIKSDQ------LKTSSSSPANSDVEIDGIGR- 818
Cdd:pfam10174  446 SEKE----RIIERLKEQREREDRERLEELESLKKEnkdlkekvsalQPELTEKesslidLKEHASSLASSGLKKDSKLKs 521

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    819 --IAMVTK--QVTDAESKLKK-HRILL---MKDESV--LKNLVQQEAKKKESVRNAEAKITKLTEQLQATE--------K 880
Cdd:pfam10174  522 leIAVEQKkeECSKLENQLKKaHNAEEavrTNPEINdrIRLLEQEVARYKEESGKAQAEVERLLGILREVEnekndkdkK 601

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    881 ILNVNRMFLKKLQEQihrvqqrvtIKKALTLKYGEELARAKAVASKEIGKRkleqdrfgpnkmmRLDSSPVSSPRKHSAE 960
Cdd:pfam10174  602 IAELESLTLRQMKEQ---------NKKVANIKHGQQEMKKKGAQLLEEARR-------------REDNLADNSQQLQLEE 659

                          250
                   ....*....|....
gi 87116683    961 LI-AMEKRRlQKLE 973
Cdd:pfam10174  660 LMgALEKTR-QELD 672
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
1605-1667 3.43e-03

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 38.61  E-value: 3.43e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 87116683 1605 YTNMIALHQLLERYEAAMELcKSLLESCPINCQLLEALVALYLQTNQHDKARAVWLTAFEKNP 1667
Cdd:COG3063   29 LNNLGLLLLEQGRYDEAIAL-EKALKLDPNNAEALLNLAELLLELGDYDEALAYLERALELDP 90
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 1348-1548 3.65e-03

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 42.29  E-value: 3.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1348 ANLEASVLENPSHVQLWLKLAYKYLnQNEGEcsesLDSALNVLARALENNKDNPEIWCHYLRLFSKRGTKDEVQEMCETA 1427
Cdd:COG3914   64 AGEAAAAAAALLLLAALLELAALLL-QALGR----YEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRA 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1428 VEYAPDYQSFWTFLhLESTFEEKDYvcERMLEFLMGAAKQETSNILSFQLLEALLFRvqlhifTGRCQSALAILQNALK- 1506
Cdd:COG3914  139 LALNPDFAEAYLNL-GEALRRLGRL--EEAIAALRRALELDPDNAEALNNLGNALQD------LGRLEEAIAAYRRALEl 209

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 87116683 1507 -----SANDGIVAEYLKTSD-----RCLAWLAYIHLIEFNILPSKF-YDPSND 1548
Cdd:COG3914  210 dpdnaDAHSNLLFALRQACDwevydRFEELLAALARGPSELSPFALlYLPDDD 262
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 244-1119 3.67e-03

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: 42.65  E-value: 3.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    244 KDEKLALSSKEENVQEDPKTLNFEDQTSTDNVSITKDSSKEVAPEEKTQVKTFQAFELKPLRQKLTLPGDKNRLKKvkdg 323
Cdd:pfam02463  168 KRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ---- 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    324 aKPLSLKSDTTDSSQGLQDKEQNLTRRISTSDILSEKKLGEDEEELSEL---------QLRLLALQSASKKWQQKEQQVM 394
Cdd:pfam02463  244 -ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLakeeeelksELLKLERRKVDDEEKLKESEKE 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    395 KESKEK-LTKTKTVQQKVKTSTKTHSAKKVS-TTAKQALRKQQTKAWKKLQQQKEQERQKEEDQRKQAEEEERRKREEEI 472
Cdd:pfam02463  323 KKKAEKeLKKEKEEIEELEKELKELEIKREAeEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE 402

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    473 RKIRDLSNQEEQYNRFM-KLVGGKRRSRSKSSDPDLRRSLDKQPTDSGGGIYQYDNYEEVAMDTDSETSSPAPSpvqppf 551
Cdd:pfam02463  403 EEKEAQLLLELARQLEDlLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKE------ 476

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    552 fSECSLGYFSPAPSLSLPPPPQVSSLPPLSQPYVEGLCVSLEPLPPLPPLPPLPPEDPEQPPKPPFADEEEEEEMLLREE 631
Cdd:pfam02463  477 -TQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSA 555

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    632 LLKSLANKRAFKPEETSSNSDPPSPPVLNNSHPVPRSNLSIVSINtvsqPRIQNPKFHRGPRLPRTVISLPKHKSVVVTL 711
Cdd:pfam02463  556 TADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEID----PILNLAQLDKATLEADEDDKRAKVVEGILKD 631

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    712 NDSDDSESDGEASKSTNSVFGGLESMIKEARRTAEQASKPKVPPKSEKENDPLRTPEALPEEKKIEyRLLKEEIANREKQ 791
Cdd:pfam02463  632 TELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRR-QLEIKKKEQREKE 710

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    792 RLIKSDQLKTSSSSPANSDVEIDGIGRIAMVTKQVTDAESKLKKHRILLMKDESVLKNLVQQEAKKKESVRNAE--AKIT 869
Cdd:pfam02463  711 ELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEklKVEE 790

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    870 KLTEQLQATEKILNVNRMFLKKLQEQIHRVQQRVTIKKALTLKYGEELArAKAVASKEIGKRKLEQDRFGPNKMMRLDSS 949
Cdd:pfam02463  791 EKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELA-LELKEEQKLEKLAEEELERLEEEITKEELL 869

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683    950 PVSSPRKHSAELIAMEKRRLQKLEYEYALKIQKLKEARalkAKEQQNISPVVEEEPEFSLPQPSLHDLTQDKLTLDTEEN 1029
Cdd:pfam02463  870 QELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQ---KLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEAD 946

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683   1030 DVDDEILSGSSRERRRSFLESNYFTKPNLKhtdtankeciNKLNKNTVEKPELFLGLKIgELQKLYSKADSLKQLILKTT 1109
Cdd:pfam02463  947 EKEKEENNKEEEEERNKRLLLAKEELGKVN----------LMAIEEFEEKEERYNKDEL-EKERLEEEKKKLIRAIIEET 1015

                          890
                   ....*....|
gi 87116683   1110 TGITEKVLHG 1119
Cdd:pfam02463 1016 CQRLKEFLEL 1025
TPR_14 pfam13428
Tetratricopeptide repeat;
1361-1410 3.73e-03

Tetratricopeptide repeat;


Pssm-ID: 463874 [Multi-domain]  Cd Length: 44  Bit Score: 37.02  E-value: 3.73e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 87116683   1361 VQLWLKLAYKYLNQNEgecsesLDSALNVLARALENNKDNPEIWCHYLRL 1410
Cdd:pfam13428    1 PEALLALARALLALGD------PDEALALLERALALDPDDPEAWLALAQL 44
PTZ00121 PTZ00121
MAEBL; Provisional
 740-1004 4.62e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 4.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683   740 EARRTAEQASKPKVPPKSEKEN--DPLRTPE--ALPEEKKIEYRLLKEEIANREKQRLIKSDQLKTSSSSPANSdveidg 815
Cdd:PTZ00121 1333 AAKKKAEEAKKAAEAAKAEAEAaaDEAEAAEekAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK------ 1406

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683   816 igriamvTKQVTDAESKLKKHRILLMKDESVLKnlvQQEAKKK-ESVRNAEAKITKLTEQLQATEKILNVNRMflKKLQE 894
Cdd:PTZ00121 1407 -------ADELKKAAAAKKKADEAKKKAEEKKK---ADEAKKKaEEAKKADEAKKKAEEAKKAEEAKKKAEEA--KKADE 1474

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683   895 QIHRVQQRvtiKKALTLKYGEELARAKA--VASKEIGKRKLEQDRFGPNKMMRLDSSPVSSPRKHSAELIAMEKRRLQKL 972
Cdd:PTZ00121 1475 AKKKAEEA---KKADEAKKKAEEAKKKAdeAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADEL 1551

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 87116683   973 ----EYEYALKIQKLKEARalKAKEQQNISPVVEEE 1004
Cdd:PTZ00121 1552 kkaeELKKAEEKKKAEEAK--KAEEDKNMALRKAEE 1585
TPR_19 pfam14559
Tetratricopeptide repeat;
1347-1404 4.64e-03

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 37.56  E-value: 4.64e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 87116683   1347 IANLEASVLENPSHVQLWLKLAYKYLNQNEgecsesLDSALNVLARALENNKDNPEIW 1404
Cdd:pfam14559    8 LELLEQALAEDPDNAEARLGLAEALLALGR------LDEAEALLAALPAADPDDPRYA 59
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 773-1036 4.93e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 4.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683  773 EKKIEYRLLKEEIANREKQRLIKSDQLKTSssspansdveidgigRIAMVTKQVTDAESKLKKHRILLMKDESVLKNLVQ 852
Cdd:COG1196  210 EKAERYRELKEELKELEAELLLLKLRELEA---------------ELEELEAELEELEAELEELEAELAELEAELEELRL 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683  853 QEAKKKESVRNAEAKITKLTEQLQATEKILNVNRMFLKKLQEQIHRVQQRVTIKKALTLKYGEELARAKAVASKEIGKRK 932
Cdd:COG1196  275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683  933 LEQDRFgpnkmmrldsspvsspRKHSAELIAMEKRRLQKLEYEYALKIQKLKEARALKAKEQQNISPVVEEEpefslpqp 1012
Cdd:COG1196  355 EAEAEL----------------AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE-------- 410

                        250       260
                 ....*....|....*....|....
gi 87116683 1013 slhDLTQDKLTLDTEENDVDDEIL 1036
Cdd:COG1196  411 ---ALLERLERLEEELEELEEALA 431
PRK12704 PRK12704
phosphodiesterase; Provisional
 735-922 5.68e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 5.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683   735 ESMIKEARRTAEQASKpkvppksekendplrtpEALPEEKKiEYRLLKEEIANREKQRLIKSDQLKtsssspansdveid 814
Cdd:PRK12704   41 KRILEEAKKEAEAIKK-----------------EALLEAKE-EIHKLRNEFEKELRERRNELQKLE-------------- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683   815 gigriamvtKQVTDAESKLKKHRILLMKDESVLKNLVQQEAKKKESVRNAEAKITKL-TEQLQATEKILNVNR-----MF 888
Cdd:PRK12704   89 ---------KRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELiEEQLQELERISGLTAeeakeIL 159

                         170       180       190
                  ....*....|....*....|....*....|....
gi 87116683   889 LKKLQEQIhRVQQRVTIKKAltlkygEELARAKA 922
Cdd:PRK12704  160 LEKVEEEA-RHEAAVLIKEI------EEEAKEEA 186
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 1589-1667 5.93e-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: 39.56  E-value: 5.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683 1589 DESLAVEERIEACLP----LYTNMIALHQLLERYEAAMELCKSLLESCPINCQLLEALVALYLQTNQHDKARAVWLTAFE 1664
Cdd:COG5010   71 EESLALLEQALQLDPnnpeLYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALG 150


                 ...
gi 87116683 1665 KNP 1667
Cdd:COG5010  151 TSP 153
PTZ00121 PTZ00121
MAEBL; Provisional
 716-1004 6.19e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 6.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683   716 DSESDGEASKSTNSVFGGLESMIKEARRTAEQASKPKVPPKSEKENDPLRTPEALPEEKKIEYRLLKEEIANREKQRLIK 795
Cdd:PTZ00121 1082 DAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAE 1161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683   796 sDQLKTSSSSPANSDVEIDGIGRIAMVTK--QVTDAESKLKKHRILLMKDESVLKNLVQ-QEAKKKESVRNAEaKITKLT 872
Cdd:PTZ00121 1162 -DARKAEEARKAEDAKKAEAARKAEEVRKaeELRKAEDARKAEAARKAEEERKAEEARKaEDAKKAEAVKKAE-EAKKDA 1239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 87116683   873 EQLQATEKILNVNRMFLKKLQEQIHRVQQRVTIK-----------KALTLKYGEELARAKAVASKEIGKRKLEQDRfgpn 941
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKaeearkadelkKAEEKKKADEAKKAEEKKKADEAKKKAEEAK---- 1315

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 87116683   942 KMMRLDSSPVSSPRKHSAeliAMEKRRLQKLEYEYALKIQKLKEARALKAKEQQNISPVVEEE 1004
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADA---AKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE 1375
 
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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