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Conserved domains on  [gi|489305997|ref|WP_003213435|]
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type VII secretion protein EsaA [Bacillus pumilus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
T7_esaA_Nterm TIGR03929
type VII secretion protein EsaA, N-terminal domain; Members of this family are associated with ...
 11-201 1.98e-85

type VII secretion protein EsaA, N-terminal domain; Members of this family are associated with type VII secretion of WXG100 family targets in the Firmicutes, but not in the Actinobacteria. This model represents the conserved N-terminal domain.


:

Pssm-ID: 274861 [Multi-domain]  Cd Length: 193  Bit Score: 272.36  E-value: 1.98e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   11 IVSTMILILVLPVLFFHLIGDDPAKQKKN--ATRNIAVVNEDMGASESENTARFGQDVVAALSERPDYTWTVVNRSAAEN 88
Cdd:TIGR03929   1 LIFLVLFIVLLPGLFFLAIGQNPKKQKTNqnAKMNIAVVNEDQGVSFDGKTYNFGASFVKAIERDNSQEWSVVSRGAAEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   89 GLKSRKYDAVLYIPSDFSKNVLSYDKDHPEKASIQFSIQDQLNSVNKEKVQRELENAQKKMNEQMSTLYWSFVSQEIGNV 168
Cdd:TIGR03929  81 GLKNNTYDAVVYIPSDFSKKVLSVNKENPEKATIQYKVNANGNAVLKEEAQREAEDILNDFNSQMSDLYWASILQNLQTA 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 489305997  169 REEFEHIVGKEVEFQNTMYNFYKPNSNKLSDAV 201
Cdd:TIGR03929 161 QDNVQAIVNKEAEFQSTYYKNYLPSSANLTNQF 193
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 302-576 2.54e-06

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 TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 51.61  E-value: 2.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   302 SQLNTTDSAIQSVQKSReDAIPKQSTGLTKLVQESQEELIKKyeERYLEDYRNKISAL----QTKLLAKRQELMDEPEPP 377
Cdd:TIGR02169  230 KEKEALERQKEAIERQL-ASLEEELEKLTEEISELEKRLEEI--EQLLEELNKKIKDLgeeeQLRVKEKIGELEAEIASL 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   378 VDSEDDgpSDQDNENPEEIGINLDEETNELSQisiEMNDLADQLGEQEtppstgdgeegeagenpaqpdtGNKNSSQDDL 457
Cdd:TIGR02169  307 ERSIAE--KERELEDAEERLAKLEAEIDKLLA---EIEELEREIEEER----------------------KRRDKLTEEY 359

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   458 KALSTRLDEVKKKIQEKaSAHNDELKDKVSQMSKELEKLTKKVEKLEKMFLWLQDRYNVIPNE---IKNQESTILSKVKE 534
Cdd:TIGR02169  360 AELKEELEDLRAELEEV-DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEladLNAAIAGIEAKINE 438

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 489305997   535 LKRRNSPIGEAFndnlfeKKFETKSTRTKKLME-YSNQLSQLE 576
Cdd:TIGR02169  439 LEEEKEDKALEI------KKQEWKLEQLAADLSkYEQELYDLK 475
ABC_export super family cl25562
Putative ABC exporter; This is a family of putative ABC_exporters from Firmicutes.
 804-945 2.21e-04

Putative ABC exporter; This is a family of putative ABC_exporters from Firmicutes.


The actual alignment was detected with superfamily member pfam16962:

Pssm-ID: 435677  Cd Length: 530  Bit Score: 44.96  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997  804 MISSLLIGFFSSYYaaAPMLVKG---------ALFGILNLLVGLMISLFGLNIYKLADD----QAIQWSIFTILLLVACS 870
Cdd:pfam16962 118 MLTSLLVGLFAIFQ--IPNLVNGfgltmggivALLLGITLLLILLGSVIILLIYSFTSKepkrKKIVKGIIVLLGVLLLA 195

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489305997  871 AFIRTAFLFGsiAGWMAATALIFFFVAPLIDLVmpnfhftnPV----TDVYLSIQYGNGDHFGMGVIGLVILTVLFMAI 945
Cdd:pfam16962 196 AVLFAIQLFS--NGGNLLEGLLAFITSPWFSYI--------PIigwtKALIMALLSGIWLSFLVYLVLLLLSLALLILL 264
CCDC158 super family cl37899
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 454-725 5.81e-04

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


The actual alignment was detected with superfamily member pfam15921:

Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.95  E-value: 5.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   454 QDDLKALSTrldEVKKKIQEKASAHNDELKDKVSQMSKELEKLTKKVEKLEKMFLWLQDRYNVIPNEIKNQESTILSKVK 533
Cdd:pfam15921  244 EDQLEALKS---ESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLS 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   534 ELK----RRNSPIGEA---FNDNL--FEKKF--------ETKSTRTKKLMEYSNQLSQLELMIANVYQPSNNSSLydAKE 596
Cdd:pfam15921  321 DLEstvsQLRSELREAkrmYEDKIeeLEKQLvlanseltEARTERDQFSQESGNLDDQLQKLLADLHKREKELSL--EKE 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   597 ENiQSILSIKKEETENWDTLKKQMltsnDDVSTfidEMQKFSDGYAEYISTQQASMEQELNTI---SESADNVAEqmadq 673
Cdd:pfam15921  399 QN-KRLWDRDTGNSITIDHLRREL----DDRNM---EVQRLEALLKAMKSECQGQMERQMAAIqgkNESLEKVSS----- 465

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 489305997   674 gdavYTADLAgssivvSAQDSIGQEVLRLSENMSSLTDRQKGVADYTNNIEE 725
Cdd:pfam15921  466 ----LTAQLE------STKEMLRKVVEELTAKKMTLESSERTVSDLTASLQE 507
 
Name Accession Description Interval E-value
T7_esaA_Nterm TIGR03929
type VII secretion protein EsaA, N-terminal domain; Members of this family are associated with ...
 11-201 1.98e-85

type VII secretion protein EsaA, N-terminal domain; Members of this family are associated with type VII secretion of WXG100 family targets in the Firmicutes, but not in the Actinobacteria. This model represents the conserved N-terminal domain.


Pssm-ID: 274861 [Multi-domain]  Cd Length: 193  Bit Score: 272.36  E-value: 1.98e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   11 IVSTMILILVLPVLFFHLIGDDPAKQKKN--ATRNIAVVNEDMGASESENTARFGQDVVAALSERPDYTWTVVNRSAAEN 88
Cdd:TIGR03929   1 LIFLVLFIVLLPGLFFLAIGQNPKKQKTNqnAKMNIAVVNEDQGVSFDGKTYNFGASFVKAIERDNSQEWSVVSRGAAEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   89 GLKSRKYDAVLYIPSDFSKNVLSYDKDHPEKASIQFSIQDQLNSVNKEKVQRELENAQKKMNEQMSTLYWSFVSQEIGNV 168
Cdd:TIGR03929  81 GLKNNTYDAVVYIPSDFSKKVLSVNKENPEKATIQYKVNANGNAVLKEEAQREAEDILNDFNSQMSDLYWASILQNLQTA 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 489305997  169 REEFEHIVGKEVEFQNTMYNFYKPNSNKLSDAV 201
Cdd:TIGR03929 161 QDNVQAIVNKEAEFQSTYYKNYLPSSANLTNQF 193
YhgE COG1511
Uncharacterized membrane protein YhgE, phage infection protein (PIP) family [Function unknown]; ...
 15-162 6.17e-33

Uncharacterized membrane protein YhgE, phage infection protein (PIP) family [Function unknown];


Pssm-ID: 441120  Cd Length: 225  Bit Score: 127.37  E-value: 6.17e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997  15 MILILVLPVLFFHLIG---DDPAKQKKNATrnIAVVNEDMGASESENTARFGQDVVAALSERPDYTWTVVNRSAAENGLK 91
Cdd:COG1511   18 LIALILVPLLYAGLYLwafWDPYGNLDNLP--VAVVNEDKGATVDGKTVNLGDELVDELKDNDSFDWQFVSEEEAEKGLK 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489305997  92 SRKYDAVLYIPSDFSKNVLSYDKDHPEKASIQFSIQDQLNSVNKEKVQRELENAQKKMNEQMSTLYWSFVS 162
Cdd:COG1511   96 DGKYYAVIVIPEDFSANLASLLSDDPEKATITYYTNEANNYLASKITDTAATTVVDQVNSQVTETYAETVS 166
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 302-576 2.54e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.61  E-value: 2.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   302 SQLNTTDSAIQSVQKSReDAIPKQSTGLTKLVQESQEELIKKyeERYLEDYRNKISAL----QTKLLAKRQELMDEPEPP 377
Cdd:TIGR02169  230 KEKEALERQKEAIERQL-ASLEEELEKLTEEISELEKRLEEI--EQLLEELNKKIKDLgeeeQLRVKEKIGELEAEIASL 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   378 VDSEDDgpSDQDNENPEEIGINLDEETNELSQisiEMNDLADQLGEQEtppstgdgeegeagenpaqpdtGNKNSSQDDL 457
Cdd:TIGR02169  307 ERSIAE--KERELEDAEERLAKLEAEIDKLLA---EIEELEREIEEER----------------------KRRDKLTEEY 359

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   458 KALSTRLDEVKKKIQEKaSAHNDELKDKVSQMSKELEKLTKKVEKLEKMFLWLQDRYNVIPNE---IKNQESTILSKVKE 534
Cdd:TIGR02169  360 AELKEELEDLRAELEEV-DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEladLNAAIAGIEAKINE 438

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 489305997   535 LKRRNSPIGEAFndnlfeKKFETKSTRTKKLME-YSNQLSQLE 576
Cdd:TIGR02169  439 LEEEKEDKALEI------KKQEWKLEQLAADLSkYEQELYDLK 475
ABC2_membrane_3 pfam12698
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ...
 13-156 9.95e-06

ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.


Pssm-ID: 463674 [Multi-domain]  Cd Length: 345  Bit Score: 48.93  E-value: 9.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   13 STMILILVLPVLF-------FHLIGDDPAKQKknatrnIAVVNEDmgasesenTARFGQDVVAALSERP--DYTWTVVNR 83
Cdd:pfam12698   2 SFLIITLLLPILLilllgliFSNAVNDPEELP------VAVVDED--------NSSLSRQLVRALEASPtvNLVQYVDSE 67

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489305997   84 SAAENGLKSRKYDAVLYIPSDFSKNVLSYdkdhpEKASIQFSIQDQLNSVNKEkVQRELENAQKKMNEQMSTL 156
Cdd:pfam12698  68 EEAKEALKNGKIDGLLVIPKGFSKDLLKG-----ESATVTVYINSSNLLVSKL-ILNALQSLLQQLNASALVL 134
ABC_export pfam16962
Putative ABC exporter; This is a family of putative ABC_exporters from Firmicutes.
 804-945 2.21e-04

Putative ABC exporter; This is a family of putative ABC_exporters from Firmicutes.


Pssm-ID: 435677  Cd Length: 530  Bit Score: 44.96  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997  804 MISSLLIGFFSSYYaaAPMLVKG---------ALFGILNLLVGLMISLFGLNIYKLADD----QAIQWSIFTILLLVACS 870
Cdd:pfam16962 118 MLTSLLVGLFAIFQ--IPNLVNGfgltmggivALLLGITLLLILLGSVIILLIYSFTSKepkrKKIVKGIIVLLGVLLLA 195

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489305997  871 AFIRTAFLFGsiAGWMAATALIFFFVAPLIDLVmpnfhftnPV----TDVYLSIQYGNGDHFGMGVIGLVILTVLFMAI 945
Cdd:pfam16962 196 AVLFAIQLFS--NGGNLLEGLLAFITSPWFSYI--------PIigwtKALIMALLSGIWLSFLVYLVLLLLSLALLILL 264
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
311-576 3.47e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 3.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997 311 IQSVQKSRE--DAIPKQSTGLTKL--VQESQEELIK--KYEERYLEDYRNKISALQTKLLAKRQELMDepeppVDSEDDG 384
Cdd:PRK03918 137 IDAILESDEsrEKVVRQILGLDDYenAYKNLGEVIKeiKRRIERLEKFIKRTENIEELIKEKEKELEE-----VLREINE 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997 385 PSDQDNENPEEIGiNLDEETNELSQISIEMNDLADQLGEQEtppstgdgeegeagenpaqpdtGNKNSSQDDLKALSTRL 464
Cdd:PRK03918 212 ISSELPELREELE-KLEKEVKELEELKEEIEELEKELESLE----------------------GSKRKLEEKIRELEERI 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997 465 DEVKKKIQekasahndELKDKVSQMsKELEKLTKKVEKLEKmflwLQDRYNVIPNEIKNQESTILSKVKELKRRnspIGE 544
Cdd:PRK03918 269 EELKKEIE--------ELEEKVKEL-KELKEKAEEYIKLSE----FYEEYLDELREIEKRLSRLEEEINGIEER---IKE 332

                        250       260       270
                 ....*....|....*....|....*....|..
gi 489305997 545 AfndnlfEKKFETKSTRTKKLMEYSNQLSQLE 576
Cdd:PRK03918 333 L------EEKEERLEELKKKLKELEKRLEELE 358
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 454-725 5.81e-04

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.95  E-value: 5.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   454 QDDLKALSTrldEVKKKIQEKASAHNDELKDKVSQMSKELEKLTKKVEKLEKMFLWLQDRYNVIPNEIKNQESTILSKVK 533
Cdd:pfam15921  244 EDQLEALKS---ESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLS 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   534 ELK----RRNSPIGEA---FNDNL--FEKKF--------ETKSTRTKKLMEYSNQLSQLELMIANVYQPSNNSSLydAKE 596
Cdd:pfam15921  321 DLEstvsQLRSELREAkrmYEDKIeeLEKQLvlanseltEARTERDQFSQESGNLDDQLQKLLADLHKREKELSL--EKE 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   597 ENiQSILSIKKEETENWDTLKKQMltsnDDVSTfidEMQKFSDGYAEYISTQQASMEQELNTI---SESADNVAEqmadq 673
Cdd:pfam15921  399 QN-KRLWDRDTGNSITIDHLRREL----DDRNM---EVQRLEALLKAMKSECQGQMERQMAAIqgkNESLEKVSS----- 465

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 489305997   674 gdavYTADLAgssivvSAQDSIGQEVLRLSENMSSLTDRQKGVADYTNNIEE 725
Cdd:pfam15921  466 ----LTAQLE------STKEMLRKVVEELTAKKMTLESSERTVSDLTASLQE 507
MFS_MdfA_MDR_like cd17320
Multidrug transporter MdfA and similar multidrug resistance (MDR) transporters of the Major ...
 804-952 2.18e-03

Multidrug transporter MdfA and similar multidrug resistance (MDR) transporters of the Major Facilitator Superfamily; This family is composed of bacterial multidrug resistance (MDR) transporters including several proteins from Escherichia coli such as MdfA (also called chloramphenicol resistance pump Cmr), EmrD, MdtM, MdtL, bicyclomycin resistance protein (also called sulfonamide resistance protein), and the uncharacterized inner membrane transport protein YdhC. EmrD is a proton-dependent secondary transporter, first identified as an efflux pump for uncouplers of oxidative phosphorylation. It expels a range of drug molecules and amphipathic compounds across the inner membrane of E. coli. Similarly, MdfA is a secondary multidrug transporter that exports a broad spectrum of structurally and electrically dissimilar toxic compounds. These MDR transporters are drug/H+ antiporters (DHA) belonging to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 340878 [Multi-domain]  Cd Length: 379  Bit Score: 41.41  E-value: 2.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997 804 MISSLLIGFFSSYYAAAPMLVKGAL------FGILNLLVGLMISLFGLNIYKLADDQAIQWSIFTILLLVACSAF---IR 874
Cdd:cd17320  208 LALGLSFAGLFAYLAAAPFIYIEQLglspaqFGLLFALNAIALILGSLLNGRLVRRFGPRRLLRLGLLLLLAAALvllLA 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997 875 TAFLFGSIAGWMAATALIFFFVAplidLVMPNfhFTNPVTDVYlsiqygnGDHFG--MGVIGLVILTVLFMAIPLVTKLW 952
Cdd:cd17320  288 ALLGGLSLWPLVAPLFLIFFGFG----LIFPN--ATSLALEPF-------PHVAGtaSALLGFLQFLIGALAGALVGLLP 354
PRK01156 PRK01156
chromosome segregation protein; Provisional
 444-726 2.22e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 41.81  E-value: 2.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997 444 QPDTGNKNSSQDDLKALSTRLDEVKKKIQEKASAHNDELKDK------VSQMSKELEKLTKKVEKLEKMfLWLQDRYNVI 517
Cdd:PRK01156 179 RAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIerlsieYNNAMDDYNNLKSALNELSSL-EDMKNRYESE 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997 518 PNEIKNQESTILSKVKELKRRNSPIGEAFNDNLFEKKfetksTRTKKLMEYSNQLSQLELMIANVYQPSNnsslydaKEE 597
Cdd:PRK01156 258 IKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNR-----NYINDYFKYKNDIENKKQILSNIDAEIN-------KYH 325

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997 598 NIQSILSIKKEETENWDTLKKQMltsnDDVSTFIDEMQKFSDGYAEYIStqqaSMEQELNTISESADNVaEQMADQGDAV 677
Cdd:PRK01156 326 AIIKKLSVLQKDYNDYIKKKSRY----DDLNNQILELEGYEMDYNSYLK----SIESLKKKIEEYSKNI-ERMSAFISEI 396

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 489305997 678 YTADLAGSSIVVSAQDSIGQEVLRLSENMSSLTDRQKGVADYTNNIEES 726
Cdd:PRK01156 397 LKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRN 445
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 459-562 3.69e-03

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 40.48  E-value: 3.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997 459 ALSTRLDEVKKKIQ------EKASAHNDELKDKVSQMSKELEKLTKKVEKLEKMFLWLQDRYNVIPNEIKNQESTILSKV 532
Cdd:COG4026  132 ELREELLELKEKIDeiakekEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLKKRLLEV 211

                         90       100       110
                 ....*....|....*....|....*....|
gi 489305997 533 KELKrrnSPIGEAFNDNLFEKKFETKSTRT 562
Cdd:COG4026  212 FSLE---ELWKELFPEELPEEDFIYFATEN 238
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 82-395 4.92e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 40.80  E-value: 4.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   82 NRSAAENGLKSRKYDAVLyipsdfSKNVLSYDKDHPEKasiqfsIQDQLNsvnkeKVQRELENAQKKMNEQMstlyWSfv 161
Cdd:PTZ00108 1075 DEDDEEELGAAVSYDYLL------SMPIWSLTKEKVEK------LNAELE-----KKEKELEKLKNTTPKDM----WL-- 1131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997  162 sQEIGNVREEFEHIVGKEVEFQNTMYNFYKPNSNKLSD-AVQQQKKQIEELKNAMTDSQKQYKDGLST--------TEEA 232
Cdd:PTZ00108 1132 -EDLDKFEEALEEQEEVEEKEIAKEQRLKSKTKGKASKlRKPKLKKKEKKKKKSSADKSKKASVVGNSkrvdsdekRKLD 1210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997  233 KSQLKGFVKVVDQYQQYQDKQKDLLIKAQSTNQKQIQQGLKQLADIQNQNARSFSDQMGGLKTDINGVQS-----QLNTT 307
Cdd:PTZ00108 1211 DKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAvqyspPPPSK 1290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997  308 DSAIQSVQKSREDAIPKQSTGltKLVQESQEELIKKYEERYLEDYRNKISAlQTKLLAKRQELMDEPEPPV-----DSED 382
Cdd:PTZ00108 1291 RPDGESNGGSKPSSPTKKKVK--KRLEGSLAALKKKKKSEKKTARKKKSKT-RVKQASASQSSRLLRRPRKkksdsSSED 1367

                         330
                  ....*....|...
gi 489305997  383 DGPSDQDNENPEE 395
Cdd:PTZ00108 1368 DDDSEVDDSEDED 1380
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 455-787 9.25e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 9.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   455 DDLKALSTRLDEVKKKIQEKASAHNdELKDKVSQMSKELEKLTKKVEKLEKMFLWLQDRYNVIPNEIKNQESTILSKVKE 534
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEEELE-ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   535 LKR--RNSPIGEAFNDNLFEKKFETKstrtKKLMEYSNQLSQLElmianvyqpsnnsSLYDAKEENIQSILSIKKEETEN 612
Cdd:TIGR02168  311 LANleRQLEELEAQLEELESKLDELA----EELAELEEKLEELK-------------EELESLEAELEELEAELEELESR 373

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   613 WDTLKKQMLTSNDDVSTFIDEMQKfsdgyaeyISTQQASMEQELNTISESADNVAEQMADQGDAVYTADLAgssivvSAQ 692
Cdd:TIGR02168  374 LEELEEQLETLRSKVAQLELQIAS--------LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK------ELQ 439

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   693 DSIGQEVLRLSENMSSLTDRQKGVADYTNNIEESVTTVQEKADTLNENWSKnVHSTKLVQQDLkgilgntlsdQGNSNYV 772
Cdd:TIGR02168  440 AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR-LDSLERLQENL----------EGFSEGV 508

                          330
                   ....*....|....*
gi 489305997   773 YNHLANPLKISGDVP 787
Cdd:TIGR02168  509 KALLKNQSGLSGILG 523
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 265-574 9.35e-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: 39.81  E-value: 9.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997  265 QKQIQQGLKQLADIQNQnarsfsdqMGGLKTDINGVQSQLNTTDSAIQSVqksrEDAIPKQSTGLTKLVQESQEELIKKY 344
Cdd:pfam10174 400 QKKIENLQEQLRDKDKQ--------LAGLKERVKSLQTDSSNTDTALTTL----EEALSEKERIIERLKEQREREDRERL 467

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997  345 EE-----RYLEDYRNKISALQTKLLAKRQELMDEPEPpVDSEDDGPSDQDNEnpeeiginldeetneLSQISIEMndlad 419
Cdd:pfam10174 468 EEleslkKENKDLKEKVSALQPELTEKESSLIDLKEH-ASSLASSGLKKDSK---------------LKSLEIAV----- 526

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997  420 qlgEQETPPSTGDGEEGEAGENPAQPDTGNKNSSqDDLKALStrlDEVKKKIQE--KASAHNDELKDKVSQMSKELEKLT 497
Cdd:pfam10174 527 ---EQKKEECSKLENQLKKAHNAEEAVRTNPEIN-DRIRLLE---QEVARYKEEsgKAQAEVERLLGILREVENEKNDKD 599

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489305997  498 KKVEKLEKMFLWLQDRYNVIPNEIKnqestilSKVKELKRRNSPIGEafnDNLFEKKFETKSTRTKKLMEYSNQLSQ 574
Cdd:pfam10174 600 KKIAELESLTLRQMKEQNKKVANIK-------HGQQEMKKKGAQLLE---EARRREDNLADNSQQLQLEELMGALEK 666
 
Name Accession Description Interval E-value
T7_esaA_Nterm TIGR03929
type VII secretion protein EsaA, N-terminal domain; Members of this family are associated with ...
 11-201 1.98e-85

type VII secretion protein EsaA, N-terminal domain; Members of this family are associated with type VII secretion of WXG100 family targets in the Firmicutes, but not in the Actinobacteria. This model represents the conserved N-terminal domain.


Pssm-ID: 274861 [Multi-domain]  Cd Length: 193  Bit Score: 272.36  E-value: 1.98e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   11 IVSTMILILVLPVLFFHLIGDDPAKQKKN--ATRNIAVVNEDMGASESENTARFGQDVVAALSERPDYTWTVVNRSAAEN 88
Cdd:TIGR03929   1 LIFLVLFIVLLPGLFFLAIGQNPKKQKTNqnAKMNIAVVNEDQGVSFDGKTYNFGASFVKAIERDNSQEWSVVSRGAAEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   89 GLKSRKYDAVLYIPSDFSKNVLSYDKDHPEKASIQFSIQDQLNSVNKEKVQRELENAQKKMNEQMSTLYWSFVSQEIGNV 168
Cdd:TIGR03929  81 GLKNNTYDAVVYIPSDFSKKVLSVNKENPEKATIQYKVNANGNAVLKEEAQREAEDILNDFNSQMSDLYWASILQNLQTA 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 489305997  169 REEFEHIVGKEVEFQNTMYNFYKPNSNKLSDAV 201
Cdd:TIGR03929 161 QDNVQAIVNKEAEFQSTYYKNYLPSSANLTNQF 193
YhgE COG1511
Uncharacterized membrane protein YhgE, phage infection protein (PIP) family [Function unknown]; ...
 15-162 6.17e-33

Uncharacterized membrane protein YhgE, phage infection protein (PIP) family [Function unknown];


Pssm-ID: 441120  Cd Length: 225  Bit Score: 127.37  E-value: 6.17e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997  15 MILILVLPVLFFHLIG---DDPAKQKKNATrnIAVVNEDMGASESENTARFGQDVVAALSERPDYTWTVVNRSAAENGLK 91
Cdd:COG1511   18 LIALILVPLLYAGLYLwafWDPYGNLDNLP--VAVVNEDKGATVDGKTVNLGDELVDELKDNDSFDWQFVSEEEAEKGLK 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489305997  92 SRKYDAVLYIPSDFSKNVLSYDKDHPEKASIQFSIQDQLNSVNKEKVQRELENAQKKMNEQMSTLYWSFVS 162
Cdd:COG1511   96 DGKYYAVIVIPEDFSANLASLLSDDPEKATITYYTNEANNYLASKITDTAATTVVDQVNSQVTETYAETVS 166
pip_yhgE_Nterm TIGR03061
YhgE/Pip N-terminal domain; This family contains the N-terminal domain of a family of multiple ...
 6-157 4.53e-20

YhgE/Pip N-terminal domain; This family contains the N-terminal domain of a family of multiple membrane-spanning proteins of Gram-positive bacteria. One member was shown to be a host protein essential for phage infection, so many members of this family are called "phage infection protein". A separate model, TIGR03062, represents the conserved C-terminal domain. The domains are separated by regions highly variable in both length and sequence, often containing extended heptad repeats as described in model TIGR03057.


Pssm-ID: 274413 [Multi-domain]  Cd Length: 164  Bit Score: 88.03  E-value: 4.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997    6 KSSIKIVsTMILILVLPVLF--FHLIGD-DPAKQkknaTRNI--AVVNEDMGASESENTARFGQDVVAALSERPDYTWTV 80
Cdd:TIGR03061   8 KNKLLRI-ALIAIMLIPLLYggLFLWAFwDPYGN----LDNLpvAVVNEDKGATYDGKTLNAGDDLVKELKKNDDLDWHF 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489305997   81 VNRSAAENGLKSRKYDAVLYIPSDFSKNVLSYDKDHPEKASIQFSIQDQLNSVNKEKVQRELENAQKKMNEQMSTLY 157
Cdd:TIGR03061  83 VSAKEAEKGLADGKYYMVITIPEDFSENATSLLDDQPKKAQLIYKTNDANNYIASQIAESAAEKVKTSVSKSITETY 159
NatB COG1668
ABC-type Na+ efflux pump, permease component NatB [Energy production and conversion, Inorganic ...
 6-150 2.31e-06

ABC-type Na+ efflux pump, permease component NatB [Energy production and conversion, Inorganic ion transport and metabolism];


Pssm-ID: 441274 [Multi-domain]  Cd Length: 402  Bit Score: 51.06  E-value: 2.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   6 KSSIKIVSTMILILVLPVLFFHLIG--DDPAKQKKNATRNIAVVNEDmgasesentarFGQDVVAALSERP---DYTWTV 80
Cdd:COG1668   13 KERLRDKSFLISTLLLPLLLVPLLGlgMLFMSGNDDEPLKVAVVDES-----------GAPALAEALKEAAvnfEVVPEV 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997  81 VNRSAAENGLKSRKYDAVLYIPSDFSKNvlsydkdhpEKASIQFSIQDQLNSVNKEKVQRELENAQKKMN 150
Cdd:COG1668   82 ADEEEAEAAVEDGEIDAVLVIPEDFSLE---------NPATVELYSDSSPDSSAVSRLESALSQALLALR 142
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 302-576 2.54e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.61  E-value: 2.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   302 SQLNTTDSAIQSVQKSReDAIPKQSTGLTKLVQESQEELIKKyeERYLEDYRNKISAL----QTKLLAKRQELMDEPEPP 377
Cdd:TIGR02169  230 KEKEALERQKEAIERQL-ASLEEELEKLTEEISELEKRLEEI--EQLLEELNKKIKDLgeeeQLRVKEKIGELEAEIASL 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   378 VDSEDDgpSDQDNENPEEIGINLDEETNELSQisiEMNDLADQLGEQEtppstgdgeegeagenpaqpdtGNKNSSQDDL 457
Cdd:TIGR02169  307 ERSIAE--KERELEDAEERLAKLEAEIDKLLA---EIEELEREIEEER----------------------KRRDKLTEEY 359

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   458 KALSTRLDEVKKKIQEKaSAHNDELKDKVSQMSKELEKLTKKVEKLEKMFLWLQDRYNVIPNE---IKNQESTILSKVKE 534
Cdd:TIGR02169  360 AELKEELEDLRAELEEV-DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEladLNAAIAGIEAKINE 438

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 489305997   535 LKRRNSPIGEAFndnlfeKKFETKSTRTKKLME-YSNQLSQLE 576
Cdd:TIGR02169  439 LEEEKEDKALEI------KKQEWKLEQLAADLSkYEQELYDLK 475
ABC2_membrane_3 pfam12698
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ...
 13-156 9.95e-06

ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.


Pssm-ID: 463674 [Multi-domain]  Cd Length: 345  Bit Score: 48.93  E-value: 9.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   13 STMILILVLPVLF-------FHLIGDDPAKQKknatrnIAVVNEDmgasesenTARFGQDVVAALSERP--DYTWTVVNR 83
Cdd:pfam12698   2 SFLIITLLLPILLilllgliFSNAVNDPEELP------VAVVDED--------NSSLSRQLVRALEASPtvNLVQYVDSE 67

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489305997   84 SAAENGLKSRKYDAVLYIPSDFSKNVLSYdkdhpEKASIQFSIQDQLNSVNKEkVQRELENAQKKMNEQMSTL 156
Cdd:pfam12698  68 EEAKEALKNGKIDGLLVIPKGFSKDLLKG-----ESATVTVYINSSNLLVSKL-ILNALQSLLQQLNASALVL 134
ABC_export pfam16962
Putative ABC exporter; This is a family of putative ABC_exporters from Firmicutes.
 804-945 2.21e-04

Putative ABC exporter; This is a family of putative ABC_exporters from Firmicutes.


Pssm-ID: 435677  Cd Length: 530  Bit Score: 44.96  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997  804 MISSLLIGFFSSYYaaAPMLVKG---------ALFGILNLLVGLMISLFGLNIYKLADD----QAIQWSIFTILLLVACS 870
Cdd:pfam16962 118 MLTSLLVGLFAIFQ--IPNLVNGfgltmggivALLLGITLLLILLGSVIILLIYSFTSKepkrKKIVKGIIVLLGVLLLA 195

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489305997  871 AFIRTAFLFGsiAGWMAATALIFFFVAPLIDLVmpnfhftnPV----TDVYLSIQYGNGDHFGMGVIGLVILTVLFMAI 945
Cdd:pfam16962 196 AVLFAIQLFS--NGGNLLEGLLAFITSPWFSYI--------PIigwtKALIMALLSGIWLSFLVYLVLLLLSLALLILL 264
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
311-576 3.47e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 3.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997 311 IQSVQKSRE--DAIPKQSTGLTKL--VQESQEELIK--KYEERYLEDYRNKISALQTKLLAKRQELMDepeppVDSEDDG 384
Cdd:PRK03918 137 IDAILESDEsrEKVVRQILGLDDYenAYKNLGEVIKeiKRRIERLEKFIKRTENIEELIKEKEKELEE-----VLREINE 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997 385 PSDQDNENPEEIGiNLDEETNELSQISIEMNDLADQLGEQEtppstgdgeegeagenpaqpdtGNKNSSQDDLKALSTRL 464
Cdd:PRK03918 212 ISSELPELREELE-KLEKEVKELEELKEEIEELEKELESLE----------------------GSKRKLEEKIRELEERI 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997 465 DEVKKKIQekasahndELKDKVSQMsKELEKLTKKVEKLEKmflwLQDRYNVIPNEIKNQESTILSKVKELKRRnspIGE 544
Cdd:PRK03918 269 EELKKEIE--------ELEEKVKEL-KELKEKAEEYIKLSE----FYEEYLDELREIEKRLSRLEEEINGIEER---IKE 332

                        250       260       270
                 ....*....|....*....|....*....|..
gi 489305997 545 AfndnlfEKKFETKSTRTKKLMEYSNQLSQLE 576
Cdd:PRK03918 333 L------EEKEERLEELKKKLKELEKRLEELE 358
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 125-548 5.75e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.86  E-value: 5.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997  125 SIQDQLNSVNKEK--VQRELENAQKKMNEQMSTLywSFVSQEIGNVREEFEHIVGKEVEFQNTMYNFYKPNSNkLSDAVQ 202
Cdd:TIGR04523 215 SLESQISELKKQNnqLKDNIEKKQQEINEKTTEI--SNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE-LEKQLN 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997  203 QQKKQIEELKN-AMTDSQKQYKDGLSTTE----EAKSQLKGFVKVVDQYQQYQDKQKDLLIKAQSTN---QKQIQQGLKQ 274
Cdd:TIGR04523 292 QLKSEISDLNNqKEQDWNKELKSELKNQEkkleEIQNQISQNNKIISQLNEQISQLKKELTNSESENsekQRELEEKQNE 371

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997  275 LADIQNQNArSFSDQMGGLKTDINGVQSQL-------NTTDSAIQSVQKSREdAIPKQSTGLTKLVQESQEEL------- 340
Cdd:TIGR04523 372 IEKLKKENQ-SYKQEIKNLESQINDLESKIqnqeklnQQKDEQIKKLQQEKE-LLEKEIERLKETIIKNNSEIkdltnqd 449

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997  341 ------------IKKYEERYLEDYRNKISALQTKLLAKRQELmDEPEPPVDSEDDGPSDQDNENPE------EIGINLDE 402
Cdd:TIGR04523 450 svkeliiknldnTRESLETQLKVLSRSINKIKQNLEQKQKEL-KSKEKELKKLNEEKKELEEKVKDltkkisSLKEKIEK 528

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997  403 ETNELSQISIEMNDLADQLGEQETppstgdgeegEAGENPAQPDTGNKNSSQDDLKALSTRLDEVKKKIQEKAsahnDEL 482
Cdd:TIGR04523 529 LESEKKEKESKISDLEDELNKDDF----------ELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELI----DQK 594

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489305997  483 KDKVSQMSKELEKLTKKVEKLEKMFLWLQDRYNVIPNEIKNQESTILSKVKELKRRNSPIGEAFND 548
Cdd:TIGR04523 595 EKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNK 660
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 454-725 5.81e-04

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.95  E-value: 5.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   454 QDDLKALSTrldEVKKKIQEKASAHNDELKDKVSQMSKELEKLTKKVEKLEKMFLWLQDRYNVIPNEIKNQESTILSKVK 533
Cdd:pfam15921  244 EDQLEALKS---ESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLS 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   534 ELK----RRNSPIGEA---FNDNL--FEKKF--------ETKSTRTKKLMEYSNQLSQLELMIANVYQPSNNSSLydAKE 596
Cdd:pfam15921  321 DLEstvsQLRSELREAkrmYEDKIeeLEKQLvlanseltEARTERDQFSQESGNLDDQLQKLLADLHKREKELSL--EKE 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   597 ENiQSILSIKKEETENWDTLKKQMltsnDDVSTfidEMQKFSDGYAEYISTQQASMEQELNTI---SESADNVAEqmadq 673
Cdd:pfam15921  399 QN-KRLWDRDTGNSITIDHLRREL----DDRNM---EVQRLEALLKAMKSECQGQMERQMAAIqgkNESLEKVSS----- 465

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 489305997   674 gdavYTADLAgssivvSAQDSIGQEVLRLSENMSSLTDRQKGVADYTNNIEE 725
Cdd:pfam15921  466 ----LTAQLE------STKEMLRKVVEELTAKKMTLESSERTVSDLTASLQE 507
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 123-737 5.86e-04

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.95  E-value: 5.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   123 QFSIQDQL-NSVNKEKVQREL-ENAQKKMNEQMSTLYWSFVS-----QEIGNVREEFEHIVGKEVEFQNTMYNF-YKPNS 194
Cdd:pfam15921  140 QEDLRNQLqNTVHELEAAKCLkEDMLEDSNTQIEQLRKMMLShegvlQEIRSILVDFEEASGKKIYEHDSMSTMhFRSLG 219

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   195 NKLSDAVQQQKKQIEELKNAMTDSQKQYkDGLSTTEEAKSQ--LKGFVKVVDQYQQYQDKQKDLLIKAQSTNQKQIQQGL 272
Cdd:pfam15921  220 SAISKILRELDTEISYLKGRIFPVEDQL-EALKSESQNKIEllLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQ 298

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   273 KQLADIQNQNARSFSDQMGGLkTDINGVQSQLNttdSAIQSVQKSREDAIPKqstgLTKLVQESQEELIKKYEER--YLE 350
Cdd:pfam15921  299 SQLEIIQEQARNQNSMYMRQL-SDLESTVSQLR---SELREAKRMYEDKIEE----LEKQLVLANSELTEARTERdqFSQ 370

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   351 DYRNKISALQtKLLA----KRQELMDEPEppvdsEDDGPSDQDNENpeeiGINLDEETNELSQISIEMNDLADQLGEQET 426
Cdd:pfam15921  371 ESGNLDDQLQ-KLLAdlhkREKELSLEKE-----QNKRLWDRDTGN----SITIDHLRRELDDRNMEVQRLEALLKAMKS 440

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   427 PPSTGDGEEGEAGEnpaqpdtgNKNSSQDDLKALSTRLDEVK---KKIQEKASAHNDELKDK---VSQMSKELEKLTKKV 500
Cdd:pfam15921  441 ECQGQMERQMAAIQ--------GKNESLEKVSSLTAQLESTKemlRKVVEELTAKKMTLESSertVSDLTASLQEKERAI 512

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   501 EKLEKMFLWLQDRYNVIPNE---IKNQESTILS----------------KVKELKRRN---------------------- 539
Cdd:pfam15921  513 EATNAEITKLRSRVDLKLQElqhLKNEGDHLRNvqtecealklqmaekdKVIEILRQQienmtqlvgqhgrtagamqvek 592

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   540 SPIGEAFNDNLFE-KKFET-KSTRTKKLMEYSNQLSQLELmianvyqpsNNSSLYDAKEENIQSILSIKKEEtenwDTLK 617
Cdd:pfam15921  593 AQLEKEINDRRLElQEFKIlKDKKDAKIRELEARVSDLEL---------EKVKLVNAGSERLRAVKDIKQER----DQLL 659

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   618 KQMLTSNDDVSTFI--------------DEMQKFSDGYAEYISTQQASMEQELNTIS--ESADNVAEQMAdqgdavytad 681
Cdd:pfam15921  660 NEVKTSRNELNSLSedyevlkrnfrnksEEMETTTNKLKMQLKSAQSELEQTRNTLKsmEGSDGHAMKVA---------- 729

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   682 lAGSSIVVSAQ----DSIGQEVLRLSENMSSLTDRQKGVADYTNNIEESVTTVQEKADTL 737
Cdd:pfam15921  730 -MGMQKQITAKrgqiDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKM 788
PRK11020 PRK11020
YibL family ribosome-associated protein;
454-503 1.76e-03

YibL family ribosome-associated protein;


Pssm-ID: 182904 [Multi-domain]  Cd Length: 118  Bit Score: 39.23  E-value: 1.76e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 489305997 454 QDDLKALSTRLDEVKKKiQEKASAHNDelKDKVSQMSKELEKLTKKVEKL 503
Cdd:PRK11020   4 KNEIKRLSDRLDAIRHK-LAAASLRGD--AEKYAQFEKEKATLEAEIARL 50
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
126-656 2.14e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 2.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997 126 IQDQLNSVNKE--KVQRELENAQKKMNEQMSTLywSFVSQEIGNVREEFEHIVGKEVEFQNTmynfyKPNSNKLSDAVQQ 203
Cdd:PRK03918 191 IEELIKEKEKEleEVLREINEISSELPELREEL--EKLEKEVKELEELKEEIEELEKELESL-----EGSKRKLEEKIRE 263

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997 204 QKKQIEELKNAMTDSQKQYKDGLSTTEEAK--SQLKGFVKVVDQYQQYqdkqkdlLIKAQSTNQKQIQQGLKQLADIQNQ 281
Cdd:PRK03918 264 LEERIEELKKEIEELEEKVKELKELKEKAEeyIKLSEFYEEYLDELRE-------IEKRLSRLEEEINGIEERIKELEEK 336

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997 282 NARsfsdqMGGLKTDINGVQSQLNTTDSAIQSVQKSRedAIPKQSTGL-TKLVQESQEELIKKYEE-----RYLEDYRNK 355
Cdd:PRK03918 337 EER-----LEELKKKLKELEKRLEELEERHELYEEAK--AKKEELERLkKRLTGLTPEKLEKELEElekakEEIEEEISK 409

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997 356 ISALQTKLLAKRQELMDEPEPPVDSEDDGP---SDQDNENPEEIginLDEETNELSQISIEMNDLADQLGEQEtppstgD 432
Cdd:PRK03918 410 ITARIGELKKEIKELKKAIEELKKAKGKCPvcgRELTEEHRKEL---LEEYTAELKRIEKELKEIEEKERKLR------K 480

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997 433 GEEGEAGENPAQPDTGNKNSSQDDLKALSTRLDEVKKKIQEKASAHNDELKDKVSQMSKELEKLTKKVEKLEkmflwlqd 512
Cdd:PRK03918 481 ELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE-------- 552

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997 513 rynvipnEIKNQESTILSKVKELKRRNSPIgeafNDNLFEKKFETkstrtkkLMEYSNQLSQLElMIANVYqpsnnSSLY 592
Cdd:PRK03918 553 -------ELKKKLAELEKKLDELEEELAEL----LKELEELGFES-------VEELEERLKELE-PFYNEY-----LELK 608

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489305997 593 DAKEEnIQSIL-SIKKEETENWDTLKKQMLTSND--DVSTFIDEMQK-FSDGYAEYISTQQASMEQEL 656
Cdd:PRK03918 609 DAEKE-LEREEkELKKLEEELDKAFEELAETEKRleELRKELEELEKkYSEEEYEELREEYLELSREL 675
MFS_MdfA_MDR_like cd17320
Multidrug transporter MdfA and similar multidrug resistance (MDR) transporters of the Major ...
 804-952 2.18e-03

Multidrug transporter MdfA and similar multidrug resistance (MDR) transporters of the Major Facilitator Superfamily; This family is composed of bacterial multidrug resistance (MDR) transporters including several proteins from Escherichia coli such as MdfA (also called chloramphenicol resistance pump Cmr), EmrD, MdtM, MdtL, bicyclomycin resistance protein (also called sulfonamide resistance protein), and the uncharacterized inner membrane transport protein YdhC. EmrD is a proton-dependent secondary transporter, first identified as an efflux pump for uncouplers of oxidative phosphorylation. It expels a range of drug molecules and amphipathic compounds across the inner membrane of E. coli. Similarly, MdfA is a secondary multidrug transporter that exports a broad spectrum of structurally and electrically dissimilar toxic compounds. These MDR transporters are drug/H+ antiporters (DHA) belonging to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 340878 [Multi-domain]  Cd Length: 379  Bit Score: 41.41  E-value: 2.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997 804 MISSLLIGFFSSYYAAAPMLVKGAL------FGILNLLVGLMISLFGLNIYKLADDQAIQWSIFTILLLVACSAF---IR 874
Cdd:cd17320  208 LALGLSFAGLFAYLAAAPFIYIEQLglspaqFGLLFALNAIALILGSLLNGRLVRRFGPRRLLRLGLLLLLAAALvllLA 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997 875 TAFLFGSIAGWMAATALIFFFVAplidLVMPNfhFTNPVTDVYlsiqygnGDHFG--MGVIGLVILTVLFMAIPLVTKLW 952
Cdd:cd17320  288 ALLGGLSLWPLVAPLFLIFFGFG----LIFPN--ATSLALEPF-------PHVAGtaSALLGFLQFLIGALAGALVGLLP 354
PRK01156 PRK01156
chromosome segregation protein; Provisional
 444-726 2.22e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 41.81  E-value: 2.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997 444 QPDTGNKNSSQDDLKALSTRLDEVKKKIQEKASAHNDELKDK------VSQMSKELEKLTKKVEKLEKMfLWLQDRYNVI 517
Cdd:PRK01156 179 RAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIerlsieYNNAMDDYNNLKSALNELSSL-EDMKNRYESE 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997 518 PNEIKNQESTILSKVKELKRRNSPIGEAFNDNLFEKKfetksTRTKKLMEYSNQLSQLELMIANVYQPSNnsslydaKEE 597
Cdd:PRK01156 258 IKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNR-----NYINDYFKYKNDIENKKQILSNIDAEIN-------KYH 325

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997 598 NIQSILSIKKEETENWDTLKKQMltsnDDVSTFIDEMQKFSDGYAEYIStqqaSMEQELNTISESADNVaEQMADQGDAV 677
Cdd:PRK01156 326 AIIKKLSVLQKDYNDYIKKKSRY----DDLNNQILELEGYEMDYNSYLK----SIESLKKKIEEYSKNI-ERMSAFISEI 396

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 489305997 678 YTADLAGSSIVVSAQDSIGQEVLRLSENMSSLTDRQKGVADYTNNIEES 726
Cdd:PRK01156 397 LKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRN 445
MATE_Wzx_like cd13128
Wzx, a subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins; ...
 805-948 2.55e-03

Wzx, a subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins; Escherichia coli Wzx and related proteins from other gram-negative bacteria are thought to act as flippases, assisting in the membrane translocation of lipopolysaccharides including those containing O-antigens. Proteins from the MATE family are involved in exporting metabolites across the cell membrane and are often responsible for multidrug resistance (MDR).


Pssm-ID: 240533 [Multi-domain]  Cd Length: 402  Bit Score: 41.37  E-value: 2.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997 805 ISSLLIGFFSSYYAAAPMLVKGalFGILNL---LVGL--MISLFGLN------IYKLADDQA--IQWSIFTILLLVACSA 871
Cdd:cd13128   13 IISKLLGFLVRVYLARYLGPEG--FGILSLalaFVGLfsIFADLGLPtalvreIARYRKEKIreIISTSLVLKLILGILA 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489305997 872 FIRTAFLFGSIAGWMAATALIFFFVAPLIdlvmpnfhFTNPVTDVYLSIQYGNGDhfgMG--VIGLVILTVLFMAIPLV 948
Cdd:cd13128   91 LLLLFLFAFLIAFYDPELVLLLYILALSL--------PFSALNSLFRGIFQGFEK---MKyiVIARIIESVLSLILALI 158
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 459-562 3.69e-03

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 40.48  E-value: 3.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997 459 ALSTRLDEVKKKIQ------EKASAHNDELKDKVSQMSKELEKLTKKVEKLEKMFLWLQDRYNVIPNEIKNQESTILSKV 532
Cdd:COG4026  132 ELREELLELKEKIDeiakekEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLKKRLLEV 211

                         90       100       110
                 ....*....|....*....|....*....|
gi 489305997 533 KELKrrnSPIGEAFNDNLFEKKFETKSTRT 562
Cdd:COG4026  212 FSLE---ELWKELFPEELPEEDFIYFATEN 238
46 PHA02562
endonuclease subunit; Provisional
 481-569 3.98e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.77  E-value: 3.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997 481 ELKDKVSQMSKELEKLTKKVEKLEK---MFLWLQDRYNVIPNEIKNQESTILSKVKELKRRNSPIGEA------------ 545
Cdd:PHA02562 303 KIKDKLKELQHSLEKLDTAIDELEEimdEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELqaefvdnaeela 382

                         90       100
                 ....*....|....*....|....*
gi 489305997 546 -FNDNLfEKKFETKSTRTKKLMEYS 569
Cdd:PHA02562 383 kLQDEL-DKIVKTKSELVKEKYHRG 406
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 82-395 4.92e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 40.80  E-value: 4.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   82 NRSAAENGLKSRKYDAVLyipsdfSKNVLSYDKDHPEKasiqfsIQDQLNsvnkeKVQRELENAQKKMNEQMstlyWSfv 161
Cdd:PTZ00108 1075 DEDDEEELGAAVSYDYLL------SMPIWSLTKEKVEK------LNAELE-----KKEKELEKLKNTTPKDM----WL-- 1131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997  162 sQEIGNVREEFEHIVGKEVEFQNTMYNFYKPNSNKLSD-AVQQQKKQIEELKNAMTDSQKQYKDGLST--------TEEA 232
Cdd:PTZ00108 1132 -EDLDKFEEALEEQEEVEEKEIAKEQRLKSKTKGKASKlRKPKLKKKEKKKKKSSADKSKKASVVGNSkrvdsdekRKLD 1210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997  233 KSQLKGFVKVVDQYQQYQDKQKDLLIKAQSTNQKQIQQGLKQLADIQNQNARSFSDQMGGLKTDINGVQS-----QLNTT 307
Cdd:PTZ00108 1211 DKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAvqyspPPPSK 1290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997  308 DSAIQSVQKSREDAIPKQSTGltKLVQESQEELIKKYEERYLEDYRNKISAlQTKLLAKRQELMDEPEPPV-----DSED 382
Cdd:PTZ00108 1291 RPDGESNGGSKPSSPTKKKVK--KRLEGSLAALKKKKKSEKKTARKKKSKT-RVKQASASQSSRLLRRPRKkksdsSSED 1367

                         330
                  ....*....|...
gi 489305997  383 DGPSDQDNENPEE 395
Cdd:PTZ00108 1368 DDDSEVDDSEDED 1380
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 455-787 9.25e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 9.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   455 DDLKALSTRLDEVKKKIQEKASAHNdELKDKVSQMSKELEKLTKKVEKLEKMFLWLQDRYNVIPNEIKNQESTILSKVKE 534
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEEELE-ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   535 LKR--RNSPIGEAFNDNLFEKKFETKstrtKKLMEYSNQLSQLElmianvyqpsnnsSLYDAKEENIQSILSIKKEETEN 612
Cdd:TIGR02168  311 LANleRQLEELEAQLEELESKLDELA----EELAELEEKLEELK-------------EELESLEAELEELEAELEELESR 373

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   613 WDTLKKQMLTSNDDVSTFIDEMQKfsdgyaeyISTQQASMEQELNTISESADNVAEQMADQGDAVYTADLAgssivvSAQ 692
Cdd:TIGR02168  374 LEELEEQLETLRSKVAQLELQIAS--------LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK------ELQ 439

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997   693 DSIGQEVLRLSENMSSLTDRQKGVADYTNNIEESVTTVQEKADTLNENWSKnVHSTKLVQQDLkgilgntlsdQGNSNYV 772
Cdd:TIGR02168  440 AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR-LDSLERLQENL----------EGFSEGV 508

                          330
                   ....*....|....*
gi 489305997   773 YNHLANPLKISGDVP 787
Cdd:TIGR02168  509 KALLKNQSGLSGILG 523
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 265-574 9.35e-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: 39.81  E-value: 9.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997  265 QKQIQQGLKQLADIQNQnarsfsdqMGGLKTDINGVQSQLNTTDSAIQSVqksrEDAIPKQSTGLTKLVQESQEELIKKY 344
Cdd:pfam10174 400 QKKIENLQEQLRDKDKQ--------LAGLKERVKSLQTDSSNTDTALTTL----EEALSEKERIIERLKEQREREDRERL 467

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997  345 EE-----RYLEDYRNKISALQTKLLAKRQELMDEPEPpVDSEDDGPSDQDNEnpeeiginldeetneLSQISIEMndlad 419
Cdd:pfam10174 468 EEleslkKENKDLKEKVSALQPELTEKESSLIDLKEH-ASSLASSGLKKDSK---------------LKSLEIAV----- 526

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489305997  420 qlgEQETPPSTGDGEEGEAGENPAQPDTGNKNSSqDDLKALStrlDEVKKKIQE--KASAHNDELKDKVSQMSKELEKLT 497
Cdd:pfam10174 527 ---EQKKEECSKLENQLKKAHNAEEAVRTNPEIN-DRIRLLE---QEVARYKEEsgKAQAEVERLLGILREVENEKNDKD 599

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489305997  498 KKVEKLEKMFLWLQDRYNVIPNEIKnqestilSKVKELKRRNSPIGEafnDNLFEKKFETKSTRTKKLMEYSNQLSQ 574
Cdd:pfam10174 600 KKIAELESLTLRQMKEQNKKVANIK-------HGQQEMKKKGAQLLE---EARRREDNLADNSQQLQLEELMGALEK 666
 
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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