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Conserved domains on  [gi|21356121|ref|NP_648929|]
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uncharacterized protein Dmel_CG9951 [Drosophila melanogaster]

Protein Classification

coiled-coil domain-containing 22 family protein( domain architecture ID 708562)

coiled-coil domain-containing 22 (CCDC22) family protein is a DUF812 domain-containing protein that may be involved in regulation of NF-kappa-B signaling

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CCDC22 super family cl25503
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 1-518 1.97e-105

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


The actual alignment was detected with superfamily member pfam05667:

Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 328.91  E-value: 1.97e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121     1 MDEVDKIIMHQLHQVDATIEPT-DELSDFTPEQVVRAVSGCLAEIRPDL--QLPRTLPGGaMAQRFGVASSLAQGCKDSG 77
Cdd:pfam05667   1 MEEVDGIIIHSLRQIGCEIAEDvQSLKDFTTELLVEAVVRCLRVINPDLgiNLPLTLPPG-MSARFRVGTSLAQACQELG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121    78 YRGDIGYQTFLYPNAVELRRLLMFLIEQLPRERQGTEDgasksQTLSHRQLLERKIRKELAQQLKTPWVPQFARSvgNRK 157
Cdd:pfam05667  80 YRGEIGYQTFLYPNEPDIRKILMFLVEKLPRESSEAAD-----QPVGKSAVLQRAIAAAIRSQLAAPWLPPECKP--HQR 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121   158 LLGCSSLGIEFRPNINLNIPSANPEERSKEQQQYLDQQAPNLFQQTSSTsTDLIASVLHKN------------------- 218
Cdd:pfam05667 153 RQGSRALRPFHTQTLVLPGRKGKTLKNSKELKEFYSEYLPPVTAQPSSR-ASVVPSLLERNaaelaaaqeweeewnsqgl 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121   219 ------------------------------------------------ELDRWGQILPDST-------------LIFVSS 237
Cdd:pfam05667 232 asrltpeeyrkrkrtkllkriaeqlrsaalagteatsgasrsaqdlaeLLSSFSGSSTTDTgltkgsrfthtekLQFTNE 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121   238 EDPAPPLIPTVKPPASAEKEEEPSPIQELSDQVQELRVQCENLLAERKAHAVAIAALKQRETKAREEISRIQPTLKLHER 317
Cdd:pfam05667 312 APAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKK 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121   318 TSLVLADSEENLAKLEALLKSTQSKRLTLTQQWQDYRKPLLESLEKLKTAK-----EAQ----EVQGIRNSIEQLEQELL 388
Cdd:pfam05667 392 TLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPLIEEYRALKEAKsnkedESQrkleEIKELREKIKEVAEEAK 471

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121   389 AKTQQHNELNATLRSASQSlAPRKEYTRRIHEFIGNIRKQRADIYKVLDDTRQLQKQLNVVGAQLQRQFNYTDDLLFQSA 468
Cdd:pfam05667 472 QKEELYKQLVAEYERLPKD-VSRSAYTRRILEIVKNIKKQKEEITKILSDTKSLQKEINSLTGKLDRTFTVTDELVFKDA 550

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|
gi 21356121   469 KHDLHAKRAYKLLAQLHANCNELVECVSLTGNVTKQIRELEVQIDGEKLK 518
Cdd:pfam05667 551 KKDESVRKAYKYLAALHENCEQLIQTVEETGTIMREIRDLEEQIETESGK 600
 
Name Accession Description Interval E-value
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 1-518 1.97e-105

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 328.91  E-value: 1.97e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121     1 MDEVDKIIMHQLHQVDATIEPT-DELSDFTPEQVVRAVSGCLAEIRPDL--QLPRTLPGGaMAQRFGVASSLAQGCKDSG 77
Cdd:pfam05667   1 MEEVDGIIIHSLRQIGCEIAEDvQSLKDFTTELLVEAVVRCLRVINPDLgiNLPLTLPPG-MSARFRVGTSLAQACQELG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121    78 YRGDIGYQTFLYPNAVELRRLLMFLIEQLPRERQGTEDgasksQTLSHRQLLERKIRKELAQQLKTPWVPQFARSvgNRK 157
Cdd:pfam05667  80 YRGEIGYQTFLYPNEPDIRKILMFLVEKLPRESSEAAD-----QPVGKSAVLQRAIAAAIRSQLAAPWLPPECKP--HQR 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121   158 LLGCSSLGIEFRPNINLNIPSANPEERSKEQQQYLDQQAPNLFQQTSSTsTDLIASVLHKN------------------- 218
Cdd:pfam05667 153 RQGSRALRPFHTQTLVLPGRKGKTLKNSKELKEFYSEYLPPVTAQPSSR-ASVVPSLLERNaaelaaaqeweeewnsqgl 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121   219 ------------------------------------------------ELDRWGQILPDST-------------LIFVSS 237
Cdd:pfam05667 232 asrltpeeyrkrkrtkllkriaeqlrsaalagteatsgasrsaqdlaeLLSSFSGSSTTDTgltkgsrfthtekLQFTNE 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121   238 EDPAPPLIPTVKPPASAEKEEEPSPIQELSDQVQELRVQCENLLAERKAHAVAIAALKQRETKAREEISRIQPTLKLHER 317
Cdd:pfam05667 312 APAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKK 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121   318 TSLVLADSEENLAKLEALLKSTQSKRLTLTQQWQDYRKPLLESLEKLKTAK-----EAQ----EVQGIRNSIEQLEQELL 388
Cdd:pfam05667 392 TLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPLIEEYRALKEAKsnkedESQrkleEIKELREKIKEVAEEAK 471

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121   389 AKTQQHNELNATLRSASQSlAPRKEYTRRIHEFIGNIRKQRADIYKVLDDTRQLQKQLNVVGAQLQRQFNYTDDLLFQSA 468
Cdd:pfam05667 472 QKEELYKQLVAEYERLPKD-VSRSAYTRRILEIVKNIKKQKEEITKILSDTKSLQKEINSLTGKLDRTFTVTDELVFKDA 550

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|
gi 21356121   469 KHDLHAKRAYKLLAQLHANCNELVECVSLTGNVTKQIRELEVQIDGEKLK 518
Cdd:pfam05667 551 KKDESVRKAYKYLAALHENCEQLIQTVEETGTIMREIRDLEEQIETESGK 600
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 263-554 1.96e-10

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: 63.92  E-value: 1.96e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121    263 IQELSDQVQELRVQCENLLAERKAHAVAIAALKQRETKAREEISRIQptlKLHERTSLVLADSEENLAKLEALLKSTQSK 342
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS---RQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121    343 RLTLTQQwqdyRKPLLESLEKLKTAKEAQEVQgirnsIEQLEQELLAKTQQHNELNATLRSASQSLAPRKEYTRRIHEFI 422
Cdd:TIGR02168  756 LTELEAE----IEELEERLEEAEEELAEAEAE-----IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121    423 GNIRKQRADIYKVLDDTRQLQKQLNVVGAQLQRQFNYTDDLLfqsAKHDLHAKRAYKLLAQLHANCNELvecVSLTGNVT 502
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI---EELESELEALLNERASLEEALALL---RSELEELS 900

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 21356121    503 KQIRELEVQIDG--EKLKNVLTSLQQITGDIQKFEQHIQELQEQIRAVEQTNAG 554
Cdd:TIGR02168  901 EELRELESKRSElrRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLE 954
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 252-456 5.38e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 5.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121 252 ASAEKEEEPSPIQELSDQVQELRVQCENLLAERKAHAVAIAALKQRETKAREEISRIQPtlklhertslVLADSEENLAK 331
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE----------ELEEAEAELAE 362

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121 332 LEALLKSTQSKRLTLTQQWQDYRKPLLESLEKLktAKEAQEVQGIRNSIEQLEQELLAKTQQHNELNATLRSASQSLAPR 411
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAA--AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 21356121 412 KEYTRRIHEFIGNIRKQRADIYKVLDDTRQLQKQLNVVGAQLQRQ 456
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
 
Name Accession Description Interval E-value
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 1-518 1.97e-105

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 328.91  E-value: 1.97e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121     1 MDEVDKIIMHQLHQVDATIEPT-DELSDFTPEQVVRAVSGCLAEIRPDL--QLPRTLPGGaMAQRFGVASSLAQGCKDSG 77
Cdd:pfam05667   1 MEEVDGIIIHSLRQIGCEIAEDvQSLKDFTTELLVEAVVRCLRVINPDLgiNLPLTLPPG-MSARFRVGTSLAQACQELG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121    78 YRGDIGYQTFLYPNAVELRRLLMFLIEQLPRERQGTEDgasksQTLSHRQLLERKIRKELAQQLKTPWVPQFARSvgNRK 157
Cdd:pfam05667  80 YRGEIGYQTFLYPNEPDIRKILMFLVEKLPRESSEAAD-----QPVGKSAVLQRAIAAAIRSQLAAPWLPPECKP--HQR 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121   158 LLGCSSLGIEFRPNINLNIPSANPEERSKEQQQYLDQQAPNLFQQTSSTsTDLIASVLHKN------------------- 218
Cdd:pfam05667 153 RQGSRALRPFHTQTLVLPGRKGKTLKNSKELKEFYSEYLPPVTAQPSSR-ASVVPSLLERNaaelaaaqeweeewnsqgl 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121   219 ------------------------------------------------ELDRWGQILPDST-------------LIFVSS 237
Cdd:pfam05667 232 asrltpeeyrkrkrtkllkriaeqlrsaalagteatsgasrsaqdlaeLLSSFSGSSTTDTgltkgsrfthtekLQFTNE 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121   238 EDPAPPLIPTVKPPASAEKEEEPSPIQELSDQVQELRVQCENLLAERKAHAVAIAALKQRETKAREEISRIQPTLKLHER 317
Cdd:pfam05667 312 APAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKK 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121   318 TSLVLADSEENLAKLEALLKSTQSKRLTLTQQWQDYRKPLLESLEKLKTAK-----EAQ----EVQGIRNSIEQLEQELL 388
Cdd:pfam05667 392 TLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPLIEEYRALKEAKsnkedESQrkleEIKELREKIKEVAEEAK 471

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121   389 AKTQQHNELNATLRSASQSlAPRKEYTRRIHEFIGNIRKQRADIYKVLDDTRQLQKQLNVVGAQLQRQFNYTDDLLFQSA 468
Cdd:pfam05667 472 QKEELYKQLVAEYERLPKD-VSRSAYTRRILEIVKNIKKQKEEITKILSDTKSLQKEINSLTGKLDRTFTVTDELVFKDA 550

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|
gi 21356121   469 KHDLHAKRAYKLLAQLHANCNELVECVSLTGNVTKQIRELEVQIDGEKLK 518
Cdd:pfam05667 551 KKDESVRKAYKYLAALHENCEQLIQTVEETGTIMREIRDLEEQIETESGK 600
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 263-554 1.96e-10

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: 63.92  E-value: 1.96e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121    263 IQELSDQVQELRVQCENLLAERKAHAVAIAALKQRETKAREEISRIQptlKLHERTSLVLADSEENLAKLEALLKSTQSK 342
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS---RQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121    343 RLTLTQQwqdyRKPLLESLEKLKTAKEAQEVQgirnsIEQLEQELLAKTQQHNELNATLRSASQSLAPRKEYTRRIHEFI 422
Cdd:TIGR02168  756 LTELEAE----IEELEERLEEAEEELAEAEAE-----IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121    423 GNIRKQRADIYKVLDDTRQLQKQLNVVGAQLQRQFNYTDDLLfqsAKHDLHAKRAYKLLAQLHANCNELvecVSLTGNVT 502
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI---EELESELEALLNERASLEEALALL---RSELEELS 900

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 21356121    503 KQIRELEVQIDG--EKLKNVLTSLQQITGDIQKFEQHIQELQEQIRAVEQTNAG 554
Cdd:TIGR02168  901 EELRELESKRSElrRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLE 954
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 252-456 5.38e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 5.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121 252 ASAEKEEEPSPIQELSDQVQELRVQCENLLAERKAHAVAIAALKQRETKAREEISRIQPtlklhertslVLADSEENLAK 331
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE----------ELEEAEAELAE 362

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121 332 LEALLKSTQSKRLTLTQQWQDYRKPLLESLEKLktAKEAQEVQGIRNSIEQLEQELLAKTQQHNELNATLRSASQSLAPR 411
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAA--AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 21356121 412 KEYTRRIHEFIGNIRKQRADIYKVLDDTRQLQKQLNVVGAQLQRQ 456
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 263-438 5.52e-06

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 48.00  E-value: 5.52e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121 263 IQELSDQVQELRVQCENLLAERKAHAVAIAALKQRETKAREEISRIQPTLKLHERTslvLADSEENLAKLEALLKSTQSK 342
Cdd:COG1579  12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELE---IEEVEARIKKYEEQLGNVRNN 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121 343 R--LTLTQQwqdyrkplLESLEKLKTAKEaQEVQGIRNSIEQLEQELLAKTQQHNELNATLRSASQSLaprKEYTRRIHE 420
Cdd:COG1579  89 KeyEALQKE--------IESLKRRISDLE-DEILELMERIEELEEELAELEAELAELEAELEEKKAEL---DEELAELEA 156

                       170
                ....*....|....*...
gi 21356121 421 FIGNIRKQRADIYKVLDD 438
Cdd:COG1579 157 ELEELEAEREELAAKIPP 174
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
263-464 3.25e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 3.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121  263 IQELSDQVQELR---------VQCENLLAERKAHAVAIAALKQRETKAREEISRIQPTLKLHERTSL--VLADSEENLAK 331
Cdd:COG4913  227 ADALVEHFDDLErahealedaREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLeaELEELRAELAR 306

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121  332 LEALLKSTQSKRLTLTQQwqdyrkplLESLEKLKTAKEAQEVQGIRNSIEQLEQELLAKTQQHNELNATLRSASQSLAP- 410
Cdd:COG4913  307 LEAELERLEARLDALREE--------LDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAs 378

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21356121  411 -------RKEYTRRIHEFIGNIRKQRADIYKVLDDTRQLQKQLNVVGAQL----QRQFNYTDDLL 464
Cdd:COG4913  379 aeefaalRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIasleRRKSNIPARLL 443
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 312-554 5.59e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 5.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121    312 LKLHER---TSLVLADSEENLAKLEALLKSTQSKRLTLTQQ---WQDYRKpLLESLEKLKTAKEAQEVQGIRNSIEQLEQ 385
Cdd:TIGR02168  168 SKYKERrkeTERKLERTRENLDRLEDILNELERQLKSLERQaekAERYKE-LKAELRELELALLVLRLEELREELEELQE 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121    386 ELLAKTQQHNELNA----------TLRSASQSLAPRK-EYTRRIHEFIGNIRKQRADIYKVLDDTRQLQKQLNVVGAQLQ 454
Cdd:TIGR02168  247 ELKEAEEELEELTAelqeleekleELRLEVSELEEEIeELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121    455 RQFNYTDDLLFQSAKhdlhAKRAYKLLAQLHANCNELV-ECVSLTGNVTKQIRELEVQIDGEKLKNVLTSLQ--QITGDI 531
Cdd:TIGR02168  327 ELESKLDELAEELAE----LEEKLEELKEELESLEAELeELEAELEELESRLEELEEQLETLRSKVAQLELQiaSLNNEI 402

                          250       260
                   ....*....|....*....|...
gi 21356121    532 QKFEQHIQELQEQIRAVEQTNAG 554
Cdd:TIGR02168  403 ERLEARLERLEDRRERLQQEIEE 425
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 252-469 6.16e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.53  E-value: 6.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121 252 ASAEKEEEPSPIQELSDQVQELRVQCENLLAERKAHAVAIAALKQRETKAREEISRIQPTLKlheRTSLVLADSEENLAK 331
Cdd:COG4942  25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA---ELEKEIAELRAELEA 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121 332 LEALLkstqSKRLTLTQQ--WQDYRKPLLES---------LEKLKT-----AKEAQEVQGIRNSIEQLEQELLAKTQQHN 395
Cdd:COG4942 102 QKEEL----AELLRALYRlgRQPPLALLLSPedfldavrrLQYLKYlaparREQAEELRADLAELAALRAELEAERAELE 177

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21356121 396 ELNATLRSASQSLAP-RKEYTRRIHEFIGNIRKQRADIYKVLDDTRQLQKQLNVVGAQLQRQFNYTDDLLFQSAK 469
Cdd:COG4942 178 ALLAELEEERAALEAlKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 258-552 6.62e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.83  E-value: 6.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121    258 EEPSPIQELSDQVQELRVQCENLLAERKAHAVAIAALKQRETKAREEISRIQPTLKLHERTslvLADSEENLAKLEALLK 337
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQE---EEKLKERLEELEEDLS 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121    338 STQSKRLTLTQQWQDYRK---PLLESLEKLKTAKEAQEVQGIRNSIEQLEQELLAKTQQHNELNATLRSASQSL------ 408
Cdd:TIGR02169  748 SLEQEIENVKSELKELEArieELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLnrltle 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121    409 -------------------APRKEYTRRIHEFIGNIRKQRADIYKVLDDTRQLQKQLnvvgAQLQRQFNytddllfqsaK 469
Cdd:TIGR02169  828 keylekeiqelqeqridlkEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL----GDLKKERD----------E 893

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121    470 HDLHAKRAYKLLAQLHANCNELVECVSLTgNVTKQIRELEV-QIdgEKLKNVLTSLQQITGDIQKFEQHIQELQEQIRAV 548
Cdd:TIGR02169  894 LEAQLRELERKIEELEAQIEKKRKRLSEL-KAKLEALEEELsEI--EDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970


                   ....
gi 21356121    549 EQTN 552
Cdd:TIGR02169  971 EPVN 974
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 263-550 2.58e-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: 43.89  E-value: 2.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121    263 IQELSDQVQELRVQCENLLAERKAHAVAIAALKQRETKAREEISRIQPTLKLHERTslvLADSEENLAKLEALLKSTQSK 342
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE---ISRLEQQKQILRERLANLERQ 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121    343 RLTLTQQWQDYRKPLLESLEKLKT-AKEAQEVQGIRNSIEQLEQELLAKTQQHNELNATLRSASQSLAprkeytRRIHEF 421
Cdd:TIGR02168  318 LEELEAQLEELESKLDELAEELAElEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR------SKVAQL 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121    422 IGNIRKQRADIykvlddtRQLQKQLNVVGAQLQRQFNYTDDLLFQSAKHDLHAKRAYklLAQLHANCNELVECVSLTGNV 501
Cdd:TIGR02168  392 ELQIASLNNEI-------ERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAE--LEELEEELEELQEELERLEEA 462

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 21356121    502 TKQIRELEVQIDGE--KLKNVLTSLQQITGDIQKFEQHIQELQEQIRAVEQ 550
Cdd:TIGR02168  463 LEELREELEEAEQAldAAERELAQLQARLDSLERLQENLEGFSEGVKALLK 513
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 365-550 6.96e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.06  E-value: 6.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121 365 KTAKEAQEVQGIRNSIEQLEQELLAKTQQHNELNATLRSASQSLAprkEYTRRIHEFIGNIRKQRADIykvlddtRQLQK 444
Cdd:COG4942  21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA---ALARRIRALEQELAALEAEL-------AELEK 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121 445 QLNVVGAQLQRQFNYTDDLLFQSAKHDLHAKRAYKLLAQlhaNCNELVECVSLTGNVTKQIRELEVQIDgEKLKNVLTSL 524
Cdd:COG4942  91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPE---DFLDAVRRLQYLKYLAPARREQAEELR-ADLAELAALR 166

                       170       180
                ....*....|....*....|....*.
gi 21356121 525 QQITGDIQKFEQHIQELQEQIRAVEQ 550
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEA 192
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
254-447 8.90e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.43  E-value: 8.90e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121 254 AEKEEEPSPIQELSDQVQELRVQCENLLAERKAHAVAIAALKQRETKAREEISRIQPTLKLHERTSLVLADSEENLAKL- 332
Cdd:COG1340  36 EELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLr 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121 333 ---EALLKSTQSKRLTLTQQWQ--DYRKPLLESLEKLKTAKEA--------QEVQGIRNSIEQLEQELLAKTQQ----HN 395
Cdd:COG1340 116 keiERLEWRQQTEVLSPEEEKElvEKIKELEKELEKAKKALEKneklkelrAELKELRKEAEEIHKKIKELAEEaqelHE 195

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 21356121 396 ELNATLRSASQSLAPRKEYTRRIHEFIGNIRKQRADIYKVLDDTRQLQKQLN 447
Cdd:COG1340 196 EMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELK 247
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
263-404 1.42e-03

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 40.19  E-value: 1.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121 263 IQELSDQVQELRVQCenllaerkahAVAIAALKQRETKAREEISRIQptlKLHERTSLVLADSEENLAKlEAL--LKSTQ 340
Cdd:COG1842  32 IRDMEEDLVEARQAL----------AQVIANQKRLERQLEELEAEAE---KWEEKARLALEKGREDLAR-EALerKAELE 97

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21356121 341 SKRLTLTQQWQDYRkpllESLEKLKTAkeaqevqgirnsIEQLEQELLAKTQQHNELNATLRSA 404
Cdd:COG1842  98 AQAEALEAQLAQLE----EQVEKLKEA------------LRQLESKLEELKAKKDTLKARAKAA 145
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
263-409 1.64e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 1.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121 263 IQELSDQVQELRVQCENLLAERKAHAVAIAALK--QRETKAREEISRIQPTLKLHERTSLVLADSEENLAKLEALLKSTQ 340
Cdd:COG4717  97 LEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQ 176

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21356121 341 ----SKRLTLTQQWQDYRKPLLESLEKLKTAKEA--QEVQGIRNSIEQLEQEL--LAKTQQHNELNATLRSASQSLA 409
Cdd:COG4717 177 eeleELLEQLSLATEEELQDLAEELEELQQRLAEleEELEEAQEELEELEEELeqLENELEAAALEERLKEARLLLL 253
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 263-432 2.15e-03

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 40.98  E-value: 2.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121    263 IQELSDQVQELRVQCENLLAERKAhavaiaalkqretKAREEISRIQPTLKLHERtslvladseenlaKLEALLKSTQSK 342
Cdd:pfam12128  655 LRRLFDEKQSEKDKKNKALAERKD-------------SANERLNSLEAQLKQLDK-------------KHQAWLEEQKEQ 708

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121    343 RLTLTQQWQDYRKPLLESLEklktAKEAQEVQGIRNSIEQLEQELLA-KTQQHNELnATLRSASQSLAPRKEYTRRIHEF 421
Cdd:pfam12128  709 KREARTEKQAYWQVVEGALD----AQLALLKAAIAARRSGAKAELKAlETWYKRDL-ASLGVDPDVIAKLKREIRTLERK 783

                          170
                   ....*....|.
gi 21356121    422 IGNIRKQRADI 432
Cdd:pfam12128  784 IERIAVRRQEV 794
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 325-550 2.58e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 2.58e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121 325 SEENLAKLEALLKstqsKRLTLTQQWQDYRKpLLESLEKLKTAKEAqEVQGIRNSIEQLEQELLAKTQQHNELNATLRSA 404
Cdd:COG1196 220 EELKELEAELLLL----KLRELEAELEELEA-ELEELEAELEELEA-ELAELEAELEELRLELEELELELEEAQAEEYEL 293

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121 405 SQSLAPRKEYTRRIHEFIGNIRKQRADIYKVLDDTRQLQKQLNVVGAQLQRQFNYTDDLLFQSAKHDLHAKRAYK-LLAQ 483
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLeAEAE 373

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21356121 484 LHANCNELVECVSLTGNVTKQIRELEvqidgEKLKNVLTSLQQITGDIQKFEQHIQELQEQIRAVEQ 550
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELA-----AQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 254-553 2.78e-03

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: 40.87  E-value: 2.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121    254 AEKEEEPSPIQELSDQVQElrvQCENLLAErkaHAVAIAALKQRETKAREEISRIQptlklhertslvladseenlAKLE 333
Cdd:pfam15921  249 ALKSESQNKIELLLQQHQD---RIEQLISE---HEVEITGLTEKASSARSQANSIQ--------------------SQLE 302

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121    334 ALLKSTQSKRLTLTQQWQDYRKPLLESLEKLKTAKEAQEvqgirNSIEQLEQELLAKTQQHNELNATLRSASQSlaprke 413
Cdd:pfam15921  303 IIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYE-----DKIEELEKQLVLANSELTEARTERDQFSQE------ 371

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121    414 ytrrihefIGNIRKQradIYKVLDDTRQLQKQLNVVGAQLQRQFN-------YTDDLLFQSAKHDLHAKRAYKLLAQLHA 486
Cdd:pfam15921  372 --------SGNLDDQ---LQKLLADLHKREKELSLEKEQNKRLWDrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKS 440

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21356121    487 NCNELVE----CVSLTGNVTKQIRELEVQIDGEK--LKNVLTSLQQITGDIQKFEQHIQEL----QEQIRAVEQTNA 553
Cdd:pfam15921  441 ECQGQMErqmaAIQGKNESLEKVSSLTAQLESTKemLRKVVEELTAKKMTLESSERTVSDLtaslQEKERAIEATNA 517
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
264-421 4.08e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 4.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121 264 QELSDQVQELRVQCENLLAERKAHAVAIAALKQRETKAREEISRIQPTLKLHERTSLVLADSEENLAKLEALLKSTQsKR 343
Cdd:COG4717 319 EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAE-EY 397

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121 344 LTLTQQWQDYRKPLLESLEKLKTAKEAQEVQGIRNSIEQLEQELLAKTQQHNELN---ATLRSASQSLAPRKEYTRRIHE 420
Cdd:COG4717 398 QELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELReelAELEAELEQLEEDGELAELLQE 477


                .
gi 21356121 421 F 421
Cdd:COG4717 478 L 478
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
278-455 6.01e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.61  E-value: 6.01e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121 278 ENLLAERKAHAVAIAALKQRETKAREEISRIQPTL-KLHERTSLVLADSE-----ENLAKLEALLKSTQSKRLTLTQQWQ 351
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALeEFRQKNGLVDLSEEaklllQQLSELESQLAEARAELAEAEARLA 243

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356121 352 DYRKPLLESLEKLKTAKEAQEVQGIRNSIEQLEQELLAKTQQHNELNATLRSASQSLA-PRKEYTRRIHEFIGNI----- 425
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAaLRAQLQQEAQRILASLeaele 323

                       170       180       190
                ....*....|....*....|....*....|..
gi 21356121 426 --RKQRADIYKVLDDTRQLQKQLNVVGAQLQR 455
Cdd:COG3206 324 alQAREASLQAQLAQLEARLAELPELEAELRR 355
 
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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