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Conserved domains on  [gi|2067662307|ref|NP_001382452|]
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protein BCAP isoform j [Homo sapiens]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
213-493 1.57e-07

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 1.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 213 RLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEdhgknscEEIL 292
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE-------QDIA 305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 293 RKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKN 372
Cdd:COG1196   306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 373 NQITKTKNKNVEKVDGNHNLLTKLSLEEEncliqlKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYT 452
Cdd:COG1196   386 EELLEALRAAAELAAQLEELEEAEEALLE------RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2067662307 453 ALARQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETE 493
Cdd:COG1196   460 ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
43-368 8.38e-03

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


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 39.28  E-value: 8.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307   43 ILNEKTELEATLKEAELVTHSVELLLPLFKDTIEKINFENANLSALNLKISEQKEILIKELDTFKSVKLALEHLLRKrdY 122
Cdd:TIGR02169  700 IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK--L 777
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  123 KQTGDNLSSMLLENLTDN-ESENTNLKKKVFEKEAHIQELSCLFQSeKSLETKIAKWNLQSRMNKNEAIVMKEASRQKTV 201
Cdd:TIGR02169  778 EEALNDLEARLSHSRIPEiQAELSKLEEEVSRIEARLREIEQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  202 ALKKAskvykqRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKME 281
Cdd:TIGR02169  857 ENLNG------KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE 930
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  282 DHGKnsceEILRKVHSIEYE-NETLNLEntKLKTTLAALKDEVVSVEN-ELSELQEVEKKQKTLIEmYKTQVQKLQEAAE 359
Cdd:TIGR02169  931 EELS----EIEDPKGEDEEIpEEELSLE--DVQAELQRVEEEIRALEPvNMLAIQEYEEVLKRLDE-LKEKRAKLEEERK 1003

                   ....*....
gi 2067662307  360 IVKSRCENL 368
Cdd:TIGR02169 1004 AILERIEEY 1012
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
213-493 1.57e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 1.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 213 RLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEdhgknscEEIL 292
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE-------QDIA 305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 293 RKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKN 372
Cdd:COG1196   306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 373 NQITKTKNKNVEKVDGNHNLLTKLSLEEEncliqlKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYT 452
Cdd:COG1196   386 EELLEALRAAAELAAQLEELEEAEEALLE------RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2067662307 453 ALARQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETE 493
Cdd:COG1196   460 ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
258-504 1.97e-07

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: 54.30  E-value: 1.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  258 ELEVQIETMKKQIINLLEDLKKME---DHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQ 334
Cdd:TIGR02169  678 RLRERLEGLKRELSSLQSELRRIEnrlDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  335 EVEKKQKTLIEMYKTQVQKLQEA-----AEIVKSRCENLLHKNNQITKTKNKNVEKVDGNHNLLTKLSLEEEncLIQLKC 409
Cdd:TIGR02169  758 SELKELEARIEELEEDLHKLEEAlndleARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE--YLEKEI 835
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  410 ENLQQKLEQMDAENKELEKKLANqeecLKHSNLKFKEKSAEYTALARQLEAALEEgrqkVAEEIEKMSSRESALQIKILD 489
Cdd:TIGR02169  836 QELQEQRIDLKEQIKSIEKEIEN----LNGKKEELEEELEELEAALRDLESRLGD----LKKERDELEAQLRELERKIEE 907
                          250
                   ....*....|....*
gi 2067662307  490 LETELRKKNEEQNQL 504
Cdd:TIGR02169  908 LEAQIEKKRKRLSEL 922
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
12-491 1.45e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.14  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  12 EELFCHLKTISEKEDLPRCTSE--SHLSCLKQDILNEKTELEATLKEAELVTHSVELLLPLFKDTIEKINFENANLSALN 89
Cdd:PRK03918  200 KELEEVLREINEISSELPELREelEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  90 LKISEQKEILIKELDTFKSVKLALEHLLRKRDYKQTGDNLSSM---LLENLTDNESENTNLKKKVFEKEAHIQELSCLFQ 166
Cdd:PRK03918  280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEingIEERIKELEEKEERLEELKKKLKELEKRLEELEE 359
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 167 SEKSLETKIAKWNLQSRMNKNEAIVMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNA-- 244
Cdd:PRK03918  360 RHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcp 439
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 245 -----WKSHYEKIVIEKTELEVQ-IETMKKQIINLLEDLKKMEDHGKN---------SCEEILRKVHSIEYENETLNLEN 309
Cdd:PRK03918  440 vcgreLTEEHRKELLEEYTAELKrIEKELKEIEEKERKLRKELRELEKvlkkeseliKLKELAEQLKELEEKLKKYNLEE 519
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 310 T--------KLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEmyktQVQKLQEAAEIVKSRCENLLHKNNQITKTKNK 381
Cdd:PRK03918  520 LekkaeeyeKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK----KLDELEEELAELLKELEELGFESVEELEERLK 595
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 382 NVEKVDGNHNLL--TKLSLEEENCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLK-HSNLKFKEKSAEYTALARQL 458
Cdd:PRK03918  596 ELEPFYNEYLELkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkYSEEEYEELREEYLELSREL 675
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 2067662307 459 EAA------LEEGRQKVAEEIEKMSSRESALQIKILDLE 491
Cdd:PRK03918  676 AGLraeleeLEKRREEIKKTLEKLKEELEEREKAKKELE 714
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
85-532 7.26e-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: 42.41  E-value: 7.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307   85 LSALNLKISEQKEILIKELDTFKSVKLALEhllrkrDYKQTGDNLSSMLLENLTDNESENTNLKKKVFEKEAHIQELSCL 164
Cdd:pfam15921  463 VSSLTAQLESTKEMLRKVVEELTAKKMTLE------SSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHL 536
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  165 FQSEKsletkiakwNLQSRMNKNEAIVMKEASRQKTValkkasKVYKQRLDHFTgaiekltsQIRDQEAKLSETISasna 244
Cdd:pfam15921  537 KNEGD---------HLRNVQTECEALKLQMAEKDKVI------EILRQQIENMT--------QLVGQHGRTAGAMQ---- 589
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  245 wkshyekivIEKTELEVQIETMKKQiinlLEDLKKMEDHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVV 324
Cdd:pfam15921  590 ---------VEKAQLEKEINDRRLE----LQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERD 656
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  325 SVENEL----SELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRcenLLHKNNQITKTKN--KNVEKVDGnHNLLTKLSL 398
Cdd:pfam15921  657 QLLNEVktsrNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQ---LKSAQSELEQTRNtlKSMEGSDG-HAMKVAMGM 732
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  399 EEEncliqlkcenLQQKLEQMDAenkeLEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEgRQKVAEEIEKMSS 478
Cdd:pfam15921  733 QKQ----------ITAKRGQIDA----LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE-KNKMAGELEVLRS 797
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2067662307  479 RESALQIKILDLETELRKKNEEQNQlvCKMNSKAQHQEVCLKEVQNSLEKSENQ 532
Cdd:pfam15921  798 QERRLKEKVANMEVALDKASLQFAE--CQDIIQRQEQESVRLKLQHTLDVKELQ 849
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
43-368 8.38e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.28  E-value: 8.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307   43 ILNEKTELEATLKEAELVTHSVELLLPLFKDTIEKINFENANLSALNLKISEQKEILIKELDTFKSVKLALEHLLRKrdY 122
Cdd:TIGR02169  700 IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK--L 777
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  123 KQTGDNLSSMLLENLTDN-ESENTNLKKKVFEKEAHIQELSCLFQSeKSLETKIAKWNLQSRMNKNEAIVMKEASRQKTV 201
Cdd:TIGR02169  778 EEALNDLEARLSHSRIPEiQAELSKLEEEVSRIEARLREIEQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  202 ALKKAskvykqRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKME 281
Cdd:TIGR02169  857 ENLNG------KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE 930
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  282 DHGKnsceEILRKVHSIEYE-NETLNLEntKLKTTLAALKDEVVSVEN-ELSELQEVEKKQKTLIEmYKTQVQKLQEAAE 359
Cdd:TIGR02169  931 EELS----EIEDPKGEDEEIpEEELSLE--DVQAELQRVEEEIRALEPvNMLAIQEYEEVLKRLDE-LKEKRAKLEEERK 1003

                   ....*....
gi 2067662307  360 IVKSRCENL 368
Cdd:TIGR02169 1004 AILERIEEY 1012
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
213-493 1.57e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 1.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 213 RLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEdhgknscEEIL 292
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE-------QDIA 305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 293 RKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKN 372
Cdd:COG1196   306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 373 NQITKTKNKNVEKVDGNHNLLTKLSLEEEncliqlKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYT 452
Cdd:COG1196   386 EELLEALRAAAELAAQLEELEEAEEALLE------RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2067662307 453 ALARQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETE 493
Cdd:COG1196   460 ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
258-504 1.97e-07

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: 54.30  E-value: 1.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  258 ELEVQIETMKKQIINLLEDLKKME---DHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQ 334
Cdd:TIGR02169  678 RLRERLEGLKRELSSLQSELRRIEnrlDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  335 EVEKKQKTLIEMYKTQVQKLQEA-----AEIVKSRCENLLHKNNQITKTKNKNVEKVDGNHNLLTKLSLEEEncLIQLKC 409
Cdd:TIGR02169  758 SELKELEARIEELEEDLHKLEEAlndleARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE--YLEKEI 835
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  410 ENLQQKLEQMDAENKELEKKLANqeecLKHSNLKFKEKSAEYTALARQLEAALEEgrqkVAEEIEKMSSRESALQIKILD 489
Cdd:TIGR02169  836 QELQEQRIDLKEQIKSIEKEIEN----LNGKKEELEEELEELEAALRDLESRLGD----LKKERDELEAQLRELERKIEE 907
                          250
                   ....*....|....*
gi 2067662307  490 LETELRKKNEEQNQL 504
Cdd:TIGR02169  908 LEAQIEKKRKRLSEL 922
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
257-504 3.00e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 3.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 257 TELEVQIETMKKQiinlledLKKMEDHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEV 336
Cdd:COG1196   196 GELERQLEPLERQ-------AEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 337 EKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLlhknnqitkTKNKNVEKVDGNHNLLTKLSLEEENCLIQLKCENLQQKL 416
Cdd:COG1196   269 LEELRLELEELELELEEAQAEEYELLAELARL---------EQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 417 EQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKVAEEIEKmSSRESALQIKILDLETELRK 496
Cdd:COG1196   340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL-AAQLEELEEAEEALLERLER 418

                  ....*...
gi 2067662307 497 KNEEQNQL 504
Cdd:COG1196   419 LEEELEEL 426
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
194-494 8.63e-07

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: 51.98  E-value: 8.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  194 EASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSET-------ISASNAWKSHYEKIVIEKTELEVQIETM 266
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALrkdlarlEAEVEQLEERIAQLSKELTELEAEIEEL 766
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  267 KKQIINLLEDLKKMEDHGKNSCEEIlrkvhsieyenETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEM 346
Cdd:TIGR02168  767 EERLEEAEEELAEAEAEIEELEAQI-----------EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  347 YKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKVDGNHNLltKLSLEEENCLIQLKCENLQQKLEQMDAENKEL 426
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE--RASLEEALALLRSELEELSEELRELESKRSEL 913
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2067662307  427 EKKLANQEECLKHSNLKFKEKSAEytaLARQLEAALEEGR---QKVAEEIEKMSSRESALQIKILDLETEL 494
Cdd:TIGR02168  914 RRELEELREKLAQLELRLEGLEVR---IDNLQERLSEEYSltlEEAEALENKIEDDEEEARRRLKRLENKI 981
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
298-536 1.20e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 1.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  298 IEYENETLNLENT--KLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQI 375
Cdd:TIGR02168  673 LERRREIEELEEKieELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  376 TKTKNKNVEKVDGNHNLLTKLSLEEENCLIQLkcENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALA 455
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEI--EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  456 RQLEAA-------------LEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKNEEQNQLVCKMNSKAQHQEVCLKEV 522
Cdd:TIGR02168  831 RRIAATerrledleeqieeLSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
                          250
                   ....*....|....
gi 2067662307  523 QNSLEKSENQNESI 536
Cdd:TIGR02168  911 SELRRELEELREKL 924
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
221-461 7.67e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.90  E-value: 7.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  221 IEKLTSQIRDQEAKLSETISASNawkshyekiviEKTELEVQIETMKKQIINLLEDLKKMEDHGKNSCEEILRKVHSIEY 300
Cdd:TIGR02168  255 LEELTAELQELEEKLEELRLEVS-----------ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  301 ENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKN 380
Cdd:TIGR02168  324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  381 KNVEKV---DGNHNLLTKLSLEEENCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQ 457
Cdd:TIGR02168  404 RLEARLerlEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483

                   ....
gi 2067662307  458 LEAA 461
Cdd:TIGR02168  484 LAQL 487
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
12-491 1.45e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.14  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  12 EELFCHLKTISEKEDLPRCTSE--SHLSCLKQDILNEKTELEATLKEAELVTHSVELLLPLFKDTIEKINFENANLSALN 89
Cdd:PRK03918  200 KELEEVLREINEISSELPELREelEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  90 LKISEQKEILIKELDTFKSVKLALEHLLRKRDYKQTGDNLSSM---LLENLTDNESENTNLKKKVFEKEAHIQELSCLFQ 166
Cdd:PRK03918  280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEingIEERIKELEEKEERLEELKKKLKELEKRLEELEE 359
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 167 SEKSLETKIAKWNLQSRMNKNEAIVMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNA-- 244
Cdd:PRK03918  360 RHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcp 439
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 245 -----WKSHYEKIVIEKTELEVQ-IETMKKQIINLLEDLKKMEDHGKN---------SCEEILRKVHSIEYENETLNLEN 309
Cdd:PRK03918  440 vcgreLTEEHRKELLEEYTAELKrIEKELKEIEEKERKLRKELRELEKvlkkeseliKLKELAEQLKELEEKLKKYNLEE 519
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 310 T--------KLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEmyktQVQKLQEAAEIVKSRCENLLHKNNQITKTKNK 381
Cdd:PRK03918  520 LekkaeeyeKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK----KLDELEEELAELLKELEELGFESVEELEERLK 595
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 382 NVEKVDGNHNLL--TKLSLEEENCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLK-HSNLKFKEKSAEYTALARQL 458
Cdd:PRK03918  596 ELEPFYNEYLELkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkYSEEEYEELREEYLELSREL 675
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 2067662307 459 EAA------LEEGRQKVAEEIEKMSSRESALQIKILDLE 491
Cdd:PRK03918  676 AGLraeleeLEKRREEIKKTLEKLKEELEEREKAKKELE 714
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
316-530 1.69e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 1.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  316 LAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKVDGNHNLLTK 395
Cdd:TIGR02168  227 LALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQI 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  396 LSLEEENCLIQLK-----CENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEaALEEGRQKVA 470
Cdd:TIGR02168  307 LRERLANLERQLEeleaqLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE-ELEEQLETLR 385
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2067662307  471 EEIEKMSSRESALQIKILDLETELRKKNEEQNQLVCKMNSKAQH-QEVCLKEVQNSLEKSE 530
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEELE 446
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
255-478 4.83e-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: 45.91  E-value: 4.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 255 EKTELEVQIETMKKQIINLLEDLKKMedhgKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQ 334
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAAL----KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 335 EVEKKQKtliEMYKTQVQKLQEAAEIvkSRCENLLHKNN------------QITKTKNKNVEKVDGNHNLLTKLSLEeen 402
Cdd:COG4942    97 AELEAQK---EELAELLRALYRLGRQ--PPLALLLSPEDfldavrrlqylkYLAPARREQAEELRADLAELAALRAE--- 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2067662307 403 clIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTAL---ARQLEAALEEGRQKVAEEIEKMSS 478
Cdd:COG4942   169 --LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELqqeAEELEALIARLEAEAAAAAERTPA 245
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
253-504 4.14e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 4.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  253 VIEKTELEVQIETMKKQIinllEDLKKMEDHGknscEEILRKVhsieyenETLnlentklkTTLAALKDEVVSVENELSE 332
Cdd:COG4913    217 MLEEPDTFEAADALVEHF----DDLERAHEAL----EDAREQI-------ELL--------EPIRELAERYAAARERLAE 273
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  333 LQEVEKKQKTLIEmyKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKVDGNHNLLTKLSLEEEncliqlkcENL 412
Cdd:COG4913    274 LEYLRAALRLWFA--QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRL--------EQL 343
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  413 QQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKVAEEIEKMSSRESALQikilDLET 492
Cdd:COG4913    344 EREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR----DLRR 419
                          250
                   ....*....|..
gi 2067662307  493 ELRKKNEEQNQL 504
Cdd:COG4913    420 ELRELEAEIASL 431
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
193-364 5.85e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.44  E-value: 5.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 193 KEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIIN 272
Cdd:COG4942    22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 273 LLEDLK-------KMEDHGK-------NSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEK 338
Cdd:COG4942   102 QKEELAellralyRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
                         170       180
                  ....*....|....*....|....*.
gi 2067662307 339 KQKTLIEMYKTQVQKLQEAAEIVKSR 364
Cdd:COG4942   182 ELEEERAALEALKAERQKLLARLEKE 207
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
85-532 7.26e-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: 42.41  E-value: 7.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307   85 LSALNLKISEQKEILIKELDTFKSVKLALEhllrkrDYKQTGDNLSSMLLENLTDNESENTNLKKKVFEKEAHIQELSCL 164
Cdd:pfam15921  463 VSSLTAQLESTKEMLRKVVEELTAKKMTLE------SSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHL 536
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  165 FQSEKsletkiakwNLQSRMNKNEAIVMKEASRQKTValkkasKVYKQRLDHFTgaiekltsQIRDQEAKLSETISasna 244
Cdd:pfam15921  537 KNEGD---------HLRNVQTECEALKLQMAEKDKVI------EILRQQIENMT--------QLVGQHGRTAGAMQ---- 589
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  245 wkshyekivIEKTELEVQIETMKKQiinlLEDLKKMEDHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVV 324
Cdd:pfam15921  590 ---------VEKAQLEKEINDRRLE----LQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERD 656
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  325 SVENEL----SELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRcenLLHKNNQITKTKN--KNVEKVDGnHNLLTKLSL 398
Cdd:pfam15921  657 QLLNEVktsrNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQ---LKSAQSELEQTRNtlKSMEGSDG-HAMKVAMGM 732
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  399 EEEncliqlkcenLQQKLEQMDAenkeLEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEgRQKVAEEIEKMSS 478
Cdd:pfam15921  733 QKQ----------ITAKRGQIDA----LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE-KNKMAGELEVLRS 797
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2067662307  479 RESALQIKILDLETELRKKNEEQNQlvCKMNSKAQHQEVCLKEVQNSLEKSENQ 532
Cdd:pfam15921  798 QERRLKEKVANMEVALDKASLQFAE--CQDIIQRQEQESVRLKLQHTLDVKELQ 849
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
132-355 8.42e-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: 42.35  E-value: 8.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  132 MLLENLTDNESENTNLKKKVFEKEAHIQELSCLFQSEKSLETKIAKWNLQSRMNKNEAIVMKEA-------SRQKTVALK 204
Cdd:TIGR02168  702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEleerleeAEEELAEAE 781
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  205 KASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKME--- 281
Cdd:TIGR02168  782 AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAaei 861
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2067662307  282 DHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQ 355
Cdd:TIGR02168  862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
PRK12704 PRK12704
phosphodiesterase; Provisional
337-486 8.69e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 8.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 337 EKKQKTLIEMYKTQVQKLQEAAEIVKSrcENLLHKNNQITKTKNKNVEKVDGNHNLLTKLsleeENCLIQlKCENLQQKL 416
Cdd:PRK12704   30 EAKIKEAEEEAKRILEEAKKEAEAIKK--EALLEAKEEIHKLRNEFEKELRERRNELQKL----EKRLLQ-KEENLDRKL 102
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2067662307 417 EQMDAENKELEKklanQEECLKHSNLKFKEKSAEYTALARQLEAALE--------EGRQKVAEEIEKMSSRESALQIK 486
Cdd:PRK12704  103 ELLEKREEELEK----KEKELEQKQQELEKKEEELEELIEEQLQELErisgltaeEAKEILLEKVEEEARHEAAVLIK 176
PLN02939 PLN02939
transferase, transferring glycosyl groups
172-478 1.14e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 41.81  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 172 ETKIAKWNLQSRMNKNEAIVMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAwkSHYEK 251
Cdd:PLN02939  116 QTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIKL--AAQEK 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 252 IVIEKteLEVQIETMKKQIINLLEDLKKMedhgknsceeilrkVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELS 331
Cdd:PLN02939  194 IHVEI--LEEQLEKLRNELLIRGATEGLC--------------VHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEE 257
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 332 ELQEVEKKQKTLIEMYKTQVQKLQEAAEIVK-----------SRCENLLHKNNQITKTKNKNVEKVDGNHNLLTKL---- 396
Cdd:PLN02939  258 RVFKLEKERSLLDASLRELESKFIVAQEDVSklsplqydcwwEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVdkle 337
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 397 -SLEEENC--LIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEksaeytalarQLEAALEEGRQKVAEE- 472
Cdd:PLN02939  338 aSLKEANVskFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQD----------TLSKLKEESKKRSLEHp 407

                  ....*.
gi 2067662307 473 IEKMSS 478
Cdd:PLN02939  408 ADDMPS 413
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
166-357 1.43e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 166 QSEKSLETKIAKwnLQSRMNKNEAIVMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKL---------S 236
Cdd:COG3206   175 KALEFLEEQLPE--LRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLaalraqlgsG 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 237 ETISASNAWKSHYEKIVIEKTELEVQIETMKK-------QIINLLEDLKKMEDHGKnscEEILRKVHSIEYENETLNLEN 309
Cdd:COG3206   253 PDALPELLQSPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQ---QEAQRILASLEAELEALQARE 329
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2067662307 310 TKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEA 357
Cdd:COG3206   330 ASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
268-381 1.52e-03

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 39.22  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 268 KQIINLLEDLKKMEDHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMY 347
Cdd:pfam11559  34 ARIINVIYELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNE 113
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2067662307 348 KTQVQKLQEAAEIVKSRCENLLHKNN-QITKTKNK 381
Cdd:pfam11559 114 KEELQRLKNALQQIKTQFAHEVKKRDrEIEKLKER 148
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
95-368 1.83e-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: 41.20  E-value: 1.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307   95 QKEILIKELDTFKSVKLALEHLLRKrdykqtGDNLSSMLLENLTDNESENTNLKKKVFEKEAHIQELSCLfQSEKSLETK 174
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEE------LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE-ISRLEQQKQ 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  175 IAKWNLQSRMNKNEAI-VMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIV 253
Cdd:TIGR02168  306 ILRERLANLERQLEELeAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  254 IEKTELEVQIETMKKQIINLLEDLKKMEDHGKNSCEEILrkvhsiEYENETLNLENTKLKTTLAALKDEVVSVENELSEL 333
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE------ELLKKLEEAELKELQAELEELEEELEELQEELERL 459
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2067662307  334 QEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENL 368
Cdd:TIGR02168  460 EEALEELREELEEAEQALDAAERELAQLQARLDSL 494
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
258-538 4.73e-03

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 39.84  E-value: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 258 ELEVQIETMKKQIINLLEDLKKMEDHGKNSCEEILRKVHSIEYENEtlnLENTKLKTTLAALKDEV--VSVENELSELQE 335
Cdd:PLN03229  433 ELEGEVEKLKEQILKAKESSSKPSELALNEMIEKLKKEIDLEYTEA---VIAMGLQERLENLREEFskANSQDQLMHPVL 509
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 336 VEKKQKTLIEM---------YKTQVQKLQEAAEIvkSRCENLLHKNNQITKTK---NKNVEKVDGNHNLLTKLSLeeenc 403
Cdd:PLN03229  510 MEKIEKLKDEFnkrlsrapnYLSLKYKLDMLNEF--SRAKALSEKKSKAEKLKaeiNKKFKEVMDRPEIKEKMEA----- 582
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 404 liqLKCENLQQKLEQMDAENKELEKKL--ANQE------ECLKHSNL-----KFKEKSAEYTALARQLEAALEEGRQKVA 470
Cdd:PLN03229  583 ---LKAEVASSGASSGDELDDDLKEKVekMKKEielelaGVLKSMGLevigvTKKNKDTAEQTPPPNLQEKIESLNEEIN 659
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 471 EEIEKMsSRESALQIKILDLETELRK----------------KNEEQNQLVCKMNSKA--QHQEVCLKEVQNSLEKSENQ 532
Cdd:PLN03229  660 KKIERV-IRSSDLKSKIELLKLEVAKasktpdvtekekiealEQQIKQKIAEALNSSElkEKFEELEAELAAARETAAES 738

                  ....*.
gi 2067662307 533 NESIKN 538
Cdd:PLN03229  739 NGSLKN 744
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
255-484 5.08e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.43  E-value: 5.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 255 EKTELEVQIETMKKQIINLLEDLKKMEDhgknsceeilrKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQ 334
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQA-----------ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 335 EVEKKQktLIEMYK-----TQVQKLQEAAEIVK--SRCENLlhknNQITKTKNKNVEKVDGnhnllTKLSLEEENCLIQL 407
Cdd:COG3883    86 EELGER--ARALYRsggsvSYLDVLLGSESFSDflDRLSAL----SKIADADADLLEELKA-----DKAELEAKKAELEA 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2067662307 408 KCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKVAEEIEKMSSRESALQ 484
Cdd:COG3883   155 KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
213-483 6.05e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.67  E-value: 6.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  213 RLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEDHGKNSCEEIL 292
Cdd:TIGR02169  682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  293 RKVHSIEYENETLNlentKLKTTLAALKDE-----VVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCEN 367
Cdd:TIGR02169  762 ELEARIEELEEDLH----KLEEALNDLEARlshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  368 LLHKNNQITKTKNKNVEKVDGNHNLLTKL------------SLEEENCLIQLKCENLQQKLEQMDAENKELEKKLANQEE 435
Cdd:TIGR02169  838 LQEQRIDLKEQIKSIEKEIENLNGKKEELeeeleeleaalrDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2067662307  436 CLKHSNLKFKEKSAEYTALARQLEAALEEGRQ-----KVAEEIEKMSSRESAL 483
Cdd:TIGR02169  918 RLSELKAKLEALEEELSEIEDPKGEDEEIPEEelsleDVQAELQRVEEEIRAL 970
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
43-368 8.38e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.28  E-value: 8.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307   43 ILNEKTELEATLKEAELVTHSVELLLPLFKDTIEKINFENANLSALNLKISEQKEILIKELDTFKSVKLALEHLLRKrdY 122
Cdd:TIGR02169  700 IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK--L 777
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  123 KQTGDNLSSMLLENLTDN-ESENTNLKKKVFEKEAHIQELSCLFQSeKSLETKIAKWNLQSRMNKNEAIVMKEASRQKTV 201
Cdd:TIGR02169  778 EEALNDLEARLSHSRIPEiQAELSKLEEEVSRIEARLREIEQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  202 ALKKAskvykqRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKME 281
Cdd:TIGR02169  857 ENLNG------KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE 930
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307  282 DHGKnsceEILRKVHSIEYE-NETLNLEntKLKTTLAALKDEVVSVEN-ELSELQEVEKKQKTLIEmYKTQVQKLQEAAE 359
Cdd:TIGR02169  931 EELS----EIEDPKGEDEEIpEEELSLE--DVQAELQRVEEEIRALEPvNMLAIQEYEEVLKRLDE-LKEKRAKLEEERK 1003

                   ....*....
gi 2067662307  360 IVKSRCENL 368
Cdd:TIGR02169 1004 AILERIEEY 1012
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
194-466 8.57e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 8.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 194 EASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSEtisasnawkshyekIVIEKTELEVQIETMKKQIINL 273
Cdd:COG1196   270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE--------------LEERLEELEEELAELEEELEEL 335
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 274 LEDLkkmedhgknscEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQK 353
Cdd:COG1196   336 EEEL-----------EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 354 LQEAAEIVKSRCENLLHKNNQITKTKNKNVEKVDGNHNLLTKLSLEEencliqlkcENLQQKLEQMDAENKELEKKLANQ 433
Cdd:COG1196   405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE---------AELEEEEEALLELLAELLEEAALL 475
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2067662307 434 EECLKHSNLKFKEKSAEYTALARQLEAALEEGR 466
Cdd:COG1196   476 EAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
408-504 9.64e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 38.69  E-value: 9.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662307 408 KCENLQQKLEQMDAENKELEKKLANQEECLKHsnlkfkeksaeytalarqLEAALEEGRQKVAEEIEKmsSRE-SALQIK 486
Cdd:COG2433   414 EIRRLEEQVERLEAEVEELEAELEEKDERIER------------------LERELSEARSEERREIRK--DREiSRLDRE 473
                          90
                  ....*....|....*...
gi 2067662307 487 ILDLETELRKKNEEQNQL 504
Cdd:COG2433   474 IERLERELEEERERIEEL 491
 
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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