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Conserved domains on  [gi|296179399|ref|NP_001171695|]
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protein BCAP isoform d [Homo sapiens]

Protein Classification

CCDC158 family protein( domain architecture ID 1016012)

CCDC158 family protein similar to Drosophila melanogaster tiggrin that is required in larvae for proper muscle structure and function and is involved in the regulation of cell adhesion during wing development

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]; ...
252-532 1.85e-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: 54.17  E-value: 1.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 252 RLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEdhgknscEEIL 331
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE-------QDIA 305
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 332 RKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKN 411
Cdd:COG1196  306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 412 NQITKTKNKNVEKVDGNHNLLTKLSLEEEncliqlKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYT 491
Cdd:COG1196  386 EELLEALRAAAELAAQLEELEEAEEALLE------RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 296179399 492 ALARQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETE 532
Cdd:COG1196  460 ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
CCDC158 super family cl37899
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
2-571 9.15e-04

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


The actual alignment was detected with superfamily member pfam15921:

Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 42.41  E-value: 9.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399     2 EKAVNDGSHSEELFCHLKTISEKEDLPRCTSESHLSCLKQDILNEKTELEATLKEAELVTHSVELLLPLFKDTIEKINFE 81
Cdd:pfam15921  285 EKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTE 364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399    82 NANLSALNLKISEQKEILIKELDTfKSVKLALEHLLRKRdykqtgdnlssmLLENLTDNESENTNLKKKVFEKEAHIQEL 161
Cdd:pfam15921  365 RDQFSQESGNLDDQLQKLLADLHK-REKELSLEKEQNKR------------LWDRDTGNSITIDHLRRELDDRNMEVQRL 431
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   162 SCLFQSEKANtlkanrfsqsvkvVHERLQIQIHKREAENDKLkEYVKSLETKI--AKWNLQSRMNKNEAIVMKEASRQKT 239
Cdd:pfam15921  432 EALLKAMKSE-------------CQGQMERQMAAIQGKNESL-EKVSSLTAQLesTKEMLRKVVEELTAKKMTLESSERT 497
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   240 VALKKASKVYKQRLDHFTGA-IEKLTSQIrdqEAKLSETISASNAW------KSHYEKIVIEKTELEVQIETMKKQIINL 312
Cdd:pfam15921  498 VSDLTASLQEKERAIEATNAeITKLRSRV---DLKLQELQHLKNEGdhlrnvQTECEALKLQMAEKDKVIEILRQQIENM 574
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   313 LEDLKKmedHGKNSCEEILRKVH-SIEYENETLNLENTK------------LKTTLAALKDEVVSVENELSE----LQEV 375
Cdd:pfam15921  575 TQLVGQ---HGRTAGAMQVEKAQlEKEINDRRLELQEFKilkdkkdakireLEARVSDLELEKVKLVNAGSErlraVKDI 651
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   376 EKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKVDGNHNLL-----TKLSLEEENCLIQLKCEN 450
Cdd:pfam15921  652 KQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELeqtrnTLKSMEGSDGHAMKVAMG 731
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   451 LQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEgRQKVAEEIEKMSSRESALQIKILDLE 530
Cdd:pfam15921  732 MQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE-KNKMAGELEVLRSQERRLKEKVANME 810
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|.
gi 296179399   531 TELRKKNEEQNQlvCKMNSKAQHQEVCLKEVQNSLEKSENQ 571
Cdd:pfam15921  811 VALDKASLQFAE--CQDIIQRQEQESVRLKLQHTLDVKELQ 849
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
252-532 1.85e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 1.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 252 RLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEdhgknscEEIL 331
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE-------QDIA 305
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 332 RKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKN 411
Cdd:COG1196  306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 412 NQITKTKNKNVEKVDGNHNLLTKLSLEEEncliqlKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYT 491
Cdd:COG1196  386 EELLEALRAAAELAAQLEELEEAEEALLE------RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 296179399 492 ALARQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETE 532
Cdd:COG1196  460 ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
297-543 2.20e-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: 2.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   297 ELEVQIETMKKQIINLLEDLKKME---DHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQ 373
Cdd:TIGR02169  678 RLRERLEGLKRELSSLQSELRRIEnrlDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   374 EVEKKQKTLIEMYKTQVQKLQEA-----AEIVKSRCENLLHKNNQITKTKNKNVEKVDGNHNLLTKLSLEEEncLIQLKC 448
Cdd:TIGR02169  758 SELKELEARIEELEEDLHKLEEAlndleARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE--YLEKEI 835
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   449 ENLQQKLEQMDAENKELEKKLANqeecLKHSNLKFKEKSAEYTALARQLEAALEEgrqkVAEEIEKMSSRESALQIKILD 528
Cdd:TIGR02169  836 QELQEQRIDLKEQIKSIEKEIEN----LNGKKEELEEELEELEAALRDLESRLGD----LKKERDELEAQLRELERKIEE 907
                          250
                   ....*....|....*
gi 296179399   529 LETELRKKNEEQNQL 543
Cdd:TIGR02169  908 LEAQIEKKRKRLSEL 922
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
85-485 4.78e-04

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.18  E-value: 4.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399    85 LSALNLKISEQKEILIKELDTFKSVKLALEhllrkrDYKQTGDNLSSMLLENLTDNESENTNLKKKVFEKEAHIQELSCL 164
Cdd:pfam15921  463 VSSLTAQLESTKEMLRKVVEELTAKKMTLE------SSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHL 536
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   165 FQSEKantlkanrFSQSVKVVHERLQIQIHKREAENDKLKEYVKSLETKIAKWNLQSRMNKNEAIVMKEASRQKTVALKK 244
Cdd:pfam15921  537 KNEGD--------HLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQE 608
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   245 AsKVYKQRLDhftGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEDHGK 324
Cdd:pfam15921  609 F-KILKDKKD---AKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFR 684
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   325 NSCEEIlrkvhsiEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRC 404
Cdd:pfam15921  685 NKSEEM-------ETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAM 757
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   405 ENLLHKNNQITKTKNKnvekvdgnhnlltklsLEEENCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFK 484
Cdd:pfam15921  758 TNANKEKHFLKEEKNK----------------LSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFA 821

                   .
gi 296179399   485 E 485
Cdd:pfam15921  822 E 822
PLN02939 PLN02939
transferase, transferring glycosyl groups
186-517 5.33e-04

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 42.97  E-value: 5.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 186 HERLQIQIHKREAENDKLKEYVKSLETKIAKWNLQsrmnknEAIVMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTS 265
Cdd:PLN02939  97 HNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLE------DLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQG 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 266 QIRDQEAKLSETISASNAwkSHYEKIVIEKteLEVQIETMKKQIINLLEDLKKMedhgknsceeilrkVHSIEYENETLN 345
Cdd:PLN02939 171 KINILEMRLSETDARIKL--AAQEKIHVEI--LEEQLEKLRNELLIRGATEGLC--------------VHSLSKELDVLK 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 346 LENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVK-----------SRCENLLHKNNQI 414
Cdd:PLN02939 233 EENMLLKDDIQFLKAELIEVAETEERVFKLEKERSLLDASLRELESKFIVAQEDVSklsplqydcwwEKVENLQDLLDRA 312
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 415 TKTKNKNVEKVDGNHNLLTKL-----SLEEENC--LIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEks 487
Cdd:PLN02939 313 TNQVEKAALVLDQNQDLRDKVdkleaSLKEANVskFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQD-- 390
                        330       340       350
                 ....*....|....*....|....*....|.
gi 296179399 488 aeytalarQLEAALEEGRQKVAEE-IEKMSS 517
Cdd:PLN02939 391 --------TLSKLKEESKKRSLEHpADDMPS 413
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
2-571 9.15e-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: 9.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399     2 EKAVNDGSHSEELFCHLKTISEKEDLPRCTSESHLSCLKQDILNEKTELEATLKEAELVTHSVELLLPLFKDTIEKINFE 81
Cdd:pfam15921  285 EKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTE 364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399    82 NANLSALNLKISEQKEILIKELDTfKSVKLALEHLLRKRdykqtgdnlssmLLENLTDNESENTNLKKKVFEKEAHIQEL 161
Cdd:pfam15921  365 RDQFSQESGNLDDQLQKLLADLHK-REKELSLEKEQNKR------------LWDRDTGNSITIDHLRRELDDRNMEVQRL 431
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   162 SCLFQSEKANtlkanrfsqsvkvVHERLQIQIHKREAENDKLkEYVKSLETKI--AKWNLQSRMNKNEAIVMKEASRQKT 239
Cdd:pfam15921  432 EALLKAMKSE-------------CQGQMERQMAAIQGKNESL-EKVSSLTAQLesTKEMLRKVVEELTAKKMTLESSERT 497
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   240 VALKKASKVYKQRLDHFTGA-IEKLTSQIrdqEAKLSETISASNAW------KSHYEKIVIEKTELEVQIETMKKQIINL 312
Cdd:pfam15921  498 VSDLTASLQEKERAIEATNAeITKLRSRV---DLKLQELQHLKNEGdhlrnvQTECEALKLQMAEKDKVIEILRQQIENM 574
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   313 LEDLKKmedHGKNSCEEILRKVH-SIEYENETLNLENTK------------LKTTLAALKDEVVSVENELSE----LQEV 375
Cdd:pfam15921  575 TQLVGQ---HGRTAGAMQVEKAQlEKEINDRRLELQEFKilkdkkdakireLEARVSDLELEKVKLVNAGSErlraVKDI 651
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   376 EKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKVDGNHNLL-----TKLSLEEENCLIQLKCEN 450
Cdd:pfam15921  652 KQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELeqtrnTLKSMEGSDGHAMKVAMG 731
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   451 LQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEgRQKVAEEIEKMSSRESALQIKILDLE 530
Cdd:pfam15921  732 MQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE-KNKMAGELEVLRSQERRLKEKVANME 810
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|.
gi 296179399   531 TELRKKNEEQNQlvCKMNSKAQHQEVCLKEVQNSLEKSENQ 571
Cdd:pfam15921  811 VALDKASLQFAE--CQDIIQRQEQESVRLKLQHTLDVKELQ 849
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
252-532 1.85e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 1.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 252 RLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEdhgknscEEIL 331
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE-------QDIA 305
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 332 RKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKN 411
Cdd:COG1196  306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 412 NQITKTKNKNVEKVDGNHNLLTKLSLEEEncliqlKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYT 491
Cdd:COG1196  386 EELLEALRAAAELAAQLEELEEAEEALLE------RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 296179399 492 ALARQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETE 532
Cdd:COG1196  460 ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
297-543 2.20e-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: 2.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   297 ELEVQIETMKKQIINLLEDLKKME---DHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQ 373
Cdd:TIGR02169  678 RLRERLEGLKRELSSLQSELRRIEnrlDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   374 EVEKKQKTLIEMYKTQVQKLQEA-----AEIVKSRCENLLHKNNQITKTKNKNVEKVDGNHNLLTKLSLEEEncLIQLKC 448
Cdd:TIGR02169  758 SELKELEARIEELEEDLHKLEEAlndleARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE--YLEKEI 835
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   449 ENLQQKLEQMDAENKELEKKLANqeecLKHSNLKFKEKSAEYTALARQLEAALEEgrqkVAEEIEKMSSRESALQIKILD 528
Cdd:TIGR02169  836 QELQEQRIDLKEQIKSIEKEIEN----LNGKKEELEEELEELEAALRDLESRLGD----LKKERDELEAQLRELERKIEE 907
                          250
                   ....*....|....*
gi 296179399   529 LETELRKKNEEQNQL 543
Cdd:TIGR02169  908 LEAQIEKKRKRLSEL 922
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
296-543 3.40e-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: 3.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 296 TELEVQIETMKKQiinlledLKKMEDHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEV 375
Cdd:COG1196  196 GELERQLEPLERQ-------AEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 376 EKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLlhknnqitkTKNKNVEKVDGNHNLLTKLSLEEENCLIQLKCENLQQKL 455
Cdd:COG1196  269 LEELRLELEELELELEEAQAEEYELLAELARL---------EQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 456 EQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKVAEEIEKmSSRESALQIKILDLETELRK 535
Cdd:COG1196  340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL-AAQLEELEEAEEALLERLER 418

                 ....*...
gi 296179399 536 KNEEQNQL 543
Cdd:COG1196  419 LEEELEEL 426
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
337-575 1.33e-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: 1.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   337 IEYENETLNLENT--KLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQI 414
Cdd:TIGR02168  673 LERRREIEELEEKieELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   415 TKTKNKNVEKVDGNHNLLTKLSLEEENCLIQLkcENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALA 494
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEI--EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   495 RQLEAA-------------LEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKNEEQNQLVCKMNSKAQHQEVCLKEV 561
Cdd:TIGR02168  831 RRIAATerrledleeqieeLSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
                          250
                   ....*....|....
gi 296179399   562 QNSLEKSENQNESI 575
Cdd:TIGR02168  911 SELRRELEELREKL 924
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
260-500 8.50e-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: 8.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   260 IEKLTSQIRDQEAKLSETISASNawkshyekiviEKTELEVQIETMKKQIINLLEDLKKMEDHGKNSCEEILRKVHSIEY 339
Cdd:TIGR02168  255 LEELTAELQELEEKLEELRLEVS-----------ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   340 ENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKN 419
Cdd:TIGR02168  324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   420 KNVEKV---DGNHNLLTKLSLEEENCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQ 496
Cdd:TIGR02168  404 RLEARLerlEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483

                   ....
gi 296179399   497 LEAA 500
Cdd:TIGR02168  484 LAQL 487
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
355-569 1.88e-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: 1.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   355 LAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKVDGNHNLLTK 434
Cdd:TIGR02168  227 LALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQI 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   435 LSLEEENCLIQLK-----CENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEaALEEGRQKVA 509
Cdd:TIGR02168  307 LRERLANLERQLEeleaqLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE-ELEEQLETLR 385
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296179399   510 EEIEKMSSRESALQIKILDLETELRKKNEEQNQLVCKMNSKAQH-QEVCLKEVQNSLEKSE 569
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEELE 446
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
135-394 2.60e-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: 47.36  E-value: 2.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   135 ENLTDNESENTNLKKKVFEKEAHIQELSCLFQSEKANTLKANRFSQSVKVVHERLQIQIHKREAENDKLKEYVKSLETKI 214
Cdd:TIGR02168  684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   215 AKWNLQsrmnkneaivmKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIE 294
Cdd:TIGR02168  764 EELEER-----------LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   295 KTELEVQIETMKKQIINLLEDLKKME---DHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSE 371
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAaeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
                          250       260
                   ....*....|....*....|...
gi 296179399   372 LQEVEKKQKTLIEMYKTQVQKLQ 394
Cdd:TIGR02168  913 LRRELEELREKLAQLELRLEGLE 935
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
294-517 7.60e-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: 45.14  E-value: 7.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 294 EKTELEVQIETMKKQIINLLEDLKKMedhgKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQ 373
Cdd:COG4942   21 AAAEAEAELEQLQQEIAELEKELAAL----KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 374 EVEKKQKtliEMYKTQVQKLQEAAEIvkSRCENLLHKNN------------QITKTKNKNVEKVDGNHNLLTKLSLEeen 441
Cdd:COG4942   97 AELEAQK---EELAELLRALYRLGRQ--PPLALLLSPEDfldavrrlqylkYLAPARREQAEELRADLAELAALRAE--- 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296179399 442 clIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTAL---ARQLEAALEEGRQKVAEEIEKMSS 517
Cdd:COG4942  169 --LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELqqeAEELEALIARLEAEAAAAAERTPA 245
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
166-505 1.67e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 166 QSEKAntLKANRFSQSVKVV-HERLQIQIHKREAENDKLKEYVKSLETKIAKWNLQSRMNKNEaivmKEASRQKTVALKK 244
Cdd:COG1196  208 QAEKA--ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE----LEELRLELEELEL 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 245 ASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSEtisasnawkshyekIVIEKTELEVQIETMKKQIINLLEDLkkmedhgk 324
Cdd:COG1196  282 ELEEAQAEEYELLAELARLEQDIARLEERRRE--------------LEERLEELEEELAELEEELEELEEEL-------- 339
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 325 nscEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRC 404
Cdd:COG1196  340 ---EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 405 ENLLHKNNQITKTKNKNVEKVDGNHNLLTKLSLEEencliqlkcENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFK 484
Cdd:COG1196  417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEE---------AELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
                        330       340
                 ....*....|....*....|.
gi 296179399 485 EKSAEYTALARQLEAALEEGR 505
Cdd:COG1196  488 EAAARLLLLLEAEADYEGFLE 508
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
196-396 3.62e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.47  E-value: 3.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 196 REAENDKLKEYVKSLETKIAKwnLQSRMNKNEAIVMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKL- 274
Cdd:COG3206  166 LELRREEARKALEFLEEQLPE--LRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLa 243
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 275 --------SETISASNAWKSHYEKIVIEKTELEVQIETMKK-------QIINLLEDLKKMEDHGKnscEEILRKVHSIEY 339
Cdd:COG3206  244 alraqlgsGPDALPELLQSPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQ---QEAQRILASLEA 320
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 296179399 340 ENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEA 396
Cdd:COG3206  321 ELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
85-485 4.78e-04

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.18  E-value: 4.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399    85 LSALNLKISEQKEILIKELDTFKSVKLALEhllrkrDYKQTGDNLSSMLLENLTDNESENTNLKKKVFEKEAHIQELSCL 164
Cdd:pfam15921  463 VSSLTAQLESTKEMLRKVVEELTAKKMTLE------SSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHL 536
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   165 FQSEKantlkanrFSQSVKVVHERLQIQIHKREAENDKLKEYVKSLETKIAKWNLQSRMNKNEAIVMKEASRQKTVALKK 244
Cdd:pfam15921  537 KNEGD--------HLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQE 608
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   245 AsKVYKQRLDhftGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEDHGK 324
Cdd:pfam15921  609 F-KILKDKKD---AKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFR 684
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   325 NSCEEIlrkvhsiEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRC 404
Cdd:pfam15921  685 NKSEEM-------ETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAM 757
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   405 ENLLHKNNQITKTKNKnvekvdgnhnlltklsLEEENCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFK 484
Cdd:pfam15921  758 TNANKEKHFLKEEKNK----------------LSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFA 821

                   .
gi 296179399   485 E 485
Cdd:pfam15921  822 E 822
PLN02939 PLN02939
transferase, transferring glycosyl groups
186-517 5.33e-04

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 42.97  E-value: 5.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 186 HERLQIQIHKREAENDKLKEYVKSLETKIAKWNLQsrmnknEAIVMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTS 265
Cdd:PLN02939  97 HNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLE------DLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQG 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 266 QIRDQEAKLSETISASNAwkSHYEKIVIEKteLEVQIETMKKQIINLLEDLKKMedhgknsceeilrkVHSIEYENETLN 345
Cdd:PLN02939 171 KINILEMRLSETDARIKL--AAQEKIHVEI--LEEQLEKLRNELLIRGATEGLC--------------VHSLSKELDVLK 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 346 LENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVK-----------SRCENLLHKNNQI 414
Cdd:PLN02939 233 EENMLLKDDIQFLKAELIEVAETEERVFKLEKERSLLDASLRELESKFIVAQEDVSklsplqydcwwEKVENLQDLLDRA 312
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 415 TKTKNKNVEKVDGNHNLLTKL-----SLEEENC--LIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEks 487
Cdd:PLN02939 313 TNQVEKAALVLDQNQDLRDKVdkleaSLKEANVskFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQD-- 390
                        330       340       350
                 ....*....|....*....|....*....|.
gi 296179399 488 aeytalarQLEAALEEGRQKVAEE-IEKMSS 517
Cdd:PLN02939 391 --------TLSKLKEESKKRSLEHpADDMPS 413
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
292-543 5.78e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 5.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399  292 VIEKTELEVQIETMKKQIinllEDLKKMEDHGknscEEILRKVhsieyenETLnlentklkTTLAALKDEVVSVENELSE 371
Cdd:COG4913   217 MLEEPDTFEAADALVEHF----DDLERAHEAL----EDAREQI-------ELL--------EPIRELAERYAAARERLAE 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399  372 LQEVEKKQKTLIEmyKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKVDGNHNLLTKLSLEEEncliqlkcENL 451
Cdd:COG4913   274 LEYLRAALRLWFA--QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRL--------EQL 343
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399  452 QQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKVAEEIEKMSSRESALQikilDLET 531
Cdd:COG4913   344 EREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR----DLRR 419
                         250
                  ....*....|..
gi 296179399  532 ELRKKNEEQNQL 543
Cdd:COG4913   420 ELRELEAEIASL 431
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
232-403 7.70e-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: 7.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 232 KEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIIN 311
Cdd:COG4942   22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 312 LLEDLK-------KMEDHGK-------NSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEK 377
Cdd:COG4942  102 QKEELAellralyRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
                        170       180
                 ....*....|....*....|....*.
gi 296179399 378 KQKTLIEMYKTQVQKLQEAAEIVKSR 403
Cdd:COG4942  182 ELEEERAALEALKAERQKLLARLEKE 207
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
2-571 9.15e-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: 9.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399     2 EKAVNDGSHSEELFCHLKTISEKEDLPRCTSESHLSCLKQDILNEKTELEATLKEAELVTHSVELLLPLFKDTIEKINFE 81
Cdd:pfam15921  285 EKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTE 364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399    82 NANLSALNLKISEQKEILIKELDTfKSVKLALEHLLRKRdykqtgdnlssmLLENLTDNESENTNLKKKVFEKEAHIQEL 161
Cdd:pfam15921  365 RDQFSQESGNLDDQLQKLLADLHK-REKELSLEKEQNKR------------LWDRDTGNSITIDHLRRELDDRNMEVQRL 431
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   162 SCLFQSEKANtlkanrfsqsvkvVHERLQIQIHKREAENDKLkEYVKSLETKI--AKWNLQSRMNKNEAIVMKEASRQKT 239
Cdd:pfam15921  432 EALLKAMKSE-------------CQGQMERQMAAIQGKNESL-EKVSSLTAQLesTKEMLRKVVEELTAKKMTLESSERT 497
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   240 VALKKASKVYKQRLDHFTGA-IEKLTSQIrdqEAKLSETISASNAW------KSHYEKIVIEKTELEVQIETMKKQIINL 312
Cdd:pfam15921  498 VSDLTASLQEKERAIEATNAeITKLRSRV---DLKLQELQHLKNEGdhlrnvQTECEALKLQMAEKDKVIEILRQQIENM 574
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   313 LEDLKKmedHGKNSCEEILRKVH-SIEYENETLNLENTK------------LKTTLAALKDEVVSVENELSE----LQEV 375
Cdd:pfam15921  575 TQLVGQ---HGRTAGAMQVEKAQlEKEINDRRLELQEFKilkdkkdakireLEARVSDLELEKVKLVNAGSErlraVKDI 651
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   376 EKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKVDGNHNLL-----TKLSLEEENCLIQLKCEN 450
Cdd:pfam15921  652 KQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELeqtrnTLKSMEGSDGHAMKVAMG 731
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   451 LQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEgRQKVAEEIEKMSSRESALQIKILDLE 530
Cdd:pfam15921  732 MQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE-KNKMAGELEVLRSQERRLKEKVANME 810
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|.
gi 296179399   531 TELRKKNEEQNQlvCKMNSKAQHQEVCLKEVQNSLEKSENQ 571
Cdd:pfam15921  811 VALDKASLQFAE--CQDIIQRQEQESVRLKLQHTLDVKELQ 849
PRK12704 PRK12704
phosphodiesterase; Provisional
376-525 1.02e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 376 EKKQKTLIEMYKTQVQKLQEAAEIVKSrcENLLHKNNQITKTKNKNVEKVDGNHNLLTKLsleeENCLIQlKCENLQQKL 455
Cdd:PRK12704  30 EAKIKEAEEEAKRILEEAKKEAEAIKK--EALLEAKEEIHKLRNEFEKELRERRNELQKL----EKRLLQ-KEENLDRKL 102
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296179399 456 EQMDAENKELEKklanQEECLKHSNLKFKEKSAEYTALARQLEAALE--------EGRQKVAEEIEKMSSRESALQIK 525
Cdd:PRK12704 103 ELLEKREEELEK----KEKELEQKQQELEKKEEELEELIEEQLQELErisgltaeEAKEILLEKVEEEARHEAAVLIK 176
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
12-530 1.28e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399  12 EELFCHLKTISEKEDLPRCTSE--SHLSCLKQDILNEKTELEATLKEAELVTHSVELLLPLFKDTIEKINFENANLSALN 89
Cdd:PRK03918 200 KELEEVLREINEISSELPELREelEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE 279
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399  90 LKISEQKEILIKELDTFKSVKLALEHLLRKRDYKQTGDNLSSML------LENLTDNESENTNLKKKVFEKEAHIQELSC 163
Cdd:PRK03918 280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIngieerIKELEEKEERLEELKKKLKELEKRLEELEE 359
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 164 ---LFQSEKANTLKANRFSQSVKVVH-ERLQIQIHKREAENDKLKEYVKSLETKIAKWNLQSRMNKNEAIVMKEASRQKT 239
Cdd:PRK03918 360 rheLYEEAKAKKEELERLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCP 439
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 240 VALKKASKVYKQRLdhftgaIEKLTSQIRDQEAKLSETISASnawkshyEKIVIEKTELEVQIETMKKqIINLLEDLKKM 319
Cdd:PRK03918 440 VCGRELTEEHRKEL------LEEYTAELKRIEKELKEIEEKE-------RKLRKELRELEKVLKKESE-LIKLKELAEQL 505
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 320 EdhgknSCEEILRKVHSIEYENETLNLEntKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEmyktQVQKLQEAAEI 399
Cdd:PRK03918 506 K-----ELEEKLKKYNLEELEKKAEEYE--KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK----KLDELEEELAE 574
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 400 VKSRCENLLHKNNQITKTKNKNVEKVDGNHNLL--TKLSLEEENCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLK 477
Cdd:PRK03918 575 LLKELEELGFESVEELEERLKELEPFYNEYLELkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 478 -HSNLKFKEKSAEYTALARQLEAA------LEEGRQKVAEEIEKMSSRESALQIKILDLE 530
Cdd:PRK03918 655 kYSEEEYEELREEYLELSRELAGLraeleeLEKRREEIKKTLEKLKEELEEREKAKKELE 714
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
307-420 1.84e-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: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399  307 KQIINLLEDLKKMEDHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMY 386
Cdd:pfam11559  34 ARIINVIYELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNE 113
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 296179399  387 KTQVQKLQEAAEIVKSRCENLLHKNN-QITKTKNK 420
Cdd:pfam11559 114 KEELQRLKNALQQIKTQFAHEVKKRDrEIEKLKER 148
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
187-538 3.26e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 3.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 187 ERLQIQIHKREAENdkLKEYVKSLETKIAKwnlqsrmnkneaivmkeaSRQKTVALKKASKVYKQRLDHFTGAIEKLTSQ 266
Cdd:PRK02224 333 CRVAAQAHNEEAES--LREDADDLEERAEE------------------LREEAAELESELEEAREAVEDRREEIEELEEE 392
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 267 IRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKME---DHGK-NSCEEILRK---VHSIEY 339
Cdd:PRK02224 393 IEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEallEAGKcPECGQPVEGsphVETIEE 472
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 340 ENEtlnlENTKLKTTLAALKDEVVSVE---NELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITK 416
Cdd:PRK02224 473 DRE----RVEELEAELEDLEEEVEEVEerlERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE 548
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 417 TKNKNVEKvdgnHNLLTKLSLEEENCLIQLKceNLQQKLEQMDAENKELEK----------------KLANQEECLKHSN 480
Cdd:PRK02224 549 LEAEAEEK----REAAAEAEEEAEEAREEVA--ELNSKLAELKERIESLERirtllaaiadaedeieRLREKREALAELN 622
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296179399 481 LKFKEKSAEYTALARQLEAALEEGR---------------QKVAEEIEKMSSRESALQIKILDLETELRKKNE 538
Cdd:PRK02224 623 DERRERLAEKRERKRELEAEFDEARieearedkeraeeylEQVEEKLDELREERDDLQAEIGAVENELEELEE 695
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
297-577 4.84e-03

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 39.84  E-value: 4.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 297 ELEVQIETMKKQIINLLEDLKKMEDHGKNSCEEILRKVHSIEYENEtlnLENTKLKTTLAALKDEV--VSVENELSELQE 374
Cdd:PLN03229 433 ELEGEVEKLKEQILKAKESSSKPSELALNEMIEKLKKEIDLEYTEA---VIAMGLQERLENLREEFskANSQDQLMHPVL 509
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 375 VEKKQKTLIEM---------YKTQVQKLQEAAEIvkSRCENLLHKNNQITKTK---NKNVEKVDGNHNLLTKLSLeeenc 442
Cdd:PLN03229 510 MEKIEKLKDEFnkrlsrapnYLSLKYKLDMLNEF--SRAKALSEKKSKAEKLKaeiNKKFKEVMDRPEIKEKMEA----- 582
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 443 liqLKCENLQQKLEQMDAENKELEKKL--ANQE------ECLKHSNL-----KFKEKSAEYTALARQLEAALEEGRQKVA 509
Cdd:PLN03229 583 ---LKAEVASSGASSGDELDDDLKEKVekMKKEielelaGVLKSMGLevigvTKKNKDTAEQTPPPNLQEKIESLNEEIN 659
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 510 EEIEKMsSRESALQIKILDLETELRK----------------KNEEQNQLVCKMNSKA--QHQEVCLKEVQNSLEKSENQ 571
Cdd:PLN03229 660 KKIERV-IRSSDLKSKIELLKLEVAKasktpdvtekekiealEQQIKQKIAEALNSSElkEKFEELEAELAAARETAAES 738

                 ....*.
gi 296179399 572 NESIKN 577
Cdd:PLN03229 739 NGSLKN 744
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
252-522 6.58e-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: 6.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   252 RLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEDHGKNSCEEIL 331
Cdd:TIGR02169  682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   332 RKVHSIEYENETLNlentKLKTTLAALKDE-----VVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCEN 406
Cdd:TIGR02169  762 ELEARIEELEEDLH----KLEEALNDLEARlshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399   407 LLHKNNQITKTKNKNVEKVDGNHNLLTKL------------SLEEENCLIQLKCENLQQKLEQMDAENKELEKKLANQEE 474
Cdd:TIGR02169  838 LQEQRIDLKEQIKSIEKEIENLNGKKEELeeeleeleaalrDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 296179399   475 CLKHSNLKFKEKSAEYTALARQLEAALEEGRQ-----KVAEEIEKMSSRESAL 522
Cdd:TIGR02169  918 RLSELKAKLEALEEELSEIEDPKGEDEEIPEEelsleDVQAELQRVEEEIRAL 970
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
294-523 7.20e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 7.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 294 EKTELEVQIETMKKQIINLLEDLKKMEDhgknsceeilrKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQ 373
Cdd:COG3883   17 QIQAKQKELSELQAELEAAQAELDALQA-----------ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296179399 374 EVEKKQktLIEMYK-----TQVQKLQEAAEIVK--SRCENLlhknNQITKTKNKNVEKVDGnhnllTKLSLEEENCLIQL 446
Cdd:COG3883   86 EELGER--ARALYRsggsvSYLDVLLGSESFSDflDRLSAL----SKIADADADLLEELKA-----DKAELEAKKAELEA 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296179399 447 KCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKVAEEIEKMSSRESALQ 523
Cdd:COG3883  155 KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
 
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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