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Conserved domains on  [gi|2067662264|ref|NP_001382451|]
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protein BCAP isoform i [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]; ...
 252-532 1.98e-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: 1.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 252 RLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEdhgknscEEIL 331
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE-------QDIA 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 332 RKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKN 411
Cdd:COG1196   306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 412 NQITKTKNKNVEKVDGNHNLLTKLSLEEEncliqlKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYT 491
Cdd:COG1196   386 EELLEALRAAAELAAQLEELEEAEEALLE------RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2067662264 492 ALARQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETE 532
Cdd:COG1196   460 ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 252-532 1.98e-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: 1.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 252 RLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEdhgknscEEIL 331
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE-------QDIA 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 332 RKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKN 411
Cdd:COG1196   306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 412 NQITKTKNKNVEKVDGNHNLLTKLSLEEEncliqlKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYT 491
Cdd:COG1196   386 EELLEALRAAAELAAQLEELEEAEEALLE------RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2067662264 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 2.22e-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: 53.92  E-value: 2.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  297 ELEVQIETMKKQIINLLEDLKKME---DHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQ 373
Cdd:TIGR02169  678 RLRERLEGLKRELSSLQSELRRIEnrlDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  374 EVEKKQKTLIEMYKTQVQKLQEA-----AEIVKSRCENLLHKNNQITKTKNKNVEKVDGNHNLLTKLSLEEEncLIQLKC 448
Cdd:TIGR02169  758 SELKELEARIEELEEDLHKLEEAlndleARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE--YLEKEI 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  449 ENLQQKLEQMDAENKELEKKLANqeecLKHSNLKFKEKSAEYTALARQLEAALEEgrqkVAEEIEKMSSRESALQIKILD 528
Cdd:TIGR02169  836 QELQEQRIDLKEQIKSIEKEIEN----LNGKKEELEEELEELEAALRDLESRLGD----LKKERDELEAQLRELERKIEE 907

                          250
                   ....*....|....*
gi 2067662264  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 3.18e-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: 43.57  E-value: 3.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264   85 LSALNLKISEQKEILIKELDTFKSVKLALEhllrkrDYKQTGDNLSSMLLENLTDNESENTNLKKKVFEKEAHIQELSCL 164
Cdd:pfam15921  463 VSSLTAQLESTKEMLRKVVEELTAKKMTLE------SSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHL 536

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  165 FQSEKantlkanrFSQSVKVVHERLQIQIHKREAENDKLKEYVKSLETKIAKWNLQSRMNKNEAIVMKEASRQKTVALKK 244
Cdd:pfam15921  537 KNEGD--------HLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQE 608

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  245 AsKVYKQRLDhftGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEDHGK 324
Cdd:pfam15921  609 F-KILKDKKD---AKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFR 684

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  325 NSCEEIlrkvhsiEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRC 404
Cdd:pfam15921  685 NKSEEM-------ETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAM 757

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  405 ENLLHKNNQITKTKNKnvekvdgnhnlltklsLEEENCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFK 484
Cdd:pfam15921  758 TNANKEKHFLKEEKNK----------------LSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFA 821


                   .
gi 2067662264  485 E 485
Cdd:pfam15921  822 E 822
PLN02939 PLN02939
transferase, transferring glycosyl groups
 186-517 4.79e-04

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 42.97  E-value: 4.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 186 HERLQIQIHKREAENDKLKEYVKSLETKIAKWNLQsrmnknEAIVMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTS 265
Cdd:PLN02939   97 HNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLE------DLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQG 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 266 QIRDQEAKLSETISASNAwkSHYEKIVIEKteLEVQIETMKKQIINLLEDLKKMedhgknsceeilrkVHSIEYENETLN 345
Cdd:PLN02939  171 KINILEMRLSETDARIKL--AAQEKIHVEI--LEEQLEKLRNELLIRGATEGLC--------------VHSLSKELDVLK 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 346 LENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVK-----------SRCENLLHKNNQI 414
Cdd:PLN02939  233 EENMLLKDDIQFLKAELIEVAETEERVFKLEKERSLLDASLRELESKFIVAQEDVSklsplqydcwwEKVENLQDLLDRA 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 415 TKTKNKNVEKVDGNHNLLTKL-----SLEEENC--LIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEks 487
Cdd:PLN02939  313 TNQVEKAALVLDQNQDLRDKVdkleaSLKEANVskFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQD-- 390

                         330       340       350
                  ....*....|....*....|....*....|.
gi 2067662264 488 aeytalarQLEAALEEGRQKVAEE-IEKMSS 517
Cdd:PLN02939  391 --------TLSKLKEESKKRSLEHpADDMPS 413
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 252-532 1.98e-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: 1.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 252 RLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEdhgknscEEIL 331
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE-------QDIA 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 332 RKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKN 411
Cdd:COG1196   306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 412 NQITKTKNKNVEKVDGNHNLLTKLSLEEEncliqlKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYT 491
Cdd:COG1196   386 EELLEALRAAAELAAQLEELEEAEEALLE------RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2067662264 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 2.22e-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: 53.92  E-value: 2.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  297 ELEVQIETMKKQIINLLEDLKKME---DHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQ 373
Cdd:TIGR02169  678 RLRERLEGLKRELSSLQSELRRIEnrlDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  374 EVEKKQKTLIEMYKTQVQKLQEA-----AEIVKSRCENLLHKNNQITKTKNKNVEKVDGNHNLLTKLSLEEEncLIQLKC 448
Cdd:TIGR02169  758 SELKELEARIEELEEDLHKLEEAlndleARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE--YLEKEI 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  449 ENLQQKLEQMDAENKELEKKLANqeecLKHSNLKFKEKSAEYTALARQLEAALEEgrqkVAEEIEKMSSRESALQIKILD 528
Cdd:TIGR02169  836 QELQEQRIDLKEQIKSIEKEIEN----LNGKKEELEEELEELEAALRDLESRLGD----LKKERDELEAQLRELERKIEE 907

                          250
                   ....*....|....*
gi 2067662264  529 LETELRKKNEEQNQL 543
Cdd:TIGR02169  908 LEAQIEKKRKRLSEL 922
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 350-543 2.41e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 2.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 350 KLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKVDGNH 429
Cdd:COG1196   236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 430 NLLTKLSLEEENclIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKVA 509
Cdd:COG1196   316 ERLEELEEELAE--LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2067662264 510 EEIEKmSSRESALQIKILDLETELRKKNEEQNQL 543
Cdd:COG1196   394 AAAEL-AAQLEELEEAEEALLERLERLEEELEEL 426
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 337-543 4.56e-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: 53.14  E-value: 4.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  337 IEYENETLNLENT--KLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQI 414
Cdd:TIGR02168  673 LERRREIEELEEKieELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  415 TKTKNKNVEKVDGNHNLLTKLSLEEENCLIQLkcENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALA 494
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEI--EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2067662264  495 RQLEAA------LEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKNEEQNQL 543
Cdd:TIGR02168  831 RRIAATerrledLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 260-500 7.71e-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: 7.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  260 IEKLTSQIRDQEAKLSETISASNawkshyekiviEKTELEVQIETMKKQIINLLEDLKKMEDHGKNSCEEILRKVHSIEY 339
Cdd:TIGR02168  255 LEELTAELQELEEKLEELRLEVS-----------ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  340 ENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKN 419
Cdd:TIGR02168  324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  420 KNVEKV---DGNHNLLTKLSLEEENCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQ 496
Cdd:TIGR02168  404 RLEARLerlEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483


                   ....
gi 2067662264  497 LEAA 500
Cdd:TIGR02168  484 LAQL 487
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 135-394 2.37e-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: 2.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  135 ENLTDNESENTNLKKKVFEKEAHIQELSCLFQSEKANTLKANRFSQSVKVVHERLQIQIHKREAENDKLKEYVKSLETKI 214
Cdd:TIGR02168  684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  215 AKWNLQsrmnkneaivmKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIE 294
Cdd:TIGR02168  764 EELEER-----------LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  295 KTELEVQIETMKKQIINLLEDLKKME---DHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSE 371
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAaeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912

                          250       260
                   ....*....|....*....|...
gi 2067662264  372 LQEVEKKQKTLIEMYKTQVQKLQ 394
Cdd:TIGR02168  913 LRRELEELREKLAQLELRLEGLE 935
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 355-543 3.04e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.97  E-value: 3.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  355 LAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKVDGNHNLLTK 434
Cdd:TIGR02168  227 LALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQI 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  435 LSLEEENCLIQLK-----CENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEaALEEGRQKVA 509
Cdd:TIGR02168  307 LRERLANLERQLEeleaqLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE-ELEEQLETLR 385

                          170       180       190
                   ....*....|....*....|....*....|....
gi 2067662264  510 EEIEKMSSRESALQIKILDLETELRKKNEEQNQL 543
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 350-543 4.68e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 4.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 350 KLKTTLAALKDEvvSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRcenLLHKNNQITKTKNKNVEKVDGNH 429
Cdd:COG1196   224 ELEAELLLLKLR--ELEAELEELEAELEELEAELEELEAELAELEAELEELRLE---LEELELELEEAQAEEYELLAELA 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 430 NLLTKLSLEEEncliqlKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKVA 509
Cdd:COG1196   299 RLEQDIARLEE------RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2067662264 510 EEIEKMSSRESALQIKILDLETELRKKNEEQNQL 543
Cdd:COG1196   373 ELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 294-517 6.26e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.53  E-value: 6.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 294 EKTELEVQIETMKKQIINLLEDLKKMedhgKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQ 373
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAAL----KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 374 EVEKKQKtliEMYKTQVQKLQEAAEIvkSRCENLLHKNN------------QITKTKNKNVEKVDGNHNLLTKLSLEeen 441
Cdd:COG4942    97 AELEAQK---EELAELLRALYRLGRQ--PPLALLLSPEDfldavrrlqylkYLAPARREQAEELRADLAELAALRAE--- 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2067662264 442 clIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTAL---ARQLEAALEEGRQKVAEEIEKMSS 517
Cdd:COG4942   169 --LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELqqeAEELEALIARLEAEAAAAAERTPA 245
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 166-505 1.71e-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: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 166 QSEKAntLKANRFSQSVKVV-HERLQIQIHKREAENDKLKEYVKSLETKIAKWNLQSRMNKNEaivmKEASRQKTVALKK 244
Cdd:COG1196   208 QAEKA--ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE----LEELRLELEELEL 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 245 ASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSEtisasnawkshyekIVIEKTELEVQIETMKKQIINLLEDLkkmedhgk 324
Cdd:COG1196   282 ELEEAQAEEYELLAELARLEQDIARLEERRRE--------------LEERLEELEEELAELEEELEELEEEL-------- 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 325 nscEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRC 404
Cdd:COG1196   340 ---EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 405 ENLLHKNNQITKTKNKNVEKVDGNHNLLTKLSLEEencliqlkcENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFK 484
Cdd:COG1196   417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEE---------AELEEEEEALLELLAELLEEAALLEAALAELLEELA 487

                         330       340
                  ....*....|....*....|.
gi 2067662264 485 EKSAEYTALARQLEAALEEGR 505
Cdd:COG1196   488 EAAARLLLLLEAEADYEGFLE 508
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 85-485 3.18e-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: 43.57  E-value: 3.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264   85 LSALNLKISEQKEILIKELDTFKSVKLALEhllrkrDYKQTGDNLSSMLLENLTDNESENTNLKKKVFEKEAHIQELSCL 164
Cdd:pfam15921  463 VSSLTAQLESTKEMLRKVVEELTAKKMTLE------SSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHL 536

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  165 FQSEKantlkanrFSQSVKVVHERLQIQIHKREAENDKLKEYVKSLETKIAKWNLQSRMNKNEAIVMKEASRQKTVALKK 244
Cdd:pfam15921  537 KNEGD--------HLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQE 608

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  245 AsKVYKQRLDhftGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEDHGK 324
Cdd:pfam15921  609 F-KILKDKKD---AKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFR 684

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  325 NSCEEIlrkvhsiEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRC 404
Cdd:pfam15921  685 NKSEEM-------ETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAM 757

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  405 ENLLHKNNQITKTKNKnvekvdgnhnlltklsLEEENCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFK 484
Cdd:pfam15921  758 TNANKEKHFLKEEKNK----------------LSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFA 821


                   .
gi 2067662264  485 E 485
Cdd:pfam15921  822 E 822
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
196-396 3.67e-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: 3.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 196 REAENDKLKEYVKSLETKIAKwnLQSRMNKNEAIVMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKL- 274
Cdd:COG3206   166 LELRREEARKALEFLEEQLPE--LRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLa 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 275 --------SETISASNAWKSHYEKIVIEKTELEVQIETMKK-------QIINLLEDLKKMEDHGKnscEEILRKVHSIEY 339
Cdd:COG3206   244 alraqlgsGPDALPELLQSPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQ---QEAQRILASLEA 320

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2067662264 340 ENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEA 396
Cdd:COG3206   321 ELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
PLN02939 PLN02939
transferase, transferring glycosyl groups
 186-517 4.79e-04

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 42.97  E-value: 4.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 186 HERLQIQIHKREAENDKLKEYVKSLETKIAKWNLQsrmnknEAIVMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTS 265
Cdd:PLN02939   97 HNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLE------DLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQG 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 266 QIRDQEAKLSETISASNAwkSHYEKIVIEKteLEVQIETMKKQIINLLEDLKKMedhgknsceeilrkVHSIEYENETLN 345
Cdd:PLN02939  171 KINILEMRLSETDARIKL--AAQEKIHVEI--LEEQLEKLRNELLIRGATEGLC--------------VHSLSKELDVLK 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 346 LENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVK-----------SRCENLLHKNNQI 414
Cdd:PLN02939  233 EENMLLKDDIQFLKAELIEVAETEERVFKLEKERSLLDASLRELESKFIVAQEDVSklsplqydcwwEKVENLQDLLDRA 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 415 TKTKNKNVEKVDGNHNLLTKL-----SLEEENC--LIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEks 487
Cdd:PLN02939  313 TNQVEKAALVLDQNQDLRDKVdkleaSLKEANVskFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQD-- 390

                         330       340       350
                  ....*....|....*....|....*....|.
gi 2067662264 488 aeytalarQLEAALEEGRQKVAEE-IEKMSS 517
Cdd:PLN02939  391 --------TLSKLKEESKKRSLEHpADDMPS 413
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
292-543 6.38e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 6.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  292 VIEKTELEVQIETMKKQIinllEDLKKMEDHGknscEEILRKVhsieyenETLnlentklkTTLAALKDEVVSVENELSE 371
Cdd:COG4913    217 MLEEPDTFEAADALVEHF----DDLERAHEAL----EDAREQI-------ELL--------EPIRELAERYAAARERLAE 273

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  372 LQEVEKKQKTLIEmyKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKVDGNHNLLTKLSLEEEncliqlkcENL 451
Cdd:COG4913    274 LEYLRAALRLWFA--QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRL--------EQL 343

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  452 QQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKVAEEIEKMSSRESALQikilDLET 531
Cdd:COG4913    344 EREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR----DLRR 419

                          250
                   ....*....|..
gi 2067662264  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 6.53e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.06  E-value: 6.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 232 KEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIIN 311
Cdd:COG4942    22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 312 LLEDLK-------KMEDHGK-------NSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEK 377
Cdd:COG4942   102 QKEELAellralyRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181

                         170       180
                  ....*....|....*....|....*.
gi 2067662264 378 KQKTLIEMYKTQVQKLQEAAEIVKSR 403
Cdd:COG4942   182 ELEEERAALEALKAERQKLLARLEKE 207
PRK12704 PRK12704
phosphodiesterase; Provisional
 376-525 9.69e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 9.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 376 EKKQKTLIEMYKTQVQKLQEAAEIVKSrcENLLHKNNQITKTKNKNVEKVDGNHNLLTKLsleeENCLIQlKCENLQQKL 455
Cdd:PRK12704   30 EAKIKEAEEEAKRILEEAKKEAEAIKK--EALLEAKEEIHKLRNEFEKELRERRNELQKL----EKRLLQ-KEENLDRKL 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2067662264 456 EQMDAENKELEKklanQEECLKHSNLKFKEKSAEYTALARQLEAALE--------EGRQKVAEEIEKMSSRESALQIK 525
Cdd:PRK12704  103 ELLEKREEELEK----KEKELEQKQQELEKKEEELEELIEEQLQELErisgltaeEAKEILLEKVEEEARHEAAVLIK 176
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 307-420 1.44e-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: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 307 KQIINLLEDLKKMEDHGKNSCEEILRKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMY 386
Cdd:pfam11559  34 ARIINVIYELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNE 113

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2067662264 387 KTQVQKLQEAAEIVKSRCENLLHKNN-QITKTKNK 420
Cdd:pfam11559 114 KEELQRLKNALQQIKTQFAHEVKKRDrEIEKLKER 148
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
12-530 1.67e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  12 EELFCHLKTISEKEDLPRCTSE--SHLSCLKQDILNEKTELEATLKEAELVTHSVELLLPLFKDTIEKINFENANLSALN 89
Cdd:PRK03918  200 KELEEVLREINEISSELPELREelEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  90 LKISEQKEILIKELDTFKSVKLALEHLLRKRDYKQTGDNLSSML------LENLTDNESENTNLKKKVFEKEAHIQELSC 163
Cdd:PRK03918  280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIngieerIKELEEKEERLEELKKKLKELEKRLEELEE 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 164 ---LFQSEKANTLKANRFSQSVKVVH-ERLQIQIHKREAENDKLKEYVKSLETKIAKWNLQSRMNKNEAIVMKEASRQKT 239
Cdd:PRK03918  360 rheLYEEAKAKKEELERLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCP 439

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 240 VALKKASKVYKQRLdhftgaIEKLTSQIRDQEAKLSETISASnawkshyEKIVIEKTELEVQIETMKKqIINLLEDLKKM 319
Cdd:PRK03918  440 VCGRELTEEHRKEL------LEEYTAELKRIEKELKEIEEKE-------RKLRKELRELEKVLKKESE-LIKLKELAEQL 505

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 320 EdhgknSCEEILRKVHSIEYENETLNLEntKLKTTLAALKDEVVSVENELSELQEVEKKQKTLIEmyktQVQKLQEAAEI 399
Cdd:PRK03918  506 K-----ELEEKLKKYNLEELEKKAEEYE--KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK----KLDELEEELAE 574

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 400 VKSRCENLLHKNNQITKTKNKNVEKVDGNHNLL--TKLSLEEENCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLK 477
Cdd:PRK03918  575 LLKELEELGFESVEELEERLKELEPFYNEYLELkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 478 -HSNLKFKEKSAEYTALARQLEAA------LEEGRQKVAEEIEKMSSRESALQIKILDLE 530
Cdd:PRK03918  655 kYSEEEYEELREEYLELSRELAGLraeleeLEKRREEIKKTLEKLKEELEEREKAKKELE 714
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 294-523 4.36e-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: 4.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 294 EKTELEVQIETMKKQIINLLEDLKKMEDhgknsceeilrKVHSIEYENETLNLENTKLKTTLAALKDEVVSVENELSELQ 373
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQA-----------ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 374 EVEKKQktLIEMYK-----TQVQKLQEAAEIVK--SRCENLlhknNQITKTKNKNVEKVDGnhnllTKLSLEEENCLIQL 446
Cdd:COG3883    86 EELGER--ARALYRsggsvSYLDVLLGSESFSDflDRLSAL----SKIADADADLLEELKA-----DKAELEAKKAELEA 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2067662264 447 KCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKVAEEIEKMSSRESALQ 523
Cdd:COG3883   155 KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 2-535 5.26e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 39.72  E-value: 5.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264    2 EKAVNDGSHSEELFCHLKTISEKEDLPRCTSESHLSCLKQDILNEKTELEATLKEAELVTHSVELLLPLFKDTIEKINFE 81
Cdd:pfam15921  285 EKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTE 364

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264   82 NANLSALNLKISEQKEILIKELDTfKSVKLALEHLLRKRdykqtgdnlssmLLENLTDNESENTNLKKKVFEKEAHIQEL 161
Cdd:pfam15921  365 RDQFSQESGNLDDQLQKLLADLHK-REKELSLEKEQNKR------------LWDRDTGNSITIDHLRRELDDRNMEVQRL 431

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  162 SCLFQSEKANtlkanrfsqsvkvVHERLQIQIHKREAENDKLkEYVKSLETKI--AKWNLQSRMNKNEAIVMKEASRQKT 239
Cdd:pfam15921  432 EALLKAMKSE-------------CQGQMERQMAAIQGKNESL-EKVSSLTAQLesTKEMLRKVVEELTAKKMTLESSERT 497

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  240 VALKKASKVYKQRLDHFTGA-IEKLTSQIrdqEAKLSETISASNAW------KSHYEKIVIEKTELEVQIETMKKQIINL 312
Cdd:pfam15921  498 VSDLTASLQEKERAIEATNAeITKLRSRV---DLKLQELQHLKNEGdhlrnvQTECEALKLQMAEKDKVIEILRQQIENM 574

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  313 LEDLKKmedHGKNSCEEILRKVH-SIEYENETLNLENTK------------LKTTLAALKDEVVSVENELSE----LQEV 375
Cdd:pfam15921  575 TQLVGQ---HGRTAGAMQVEKAQlEKEINDRRLELQEFKilkdkkdakireLEARVSDLELEKVKLVNAGSErlraVKDI 651

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  376 EKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKVDGNHNLL-----TKLSLEEENCLIQLKCEN 450
Cdd:pfam15921  652 KQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELeqtrnTLKSMEGSDGHAMKVAMG 731

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  451 LQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEgRQKVAEEIEKMSSRESALQIKILDLE 530
Cdd:pfam15921  732 MQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE-KNKMAGELEVLRSQERRLKEKVANME 810


                   ....*
gi 2067662264  531 TELRK 535
Cdd:pfam15921  811 VALDK 815
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
187-538 5.63e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 5.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 187 ERLQIQIHKREAENdkLKEYVKSLETKIAKwnlqsrmnkneaivmkeaSRQKTVALKKASKVYKQRLDHFTGAIEKLTSQ 266
Cdd:PRK02224  333 CRVAAQAHNEEAES--LREDADDLEERAEE------------------LREEAAELESELEEAREAVEDRREEIEELEEE 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 267 IRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKME---DHGK-NSCEEILRK---VHSIEY 339
Cdd:PRK02224  393 IEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEallEAGKcPECGQPVEGsphVETIEE 472

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 340 ENEtlnlENTKLKTTLAALKDEVVSVE---NELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITK 416
Cdd:PRK02224  473 DRE----RVEELEAELEDLEEEVEEVEerlERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE 548

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264 417 TKNKNVEKvdgnHNLLTKLSLEEENCLIQLKceNLQQKLEQMDAENKELEK----------------KLANQEECLKHSN 480
Cdd:PRK02224  549 LEAEAEEK----REAAAEAEEEAEEAREEVA--ELNSKLAELKERIESLERirtllaaiadaedeieRLREKREALAELN 622

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2067662264 481 LKFKEKSAEYTALARQLEAALEEGR---------------QKVAEEIEKMSSRESALQIKILDLETELRKKNE 538
Cdd:PRK02224  623 DERRERLAEKRERKRELEAEFDEARieearedkeraeeylEQVEEKLDELREERDDLQAEIGAVENELEELEE 695
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 252-522 6.86e-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: 6.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  252 RLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEDHGKNSCEEIL 331
Cdd:TIGR02169  682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  332 RKVHSIEYENETLNlentKLKTTLAALKDE-----VVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCEN 406
Cdd:TIGR02169  762 ELEARIEELEEDLH----KLEEALNDLEARlshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662264  407 LLHKNNQITKTKNKNVEKVDGNHNLLTKL------------SLEEENCLIQLKCENLQQKLEQMDAENKELEKKLANQEE 474
Cdd:TIGR02169  838 LQEQRIDLKEQIKSIEKEIENLNGKKEELeeeleeleaalrDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2067662264  475 CLKHSNLKFKEKSAEYTALARQLEAALEEGRQ-----KVAEEIEKMSSRESAL 522
Cdd:TIGR02169  918 RLSELKAKLEALEEELSEIEDPKGEDEEIPEEelsleDVQAELQRVEEEIRAL 970
 
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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