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Conserved domains on  [gi|568982040|ref|XP_006516839|]
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cancer-associated gene 1 protein homolog isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CAGE1 pfam15066
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ...
1-526 0e+00

Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.


:

Pssm-ID: 464481  Cd Length: 528  Bit Score: 810.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040    1 MSESETINVNGPSQDFSYSDSPFCMEASFSSSDLLQSETKNVKRGNESTHTFSEDIYSTEGSLLGDINLGNYPESEQNQP 80
Cdd:pfam15066   1 MSESDAMNVSGLSQDLTHSDSPLCMETSSTTSDLPQNEIKNVKRENESKFTLSEDIYSTLDNLLGDINIGSYSQNVLIQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   81 ANTRLSSLRQFEPICKFHWIEAFNDEM-TVEDLRGAFSYSEKPELPSQVYNDAADGSEKPDPFKEESSVESSISENKDEL 159
Cdd:pfam15066  81 VDTSISSLRQFEPICKFHWTEAFNDEMtTFQNLTEGFSYTEKPELQSHVYNYAKDTNIKQDSFKEENPVETSISTNKDQL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040  160 VPAPVRKSPRSLCLNYYRGEAQPLTEAPFVRSAVVDVGLNISQPQSFLDKENVCKNGDNSSDRENCFEQLDLRAIYKAEE 239
Cdd:pfam15066 161 ANECVRQSSRSPPLIHCSGETLPFTEKSLAKSTAKESALNPSQPQSFLYEENVPRNVEKPFYKENSFSLLDLRANYKTEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040  240 PEVSSKEVQNSGEISELSVSHQEEVTEDGVDSLAITSPWSPAGI-FKGSGPQDNSLRPDREVSCEGLEPLEEDMALNEAL 318
Cdd:pfam15066 241 TEVSSKEIQNSGEIPEMSVSHQKEVTEEGVESPEIASTWSPAGIsWSSGASQENCKTPDTEQSFESLQPLEEDMALNEVL 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040  319 QKLKQTNKKQELQIQDLHGKNLNLENRVQELQTKVTKQHVLVDIINKLKVNIEELINDKYNVILEKNDINKKLQDLQEAS 398
Cdd:pfam15066 321 QKLKHTNRKQQMQIQDLQCSNLYLEKKVKELQMKITKQQVFVDIINKLKENVEELIEDKYNVILEKNDINKTLQNLQEIL 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040  399 AHTKKHLQESKKDKESLQLQVKKIKVHYVRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEELQRLQRHKGELEKATSSA 478
Cdd:pfam15066 401 ANTQKHLQESRKEKETLQLELKKIKVNYVHLQERYITEMQQKNKSVSQCLEMDKTLSKKEEEVERLQQLKGELEKATTSA 480
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 568982040  479 LDLLKREKEIREQEFLSFQEEFQRREKESLKERRKLKSRVEKLVAQVK 526
Cdd:pfam15066 481 LDLLKREKETREQEFLSLQEEFQKHEKENLEERQKLKSRLEKLVAQVK 528
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
385-691 2.00e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.51  E-value: 2.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   385 NDINKKLQDLQEASAHTKKhLQESKKDKESLQLQVkkIKVHYVRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEELQRL 464
Cdd:TIGR02168  196 NELERQLKSLERQAEKAER-YKELKAELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   465 QRHKGELEKATSSA---LDLLKREKEIREQEFLSFQEEFQRREKESLK---ERRKLKSRVEKLVAQVKSLLFTCESERAQ 538
Cdd:TIGR02168  273 RLEVSELEEEIEELqkeLYALANEISRLEQQKQILRERLANLERQLEEleaQLEELESKLDELAEELAELEEKLEELKEE 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   539 TMALQRQVEELKLENLELRQLAAKREAQACTPSFEITQSKEQLEEAVEPDITQETKGTHcnLFLNRSSCKENLELQPLKK 618
Cdd:TIGR02168  353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER--LEDRRERLQQEIEELLKKL 430
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568982040   619 TSPLASGIHSLLALRIGLLTcqDLATPDAELCQESKKANdimlQRLKDCQLKKKDLDKELLKHKNRIATLKEL 691
Cdd:TIGR02168  431 EEAELKELQAELEELEEELE--ELQEELERLEEALEELR----EELEEAEQALDAAERELAQLQARLDSLERL 497
 
Name Accession Description Interval E-value
CAGE1 pfam15066
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ...
1-526 0e+00

Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.


Pssm-ID: 464481  Cd Length: 528  Bit Score: 810.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040    1 MSESETINVNGPSQDFSYSDSPFCMEASFSSSDLLQSETKNVKRGNESTHTFSEDIYSTEGSLLGDINLGNYPESEQNQP 80
Cdd:pfam15066   1 MSESDAMNVSGLSQDLTHSDSPLCMETSSTTSDLPQNEIKNVKRENESKFTLSEDIYSTLDNLLGDINIGSYSQNVLIQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   81 ANTRLSSLRQFEPICKFHWIEAFNDEM-TVEDLRGAFSYSEKPELPSQVYNDAADGSEKPDPFKEESSVESSISENKDEL 159
Cdd:pfam15066  81 VDTSISSLRQFEPICKFHWTEAFNDEMtTFQNLTEGFSYTEKPELQSHVYNYAKDTNIKQDSFKEENPVETSISTNKDQL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040  160 VPAPVRKSPRSLCLNYYRGEAQPLTEAPFVRSAVVDVGLNISQPQSFLDKENVCKNGDNSSDRENCFEQLDLRAIYKAEE 239
Cdd:pfam15066 161 ANECVRQSSRSPPLIHCSGETLPFTEKSLAKSTAKESALNPSQPQSFLYEENVPRNVEKPFYKENSFSLLDLRANYKTEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040  240 PEVSSKEVQNSGEISELSVSHQEEVTEDGVDSLAITSPWSPAGI-FKGSGPQDNSLRPDREVSCEGLEPLEEDMALNEAL 318
Cdd:pfam15066 241 TEVSSKEIQNSGEIPEMSVSHQKEVTEEGVESPEIASTWSPAGIsWSSGASQENCKTPDTEQSFESLQPLEEDMALNEVL 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040  319 QKLKQTNKKQELQIQDLHGKNLNLENRVQELQTKVTKQHVLVDIINKLKVNIEELINDKYNVILEKNDINKKLQDLQEAS 398
Cdd:pfam15066 321 QKLKHTNRKQQMQIQDLQCSNLYLEKKVKELQMKITKQQVFVDIINKLKENVEELIEDKYNVILEKNDINKTLQNLQEIL 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040  399 AHTKKHLQESKKDKESLQLQVKKIKVHYVRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEELQRLQRHKGELEKATSSA 478
Cdd:pfam15066 401 ANTQKHLQESRKEKETLQLELKKIKVNYVHLQERYITEMQQKNKSVSQCLEMDKTLSKKEEEVERLQQLKGELEKATTSA 480
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 568982040  479 LDLLKREKEIREQEFLSFQEEFQRREKESLKERRKLKSRVEKLVAQVK 526
Cdd:pfam15066 481 LDLLKREKETREQEFLSLQEEFQKHEKENLEERQKLKSRLEKLVAQVK 528
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
309-546 9.79e-09

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: 59.30  E-value: 9.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   309 EEDMALNEALQKLKQTNKKQ---ELQIQDLHGKNLNLENRVQELQTKV----TKQHVLVDIINKLKVNIEELINDKYNVI 381
Cdd:TIGR02168  257 ELTAELQELEEKLEELRLEVselEEEIEELQKELYALANEISRLEQQKqilrERLANLERQLEELEAQLEELESKLDELA 336
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   382 LEKNDINKKLQDLQEASAHTKKHLQESKKDKESLQLQVKKIKVHYVRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEEL 461
Cdd:TIGR02168  337 EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   462 QRLQRHKGELE-KATSSALDLLKREKEIREQEFLSFQEEFQRRE--KESLKERRKLKSR----VEKLVAQVKSLLFTCES 534
Cdd:TIGR02168  417 ERLQQEIEELLkKLEEAELKELQAELEELEEELEELQEELERLEeaLEELREELEEAEQaldaAERELAQLQARLDSLER 496
                          250
                   ....*....|..
gi 568982040   535 ERAQTMALQRQV 546
Cdd:TIGR02168  497 LQENLEGFSEGV 508
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
313-566 8.42e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.10  E-value: 8.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 313 ALNEALQKLKQTNKKQELQIQDLHGKNLNLENRVQELQTKVTKQHvlvDIINKLKVNIEELINDKYNVILEKNDINKKLQ 392
Cdd:COG1196  243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ---AEEYELLAELARLEQDIARLEERRRELEERLE 319
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 393 DLQEASAHTKKHLQESKKDKESLQLQVKkikvhyvRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEELQRLQRHKGELE 472
Cdd:COG1196  320 ELEEELAELEEELEELEEELEELEEELE-------EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 473 KAtssALDLLKREKEIREQEflsfQEEFQRREkESLKERRKLKSRVEKLVAQVKSLLFTCESERAQTMALQRQVEELKLE 552
Cdd:COG1196  393 RA---AAELAAQLEELEEAE----EALLERLE-RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
                        250
                 ....*....|....
gi 568982040 553 NLELRQLAAKREAQ 566
Cdd:COG1196  465 LAELLEEAALLEAA 478
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
306-528 5.95e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.06  E-value: 5.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 306 EPLEEDMALNEALQKLKQTNKKQELQIqdLHGKNlNLENRVQELQTKVTKQHVLVDIINKLKVNIEELINDKYNVILEKN 385
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEV--LREIN-EISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKR 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 386 DINKKLQDLQEASAHTKKHLQESKKDKESLQlQVKKIKVHYVRLQERYIAEIQQKNrsasqclEIEKTLSKKDEELQRLQ 465
Cdd:PRK03918 256 KLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELR-------EIEKRLSRLEEEINGIE 327
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 466 RHKGELEKATSSALDLLKREKEIREQ--EFLSFQEEFQR-----REKESLKERRKLKSrVEKLVAQVKSL 528
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRleELEERHELYEEakakkEELERLKKRLTGLT-PEKLEKELEEL 396
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
385-691 2.00e-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: 48.51  E-value: 2.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   385 NDINKKLQDLQEASAHTKKhLQESKKDKESLQLQVkkIKVHYVRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEELQRL 464
Cdd:TIGR02168  196 NELERQLKSLERQAEKAER-YKELKAELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   465 QRHKGELEKATSSA---LDLLKREKEIREQEFLSFQEEFQRREKESLK---ERRKLKSRVEKLVAQVKSLLFTCESERAQ 538
Cdd:TIGR02168  273 RLEVSELEEEIEELqkeLYALANEISRLEQQKQILRERLANLERQLEEleaQLEELESKLDELAEELAELEEKLEELKEE 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   539 TMALQRQVEELKLENLELRQLAAKREAQACTPSFEITQSKEQLEEAVEPDITQETKGTHcnLFLNRSSCKENLELQPLKK 618
Cdd:TIGR02168  353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER--LEDRRERLQQEIEELLKKL 430
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568982040   619 TSPLASGIHSLLALRIGLLTcqDLATPDAELCQESKKANdimlQRLKDCQLKKKDLDKELLKHKNRIATLKEL 691
Cdd:TIGR02168  431 EEAELKELQAELEELEEELE--ELQEELERLEEALEELR----EELEEAEQALDAAERELAQLQARLDSLERL 497
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
268-525 6.84e-03

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 40.00  E-value: 6.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 268 GVDSLAITSpwspagIFKGS--GPQDNSLRPDREVSCEGLEPLEEDM-ALNEALQK-LKQTNKKQElqiQDLHGKNLNLE 343
Cdd:NF033838  20 GVASVVVAS------LFLGGvvHAEEVRGGNNPTVTSSGNESQKEHAkEVESHLEKiLSEIQKSLD---KRKHTQNVALN 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 344 NRVQELQTKVTkqHVLVDIINKLKVNIEELINDKYNVILEKndINKKLQDLQEASAHTKKHLQESKKDKESlqlQVKKIK 423
Cdd:NF033838  91 KKLSDIKTEYL--YELNVLKEKSEAELTSKTKKELDAAFEQ--FKKDTLEPGKKVAEATKKVEEAEKKAKD---QKEEDR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 424 VHY----VRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEELQRLQRHKGELEKATSSALDLLKREKEIREQEFLSFQEE 499
Cdd:NF033838 164 RNYptntYKTLELEIAESDVEVKKAELELVKEEAKEPRDEEKIKQAKAKVESKKAEATRLEKIKTDREKAEEEAKRRADA 243
                        250       260
                 ....*....|....*....|....*....
gi 568982040 500 FQRREKESL---KERRKLKSRVEKLVAQV 525
Cdd:NF033838 244 KLKEAVEKNvatSEQDKPKRRAKRGVLGE 272
 
Name Accession Description Interval E-value
CAGE1 pfam15066
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ...
1-526 0e+00

Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.


Pssm-ID: 464481  Cd Length: 528  Bit Score: 810.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040    1 MSESETINVNGPSQDFSYSDSPFCMEASFSSSDLLQSETKNVKRGNESTHTFSEDIYSTEGSLLGDINLGNYPESEQNQP 80
Cdd:pfam15066   1 MSESDAMNVSGLSQDLTHSDSPLCMETSSTTSDLPQNEIKNVKRENESKFTLSEDIYSTLDNLLGDINIGSYSQNVLIQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   81 ANTRLSSLRQFEPICKFHWIEAFNDEM-TVEDLRGAFSYSEKPELPSQVYNDAADGSEKPDPFKEESSVESSISENKDEL 159
Cdd:pfam15066  81 VDTSISSLRQFEPICKFHWTEAFNDEMtTFQNLTEGFSYTEKPELQSHVYNYAKDTNIKQDSFKEENPVETSISTNKDQL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040  160 VPAPVRKSPRSLCLNYYRGEAQPLTEAPFVRSAVVDVGLNISQPQSFLDKENVCKNGDNSSDRENCFEQLDLRAIYKAEE 239
Cdd:pfam15066 161 ANECVRQSSRSPPLIHCSGETLPFTEKSLAKSTAKESALNPSQPQSFLYEENVPRNVEKPFYKENSFSLLDLRANYKTEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040  240 PEVSSKEVQNSGEISELSVSHQEEVTEDGVDSLAITSPWSPAGI-FKGSGPQDNSLRPDREVSCEGLEPLEEDMALNEAL 318
Cdd:pfam15066 241 TEVSSKEIQNSGEIPEMSVSHQKEVTEEGVESPEIASTWSPAGIsWSSGASQENCKTPDTEQSFESLQPLEEDMALNEVL 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040  319 QKLKQTNKKQELQIQDLHGKNLNLENRVQELQTKVTKQHVLVDIINKLKVNIEELINDKYNVILEKNDINKKLQDLQEAS 398
Cdd:pfam15066 321 QKLKHTNRKQQMQIQDLQCSNLYLEKKVKELQMKITKQQVFVDIINKLKENVEELIEDKYNVILEKNDINKTLQNLQEIL 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040  399 AHTKKHLQESKKDKESLQLQVKKIKVHYVRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEELQRLQRHKGELEKATSSA 478
Cdd:pfam15066 401 ANTQKHLQESRKEKETLQLELKKIKVNYVHLQERYITEMQQKNKSVSQCLEMDKTLSKKEEEVERLQQLKGELEKATTSA 480
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 568982040  479 LDLLKREKEIREQEFLSFQEEFQRREKESLKERRKLKSRVEKLVAQVK 526
Cdd:pfam15066 481 LDLLKREKETREQEFLSLQEEFQKHEKENLEERQKLKSRLEKLVAQVK 528
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
309-546 9.79e-09

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: 59.30  E-value: 9.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   309 EEDMALNEALQKLKQTNKKQ---ELQIQDLHGKNLNLENRVQELQTKV----TKQHVLVDIINKLKVNIEELINDKYNVI 381
Cdd:TIGR02168  257 ELTAELQELEEKLEELRLEVselEEEIEELQKELYALANEISRLEQQKqilrERLANLERQLEELEAQLEELESKLDELA 336
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   382 LEKNDINKKLQDLQEASAHTKKHLQESKKDKESLQLQVKKIKVHYVRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEEL 461
Cdd:TIGR02168  337 EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   462 QRLQRHKGELE-KATSSALDLLKREKEIREQEFLSFQEEFQRRE--KESLKERRKLKSR----VEKLVAQVKSLLFTCES 534
Cdd:TIGR02168  417 ERLQQEIEELLkKLEEAELKELQAELEELEEELEELQEELERLEeaLEELREELEEAEQaldaAERELAQLQARLDSLER 496
                          250
                   ....*....|..
gi 568982040   535 ERAQTMALQRQV 546
Cdd:TIGR02168  497 LQENLEGFSEGV 508
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
313-566 8.42e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.10  E-value: 8.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 313 ALNEALQKLKQTNKKQELQIQDLHGKNLNLENRVQELQTKVTKQHvlvDIINKLKVNIEELINDKYNVILEKNDINKKLQ 392
Cdd:COG1196  243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ---AEEYELLAELARLEQDIARLEERRRELEERLE 319
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 393 DLQEASAHTKKHLQESKKDKESLQLQVKkikvhyvRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEELQRLQRHKGELE 472
Cdd:COG1196  320 ELEEELAELEEELEELEEELEELEEELE-------EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 473 KAtssALDLLKREKEIREQEflsfQEEFQRREkESLKERRKLKSRVEKLVAQVKSLLFTCESERAQTMALQRQVEELKLE 552
Cdd:COG1196  393 RA---AAELAAQLEELEEAE----EALLERLE-RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
                        250
                 ....*....|....
gi 568982040 553 NLELRQLAAKREAQ 566
Cdd:COG1196  465 LAELLEEAALLEAA 478
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
316-586 5.16e-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: 5.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 316 EALQKLKQTnkKQELQ-IQDLHGknlNLENRVQEL--QTKVTKQHvlvdiiNKLKVNIEELinDKYNVILEKNDINKKLQ 392
Cdd:COG1196  176 EAERKLEAT--EENLErLEDILG---ELERQLEPLerQAEKAERY------RELKEELKEL--EAELLLLKLRELEAELE 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 393 DLQEASAHTKKHLQESKKDKESLQLQVKKIKVHYVRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEELQRLQRHKGELE 472
Cdd:COG1196  243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 473 KATSSA---LDLLKREKEIREQEFLSFQEEFQRREKESLKERRKLKSRVEKLVAQVKSLLftcESERAQTMALQRQVEEL 549
Cdd:COG1196  323 EELAELeeeLEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE---ELAEELLEALRAAAELA 399
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 568982040 550 KLENLELRQLAAKREAQActpsfEITQSKEQLEEAVE 586
Cdd:COG1196  400 AQLEELEEAEEALLERLE-----RLEEELEELEEALA 431
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
233-528 9.47e-07

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 52.45  E-value: 9.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040  233 AIYKAEEPEVSSKEVQNSGEISELSVSHQEEVTEDGVDSLAITSPWSPAGIFKGSGPQDNSLRPDREVSCEGLEPLEEDm 312
Cdd:pfam09731 149 KEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEH- 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040  313 aLNEALQKLkQTNKKQELQIQDLHGknLNLENRVQELQTkvtkqhvLVDIINKLKVNIEE---LINDKYNVILEK----- 384
Cdd:pfam09731 228 -LDNVEEKV-EKAQSLAKLVDQYKE--LVASERIVFQQE-------LVSIFPDIIPVLKEdnlLSNDDLNSLIAHahrei 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040  385 NDINKKLQDLQ-EASAHTKKHLQESKKDKESLQLQVKKIKVHYVRLQERYIAEIQQKnrsasqclEIEKTLSKKDEELqr 463
Cdd:pfam09731 297 DQLSKKLAELKkREEKHIERALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFER--------EREEIRESYEEKL-- 366
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568982040  464 lqrhKGELEKATSSALDLLKREKEIREQEflsFQEEFQRREKESL-KERRKLKSRVEKLVAQVKSL 528
Cdd:pfam09731 367 ----RTELERQAEAHEEHLKDVLVEQEIE---LQREFLQDIKEKVeEERAGRLLKLNELLANLKGL 425
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
383-586 5.43e-06

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: 49.38  E-value: 5.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 383 EKNDINKKLQDLQEASAHTKKHLQESKKDKESLQLQVKKIkvhyvrlqERYIAEIQQKNRSASQCL-EIEKTLSKKDEEL 461
Cdd:COG4942   21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL--------ERRIAALARRIRALEQELaALEAELAELEKEI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 462 QRLQRHKGELEKATSSALDLLKREKEIREQEFLSFQEEFQR--REKESLKE-RRKLKSRVEKLVAQVKSLLftcESERAQ 538
Cdd:COG4942   93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDavRRLQYLKYlAPARREQAEELRADLAELA---ALRAEL 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 568982040 539 TMALQRQVEELKLENLELRQLAAKREAQACTPSfEITQSKEQLEEAVE 586
Cdd:COG4942  170 EAERAELEALLAELEEERAALEALKAERQKLLA-RLEKELAELAAELA 216
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
306-528 5.95e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.06  E-value: 5.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 306 EPLEEDMALNEALQKLKQTNKKQELQIqdLHGKNlNLENRVQELQTKVTKQHVLVDIINKLKVNIEELINDKYNVILEKN 385
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEV--LREIN-EISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKR 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 386 DINKKLQDLQEASAHTKKHLQESKKDKESLQlQVKKIKVHYVRLQERYIAEIQQKNrsasqclEIEKTLSKKDEELQRLQ 465
Cdd:PRK03918 256 KLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELR-------EIEKRLSRLEEEINGIE 327
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 466 RHKGELEKATSSALDLLKREKEIREQ--EFLSFQEEFQR-----REKESLKERRKLKSrVEKLVAQVKSL 528
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRleELEERHELYEEakakkEELERLKKRLTGLT-PEKLEKELEEL 396
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
363-584 1.97e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.90  E-value: 1.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 363 INKLKVNIEELINDKYNVILEKNDINKKLQDLQEASAHTKKHLQESKKDKESLQLQVKKIKVHYVRLQERYIAEIQQKNR 442
Cdd:COG3883   18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 443 SASQCLEIEKTLSKKD--EELQRLQRhkgeLEKATSSALDLLKREKEIREQefLSFQEEFQRREKESLKERRK----LKS 516
Cdd:COG3883   98 SGGSVSYLDVLLGSESfsDFLDRLSA----LSKIADADADLLEELKADKAE--LEAKKAELEAKLAELEALKAeleaAKA 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568982040 517 RVEKLVAQVKSLLFTCESERAQtmALQRQVEELKLENLELRQLAAKREAQACTPSFEITQSKEQLEEA 584
Cdd:COG3883  172 ELEAQQAEQEALLAQLSAEEAA--AEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
385-691 2.00e-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: 48.51  E-value: 2.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   385 NDINKKLQDLQEASAHTKKhLQESKKDKESLQLQVkkIKVHYVRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEELQRL 464
Cdd:TIGR02168  196 NELERQLKSLERQAEKAER-YKELKAELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   465 QRHKGELEKATSSA---LDLLKREKEIREQEFLSFQEEFQRREKESLK---ERRKLKSRVEKLVAQVKSLLFTCESERAQ 538
Cdd:TIGR02168  273 RLEVSELEEEIEELqkeLYALANEISRLEQQKQILRERLANLERQLEEleaQLEELESKLDELAEELAELEEKLEELKEE 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   539 TMALQRQVEELKLENLELRQLAAKREAQACTPSFEITQSKEQLEEAVEPDITQETKGTHcnLFLNRSSCKENLELQPLKK 618
Cdd:TIGR02168  353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER--LEDRRERLQQEIEELLKKL 430
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568982040   619 TSPLASGIHSLLALRIGLLTcqDLATPDAELCQESKKANdimlQRLKDCQLKKKDLDKELLKHKNRIATLKEL 691
Cdd:TIGR02168  431 EEAELKELQAELEELEEELE--ELQEELERLEEALEELR----EELEEAEQALDAAERELAQLQARLDSLERL 497
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
303-584 3.03e-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: 3.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   303 EGLEPLEEDMALNEALQKLKQTNKKQ-ELQIQDLHGKNLNLENRVQELQTKVtkqHVLVDIINKLKVNIEElindkynvi 381
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAELQElEEKLEELRLEVSELEEEIEELQKEL---YALANEISRLEQQKQI--------- 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   382 lekndINKKLQDLQEASAHTKKHLQESKKDKESLQLQVKKIKVHYVRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEEL 461
Cdd:TIGR02168  307 -----LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   462 QRLqrhkgelekatSSALDLLKREKEireqeflsfQEEFQRREKESLKERrkLKSRVEKLVAQVKSLLftCESERAQTMA 541
Cdd:TIGR02168  382 ETL-----------RSKVAQLELQIA---------SLNNEIERLEARLER--LEDRRERLQQEIEELL--KKLEEAELKE 437
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 568982040   542 LQRQVEELKLENLELRQLAAKREAQACTPSFEITQSKEQLEEA 584
Cdd:TIGR02168  438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
309-584 3.39e-05

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 47.66  E-value: 3.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   309 EEDMALNEALQKLKQTNKKQELQIQDLHGKNLN-----------LENRVQELQTKVTKQHVLVDIINKLKVNIEELINDK 377
Cdd:pfam02463  166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQelklkeqakkaLEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   378 YNVILEKNDINKKLQDLQEASAHTKKHLQESKKDKESLQLQVKKIKVHYVRLQER-YIAEIQQKNRSASQCLEIEKTLSK 456
Cdd:pfam02463  246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSeLLKLERRKVDDEEKLKESEKEKKK 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   457 KDEELQRLQRHKGELEKATSSAldLLKREKEIREQEFLSFQEEFQRREKESLKERRKLKSRVEKLVAQVKSLLFTCESER 536
Cdd:pfam02463  326 AEKELKKEKEEIEELEKELKEL--EIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 568982040   537 AQTMALQRQVEELKLENLELRQLAAKREAQACTPSFEITQSKEQLEEA 584
Cdd:pfam02463  404 EKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKE 451
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
315-521 1.80e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.40  E-value: 1.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040  315 NEALQKLKQTNKKQELQIQDLHGKNLNLENRVQELQTKvtkqhvlvdiINKLKVNIEELINDKYNVILEKNDINKKLQDL 394
Cdd:TIGR04523 334 NKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNE----------IEKLKKENQSYKQEIKNLESQINDLESKIQNQ 403
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040  395 QEASAHTKKHLQESKKDKESLQLQVKKIKVHYVRLQEryiaEIQQ-KNRSASQCLEIEKTLSKKDEELQRLQRHKGELEK 473
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNS----EIKDlTNQDSVKELIIKNLDNTRESLETQLKVLSRSINK 479
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568982040  474 ATSSaLDLLKREKEIREQEFLSFQEEFQRRE---KESLKERRKLKSRVEKL 521
Cdd:TIGR04523 480 IKQN-LEQKQKELKSKEKELKKLNEEKKELEekvKDLTKKISSLKEKIEKL 529
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
303-586 2.06e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.06  E-value: 2.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   303 EGLEPLEEDmaLNEALQKLKQTNKKQELQIQDLHGKNLNLENRVQELQTKVTKQhvlVDIINKLKVNIEELINDKYNVIL 382
Cdd:TIGR02169  684 EGLKRELSS--LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKL---KERLEELEEDLSSLEQEIENVKS 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   383 EKNDINKKLQDLQEASAHTKKHLQESKKDK-----ESLQLQVKKIKVHYVRLQERyIAEIQQKNRSASQCLEIEKTLSKK 457
Cdd:TIGR02169  759 ELKELEARIEELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEAR-LREIEQKLNRLTLEKEYLEKEIQE 837
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   458 DEELQRLQRHKGELEKATSSALDLLKREKEIREQEFLSFQEEFQRREKESLKERRKLKSRVEKLVAQVKSLLFTCESERA 537
Cdd:TIGR02169  838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568982040   538 QTMALQRQVEELKLENLE-LRQLAAKREAQACTPSFE-ITQSKEQLEEAVE 586
Cdd:TIGR02169  918 RLSELKAKLEALEEELSEiEDPKGEDEEIPEEELSLEdVQAELQRVEEEIR 968
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
313-526 6.80e-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: 42.83  E-value: 6.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 313 ALNEALQKLKQTNKKQELQIQDLHGKNLNLENRVQELQTKVTKqhvLVDIINKLKVNIEELINDKYNVILEKNDINKKLQ 392
Cdd:COG4942   24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA---LARRIRALEQELAALEAELAELEKEIAELRAELE 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 393 DLQEASAHTKKHLQE-SKKDKESLQLQVKKIKVHYVRLQ-ERYIAEIQQKNRSA--SQCLEIEKTLSKKDEELQRLQRHK 468
Cdd:COG4942  101 AQKEELAELLRALYRlGRQPPLALLLSPEDFLDAVRRLQyLKYLAPARREQAEElrADLAELAALRAELEAERAELEALL 180
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568982040 469 GELEKATsSALDLLKREKEIREQEFLSFQEEFQRREKESLKERRKLKSRVEKLVAQVK 526
Cdd:COG4942  181 AELEEER-AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
405-566 9.50e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.80  E-value: 9.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040  405 LQESKKDKESLQLQVKKIKVHYVRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEELQR--------LQRHKGELEKATS 476
Cdd:pfam17380 355 QEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRkiqqqkveMEQIRAEQEEARQ 434
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040  477 SALDLLKREKE-----IREQEF--------LSFQEEFQRREKESLKERRKLKSRVEKlvaQVKSLLFTCESERAQTMALQ 543
Cdd:pfam17380 435 REVRRLEEERAremerVRLEEQerqqqverLRQQEEERKRKKLELEKEKRDRKRAEE---QRRKILEKELEERKQAMIEE 511
                         170       180
                  ....*....|....*....|...
gi 568982040  544 RQVEELKLENLELRQLAAKREAQ 566
Cdd:pfam17380 512 ERKRKLLEKEMEERQKAIYEEER 534
PRK11637 PRK11637
AmiB activator; Provisional
385-545 1.16e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 42.37  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 385 NDINKKLQDLQEASAHTKKHLQESKKDKESLQLQVKKikvhyvrlQERYIAEIQQKNRSASQCLE-IEKTLSKKDEELQR 463
Cdd:PRK11637  43 SDNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKK--------QEEAISQASRKLRETQNTLNqLNKQIDELNASIAK 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 464 LQRHKGELEKATSSALDLLKREKEIREQEFLSFQEEFQRREK-----ESLKERRK-----LKSRVEKLVAQvKSLLFTCE 533
Cdd:PRK11637 115 LEQQQAAQERLLAAQLDAAFRQGEHTGLQLILSGEESQRGERilayfGYLNQARQetiaeLKQTREELAAQ-KAELEEKQ 193
                        170
                 ....*....|..
gi 568982040 534 SERAQTMALQRQ 545
Cdd:PRK11637 194 SQQKTLLYEQQA 205
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
405-586 1.94e-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: 41.98  E-value: 1.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   405 LQESKKDKESLQ-LQVKKIKVH-YVRLQERYIAEIQQKNrsasqcleIEKTLSKKDEELQRLQRHKGELEKATSSALDLL 482
Cdd:TIGR02169  203 LRREREKAERYQaLLKEKREYEgYELLKEKEALERQKEA--------IERQLASLEEELEKLTEEISELEKRLEEIEQLL 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   483 ----KREKEIREQEFLSFQEEF-----------------QRREKESLKERRKLKSRVEKLVAQVKSLLFTCESERAQTMA 541
Cdd:TIGR02169  275 eelnKKIKDLGEEEQLRVKEKIgeleaeiaslersiaekERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK 354
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 568982040   542 LQRQVEELKLENLELRQLAAKREAQACTPSFEITQSKEQLEEAVE 586
Cdd:TIGR02169  355 LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR 399
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
313-528 2.20e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 2.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   313 ALNEALQKLKQTNKKQELQIQDLHGKNLNLENRVQELQTKVTKQHVLVDIINKLKVNIEELINDKYNVILEKNDINKKLQ 392
Cdd:TIGR02168  706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   393 DLQEASAHTKKHLQESKKDKESLQLQVKKIKVHYVRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEELQRL---QRHKG 469
Cdd:TIGR02168  786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLaaeIEELE 865
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568982040   470 ELEKATSSALDLLKREKEIREQEFLSFQEEFQ---RREKESLKERRKLKSRVEKLVAQVKSL 528
Cdd:TIGR02168  866 ELIEELESELEALLNERASLEEALALLRSELEelsEELRELESKRSELRRELEELREKLAQL 927
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
303-528 2.40e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 2.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 303 EGLEPLEEDmaLNEALQKLKQTNKKQElQIQDLHGKNLNLENRVQELQTKvtkqHVLVDIINKLKVNIEELinDKYNVIL 382
Cdd:PRK03918 314 KRLSRLEEE--INGIEERIKELEEKEE-RLEELKKKLKELEKRLEELEER----HELYEEAKAKKEELERL--KKRLTGL 384
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 383 EKNDINKKLQDLQEASAHTKKHLQESKKDKESLQLQVKKIKVHYVRLQE---------RYIAEIQQKNRSASQCLE---I 450
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgRELTEEHRKELLEEYTAElkrI 464
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 451 EKTLSKKDEELQRLQRHKGELEKATSSALDLLKrEKEIREQeFLSFQEEFQRREKESL----KERRKLKSRVEKLVAQVK 526
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEKVLKKESELIK-LKELAEQ-LKELEEKLKKYNLEELekkaEEYEKLKEKLIKLKGEIK 542

                 ..
gi 568982040 527 SL 528
Cdd:PRK03918 543 SL 544
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
313-472 2.61e-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: 41.59  E-value: 2.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   313 ALNEALQKLKQTNKKQELQIQDLHGKNLNLENRVQELQTKvtkqhvlvdiINKLKVNIEELINDKYNVILEKNDINKKLQ 392
Cdd:TIGR02169  354 KLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK----------LEKLKREINELKRELDRLQEELQRLSEELA 423
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   393 DLQEASAHTKKHLQESKKDKESLQLQVKKIKVHYVRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEELQRLQRHKGELE 472
Cdd:TIGR02169  424 DLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASE 503
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
309-531 6.29e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.00  E-value: 6.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040  309 EEDMALNEALQKLKQTNKKQELQIQDLHGK----NLNLENRVQELQTKVTKqhvlvdiINKLKVNIEELINDKYNVILEK 384
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLKVLSRSinkiKQNLEQKQKELKSKEKE-------LKKLNEEKKELEEKVKDLTKKI 519
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040  385 NDINKKLQDLQeasahtkkhLQESKKDKESLQLQVKKIKVHYVRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEELQrl 464
Cdd:TIGR04523 520 SSLKEKIEKLE---------SEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQ-- 588
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040  465 qrhkgELEKATSSALDLLKREKEIREQEFLSFQEEFQRREKESLK---ERRKLKSRVEKLVAQVKSLLFT 531
Cdd:TIGR04523 589 -----ELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKlssIIKNIKSKKNKLKQEVKQIKET 653
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
434-805 6.36e-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: 40.44  E-value: 6.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   434 IAEIQQKNRSASQCLE-----IEKTLSKKDEELQRLQRHKGELEKATSsaLDLLKREKEIREQEFLSFQEEFQRREKESL 508
Cdd:TIGR02169  165 VAEFDRKKEKALEELEeveenIERLDLIIDEKRQQLERLRREREKAER--YQALLKEKREYEGYELLKEKEALERQKEAI 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   509 KERRklkSRVEKLVAQVKSLLFTCESERAQTMALQRQVEELKLENLELRQLAAKREAQactpSFEITQSKEQLEEAVEPD 588
Cdd:TIGR02169  243 ERQL---ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIG----ELEAEIASLERSIAEKER 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   589 ITQETKGTHCNLFLNRSSCKENLElqplkktsPLASGIHSLLALRIGLLT-CQDLATPDAEL---CQESKKANDIMLQRL 664
Cdd:TIGR02169  316 ELEDAEERLAKLEAEIDKLLAEIE--------ELEREIEEERKRRDKLTEeYAELKEELEDLraeLEEVDKEFAETRDEL 387
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040   665 KDCQLKKKDLDKELLKHKNRIATLKELiasekaLQAHTIEITDFDADevksardapvlLAVKLDKYHSLNEELDVLITKl 744
Cdd:TIGR02169  388 KDYREKLEKLKREINELKRELDRLQEE------LQRLSEELADLNAA-----------IAGIEAKINELEEEKEDKALE- 449
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568982040   745 gglLESKEDHYSRLIEENDKYRRHVGSLINKVTSYEEIIKCADQRLEISHSQIAHLEERNR 805
Cdd:TIGR02169  450 ---IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVR 507
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
268-525 6.84e-03

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 40.00  E-value: 6.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 268 GVDSLAITSpwspagIFKGS--GPQDNSLRPDREVSCEGLEPLEEDM-ALNEALQK-LKQTNKKQElqiQDLHGKNLNLE 343
Cdd:NF033838  20 GVASVVVAS------LFLGGvvHAEEVRGGNNPTVTSSGNESQKEHAkEVESHLEKiLSEIQKSLD---KRKHTQNVALN 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 344 NRVQELQTKVTkqHVLVDIINKLKVNIEELINDKYNVILEKndINKKLQDLQEASAHTKKHLQESKKDKESlqlQVKKIK 423
Cdd:NF033838  91 KKLSDIKTEYL--YELNVLKEKSEAELTSKTKKELDAAFEQ--FKKDTLEPGKKVAEATKKVEEAEKKAKD---QKEEDR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 424 VHY----VRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEELQRLQRHKGELEKATSSALDLLKREKEIREQEFLSFQEE 499
Cdd:NF033838 164 RNYptntYKTLELEIAESDVEVKKAELELVKEEAKEPRDEEKIKQAKAKVESKKAEATRLEKIKTDREKAEEEAKRRADA 243
                        250       260
                 ....*....|....*....|....*....
gi 568982040 500 FQRREKESL---KERRKLKSRVEKLVAQV 525
Cdd:NF033838 244 KLKEAVEKNvatSEQDKPKRRAKRGVLGE 272
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
383-525 8.08e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.75  E-value: 8.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 383 EKNDINKKLQDLQEASAHTKKHLQESKKDKESLQLQVKKIKVHYVRLQERyIAEIQQKNRSAS-----QCLEIEKTLSKK 457
Cdd:COG1579   25 RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR-IKKYEEQLGNVRnnkeyEALQKEIESLKR 103
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 458 DEEL--QRLQRHKGELEKATSsALDLLKREKEIREQEFLSFQEEFQRREKESLKERRKLKSRVEKLVAQV 525
Cdd:COG1579  104 RISDleDEILELMERIEELEE-ELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
340-526 8.53e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.84  E-value: 8.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 340 LNLENRVQELQTKVTKQH----VLVDIINKLKVN--IEELINDkynvileknDINKKLQDLQEASAHTKKHLQESKKDKE 413
Cdd:COG2433  346 DAYKNKFERVEKKVPPDVdrdeVKARVIRGLSIEeaLEELIEK---------ELPEEEPEAEREKEHEERELTEEEEEIR 416
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982040 414 SLQLQVKKIKVHYVRLQ----------ERYIAEIQQKNRSASQCLEIEKTLSKKDEELQRLQRHKGELEKATSSALDLLK 483
Cdd:COG2433  417 RLEEQVERLEAEVEELEaeleekderiERLERELSEARSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLE 496
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 568982040 484 REKEIREQEFlsfqeefqRREKESLKERRKL-KSRVEKLVAQVK 526
Cdd:COG2433  497 RLKELWKLEH--------SGELVPVKVVEKFtKEAIRRLEEEYG 532
 
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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