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Conserved domains on  [gi|1720375799|ref|XP_030103268|]
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cancer-associated gene 1 protein homolog isoform X6 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CAGE1 super family cl25929
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ...
2-420 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.


The actual alignment was detected with superfamily member pfam15066:

Pssm-ID: 464481  Cd Length: 528  Bit Score: 633.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799   2 TVEDLRGAFSYSEKPELPSQVYNDAADGSEKPDPFKEESSVESSISENKDELVPAPVRKSPRSLCLNYYRGEAQPLTEAP 81
Cdd:pfam15066 109 TFQNLTEGFSYTEKPELQSHVYNYAKDTNIKQDSFKEENPVETSISTNKDQLANECVRQSSRSPPLIHCSGETLPFTEKS 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  82 FVRSAVVDVGLNISQPQSFLDKENVCKNGDNSSDRENCFEQLDLRAIYKAEEPEVSSKEVQNSGEISELSVSHQEEVTED 161
Cdd:pfam15066 189 LAKSTAKESALNPSQPQSFLYEENVPRNVEKPFYKENSFSLLDLRANYKTEETEVSSKEIQNSGEIPEMSVSHQKEVTEE 268
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 162 GVDSLAITSPWSPAGI-FKGSGPQDNSLRPDREVSCEGLEPLEEDMALNEALQKLKQTNKKQELQIQDLHGKNLNLENRV 240
Cdd:pfam15066 269 GVESPEIASTWSPAGIsWSSGASQENCKTPDTEQSFESLQPLEEDMALNEVLQKLKHTNRKQQMQIQDLQCSNLYLEKKV 348
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 241 QELQTKVTKQHVLVDIINKLKVNIEELINDKYNVILEKNDINKKLQDLQEASAHTKKHLQESKKDKESLQLQVKKIKVHY 320
Cdd:pfam15066 349 KELQMKITKQQVFVDIINKLKENVEELIEDKYNVILEKNDINKTLQNLQEILANTQKHLQESRKEKETLQLELKKIKVNY 428
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 321 VRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEELQRLQRHKGELEKATSSALDLLKREKEIREQEFLSFQEEFQRREKE 400
Cdd:pfam15066 429 VHLQERYITEMQQKNKSVSQCLEMDKTLSKKEEEVERLQQLKGELEKATTSALDLLKREKETREQEFLSLQEEFQKHEKE 508
                         410       420
                  ....*....|....*....|
gi 1720375799 401 SLKERRKLKSRVEKLVAQVK 420
Cdd:pfam15066 509 NLEERQKLKSRLEKLVAQVK 528
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
279-585 4.61e-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: 46.97  E-value: 4.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  279 NDINKKLQDLQEASAHTKKhLQESKKDKESLQLQVkkIKVHYVRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEELQRL 358
Cdd:TIGR02168  196 NELERQLKSLERQAEKAER-YKELKAELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  359 QRHKGELEKATSSA---LDLLKREKEIREQEFLSFQEEFQRREKESLK---ERRKLKSRVEKLVAQVKSLLFTCESERAQ 432
Cdd:TIGR02168  273 RLEVSELEEEIEELqkeLYALANEISRLEQQKQILRERLANLERQLEEleaQLEELESKLDELAEELAELEEKLEELKEE 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  433 TMALQRQVEELKLENLELRQLAAKREAQACTPSFEITQSKEQLEEAVEPDITQETKGTHcnLFLNRSSCKENLELQPLKK 512
Cdd:TIGR02168  353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER--LEDRRERLQQEIEELLKKL 430
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720375799  513 TSPLASGIHSLLALRIGLLTcqDLATPDAELCQESKKANdimlQRLKDCQLKKKDLDKELLKHKNRIATLKEL 585
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 ...
2-420 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: 633.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799   2 TVEDLRGAFSYSEKPELPSQVYNDAADGSEKPDPFKEESSVESSISENKDELVPAPVRKSPRSLCLNYYRGEAQPLTEAP 81
Cdd:pfam15066 109 TFQNLTEGFSYTEKPELQSHVYNYAKDTNIKQDSFKEENPVETSISTNKDQLANECVRQSSRSPPLIHCSGETLPFTEKS 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  82 FVRSAVVDVGLNISQPQSFLDKENVCKNGDNSSDRENCFEQLDLRAIYKAEEPEVSSKEVQNSGEISELSVSHQEEVTED 161
Cdd:pfam15066 189 LAKSTAKESALNPSQPQSFLYEENVPRNVEKPFYKENSFSLLDLRANYKTEETEVSSKEIQNSGEIPEMSVSHQKEVTEE 268
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 162 GVDSLAITSPWSPAGI-FKGSGPQDNSLRPDREVSCEGLEPLEEDMALNEALQKLKQTNKKQELQIQDLHGKNLNLENRV 240
Cdd:pfam15066 269 GVESPEIASTWSPAGIsWSSGASQENCKTPDTEQSFESLQPLEEDMALNEVLQKLKHTNRKQQMQIQDLQCSNLYLEKKV 348
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 241 QELQTKVTKQHVLVDIINKLKVNIEELINDKYNVILEKNDINKKLQDLQEASAHTKKHLQESKKDKESLQLQVKKIKVHY 320
Cdd:pfam15066 349 KELQMKITKQQVFVDIINKLKENVEELIEDKYNVILEKNDINKTLQNLQEILANTQKHLQESRKEKETLQLELKKIKVNY 428
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 321 VRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEELQRLQRHKGELEKATSSALDLLKREKEIREQEFLSFQEEFQRREKE 400
Cdd:pfam15066 429 VHLQERYITEMQQKNKSVSQCLEMDKTLSKKEEEVERLQQLKGELEKATTSALDLLKREKETREQEFLSLQEEFQKHEKE 508
                         410       420
                  ....*....|....*....|
gi 1720375799 401 SLKERRKLKSRVEKLVAQVK 420
Cdd:pfam15066 509 NLEERQKLKSRLEKLVAQVK 528
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
207-461 6.90e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.65  E-value: 6.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 207 ALNEALQKLKQTNKKQELQIQDLHGKNLNLENRVQELQTKVTKQHvlvDIINKLKVNIEELINDKYNVILEKNDINKKLQ 286
Cdd:COG1196   243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ---AEEYELLAELARLEQDIARLEERRRELEERLE 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 287 DLQEASAHTKKHLQESKKDKESLQLQVKKIKVHYVRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEELQRLQRHKGELE 366
Cdd:COG1196   320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 367 KATSSALDLLKREKEiREQEFLSFQEEFQRREKESLKERRKLKSRVEKLVAQVKSLLFTCESERAQTMALQRQVEELKLE 446
Cdd:COG1196   400 AQLEELEEAEEALLE-RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
                         250
                  ....*....|....*
gi 1720375799 447 NLELRQLAAKREAQA 461
Cdd:COG1196   479 LAELLEELAEAAARL 493
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
203-440 2.45e-08

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: 57.76  E-value: 2.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  203 EEDMALNEALQKLKQTNKKQ---ELQIQDLHGKNLNLENRVQELQTKV----TKQHVLVDIINKLKVNIEELINDKYNVI 275
Cdd:TIGR02168  257 ELTAELQELEEKLEELRLEVselEEEIEELQKELYALANEISRLEQQKqilrERLANLERQLEELEAQLEELESKLDELA 336
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  276 LEKNDINKKLQDLQEASAHTKKHLQESKKDKESLQLQVKKIKVHYVRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEEL 355
Cdd:TIGR02168  337 EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  356 QRLQRHKGELEKATSSA-LDLLKREKEIREQEFLSFQEEFQRRE--KESLKERRKLKSR----VEKLVAQVKSLLFTCES 428
Cdd:TIGR02168  417 ERLQQEIEELLKKLEEAeLKELQAELEELEEELEELQEELERLEeaLEELREELEEAEQaldaAERELAQLQARLDSLER 496
                          250
                   ....*....|..
gi 1720375799  429 ERAQTMALQRQV 440
Cdd:TIGR02168  497 LQENLEGFSEGV 508
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
200-422 2.16e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.14  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 200 EPLEEDMALNEALQKLKQTNKKQELQIqdLHGKNlNLENRVQELQTKVTKQHVLVDIINKLKVNIEELINDKYNVILEKN 279
Cdd:PRK03918  179 ERLEKFIKRTENIEELIKEKEKELEEV--LREIN-EISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKR 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 280 DINKKLQDLQEASAHTKKHLQESKKDKESLQlQVKKIKVHYVRLQERYIAEIQQKNrsasqclEIEKTLSKKDEELQRLQ 359
Cdd:PRK03918  256 KLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELR-------EIEKRLSRLEEEINGIE 327
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 360 RHKGELEKATSSALDLLKREKEIREQ--EFLSFQEEFQR-----REKESLKERRKLKSrVEKLVAQVKSL 422
Cdd:PRK03918  328 ERIKELEEKEERLEELKKKLKELEKRleELEERHELYEEakakkEELERLKKRLTGLT-PEKLEKELEEL 396
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
279-585 4.61e-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: 4.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  279 NDINKKLQDLQEASAHTKKhLQESKKDKESLQLQVkkIKVHYVRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEELQRL 358
Cdd:TIGR02168  196 NELERQLKSLERQAEKAER-YKELKAELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  359 QRHKGELEKATSSA---LDLLKREKEIREQEFLSFQEEFQRREKESLK---ERRKLKSRVEKLVAQVKSLLFTCESERAQ 432
Cdd:TIGR02168  273 RLEVSELEEEIEELqkeLYALANEISRLEQQKQILRERLANLERQLEEleaQLEELESKLDELAEELAELEEKLEELKEE 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  433 TMALQRQVEELKLENLELRQLAAKREAQACTPSFEITQSKEQLEEAVEPDITQETKGTHcnLFLNRSSCKENLELQPLKK 512
Cdd:TIGR02168  353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER--LEDRRERLQQEIEELLKKL 430
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720375799  513 TSPLASGIHSLLALRIGLLTcqDLATPDAELCQESKKANdimlQRLKDCQLKKKDLDKELLKHKNRIATLKEL 585
Cdd:TIGR02168  431 EEAELKELQAELEELEEELE--ELQEELERLEEALEELR----EELEEAEQALDAAERELAQLQARLDSLERL 497
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
162-419 8.14e-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: 39.61  E-value: 8.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 162 GVDSLAITSpwspagIFKGS--GPQDNSLRPDREVSCEGLEPLEEDM-ALNEALQK-LKQTNKKQElqiQDLHGKNLNLE 237
Cdd:NF033838   20 GVASVVVAS------LFLGGvvHAEEVRGGNNPTVTSSGNESQKEHAkEVESHLEKiLSEIQKSLD---KRKHTQNVALN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 238 NRVQELQTKVTkqHVLVDIINKLKVNIEELINDKYNVILEKndINKKLQDLQEASAHTKKHLQESKKDKESlqlQVKKIK 317
Cdd:NF033838   91 KKLSDIKTEYL--YELNVLKEKSEAELTSKTKKELDAAFEQ--FKKDTLEPGKKVAEATKKVEEAEKKAKD---QKEEDR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 318 VHY----VRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEELQRLQRHKGELEKATSSALDLLKREKEIREQEFLSFQEE 393
Cdd:NF033838  164 RNYptntYKTLELEIAESDVEVKKAELELVKEEAKEPRDEEKIKQAKAKVESKKAEATRLEKIKTDREKAEEEAKRRADA 243
                         250       260
                  ....*....|....*....|....*....
gi 1720375799 394 FQRREKESL---KERRKLKSRVEKLVAQV 419
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 ...
2-420 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: 633.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799   2 TVEDLRGAFSYSEKPELPSQVYNDAADGSEKPDPFKEESSVESSISENKDELVPAPVRKSPRSLCLNYYRGEAQPLTEAP 81
Cdd:pfam15066 109 TFQNLTEGFSYTEKPELQSHVYNYAKDTNIKQDSFKEENPVETSISTNKDQLANECVRQSSRSPPLIHCSGETLPFTEKS 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  82 FVRSAVVDVGLNISQPQSFLDKENVCKNGDNSSDRENCFEQLDLRAIYKAEEPEVSSKEVQNSGEISELSVSHQEEVTED 161
Cdd:pfam15066 189 LAKSTAKESALNPSQPQSFLYEENVPRNVEKPFYKENSFSLLDLRANYKTEETEVSSKEIQNSGEIPEMSVSHQKEVTEE 268
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 162 GVDSLAITSPWSPAGI-FKGSGPQDNSLRPDREVSCEGLEPLEEDMALNEALQKLKQTNKKQELQIQDLHGKNLNLENRV 240
Cdd:pfam15066 269 GVESPEIASTWSPAGIsWSSGASQENCKTPDTEQSFESLQPLEEDMALNEVLQKLKHTNRKQQMQIQDLQCSNLYLEKKV 348
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 241 QELQTKVTKQHVLVDIINKLKVNIEELINDKYNVILEKNDINKKLQDLQEASAHTKKHLQESKKDKESLQLQVKKIKVHY 320
Cdd:pfam15066 349 KELQMKITKQQVFVDIINKLKENVEELIEDKYNVILEKNDINKTLQNLQEILANTQKHLQESRKEKETLQLELKKIKVNY 428
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 321 VRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEELQRLQRHKGELEKATSSALDLLKREKEIREQEFLSFQEEFQRREKE 400
Cdd:pfam15066 429 VHLQERYITEMQQKNKSVSQCLEMDKTLSKKEEEVERLQQLKGELEKATTSALDLLKREKETREQEFLSLQEEFQKHEKE 508
                         410       420
                  ....*....|....*....|
gi 1720375799 401 SLKERRKLKSRVEKLVAQVK 420
Cdd:pfam15066 509 NLEERQKLKSRLEKLVAQVK 528
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
207-461 6.90e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.65  E-value: 6.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 207 ALNEALQKLKQTNKKQELQIQDLHGKNLNLENRVQELQTKVTKQHvlvDIINKLKVNIEELINDKYNVILEKNDINKKLQ 286
Cdd:COG1196   243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ---AEEYELLAELARLEQDIARLEERRRELEERLE 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 287 DLQEASAHTKKHLQESKKDKESLQLQVKKIKVHYVRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEELQRLQRHKGELE 366
Cdd:COG1196   320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 367 KATSSALDLLKREKEiREQEFLSFQEEFQRREKESLKERRKLKSRVEKLVAQVKSLLFTCESERAQTMALQRQVEELKLE 446
Cdd:COG1196   400 AQLEELEEAEEALLE-RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
                         250
                  ....*....|....*
gi 1720375799 447 NLELRQLAAKREAQA 461
Cdd:COG1196   479 LAELLEELAEAAARL 493
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
203-440 2.45e-08

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: 57.76  E-value: 2.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  203 EEDMALNEALQKLKQTNKKQ---ELQIQDLHGKNLNLENRVQELQTKV----TKQHVLVDIINKLKVNIEELINDKYNVI 275
Cdd:TIGR02168  257 ELTAELQELEEKLEELRLEVselEEEIEELQKELYALANEISRLEQQKqilrERLANLERQLEELEAQLEELESKLDELA 336
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  276 LEKNDINKKLQDLQEASAHTKKHLQESKKDKESLQLQVKKIKVHYVRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEEL 355
Cdd:TIGR02168  337 EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  356 QRLQRHKGELEKATSSA-LDLLKREKEIREQEFLSFQEEFQRRE--KESLKERRKLKSR----VEKLVAQVKSLLFTCES 428
Cdd:TIGR02168  417 ERLQQEIEELLKKLEEAeLKELQAELEELEEELEELQEELERLEeaLEELREELEEAEQaldaAERELAQLQARLDSLER 496
                          250
                   ....*....|..
gi 1720375799  429 ERAQTMALQRQV 440
Cdd:TIGR02168  497 LQENLEGFSEGV 508
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
210-487 1.65e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 1.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 210 EALQKLKQTnkKQELQ-IQDLHGknlNLENRVQEL--QTKVTKQHvlvdiiNKLKVNIEELinDKYNVILEKNDINKKLQ 286
Cdd:COG1196   176 EAERKLEAT--EENLErLEDILG---ELERQLEPLerQAEKAERY------RELKEELKEL--EAELLLLKLRELEAELE 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 287 DLQEASAHTKKHLQESKKDKESLQLQVKKIKVHYVRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEELQRLQRHKGELE 366
Cdd:COG1196   243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 367 KATSSA---LDLLKREKEIREQEFLSFQEEFQRREKESLKERRKLKSRVEKLVAQVKSLLftcESERAQTMALQRQVEEL 443
Cdd:COG1196   323 EELAELeeeLEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE---ELAEELLEALRAAAELA 399
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1720375799 444 KLENLELRQLAAKREAQACTPSFEITQSKEQLEEAVEPDITQET 487
Cdd:COG1196   400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
127-422 3.80e-06

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: 50.14  E-value: 3.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 127 AIYKAEEPEVSSKEVQNSGEISELSVSHQEEVTEDGVDSLAITSPWSPAGIFKGSGPQDNSLRPDREVSCEGLEPLEEDm 206
Cdd:pfam09731 149 KEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEH- 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 207 aLNEALQKLkqtNKKQELQIQDLHGKNLNLENRVQELQTkvtkqhvLVDIINKLKVNIEE---LINDKYNVILEK----- 278
Cdd:pfam09731 228 -LDNVEEKV---EKAQSLAKLVDQYKELVASERIVFQQE-------LVSIFPDIIPVLKEdnlLSNDDLNSLIAHahrei 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 279 NDINKKLQDLQ-EASAHTKKHLQESKKDKESLQLQVKKIKVHYVRLQERYIAEIQQKnrsasqclEIEKTLSKKDEELqr 357
Cdd:pfam09731 297 DQLSKKLAELKkREEKHIERALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFER--------EREEIRESYEEKL-- 366
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720375799 358 lqrhKGELEKATSSALDLLKREKEIREQEflsFQEEFQRREKESL-KERRKLKSRVEKLVAQVKSL 422
Cdd:pfam09731 367 ----RTELERQAEAHEEHLKDVLVEQEIE---LQREFLQDIKEKVeEERAGRLLKLNELLANLKGL 425
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
277-480 1.79e-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: 47.84  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 277 EKNDINKKLQDLQEASAHTKKHLQESKKDKESLQLQVKKIkvhyvrlqERYIAEIQQKNRSASQCL-EIEKTLSKKDEEL 355
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL--------ERRIAALARRIRALEQELaALEAELAELEKEI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 356 QRLQRHKGELEKATSSALDLLKREKEIREQEFLSFQEEFQR--REKESLKE-RRKLKSRVEKLVAQVKSLLftcESERAQ 432
Cdd:COG4942    93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDavRRLQYLKYlAPARREQAEELRADLAELA---ALRAEL 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1720375799 433 TMALQRQVEELKLENLELRQLAAKREAQACTPSfEITQSKEQLEEAVE 480
Cdd:COG4942   170 EAERAELEALLAELEEERAALEALKAERQKLLA-RLEKELAELAAELA 216
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
200-422 2.16e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.14  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 200 EPLEEDMALNEALQKLKQTNKKQELQIqdLHGKNlNLENRVQELQTKVTKQHVLVDIINKLKVNIEELINDKYNVILEKN 279
Cdd:PRK03918  179 ERLEKFIKRTENIEELIKEKEKELEEV--LREIN-EISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKR 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 280 DINKKLQDLQEASAHTKKHLQESKKDKESLQlQVKKIKVHYVRLQERYIAEIQQKNrsasqclEIEKTLSKKDEELQRLQ 359
Cdd:PRK03918  256 KLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELR-------EIEKRLSRLEEEINGIE 327
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 360 RHKGELEKATSSALDLLKREKEIREQ--EFLSFQEEFQR-----REKESLKERRKLKSrVEKLVAQVKSL 422
Cdd:PRK03918  328 ERIKELEEKEERLEELKKKLKELEKRleELEERHELYEEakakkEELERLKKRLTGLT-PEKLEKELEEL 396
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
257-478 4.38e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.36  E-value: 4.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 257 INKLKVNIEELINDKYNVILEKNDINKKLQDLQEASAHTKKHLQESKKDKESLQLQVKKIKVHYVRLQERYIAEIQQKNR 336
Cdd:COG3883    18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 337 SASQCLEIEKTLSKKD--EELQRLQRhkgeLEKATSSALDLLKREKEIREQefLSFQEEFQRREKESLKERRK----LKS 410
Cdd:COG3883    98 SGGSVSYLDVLLGSESfsDFLDRLSA----LSKIADADADLLEELKADKAE--LEAKKAELEAKLAELEALKAeleaAKA 171
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720375799 411 RVEKLVAQVKSLLFTCESERAQtmALQRQVEELKLENLELRQLAAKREAQACTPSFEITQSKEQLEEA 478
Cdd:COG3883   172 ELEAQQAEQEALLAQLSAEEAA--AEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
279-585 4.61e-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: 4.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  279 NDINKKLQDLQEASAHTKKhLQESKKDKESLQLQVkkIKVHYVRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEELQRL 358
Cdd:TIGR02168  196 NELERQLKSLERQAEKAER-YKELKAELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  359 QRHKGELEKATSSA---LDLLKREKEIREQEFLSFQEEFQRREKESLK---ERRKLKSRVEKLVAQVKSLLFTCESERAQ 432
Cdd:TIGR02168  273 RLEVSELEEEIEELqkeLYALANEISRLEQQKQILRERLANLERQLEEleaQLEELESKLDELAEELAELEEKLEELKEE 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  433 TMALQRQVEELKLENLELRQLAAKREAQACTPSFEITQSKEQLEEAVEPDITQETKGTHcnLFLNRSSCKENLELQPLKK 512
Cdd:TIGR02168  353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER--LEDRRERLQQEIEELLKKL 430
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720375799  513 TSPLASGIHSLLALRIGLLTcqDLATPDAELCQESKKANdimlQRLKDCQLKKKDLDKELLKHKNRIATLKEL 585
Cdd:TIGR02168  431 EEAELKELQAELEELEEELE--ELQEELERLEEALEELR----EELEEAEQALDAAERELAQLQARLDSLERL 497
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
197-461 7.11e-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: 46.59  E-value: 7.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  197 EGLEPLEEDMALNEALQKLKQTNKKQ-ELQIQDLHGKNLNLENRVQELQTKVtkqHVLVDIINKLKVNIEElindkynvi 275
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAELQElEEKLEELRLEVSELEEEIEELQKEL---YALANEISRLEQQKQI--------- 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  276 lekndINKKLQDLQEASAHTKKHLQESKKDKESLQLQVKKIKVHYVRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEEL 355
Cdd:TIGR02168  307 -----LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  356 QRLQRHKGELEK---ATSSALDLLKREKEIREQEFLSFQEEFQRREKESLKERRKlksRVEKLVAQVKSLLFTCESERAQ 432
Cdd:TIGR02168  382 ETLRSKVAQLELqiaSLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK---ELQAELEELEEELEELQEELER 458
                          250       260
                   ....*....|....*....|....*....
gi 1720375799  433 TMALQRQVEELKLENLELRQLAAKREAQA 461
Cdd:TIGR02168  459 LEEALEELREELEEAEQALDAAERELAQL 487
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
203-478 1.14e-04

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: 45.73  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  203 EEDMALNEALQKLKQTNKKQELQIQDLHGKNLN-----------LENRVQELQTKVTKQHVLVDIINKLKVNIEELINDK 271
Cdd:pfam02463  166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQelklkeqakkaLEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  272 YNVILEKNDINKKLQDLQEASAHTKKHLQESKKDKESLQLQVKKIKVHYVRLQER-YIAEIQQKNRSASQCLEIEKTLSK 350
Cdd:pfam02463  246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSeLLKLERRKVDDEEKLKESEKEKKK 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  351 KDEELQRLQRHKGELEKATSSAldLLKREKEIREQEFLSFQEEFQRREKESLKERRKLKSRVEKLVAQVKSLLFTCESER 430
Cdd:pfam02463  326 AEKELKKEKEEIEELEKELKEL--EIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1720375799  431 AQTMALQRQVEELKLENLELRQLAAKREAQACTPSFEITQSKEQLEEA 478
Cdd:pfam02463  404 EKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKE 451
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
209-415 4.79e-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: 43.47  E-value: 4.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 209 NEALQKLKQTNKKQELQIQDLHGKNLNLENRVQELQTKvtkqhvlvdiINKLKVNIEELINDKYNVILEKNDINKKLQDL 288
Cdd:TIGR04523 334 NKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNE----------IEKLKKENQSYKQEIKNLESQINDLESKIQNQ 403
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 289 QEASAHTKKHLQESKKDKESLQLQVKKIKVHYVRLQEryiaEIQQ-KNRSASQCLEIEKTLSKKDEELQRLQRHKGELEK 367
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNS----EIKDlTNQDSVKELIIKNLDNTRESLETQLKVLSRSINK 479
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720375799 368 ATSSaLDLLKREKEIREQEFLSFQEEFQRRE---KESLKERRKLKSRVEKL 415
Cdd:TIGR04523 480 IKQN-LEQKQKELKSKEKELKKLNEEKKELEekvKDLTKKISSLKEKIEKL 529
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
197-480 4.85e-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: 43.90  E-value: 4.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  197 EGLEPLEEDmaLNEALQKLKQTNKKQELQIQDLHGKNLNLENRVQELQTKVTKQhvlVDIINKLKVNIEELINDKYNVIL 276
Cdd:TIGR02169  684 EGLKRELSS--LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKL---KERLEELEEDLSSLEQEIENVKS 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  277 EKNDINKKLQDLQEASAHTKKHLQESKKDK-----ESLQLQVKKIKVHYVRLQERyIAEIQQKNRSASQCLEIEKTLSKK 351
Cdd:TIGR02169  759 ELKELEARIEELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEAR-LREIEQKLNRLTLEKEYLEKEIQE 837
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  352 DEELQRLQRHKGELEKATSSALDLLKREKEIREQEFLSFQEEFQRREKESLKERRKLKSRVEKLVAQVKSLLFTCESERA 431
Cdd:TIGR02169  838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720375799  432 QTMALQRQVEELKLENLE-LRQLAAKREAQACTPSFE-ITQSKEQLEEAVE 480
Cdd:TIGR02169  918 RLSELKAKLEALEEELSEiEDPKGEDEEIPEEELSLEdVQAELQRVEEEIR 968
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
299-460 1.67e-03

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: 42.03  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 299 LQESKKDKESLQLQVKKIKVHYVRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEELQR--------LQRHKGELEKATS 370
Cdd:pfam17380 355 QEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRkiqqqkveMEQIRAEQEEARQ 434
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 371 SALDLLKREKE-----IREQEF--------LSFQEEFQRREKESLKERRKLKSRVEKlvaQVKSLLFTCESERAQTMALQ 437
Cdd:pfam17380 435 REVRRLEEERAremerVRLEEQerqqqverLRQQEEERKRKKLELEKEKRDRKRAEE---QRRKILEKELEERKQAMIEE 511
                         170       180
                  ....*....|....*....|...
gi 1720375799 438 RQVEELKLENLELRQLAAKREAQ 460
Cdd:pfam17380 512 ERKRKLLEKEMEERQKAIYEEER 534
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
207-436 2.07e-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: 2.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  207 ALNEALQKLKQTNKKQELQIQDLHGKNLNLENRVQELQTKVTKQhvlvdiinklkvnIEELINDKYnvilEKNDINKKLQ 286
Cdd:TIGR02169  312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKL-------------TEEYAELKE----ELEDLRAELE 374
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  287 DLQEASAHTKKHLQESKKDKESLQLQVKKIKVHYVRLQERyiaeiqqKNRSASQCLEIEKTLSKKDEELQRLQRHKGELE 366
Cdd:TIGR02169  375 EVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE-------LQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720375799  367 KATSSALDLLKREKEIR---EQEFLSFQEEFQRREkeslKERRKLKSRVEKLVAQVKSLLFTCESERAQTMAL 436
Cdd:TIGR02169  448 LEIKKQEWKLEQLAADLskyEQELYDLKEEYDRVE----KELSKLQRELAEAEAQARASEERVRGGRAVEEVL 516
PRK11637 PRK11637
AmiB activator; Provisional
279-452 2.15e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 41.22  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 279 NDINKKLQDLQEASAHTKKHLQESKKDKESLQLQVKKikvhyvrlQERYIAEIQQKNRSASQCLE-IEKTLSKKDEELQR 357
Cdd:PRK11637   43 SDNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKK--------QEEAISQASRKLRETQNTLNqLNKQIDELNASIAK 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 358 LQRHKGELEKATSSALDLLKREKEIREQEFLSFQEEFQRREK-----ESLKERRK-----LKSRVEKLVAQvKSLLFTCE 427
Cdd:PRK11637  115 LEQQQAAQERLLAAQLDAAFRQGEHTGLQLILSGEESQRGERilayfGYLNQARQetiaeLKQTREELAAQ-KAELEEKQ 193
                         170       180
                  ....*....|....*....|....*
gi 1720375799 428 SERAQTMALQRQVEELKLENLELRQ 452
Cdd:PRK11637  194 SQQKTLLYEQQAQQQKLEQARNERK 218
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
207-420 2.23e-03

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: 40.90  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 207 ALNEALQKLKQTNKKQELQIQDLHGKNLNLENRVQELQTKVTKqhvLVDIINKLKVNIEELINDKYNVILEKNDINKKLQ 286
Cdd:COG4942    24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA---LARRIRALEQELAALEAELAELEKEIAELRAELE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 287 DLQEASAHTKKHLQE-SKKDKESLQLQVKKIKVHYVRLQ-ERYIAEIQQKNRSA--SQCLEIEKTLSKKDEELQRLQRHK 362
Cdd:COG4942   101 AQKEELAELLRALYRlGRQPPLALLLSPEDFLDAVRRLQyLKYLAPARREQAEElrADLAELAALRAELEAERAELEALL 180
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720375799 363 GELEKATsSALDLLKREKEIREQEFLSFQEEFQRREKESLKERRKLKSRVEKLVAQVK 420
Cdd:COG4942   181 AELEEER-AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
207-422 3.73e-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: 40.81  E-value: 3.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  207 ALNEALQKLKQTNKKQELQIQDLHGKNLNLENRVQELQTKVTKQHVLVDIINKLKVNIEELINDKYNVILEKNDINKKLQ 286
Cdd:TIGR02168  706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  287 DLQEASAHTKKHLQESKKDKESLQLQVKKIKVHYVRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEELQRL---QRHKG 363
Cdd:TIGR02168  786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLaaeIEELE 865
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720375799  364 ELEKATSSALDLLKREKEIREQEFLSFQEEFQ---RREKESLKERRKLKSRVEKLVAQVKSL 422
Cdd:TIGR02168  866 ELIEELESELEALLNERASLEEALALLRSELEelsEELRELESKRSELRRELEELREKLAQL 927
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
299-480 3.83e-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: 40.82  E-value: 3.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  299 LQESKKDKESLQ-LQVKKIKVH-YVRLQERYIAEIQQKNrsasqcleIEKTLSKKDEELQRLQRHKGELEKATSSALDLL 376
Cdd:TIGR02169  203 LRREREKAERYQaLLKEKREYEgYELLKEKEALERQKEA--------IERQLASLEEELEKLTEEISELEKRLEEIEQLL 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  377 ----KREKEIREQEFLSFQEEF-----------------QRREKESLKERRKLKSRVEKLVAQVKSLLFTCESERAQTMA 435
Cdd:TIGR02169  275 eelnKKIKDLGEEEQLRVKEKIgeleaeiaslersiaekERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK 354
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1720375799  436 LQRQVEELKLENLELRQLAAKREAQACTPSFEITQSKEQLEEAVE 480
Cdd:TIGR02169  355 LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR 399
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
207-488 4.46e-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: 40.43  E-value: 4.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  207 ALNEALQKLKQTNKKQELQIQDLHGKNLNLENRVQELQTKVTKQHVLVDIINKLKVNIEELINdkyNVILEKNDINKKLQ 286
Cdd:TIGR02168  730 ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE---QLKEELKALREALD 806
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  287 DLQEASAHTKKHLQESKKDKESLQLQVKKIKVHYVRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEELQRLQRHKGELE 366
Cdd:TIGR02168  807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799  367 KATSSALDLL-KREKEIREQEflSFQEEFQRREKESLKERRKLKSRVEKLVAQVKSLL--FTCESERAQTMALQRQVEEL 443
Cdd:TIGR02168  887 EALALLRSELeELSEELRELE--SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQerLSEEYSLTLEEAEALENKIE 964
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720375799  444 KLENLELRQ---------------LAAKREAQACTPSFE--------ITQSKEQLEEAVEpDITQETK 488
Cdd:TIGR02168  965 DDEEEARRRlkrlenkikelgpvnLAAIEEYEELKERYDfltaqkedLTEAKETLEEAIE-EIDREAR 1031
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
162-419 8.14e-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: 39.61  E-value: 8.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 162 GVDSLAITSpwspagIFKGS--GPQDNSLRPDREVSCEGLEPLEEDM-ALNEALQK-LKQTNKKQElqiQDLHGKNLNLE 237
Cdd:NF033838   20 GVASVVVAS------LFLGGvvHAEEVRGGNNPTVTSSGNESQKEHAkEVESHLEKiLSEIQKSLD---KRKHTQNVALN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 238 NRVQELQTKVTkqHVLVDIINKLKVNIEELINDKYNVILEKndINKKLQDLQEASAHTKKHLQESKKDKESlqlQVKKIK 317
Cdd:NF033838   91 KKLSDIKTEYL--YELNVLKEKSEAELTSKTKKELDAAFEQ--FKKDTLEPGKKVAEATKKVEEAEKKAKD---QKEEDR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 318 VHY----VRLQERYIAEIQQKNRSASQCLEIEKTLSKKDEELQRLQRHKGELEKATSSALDLLKREKEIREQEFLSFQEE 393
Cdd:NF033838  164 RNYptntYKTLELEIAESDVEVKKAELELVKEEAKEPRDEEKIKQAKAKVESKKAEATRLEKIKTDREKAEEEAKRRADA 243
                         250       260
                  ....*....|....*....|....*....
gi 1720375799 394 FQRREKESL---KERRKLKSRVEKLVAQV 419
Cdd:NF033838  244 KLKEAVEKNvatSEQDKPKRRAKRGVLGE 272
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
197-422 8.78e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 8.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 197 EGLEPLEEDmaLNEALQKLKQTNKKQElQIQDLHGKNLNLENRVQELQTKvtkqHVLVDIINKLKVNIEELinDKYNVIL 276
Cdd:PRK03918  314 KRLSRLEEE--INGIEERIKELEEKEE-RLEELKKKLKELEKRLEELEER----HELYEEAKAKKEELERL--KKRLTGL 384
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 277 EKNDINKKLQDLQEASAHTKKHLQESKKDKESLQLQVKKIKVHYVRLQE---------RYIAEIQQKNRSASQCLE---I 344
Cdd:PRK03918  385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgRELTEEHRKELLEEYTAElkrI 464
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720375799 345 EKTLSKKDEELQRLQRHKGELEKATSSALDLLKrEKEIREQeFLSFQEEFQRREKESL----KERRKLKSRVEKLVAQVK 420
Cdd:PRK03918  465 EKELKEIEEKERKLRKELRELEKVLKKESELIK-LKELAEQ-LKELEEKLKKYNLEELekkaEEYEKLKEKLIKLKGEIK 542

                  ..
gi 1720375799 421 SL 422
Cdd:PRK03918  543 SL 544
 
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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