|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
571-1076 |
3.43e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.48 E-value: 3.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 571 LKLEVEEKKQAMLLLQRALAQQRDLTVRRVKETEKALSRQLQRQREHYEATIQRHLAFIDQLIEDKKVLSEKCEAVVAEL 650
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 651 KQEDQRCTERVAQVQAQHELEIKKLKELMSATEKVRREkwisEKTKKIKEVTVRGLEPEIQKLIARHKQEVRRLKSLhEA 730
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEEL----EEELEELEEELEEAEEELEEAEAELAEAEEALLEA-EA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 731 ELLQSDERASQRCLRQAEELREQLEREKEALGQQERERARQRFQQHLEQEQWALQQQRQRLYSEVAEERERLGQQAARQR 810
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 811 AELEELRQQLEESSSALTRALRAEFEKGREEQERRHQMELKALKQQLELERQAWEAGCARKEEAWLLNREQELREEIRKG 890
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 891 RDKEIELVIHRLEADMALAKEESEKAAESRIKRLRDKYEAELSELEQSERKLHERCSELKGQLGEAEGENLRLQGLVRQK 970
Cdd:COG1196 533 EAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREAD 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 971 ERALEDTQAVSGQ--------MNEQLSSERSNLAQVIRQEFEDRLAASEEETRQAKAELAALQARQQLELEEVHRRVKTA 1042
Cdd:COG1196 613 ARYYVLGDTLLGRtlvaarleAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE 692
|
490 500 510
....*....|....*....|....*....|....
gi 1622882005 1043 LARKEEAVSSLRTQHEAAVKRADHLEELLEQHRR 1076
Cdd:COG1196 693 LELEEALLAEEEEERELAEAEEERLEEELEEEAL 726
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
570-1073 |
6.98e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 102.32 E-value: 6.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 570 RLKLEVEEKKQAMLLLQRALaQQRDLTVRRVKETEKALSRQLQRQREHYEATIQRhlafIDQLIEDKKVLSEKCEAVVAE 649
Cdd:COG1196 243 ELEAELEELEAELEELEAEL-AELEAELEELRLELEELELELEEAQAEEYELLAE----LARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 650 LKQEDQRCTERVAQVQAQHELEIKKLKELMSATEKVRREKWISEKTKKIKEVTVRGLEPEIQKLIARHKQEVRRLKSLHE 729
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 730 AE-LLQSDERASQRCLRQAEELREQLEREKEALGQQERERARQRfQQHLEQEQWALQQQRQRLysEVAEERERLGQQAAR 808
Cdd:COG1196 398 LAaQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE-EALEEAAEEEAELEEEEE--ALLELLAELLEEAAL 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 809 QRAELEELRQQLEESSS--ALTRALRAEFEKGREEQERRHQMELKALKQQLELERQAWEAGCARKEEAWLLNREQELREE 886
Cdd:COG1196 475 LEAALAELLEELAEAAArlLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVE 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 887 IRKGRDKEIE-LVIHRLEADMALAKEESEKAAESRIKRLRDKYEAELSELEQSERKLHERCSELKGQLGEAEGENLRLQG 965
Cdd:COG1196 555 DDEVAAAAIEyLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 966 LVRQKERALEDTQAVSGQM--NEQLSSERSNLAQVIRQEFEDRLAASEEETRQAKAELAALQARQQLELEEVHRRVKTAL 1043
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGegGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE 714
|
490 500 510
....*....|....*....|....*....|
gi 1622882005 1044 ARKEEAVSSLRTQHEAAVKRADHLEELLEQ 1073
Cdd:COG1196 715 ERLEEELEEEALEEQLEAEREELLEELLEE 744
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
763-1079 |
5.86e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.61 E-value: 5.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 763 QQERERARqRFQQHLEQEQWALQQQRQRLYSEVAEERERLGQQAARQRAELEELRQQLEESSSALtRALRAEFEKGREEQ 842
Cdd:COG1196 206 ERQAEKAE-RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL-EELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 843 ERRHQMELKALKQQLELERQAwEAGCARKEEawLLNREQELREEIRKGRDKEIELV--IHRLEADMALAKEESEKAAESR 920
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDI-ARLEERRRE--LEERLEELEEELAELEEELEELEeeLEELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 921 IKRlrdkyEAELSELEQSERKLHERCSELKGQLGEAEGENLRLQGLVRQKERALEDTQAVSGQMNEQLSSERSNLAQVIR 1000
Cdd:COG1196 361 AEA-----EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 1001 QEFEDRLAASEEETRQAKAELAALQARQQL-ELEEVHRRVKTALARKEEAVSSLRTQHEAAVKRADHLEELLEQHRRPTL 1079
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLaELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
786-1071 |
3.58e-13 |
|
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: 74.32 E-value: 3.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 786 QQRQRLYSEVAEERERLGQQAARQRAELEELRQQLEESSSALTRALRAEFEKGREEQERRhqMELKALKQQLELERQAWE 865
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALR--KDLARLEAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 866 AgcARKEEAWLLNREQELREEIRKGRD--KEIELVIHRLEADMALAKEESeKAAESRIKRLRdkyeAELSELEQSERKLH 943
Cdd:TIGR02168 751 Q--LSKELTELEAEIEELEERLEEAEEelAEAEAEIEELEAQIEQLKEEL-KALREALDELR----AELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 944 ERCSELKGQLGEAEgenLRLQGLVRQKERALEDTQAVSGQMNEQLSSERSNLAQVirQEFEDRLAASEEETRQAKAELAA 1023
Cdd:TIGR02168 824 ERLESLERRIAATE---RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL--EALLNERASLEEALALLRSELEE 898
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1622882005 1024 LQARQQlELEEVHRRVKTALARKEEAVSSLRTQHEAAVKRADHLEELL 1071
Cdd:TIGR02168 899 LSEELR-ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
562-986 |
3.96e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.94 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 562 SEASTSVMRLKLEVEEKKQAMLLLQRALAQQRDLTVRRVKETEKALSRQLQRQREHYEATIQRHLAFIDQLIEDKKVLSE 641
Cdd:PTZ00121 1414 AAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE 1493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 642 KCEAVVAELKQEDQrctERVAQVQAQHELEIKKLKELMSATEKVRREKW-ISEKTKKIKEVtvrglepeiqkliaRHKQE 720
Cdd:PTZ00121 1494 EAKKKADEAKKAAE---AKKKADEAKKAEEAKKADEAKKAEEAKKADEAkKAEEKKKADEL--------------KKAEE 1556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 721 VRRLKSLHEAELLQSDERASQRCLRQAEELREQLEREKEALGQQERERARQRFQQHLEQEQWALQQQRQRLYSEVAEERE 800
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE 1636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 801 RLGQQAARQRAELEELRQQLEESSsaltraLRAEFEKGREEQERRHQMElkaLKQQLELERQAWEAGCARKEEAwllNRE 880
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKAEEENK------IKAAEEAKKAEEDKKKAEE---AKKAEEDEKKAAEALKKEAEEA---KKA 1704
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 881 QELR----EEIRKGRDKEIELVIHRLEADMALAKEESEKAAESRIKrlrdKYEAELSELEQSERKLHERCSELKGQLGEA 956
Cdd:PTZ00121 1705 EELKkkeaEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK----KDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
410 420 430
....*....|....*....|....*....|..
gi 1622882005 957 EGENLRLQGLVR--QKERALEDTQAVSGQMNE 986
Cdd:PTZ00121 1781 IEEELDEEDEKRrmEVDKKIKDIFDNFANIIE 1812
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
570-1024 |
6.12e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 6.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 570 RLKLEVEEKKQAMLLLQRALAQQRDLTVRRVKETEKALSRQLQRQREhyEATIQRHLAFIDQLIEDKKVLSEKCEAVVAE 649
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE--LLEALRAAAELAAQLEELEEAEEALLERLER 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 650 LKQEDQRCTERVAQVQAQHELEIKKLKELMSATEKVRREKWISEKTKKIKEVTVRGLEPEIQKLIARHKQEVRRLKSLHE 729
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 730 AELLQSDERASQRCLRQAEELREQLEREKEALGQQERERArqrfqqHLEQEQWALQQQRQRLYSEVAEERERLGQQAARQ 809
Cdd:COG1196 499 AEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA------ALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 810 RAELEELRQQLEESSSALTRALRAEFEKGREEQERRHQMELKALKQQLELERQAWEAGCARKEEAWLLNREQELREEIRK 889
Cdd:COG1196 573 RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLE 652
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 890 GRDKEIELVIHRLEADMALAKEESEKAAESRIKRLRDKYEAELSELEQSERKLHERCSELKGQLGEAEGENLRLQGLVRQ 969
Cdd:COG1196 653 GEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEA 732
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1622882005 970 KERALEDTQAVSGQMNEQlssersnlAQVIRQEFEDRLAASEEETRQAKAELAAL 1024
Cdd:COG1196 733 EREELLEELLEEEELLEE--------EALEELPEPPDLEELERELERLEREIEAL 779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
791-1076 |
6.84e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 6.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 791 LYSEVAEERERLGQQA--ARQRAELEELRQQLEESSSALT-RALRAEFEKGREEQErrhqmELKALKQQLELERQAWEAg 867
Cdd:COG1196 194 ILGELERQLEPLERQAekAERYRELKEELKELEAELLLLKlRELEAELEELEAELE-----ELEAELEELEAELAELEA- 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 868 carkeeawllnREQELREEIrkgrdkeielviHRLEADM--ALAKEESEKAAESRIKRLRDKYEAELSELEQSERKLHER 945
Cdd:COG1196 268 -----------ELEELRLEL------------EELELELeeAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 946 CSELKGQLGEAEGENLRLQGLVRQKERALEDTQAVSGQMNEQLSSERSNLAQVIRQEFEDRLAASEEETRQAK-----AE 1020
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAElaaqlEE 404
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622882005 1021 LAALQARQQLELEEVHRRVKTALARKEEAVSSLRTQHEAAVKRADHLEELLEQHRR 1076
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
693-1055 |
2.27e-11 |
|
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: 68.16 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 693 EKTKKIKEVT--VRGLEPEIQKLiarhKQEVRRLKslHEAELLQSDERASQRCLRQAEELREQLEREKEALGQQERERAR 770
Cdd:TIGR02168 674 ERRREIEELEekIEELEEKIAEL----EKALAELR--KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 771 QRFQQHLEQEQwaLQQQRQRLYSEVAEERERLgqqaarqrAELEELRQQLEESSSALTRALRAEFEKGREEQERRHQMEL 850
Cdd:TIGR02168 748 RIAQLSKELTE--LEAEIEELEERLEEAEEEL--------AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 851 KALKQQLELERQAWEAGCARKEEAWLLNREQELREEIRK--GRDKEIELVIHRLEADMALAKEESEKAAEsRIKRLRDKY 928
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESlaAEIEELEELIEELESELEALLNERASLEE-ALALLRSEL 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 929 EAELSELEQSERKLHE---RCSELKGQLGEAegeNLRLQGLvRQKERALEDTQAVSGQMNEQLSSERSNLAQVIRQEFED 1005
Cdd:TIGR02168 897 EELSEELRELESKRSElrrELEELREKLAQL---ELRLEGL-EVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARR 972
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1622882005 1006 RLAASEEE-TRQAKAELAALQarqqlELEEVHRRVKTALARKEEAVSSLRT 1055
Cdd:TIGR02168 973 RLKRLENKiKELGPVNLAAIE-----EYEELKERYDFLTAQKEDLTEAKET 1018
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
572-1048 |
4.44e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.47 E-value: 4.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 572 KLEVEEKKQAMLLLQRALAQQRDLTVRRVKETEKALSRQLQRQREHYEATIQRHLAFIDQLIEDKKVLSEKCEAVVAELK 651
Cdd:PTZ00121 1244 KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKK 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 652 QED---------QRCTERVAQVQAQHELEIKKLKELMSATEKVRREKWISEKTKKIKEVTVRGLEP-----EIQKLIARH 717
Cdd:PTZ00121 1324 AEEakkkadaakKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkkkadEAKKKAEED 1403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 718 KQEVRRLKSlHEAELLQSDE--------RASQRCLRQAEELREQLEREKEALGQQERERARQRFQQHLEQEQWALQQQRQ 789
Cdd:PTZ00121 1404 KKKADELKK-AAAAKKKADEakkkaeekKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEA 1482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 790 RLYSEVAEERERLGQQAARQRAELEELRQQLE----ESSSALTRALRAEFEKGREE----QERRHQMELKAlKQQLELER 861
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKAAEAKKKADEakkaEEAKKADEAKKAEEAKKADEakkaEEKKKADELKK-AEELKKAE 1561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 862 QAWEAGCARKEEAwllNREQELR--EEIRKGRDKEIELVIHRLEADMALAKEESEKAAESRIKRLRDKYEAELSELEQSE 939
Cdd:PTZ00121 1562 EKKKAEEAKKAEE---DKNMALRkaEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQL 1638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 940 RKLHERCSELKGQLGEAEGENLRLQGLVRQKEralEDTQAVSGQMNEQLSSERSNLAQVIRQEFEDRLAaseEETRQAKA 1019
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKAEEENKIKAAEEAKKA---EEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA---EELKKKEA 1712
|
490 500
....*....|....*....|....*....
gi 1622882005 1020 ElaALQARQQLELEEVHRRVKTALARKEE 1048
Cdd:PTZ00121 1713 E--EKKKAEELKKAEEENKIKAEEAKKEA 1739
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
675-1048 |
6.54e-11 |
|
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: 67.00 E-value: 6.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 675 LKELMSATEKVRREkwiSEKTKKIKEVTVRGLEPEIQKLIARHKQEVRRLKSLHEAEL-LQSDERASQRCLRQAEELREQ 753
Cdd:TIGR02168 195 LNELERQLKSLERQ---AEKAERYKELKAELRELELALLVLRLEELREELEELQEELKeAEEELEELTAELQELEEKLEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 754 LEREKEALgqQERERARQRFQQHLEQEQWALQQQRQRLysevAEERERLGQQAARQRAELEELRQQLEESSSALTRalra 833
Cdd:TIGR02168 272 LRLEVSEL--EEEIEELQKELYALANEISRLEQQKQIL----RERLANLERQLEELEAQLEELESKLDELAEELAE---- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 834 efekgREEQERRHQMELKALKQQLELERQAWEAgcarkeeawLLNREQELREEIRKGRDKeielvIHRLEADMALAKEES 913
Cdd:TIGR02168 342 -----LEEKLEELKEELESLEAELEELEAELEE---------LESRLEELEEQLETLRSK-----VAQLELQIASLNNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 914 EkAAESRIKRLRDKYEAELSELEQSERKLHE-RCSELKGQLGEaegenlrlqglvrqKERALEDTQAVSGQMNEQLSSER 992
Cdd:TIGR02168 403 E-RLEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEE--------------LEEELEELQEELERLEEALEELR 467
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622882005 993 SNLAQVirqefEDRLAASEEETRQAKAELAALQARQQlELEEVHRRVKTALARKEE 1048
Cdd:TIGR02168 468 EELEEA-----EQALDAAERELAQLQARLDSLERLQE-NLEGFSEGVKALLKNQSG 517
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
758-1035 |
1.15e-10 |
|
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: 65.86 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 758 KEALGQQERERARQRfqQHLEQEQWALQQQRQRLYSEVAEERERLGQQAARQRAELEE----LRQQLEESSSALTRALRA 833
Cdd:TIGR02169 232 KEALERQKEAIERQL--ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEeqlrVKEKIGELEAEIASLERS 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 834 EFEKGREEQerrhQMELKALKQQLELERQAWEA-GCARKEEAWLLNREQeLREEIRKGRDKEIELVihrleadmALAKEE 912
Cdd:TIGR02169 310 IAEKERELE----DAEERLAKLEAEIDKLLAEIeELEREIEEERKRRDK-LTEEYAELKEELEDLR--------AELEEV 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 913 SEKAAESR-----IKRLRDKYEAELSELEQSERKLHERCSELKGQLGEAEGENLRLQGLVRQKERALEDTQAVSGQMNEQ 987
Cdd:TIGR02169 377 DKEFAETRdelkdYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWK 456
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1622882005 988 LSSERSNLAQVIRQEFEDR--LAASEEETRQAKAELAALQARQQLELEEV 1035
Cdd:TIGR02169 457 LEQLAADLSKYEQELYDLKeeYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
562-1073 |
1.38e-10 |
|
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: 65.85 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 562 SEASTSVMRLKLEVEEKKQAMLLLQRAL----AQQRDLTvRRVKETEKALsRQLQRQREHYEATIQRHLAFIDQLIEDKK 637
Cdd:TIGR02168 263 QELEEKLEELRLEVSELEEEIEELQKELyalaNEISRLE-QQKQILRERL-ANLERQLEELEAQLEELESKLDELAEELA 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 638 VLSEKCEAVVAELKQEDQRCTERVAQVQAQHELEIKKLKELMSATEKVRREKwisEKTKKIKEvTVRGLEPEIQKLIARH 717
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE---LQIASLNN-EIERLEARLERLEDRR 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 718 KQEVRRLKSlHEAELLQSDERASQRCLRQAEELREQLEREKEALgQQERERARQRFQQhLEQEQWALQQQRQRLYSEVAE 797
Cdd:TIGR02168 417 ERLQQEIEE-LLKKLEEAELKELQAELEELEEELEELQEELERL-EEALEELREELEE-AEQALDAAERELAQLQARLDS 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 798 ERERLGQQAARQRAELEELRQQL----------------EESSSALTRALRA-----------------EFEKgREEQER 844
Cdd:TIGR02168 494 LERLQENLEGFSEGVKALLKNQSglsgilgvlselisvdEGYEAAIEAALGGrlqavvvenlnaakkaiAFLK-QNELGR 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 845 RHQMELKALKQQL----ELERQAWEAGCARKE--------------EAWL--------LNREQELREEIRKG-------- 890
Cdd:TIGR02168 573 VTFLPLDSIKGTEiqgnDREILKNIEGFLGVAkdlvkfdpklrkalSYLLggvlvvddLDNALELAKKLRPGyrivtldg 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 891 ----------------------RDKEIElvihRLEADMALAkEESEKAAESRIKRLRDKYEAELSELEQSERKLHE---R 945
Cdd:TIGR02168 653 dlvrpggvitggsaktnssileRRREIE----ELEEKIEEL-EEKIAELEKALAELRKELEELEEELEQLRKELEElsrQ 727
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 946 CSELKGQLGEAEGENLRLQGLVRQKERALEDTQAVSGQMNEQLSSERSNLAqvirqEFEDRLAASEEETRQAKAELAALQ 1025
Cdd:TIGR02168 728 ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA-----EAEAEIEELEAQIEQLKEELKALR 802
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1622882005 1026 aRQQLELEEVHRRVKTALARKEEAVSSLRTQHEAAVKRADHLEELLEQ 1073
Cdd:TIGR02168 803 -EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
598-1076 |
6.88e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 6.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 598 RRVKETEKALSR--QLQRQREHYEATIQRHLAFIDQLIEDKKVLSEKCEAVVAELKQEDQRcTERVAQVQAQHEL---EI 672
Cdd:PRK03918 176 RRIERLEKFIKRteNIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL-KEEIEELEKELESlegSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 673 KKLKELMSATEKVRRE--KWISEKTKKIKEVT-VRGLEPEIQKLIARHKQEVRRLKSLH-EAELLQSDERASQRCLRQAE 748
Cdd:PRK03918 255 RKLEEKIRELEERIEElkKEIEELEEKVKELKeLKEKAEEYIKLSEFYEEYLDELREIEkRLSRLEEEINGIEERIKELE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 749 ELREQLEREKEALGQQERERARQRFQQHLEQEQWALQQQRQRLYS----------------------EVAEERERLGQQA 806
Cdd:PRK03918 335 EKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKrltgltpeklekeleelekakeEIEEEISKITARI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 807 ARQRAELEELRQQLEESSSALTRAL---RAEFEKGREEQERRHQMELKALKQQL--------ELERQAWEAGCARKEEAW 875
Cdd:PRK03918 415 GELKKEIKELKKAIEELKKAKGKCPvcgRELTEEHRKELLEEYTAELKRIEKELkeieekerKLRKELRELEKVLKKESE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 876 LLnREQELREEIRKGRDKEIELVIHRLEADMALAKEESEKAA--ESRIKRLRDK------YEAELSELEQSERKLHERCS 947
Cdd:PRK03918 495 LI-KLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIklKGEIKSLKKElekleeLKKKLAELEKKLDELEEELA 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 948 ELKGQLGE-----AEGENLRLQGLVRQKERALEDTQAVSGQmnEQLSSERSNLAQVIRQEFEDrLAASEEETRQAKAELA 1022
Cdd:PRK03918 574 ELLKELEElgfesVEELEERLKELEPFYNEYLELKDAEKEL--EREEKELKKLEEELDKAFEE-LAETEKRLEELRKELE 650
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622882005 1023 ALQARQQLE----LEEVHRRVKTALARKEEAVSSLRTQHEAAVKRADHLEELLEQHRR 1076
Cdd:PRK03918 651 ELEKKYSEEeyeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREK 708
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
707-959 |
7.44e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.40 E-value: 7.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 707 EPEIQKLIARHKQEVRRLKSLHEAELlqsDERASQRCLRQAEELREQLEREKEALGQQERERAR------QRFQQHLEQE 780
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALE---DAREQIELLEPIRELAERYAAARERLAELEYLRAAlrlwfaQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 781 QWALQQQRQRLysevAEERERLGQQAARQRAELEELRQQLEESSSALTRALRAEFEKGREEQERRhqmelkalkqqlELE 860
Cdd:COG4913 297 LEELRAELARL----EAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEER------------ERR 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 861 RQAWEAGCARKEEAWLLNRE--QELREEIRKGRDKEIELvIHRLEADMALAKEEsEKAAESRIKRLrdkyEAELSELEQS 938
Cdd:COG4913 361 RARLEALLAALGLPLPASAEefAALRAEAAALLEALEEE-LEALEEALAEAEAA-LRDLRRELREL----EAEIASLERR 434
|
250 260
....*....|....*....|....*
gi 1622882005 939 ----ERKLHERCSELKGQLGEAEGE 959
Cdd:COG4913 435 ksniPARLLALRDALAEALGLDEAE 459
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
576-1076 |
8.42e-10 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 63.06 E-value: 8.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 576 EEKKQAMLLLQRALAQQRDLTVrrVKETEKALSRQLQRQREHYEATIQRHLAFIDqliedkkvlsEKCEAVVAELKQEDQ 655
Cdd:TIGR00618 369 EISCQQHTLTQHIHTLQQQKTT--LTQKLQSLCKELDILQREQATIDTRTSAFRD----------LQGQLAHAKKQQELQ 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 656 RCTERVAQVQAQHELEIKKLKELMsATEKVRREKWISEKTKKIKEVTVRglEPEIQKLIARHKQEVRRLKSLHEAELLQS 735
Cdd:TIGR00618 437 QRYAELCAAAITCTAQCEKLEKIH-LQESAQSLKEREQQLQTKEQIHLQ--ETRKKAVVLARLLELQEEPCPLCGSCIHP 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 736 DERASQRCLRQAEELREQLEREKEALGQQERERARQRFQQHLEQeQWALQQQRQRLysevAEERERLGQQAARQRAELEE 815
Cdd:TIGR00618 514 NPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQ-RASLKEQMQEI----QQSFSILTQCDNRSKEDIPN 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 816 LRQQLEESSSALTRALRAEFEKGREEQERRHQMELKALKQQLELERQAWEagcarKEEAWLLNREQELREEIRKGRDKEI 895
Cdd:TIGR00618 589 LQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCS-----QELALKLTALHALQLTLTQERVREH 663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 896 ELVIHRLEADMALAKEESEKAAESRIKRLRDKYE----------AELSELEQSERKLHERCSELKGQLGEAEGENLRLQG 965
Cdd:TIGR00618 664 ALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEmlaqcqtllrELETHIEEYDREFNEIENASSSLGSDLAAREDALNQ 743
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 966 LVRQKER-------ALEDTQAVSGQ---MNEQLSSERSNLAQVI------RQEFEDRLAASEEETRQAKAELAALQARQQ 1029
Cdd:TIGR00618 744 SLKELMHqartvlkARTEAHFNNNEevtAALQTGAELSHLAAEIqffnrlREEDTHLLKTLEAEIGQEIPSDEDILNLQC 823
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1622882005 1030 LELEEVHRRVKTALARKEEAVSSLRTQHEAAVKRADHLEELLEQHRR 1076
Cdd:TIGR00618 824 ETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAK 870
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
797-1073 |
9.19e-10 |
|
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: 63.16 E-value: 9.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 797 EERERLGQQAARQRAELEELRQQLEesssaltralraefekgREEQERRHQMELKALKQQLElERQAWEagcarkeeawL 876
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLE-----------------RLRREREKAERYQALLKEKR-EYEGYE----------L 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 877 LNREQELREEIRKGrDKEIElvihrleadmalAKEESEKAAESRIKRLRDKYEAELSELEQSERKLHERCSE----LKGQ 952
Cdd:TIGR02169 229 LKEKEALERQKEAI-ERQLA------------SLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEeqlrVKEK 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 953 LGEAEGENLRLQGLVRQKERALEDTQAVSGQMNEQLSSERSNLAQVIRQ--EFEDRLAASEEETRQAKAELAALQARQQl 1030
Cdd:TIGR02169 296 IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREieEERKRRDKLTEEYAELKEELEDLRAELE- 374
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1622882005 1031 ELEEVHRRVKTALARKEEAVSSLRTQHEAAVKRADHLEELLEQ 1073
Cdd:TIGR02169 375 EVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR 417
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
532-1076 |
1.80e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.47 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 532 DEMEKSGQDQPDPQQEGWVLEAGPGPLELGSEASTSvmrlklevEEKKQAMLLLQRALAQQRDLTVRRVKETEKAL-SRQ 610
Cdd:PTZ00121 1082 DAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKA--------EEAKKKAEDARKAEEARKAEDARKAEEARKAEdAKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 611 LQRQREHYEAtiqrHLAFIDQLIEDKKVLSEKCEAVVAElKQEDQRCTERVAQVQAQHELE-IKKLKELMSATEKVRRE- 688
Cdd:PTZ00121 1154 VEIARKAEDA----RKAEEARKAEDAKKAEAARKAEEVR-KAEELRKAEDARKAEAARKAEeERKAEEARKAEDAKKAEa 1228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 689 -KWISEKTKKIKEV----TVRGLEPEIQKLIARHKQEVRRLKSLHEAELLQSDERASQRCLRQAEELREQLEREK----- 758
Cdd:PTZ00121 1229 vKKAEEAKKDAEEAkkaeEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKadeak 1308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 759 -----------------------EALGQQERERARQRFQQHLEQEQWALQQQRQRLYSEVAE---ERERLGQQAARQRAE 812
Cdd:PTZ00121 1309 kkaeeakkadeakkkaeeakkkaDAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEkkkEEAKKKADAAKKKAE 1388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 813 ----LEELRQQLEESSSALTRALRAEFEKGREE------QERRHQMELKA----------LKQQLELERQAWEAGcARKE 872
Cdd:PTZ00121 1389 ekkkADEAKKKAEEDKKKADELKKAAAAKKKADeakkkaEEKKKADEAKKkaeeakkadeAKKKAEEAKKAEEAK-KKAE 1467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 873 EAWLLNREQELREEIRKGRDKEIELVIHRLEADMALAKEESEKAAESRIKRLRDKYEAELSELEQSERKLHERCSELKGQ 952
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK 1547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 953 LGEA-EGENLRLQGLVR---QKERALEDTQAVSGQMNEQLSSERSNLAQVIRQEFEDRLAASEEETRQAKAELAALQARQ 1028
Cdd:PTZ00121 1548 ADELkKAEELKKAEEKKkaeEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1622882005 1029 QLELEEVHRRVKTALARKEEAVSSLRTQHEAAVKRADHLEELLEQHRR 1076
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK 1675
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
633-959 |
2.89e-09 |
|
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: 61.62 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 633 IEDKKVLSEKCEAVVAELKQEDQRC-TERVaqvQAQHELEIKKLKELMSATEKVRrEKWISEKTKKIKEVTVRGLEPEIQ 711
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQLERLrRERE---KAERYQALLKEKREYEGYELLK-EKEALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 712 KLIARHKQEVRRLKSLhEAELLQSDERASQRCLRQAEELREQLEREKEALGQQER-ERARQRFQQHLEQEQWALQQQRQR 790
Cdd:TIGR02169 255 KLTEEISELEKRLEEI-EQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERsIAEKERELEDAEERLAKLEAEIDK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 791 LYSEVAEERERLGQQAARQ----------RAELEELRQQLEESSSALtRALRAEFEKGREEqerrhqmeLKALKQQL-EL 859
Cdd:TIGR02169 334 LLAEIEELEREIEEERKRRdklteeyaelKEELEDLRAELEEVDKEF-AETRDELKDYREK--------LEKLKREInEL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 860 ERqaweagcarkEEAWLLNREQELREEIRKGRDK--EIELVIHRLEADMALAKEESEKAAE--SRIKRLRDKYEAELSEL 935
Cdd:TIGR02169 405 KR----------ELDRLQEELQRLSEELADLNAAiaGIEAKINELEEEKEDKALEIKKQEWklEQLAADLSKYEQELYDL 474
|
330 340
....*....|....*....|....
gi 1622882005 936 EQSERKLHERCSELKGQLGEAEGE 959
Cdd:TIGR02169 475 KEEYDRVEKELSKLQRELAEAEAQ 498
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
563-1062 |
3.85e-09 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 61.01 E-value: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 563 EASTSVMRLKLEVEEKKQAMLLLQRALAQQRDLTVRRVKETEKALSRQLQRQREHYEATIQRHLAFIDQLIEDKKVLSEK 642
Cdd:pfam12128 269 SDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 643 CEAVVAELKQEDQRC---TERVAQVQAQHELEIKKLKElmsatEKVRREKWISEKTKKIKEVTVRGLEPE---IQKLIA- 715
Cdd:pfam12128 349 LPSWQSELENLEERLkalTGKHQDVTAKYNRRRSKIKE-----QNNRDIAGIKDKLAKIREARDRQLAVAeddLQALESe 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 716 -RHKQEVRRLKSLHEAELLQSdeRASQRCLRQAEELREQLEREKEALGQQERERARQRfQQHLEQEQWALQQQRQRLYSE 794
Cdd:pfam12128 424 lREQLEAGKLEFNEEEYRLKS--RLGELKLRLNQATATPELLLQLENFDERIERAREE-QEAANAEVERLQSELRQARKR 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 795 VAEERERLGQQAAR---QRAELEELRQQLEESSSALTRALRAefekgreeqerrhqmelkalkqqlelERQAWEAGCARK 871
Cdd:pfam12128 501 RDQASEALRQASRRleeRQSALDELELQLFPQAGTLLHFLRK--------------------------EAPDWEQSIGKV 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 872 EEAWLLNReQELREEIRKGRDKEiELVIHRLEADMALAKEESEKAAESRIKRLRDKYEAELseleQSERKLHERCSELKG 951
Cdd:pfam12128 555 ISPELLHR-TDLDPEVWDGSVGG-ELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEAL----QSAREKQAAAEEQLV 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 952 QLGEAEGENLRLQGLVRQKERALEDTQavsgqmnEQLSSERSNLAQVIRQEFEDRLAASEEETRQAKAELAALQARQQLE 1031
Cdd:pfam12128 629 QANGELEKASREETFARTALKNARLDL-------RRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAW 701
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1622882005 1032 LEEVHRRVKTA------------------LARKEEAVSSLRTQHEAAVK 1062
Cdd:pfam12128 702 LEEQKEQKREArtekqaywqvvegaldaqLALLKAAIAARRSGAKAELK 750
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
605-1076 |
4.25e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 605 KALSRQLQRQREHYEATIQRHlAFIDQLIEDKKVLSEKCEAVVAELKQEDQRCTERVAQVQAqhelEIKKLKELMSATEK 684
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRT-ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEK----EVKELEELKEEIEE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 685 VRREKWISEKTKKIKEVTVRGLEPEIQKLIARHK---QEVRRLKSLHEAEllqsderasqrclrqaeelreqlerekeal 761
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEeleEKVKELKELKEKA------------------------------ 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 762 gqqERERARQRFQQHLEQEQWALQQQRQRLYSEVAEERERLgQQAARQRAELEELRQQLEESSSALtralrAEFEKGREE 841
Cdd:PRK03918 293 ---EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI-KELEEKEERLEELKKKLKELEKRL-----EELEERHEL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 842 QERrhQMELKALKQQLELERQAWEAGCARKEEAWLLNREQELREEIRKGRDKEIELviHRLEADMALAKEESEKA----- 916
Cdd:PRK03918 364 YEE--AKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGEL--KKEIKELKKAIEELKKAkgkcp 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 917 ------AESRIKRLRDKYEAELSELEQSERKLHERCSELKGQLGEAEGENLRLQGLVRQKERAledtqavsgqmnEQLSS 990
Cdd:PRK03918 440 vcgrelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELA------------EQLKE 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 991 ERSNLAQVIRQEFEdrlaASEEETRQAKAELAALQARQqleleevhRRVKTALARKEEAVSSLRTQHEAAVKRADHLEEL 1070
Cdd:PRK03918 508 LEEKLKKYNLEELE----KKAEEYEKLKEKLIKLKGEI--------KSLKKELEKLEELKKKLAELEKKLDELEEELAEL 575
|
....*.
gi 1622882005 1071 LEQHRR 1076
Cdd:PRK03918 576 LKELEE 581
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
591-897 |
4.98e-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: 60.84 E-value: 4.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 591 QQRDLTVRRVKETEKALSR------QLQRQREHYEATIQRHLAFIDQ-----------LIEDKKVLSEKCEAVVAELKQE 653
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRledilnELERQLKSLERQAEKAERYKELkaelrelelalLVLRLEELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 654 DQRCTERVAQVQAQHEleikKLKELMSATEKVRREkwISEKTKKIKEVT--VRGLEPEIQKLIARHKQEVRRLKSLhEAE 731
Cdd:TIGR02168 252 EEELEELTAELQELEE----KLEELRLEVSELEEE--IEELQKELYALAneISRLEQQKQILRERLANLERQLEEL-EAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 732 LLQSDERASQRCLRQAEELREQLEREKEALGQQERERARQRFQQHLEQEQWALQQQRQRLYSEVAEERerlgQQAARQRA 811
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE----LQIASLNN 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 812 ELEELRQQLEESSSALTRA---LRAEFEKGREEQERRHQMELKALKQQLELERQAWEAGCARKEEawLLNREQELREEIR 888
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLqqeIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE--LREELEEAEQALD 478
|
....*....
gi 1622882005 889 KGRDKEIEL 897
Cdd:TIGR02168 479 AAERELAQL 487
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
673-1076 |
8.24e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 8.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 673 KKLKELMSATEKVRREKWISEKTKKIKEvTVRGLEPEIQKLIARHKQEVRRLKSLHEAELLQSDERASQRCLRQAEELRE 752
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEELEEELE-ELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 753 QLEREKEALgqQERERARQRFQQHLEQEQWALQQQRQRLYSEVAEERERLGQQAARQRAELEELRQQLEESSSALTRALR 832
Cdd:COG4717 157 ELRELEEEL--EELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 833 AEFEKGREEQERRHQMELKALKQQLELERQAWEAGCA----------------------RKEEAWLLNREQELR--EEIR 888
Cdd:COG4717 235 ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLiltiagvlflvlgllallflllAREKASLGKEAEELQalPALE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 889 KGRDKEIELVIHRLEADMALAKEESEKAAES--RIKRLRDKYEAELSELEQSERKlHERCSELKGQLGEAEGENLRLQGL 966
Cdd:COG4717 315 ELEEEELEELLAALGLPPDLSPEELLELLDRieELQELLREAEELEEELQLEELE-QEIAALLAEAGVEDEEELRAALEQ 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 967 VRQKERALEDTQAVSGQMNEQLSSERSNLAQVIR-------QEFEDRLAASEEETRQAKAELAALQAR-QQLELEEVHRR 1038
Cdd:COG4717 394 AEEYQELKEELEELEEQLEELLGELEELLEALDEeeleeelEELEEELEELEEELEELREELAELEAElEQLEEDGELAE 473
|
410 420 430
....*....|....*....|....*....|....*...
gi 1622882005 1039 VKTALARKEEAVSSLRTQHEAAVKRADHLEELLEQHRR 1076
Cdd:COG4717 474 LLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
790-1073 |
2.32e-08 |
|
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: 58.54 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 790 RLYSEVAEERERLGQ---QAARQRAELEELRQQLEESSSALTRALRAEFEKGRE-----EQERRHQMELKALKQQLELER 861
Cdd:TIGR02169 671 SEPAELQRLRERLEGlkrELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEieqleQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 862 QAWEAgcARKEEAWLLNREQELREEIRKgrdkeIELVIHRLEADMALAKEESEKAAESRIKRLRDKYEAELSELEQSERK 941
Cdd:TIGR02169 751 QEIEN--VKSELKELEARIEELEEDLHK-----LEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 942 LHERCSELKGQLGEAEGENLRLQGLVRQKERALEDTQAVSGQMNEQLSSERSNLAqvirqEFEDRLAASEEETRQAKAEL 1021
Cdd:TIGR02169 824 LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR-----DLESRLGDLKKERDELEAQL 898
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1622882005 1022 AALQARQQleleevhrRVKTALARKEEAVSSLRTQHEAAVKRADHLEELLEQ 1073
Cdd:TIGR02169 899 RELERKIE--------ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE 942
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
876-1057 |
2.76e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 876 LLNREQELREEIRKGRDK--EIELVIHRLEADMALAKEESEKAAESRIKRLRDKYEAELSELEQSERKLHERCSELKGQL 953
Cdd:COG4913 253 LLEPIRELAERYAAARERlaELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 954 GEAEGENL-RLQGLVRQKERALEDTQAVSGQMNEQLSSERSNLAQViRQEFEDRLAASEEETRQAKAELAALQARQQlEL 1032
Cdd:COG4913 333 RGNGGDRLeQLEREIERLERELEERERRRARLEALLAALGLPLPAS-AEEFAALRAEAAALLEALEEELEALEEALA-EA 410
|
170 180
....*....|....*....|....*
gi 1622882005 1033 EEVHRRVKTALARKEEAVSSLRTQH 1057
Cdd:COG4913 411 EAALRDLRRELRELEAEIASLERRK 435
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
709-1073 |
3.49e-08 |
|
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: 57.77 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 709 EIQKLIARHKQEVRRLKSlHEAELLQSDERASQRclrqaeelreQLEREKEALGQQERERARQRFQQHLEQEQWALQQQR 788
Cdd:TIGR02169 685 GLKRELSSLQSELRRIEN-RLDELSQELSDASRK----------IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 789 QRLYSEVAEERERLgqqaARQRAELEELRQQLEEsssaLTRALRAEFEKgreeqerrhqmELKALKQQLELERQAWEAGC 868
Cdd:TIGR02169 754 ENVKSELKELEARI----EELEEDLHKLEEALND----LEARLSHSRIP-----------EIQAELSKLEEEVSRIEARL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 869 ARKEEAwlLNREQELREEIRKGRDKEIELVIhrleaDMALAKEESEKAAESRIKRLRDKyEAELSELEQSERKLHERCSE 948
Cdd:TIGR02169 815 REIEQK--LNRLTLEKEYLEKEIQELQEQRI-----DLKEQIKSIEKEIENLNGKKEEL-EEELEELEAALRDLESRLGD 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 949 LKGQLGEAEGENLRLQGLVRQKERALEDTQAVSGQMNEQLSSERSNLAQVIRQEFEDRLAASEEET-RQAKAELAALQAR 1027
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSlEDVQAELQRVEEE 966
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1622882005 1028 QQlELEEVHRRVKTALARKEEAVSSLRTQHEAAVKRADHLEELLEQ 1073
Cdd:TIGR02169 967 IR-ALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
793-1076 |
3.78e-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: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 793 SEVAEERERLGQQAarQRAE-LEELRQQLEESSSALTralraefeKGREEQERRHQMELKALKQQLELERQAWEAGCARK 871
Cdd:TIGR02168 196 NELERQLKSLERQA--EKAErYKELKAELRELELALL--------VLRLEELREELEELQEELKEAEEELEELTAELQEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 872 EEAWLLNREQ--ELREEIRKGRDKEIELV--IHRLEADMALAKEEsekaaESRIKRLRDKYEAELSELEQSERKLHERCS 947
Cdd:TIGR02168 266 EEKLEELRLEvsELEEEIEELQKELYALAneISRLEQQKQILRER-----LANLERQLEELEAQLEELESKLDELAEELA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 948 ELKGQLGEAEGENLRLQGLVRQKERALEDTQAVSGQMNEQLSSERSNLAQVIRQE---------FEDRLAASEEETRQAK 1018
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIaslnneierLEARLERLEDRRERLQ 420
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622882005 1019 AELAALQARQQ-LELEEVHRRvktaLARKEEAVSSLRTQHEAAVKRADHLEELLEQHRR 1076
Cdd:TIGR02168 421 QEIEELLKKLEeAELKELQAE----LEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
775-1075 |
7.03e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.97 E-value: 7.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 775 QHLEQEQWALQQQRQRLYSEVAEERERlgqqaarqRAELEELRQQLEESSSALTRALRAEFEKGREEQERRHQM-----E 849
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEEHEER--------REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLeeleeE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 850 LKALKQQLELERQAWEAGCARKEEawLLNREQELREEIRKGRdkeIELVIHRLEADMALakeESEKAAESRIKRLRDKYE 929
Cdd:PRK02224 295 RDDLLAEAGLDDADAEAVEARREE--LEDRDEELRDRLEECR---VAAQAHNEEAESLR---EDADDLEERAEELREEAA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 930 AELSELEQSERKLHER---CSELKGQLGEAEGE----NLRLQGLVRQKERALEDTQAVSGQMNEqLSSERSNLAQVIR-- 1000
Cdd:PRK02224 367 ELESELEEAREAVEDRreeIEELEEEIEELRERfgdaPVDLGNAEDFLEELREERDELREREAE-LEATLRTARERVEea 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 1001 -------------QEFEDR-LAASEEETRQAKAELAALQARQQLELEEVHRRVKTA------------LARKEEAVSSLR 1054
Cdd:PRK02224 446 ealleagkcpecgQPVEGSpHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAedlveaedrierLEERREDLEELI 525
|
330 340 350
....*....|....*....|....*....|..
gi 1622882005 1055 TQHEAAV-----------KRADHLEELLEQHR 1075
Cdd:PRK02224 526 AERRETIeekreraeelrERAAELEAEAEEKR 557
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
694-1076 |
7.56e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 7.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 694 KTKKIKEVTVRGLEPEIQKLIARHKQEVRRLKSLHEAELLQSDERASQRCLRQAEELREQLEREKEALgqQERERARQRF 773
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY--QELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 774 QQhlEQEQWALQQQRQRLYSEVAEERERLGQQAARQRAELEELRQQLEESSSALTRALRAEFEKGREEQERRHQmELKAL 853
Cdd:COG4717 142 AE--LPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEE-ELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 854 KQQLELERQAWEagcARKEEAWLLNREQELREEIRK-----------GRDKEIELVI----------------------- 899
Cdd:COG4717 219 QEELEELEEELE---QLENELEAAALEERLKEARLLlliaaallallGLGGSLLSLIltiagvlflvlgllallflllar 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 900 ----HRLEADMALAKEESEKAAESRIKRLRDKYEAELSELEQSERKLHERCSELKGQLGEAEGENLRLQGLVRQKERA-- 973
Cdd:COG4717 296 ekasLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAal 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 974 LEDTQAVSGQM----------NEQLSSERSNLAQVIRQEFEDRLAASEEETR-QAKAELAALQARQQlELEEVHRRVKTA 1042
Cdd:COG4717 376 LAEAGVEDEEElraaleqaeeYQELKEELEELEEQLEELLGELEELLEALDEeELEEELEELEEELE-ELEEELEELREE 454
|
410 420 430
....*....|....*....|....*....|....
gi 1622882005 1043 LARKEEAVSSLRTQHEAAVKRADHlEELLEQHRR 1076
Cdd:COG4717 455 LAELEAELEQLEEDGELAELLQEL-EELKAELRE 487
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
776-1070 |
1.50e-07 |
|
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: 55.51 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 776 HLEQEQWALQQQRQRLYSEVAEErERLGQQAARQRAELEElRQQLEESSSALTRAL-----------RAEFEKGREeQER 844
Cdd:pfam17380 276 HIVQHQKAVSERQQQEKFEKMEQ-ERLRQEKEEKAREVER-RRKLEEAEKARQAEMdrqaaiyaeqeRMAMERERE-LER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 845 RHQMELKALKQQLELERQAWEAGCARKEEAWLLNREQE---LREEIRKGR-----DKEIELVIHRLEADMALAKEESEKA 916
Cdd:pfam17380 353 IRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKnerVRQELEAARkvkilEEERQRKIQQQKVEMEQIRAEQEEA 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 917 AESRIKRLRDKYEAELSELEQSERKLHERCSELKGQLGEAEGENLRLQGLVRQKERALEDTQavsgqmneqlssersnla 996
Cdd:pfam17380 433 RQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRR------------------ 494
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622882005 997 QVIRQEFEDRLAASEEETRQAKAELAALQARQQLELEEVHRRVKTALARKEEAVSSLRTQHEAAVKRADHLEEL 1070
Cdd:pfam17380 495 KILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRL 568
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
603-936 |
1.63e-07 |
|
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: 55.51 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 603 TEKALSRQLQRQREHYEATIQRHLAFIDQLIEDKKVLSEKCEAVVAELKQEDQRCTERVAQVQAQHELEIKKLKELMsAT 682
Cdd:pfam17380 266 TENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERM-AM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 683 EKVRREKWISEKTKKikevtvRGLEPEIQKLIARHKQEVRRLKSLhEAELLQSDERASQRcLRQAEELREQLEREKEALG 762
Cdd:pfam17380 345 ERERELERIRQEERK------RELERIRQEEIAMEISRMRELERL-QMERQQKNERVRQE-LEAARKVKILEEERQRKIQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 763 QQERERARQRFQQhleqeQWALQQQRQRLYSEVAEERERLGQQAARQRAELEELRQQLEESSSALTRALRAEFEKGREEQ 842
Cdd:pfam17380 417 QQKVEMEQIRAEQ-----EEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEE 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 843 ERRH--QMELKALKQQLELERQAWEAGCARKEEAWLLNREQELREEIRKGRDKEIEL-VIHRLEADMALAKEESEK--AA 917
Cdd:pfam17380 492 QRRKilEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMeERRRIQEQMRKATEERSRleAM 571
|
330
....*....|....*....
gi 1622882005 918 ESRIKRLRDKYEAELSELE 936
Cdd:pfam17380 572 EREREMMRQIVESEKARAE 590
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
794-1074 |
2.41e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 794 EVAEERERLGQQAARQRAELEELRQQLEESSSALTRALRAEFEKGREE-------QERRHQME-LKALKQQLELERQAWE 865
Cdd:PRK02224 416 ELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGsphvetiEEDRERVEeLEAELEDLEEEVEEVE 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 866 AGCARKEEAWLLNREQELREEIRkgrdkeiELVIHRLEADMALAKEESEKAAESRIKrlRDKYEAELSELEQSERKLHER 945
Cdd:PRK02224 496 ERLERAEDLVEAEDRIERLEERR-------EDLEELIAERRETIEEKRERAEELRER--AAELEAEAEEKREAAAEAEEE 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 946 CSELKGQLGEAEGE----NLRLQGLvrQKERALEDTQAVSGQMNEQLSSERSNLAQVIRQEfEDRLAASEEETRQAKAEL 1021
Cdd:PRK02224 567 AEEAREEVAELNSKlaelKERIESL--ERIRTLLAAIADAEDEIERLREKREALAELNDER-RERLAEKRERKRELEAEF 643
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622882005 1022 ---AALQARQQLE-LEEVHRRVKTALARKEEAVSSLRTQHEAAVKRADHLEELLEQH 1074
Cdd:PRK02224 644 deaRIEEAREDKErAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERR 700
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
599-897 |
2.74e-07 |
|
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: 54.74 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 599 RVKETEKALSRQLQRQREHYEATIQRHLAFidqliedkkvlsEKCEAVVAE---LKQEDQRCTERVAQVQAQHELEIKKL 675
Cdd:pfam17380 300 RLRQEKEEKAREVERRRKLEEAEKARQAEM------------DRQAAIYAEqerMAMERERELERIRQEERKRELERIRQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 676 KELMSATEKVRR-EKWISEKTKKIKEV--------TVRGLEPEIQKLIARHKQEVRRLKSLHE---AELLQSDERASQRC 743
Cdd:pfam17380 368 EEIAMEISRMRElERLQMERQQKNERVrqeleaarKVKILEEERQRKIQQQKVEMEQIRAEQEearQREVRRLEEERARE 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 744 LRQAEELREQLEREKEALGQQERERARQRFQQHLEQEQWAL-QQQRQRLYSEVAEERERLGQQAARQRAELEelrQQLEE 822
Cdd:pfam17380 448 MERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRaEEQRRKILEKELEERKQAMIEEERKRKLLE---KEMEE 524
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622882005 823 SSSALTralraefekgrEEQERRHQMELKALKQQLELERQAWEAGCARKEEAWLLN---REQELREEIRKGRDKEIEL 897
Cdd:pfam17380 525 RQKAIY-----------EEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEameREREMMRQIVESEKARAEY 591
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
779-1023 |
3.28e-07 |
|
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: 54.00 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 779 QEQWALQQQRQRLYSEVAEERERLgQQAARQRAELEELRQQLEESSSALTRALRAefekgREEQERRHQMELKALKQQLE 858
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKEL-AALKKEEKALLKQLAALERRIAALARRIRA-----LEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 859 LERQAWEAgcaRKEEAwllnrEQELREEIRKGRDKEIELVIHRLEADMALAKEESEKAAESRIKRLRDKYEAELSELEQS 938
Cdd:COG4942 94 ELRAELEA---QKEEL-----AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 939 ERKLHERCSELKGQLGEAEGENLRLQGLVRQKERALEdtqavsgQMNEQLSSERSNLAQVIRQEFE-DRLAASEEETRQA 1017
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLA-------RLEKELAELAAELAELQQEAEElEALIARLEAEAAA 238
|
....*.
gi 1622882005 1018 KAELAA 1023
Cdd:COG4942 239 AAERTP 244
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
724-918 |
3.89e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 54.01 E-value: 3.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 724 LKSLHEAELLQSDERAsQRCLRQAEELREQLEREKEALGQQERERARQRFQQHLEQEQWALQQQRQRLysevaEERErlg 803
Cdd:PRK12704 25 RKKIAEAKIKEAEEEA-KRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRL-----LQKE--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 804 QQAARQRAELEELRQQLEESSSALTRaLRAEFEKGREEQERRHQmelkalKQQLELERQAweagCARKEEAwllnrEQEL 883
Cdd:PRK12704 96 ENLDRKLELLEKREEELEKKEKELEQ-KQQELEKKEEELEELIE------EQLQELERIS----GLTAEEA-----KEIL 159
|
170 180 190
....*....|....*....|....*....|....*
gi 1622882005 884 REEIRKGRDKEIELVIHRLEADmalAKEESEKAAE 918
Cdd:PRK12704 160 LEKVEEEARHEAAVLIKEIEEE---AKEEADKKAK 191
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
758-1074 |
6.82e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.81 E-value: 6.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 758 KEALGQQERERARQRFQQHLEQEQWALQQQRQRLYSEVAEERERLGQQAARQR--AELEELRQQLEESSSAltRALRAEF 835
Cdd:PRK04863 300 RQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIERyqADLEELEERLEEQNEV--VEEADEQ 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 836 EKGREEQERRHQMELKALKQQLELERQAWEAGCARK----------EEAWLLNREQELREE-----IRKGRDKEIELVIH 900
Cdd:PRK04863 378 QEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAiqyqqavqalERAKQLCGLPDLTADnaedwLEEFQAKEQEATEE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 901 RLEADMAL-----AKEESEKAAESrIKRLRDKYEAE---------LSELEqSERKLHERCSELKGQLGEAEGEnLRLQgl 966
Cdd:PRK04863 458 LLSLEQKLsvaqaAHSQFEQAYQL-VRKIAGEVSRSeawdvarelLRRLR-EQRHLAEQLQQLRMRLSELEQR-LRQQ-- 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 967 vRQKERALEDTQAVSGQMneqLSSErsNLAQVIRQEFEDRLAASEEEtrqaKAELAALQARQQLELEEVHRRVKTALARK 1046
Cdd:PRK04863 533 -QRAERLLAEFCKRLGKN---LDDE--DELEQLQEELEARLESLSES----VSEARERRMALRQQLEQLQARIQRLAARA 602
|
330 340 350
....*....|....*....|....*....|....
gi 1622882005 1047 ------EEAVSSLRTQHEAAVKRADHLEELLEQH 1074
Cdd:PRK04863 603 pawlaaQDALARLREQSGEEFEDSQDVTEYMQQL 636
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
597-1070 |
1.21e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 52.66 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 597 VRRVKETEKALSRQLQRQREHYEATIQRHLAFIDQLIEDKKVLSEkcEAVVAELKQE-DQRCTERVAQVQAQHELEIKKL 675
Cdd:TIGR00618 231 LREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQ--EAVLEETQERiNRARKAAPLAAHIKAVTQIEQQ 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 676 KELMSATEKVRREKWISEKTKKIKEVTVRGLEPEIQKLIARHKQEVRRLKSLHEAELLQSDERASQRCLRQ-----AEEL 750
Cdd:TIGR00618 309 AQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQhihtlQQQK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 751 REQLEREKEALGQQERERARQRFQQHLEQEQWALQQQRQRLYSEVAEERERLGQQAARQRAELEELRQQLEESSSALTRA 830
Cdd:TIGR00618 389 TTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSL 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 831 LRAEFEKGREEQ-----ERRHQMELKALKQQLELER--------------QAWEAGCARKEEAWLLNREQELREEIRKGR 891
Cdd:TIGR00618 469 KEREQQLQTKEQihlqeTRKKAVVLARLLELQEEPCplcgscihpnparqDIDNPGPLTRRMQRGEQTYAQLETSEEDVY 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 892 DKEIELVIHRLEADmalAKEESEKAAESRIKRLRDKYEAELSELEQSE---RKLHERCSELKGQLGEAegenLRLQGLVR 968
Cdd:TIGR00618 549 HQLTSERKQRASLK---EQMQEIQQSFSILTQCDNRSKEDIPNLQNITvrlQDLTEKLSEAEDMLACE----QHALLRKL 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 969 QKERALEDTQAVSGQMNEQLSSERSNLAQVIRQEFEDRLAASEEETRQAKAELAALQARQQLELEEVHRRVKTALARKEE 1048
Cdd:TIGR00618 622 QPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQ 701
|
490 500
....*....|....*....|..
gi 1622882005 1049 AVSSLRTQHEAAVKRADHLEEL 1070
Cdd:TIGR00618 702 CQTLLRELETHIEEYDREFNEI 723
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
595-1073 |
1.81e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 595 LTVRRVKETEKALSRQLQRQREHYE-----ATIQRHLAFIDQLIEDKKVLSEKCEAVVAELKQEDQRCTERVAQVQAQHE 669
Cdd:PRK02224 176 LGVERVLSDQRGSLDQLKAQIEEKEekdlhERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELET 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 670 LE--IKKLKELMSATEKVRREkwISEKTKKIKEvTVRGLEPEIQKLIARHKQEVRRLKSLHEA-ELLQSDERASQRCLRQ 746
Cdd:PRK02224 256 LEaeIEDLRETIAETEREREE--LAEEVRDLRE-RLEELEEERDDLLAEAGLDDADAEAVEARrEELEDRDEELRDRLEE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 747 AEELREQLEREKEALgqqeRERARQrfqqhLEQEQWALQQQRQRLYSEVAEERErlgqQAARQRAELEELRQQLEESSSA 826
Cdd:PRK02224 333 CRVAAQAHNEEAESL----REDADD-----LEERAEELREEAAELESELEEARE----AVEDRREEIEELEEEIEELRER 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 827 LTRA------LRAEFEKGREEQERRHQME------LKALKQQLELERQAWEAG----CARK-EEAWLLNREQELREEIRK 889
Cdd:PRK02224 400 FGDApvdlgnAEDFLEELREERDELREREaeleatLRTARERVEEAEALLEAGkcpeCGQPvEGSPHVETIEEDRERVEE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 890 GRDKEIELVIHRLEADMALAKEESEKAAESRIKRLRDKYEAELSELEQSERKLHE---RCSELKGQLGEAEGENLRLQGL 966
Cdd:PRK02224 480 LEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEkreRAEELRERAAELEAEAEEKREA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 967 VRQKERALEDTQAVSGQMNEQLS---SERSNLAQV---------IRQEFE---DRLAASEEETRQAKAELAALQAR-QQL 1030
Cdd:PRK02224 560 AAEAEEEAEEAREEVAELNSKLAelkERIESLERIrtllaaiadAEDEIErlrEKREALAELNDERRERLAEKRERkREL 639
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622882005 1031 ELEEVHRRVKTALARKEEAVS----------------------------------SLRTQHEAAVKRADHLEELLEQ 1073
Cdd:PRK02224 640 EAEFDEARIEEAREDKERAEEyleqveekldelreerddlqaeigaveneleeleELRERREALENRVEALEALYDE 716
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
599-1041 |
2.79e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 51.66 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 599 RVKETEKALSRQLQRQREHYEATIQRHLAFIDQLIEDKKV----LSEKCEAVVAELKQEDQRCTERVAQVQAQHELEIKK 674
Cdd:pfam15921 239 RIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVeitgLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQ 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 675 LKELMSATEKVRREKwisEKTKKIKEVTVRGLEPEIQkLIARHKQEVRRLKSLHEAELLQSDERAsQRCLRQAEELREQL 754
Cdd:pfam15921 319 LSDLESTVSQLRSEL---REAKRMYEDKIEELEKQLV-LANSELTEARTERDQFSQESGNLDDQL-QKLLADLHKREKEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 755 EREKEALGQ-QERERARQRFQQHLEQEQWALQQQRQRLYSEVAEERERLGQQAARQRAELEELRQQLEESSSaLTRALRA 833
Cdd:pfam15921 394 SLEKEQNKRlWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSS-LTAQLES 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 834 EFEKGRE--EQERRHQMELKA-------LKQQLELERQAWEAGCAR------------KEEAWLLNREQELR------EE 886
Cdd:pfam15921 473 TKEMLRKvvEELTAKKMTLESsertvsdLTASLQEKERAIEATNAEitklrsrvdlklQELQHLKNEGDHLRnvqtecEA 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 887 IR---KGRDKEIELVIHRLEADMALAKEESEKAAESRIKRLRDKYE-----AELSELEQSERKLHERCSELKGQLGEAEG 958
Cdd:pfam15921 553 LKlqmAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEindrrLELQEFKILKDKKDAKIRELEARVSDLEL 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 959 ENLRLQGLVRQKERALEDTQAVSGQMNEQLSSERSNLA------QVIRQEFEDRLAASEEETRQAKAELAALQArqqlEL 1032
Cdd:pfam15921 633 EKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNslsedyEVLKRNFRNKSEEMETTTNKLKMQLKSAQS----EL 708
|
....*....
gi 1622882005 1033 EEVHRRVKT 1041
Cdd:pfam15921 709 EQTRNTLKS 717
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
841-1076 |
5.20e-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: 50.15 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 841 EQERRHQMELKALKQQLELERQAWEAgcARKEEAWLLNREQELREEIRKGRDKeielvIHRLEADMAlakeesekAAESR 920
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAA--LKKEEKALLKQLAALERRIAALARR-----IRALEQELA--------ALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 921 IKRLRdkyeaelSELEQSERKLHERCSELKGQLGEAE--GENLRLQGLVRQKE-----RALEDTQAVSGQMNEQLSSERS 993
Cdd:COG4942 85 LAELE-------KEIAELRAELEAQKEELAELLRALYrlGRQPPLALLLSPEDfldavRRLQYLKYLAPARREQAEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 994 NLAQVirqefeDRLAASEEETRQAKAELAALQARQQLELEEVHRRVKTALARKEEAVSSLRTQHEAAVKRADHLEELLEQ 1073
Cdd:COG4942 158 DLAEL------AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
...
gi 1622882005 1074 HRR 1076
Cdd:COG4942 232 LEA 234
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
759-1016 |
6.93e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.34 E-value: 6.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 759 EALGQQErerARQRFQQHLEQEQWALQQQRQRLySEVAEERERLGQQAARQRAELEELRQQLEESSSAL----TRA---- 830
Cdd:COG3096 341 TALRQQE---KIERYQEDLEELTERLEEQEEVV-EEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALdvqqTRAiqyq 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 831 -----------------LRAEFEKGREEQERRHQME----LKALKQQLELE-------RQAWEAGCA-----RKEEAWll 877
Cdd:COG3096 417 qavqalekaralcglpdLTPENAEDYLAAFRAKEQQateeVLELEQKLSVAdaarrqfEKAYELVCKiagevERSQAW-- 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 878 nreQELREEIRKGRD---------------KEIELVIHRLEADMALAKEESEKAAESR-----IKRLRDKYEAELSELEQ 937
Cdd:COG3096 495 ---QTARELLRRYRSqqalaqrlqqlraqlAELEQRLRQQQNAERLLEEFCQRIGQQLdaaeeLEELLAELEAQLEELEE 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 938 SERKLHERCSELKGQLGEAEGE--------------NLRLQGLVRQKERALEDTQAVSGQMNEQLSSERSnlAQVIRQEF 1003
Cdd:COG3096 572 QAAEAVEQRSELRQQLEQLRARikelaarapawlaaQDALERLREQSGEALADSQEVTAAMQQLLERERE--ATVERDEL 649
|
330
....*....|...
gi 1622882005 1004 EDRLAASEEETRQ 1016
Cdd:COG3096 650 AARKQALESQIER 662
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
563-858 |
6.98e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 6.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 563 EASTSVMRLKLEVEEKKQAMLLLQRALAQQRDLTVRRVKETEKALSR-----QLQRQREHYEATIQRHLA---------F 628
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARlllllEAEADYEGFLEGVKAALLlaglrglagA 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 629 IDQLIEDKKVLSEKCEAVVAELKQEDQRCTERVAQVQAQHELEIKKLKELMSATEKVRREKWISEKTKKIKEV------- 701
Cdd:COG1196 526 VAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGaavdlva 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 702 ---------------TVRGLEPEIQKLIARHKQEVRRLKSLHEAELLQSDERASQRCLRQAEELREQLEREKEALGQQER 766
Cdd:COG1196 606 sdlreadaryyvlgdTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 767 ERARQRFQQHLEQEQWALQQQRQRLYSEVAEERERLGQQAARQRAELEELRQQLEESSSALTRALRAEFEKGREEQERRH 846
Cdd:COG1196 686 ERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEL 765
|
330
....*....|..
gi 1622882005 847 QMELKALKQQLE 858
Cdd:COG1196 766 ERELERLEREIE 777
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
804-1072 |
7.67e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.17 E-value: 7.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 804 QQAARQRAELEELRQQLEESSSALTRALRAEFEKGREEQERRhqMELKALKQQLELERQAWEAGCARKEEawllnREQEL 883
Cdd:pfam01576 22 QKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMR--ARLAARKQELEEILHELESRLEEEEE-----RSQQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 884 REEIRKGRDKEIELVIHRLEADMALAKEESEK-AAESRIKRLRDK---YEAELSELEQSERKLHERCSELKGQLGEAEGE 959
Cdd:pfam01576 95 QNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKvTTEAKIKKLEEDillLEDQNSKLSKERKLLEERISEFTSNLAEEEEK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 960 NLRLQGLVRQKERALEDTQ---------------------AVSGQMNEQLSSERSNLAQVIRQefedrLAASEEETRQAK 1018
Cdd:pfam01576 175 AKSLSKLKNKHEAMISDLEerlkkeekgrqelekakrkleGESTDLQEQIAELQAQIAELRAQ-----LAKKEEELQAAL 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1622882005 1019 AELAALQArQQLELEEVHRRVKTALARKEEAVSSLRTQHEAAVKRADHLEELLE 1072
Cdd:pfam01576 250 ARLEEETA-QKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELE 302
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
716-1076 |
8.07e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.34 E-value: 8.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 716 RHKQEVRRLksLHEAELLQSDERASQRCLRQAEELREQLEREKEALGQQER--ERARQRFQQHLEQEQWALQQQR--QRL 791
Cdd:COG3096 275 RHANERREL--SERALELRRELFGARRQLAEEQYRLVEMARELEELSARESdlEQDYQAASDHLNLVQTALRQQEkiERY 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 792 YSEVAEERERLGQQ------AARQRAELEELRQQLEESSSALTRALrAEFEKGREEQERR---HQMELKAL---KQQLEL 859
Cdd:COG3096 353 QEDLEELTERLEEQeevveeAAEQLAEAEARLEAAEEEVDSLKSQL-ADYQQALDVQQTRaiqYQQAVQALekaRALCGL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 860 ERQAWEAgcARKEEAWLLNREQELREEIRKGRDKEIELVIHRLEADMALA----------KEESEKAAESRIKRLRD--- 926
Cdd:COG3096 432 PDLTPEN--AEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYElvckiageveRSQAWQTARELLRRYRSqqa 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 927 ------KYEAELSELEQSERKLHErCSELKGQLGeaegenlRLQGLVRQKERALEDTQAVSGQMNEQLSSERSNLAQ--- 997
Cdd:COG3096 510 laqrlqQLRAQLAELEQRLRQQQN-AERLLEEFC-------QRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEqrs 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 998 VIRQEFEDRLAASEEETRQAKAELAALQARQQLElEEVHRRVKTALARKEEAVSSLRTQHEAAVKRaDHL----EELLEQ 1073
Cdd:COG3096 582 ELRQQLEQLRARIKELAARAPAWLAAQDALERLR-EQSGEALADSQEVTAAMQQLLEREREATVER-DELaarkQALESQ 659
|
...
gi 1622882005 1074 HRR 1076
Cdd:COG3096 660 IER 662
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
647-1069 |
1.11e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 49.66 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 647 VAELKQEDQRCT---ERVAQVQAQHELEIKKL--KELMSATEKVRREKWISEKTKKIKEVTvrGLEPEIQKLIARHKQEV 721
Cdd:TIGR00606 669 ITQLTDENQSCCpvcQRVFQTEAELQEFISDLqsKLRLAPDKLKSTESELKKKEKRRDEML--GLAPGRQSIIDLKEKEI 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 722 RRLKslheaELLQSDERASQRclrqaeelreqlerEKEALGQQERERARQRFQQHLEQEQWALQQQRQRLYSEVAEERER 801
Cdd:TIGR00606 747 PELR-----NKLQKVNRDIQR--------------LKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERK 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 802 LGQQAARQRA-----ELEELRQQLEESSSALTRA-----LRAEFEKGREEQERRHQMELKALK-QQLELERQAWEAGCAR 870
Cdd:TIGR00606 808 IAQQAAKLQGsdldrTVQQVNQEKQEKQHELDTVvskieLNRKLIQDQQEQIQHLKSKTNELKsEKLQIGTNLQRRQQFE 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 871 KEEAWLLNREQELREEIRKGRDKEIELV-----IHRLEADMALAKEESEKAAESRIKRLRDKYEAELSELEQSERKLHER 945
Cdd:TIGR00606 888 EQLVELSTEVQSLIREIKDAKEQDSPLEtflekDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDG 967
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 946 CSE-LKGQLGEAEGENLRLQGLVRQKERALEDTQAVSGQMNEQLSSERSNLAQVIRQEFEDRLAASEEETRQAKAELAAL 1024
Cdd:TIGR00606 968 KDDyLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQM 1047
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1622882005 1025 QARQQleleevhrrvKTALARKEEAVSSLRTQHEAAVKRADHLEE 1069
Cdd:TIGR00606 1048 QVLQM----------KQEHQKLEENIDLIKRNHVLALGRQKGYEK 1082
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
573-950 |
1.29e-05 |
|
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: 49.68 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 573 LEVEEKKQAMLLLQRALAQQRDLTVRRVKETEKALS------RQLQRQREhyeaTIQRHLAFIDQLIEDKKVLSEKCEAV 646
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSdasrkiGEIEKEIE----QLEQEEEKLKERLEELEEDLSSLEQE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 647 VAELKQEdqrcTERVAQVQAQHELEIKKLKELMSATEKVRREKWISEKTKKIKEvtvrgLEPEIQKLIARHKQEVRRLKS 726
Cdd:TIGR02169 753 IENVKSE----LKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSK-----LEEEVSRIEARLREIEQKLNR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 727 LHEAELLQSDERASQRCLRQAEELREQLEREKEALGQQERErarqRFQQHLEQEQWALQQQRQRLySEVAEERERLgqqa 806
Cdd:TIGR02169 824 LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE----ELEEELEELEAALRDLESRL-GDLKKERDEL---- 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 807 arqRAELEELRQQLEESSSALtralraefekgreEQERRHQMELKALKQQLELERQAWEAGCARKEEAwllnREQELREE 886
Cdd:TIGR02169 895 ---EAQLRELERKIEELEAQI-------------EKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI----PEEELSLE 954
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622882005 887 IRKGRDKEIELVIHRLEADMALAKEESEKAAESR--IKRLRDKYEAELSELeqseRKLHERCSELK 950
Cdd:TIGR02169 955 DVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLdeLKEKRAKLEEERKAI----LERIEEYEKKK 1016
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
645-1078 |
1.69e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.20 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 645 AVVAELKQEDQRCTERVAQVQAQHEleiKKLKELMSATEKVRREKWISEKTKKIKEVtvRGLEPEIQKLIARHKQEVRRL 724
Cdd:TIGR00618 219 ERKQVLEKELKHLREALQQTQQSHA---YLTQKREAQEEQLKKQQLLKQLRARIEEL--RAQEAVLEETQERINRARKAA 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 725 KSLHEAELLQSDERASQRCLRQaeelreqlerekeaLGQQERERARQRFQQHLEQEQWALQQQRQRLYSEVAEERERLGQ 804
Cdd:TIGR00618 294 PLAAHIKAVTQIEQQAQRIHTE--------------LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRD 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 805 QAARQRAELEELRQQLEESSSALT------------RALRAEFEKGREEQ---------ERRHQMELKALKQQLELERQ- 862
Cdd:TIGR00618 360 AHEVATSIREISCQQHTLTQHIHTlqqqkttltqklQSLCKELDILQREQatidtrtsaFRDLQGQLAHAKKQQELQQRy 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 863 --------AWEAGCARKEEAWLLNREQELREEIRKGRDKEI----ELVIHRLEADMALAKEESEKAAESRIKRLR----- 925
Cdd:TIGR00618 440 aelcaaaiTCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQihlqETRKKAVVLARLLELQEEPCPLCGSCIHPNparqd 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 926 -DKYEAELSELEQSERKLHERCSELKGQLGEAEGENLRLQGLVRQKERALEDTQAVSGQMNEqlSSERSNLAQVIRQEFE 1004
Cdd:TIGR00618 520 iDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNR--SKEDIPNLQNITVRLQ 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 1005 DRLAASEEETRQAKAELAALQARQQLEL------------EEVHRRVKTALARKEEAVSSLRTQHEAAVKRADHLEELLE 1072
Cdd:TIGR00618 598 DLTEKLSEAEDMLACEQHALLRKLQPEQdlqdvrlhlqqcSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLAS 677
|
....*.
gi 1622882005 1073 QHRRPT 1078
Cdd:TIGR00618 678 RQLALQ 683
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
571-1034 |
1.86e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.81 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 571 LKLEVEEKKQAMLLLQRALAQQRDLTVRRVKETEKALSRQLQRQR---EHYEATIQRHLAFIDQLIEDKKVLSEKC---- 643
Cdd:TIGR00618 435 LQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEqihLQETRKKAVVLARLLELQEEPCPLCGSCihpn 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 644 -EAVVAELKQEDQRCTERVAQVQAQHELEIKKLKELMSATEKVRREKWISEKTKKIKEVTVRGLEPEIQKLIARHKQEVR 722
Cdd:TIGR00618 515 pARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITV 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 723 RLKSLHEAellQSDERASQRCLRQAEELREQLEREKE--ALGQQERERARQRFQQHLEQEQWALQQQRQRLYS-EVAEER 799
Cdd:TIGR00618 595 RLQDLTEK---LSEAEDMLACEQHALLRKLQPEQDLQdvRLHLQQCSQELALKLTALHALQLTLTQERVREHAlSIRVLP 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 800 ERLGQQAARQRAELEELRQQLEESSSALTR---ALRAEFEKGREEQERRHQMELKALKQQLELERQAWEAgcarkeeAWL 876
Cdd:TIGR00618 672 KELLASRQLALQKMQSEKEQLTYWKEMLAQcqtLLRELETHIEEYDREFNEIENASSSLGSDLAAREDAL-------NQS 744
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 877 LNREQELREEIRKGRDKEIELVIHRLEADMALAKEESEKAAESRIKRlrdkyeaelSELEQSERKLHERCSELKGQLGEA 956
Cdd:TIGR00618 745 LKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFN---------RLREEDTHLLKTLEAEIGQEIPSD 815
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622882005 957 EGEnLRLQGLVRQKERAledtqavsgQMNEQLSSERSNLAQVIRQEFEDrlaaseEETRQAKAELAALQARQQLELEE 1034
Cdd:TIGR00618 816 EDI-LNLQCETLVQEEE---------QFLSRLEEKSATLGEITHQLLKY------EECSKQLAQLTQEQAKIIQLSDK 877
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
763-1054 |
1.93e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.02 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 763 QQERERARQRFQQHLEQEQWALQQQRQRLySEVAEERERLGQQAARQRAELEELRQQLEESSSALTRAlraefekgrEEQ 842
Cdd:pfam01576 505 LEEEEEAKRNVERQLSTLQAQLSDMKKKL-EEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL---------EKT 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 843 ERRHQMELKALKQQLELERQAWEAGCARK--------EEAWLLNREQELREEI-RKGRDKEIE-LVIHRLEADMALAKEE 912
Cdd:pfam01576 575 KNRLQQELDDLLVDLDHQRQLVSNLEKKQkkfdqmlaEEKAISARYAEERDRAeAEAREKETRaLSLARALEEALEAKEE 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 913 SEKAAesriKRLRDKYEAELS----------ELEQSERKLHERCSELKGQLGEAEGEnlrLQGLVRQKERALEDTQAVSG 982
Cdd:pfam01576 655 LERTN----KQLRAEMEDLVSskddvgknvhELERSKRALEQQVEEMKTQLEELEDE---LQATEDAKLRLEVNMQALKA 727
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622882005 983 QM-------NEQLSSERSNLAQVIRQefedrLAASEEETRQAKAELAALQARQQLELEEVHRRVKTALARKEEAVSSLR 1054
Cdd:pfam01576 728 QFerdlqarDEQGEEKRRQLVKQVRE-----LEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLK 801
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
558-822 |
3.52e-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: 48.13 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 558 LELGSEASTSVMRLKLEVEEKKQAMLLLQRALAQQRDLTVRRVKETEKALSRQLQRQREHYEATIQRHLAFIDQLIEDKK 637
Cdd:TIGR02168 720 ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 638 VLSE---KCEAVVAELKQEDQRCTERVAQVQAQHELEIKKLKELMSATEKVRREkwISEKTKKIKEVTVRGLEPEIQ--- 711
Cdd:TIGR02168 800 ALREaldELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED--IESLAAEIEELEELIEELESElea 877
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 712 KLIARHKQEVRRLKSLHEAELLQSDERASQRCLRQAEELREQLEREKEALgQQERERARQRFQQHLEQeqwaLQQQRQRL 791
Cdd:TIGR02168 878 LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL-ELRLEGLEVRIDNLQER----LSEEYSLT 952
|
250 260 270
....*....|....*....|....*....|.
gi 1622882005 792 YSEVAEERERLGQQAARQRAELEELRQQLEE 822
Cdd:TIGR02168 953 LEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
902-1076 |
3.64e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 902 LEADMALAKEESEkAAESRIKRLRDKYEaeLSELEQSERKLHERCSELKGQLGEAEGENLRLQGLVRQKERALEDTQAVS 981
Cdd:COG3206 180 LEEQLPELRKELE-EAEAALEEFRQKNG--LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDAL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 982 GQM--NEQLSSERSNLAQVIRQ--EFEDRLAASEEETRQAKAELAALQARQQLELEEVHRRVKTALARKEEAVSSLRTQH 1057
Cdd:COG3206 257 PELlqSPVIQQLRAQLAELEAElaELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQL 336
|
170
....*....|....*....
gi 1622882005 1058 EAAVKRADHLEELLEQHRR 1076
Cdd:COG3206 337 AQLEARLAELPELEAELRR 355
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
574-872 |
4.92e-05 |
|
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: 47.43 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 574 EVEEKKQAMLLLQRAL-AQQRDLTVRRVKETEKAlsRQLQRQREHYEATIQRHLAFIDQLIEdkkvlsekceavVAELKQ 652
Cdd:pfam17380 320 EAEKARQAEMDRQAAIyAEQERMAMERERELERI--RQEERKRELERIRQEEIAMEISRMRE------------LERLQM 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 653 EDQRCTERVAQ-------VQAQHELEIKKLKELMSATEKVRREKwisektKKIKEVTVRGLEPEIQKLIARHKQEvrRLK 725
Cdd:pfam17380 386 ERQQKNERVRQeleaarkVKILEEERQRKIQQQKVEMEQIRAEQ------EEARQREVRRLEEERAREMERVRLE--EQE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 726 SLHEAELLQSDERASQR---CLRQAEELREQLEREKEALGQQERERARQRFQQHLEQEQWALQQQRQRLYSEVAEERERL 802
Cdd:pfam17380 458 RQQQVERLRQQEEERKRkklELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRRE 537
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 803 GQQAARQRAELEELRQqleesssaltraLRAEFEKGREEQERrhqmeLKALKQQLELERQAWEAGCARKE 872
Cdd:pfam17380 538 AEEERRKQQEMEERRR------------IQEQMRKATEERSR-----LEAMEREREMMRQIVESEKARAE 590
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
883-1046 |
1.06e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.73 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 883 LREEIrKGRDKEIELVIHRLeADMA--LAKEESEKAA-ESRIKRLRdkyeAELSELEqserklHERcSELKGQLGEAEGE 959
Cdd:PRK09039 44 LSREI-SGKDSALDRLNSQI-AELAdlLSLERQGNQDlQDSVANLR----ASLSAAE------AER-SRLQALLAELAGA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 960 NLRLQGLVRQKERALEDTQAVSGQ-------MNEQLSSERSNLAQVirqefEDRLAASEEETRQAKAELAALQarqqlel 1032
Cdd:PRK09039 111 GAAAEGRAGELAQELDSEKQVSARalaqvelLNQQIAALRRQLAAL-----EAALDASEKRDRESQAKIADLG------- 178
|
170
....*....|....
gi 1622882005 1033 eevhRRVKTALARK 1046
Cdd:PRK09039 179 ----RRLNVALAQR 188
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
785-918 |
1.36e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 45.63 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 785 QQQRQRLYSEVAEERERLGQQAARQRAELEELRQQLEESSSALTRALRAEFEKGREEQERRHQMELKALKQQLELERQAw 864
Cdd:COG2268 218 QANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQE- 296
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1622882005 865 eagcARKEEawllnREQELREEIRKGRDKEIELVIHRLEADMALAKEESEKAAE 918
Cdd:COG2268 297 ----KEAER-----EEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAE 341
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
790-1037 |
1.62e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.66 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 790 RLYSEVAEERERLGQQAARQRAELEELRQQLEESSSALTRALRAEFEKGREEQERrhQMELKALKQQLELERQAWEAGCA 869
Cdd:pfam07888 48 QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEK--YKELSASSEELSEEKDALLAQRA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 870 RKEeAWLLNREQELREEIRKGRDKEIELVIHRLEADMALAKEESEKAAesrikrlRDKYEAELSELEQSERKLHERCSEL 949
Cdd:pfam07888 126 AHE-ARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAE-------RKQLQAKLQQTEEELRSLSKEFQEL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 950 KGQLGEAEGENLRLQGLVRQKERALEDTQAVSGQmNEQLSSERSNLaqvirqefEDRLAASEEETRQAKAELAALQARQQ 1029
Cdd:pfam07888 198 RNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAE-NEALLEELRSL--------QERLNASERKVEGLGEELSSMAAQRD 268
|
....*...
gi 1622882005 1030 LELEEVHR 1037
Cdd:pfam07888 269 RTQAELHQ 276
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
662-893 |
1.87e-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: 45.14 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 662 AQVQAQHELEIKKLKELMSATEKVRrekwisEKTKKIKEVTVRGLEpEIQKLIARHKQEVRRLKSlhEAELLQSDERASQ 741
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKEL------AALKKEEKALLKQLA-ALERRIAALARRIRALEQ--ELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 742 RclrQAEELREQLEREKEALGQQERERARQRFQQHLE----QEQWALQQQRQRLYSEVAEERERLGQQAARQRAELEELR 817
Cdd:COG4942 90 K---EIAELRAELEAQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622882005 818 QQLEESSSALTRALRAEFEKGR--EEQERRHQMELKALKQQLELERQAWEAgcARKEEAWLLNREQELREEIRKGRDK 893
Cdd:COG4942 167 AELEAERAELEALLAELEEERAalEALKAERQKLLARLEKELAELAAELAE--LQQEAEELEALIARLEAEAAAAAER 242
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
764-950 |
2.78e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 764 QERERARQRFQQHLEQEQWALQQQRQRLYSEVAEERERLGQQAARQRAELEELRQQLEESSSALT--RALRAEFEKGREE 841
Cdd:PHA02562 194 QQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNklNTAAAKIKSKIEQ 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 842 QERRHQM-----ELKALKQQLELERQAWEAGCARKEEAWL-LNREQELREEIRKGRDK--EIELVIHRLEADMALAK--- 910
Cdd:PHA02562 274 FQKVIKMyekggVCPTCTQQISEGPDRITKIKDKLKELQHsLEKLDTAIDELEEIMDEfnEQSKKLLELKNKISTNKqsl 353
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622882005 911 ---EESEKAAESRIKRLRDK---YEAELSELEQSERKLHERCSELK 950
Cdd:PHA02562 354 itlVDKAKKVKAAIEELQAEfvdNAEELAKLQDELDKIVKTKSELV 399
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
814-1073 |
3.80e-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: 44.58 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 814 EELRQQLEESS--SALTRALRAEFEKGREEQERRHQMELKALKQQLELERQAWEAgcarKEEAWLLNREQELREEirKGR 891
Cdd:pfam02463 152 PERRLEIEEEAagSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQA----KKALEYYQLKEKLELE--EEY 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 892 DKEIELVIHRLEADMALAKEESEKAAESRIKRLRDKYEAELSELEQSERKLHERC----SELKGQLGEAEGENLRLQGLV 967
Cdd:pfam02463 226 LLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEkklqEEELKLLAKEEEELKSELLKL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 968 RQKERALEDTQAVSGQMNEQLSSERSNLAQVI----------------RQEFEDRLAASEEETRQAKAELAALQARQQLE 1031
Cdd:pfam02463 306 ERRKVDDEEKLKESEKEKKKAEKELKKEKEEIeelekelkeleikreaEEEEEEELEKLQEKLEQLEEELLAKKKLESER 385
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1622882005 1032 LEEVHRRVKTALARKEEAVSSLRTQHEAAVKRADHLEELLEQ 1073
Cdd:pfam02463 386 LSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKE 427
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
920-1053 |
4.21e-04 |
|
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: 42.99 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 920 RIKRLRDKYEAELSELEQSERKLHERCSELKGQLGEAEGENLRLQGLVRQKERALEDTQAVSGQMN------------EQ 987
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeyealqkeiES 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622882005 988 LSSERSNLAQVIRQ------EFEDRLAASEEETRQAKAELAALQARQQLELEEVHRRVKTALARKEEAVSSL 1053
Cdd:COG1579 101 LKRRISDLEDEILElmerieELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
629-971 |
4.98e-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: 44.24 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 629 IDQLIEDKKVLSEKceavVAELKQEDQRCTERVAQVQaQHELEIKKLKelmsateKVRREKWISEKTKKIKEV--TVRGL 706
Cdd:TIGR04523 259 KDEQNKIKKQLSEK----QKELEQNNKKIKELEKQLN-QLKSEISDLN-------NQKEQDWNKELKSELKNQekKLEEI 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 707 EPEI---QKLIARHKQEVRRLKSlhEAELLQSDERASQRCLRQAEELREQLEREKEALGQQ------ERERARQRFQQHL 777
Cdd:TIGR04523 327 QNQIsqnNKIISQLNEQISQLKK--ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEiknlesQINDLESKIQNQE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 778 EQEQwALQQQRQRL---YSEVAEERERLGQQAARQRAELEELrqqlEESSSALTRALRaEFEKGREEQERrhqmELKALK 854
Cdd:TIGR04523 405 KLNQ-QKDEQIKKLqqeKELLEKEIERLKETIIKNNSEIKDL----TNQDSVKELIIK-NLDNTRESLET----QLKVLS 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 855 QQLELERQAWEAG---CARKE-EAWLLNREQELREEIRKGRDKEIELVIHRLEAdmaLAKEESEKaaESRIKRLRDK--- 927
Cdd:TIGR04523 475 RSINKIKQNLEQKqkeLKSKEkELKKLNEEKKELEEKVKDLTKKISSLKEKIEK---LESEKKEK--ESKISDLEDElnk 549
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1622882005 928 --YEAELSELEQSERKLHERCSELKGQLGEAEGENLRLQGLVRQKE 971
Cdd:TIGR04523 550 ddFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKE 595
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
893-979 |
5.07e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.30 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 893 KEIELVIHRLEADMALAKEESEKAAESRIKRLRDKY---EAELSELE---QSERKLHERCSELKGQLGEAEGENLRLQGL 966
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEASFERLAELRDELaelEEELEALKarwEAEKELIEEIQELKEELEQRYGKIPELEKE 493
|
90
....*....|...
gi 1622882005 967 VRQKERALEDTQA 979
Cdd:COG0542 494 LAELEEELAELAP 506
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
763-889 |
5.38e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 763 QQERERARQRFQQHLEQeQWALQQQRQRLYSEVAEERERLGQQAARQRAELEELRQQLEE-----------------SSS 825
Cdd:PRK04863 532 QQRAERLLAEFCKRLGK-NLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQlqariqrlaarapawlaAQD 610
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622882005 826 ALTRaLRAEFEkgrEEQERRHQMElKALKQQLELERQaweagcARKEEAWLLNREQELREEIRK 889
Cdd:PRK04863 611 ALAR-LREQSG---EEFEDSQDVT-EYMQQLLERERE------LTVERDELAARKQALDEEIER 663
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
783-896 |
6.64e-04 |
|
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: 43.59 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 783 ALQQQRQRLYSEVAEERERLGQQAARQRAEL----EELRQQLEESSSALTRALRAEFEKGREEQERRHQMELKAlkqqlE 858
Cdd:pfam09731 295 EIDQLSKKLAELKKREEKHIERALEKQKEELdklaEELSARLEEVRAADEAQLRLEFEREREEIRESYEEKLRT-----E 369
|
90 100 110
....*....|....*....|....*....|....*...
gi 1622882005 859 LERQAWEAGCARKEEawLLNREQELREEIRKGRDKEIE 896
Cdd:pfam09731 370 LERQAEAHEEHLKDV--LVEQEIELQREFLQDIKEKVE 405
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
676-867 |
6.87e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 6.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 676 KELMSATEKVRREKWISEKTKKIKEVTVRGLEPEIQKLIARHKQEVRRLkslheaELLQSDERASQRCLRQAEELREQLE 755
Cdd:COG4913 242 EALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRL------ELLEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 756 REKEALGQQERERARQRFQ------QHLEQEQWALQQ---QRQRLYSEVAEERERLGQQAARQRAELEELRQQLEESSSA 826
Cdd:COG4913 316 ARLDALREELDELEAQIRGnggdrlEQLEREIERLEReleERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA 395
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622882005 827 LTrALRAEFEKGREEQERRHQmELKALKQQLELERQAWEAG 867
Cdd:COG4913 396 LE-EELEALEEALAEAEAALR-DLRRELRELEAEIASLERR 434
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
760-1056 |
8.51e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.41 E-value: 8.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 760 ALGQQERERARQRFQQHlEQEQWALQQQRQRlYSEVAEERERLGQQAARQRAELEelrQQLEESSSALTRALRAEFEKGR 839
Cdd:COG5185 225 AKEIINIEEALKGFQDP-ESELEDLAQTSDK-LEKLVEQNTDLRLEKLGENAESS---KRLNENANNLIKQFENTKEKIA 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 840 EEQErrhqmELKALKQQLELERQAWEAGCARKEEAWLLNRE---QELREEIRKGRDKEielvihrLEADMALAKEESEKA 916
Cdd:COG5185 300 EYTK-----SIDIKKATESLEEQLAAAEAEQELEESKRETEtgiQNLTAEIEQGQESL-------TENLEAIKEEIENIV 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 917 AESRIKRLRDKYEAELSELEQSERKLHERCSELKGQLGEAegenlrLQGLVRQKERALEDTQavsgQMNEQLSSERSNLA 996
Cdd:COG5185 368 GEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEI------LATLEDTLKAADRQIE----ELQRQIEQATSSNE 437
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 997 QVIRQefedRLAASEEETRQAKAELAALQARQQLELEEVHRRVKTALARKEEAVSSLRTQ 1056
Cdd:COG5185 438 EVSKL----LNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESR 493
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
667-1053 |
1.02e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.50 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 667 QHELEIKKLKELMSATEKVRREKWISEKTKKIKEVTVRGLEPEIQKLIARHKQEVRRLKSLHEAE----LLQSDERASQR 742
Cdd:TIGR00606 204 EHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDneikALKSRKKQMEK 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 743 CLRQAEELREQLEREKE------------ALGQQERERAR-QRFQQHLEQEQWALQQQRQRLYSEVAE---ERERLGQQA 806
Cdd:TIGR00606 284 DNSELELKMEKVFQGTDeqlndlyhnhqrTVREKERELVDcQRELEKLNKERRLLNQEKTELLVEQGRlqlQADRHQEHI 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 807 ARQRAELEELRQQLE----ESSSALTRALRAEFEKGREEQERRHQMELKALKQQLELERQAWEAGCARKEEAWLLNREQE 882
Cdd:TIGR00606 364 RARDSLIQSLATRLEldgfERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIE 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 883 LREEIRKGRDKEIELVIHR-----------LEADMALAKEES-----EKAAESRIKRLRDKY-EAELSELEQSERKLHER 945
Cdd:TIGR00606 444 LKKEILEKKQEELKFVIKElqqlegssdriLELDQELRKAERelskaEKNSLTETLKKEVKSlQNEKADLDRKLRKLDQE 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 946 CSELkgqlgEAEGENL-RLQGLVRQKERALEDTQAVSGQMNEQLSSERSNLAQviRQEFEDRLAASEEETRQAKAELAAL 1024
Cdd:TIGR00606 524 MEQL-----NHHTTTRtQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPN--KKQLEDWLHSKSKEINQTRDRLAKL 596
|
410 420
....*....|....*....|....*....
gi 1622882005 1025 QARQQlELEEVHRRVKTALARKEEAVSSL 1053
Cdd:TIGR00606 597 NKELA-SLEQNKNHINNELESKEEQLSSY 624
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
559-865 |
1.21e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.79 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 559 ELGSEASTSVMRLKLEVEEKKQAMLLLQRALAQqrdltVRRVKETEKALSRQLQRQREHYEATIQRHLAFIDQLIEDKKV 638
Cdd:pfam05483 503 ELTQEASDMTLELKKHQEDIINCKKQEERMLKQ-----IENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARS 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 639 LSEKCEAVVAELKQEDQRCTERVAQVQAQHeleiKKLKELMSATEKVRREKWISEKTKKIKEVTVRGLEPEIQ------- 711
Cdd:pfam05483 578 IEYEVLKKEKQMKILENKCNNLKKQIENKN----KNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAsakqkfe 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 712 KLIARHKQEVRrLKSLHEAELLQSDERAsqrclrqaeelreqLEREKEALGQQERERARQrfqQHLEQEQWALQQQRQRL 791
Cdd:pfam05483 654 EIIDNYQKEIE-DKKISEEKLLEEVEKA--------------KAIADEAVKLQKEIDKRC---QHKIAEMVALMEKHKHQ 715
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622882005 792 YSEVAEERErlgqqaarqrAELEeLRQQLEESSSALTRALRAEFEKGREEqerrhqmeLKALKQQLELERQAWE 865
Cdd:pfam05483 716 YDKIIEERD----------SELG-LYKNKEQEQSSAKAALEIELSNIKAE--------LLSLKKQLEIEKEEKE 770
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
783-1035 |
1.27e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.89 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 783 ALQQQRQRlysevaEERERLgQQAARQRAELEELRQQLeessSALTRALRAEFEKGREEQERRHQMELKALK-----QQL 857
Cdd:pfam10174 454 RLKEQRER------EDRERL-EELESLKKENKDLKEKV----SALQPELTEKESSLIDLKEHASSLASSGLKkdsklKSL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 858 ELERQAWEAGCARKEEAwlLNREQELREEIRKGrdKEIELVIHRLEADMALAKEESEKaAESRIKRLRDKYEAELSELEQ 937
Cdd:pfam10174 523 EIAVEQKKEECSKLENQ--LKKAHNAEEAVRTN--PEINDRIRLLEQEVARYKEESGK-AQAEVERLLGILREVENEKND 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 938 SERKLH--ERCSELKGQLGEAEGENLRLQGLVRQKERALEDTQAVSGQMNEQLSSERSNLAQVI------RQEFED---R 1006
Cdd:pfam10174 598 KDKKIAelESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMgalektRQELDAtkaR 677
|
250 260
....*....|....*....|....*....
gi 1622882005 1007 LAASEEETRQAKAELAALQARQQLELEEV 1035
Cdd:pfam10174 678 LSSTQQSLAEKDGHLTNLRAERRKQLEEI 706
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
634-975 |
1.32e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.57 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 634 EDKKVLSEKCEAVVAELKQEDQRCTERVAQVQAQHELEIKKLKELMSATEKVRREKWISEKTKKIKEVTVRGLEPEIQKL 713
Cdd:pfam07888 62 ERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 714 IARhkqevrrlKSLHEAELLQSDERAsQRCLRQAEELREQLEREKEALGQQERE-RARQRFQQHLEQEQWALQQQRQRLY 792
Cdd:pfam07888 142 TQR--------VLERETELERMKERA-KKAGAQRKEEEAERKQLQAKLQQTEEElRSLSKEFQELRNSLAQRDTQVLQLQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 793 SEVAEERERLGqQAARQRAELEELRQQLE------ESSSALTRALRAEFEKGREEQERRHQMELKALKQQLELERQAWEA 866
Cdd:pfam07888 213 DTITTLTQKLT-TAHRKEAENEALLEELRslqerlNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 867 GCARKEEAWLLNREQE-LREEIRKGRDKEIELVIHRLEADMALAKEESEK-AAESRIKRLRDKYEAELSEleqSERKLHE 944
Cdd:pfam07888 292 SLALREGRARWAQEREtLQQSAEADKDRIEKLSAELQRLEERLQEERMEReKLEVELGREKDCNRVQLSE---SRRELQE 368
|
330 340 350
....*....|....*....|....*....|....
gi 1622882005 945 RCSELKGQLGEAEGENLRLQGL---VRQKERALE 975
Cdd:pfam07888 369 LKASLRVAQKEKEQLQAEKQELleyIRQLEQRLE 402
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
568-1002 |
1.40e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 568 VMRLKLEVEEKKQAMLLLQRALAQQRDLTVRRVKETEKALsRQLQRQREHYEATIQRHLAFIDQLiedKKVLSEKCEAVV 647
Cdd:PRK03918 354 LEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKEL-EELEKAKEEIEEEISKITARIGEL---KKEIKELKKAIE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 648 aELKQEDQRCTERVAQVQAQHELEIkkLKELMSATEKVRRE-KWISEKTKKIKEVTVrglepEIQKLIARHKqEVRRLKS 726
Cdd:PRK03918 430 -ELKKAKGKCPVCGRELTEEHRKEL--LEEYTAELKRIEKElKEIEEKERKLRKELR-----ELEKVLKKES-ELIKLKE 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 727 LHEaELLQSDERASQRCLRQAEELREQLEREKEAL----GQQERERARQRFQQHLEQEQWALQQQRQRLYSEVAEERERL 802
Cdd:PRK03918 501 LAE-QLKELEEKLKKYNLEELEKKAEEYEKLKEKLiklkGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEL 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 803 GQQAARQRAELEELRQQLEESSSALTRALRAEFEKGREEQerrhqmELKALKQQLELERQAWEAGCARKEEawLLNREQE 882
Cdd:PRK03918 580 EELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEK------ELKKLEEELDKAFEELAETEKRLEE--LRKELEE 651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 883 LREEIRKGRDKEIELVIHRLEADMALAKEESEKAAESR--IKRLRDKYEAELSELEQSERKLhERCSELKGQLGEAEGEN 960
Cdd:PRK03918 652 LEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRReeIKKTLEKLKEELEEREKAKKEL-EKLEKALERVEELREKV 730
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1622882005 961 LRLQGLVrqKERALEDTQAVSGQMNEQLSSERSNLAQVIRQE 1002
Cdd:PRK03918 731 KKYKALL--KERALSKVGEIASEIFEELTEGKYSGVRVKAEE 770
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
790-1078 |
1.49e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 790 RLYSEVAEERER-LGQQAARQRAELEELRQQLE--ESSSALTRALRAEFEKGREEQERRHQmELKALKQQLElERQAWEA 866
Cdd:PRK02224 191 QLKAQIEEKEEKdLHERLNGLESELAELDEEIEryEEQREQARETRDEADEVLEEHEERRE-ELETLEAEIE-DLRETIA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 867 GCARKEEawllnreqELREEIRKGRDKEIELvihRLEADMALAKEESEKAAESRIKRLRDKYEAELSELEqserklhERC 946
Cdd:PRK02224 269 ETERERE--------ELAEEVRDLRERLEEL---EEERDDLLAEAGLDDADAEAVEARREELEDRDEELR-------DRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 947 SELKGQLGEAEGENLRLQGLVRQKERALEDTQAVSGQMNEQLSSERSNLAqvirqEFEDRLAASEEETRQAKAELAALQA 1026
Cdd:PRK02224 331 EECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVE-----DRREEIEELEEEIEELRERFGDAPV 405
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1622882005 1027 RQQlELEEVHRRVKTALARKEEAVSSLRTQHEAAVKRADHLEELLEQHRRPT 1078
Cdd:PRK02224 406 DLG-NAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPE 456
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
763-1076 |
1.56e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 763 QQERERARQRFQQHLEQEqwalqqqrqrLYSEVAEERERLgqqaARQRAELEELRQQLE---ESSSALTRALRAEFEKGR 839
Cdd:pfam01576 37 QLCEEKNALQEQLQAETE----------LCAEAEEMRARL----AARKQELEEILHELEsrlEEEEERSQQLQNEKKKMQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 840 EE-QERRHQM-ELKALKQQLELERQAWEAGCARKEEAWL--------LNREQELREEI----------RKGRDKEIELVI 899
Cdd:pfam01576 103 QHiQDLEEQLdEEEAARQKLQLEKVTTEAKIKKLEEDILlledqnskLSKERKLLEERiseftsnlaeEEEKAKSLSKLK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 900 HRLEADMALAKEESEKAAESR--IKRLRDKYEAELSELEQSERKLHERCSELKGQLGEAEGENLRLQGLVRQK------- 970
Cdd:pfam01576 183 NKHEAMISDLEERLKKEEKGRqeLEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEEtaqknna 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 971 ERALEDTQAVSGQMNEQLSSERS--NLAQVIRQEFEDRLAASE---EETRQAKAELAALQARQQLELEEVHRRVKTALAR 1045
Cdd:pfam01576 263 LKKIRELEAQISELQEDLESERAarNKAEKQRRDLGEELEALKtelEDTLDTTAAQQELRSKREQEVTELKKALEEETRS 342
|
330 340 350
....*....|....*....|....*....|.
gi 1622882005 1046 KEEAVSSLRTQHEAAVkraDHLEELLEQHRR 1076
Cdd:pfam01576 343 HEAQLQEMRQKHTQAL---EELTEQLEQAKR 370
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
630-995 |
1.57e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 630 DQLIEDKKVLSEKCEAVVAELkqEDQRcTERVAQVQAQHELEIKkLKELMSATEKVRREKWISEKTKKIKEVTVRGLEPE 709
Cdd:pfam01576 738 EQGEEKRRQLVKQVRELEAEL--EDER-KQRAQAVAAKKKLELD-LKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRE 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 710 IQ-------KLIARHKQEVRRLKSLhEAELLQSDER--ASQRCLRQAeelreqlerekealgQQERERARQRFQQHLEQE 780
Cdd:pfam01576 814 LEearasrdEILAQSKESEKKLKNL-EAELLQLQEDlaASERARRQA---------------QQERDELADEIASGASGK 877
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 781 QwALQQQRQRLYSEVAEERERLGQQAARQRAELEELR---QQLEESSSALT--RALRAEFEKGREEQERRHQmELKALKQ 855
Cdd:pfam01576 878 S-ALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRkstLQVEQLTTELAaeRSTSQKSESARQQLERQNK-ELKAKLQ 955
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 856 QLELERQAWEAGCARKEEAWLLNREQELREEIRkgrdkeielvihrleadmalakeesEKAAESRIKRLRDKYEAELSEL 935
Cdd:pfam01576 956 EMEGTVKSKFKSSIAALEAKIAQLEEQLEQESR-------------------------ERQAANKLVRRTEKKLKEVLLQ 1010
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622882005 936 EQSER-----------KLHERCSELKGQLGEAEGENLRLQGLVRQKERALEDTQAVSGQMNEQLSSERSNL 995
Cdd:pfam01576 1011 VEDERrhadqykdqaeKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
709-1073 |
1.68e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.20 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 709 EIQKLIARHKQEVRRLKSLHEAELLQSDERASQRCLRQAEELREQLEREKEALGQQERERARQRFQQHLEQEQWALQQQR 788
Cdd:COG5278 94 ELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 789 QRLYSEVAEERERLGQQAARQRAELEELRQQLEESSSALTRALRAEFEKGREEQERRHQMELKALKQQLELERQAWEAGC 868
Cdd:COG5278 174 ALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLAL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 869 ARKEEAWLLNREQELREEIRKGRDKEIELVIHRLEADMALAKEESEKAAESRIKRLRDKYEAELSELEQSERKLHERCSE 948
Cdd:COG5278 254 LAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALAL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 949 LKGQLGEAEGENLRLQGLVRQKERALEDTQAVSGQMNEQLSSERSNLAQVIRQEFEDRLAASEEETRQAKAELAALQARQ 1028
Cdd:COG5278 334 ATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAA 413
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1622882005 1029 QLELEEVHRRVKTALARKEEAVSSLRTQHEAAVKRADHLEELLEQ 1073
Cdd:COG5278 414 AAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALAL 458
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
588-1029 |
1.78e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.63 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 588 ALAQQRDLTVRRVKETeKALSRQLQRQREHYEATIQRHLAFidqliedkkVLSEKCEAVVAELKQEDQRCTERVAQVQA- 666
Cdd:COG3096 789 ELRAERDELAEQYAKA-SFDVQKLQRLHQAFSQFVGGHLAV---------AFAPDPEAELAALRQRRSELERELAQHRAq 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 667 --QHELEIKKLKELMSAtekvrrekwisektkkikevtVRGLEPEIQKLIARHKQEvrRLKSLHE-AELLQSDERASQRC 743
Cdd:COG3096 859 eqQLRQQLDQLKEQLQL---------------------LNKLLPQANLLADETLAD--RLEELREeLDAAQEAQAFIQQH 915
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 744 LRQAEELREQLEREKEALGQQERerarqrFQQHLEQEQWALQQQRQRLY--SEVAEERERLGQQAArqraeleelrQQLE 821
Cdd:COG3096 916 GKALAQLEPLVAVLQSDPEQFEQ------LQADYLQAKEQQRRLKQQIFalSEVVQRRPHFSYEDA----------VGLL 979
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 822 ESSSALTRALRAEFEKGrEEQERRHQMELKALKQQLELERQAWEAGCARKEeawllNREQELREEIRkgrdkeielvihR 901
Cdd:COG3096 980 GENSDLNEKLRARLEQA-EEARREAREQLRQAQAQYSQYNQVLASLKSSRD-----AKQQTLQELEQ------------E 1041
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 902 LEADMALAKEESEKAAESRikrlRDKYEAELSELEQserklheRCSELKGQLGEAEGENLRLQGLVRQKERALedtqavs 981
Cdd:COG3096 1042 LEELGVQADAEAEERARIR----RDELHEELSQNRS-------RRSQLEKQLTRCEAEMDSLQKRLRKAERDY------- 1103
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1622882005 982 GQMNEQLSSERSNLAQVIRqefedRLAASEEETRQAKAELAALQARQQ 1029
Cdd:COG3096 1104 KQEREQVVQAKAGWCAVLR-----LARDNDVERRLHRRELAYLSADEL 1146
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
707-839 |
1.89e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.25 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 707 EPEIQKLIARH-KQEVRRLKslHEAELLQSDERASQRCLRQAEELREQLerekEALgQQERERARQRFQQHLEQeqwaLQ 785
Cdd:PRK11448 136 PPEDPENLLHAlQQEVLTLK--QQLELQAREKAQSQALAEAQQQELVAL----EGL-AAELEEKQQELEAQLEQ----LQ 204
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622882005 786 QQRQRLYSEVAEERERLGQQAArQRAEL--EELR----QQL-----EESSSALTRALRAEFEKGR 839
Cdd:PRK11448 205 EKAAETSQERKQKRKEITDQAA-KRLELseEETRilidQQLrkagwEADSKTLRFSKGARPEKGR 268
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
562-835 |
1.98e-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: 42.35 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 562 SEASTSVMRLKLEVEEKKQAMLLLQRA---LAQQRDLTVRRVKETEKALSRQLQrQREHYEATIQRHLAFIDQLIEDKKV 638
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKElteLEAEIEELEERLEEAEEELAEAEA-EIEELEAQIEQLKEELKALREALDE 807
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 639 LsekcEAVVAELKQEDQRCTERVAQVQAQHELEIKKLKELMSATEKVRREkwISEKTKKIKEVTVRGLEPEIQ---KLIA 715
Cdd:TIGR02168 808 L----RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED--IESLAAEIEELEELIEELESEleaLLNE 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 716 RHKQEVRRLKSLHEAELLQSDERASQRCLRQAEELREQLEREKEALgQQERERARQRFQQHLEQ--EQWAL--------- 784
Cdd:TIGR02168 882 RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL-ELRLEGLEVRIDNLQERlsEEYSLtleeaeale 960
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622882005 785 -------QQQRQRL--------------------YSEVAEERERLgqqaARQRAELEELRQQLEESSSALTRALRAEF 835
Cdd:TIGR02168 961 nkieddeEEARRRLkrlenkikelgpvnlaaieeYEELKERYDFL----TAQKEDLTEAKETLEEAIEEIDREARERF 1034
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
775-955 |
2.18e-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: 41.06 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 775 QHLEQEQWALQQQRQRLYSEVAE---ERERLGQQAARQRAELEELRQQLEESSSALtRALRAEFEKGREEQER-RHQMEL 850
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAEledELAALEARLEAAKTELEDLEKEIKRLELEI-EEVEARIKKYEEQLGNvRNNKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 851 KALKQQLElerqaweagcarkeeawLLNREQELREEIRKGRDKEIElvihRLEADMALAKEEsEKAAESRIKRLRDKYEA 930
Cdd:COG1579 92 EALQKEIE-----------------SLKRRISDLEDEILELMERIE----ELEEELAELEAE-LAELEAELEEKKAELDE 149
|
170 180
....*....|....*....|....*
gi 1622882005 931 ELSELEQSERKLHERCSELKGQLGE 955
Cdd:COG1579 150 ELAELEAELEELEAEREELAAKIPP 174
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
571-1034 |
2.21e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.02 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 571 LKLEVEEKKQAMlllQRALAQQRDL---------TVRRVKETEKALSRQLQRQREHYEATI---QRHLAFIDQLIEDKKV 638
Cdd:pfam05483 294 LTKELEDIKMSL---QRSMSTQKALeedlqiatkTICQLTEEKEAQMEELNKAKAAHSFVVtefEATTCSLEELLRTEQQ 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 639 LSEKCEAVVAELKQEDQRCT---ERVAQVQAQHELEIKKLKELMSATEKVRREKwisEKTKKIKEvTVRGLEPEIQKLIA 715
Cdd:pfam05483 371 RLEKNEDQLKIITMELQKKSselEEMTKFKNNKEVELEELKKILAEDEKLLDEK---KQFEKIAE-ELKGKEQELIFLLQ 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 716 RHKQEVrrlkslHEAEL-LQSDERASQRCLRQAEELREQLEREK----------EALGQQERERARQRFQQHLEQEqwal 784
Cdd:pfam05483 447 AREKEI------HDLEIqLTAIKTSEEHYLKEVEDLKTELEKEKlknieltahcDKLLLENKELTQEASDMTLELK---- 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 785 QQQRQRLYSEVAEER-----ERLGQQAARQRAELEELRQQLEESSSALTRALRAEFEKGR--EEQERRHQMELKALKQQL 857
Cdd:pfam05483 517 KHQEDIINCKKQEERmlkqiENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARsiEYEVLKKEKQMKILENKC 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 858 ELERQAWEAGCARKEEAWLLNREQELREEIRKGRDKEIELVIHRLEADMALAKEESEKaaesrikrLRDKYEAELSELEQ 937
Cdd:pfam05483 597 NNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEE--------IIDNYQKEIEDKKI 668
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 938 SERKLHERCSELKGQLGEA----EGENLRLQGLVRQKERALEDTQAVSGQMNEQLSSERSnLAQVIRQEFEDRLAASEEE 1013
Cdd:pfam05483 669 SEEKLLEEVEKAKAIADEAvklqKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELG-LYKNKEQEQSSAKAALEIE 747
|
490 500
....*....|....*....|.
gi 1622882005 1014 TRQAKAELAALQARQQLELEE 1034
Cdd:pfam05483 748 LSNIKAELLSLKKQLEIEKEE 768
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
806-912 |
2.34e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 806 AARQR-------AELEELRQQLEEsssaLTR---ALRAEFEKGREEQERRHQMELKALKQQLELERQAWEAGCARKEEAW 875
Cdd:COG0542 399 AARVRmeidskpEELDELERRLEQ----LEIekeALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQ 474
|
90 100 110
....*....|....*....|....*....|....*..
gi 1622882005 876 LLNREQELREEIRKGRDKEIELVIHRLEADMALAKEE 912
Cdd:COG0542 475 ELKEELEQRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
765-953 |
2.36e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 41.59 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 765 ERERARQRFQQhLEQEQWALQQQRQR---LYSEVAEERERLgqqaARQRAELEELRQQLEESSSALTRALRAEFEKGREE 841
Cdd:pfam15742 84 EWKHCQQKIRE-LELEVLKQAQSIKSqnsLQEKLAQEKSRV----ADAEEKILELQQKLEHAHKVCLTDTCILEKKQLEE 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 842 QERRHQMELKALKQQLELERQAweagcaRKeeawLLN-REQELREEIRKGRDKEIELVI------HRLEADMALAKE-ES 913
Cdd:pfam15742 159 RIKEASENEAKLKQQYQEEQQK------RK----LLDqNVNELQQQVRSLQDKEAQLEMtnsqqqLRIQQQEAQLKQlEN 228
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622882005 914 EKAAESRIKRLRDKYEAELSELEQSERKLHERCSELKGQL 953
Cdd:pfam15742 229 EKRKSDEHLKSNQELSEKLSSLQQEKEALQEELQQVLKQL 268
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
813-1075 |
3.54e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.03 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 813 LEELRQQLEESSSALTRALRAEFEKGREEQERRHQMEL----KALKQQLELERQAWEagcaRKEEAW------LLNREQE 882
Cdd:pfam07888 9 LEEESHGEEGGTDMLLVVPRAELLQNRLEECLQERAELlqaqEAANRQREKEKERYK----RDREQWerqrreLESRVAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 883 LREEIRKGRDKEIELVIHRLEADMALAKEESEKAA--------ESRIKRLRDKYEA---ELSELEQSERKLHERCSELKG 951
Cdd:pfam07888 85 LKEELRQSREKHEELEEKYKELSASSEELSEEKDAllaqraahEARIRELEEDIKTltqRVLERETELERMKERAKKAGA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 952 QLGEAEGENLRLQGlvrqkerALEDTQAVSGQMNEQLSSERSNLAQVIRQEFEDRLAASEEETRQAKAElaalqaRQQLE 1031
Cdd:pfam07888 165 QRKEEEAERKQLQA-------KLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH------RKEAE 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1622882005 1032 LEEVHRRVKTA---LARKEEAVSSLRTQHEAAVKRADHLEELLEQHR 1075
Cdd:pfam07888 232 NEALLEELRSLqerLNASERKVEGLGEELSSMAAQRDRTQAELHQAR 278
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
720-1032 |
3.79e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.60 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 720 EVRRLKSLHE-AELLQSDERAS--QRCLRQAEELREQLEREKEALgqqereRARQRFQQHL-------EQEQWALQQQRQ 789
Cdd:COG5022 737 EDMRDAKLDNiATRIQRAIRGRylRRRYLQALKRIKKIQVIQHGF------RLRRLVDYELkwrlfikLQPLLSLLGSRK 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 790 RLYSEVAE--------ERERLGQQAARQRAEL--EELRQQLEESSSALTRALR------AEFEKGREEQERRHQMELK-- 851
Cdd:COG5022 811 EYRSYLACiiklqktiKREKKLRETEEVEFSLkaEVLIQKFGRSLKAKKRFSLlkketiYLQSAQRVELAERQLQELKid 890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 852 -----ALKQQ-LELERQAWEAGCA-----RKEEAWLLNREQELrEEIRKGRDKEIELVIHRLEADmalaKEESEKAAESR 920
Cdd:COG5022 891 vksisSLKLVnLELESEIIELKKSlssdlIENLEFKTELIARL-KKLLNNIDLEEGPSIEYVKLP----ELNKLHEVESK 965
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 921 IKRLRDKYEAELSELEQSERKLHERCSELKG---QLGEAEGENLRLQ---GLVRQKERALEDTQAVSgqmnEQLSSERSN 994
Cdd:COG5022 966 LKETSEEYEDLLKKSTILVREGNKANSELKNfkkELAELSKQYGALQestKQLKELPVEVAELQSAS----KIISSESTE 1041
|
330 340 350
....*....|....*....|....*....|....*...
gi 1622882005 995 LAQviRQEFEDRLAASEEETRQAKAELAALQARQQLEL 1032
Cdd:COG5022 1042 LSI--LKPLQKLKGLLLLENNQLQARYKALKLRRENSL 1077
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
794-897 |
3.87e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 40.64 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 794 EVAEERERlGQQAARQRAELEELRQQLEESssaltralraefekgREEQERRHQMELKALKQQLELERQaweagCARKEE 873
Cdd:cd16269 199 EIEAERAK-AEAAEQERKLLEEQQRELEQK---------------LEDQERSYEEHLRQLKEKMEEERE-----NLLKEQ 257
|
90 100
....*....|....*....|....*
gi 1622882005 874 AWLL-NREQELREEIRKGRDKEIEL 897
Cdd:cd16269 258 ERALeSKLKEQEALLEEGFKEQAEL 282
|
|
| LXG |
pfam04740 |
LXG domain of WXG superfamily; This domain is present is the N-terminal region of a group of ... |
916-1073 |
4.13e-03 |
|
LXG domain of WXG superfamily; This domain is present is the N-terminal region of a group of polymorphic toxin proteins in bacteria. It is predicted to use Type VII secretion pathway to mediate export of bacterial toxins.
Pssm-ID: 428100 [Multi-domain] Cd Length: 202 Bit Score: 39.92 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 916 AAESRIKRLRDkYEAELSELEQSERKLHERCSELKGQLGEAEGENLR--LQGLVRQKERALEDTQAVSGQMNEQLSSERS 993
Cdd:pfam04740 11 GIDQTISELKE-LRDQLEKVKKAIEGLANLEDSLKGKGGEAIKNFYSelHLPFLDFLQDFIDEYIEFLEQIKAALESFEP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 994 NLAQVIRQEF-----EDRLAASEEETRQAKAELAA-------LQARQQLELEEVHRRVKTALARKEEAVSSLRT---QHE 1058
Cdd:pfam04740 90 SSNAFIDESFlehelENGLKKAKEKTEELTDEINSilasvsdIVSLPKLSDSEVQDSLQKAKKKVKDTIEKLYDfdqEQT 169
|
170
....*....|....*
gi 1622882005 1059 AAVKRADHLEELLEQ 1073
Cdd:pfam04740 170 SELSELEADLQALKT 184
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
763-927 |
4.26e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 763 QQERERARQRFQQHLEQEQWALQQQRQRLYSEVaeerERLGQQAARQRAELEELRQQLEESSSALTRALRAEFEKGREEQ 842
Cdd:COG2433 390 LPEEEPEAEREKEHEERELTEEEEEIRRLEEQV----ERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDR 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 843 E-RRHQMELKALKQQLELERQaweagcARKEEAWLLNREQELREEIRKGRD---KEIELV----IHRLEADMALAK---- 910
Cdd:COG2433 466 EiSRLDREIERLERELEEERE------RIEELKRKLERLKELWKLEHSGELvpvKVVEKFtkeaIRRLEEEYGLKEgdvv 539
|
170
....*....|....*....
gi 1622882005 911 --EESEKAAESRIKRLRDK 927
Cdd:COG2433 540 ylRDASGAGRSTAELLAEA 558
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
569-1073 |
4.84e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 569 MRLKLEVEEKKQAMLLLQRALAQQRDLTVRRVKETEKALSRQLQRQREHYEATIQRHLAFI-------DQLIEDKKVLSE 641
Cdd:pfam01576 80 LESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDIllledqnSKLSKERKLLEE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 642 KCEAVVAELKQEDQRcTERVAQVQAQHELEIKKLKELMSATEKVRREkwiSEKTKKIKEVTVRGLEPEI---QKLIARHK 718
Cdd:pfam01576 160 RISEFTSNLAEEEEK-AKSLSKLKNKHEAMISDLEERLKKEEKGRQE---LEKAKRKLEGESTDLQEQIaelQAQIAELR 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 719 QEVRRLKSLHEAELLQSDERASQRCL---------RQAEELREQLEREKEALGQQERERarqrfqQHLEQEQWALQqqrq 789
Cdd:pfam01576 236 AQLAKKEEELQAALARLEEETAQKNNalkkireleAQISELQEDLESERAARNKAEKQR------RDLGEELEALK---- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 790 rlysevAEERERLGQQAARQraeleELRQQLEESSSALTRALRAE---FEKGREEQERRHQMELKALKQQLELERQAweA 866
Cdd:pfam01576 306 ------TELEDTLDTTAAQQ-----ELRSKREQEVTELKKALEEEtrsHEAQLQEMRQKHTQALEELTEQLEQAKRN--K 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 867 GCARKEEAWLLNREQELREEIRKgrdkeielvihrleadMALAKEESE---KAAESRIKRLRDKY-EAELSELEQSER-- 940
Cdd:pfam01576 373 ANLEKAKQALESENAELQAELRT----------------LQQAKQDSEhkrKKLEGQLQELQARLsESERQRAELAEKls 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 941 KLHERCSELKGQLGEAEGENLRLQGLVRQKERALEDTQavsgqmnEQLSSE---RSNLAQVIRQEFEDRLAASE--EETR 1015
Cdd:pfam01576 437 KLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQ-------ELLQEEtrqKLNLSTRLRQLEDERNSLQEqlEEEE 509
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622882005 1016 QAKAELAALQARQQLELEEVHRRVktalarkEEAVSSLRTQHEAAVKRADHLEELLEQ 1073
Cdd:pfam01576 510 EAKRNVERQLSTLQAQLSDMKKKL-------EEDAGTLEALEEGKKRLQRELEALTQQ 560
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
784-998 |
5.64e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 784 LQQQRQRLYSEVAEERERLGQQAARQRAELEELRQQLEE--------SSSALTRALRAEFEKGREEQERRhQMELKALKQ 855
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvDLSEEAKLLLQQLSELESQLAEA-RAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 856 QLELERQAWEAGCARKEEAWLLNREQELREEIRKGRDKEIEL---------VIHRLEADMAlakeESEKAAESRIKRLRD 926
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELsarytpnhpDVIALRAQIA----ALRAQLQQEAQRILA 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622882005 927 KYEAELSELEQSERKLHERCSELKGQLGEAEGENLRLQGLVRQKERALEDTQAVSGQMNEQLSSERSNLAQV 998
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNV 388
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
707-862 |
5.83e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 39.12 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 707 EPEIQKLIARHKQEVRRLKSLheaellqsderasqrcLRQAeelreqlerekealgqQERERARQRFQQHLEQEQWALQQ 786
Cdd:pfam15619 55 ESELPQLIARHNEEVRVLRER----------------LRRL----------------QEKERDLERKLKEKEAELLRLRD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 787 QRQRLYSEVAE----ERERLGQQAARQRAELEE-------LRQQLEESSSALTRALRAEFEKGREEQE--RRHQMELKAL 853
Cdd:pfam15619 103 QLKRLEKLSEDknlaEREELQKKLEQLEAKLEDkdekiqdLERKLELENKSFRRQLAAEKKKHKEAQEevKILQEEIERL 182
|
170
....*....|
gi 1622882005 854 KQQL-ELERQ 862
Cdd:pfam15619 183 QQKLkEKERE 192
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
588-972 |
5.84e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 588 ALAQQRDLTVRRVkETEKALSRQLQRQREHYEATIQRHLAFidqliedkkVLSEKCEAVVAELKQEDQRCTERVAQVQA- 666
Cdd:PRK04863 790 QLRAEREELAERY-ATLSFDVQKLQRLHQAFSRFIGSHLAV---------AFEADPEAELRQLNRRRVELERALADHESq 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 667 --QHELEIKKLKELMSATEKVRREKWISEKTKKIKEVtvRGLEPEIQKL------IARHKQEVRRLKSLheAELLQSDer 738
Cdd:PRK04863 860 eqQQRSQLEQAKEGLSALNRLLPRLNLLADETLADRV--EEIREQLDEAeeakrfVQQHGNALAQLEPI--VSVLQSD-- 933
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 739 asqrclrqaeelreqlerekealgQQERERARQRFQQhlEQEQWALQQQRQRLYSEVAEERERLGQQAArqraeleelrQ 818
Cdd:PRK04863 934 ------------------------PEQFEQLKQDYQQ--AQQTQRDAKQQAFALTEVVQRRAHFSYEDA----------A 977
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 819 QLEESSSALTRALRAEFEKGREEQERrhqmelkaLKQQLeleRQAwEAGCARKEEawllnREQELREEIRKGRDKEIELv 898
Cdd:PRK04863 978 EMLAKNSDLNEKLRQRLEQAEQERTR--------AREQL---RQA-QAQLAQYNQ-----VLASLKSSYDAKRQMLQEL- 1039
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622882005 899 IHRLEADMALAKEESEKAAESRikrlRDKYEAELSELEQserklheRCSELKGQLGEAEGENLRLQGLVRQKER 972
Cdd:PRK04863 1040 KQELQDLGVPADSGAEERARAR----RDELHARLSANRS-------RRNQLEKQLTFCEAEMDNLTKKLRKLER 1102
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
720-875 |
6.23e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 40.24 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 720 EVRRLKSLHEAELLQSDERASQRCLRQAEELREQLEREKEALGQQERERARQRFQQHLEQEQWALQQQRQRLYSEVAEER 799
Cdd:COG2268 196 EIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANA 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 800 ERLGQQ----AARQRA-ELEELRQQLEESSSALTRALRAEFEKGREEQERRhqMELKALKQQLELERQAWEAgcarKEEA 874
Cdd:COG2268 276 EREVQRqleiAEREREiELQEKEAEREEAELEADVRKPAEAEKQAAEAEAE--AEAEAIRAKGLAEAEGKRA----LAEA 349
|
.
gi 1622882005 875 W 875
Cdd:COG2268 350 W 350
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
763-975 |
6.24e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 40.21 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 763 QQERERARQRFQQHLEQEQWALQQQRQRLYSEVAEERERlgQQAARQRAELEELRQQLEEsssaltRALRAEFEKGREEQ 842
Cdd:TIGR02794 66 EQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAA--KQAEQAAKQAEEKQKQAEE------AKAKQAAEAKAKAE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 843 ERRHQMELKALKQQLELERQAWEAGCARKeeawllnrEQELREEIRKGRDKEIELVIHRLEADMALAKeeSEKAAESRIK 922
Cdd:TIGR02794 138 AEAERKAKEEAAKQAEEEAKAKAAAEAKK--------KAEEAKKKAEAEAKAKAEAEAKAKAEEAKAK--AEAAKAKAAA 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622882005 923 RLRDKYEAELSELEQSERKLHERCSELKGQLGEAEGENLRLQGLVRQKERALE 975
Cdd:TIGR02794 208 EAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
570-1048 |
6.74e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 570 RLKLEVEEKKQAMLLLQRALAQQRDLTVRRVKETEKALSrQLQRQREHYEATIQRHLAFIDQLIEDKKVLSEKCEAVVAE 649
Cdd:pfam01576 482 RQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLS-TLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 650 LKQEDQ------RCTERVAQVQAQHELEIKKLKELMSATEKvrREKWISEKTKKIKEVTVRGLEPEIQKLIARHKQEVRR 723
Cdd:pfam01576 561 LEEKAAaydkleKTKNRLQQELDDLLVDLDHQRQLVSNLEK--KQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRA 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 724 LKSLHEAELLQSDERASQRCLRQAEELREQLEREKEALGQ--QERERARQRFQQHLEQEQWALQQQRQRLY-SEVAEERE 800
Cdd:pfam01576 639 LSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKnvHELERSKRALEQQVEEMKTQLEELEDELQaTEDAKLRL 718
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 801 RLGQQAARQRAE--LEELRQQLEESSSALTRALRaEFEKGREEqERRHQMELKALKQQLELERQAWEAGCA--------- 869
Cdd:pfam01576 719 EVNMQALKAQFErdLQARDEQGEEKRRQLVKQVR-ELEAELED-ERKQRAQAVAAKKKLELDLKELEAQIDaankgreea 796
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 870 ----RKEEAWLLNREQELrEEIRKGRD------KEIELVIHRLEADMALAKEEseKAAESRIKRL----RDKYEAELSEL 935
Cdd:pfam01576 797 vkqlKKLQAQMKDLQREL-EEARASRDeilaqsKESEKKLKNLEAELLQLQED--LAASERARRQaqqeRDELADEIASG 873
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 936 EQSERKLHERCSELKGQLGEAEGENLRLQGLVRQKERALEDTQAVSGQMNEQLSSERSNLA-------QVIRQEFEDRLA 1008
Cdd:pfam01576 874 ASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQksesarqQLERQNKELKAK 953
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1622882005 1009 ASEEETR---QAKAELAALQAR-----QQLELEEVHRRVKTALARKEE 1048
Cdd:pfam01576 954 LQEMEGTvksKFKSSIAALEAKiaqleEQLEQESRERQAANKLVRRTE 1001
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
783-896 |
8.54e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 38.07 E-value: 8.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 783 ALQQQRQRlyseVAEERERLGQQAARQRAELEELR---QQLEESSSALTRALRAEfekgrEEQERRHQMELKALKQQLEL 859
Cdd:pfam11559 42 ELLQQRDR----DLEFRESLNETIRTLEAEIERLQskiERLKTQLEDLERELALL-----QAKERQLEKKLKTLEQKLKN 112
|
90 100 110
....*....|....*....|....*....|....*..
gi 1622882005 860 ERQAweagcARKEEAWLLNREQELREEIRKgRDKEIE 896
Cdd:pfam11559 113 EKEE-----LQRLKNALQQIKTQFAHEVKK-RDREIE 143
|
|
| DDRGK |
pfam09756 |
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ... |
769-873 |
9.54e-03 |
|
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.
Pssm-ID: 370664 [Multi-domain] Cd Length: 188 Bit Score: 38.48 E-value: 9.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882005 769 ARQRFQQHLEQEQWALQQQRQRLYsevaEERERLGQQAARQRAELEELRQQLEEsssaltrALRAEFEKGREEQERRHQM 848
Cdd:pfam09756 5 AKKRAKLELKEAKRQQREAEEEER----EEREKLEEKREEEYKEREEREEEAEK-------EKEEEERKQEEEQERKEQE 73
|
90 100
....*....|....*....|....*
gi 1622882005 849 ELKALKQQLELERQAWEAGCARKEE 873
Cdd:pfam09756 74 EYEKLKSQFVVEEEGTDKLSAEDES 98
|
|
| |
