NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|499171829|ref|WP_010869416|]
View 

chromosome segregation protein SMC [Mycoplasmoides genitalium]

Protein Classification

chromosome segregation protein SMC( domain architecture ID 11493846)

chromosome segregation protein SMC is required for chromosome condensation and partitioning

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3-969 0e+00

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: 884.01  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829     3 FLKRFRAYGFKSYADEITIDFTHSMTGIVGPNGSGKSNVVDALKWVLGERSMKHLRSKSGDDMIFFGSKDKPASKLAEIE 82
Cdd:TIGR02168    1 RLKKLELAGFKSFADPTTINFDKGITGIVGPNGCGKSNIVDAIRWVLGEQSAKALRGGKMEDVIFNGSETRKPLSLAEVE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829    83 LTFDNSNRLLH-DSRKEISVMRRVYRgSGQSEYFINSNPATLKEISGIFADIGLEKGSLGIISQGSVSWFVEAKPEERRK 161
Cdd:TIGR02168   81 LVFDNSDGLLPgADYSEISITRRLYR-DGESEYFINGQPCRLKDIQDLFLDTGLGKRSYSIIEQGKISEIIEAKPEERRA 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   162 IFEDASGIGRYTKRKEEVVNQLNRTLINLKQVSVVLNELKKDLKKLTLQAEKAQQFIRVKNELKELELAVLVGEYLQAQT 241
Cdd:TIGR02168  160 IFEEAAGISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELRE 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   242 ELDKFNFQINSSEHDFKIHEPQLELLEEQIVIFNSRFHSADMQSNELQKELQDIYQKINELEQRKVIIDV---------- 311
Cdd:TIGR02168  240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRErlanlerqle 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   312 ----QLRQGFSQKDEKQK-AAALKKLILVDQTQLDGFENQLS-------NSKTTITDLEKLINEQKSLVDQIKLQIEKNT 379
Cdd:TIGR02168  320 eleaQLEELESKLDELAEeLAELEEKLEELKEELESLEAELEeleaeleELESRLEELEEQLETLRSKVAQLELQIASLN 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   380 ADLIYQRSLKTIIE------------------------------------------------------------------ 393
Cdd:TIGR02168  400 NEIERLEARLERLEdrrerlqqeieellkkleeaelkelqaeleeleeeleelqeelerleealeelreeleeaeqalda 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   394 -----------------LQTNELKKTNNANILVKNANALTGILNTLGTFLKFDKQYEKAILKALGKSIGYLVVNNNNAAI 456
Cdd:TIGR02168  480 aerelaqlqarldslerLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVVENLNAAK 559
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   457 QAIDFLVKNEIGKVTFLPLDDVaSDTKITNEHMEILKQLDGFLGVCSDHVKCDPLFQPVVNTLLAQVIIAKDLNSAINLS 536
Cdd:TIGR02168  560 KAIAFLKQNELGRVTFLPLDSI-KGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELA 638
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   537 NYTYKLYRIVTLDGETVYAGGIINGGFEKTNLSDGYLSSASLDNEQNINKLENNERELKKELTELEVKLDEMN------- 609
Cdd:TIGR02168  639 KKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEeeleqlr 718
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   610 ---------------------------------------------------------------RKLKYEELLQAKFIERI 626
Cdd:TIGR02168  719 keleelsrqisalrkdlarleaeveqleeriaqlskelteleaeieeleerleeaeeelaeaeAEIEELEAQIEQLKEEL 798
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   627 VQIKKIILELKMEYEQL-----------------------TNTTFDGKKAVASE--AELIHSLNSAWAKRDEINSKLKLN 681
Cdd:TIGR02168  799 KALREALDELRAELTLLneeaanlrerleslerriaaterRLEDLEEQIEELSEdiESLAAEIEELEELIEELESELEAL 878
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   682 QELKLQ--------------LAKTIKQSEEKIVDLRALLDEQRAKLVSAREGKIRFENTIQNITEKINSVYKMTMEFAIA 747
Cdd:TIGR02168  879 LNERASleealallrseleeLSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEA 958
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   748 NHNKpVKLSSMQAHNKIAKLQNQLNEMGVINMESIAEISEKQKRFDDINAEYESAQQAVENLQKAITEIDEIASNEFDQL 827
Cdd:TIGR02168  959 LENK-IEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDT 1037
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   828 IQKLNQELPKTFKYLFGGGSCQIRYTDPSNVLVSGIDVFANPPGKNIANLMLLSGGEKTLVALSVLFSILKVSAFPLVIL 907
Cdd:TIGR02168 1038 FDQVNENFQRVFPKLFGGGEAELRLTDPEDLLEAGIEIFAQPPGKKNQNLSLLSGGEKALTALALLFAIFKVKPAPFCIL 1117
                         1130      1140      1150      1160      1170      1180
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499171829   908 DEAESALDPANVERFANIIKTASKNTQFLIITHRQGTMMKCDMLLGAAMQTKGVTKTFAVEL 969
Cdd:TIGR02168 1118 DEVDAPLDDANVERFANLLKEFSKNTQFIVITHNKGTMEVADQLYGVTMQEKGVSKIVSVDL 1179
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3-969 0e+00

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: 884.01  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829     3 FLKRFRAYGFKSYADEITIDFTHSMTGIVGPNGSGKSNVVDALKWVLGERSMKHLRSKSGDDMIFFGSKDKPASKLAEIE 82
Cdd:TIGR02168    1 RLKKLELAGFKSFADPTTINFDKGITGIVGPNGCGKSNIVDAIRWVLGEQSAKALRGGKMEDVIFNGSETRKPLSLAEVE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829    83 LTFDNSNRLLH-DSRKEISVMRRVYRgSGQSEYFINSNPATLKEISGIFADIGLEKGSLGIISQGSVSWFVEAKPEERRK 161
Cdd:TIGR02168   81 LVFDNSDGLLPgADYSEISITRRLYR-DGESEYFINGQPCRLKDIQDLFLDTGLGKRSYSIIEQGKISEIIEAKPEERRA 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   162 IFEDASGIGRYTKRKEEVVNQLNRTLINLKQVSVVLNELKKDLKKLTLQAEKAQQFIRVKNELKELELAVLVGEYLQAQT 241
Cdd:TIGR02168  160 IFEEAAGISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELRE 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   242 ELDKFNFQINSSEHDFKIHEPQLELLEEQIVIFNSRFHSADMQSNELQKELQDIYQKINELEQRKVIIDV---------- 311
Cdd:TIGR02168  240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRErlanlerqle 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   312 ----QLRQGFSQKDEKQK-AAALKKLILVDQTQLDGFENQLS-------NSKTTITDLEKLINEQKSLVDQIKLQIEKNT 379
Cdd:TIGR02168  320 eleaQLEELESKLDELAEeLAELEEKLEELKEELESLEAELEeleaeleELESRLEELEEQLETLRSKVAQLELQIASLN 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   380 ADLIYQRSLKTIIE------------------------------------------------------------------ 393
Cdd:TIGR02168  400 NEIERLEARLERLEdrrerlqqeieellkkleeaelkelqaeleeleeeleelqeelerleealeelreeleeaeqalda 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   394 -----------------LQTNELKKTNNANILVKNANALTGILNTLGTFLKFDKQYEKAILKALGKSIGYLVVNNNNAAI 456
Cdd:TIGR02168  480 aerelaqlqarldslerLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVVENLNAAK 559
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   457 QAIDFLVKNEIGKVTFLPLDDVaSDTKITNEHMEILKQLDGFLGVCSDHVKCDPLFQPVVNTLLAQVIIAKDLNSAINLS 536
Cdd:TIGR02168  560 KAIAFLKQNELGRVTFLPLDSI-KGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELA 638
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   537 NYTYKLYRIVTLDGETVYAGGIINGGFEKTNLSDGYLSSASLDNEQNINKLENNERELKKELTELEVKLDEMN------- 609
Cdd:TIGR02168  639 KKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEeeleqlr 718
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   610 ---------------------------------------------------------------RKLKYEELLQAKFIERI 626
Cdd:TIGR02168  719 keleelsrqisalrkdlarleaeveqleeriaqlskelteleaeieeleerleeaeeelaeaeAEIEELEAQIEQLKEEL 798
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   627 VQIKKIILELKMEYEQL-----------------------TNTTFDGKKAVASE--AELIHSLNSAWAKRDEINSKLKLN 681
Cdd:TIGR02168  799 KALREALDELRAELTLLneeaanlrerleslerriaaterRLEDLEEQIEELSEdiESLAAEIEELEELIEELESELEAL 878
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   682 QELKLQ--------------LAKTIKQSEEKIVDLRALLDEQRAKLVSAREGKIRFENTIQNITEKINSVYKMTMEFAIA 747
Cdd:TIGR02168  879 LNERASleealallrseleeLSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEA 958
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   748 NHNKpVKLSSMQAHNKIAKLQNQLNEMGVINMESIAEISEKQKRFDDINAEYESAQQAVENLQKAITEIDEIASNEFDQL 827
Cdd:TIGR02168  959 LENK-IEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDT 1037
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   828 IQKLNQELPKTFKYLFGGGSCQIRYTDPSNVLVSGIDVFANPPGKNIANLMLLSGGEKTLVALSVLFSILKVSAFPLVIL 907
Cdd:TIGR02168 1038 FDQVNENFQRVFPKLFGGGEAELRLTDPEDLLEAGIEIFAQPPGKKNQNLSLLSGGEKALTALALLFAIFKVKPAPFCIL 1117
                         1130      1140      1150      1160      1170      1180
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499171829   908 DEAESALDPANVERFANIIKTASKNTQFLIITHRQGTMMKCDMLLGAAMQTKGVTKTFAVEL 969
Cdd:TIGR02168 1118 DEVDAPLDDANVERFANLLKEFSKNTQFIVITHNKGTMEVADQLYGVTMQEKGVSKIVSVDL 1179
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2-978 3.10e-151

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 473.27  E-value: 3.10e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   2 VFLKRFRAYGFKSYADEITIDFTHSMTGIVGPNGSGKSNVVDALKWVLGERSMKHLRSKSGDDMIFFGSKDKPASKLAEI 81
Cdd:COG1196    1 MRLKRLELAGFKSFADPTTIPFEPGITAIVGPNGSGKSNIVDAIRWVLGEQSAKSLRGGKMEDVIFAGSSSRKPLGRAEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  82 ELTFDNSNRLLHDSRKEISVMRRVYRgSGQSEYFINSNPATLKEISGIFADIGLEKGSLGIISQGSVSWFVEAKPEERRK 161
Cdd:COG1196   81 SLTFDNSDGTLPIDYDEVTITRRLYR-SGESEYYINGKPCRLKDIQDLFLDTGLGPESYSIIGQGMIDRIIEAKPEERRA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 162 IFEDASGIGRYTKRKEEVVNQLNRTLINLKQVSVVLNELKKDLKKLTLQAEKAQQFIRVKNELKELELAVLVGEYLQAQT 241
Cdd:COG1196  160 IIEEAAGISKYKERKEEAERKLEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 242 ELDKFNFQINSSEHDFKIHEPQLELLEEQIVIFNSRFHSADMQSNELQKELQDIYQKINELEQRkvIIDVQLRQGFSQKD 321
Cdd:COG1196  240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD--IARLEERRRELEER 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 322 EKQKAAALKKL-----------------------------------------------------------ILVDQTQLDG 342
Cdd:COG1196  318 LEELEEELAELeeeleeleeeleeleeeleeaeeeleeaeaelaeaeealleaeaelaeaeeeleelaeeLLEALRAAAE 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 343 FENQLSNSKTTITDLEKLINEQKSLVDQIKLQIEKNTADLIYQRSLKTIIELQTNELKKTNNANIL-------------- 408
Cdd:COG1196  398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEllaelleeaallea 477
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 409 -----------------------------------VKNANALTGILNTLGTFLKFDKQYEKAILKALGKSIGYLVVNNNN 453
Cdd:COG1196  478 alaelleelaeaaarllllleaeadyegflegvkaALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDE 557
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 454 AAIQAIDFLVKNEIGKVTFLPLdDVASDTKITNEHMEILKQLDGFLGVCSDHVKCDPLFQPVVNTLLAQVIIAKDLNSAI 533
Cdd:COG1196  558 VAAAAIEYLKAAKAGRATFLPL-DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 534 NLSNYTYKLYRIVTLDGETVYAGGIINGGFEKTNLsdgylsSASLDNEQNINKLENNERELKKELTELEVKLDEMNRKLK 613
Cdd:COG1196  637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL------AALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 614 YEELLQAkfierivqikkiilelkmeyeqltnttfdgkkavaseaelihslnsawakRDEINSKLKLNQELKLQLAKTIK 693
Cdd:COG1196  711 EAEEERL--------------------------------------------------EEELEEEALEEQLEAEREELLEE 740
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 694 QSEEKIVDLRALLDEqraklvsaregkirfentiqnitekinsvykmtmefaianhnKPVKLSSMQAHNKIAKLQNQLNE 773
Cdd:COG1196  741 LLEEEELLEEEALEE------------------------------------------LPEPPDLEELERELERLEREIEA 778
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 774 MGVINMESIAEISEKQKRFDDINAEYESAQQAVENLQKAITEIDEIASNEFDQLIQKLNQELPKTFKYLFGGGSCQIRYT 853
Cdd:COG1196  779 LGPVNLLAIEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRERFLETFDAVNENFQELFPRLFGGGEAELLLT 858
                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 854 DPSNVLVSGIDVFANPPGKNIANLMLLSGGEKTLVALSVLFSILKVSAFPLVILDEAESALDPANVERFANIIKTASKNT 933
Cdd:COG1196  859 DPDDPLETGIEIMAQPPGKKLQRLSLLSGGEKALTALALLFAIFRLNPSPFCVLDEVDAPLDDANVERFAELLKEMSEDT 938
                       1050      1060      1070      1080
                 ....*....|....*....|....*....|....*....|....*
gi 499171829 934 QFLIITHRQGTMMKCDMLLGAAMQTKGVTKTFAVELENAEKYVSE 978
Cdd:COG1196  939 QFIVITHNKRTMEAADRLYGVTMQEPGVSRVVSVDLEEAEELAEA 983
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
3-963 2.93e-110

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: 368.14  E-value: 2.93e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829     3 FLKRFRAYGFKSYADEITIDFTHSMTGIVGPNGSGKSNVVDALKWVLGERSMKHLRSKSGDDMIFfgSKDKPASKLAEIE 82
Cdd:pfam02463    1 YLKRIEIEGFKSYAKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIH--SKSGAFVNSAEVE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829    83 LTFDNSNRLLHDSRKEISVMRRVYRGsGQSEYFINSNPATLKEISGIFADIGLEKGSLGIISQGSVSWFVEAKPEERRKI 162
Cdd:pfam02463   79 ITFDNEDHELPIDKEEVSIRRRVYRG-GDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLE 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   163 FEDASGIGRYTKRKEEVVNQLNRTLINLKQVSVVLNELKKDLKKLTLQAEKAQQFIRVKNELKELELAVLVGEYLQAQTE 242
Cdd:pfam02463  158 IEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEE 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   243 LDKFNFQINSSEHDFKIHEPQLELLEEQIVIFNSRFHSADMQSNELQKELQDIYQKINELEQRKVIIDVQL------RQG 316
Cdd:pfam02463  238 RIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRkvddeeKLK 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   317 FSQKDEKQKAAALKKLILV------------------------------------------------------------- 335
Cdd:pfam02463  318 ESEKEKKKAEKELKKEKEEieelekelkeleikreaeeeeeeeleklqekleqleeellakkkleserlssaaklkeeel 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   336 ---------DQTQLDGFENQLSNSKTTITDLEKLINEQKSLVDQIKLQIEKNTADLIYQRSLKTI----IELQTNELKKT 402
Cdd:pfam02463  398 elkseeekeAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKdeleLKKSEDLLKET 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   403 NNANILVKNANALTGILNTLGTFLKFDKQYEKAILKALGKS---------------IGYLVVNNNNAAIQAIDFLV---- 463
Cdd:pfam02463  478 QLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDgvggriisahgrlgdLGVAVENYKVAISTAVIVEVsata 557
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   464 ---------------------------------KNEIGKVTFLPLDDVASDTKITNEHMEILKQLDGFLGVCSDHVKCDP 510
Cdd:pfam02463  558 deveerqklvraltelplgarklrllipklklpLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKL 637
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   511 L-----------------------------------------------------------------------FQPVVNTL 519
Cdd:pfam02463  638 KesakakesglrkgvsleeglaeksevkaslseltkelleiqelqekaeselakeeilrrqleikkkeqrekEELKKLKL 717
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   520 LAQVIIAKDLNSAINLSNYTYKLYRIVTLDGETVYAGGIINGGFEKTNLSDGYLSSASLDNEQNINKLENNERELKKELT 599
Cdd:pfam02463  718 EAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLK 797
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   600 ELEVKLDEMNRKLKYEELLQAKFIERIVQIKKIILELKMEYEQLTNTTFDGKKAVASEAELIHSLNSAWAKRDEINSKLK 679
Cdd:pfam02463  798 AQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEE 877
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   680 LNQELKLQLAKTIKQSEEKIVDLRALLDEQRAKLVSAREGKIRFENTIQNITEKINSVYKMTMEFAIANHNKPVKLSSMQ 759
Cdd:pfam02463  878 ELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEE 957
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   760 AHNKIAKLQNQLNEMGVINMESIAEISEKQKRFDDINAEYESAQQAVENLQKAITEIDEIASNEFDQLIQKLNQELPKTF 839
Cdd:pfam02463  958 EEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVF 1037
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   840 KYLFGGGSCQIRYTDPSNVLVSGIDVFANPPGKNIANLMLLSGGEKTLVALSVLFSILKVSAFPLVILDEAESALDPANV 919
Cdd:pfam02463 1038 FYLELGGSAELRLEDPDDPFSGGIEISARPPGKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNV 1117
                         1130      1140      1150      1160
                   ....*....|....*....|....*....|....*....|....
gi 499171829   920 ERFANIIKTASKNTQFLIITHRQGTMMKCDMLLGAAMQTKGVTK 963
Cdd:pfam02463 1118 SRVANLLKELSKNAQFIVISLREEMLEKADKLVGVTMVENGVST 1161
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
863-963 4.41e-45

ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213245 [Multi-domain]  Cd Length: 197  Bit Score: 161.09  E-value: 4.41e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 863 IDVFANPPGKNIANLMLLSGGEKTLVALSVLFSILKVSAFPLVILDEAESALDPANVERFANIIKTASKNTQFLIITHRQ 942
Cdd:cd03278   97 VSEIIEAPGKKVQRLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRK 176
                         90       100
                 ....*....|....*....|.
gi 499171829 943 GTMMKCDMLLGAAMQTKGVTK 963
Cdd:cd03278  177 GTMEAADRLYGVTMQESGVSK 197
SMC_hinge smart00968
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ...
417-535 9.59e-31

SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.


Pssm-ID: 214944 [Multi-domain]  Cd Length: 120  Bit Score: 117.33  E-value: 9.59e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   417 GILNTLGTFLKFDKQYEKAILKALGKSIGYLVVNNNNAAIQAIDFLVKNEIGKVTFLPLDDVASDTKITNEHMEILKQLD 496
Cdd:smart00968   2 GVLGRVADLISVDPKYETALEAALGGRLQAVVVDTEETAKKAIEFLKKNRLGRATFLPLDKIKPRSPAGSKLREALLPEP 81
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 499171829   497 GFLGVCSDHVKCDPLFQPVVNTLLAQVIIAKDLNSAINL 535
Cdd:smart00968  82 GFVGPAIDLVEYDPELRPALEYLLGNTLVVDDLETARRL 120
PRK01156 PRK01156
chromosome segregation protein; Provisional
4-940 2.99e-09

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 61.07  E-value: 2.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   4 LKRFRAYGFKSYADEiTIDFTHSMTGIVGPNGSGKSNVVDALKWVLgersMKHLRSKSGDDMIffgskdKPASKLAEIEL 83
Cdd:PRK01156   3 IKRIRLKNFLSHDDS-EIEFDTGINIITGKNGAGKSSIVDAIRFAL----FTDKRTEKIEDMI------KKGKNNLEVEL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  84 TFDNS----------NRLLHDSRKEISVMRrvyRGSGQSEYFINSNPATLKEISGIFADIGLEKGSLGiisQGSVSWFVE 153
Cdd:PRK01156  72 EFRIGghvyqirrsiERRGKGSRREAYIKK---DGSIIAEGFDDTTKYIEKNILGISKDVFLNSIFVG---QGEMDSLIS 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 154 AKPEERRKIFEDASGIGR----YTKRKeEVVNQLNRTLINLKQVSVVLNELKKDLKKLTLQAEKAQQfirvKNELKELEL 229
Cdd:PRK01156 146 GDPAQRKKILDEILEINSlernYDKLK-DVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEK----SHSITLKEI 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 230 AVLVGEYLQAQTELDkfnfQINSSEHDFKIHEPQLELLEEQIVIFNSRFHSADMQSNelqkELQDIYQKINELEQRKVii 309
Cdd:PRK01156 221 ERLSIEYNNAMDDYN----NLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNN----YYKELEERHMKIINDPV-- 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 310 dvqlrqgFSQKDEKQKAAALKKLILVDQTQLDGFENQLSNSKTTITDLEKLineQKSLVDQIKLQIEKNTADliyqrslK 389
Cdd:PRK01156 291 -------YKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVL---QKDYNDYIKKKSRYDDLN-------N 353
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 390 TIIELQTNELKktnnanilvknanaLTGILNTLGTFLKFDKQYEKAIlKALGKSIGYLVvnnnnaAIQAIDFLVKNEIGK 469
Cdd:PRK01156 354 QILELEGYEMD--------------YNSYLKSIESLKKKIEEYSKNI-ERMSAFISEIL------KIQEIDPDAIKKELN 412
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 470 VTFLPLDDVASDTKITNEHMEILKQ----LDGFLGVCSDHVKCdplfqPVVNTLLAQVIIAKDLNsainlsNYTYKLYRI 545
Cdd:PRK01156 413 EINVKLQDISSKVSSLNQRIRALREnldeLSRNMEMLNGQSVC-----PVCGTTLGEEKSNHIIN------HYNEKKSRL 481
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 546 VTLDGETVYAGGIINGGFEKTNLSDGYLssasldNEQNINKLENNERELKKELTELEVKLDEMNRkLKYEELLQAKFIER 625
Cdd:PRK01156 482 EEKIREIEIEVKDIDEKIVDLKKRKEYL------ESEEINKSINEYNKIESARADLEDIKIKINE-LKDKHDKYEEIKNR 554
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 626 IVQIKKIILELKmeyeqltNTTFDGKKAVASEAElIHSLNSawaKRDEINSKLK----LNQELKLQLAKTIKQSEEKIVD 701
Cdd:PRK01156 555 YKSLKLEDLDSK-------RTSWLNALAVISLID-IETNRS---RSNEIKKQLNdlesRLQEIEIGFPDDKSYIDKSIRE 623
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 702 LRALLDEQRAKLVSAREGKIRfentIQNITEKINSVYKMTMEF-AIANHNKPVKLSSMQAHNKIAKLQNQLNEMGV--IN 778
Cdd:PRK01156 624 IENEANNLNNKYNEIQENKIL----IEKLRGKIDNYKKQIAEIdSIIPDLKEITSRINDIEDNLKKSRKALDDAKAnrAR 699
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 779 MESIAEI-----SEKQKRFDDINAEYESaqqaVENLQKAITEIDEIaSNEFDQ-----LIQKLNQEL--PKTFKYLFggg 846
Cdd:PRK01156 700 LESTIEIlrtriNELSDRINDINETLES----MKKIKKAIGDLKRL-REAFDKsgvpaMIRKSASQAmtSLTRKYLF--- 771
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 847 SCQIRYTDPSNVLVSGIDVFANPPGKNIANlmlLSGGEKTLVALSVLFSILKV--SAFPLVILDEAESALDPANVERFAN 924
Cdd:PRK01156 772 EFNLDFDDIDVDQDFNITVSRGGMVEGIDS---LSGGEKTAVAFALRVAVAQFlnNDKSLLIMDEPTAFLDEDRRTNLKD 848
                        970       980
                 ....*....|....*....|
gi 499171829 925 IIKTASKNT----QFLIITH 940
Cdd:PRK01156 849 IIEYSLKDSsdipQVIMISH 868
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3-969 0e+00

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: 884.01  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829     3 FLKRFRAYGFKSYADEITIDFTHSMTGIVGPNGSGKSNVVDALKWVLGERSMKHLRSKSGDDMIFFGSKDKPASKLAEIE 82
Cdd:TIGR02168    1 RLKKLELAGFKSFADPTTINFDKGITGIVGPNGCGKSNIVDAIRWVLGEQSAKALRGGKMEDVIFNGSETRKPLSLAEVE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829    83 LTFDNSNRLLH-DSRKEISVMRRVYRgSGQSEYFINSNPATLKEISGIFADIGLEKGSLGIISQGSVSWFVEAKPEERRK 161
Cdd:TIGR02168   81 LVFDNSDGLLPgADYSEISITRRLYR-DGESEYFINGQPCRLKDIQDLFLDTGLGKRSYSIIEQGKISEIIEAKPEERRA 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   162 IFEDASGIGRYTKRKEEVVNQLNRTLINLKQVSVVLNELKKDLKKLTLQAEKAQQFIRVKNELKELELAVLVGEYLQAQT 241
Cdd:TIGR02168  160 IFEEAAGISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELRE 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   242 ELDKFNFQINSSEHDFKIHEPQLELLEEQIVIFNSRFHSADMQSNELQKELQDIYQKINELEQRKVIIDV---------- 311
Cdd:TIGR02168  240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRErlanlerqle 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   312 ----QLRQGFSQKDEKQK-AAALKKLILVDQTQLDGFENQLS-------NSKTTITDLEKLINEQKSLVDQIKLQIEKNT 379
Cdd:TIGR02168  320 eleaQLEELESKLDELAEeLAELEEKLEELKEELESLEAELEeleaeleELESRLEELEEQLETLRSKVAQLELQIASLN 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   380 ADLIYQRSLKTIIE------------------------------------------------------------------ 393
Cdd:TIGR02168  400 NEIERLEARLERLEdrrerlqqeieellkkleeaelkelqaeleeleeeleelqeelerleealeelreeleeaeqalda 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   394 -----------------LQTNELKKTNNANILVKNANALTGILNTLGTFLKFDKQYEKAILKALGKSIGYLVVNNNNAAI 456
Cdd:TIGR02168  480 aerelaqlqarldslerLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVVENLNAAK 559
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   457 QAIDFLVKNEIGKVTFLPLDDVaSDTKITNEHMEILKQLDGFLGVCSDHVKCDPLFQPVVNTLLAQVIIAKDLNSAINLS 536
Cdd:TIGR02168  560 KAIAFLKQNELGRVTFLPLDSI-KGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELA 638
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   537 NYTYKLYRIVTLDGETVYAGGIINGGFEKTNLSDGYLSSASLDNEQNINKLENNERELKKELTELEVKLDEMN------- 609
Cdd:TIGR02168  639 KKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEeeleqlr 718
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   610 ---------------------------------------------------------------RKLKYEELLQAKFIERI 626
Cdd:TIGR02168  719 keleelsrqisalrkdlarleaeveqleeriaqlskelteleaeieeleerleeaeeelaeaeAEIEELEAQIEQLKEEL 798
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   627 VQIKKIILELKMEYEQL-----------------------TNTTFDGKKAVASE--AELIHSLNSAWAKRDEINSKLKLN 681
Cdd:TIGR02168  799 KALREALDELRAELTLLneeaanlrerleslerriaaterRLEDLEEQIEELSEdiESLAAEIEELEELIEELESELEAL 878
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   682 QELKLQ--------------LAKTIKQSEEKIVDLRALLDEQRAKLVSAREGKIRFENTIQNITEKINSVYKMTMEFAIA 747
Cdd:TIGR02168  879 LNERASleealallrseleeLSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEA 958
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   748 NHNKpVKLSSMQAHNKIAKLQNQLNEMGVINMESIAEISEKQKRFDDINAEYESAQQAVENLQKAITEIDEIASNEFDQL 827
Cdd:TIGR02168  959 LENK-IEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDT 1037
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   828 IQKLNQELPKTFKYLFGGGSCQIRYTDPSNVLVSGIDVFANPPGKNIANLMLLSGGEKTLVALSVLFSILKVSAFPLVIL 907
Cdd:TIGR02168 1038 FDQVNENFQRVFPKLFGGGEAELRLTDPEDLLEAGIEIFAQPPGKKNQNLSLLSGGEKALTALALLFAIFKVKPAPFCIL 1117
                         1130      1140      1150      1160      1170      1180
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499171829   908 DEAESALDPANVERFANIIKTASKNTQFLIITHRQGTMMKCDMLLGAAMQTKGVTKTFAVEL 969
Cdd:TIGR02168 1118 DEVDAPLDDANVERFANLLKEFSKNTQFIVITHNKGTMEVADQLYGVTMQEKGVSKIVSVDL 1179
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2-978 3.10e-151

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 473.27  E-value: 3.10e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   2 VFLKRFRAYGFKSYADEITIDFTHSMTGIVGPNGSGKSNVVDALKWVLGERSMKHLRSKSGDDMIFFGSKDKPASKLAEI 81
Cdd:COG1196    1 MRLKRLELAGFKSFADPTTIPFEPGITAIVGPNGSGKSNIVDAIRWVLGEQSAKSLRGGKMEDVIFAGSSSRKPLGRAEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  82 ELTFDNSNRLLHDSRKEISVMRRVYRgSGQSEYFINSNPATLKEISGIFADIGLEKGSLGIISQGSVSWFVEAKPEERRK 161
Cdd:COG1196   81 SLTFDNSDGTLPIDYDEVTITRRLYR-SGESEYYINGKPCRLKDIQDLFLDTGLGPESYSIIGQGMIDRIIEAKPEERRA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 162 IFEDASGIGRYTKRKEEVVNQLNRTLINLKQVSVVLNELKKDLKKLTLQAEKAQQFIRVKNELKELELAVLVGEYLQAQT 241
Cdd:COG1196  160 IIEEAAGISKYKERKEEAERKLEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 242 ELDKFNFQINSSEHDFKIHEPQLELLEEQIVIFNSRFHSADMQSNELQKELQDIYQKINELEQRkvIIDVQLRQGFSQKD 321
Cdd:COG1196  240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD--IARLEERRRELEER 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 322 EKQKAAALKKL-----------------------------------------------------------ILVDQTQLDG 342
Cdd:COG1196  318 LEELEEELAELeeeleeleeeleeleeeleeaeeeleeaeaelaeaeealleaeaelaeaeeeleelaeeLLEALRAAAE 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 343 FENQLSNSKTTITDLEKLINEQKSLVDQIKLQIEKNTADLIYQRSLKTIIELQTNELKKTNNANIL-------------- 408
Cdd:COG1196  398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEllaelleeaallea 477
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 409 -----------------------------------VKNANALTGILNTLGTFLKFDKQYEKAILKALGKSIGYLVVNNNN 453
Cdd:COG1196  478 alaelleelaeaaarllllleaeadyegflegvkaALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDE 557
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 454 AAIQAIDFLVKNEIGKVTFLPLdDVASDTKITNEHMEILKQLDGFLGVCSDHVKCDPLFQPVVNTLLAQVIIAKDLNSAI 533
Cdd:COG1196  558 VAAAAIEYLKAAKAGRATFLPL-DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 534 NLSNYTYKLYRIVTLDGETVYAGGIINGGFEKTNLsdgylsSASLDNEQNINKLENNERELKKELTELEVKLDEMNRKLK 613
Cdd:COG1196  637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL------AALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 614 YEELLQAkfierivqikkiilelkmeyeqltnttfdgkkavaseaelihslnsawakRDEINSKLKLNQELKLQLAKTIK 693
Cdd:COG1196  711 EAEEERL--------------------------------------------------EEELEEEALEEQLEAEREELLEE 740
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 694 QSEEKIVDLRALLDEqraklvsaregkirfentiqnitekinsvykmtmefaianhnKPVKLSSMQAHNKIAKLQNQLNE 773
Cdd:COG1196  741 LLEEEELLEEEALEE------------------------------------------LPEPPDLEELERELERLEREIEA 778
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 774 MGVINMESIAEISEKQKRFDDINAEYESAQQAVENLQKAITEIDEIASNEFDQLIQKLNQELPKTFKYLFGGGSCQIRYT 853
Cdd:COG1196  779 LGPVNLLAIEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRERFLETFDAVNENFQELFPRLFGGGEAELLLT 858
                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 854 DPSNVLVSGIDVFANPPGKNIANLMLLSGGEKTLVALSVLFSILKVSAFPLVILDEAESALDPANVERFANIIKTASKNT 933
Cdd:COG1196  859 DPDDPLETGIEIMAQPPGKKLQRLSLLSGGEKALTALALLFAIFRLNPSPFCVLDEVDAPLDDANVERFAELLKEMSEDT 938
                       1050      1060      1070      1080
                 ....*....|....*....|....*....|....*....|....*
gi 499171829 934 QFLIITHRQGTMMKCDMLLGAAMQTKGVTKTFAVELENAEKYVSE 978
Cdd:COG1196  939 QFIVITHNKRTMEAADRLYGVTMQEPGVSRVVSVDLEEAEELAEA 983
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
3-963 2.93e-110

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: 368.14  E-value: 2.93e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829     3 FLKRFRAYGFKSYADEITIDFTHSMTGIVGPNGSGKSNVVDALKWVLGERSMKHLRSKSGDDMIFfgSKDKPASKLAEIE 82
Cdd:pfam02463    1 YLKRIEIEGFKSYAKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIH--SKSGAFVNSAEVE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829    83 LTFDNSNRLLHDSRKEISVMRRVYRGsGQSEYFINSNPATLKEISGIFADIGLEKGSLGIISQGSVSWFVEAKPEERRKI 162
Cdd:pfam02463   79 ITFDNEDHELPIDKEEVSIRRRVYRG-GDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLE 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   163 FEDASGIGRYTKRKEEVVNQLNRTLINLKQVSVVLNELKKDLKKLTLQAEKAQQFIRVKNELKELELAVLVGEYLQAQTE 242
Cdd:pfam02463  158 IEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEE 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   243 LDKFNFQINSSEHDFKIHEPQLELLEEQIVIFNSRFHSADMQSNELQKELQDIYQKINELEQRKVIIDVQL------RQG 316
Cdd:pfam02463  238 RIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRkvddeeKLK 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   317 FSQKDEKQKAAALKKLILV------------------------------------------------------------- 335
Cdd:pfam02463  318 ESEKEKKKAEKELKKEKEEieelekelkeleikreaeeeeeeeleklqekleqleeellakkkleserlssaaklkeeel 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   336 ---------DQTQLDGFENQLSNSKTTITDLEKLINEQKSLVDQIKLQIEKNTADLIYQRSLKTI----IELQTNELKKT 402
Cdd:pfam02463  398 elkseeekeAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKdeleLKKSEDLLKET 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   403 NNANILVKNANALTGILNTLGTFLKFDKQYEKAILKALGKS---------------IGYLVVNNNNAAIQAIDFLV---- 463
Cdd:pfam02463  478 QLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDgvggriisahgrlgdLGVAVENYKVAISTAVIVEVsata 557
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   464 ---------------------------------KNEIGKVTFLPLDDVASDTKITNEHMEILKQLDGFLGVCSDHVKCDP 510
Cdd:pfam02463  558 deveerqklvraltelplgarklrllipklklpLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKL 637
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   511 L-----------------------------------------------------------------------FQPVVNTL 519
Cdd:pfam02463  638 KesakakesglrkgvsleeglaeksevkaslseltkelleiqelqekaeselakeeilrrqleikkkeqrekEELKKLKL 717
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   520 LAQVIIAKDLNSAINLSNYTYKLYRIVTLDGETVYAGGIINGGFEKTNLSDGYLSSASLDNEQNINKLENNERELKKELT 599
Cdd:pfam02463  718 EAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLK 797
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   600 ELEVKLDEMNRKLKYEELLQAKFIERIVQIKKIILELKMEYEQLTNTTFDGKKAVASEAELIHSLNSAWAKRDEINSKLK 679
Cdd:pfam02463  798 AQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEE 877
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   680 LNQELKLQLAKTIKQSEEKIVDLRALLDEQRAKLVSAREGKIRFENTIQNITEKINSVYKMTMEFAIANHNKPVKLSSMQ 759
Cdd:pfam02463  878 ELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEE 957
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   760 AHNKIAKLQNQLNEMGVINMESIAEISEKQKRFDDINAEYESAQQAVENLQKAITEIDEIASNEFDQLIQKLNQELPKTF 839
Cdd:pfam02463  958 EEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVF 1037
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   840 KYLFGGGSCQIRYTDPSNVLVSGIDVFANPPGKNIANLMLLSGGEKTLVALSVLFSILKVSAFPLVILDEAESALDPANV 919
Cdd:pfam02463 1038 FYLELGGSAELRLEDPDDPFSGGIEISARPPGKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNV 1117
                         1130      1140      1150      1160
                   ....*....|....*....|....*....|....*....|....
gi 499171829   920 ERFANIIKTASKNTQFLIITHRQGTMMKCDMLLGAAMQTKGVTK 963
Cdd:pfam02463 1118 SRVANLLKELSKNAQFIVISLREEMLEKADKLVGVTMVENGVST 1161
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
3-969 5.25e-80

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: 283.11  E-value: 5.25e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829     3 FLKRFRAYGFKSYADEITIDFTHSMTGIVGPNGSGKSNVVDALKWVLGERSMKHLRSKSGDDMIFFGSKDKPAsKLAEIE 82
Cdd:TIGR02169    1 YIERIELENFKSFGKKKVIPFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKAMRAERLSDLISNGKNGQSG-NEAYVT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829    83 LTFDNSNRLLHDSrKEISVMRRVYRGSGQSEYFINSNPATLKEISGIFADIGLEKGSLGIISQGSVSWFVEAKPEERRKI 162
Cdd:TIGR02169   80 VTFKNDDGKFPDE-LEVVRRLKVTDDGKYSYYYLNGQRVRLSEIHDFLAAAGIYPEGYNVVLQGDVTDFISMSPVERRKI 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   163 FEDASGIGRYTKRKEEVVNQLNRTLINLKQVSVVLNELKKDLKKLTLQAEKAQQFIRVKNELKELELAVLV--------- 233
Cdd:TIGR02169  159 IDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLkekealerq 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   234 ------------------------------------------------GEYLQAQTELDKFNFQINSSEHDFKIHEPQLE 265
Cdd:TIGR02169  239 keaierqlasleeeleklteeiselekrleeieqlleelnkkikdlgeEEQLRVKEKIGELEAEIASLERSIAEKERELE 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   266 LLEEQIVIFNSRFHSADMQSNELQKELQ--------------DIYQKINELEQRKVIIDVQLRQGF-SQKDEKQKAAALK 330
Cdd:TIGR02169  319 DAEERLAKLEAEIDKLLAEIEELEREIEeerkrrdklteeyaELKEELEDLRAELEEVDKEFAETRdELKDYREKLEKLK 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   331 KLILVDQTQLDGF-------ENQLSNSKTTITDLEKLINEQKSLVDQIKLQIEKNT-------ADLI-YQRSLKTI---- 391
Cdd:TIGR02169  399 REINELKRELDRLqeelqrlSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEwkleqlaADLSkYEQELYDLkeey 478
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   392 ---------IELQTNELKKT----------NNANILVKNANaLTGILNTLGTFLKFDKQYEKAILKALGKSIGYLVVNNN 452
Cdd:TIGR02169  479 drvekelskLQRELAEAEAQaraseervrgGRAVEEVLKAS-IQGVHGTVAQLGSVGERYATAIEVAAGNRLNNVVVEDD 557
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   453 NAAIQAIDFLVKNEIGKVTFLPLDDVASDTKitneHMEILKqLDGFLGVCSDHVKCDPLFQPVVNTLLAQVIIAKDLNSA 532
Cdd:TIGR02169  558 AVAKEAIELLKRRKAGRATFLPLNKMRDERR----DLSILS-EDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVEDIEAA 632
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   533 INLSNytykLYRIVTLDGETVYAGGIINGGFEKtnLSDGYLSSAS--------------LDNEQN--------------- 583
Cdd:TIGR02169  633 RRLMG----KYRMVTLEGELFEKSGAMTGGSRA--PRGGILFSRSepaelqrlrerlegLKRELSslqselrrienrlde 706
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   584 ------------------INKLENNERELKKELTELEVKLDEMNRKLKYEELLQAKFIERIVQIKKIILELKMEYE---- 641
Cdd:TIGR02169  707 lsqelsdasrkigeiekeIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNdlea 786
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   642 --------QLTNTTFDGKKAVASEAELIHSLNSAWAKR--------DEINSKLKLNQELKLQ------------------ 687
Cdd:TIGR02169  787 rlshsripEIQAELSKLEEEVSRIEARLREIEQKLNRLtlekeyleKEIQELQEQRIDLKEQiksiekeienlngkkeel 866
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   688 ------LAKTIKQSEEKIVDLRALLDEQRAKLVSAREGKIRFENTIQnITEKINSVYKMTMEFA---IANHNKPVK---- 754
Cdd:TIGR02169  867 eeeleeLEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE-KKRKRLSELKAKLEALeeeLSEIEDPKGedee 945
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   755 -----LSSMQAHNKIAKLQNQLNEMGVINMESIAEISEKQKRFDDINAEYESAQQAVENLQKAITEIDEIASNEFDQLIQ 829
Cdd:TIGR02169  946 ipeeeLSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFE 1025
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   830 KLNqelpKTFKYLFG---GGSCQIRYTDPSNVLVSGIDVFANPPGKNIANLMLLSGGEKTLVALSVLFSILKVSAFPLVI 906
Cdd:TIGR02169 1026 AIN----ENFNEIFAelsGGTGELILENPDDPFAGGLELSAKPKGKPVQRLEAMSGGEKSLTALSFIFAIQRYKPSPFYA 1101
                         1130      1140      1150      1160      1170      1180
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499171829   907 LDEAESALDPANVERFANIIKTASKNTQFLIITHRQGTMMKCDMLLGAAMQTKGVTKTFAVEL 969
Cdd:TIGR02169 1102 FDEVDMFLDGVNVERVAKLIREKAGEAQFIVVSLRSPMIEYADRAIGVTMRRNGESQVFGLKL 1164
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
863-963 4.41e-45

ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213245 [Multi-domain]  Cd Length: 197  Bit Score: 161.09  E-value: 4.41e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 863 IDVFANPPGKNIANLMLLSGGEKTLVALSVLFSILKVSAFPLVILDEAESALDPANVERFANIIKTASKNTQFLIITHRQ 942
Cdd:cd03278   97 VSEIIEAPGKKVQRLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRK 176
                         90       100
                 ....*....|....*....|.
gi 499171829 943 GTMMKCDMLLGAAMQTKGVTK 963
Cdd:cd03278  177 GTMEAADRLYGVTMQESGVSK 197
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
4-92 6.77e-41

ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213245 [Multi-domain]  Cd Length: 197  Bit Score: 149.15  E-value: 6.77e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   4 LKRFRAYGFKSYADEITIDFTHSMTGIVGPNGSGKSNVVDALKWVLGERSMKHLRSKSGDDMIFFGSKDKPASKLAEIEL 83
Cdd:cd03278    1 LKKLELKGFKSFADKTTIPFPPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAKSLRGEKMSDVIFAGSETRKPANFAEVTL 80

                 ....*....
gi 499171829  84 TFDNSNRLL 92
Cdd:cd03278   81 TFDNSDGRY 89
SMC_hinge smart00968
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ...
417-535 9.59e-31

SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.


Pssm-ID: 214944 [Multi-domain]  Cd Length: 120  Bit Score: 117.33  E-value: 9.59e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   417 GILNTLGTFLKFDKQYEKAILKALGKSIGYLVVNNNNAAIQAIDFLVKNEIGKVTFLPLDDVASDTKITNEHMEILKQLD 496
Cdd:smart00968   2 GVLGRVADLISVDPKYETALEAALGGRLQAVVVDTEETAKKAIEFLKKNRLGRATFLPLDKIKPRSPAGSKLREALLPEP 81
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 499171829   497 GFLGVCSDHVKCDPLFQPVVNTLLAQVIIAKDLNSAINL 535
Cdd:smart00968  82 GFVGPAIDLVEYDPELRPALEYLLGNTLVVDDLETARRL 120
ABC_SMC1_euk cd03275
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ...
4-135 1.51e-24

ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213242 [Multi-domain]  Cd Length: 247  Bit Score: 103.81  E-value: 1.51e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   4 LKRFRAYGFKSYADEITIDFTHSMTGIVGPNGSGKSNVVDALKWVLGERSmKHLRSKSGDDMIFFGSKDKPASKLAEIEL 83
Cdd:cd03275    1 LKRLELENFKSYKGRHVIGPFDRFTCIIGPNGSGKSNLMDAISFVLGEKS-SHLRSKNLKDLIYRARVGKPDSNSAYVTA 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499171829  84 TFdnsnrllHDSRKEISVMRRVYRGSGqSEYFINSNPATLKEISGIFADIGL 135
Cdd:cd03275   80 VY-------EDDDGEEKTFRRIITGGS-SSYRINGKVVSLKEYNEELEKINI 123
SMC_hinge pfam06470
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ...
415-536 1.32e-22

SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.


Pssm-ID: 461926 [Multi-domain]  Cd Length: 116  Bit Score: 93.87  E-value: 1.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  415 LTGILNTLGTFLKFDKQYEKAILKALGKSIGYLVVNNNNAAIQAIDFLVKNEIGKVTFLPLDDVASDTKITNEHmeilkq 494
Cdd:pfam06470   1 LKGVLGRLADLIEVDEGYEKAVEAALGGRLQAVVVDDEDDAKRAIEFLKKNKLGRATFLPLDRLKPRPRRPGAD------ 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 499171829  495 LDGFLGVCSDHVKCDPLFQPVVNTLLAQVIIAKDLNSAINLS 536
Cdd:pfam06470  75 LKGGAGPLLDLVEYDDEYRKALRYLLGNTLVVDDLDEALELA 116
ABC_SMC1_euk cd03275
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ...
868-953 3.15e-17

ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213242 [Multi-domain]  Cd Length: 247  Bit Score: 82.24  E-value: 3.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 868 NPPGKNIANLMLLSGGEKTLVALSVLFSILKVSAFPLVILDEAESALDPANVERFANIIKT-ASKNTQFLIITHRQGTMM 946
Cdd:cd03275  144 NPPGKRFRDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREqAGPNFQFIVISLKEEFFS 223

                 ....*..
gi 499171829 947 KCDMLLG 953
Cdd:cd03275  224 KADALVG 230
ABC_SMC_head cd03239
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ...
4-92 3.60e-17

The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.


Pssm-ID: 213206 [Multi-domain]  Cd Length: 178  Bit Score: 80.43  E-value: 3.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   4 LKRFRAYGFKSYADEITIDFTHSMTGIVGPNGSGKSNVVDALKWVLGERSmKHLRSKSGddMIFFGSKDKPASKLAEIEL 83
Cdd:cd03239    1 IKQITLKNFKSYRDETVVGGSNSFNAIVGPNGSGKSNIVDAICFVLGGKA-AKLRRGSL--LFLAGGGVKAGINSASVEI 77

                 ....*....
gi 499171829  84 TFDNSNRLL 92
Cdd:cd03239   78 TFDKSYFLV 86
ABC_SMC2_euk cd03273
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ...
11-148 1.45e-16

ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213240 [Multi-domain]  Cd Length: 251  Bit Score: 80.42  E-value: 1.45e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  11 GFKSYADEITI-DFTHSMTGIVGPNGSGKSNVVDALKWVLGERSMKHLRSKSGDDMIFFGSKDKPASklAEIELTFDNSN 89
Cdd:cd03273   10 GFKSYATRTVIsGFDPQFNAITGLNGSGKSNILDAICFVLGITNLSTVRASNLQDLIYKRGQAGITK--ASVTIVFDNSD 87
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499171829  90 R----LLHDSRKEISVMRRVYRGsGQSEYFINSNPATLKEISGIFADIGLEKGSLG-IISQGSV 148
Cdd:cd03273   88 KsqspIGFENYPEITVTRQIVLG-GTNKYLINGHRAQQQRVQDLFQSVQLNVNNPHfLIMQGRI 150
ABC_SMC_head cd03239
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ...
879-963 1.61e-16

The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.


Pssm-ID: 213206 [Multi-domain]  Cd Length: 178  Bit Score: 78.50  E-value: 1.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 879 LLSGGEKTLVALSVLFSILKVSAFPLVILDEAESALDPANVERFANIIK-TASKNTQFLIITHRQGTMMKCDMLLGAAMQ 957
Cdd:cd03239   94 ILSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKeMAKHTSQFIVITLKKEMFENADKLIGVLFV 173

                 ....*.
gi 499171829 958 tKGVTK 963
Cdd:cd03239  174 -HGVST 178
ABC_SMC3_euk cd03272
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ...
4-162 5.82e-16

ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213239 [Multi-domain]  Cd Length: 243  Bit Score: 78.46  E-value: 5.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   4 LKRFRAYGFKSYADEITIDFTHSMTG-IVGPNGSGKSNVVDALKWVLGErSMKHLRSKSGDDMIFFGSKDKPASklAEIE 82
Cdd:cd03272    1 IKQVIIQGFKSYKDQTVIEPFSPKHNvVVGRNGSGKSNFFAAIRFVLSD-EYTHLREEQRQALLHEGSGPSVMS--AYVE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  83 LTFDNSNRLLHDSRKEISVMRRVyrGSGQSEYFINSNPATLKEISGIFADIGLEKGSL-GIISQGSVSWFVEAKPEERRK 161
Cdd:cd03272   78 IIFDNSDNRFPIDKEEVRLRRTI--GLKKDEYFLDKKNVTKNDVMNLLESAGFSRSNPyYIVPQGKINSLTNMKQDEQQE 155

                 .
gi 499171829 162 I 162
Cdd:cd03272  156 M 156
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
4-179 8.16e-15

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 74.28  E-value: 8.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   4 LKRFRAYGFKSYADEITIDFTHSMTGIVGPNGSGKSNVVDALKWVLGERSMKhlRSKSGDDMIFFGSKDkpasklAEIEL 83
Cdd:COG0419    2 LLRLRLENFRSYRDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARS--RSKLRSDLINVGSEE------ASVEL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  84 TFDNSNRLLHDSRkeisvmrrvyrgsgqseyfinsnpatlkeisgifadiglekgslgiiSQGSVSWFVEAKPEERRKIF 163
Cdd:COG0419   74 EFEHGGKRYRIER-----------------------------------------------RQGEFAEFLEAKPSERKEAL 106
                        170
                 ....*....|....*.
gi 499171829 164 EDASGIGRYTKRKEEV 179
Cdd:COG0419  107 KRLLGLEIYEELKERL 122
ABC_SMC4_euk cd03274
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ...
872-964 1.45e-13

ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213241 [Multi-domain]  Cd Length: 212  Bit Score: 70.79  E-value: 1.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 872 KNIANLmllSGGEKTLVALSVLFSILKVSAFPLVILDEAESALDPANVERFANIIKTASKNTQFLIITHRQGTMMKCDML 951
Cdd:cd03274  123 KNISNL---SGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELADRL 199
                         90
                 ....*....|...
gi 499171829 952 LGaAMQTKGVTKT 964
Cdd:cd03274  200 VG-IYKTNNCTKS 211
ABC_SMC2_euk cd03273
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ...
876-943 6.28e-13

ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213240 [Multi-domain]  Cd Length: 251  Bit Score: 69.63  E-value: 6.28e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499171829 876 NLMLLSGGEKTLVALSVLFSILKVSAFPLVILDEAESALDPANVERFANIIKTASKNTQFLIITHRQG 943
Cdd:cd03273  163 SLTELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGSQFIVVSLKEG 230
ABC_SMC4_euk cd03274
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ...
3-85 1.89e-12

ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213241 [Multi-domain]  Cd Length: 212  Bit Score: 67.32  E-value: 1.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   3 FLKRFRAYGFKSYADEITID-FTHSMTGIVGPNGSGKSNVVDALKWVLGERSmKHLRSKSGDDMIfFGSKDKPASKLAEI 81
Cdd:cd03274    2 IITKLVLENFKSYAGEQVIGpFHKSFSAIVGPNGSGKSNVIDSMLFVFGFRA-SKMRQKKLSDLI-HNSAGHPNLDSCSV 79

                 ....
gi 499171829  82 ELTF 85
Cdd:cd03274   80 EVHF 83
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
877-963 2.63e-12

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 65.84  E-value: 2.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 877 LMLLSGGEKTLVALSVLFSILKVSAFPLVILDEAESALDPANVERFANIIK-TASKNTQFLIITHRQGTMMKCDMLLGAA 955
Cdd:cd03227   75 RLQLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILeHLVKGAQVIVITHLPELAELADKLIHIK 154

                 ....*...
gi 499171829 956 MQTKGVTK 963
Cdd:cd03227  155 KVITGVYK 162
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
857-952 2.17e-11

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 63.03  E-value: 2.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 857 NVLVSGIDVFANPPG---KNIANLMLLSGGEKTLVALSVLFsilkVSAFPLVILDEAESALDPANVERFANIIKT-ASKN 932
Cdd:cd00267   55 EILIDGKDIAKLPLEelrRRIGYVPQLSGGQRQRVALARAL----LLNPDLLLLDEPTSGLDPASRERLLELLRElAEEG 130
                         90       100
                 ....*....|....*....|.
gi 499171829 933 TQFLIITHRQGTMMK-CDMLL 952
Cdd:cd00267  131 RTVIIVTHDPELAELaADRVI 151
ABC_SMC3_euk cd03272
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ...
880-941 2.49e-11

ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213239 [Multi-domain]  Cd Length: 243  Bit Score: 64.97  E-value: 2.49e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499171829 880 LSGGEKTLVALSVLFSILKVSAFPLVILDEAESALDPANVERFANIIKTASKNTQFLIITHR 941
Cdd:cd03272  159 LSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFR 220
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
4-105 4.44e-10

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 60.31  E-value: 4.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   4 LKRFRAYGFKSYADEITIDFTHSMTGIVGPNGSGKSNVVDALKWVL-GERSMKHLRSKSGDDMIFFGskdkpaSKLAEIE 82
Cdd:cd03240    1 IDKLSIRNIRSFHERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALtGELPPNSKGGAHDPKLIREG------EVRAQVK 74
                         90       100
                 ....*....|....*....|...
gi 499171829  83 LTFDNSNRLLHDSRKEISVMRRV 105
Cdd:cd03240   75 LAFENANGKKYTITRSLAILENV 97
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
3-98 5.74e-10

Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];


Pssm-ID: 442812 [Multi-domain]  Cd Length: 359  Bit Score: 62.33  E-value: 5.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   3 FLKRFRAYGFKSYADeITIDFTHSMTGIVGPNGSGKSNVVDALKWVLGERSMKHLRSksgDDmifFGSKDKPASKLAEIE 82
Cdd:COG3593    2 KLEKIKIKNFRSIKD-LSIELSDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFDE---ED---FYLGDDPDLPEIEIE 74
                         90
                 ....*....|....*..
gi 499171829  83 LTFDNS-NRLLHDSRKE 98
Cdd:COG3593   75 LTFGSLlSRLLRLLLKE 91
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
11-60 1.33e-09

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 58.14  E-value: 1.33e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499171829  11 GFKSYADEITIDFTH-SMTGIVGPNGSGKSNVVDALKWVLGERSMKHLRSK 60
Cdd:cd03227    6 RFPSYFVPNDVTFGEgSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRS 56
ABC_RecN cd03241
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ...
17-162 2.31e-09

ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213208 [Multi-domain]  Cd Length: 276  Bit Score: 59.52  E-value: 2.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  17 DEITIDFTHSMTGIVGPNGSGKSNVVDALKWVLGERSMKhlrsksgdDMIFFGSKDkpasklAEIELTFDNSNR------ 90
Cdd:cd03241   13 EELELDFEEGLTVLTGETGAGKSILLDALSLLLGGRASA--------DLIRSGAEK------AVVEGVFDISDEeeakal 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499171829  91 --LLHDSRKEISVMRRVYRGSGQSEYFINSNPATLKEISGIfadiglekGSLGIISQGSVSWFVEAKPEERRKI 162
Cdd:cd03241   79 llELGIEDDDDLIIRREISRKGRSRYFINGQSVTLKLLREL--------GSLLVDIHGQHDHQNLLNPERQLDL 144
COG4637 COG4637
Predicted ATPase [General function prediction only];
4-89 2.78e-09

Predicted ATPase [General function prediction only];


Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 60.33  E-value: 2.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   4 LKRFRAYGFKSYADeITIDFtHSMTGIVGPNGSGKSNVVDA---LKWVLGERSMKHLRSKSG-DDMIFFGSKDKPASklA 79
Cdd:COG4637    2 ITRIRIKNFKSLRD-LELPL-GPLTVLIGANGSGKSNLLDAlrfLSDAARGGLQDALARRGGlEELLWRGPRTITEP--I 77
                         90
                 ....*....|
gi 499171829  80 EIELTFDNSN 89
Cdd:COG4637   78 RLELEFAEED 87
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
879-949 2.90e-09

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 57.01  E-value: 2.90e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499171829 879 LLSGGEKTLVALSVLFsilkVSAFPLVILDEAESALDPANVERFANIIKTASKNTQFLIITHRQGTMMKCD 949
Cdd:cd03228   96 ILSGGQRQRIAIARAL----LRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDAD 162
PRK01156 PRK01156
chromosome segregation protein; Provisional
4-940 2.99e-09

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 61.07  E-value: 2.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   4 LKRFRAYGFKSYADEiTIDFTHSMTGIVGPNGSGKSNVVDALKWVLgersMKHLRSKSGDDMIffgskdKPASKLAEIEL 83
Cdd:PRK01156   3 IKRIRLKNFLSHDDS-EIEFDTGINIITGKNGAGKSSIVDAIRFAL----FTDKRTEKIEDMI------KKGKNNLEVEL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  84 TFDNS----------NRLLHDSRKEISVMRrvyRGSGQSEYFINSNPATLKEISGIFADIGLEKGSLGiisQGSVSWFVE 153
Cdd:PRK01156  72 EFRIGghvyqirrsiERRGKGSRREAYIKK---DGSIIAEGFDDTTKYIEKNILGISKDVFLNSIFVG---QGEMDSLIS 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 154 AKPEERRKIFEDASGIGR----YTKRKeEVVNQLNRTLINLKQVSVVLNELKKDLKKLTLQAEKAQQfirvKNELKELEL 229
Cdd:PRK01156 146 GDPAQRKKILDEILEINSlernYDKLK-DVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEK----SHSITLKEI 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 230 AVLVGEYLQAQTELDkfnfQINSSEHDFKIHEPQLELLEEQIVIFNSRFHSADMQSNelqkELQDIYQKINELEQRKVii 309
Cdd:PRK01156 221 ERLSIEYNNAMDDYN----NLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNN----YYKELEERHMKIINDPV-- 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 310 dvqlrqgFSQKDEKQKAAALKKLILVDQTQLDGFENQLSNSKTTITDLEKLineQKSLVDQIKLQIEKNTADliyqrslK 389
Cdd:PRK01156 291 -------YKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVL---QKDYNDYIKKKSRYDDLN-------N 353
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 390 TIIELQTNELKktnnanilvknanaLTGILNTLGTFLKFDKQYEKAIlKALGKSIGYLVvnnnnaAIQAIDFLVKNEIGK 469
Cdd:PRK01156 354 QILELEGYEMD--------------YNSYLKSIESLKKKIEEYSKNI-ERMSAFISEIL------KIQEIDPDAIKKELN 412
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 470 VTFLPLDDVASDTKITNEHMEILKQ----LDGFLGVCSDHVKCdplfqPVVNTLLAQVIIAKDLNsainlsNYTYKLYRI 545
Cdd:PRK01156 413 EINVKLQDISSKVSSLNQRIRALREnldeLSRNMEMLNGQSVC-----PVCGTTLGEEKSNHIIN------HYNEKKSRL 481
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 546 VTLDGETVYAGGIINGGFEKTNLSDGYLssasldNEQNINKLENNERELKKELTELEVKLDEMNRkLKYEELLQAKFIER 625
Cdd:PRK01156 482 EEKIREIEIEVKDIDEKIVDLKKRKEYL------ESEEINKSINEYNKIESARADLEDIKIKINE-LKDKHDKYEEIKNR 554
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 626 IVQIKKIILELKmeyeqltNTTFDGKKAVASEAElIHSLNSawaKRDEINSKLK----LNQELKLQLAKTIKQSEEKIVD 701
Cdd:PRK01156 555 YKSLKLEDLDSK-------RTSWLNALAVISLID-IETNRS---RSNEIKKQLNdlesRLQEIEIGFPDDKSYIDKSIRE 623
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 702 LRALLDEQRAKLVSAREGKIRfentIQNITEKINSVYKMTMEF-AIANHNKPVKLSSMQAHNKIAKLQNQLNEMGV--IN 778
Cdd:PRK01156 624 IENEANNLNNKYNEIQENKIL----IEKLRGKIDNYKKQIAEIdSIIPDLKEITSRINDIEDNLKKSRKALDDAKAnrAR 699
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 779 MESIAEI-----SEKQKRFDDINAEYESaqqaVENLQKAITEIDEIaSNEFDQ-----LIQKLNQEL--PKTFKYLFggg 846
Cdd:PRK01156 700 LESTIEIlrtriNELSDRINDINETLES----MKKIKKAIGDLKRL-REAFDKsgvpaMIRKSASQAmtSLTRKYLF--- 771
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 847 SCQIRYTDPSNVLVSGIDVFANPPGKNIANlmlLSGGEKTLVALSVLFSILKV--SAFPLVILDEAESALDPANVERFAN 924
Cdd:PRK01156 772 EFNLDFDDIDVDQDFNITVSRGGMVEGIDS---LSGGEKTAVAFALRVAVAQFlnNDKSLLIMDEPTAFLDEDRRTNLKD 848
                        970       980
                 ....*....|....*....|
gi 499171829 925 IIKTASKNT----QFLIITH 940
Cdd:PRK01156 849 IIEYSLKDSsdipQVIMISH 868
RecF COG1195
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
3-161 5.43e-09

Recombinational DNA repair ATPase RecF [Replication, recombination and repair];


Pssm-ID: 440808 [Multi-domain]  Cd Length: 352  Bit Score: 59.01  E-value: 5.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   3 FLKRFRAYGFKSYAdEITIDFTHSMTGIVGPNGSGKSNVVDALkWVLGersmkHLRSksgddmiFFGSKDKPA----SKL 78
Cdd:COG1195    1 RLKRLSLTNFRNYE-SLELEFSPGINVLVGPNGQGKTNLLEAI-YLLA-----TGRS-------FRTARDAELirfgADG 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  79 AEIELTFDNSNRLLhdsrkEISVmrrVYRGSGQSEYFINSNPA-TLKEISGIF-------ADIGLEKGSlgiisqgsvsw 150
Cdd:COG1195   67 FRVRAEVERDGREV-----RLGL---GLSRGGKKRVRINGKPVrRLSDLAGLLpvvlfspEDLRLVKGG----------- 127
                        170
                 ....*....|.
gi 499171829 151 fveakPEERRK 161
Cdd:COG1195  128 -----PSERRR 133
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
6-398 1.20e-08

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: 59.21  E-value: 1.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829     6 RFRAYGFKSYADEITIDFT--HSMTGIVGPNGSGKSNVVDALKWVL-GErsmkhLRSKSGDDMIFFG-SKDKPASKLAEI 81
Cdd:TIGR00618    5 RLTLKNFGSYKGTHTIDFTalGPIFLICGKTGAGKTTLLDAITYALyGK-----LPRRSEVIRSLNSlYAAPSEAAFAEL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829    82 ELTFDNSNRLLHDSRK--------EISVMRRVYRGSGQSEYFINSNPATLKEISGIfadIGLEKGSL---GIISQGSVSW 150
Cdd:TIGR00618   80 EFSLGTKIYRVHRTLRctrshrktEQPEQLYLEQKKGRGRILAAKKSETEEVIHDL---LKLDYKTFtrvVLLPQGEFAQ 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   151 FVEAKPEERRKIFEDASGIGRYTKRKEEVVNQLN--RTLINLKQVSVVLNELKKDLKKLTLQAEKAQQFIRVKNELKELE 228
Cdd:TIGR00618  157 FLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKslHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQ 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   229 LAVLVGEYLQ----AQTELDKFNFQINSSEHDFKIHEPQLELLEEQIVIFNSRFHSADMQsnELQKELQDIYQKINELEQ 304
Cdd:TIGR00618  237 QTQQSHAYLTqkreAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLA--AHIKAVTQIEQQAQRIHT 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   305 RkviidVQLRQGFSQKDEKQKAAALK-KLILVDQTQLDGFENQLSNSKTTITDLEKLINE----QKSLVDQIKLQIEKNT 379
Cdd:TIGR00618  315 E-----LQSKMRSRAKLLMKRAAHVKqQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREiscqQHTLTQHIHTLQQQKT 389
                          410
                   ....*....|....*....
gi 499171829   380 ADLIYQRSLKTIIELQTNE 398
Cdd:TIGR00618  390 TLTQKLQSLCKELDILQRE 408
AAA_23 pfam13476
AAA domain;
11-193 1.50e-08

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 55.58  E-value: 1.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   11 GFKSYADEiTIDFTHSMTGIVGPNGSGKSNVVDALKWVLGERSMKHLRSKSGDDMIFFGSKDKPASKLAEIELTFDNSNR 90
Cdd:pfam13476   5 NFRSFRDQ-TIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGDIRIGLEGKGKAYVEITFENNDG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   91 llhDSRKEISVMRRVYRGSGQSEYFINSNpatLKEISGIFADIGLEKGSLGIIS-------QGSVSWFVEAKPEERRKIF 163
Cdd:pfam13476  84 ---RYTYAIERSRELSKKKGKTKKKEILE---ILEIDELQQFISELLKSDKIILpllvflgQEREEEFERKEKKERLEEL 157
                         170       180       190
                  ....*....|....*....|....*....|
gi 499171829  164 EDASGIGRYTKRKEEVVNQLNRTLINLKQV 193
Cdd:pfam13476 158 EKALEEKEDEKKLLEKLLQLKEKKKELEEL 187
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
880-941 1.44e-07

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 53.24  E-value: 1.44e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499171829 880 LSGGEKTLVAL-SVLfsilkVSAFPLVILDEAESALDPANVERFANIIKT-ASKNTQFLIITHR 941
Cdd:cd03225  135 LSGGQKQRVAIaGVL-----AMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHD 193
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
880-940 2.74e-07

Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];


Pssm-ID: 440739 [Multi-domain]  Cd Length: 230  Bit Score: 52.72  E-value: 2.74e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499171829 880 LSGGEKTLVAL-SVLfsILKvsafP-LVILDEAESALDPANVERFANIIKT-ASKNTQFLIITH 940
Cdd:COG1122  135 LSGGQKQRVAIaGVL--AME----PeVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTH 192
PRK10869 PRK10869
recombination and repair protein; Provisional
18-126 1.23e-06

recombination and repair protein; Provisional


Pssm-ID: 236781 [Multi-domain]  Cd Length: 553  Bit Score: 52.24  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  18 EITIDFTHSMTGIVGPNGSGKSNVVDALKWVLGER---SMKHLRSKSGDDMIFFGSKDKPASK--LAEIELtfDNSNRLL 92
Cdd:PRK10869  15 ELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRaeaSMVRPGATRADLCARFSLKDTPAALrwLEDNQL--EDGNECL 92
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 499171829  93 hdsrkeisvMRRVYRGSGQSEYFINSNP---ATLKEI 126
Cdd:PRK10869  93 ---------LRRVISSDGRSRGFINGTPvplSQLREL 120
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
17-133 1.44e-06

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 52.00  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  17 DEITIDFTHSMTGIVGPNGSGKSNVVDALKWVLGERsmkhlrsksGD-DMIFFGSkDKpasklAEIELTFDNSN-----R 90
Cdd:COG0497   14 DELELEFGPGLTVLTGETGAGKSILLDALGLLLGGR---------ADaSLVRHGA-DK-----AEVEAVFDLSDdpplaA 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499171829  91 LLHDsrKEIS------VMRRVYRGSGQSEYFINSNPAT---LKEISGIFADI 133
Cdd:COG0497   79 WLEE--NGLDlddgelILRREISADGRSRAFINGRPVTlsqLRELGELLVDI 128
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
11-91 2.10e-06

ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.


Pssm-ID: 213246 [Multi-domain]  Cd Length: 213  Bit Score: 49.57  E-value: 2.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  11 GFKSYADEITIDFT----HSMTGIVGPNGSGKSNVVDALKWVL-GERSMKhlrSKSGDDMIFFGSKDKPasklAEIELTF 85
Cdd:cd03279   10 NFGPFREEQVIDFTgldnNGLFLICGPTGAGKSTILDAITYALyGKTPRY---GRQENLRSVFAPGEDT----AEVSFTF 82

                 ....*.
gi 499171829  86 DNSNRL 91
Cdd:cd03279   83 QLGGKK 88
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
880-952 4.08e-06

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 50.73  E-value: 4.08e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499171829 880 LSGGEKTlvALSVLFSILKVSafPLVILDEAESALDPANVERFANIIKTASKNTQFLIITHRQGTMMKCDMLL 952
Cdd:PRK13657 472 LSGGERQ--RLAIARALLKDP--PILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRIL 540
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
212-835 4.14e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.07  E-value: 4.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  212 EKAQQFIRVKNELKELELAVLVGEYLQAQTELDKFNFQINSSEHdfkihepQLELLEEQIVIFNSRFHSADMQSNELQKE 291
Cdd:COG4913   259 ELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRA-------ELARLEAELERLEARLDALREELDELEAQ 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  292 LQDI-YQKINELEQRKVIIDVQLRQgfSQKDEKQKAAALKKLILVDQTQLDGFENQLSNSKTTITDLEKLINEQKSLVDQ 370
Cdd:COG4913   332 IRGNgGDRLEQLEREIERLERELEE--RERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAE 409
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  371 IKLQIEKNTADLiyqRSLKTIIElqtnELKKtNNANI----------LVKNA------------------------NALT 416
Cdd:COG4913   410 AEAALRDLRREL---RELEAEIA----SLER-RKSNIparllalrdaLAEALgldeaelpfvgelievrpeeerwrGAIE 481
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  417 GILNTLGTFLKFDKQYEKAILKA-----LGKSIGYLVVNNNNAAIQAIDFLVKNEIGKVTFLPlddvasdtkitNEHMEI 491
Cdd:COG4913   482 RVLGGFALTLLVPPEHYAAALRWvnrlhLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKP-----------HPFRAW 550
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  492 LKQLdgfLGVCSDHVKCDplfqpvvntllaqviiakdlnSAINLSNYTyklyRIVTLDGeTVYAGGiinGGFEKtnlsDG 571
Cdd:COG4913   551 LEAE---LGRRFDYVCVD---------------------SPEELRRHP----RAITRAG-QVKGNG---TRHEK----DD 594
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  572 --YLSSASL---DNEQNINKLENNERELKKELTELEVKLDEMNRKLK--------YEELLQAKFIE-RIVQIKKIILELK 637
Cdd:COG4913   595 rrRIRSRYVlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDalqerreaLQRLAEYSWDEiDVASAEREIAELE 674
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  638 MEYEQLTNTTFDGkkavaseAELIHSLNSAWAKRDEINSKLKLNQELKLQLAKTIKQSEEKI---------------VDL 702
Cdd:COG4913   675 AELERLDASSDDL-------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELdelqdrleaaedlarLEL 747
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  703 RALLDEQRAKL-VSAREGKIR--FENTIQNITEKINSVYKMTMEfaianhnkpvklsSMQAHNKiaKLQNQLNEMGVinm 779
Cdd:COG4913   748 RALLEERFAAAlGDAVERELRenLEERIDALRARLNRAEEELER-------------AMRAFNR--EWPAETADLDA--- 809
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  780 eSIAEISEKQKRFDDINA----EYE---------SAQQAVENLQKAI-TEIDEIASNefdqlIQKLNQEL 835
Cdd:COG4913   810 -DLESLPEYLALLDRLEEdglpEYEerfkellneNSIEFVADLLSKLrRAIREIKER-----IDPLNDSL 873
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
880-952 4.25e-06

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213211 [Multi-domain]  Cd Length: 221  Bit Score: 49.03  E-value: 4.25e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499171829 880 LSGGEKTLVALSVlfSILKVSafPLVILDEAESALDPANVERFANIIKTASKNTQFLIITHRQGTMMKCDMLL 952
Cdd:cd03244  140 LSVGQRQLLCLAR--ALLRKS--KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRIL 208
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
880-952 4.37e-06

ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213220 [Multi-domain]  Cd Length: 236  Bit Score: 49.15  E-value: 4.37e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499171829 880 LSGGEKTLVALSVLfsILKvsAFPLVILDEAESALDpANVER--FANIIKtASKNTQFLIITHRQGTMMKCDMLL 952
Cdd:cd03253  138 LSGGEKQRVAIARA--ILK--NPPILLLDEATSALD-THTEReiQAALRD-VSKGRTTIVIAHRLSTIVNADKII 206
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
4-841 4.92e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.45  E-value: 4.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   4 LKRFRAYGFKSYADEItIDFTHSMTGIVGPNGSGKSNVVDA----LKWVLGERsmkhLRSKSGDDMIFFGSKDkpasklA 79
Cdd:PRK03918   3 IEELKIKNFRSHKSSV-VEFDDGINLIIGQNGSGKSSILEAilvgLYWGHGSK----PKGLKKDDFTRIGGSG------T 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  80 EIELTFDNSNR---LLHDSRKEISVMRRvyrgSGQSEYFINSNPATLKEISGIF-ADIGLekGSLgIISQGSVSWFVEAK 155
Cdd:PRK03918  72 EIELKFEKNGRkyrIVRSFNRGESYLKY----LDGSEVLEEGDSSVREWVERLIpYHVFL--NAI-YIRQGEIDAILESD 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 156 pEERRKIFEDASGIGRYTKRKE---EVVNQLNRTLINLKQvsvvlnELKKDLKKLTLQAEKAQQFIRVKNELKEL----- 227
Cdd:PRK03918 145 -ESREKVVRQILGLDDYENAYKnlgEVIKEIKRRIERLEK------FIKRTENIEELIKEKEKELEEVLREINEIsselp 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 228 ELAVLVGEYLQAQTELDKFNFQINSSEHDFKIHEPQLELLEEQIVIFNSRFhsadmqsNELQKELQDIYQKINELEQRKV 307
Cdd:PRK03918 218 ELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERI-------EELKKEIEELEEKVKELKELKE 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 308 IIDVQLRQGFSQKDEKQKAAALKKLILVDQTQLDGFENQLSNSKTTITDLEKLINEQKSLVDqiKLQIEKNTADLiYQRS 387
Cdd:PRK03918 291 KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK--RLEELEERHEL-YEEA 367
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 388 LKTIIELQTNELKKTNNanilvknanaltgilnTLGTFLKFDKQYEKAILKalgksigylvvnnnnaaiqaidflVKNEI 467
Cdd:PRK03918 368 KAKKEELERLKKRLTGL----------------TPEKLEKELEELEKAKEE------------------------IEEEI 407
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 468 GKVTflplDDVASDTKITNEHMEILKQLDGFLGVCsdhvkcdplfqPVVNTLLAQVIiAKDLnsainLSNYTYKLYRIvt 547
Cdd:PRK03918 408 SKIT----ARIGELKKEIKELKKAIEELKKAKGKC-----------PVCGRELTEEH-RKEL-----LEEYTAELKRI-- 464
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 548 ldgetvyaggiinggfektnlsdgylssasldnEQNINKLENNERELKKELTELEVKLDEMNRKLKYEELL-QAKFIERi 626
Cdd:PRK03918 465 ---------------------------------EKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAeQLKELEE- 510
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 627 vQIKKIILE----LKMEYEQLTNTTFDGKKAVASEAELIHSLNSAWAKRDEINSKLKlnqELKLQLAKTIKQSEEKIVDL 702
Cdd:PRK03918 511 -KLKKYNLEelekKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLD---ELEEELAELLKELEELGFES 586
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 703 RALLDEQRAKLVSAREGKIRFENTIQNITEKINSVYKM--TMEFAIANHNKpvklssmqAHNKIAKLQNQLNEMGVINME 780
Cdd:PRK03918 587 VEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLeeELDKAFEELAE--------TEKRLEELRKELEELEKKYSE 658
                        810       820       830       840       850       860
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499171829 781 SiaEISEKQKRFDDINAEYESAQQAVENLQKaitEIDEIASNefdqlIQKLNQELPKTFKY 841
Cdd:PRK03918 659 E--EYEELREEYLELSRELAGLRAELEELEK---RREEIKKT-----LEKLKEELEEREKA 709
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
880-948 5.32e-06

Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 48.41  E-value: 5.32e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 880 LSGGEKTLVALSVLFsilkVSAFPLVILDEAESALDPANVERFANIIKT-ASKNTQFLIITHRQGTMMKC 948
Cdd:cd03226  127 LSGGQKQRLAIAAAL----LSGKDLLIFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKV 192
COG1106 COG1106
ATPase/GTPase, AAA15 family [General function prediction only];
3-91 6.99e-06

ATPase/GTPase, AAA15 family [General function prediction only];


Pssm-ID: 440723 [Multi-domain]  Cd Length: 330  Bit Score: 49.27  E-value: 6.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   3 FLKRFRAYGFKSYADEITIDFTHS------MTGIVGPNGSGKSNVVDALKWvlgersMKH--LRSKSGDDMIF--FGSKD 72
Cdd:COG1106    1 MLISFSIENFRSFKDELTLSMVASglrllrVNLIYGANASGKSNLLEALYF------LRNlvLNSSQPGDKLVepFLLDS 74
                         90
                 ....*....|....*....
gi 499171829  73 KPASKLAEIELTFDNSNRL 91
Cdd:COG1106   75 ESKNEPSEFEILFLLDGVR 93
recF PRK00064
recombination protein F; Reviewed
2-161 8.56e-06

recombination protein F; Reviewed


Pssm-ID: 234608 [Multi-domain]  Cd Length: 361  Bit Score: 49.00  E-value: 8.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   2 VFLKRFRAYGFKSYAdEITIDFTHSMTGIVGPNGSGKSNVVDALkWVLGE-RSmkhLRSKSGDDMIFFGSKDkpasklAE 80
Cdd:PRK00064   1 MYLTRLSLTDFRNYE-ELDLELSPGVNVLVGENGQGKTNLLEAI-YLLAPgRS---HRTARDKELIRFGAEA------AV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  81 IELTFDNSNRllhDSRKEISVmrrvyRGSGQSEYFINSNPA-TLKEISGIF-------ADIGLEKGSlgiisqgsvswfv 152
Cdd:PRK00064  70 IHGRVEKGGR---ELPLGLEI-----DKKGGRKVRINGEPQrKLAELAGLLnvvlftpEDLRLVKGG------------- 128

                 ....*....
gi 499171829 153 eakPEERRK 161
Cdd:PRK00064 129 ---PSERRR 134
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
804-940 1.07e-05

Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];


Pssm-ID: 442812 [Multi-domain]  Cd Length: 359  Bit Score: 48.85  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 804 QAVENLQKAITEIDEiasnEFDQLIQKLNQELPKTFKYLFGGGSCQIRYT-DPSNVLVSGIDVFANppGKNIANLMLLSG 882
Cdd:COG3593   92 EDKEELEEALEELNE----ELKEALKALNELLSEYLKELLDGLDLELELSlDELEDLLKSLSLRIE--DGKELPLDRLGS 165
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499171829 883 GEKTLVALSVLFSILKV---SAFPLVILDEAESALDPANVERFANIIKT-ASKNTQFLIITH 940
Cdd:COG3593  166 GFQRLILLALLSALAELkraPANPILLIEEPEAHLHPQAQRRLLKLLKElSEKPNQVIITTH 227
COG3950 COG3950
Predicted ATP-binding protein involved in virulence [General function prediction only];
3-99 1.17e-05

Predicted ATP-binding protein involved in virulence [General function prediction only];


Pssm-ID: 443150 [Multi-domain]  Cd Length: 276  Bit Score: 48.07  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   3 FLKRFRAYGFKSYADeITIDFTH--SMTGIVGPNGSGKSNVVDALKWVLGeRSMKHLRSKSGDDMIFFGSKDKPASKLae 80
Cdd:COG3950    2 RIKSLTIENFRGFED-LEIDFDNppRLTVLVGENGSGKTTLLEAIALALS-GLLSRLDDVKFRKLLIRNGEFGDSAKL-- 77
                         90
                 ....*....|....*....
gi 499171829  81 ieLTFDNSNRLLHDSRKEI 99
Cdd:COG3950   78 --ILYYGTSRLLLDGPLKK 94
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
880-940 1.26e-05

ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443308 [Multi-domain]  Cd Length: 206  Bit Score: 47.09  E-value: 1.26e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499171829 880 LSGGEKTLVALSVLFsilkVSAFPLVILDEAESALDPANVERFANIIKTASKNTQ-FLIITH 940
Cdd:COG4133  132 LSAGQKRRVALARLL----LSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGaVLLTTH 189
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
880-949 1.36e-05

ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444012 [Multi-domain]  Cd Length: 563  Bit Score: 48.99  E-value: 1.36e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 880 LSGGEKTLVALSVLFsiLKVSafPLVILDEAESALDPANVERFANIIKTASKNTQFLIITHRQGTMMKCD 949
Cdd:COG4988  474 LSGGQAQRLALARAL--LRDA--PLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQAD 539
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
865-940 1.46e-05

AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.


Pssm-ID: 433102 [Multi-domain]  Cd Length: 303  Bit Score: 48.15  E-value: 1.46e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499171829  865 VFANPPGKNIANLMLLSGGEKTLVALSVLFSILKVSAfPLVILDEAESALDPANVERFANIIK-TASKNTQFLIITH 940
Cdd:pfam13304 222 ILLENGGGGELPAFELSDGTKRLLALLAALLSALPKG-GLLLIDEPESGLHPKLLRRLLELLKeLSRNGAQLILTTH 297
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
591-942 1.86e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 1.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 591 ERELKKELTELEVKLDEMNRKLKYEELLQAKFIERIVQIKKIILELKMEYEQLTNTTFDGKKAVASEAELIHSLNsAWAK 670
Cdd:COG4717  318 EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALE-QAEE 396
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 671 RDEINSKLklnQELKLQLaktikqsEEKIVDLRALLDEQRAKLVSAREGKIrfENTIQNITEKINsvykmtmefaianhn 750
Cdd:COG4717  397 YQELKEEL---EELEEQL-------EELLGELEELLEALDEEELEEELEEL--EEELEELEEELE--------------- 449
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 751 kpvklssmQAHNKIAKLQNQLNEmgvinMESIAEISEKQKRFDDINAEYESAQQAVENLQKAITEIDEIASNEFDQLIQK 830
Cdd:COG4717  450 --------ELREELAELEAELEQ-----LEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPP 516
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 831 LNQELPKTFKYLFGGGSCQIRYTDPSNVLVSGIDVFANPPGKnianlmlLSGGEKTLVALSVLFSILK-VSAFPL-VILD 908
Cdd:COG4717  517 VLERASEYFSRLTDGRYRLIRIDEDLSLKVDTEDGRTRPVEE-------LSRGTREQLYLALRLALAElLAGEPLpLILD 589
                        330       340       350
                 ....*....|....*....|....*....|....
gi 499171829 909 EAESALDPANVERFANIIKTASKNTQFLIITHRQ 942
Cdd:COG4717  590 DAFVNFDDERLRAALELLAELAKGRQVIYFTCHE 623
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
880-952 2.02e-05

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 48.68  E-value: 2.02e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499171829 880 LSGGEKTLVALSvlfsilkvSAF----PLVILDEAESALDPANVERFANIIKTASKNTQFLIITHRQGTMMKCDMLL 952
Cdd:COG2274  612 LSGGQRQRLAIA--------RALlrnpRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRII 680
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
880-941 2.22e-05

First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.


Pssm-ID: 213183 [Multi-domain]  Cd Length: 163  Bit Score: 45.88  E-value: 2.22e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499171829 880 LSGGEKTLVAlsvlfsILKVSAFP--LVILDEAESALDPANVERFANIIKT-ASKNTQFLIITHR 941
Cdd:cd03216   83 LSVGERQMVE------IARALARNarLLILDEPTAALTPAEVERLFKVIRRlRAQGVAVIFISHR 141
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
880-952 3.32e-05

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444078 [Multi-domain]  Cd Length: 605  Bit Score: 47.89  E-value: 3.32e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499171829 880 LSGGEKTLVALSVlfSILKvsAFPLVILDEAESALDPANvERfaNI---IKTASKNTQFLIITHRQGTMMKCDMLL 952
Cdd:COG5265  495 LSGGEKQRVAIAR--TLLK--NPPILIFDEATSALDSRT-ER--AIqaaLREVARGRTTLVIAHRLSTIVDADEIL 563
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
572-698 1.34e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 45.97  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 572 YLSSASLDNEQNINKLENNERELKKELTELEVKLDEMNRklKYEELLQaKFIERIVQIKKIILELKMEYEQLTNTTfdgK 651
Cdd:PRK00409 510 LIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEK--LKEELEE-KKEKLQEEEDKLLEEAEKEAQQAIKEA---K 583
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499171829 652 KAVA----SEAELIHSLNSAWAKRDEINSKLKLNQELKLQLAKTIKQSEEK 698
Cdd:PRK00409 584 KEADeiikELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQ 634
COG4637 COG4637
Predicted ATPase [General function prediction only];
880-940 1.36e-04

Predicted ATPase [General function prediction only];


Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 45.31  E-value: 1.36e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499171829 880 LSGGekTLVALSVLFSILKVSAFPLVILDEAESALDPANVERFANIIKTASKNTQFLIITH 940
Cdd:COG4637  259 LSDG--TLRFLALLAALLSPRPPPLLCIEEPENGLHPDLLPALAELLREASERTQVIVTTH 317
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
880-949 1.62e-04

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD


Pssm-ID: 274323 [Multi-domain]  Cd Length: 529  Bit Score: 45.36  E-value: 1.62e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  880 LSGGEKTLVALSVLFsiLKVSafPLVILDEAESALDPANVERFANIIKTASKNTQFLIITHRQGTMMKCD 949
Cdd:TIGR02857 459 LSGGQAQRLALARAF--LRDA--PLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALAD 524
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
879-941 1.81e-04

ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 45.18  E-value: 1.81e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499171829 879 LLSGGEKTLVALSVLFsILKvsafP-LVILDEAESALDPANVERFANIIKTASKNTQFLIITHR 941
Cdd:COG4178  485 VLSLGEQQRLAFARLL-LHK----PdWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
238-422 1.98e-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: 44.75  E-value: 1.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 238 QAQTELDKFNFQINSSEHDFKIHEPQLELLEEQIVIFNSRFHSADMQSNELQKELQDIYQKINELEQRKV--------II 309
Cdd:COG4942   31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEaqkeelaeLL 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 310 DVQLRQG--------FSQKDEKQ---KAAALKKLILVDQTQLDGFENQLSNSKTTITDLEKLINEQKSLVDQikLQIEKN 378
Cdd:COG4942  111 RALYRLGrqpplallLSPEDFLDavrRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE--LEEERA 188
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 499171829 379 TADLIYQRSLKTIIELQTNELKKTNNANILVKNANALTGILNTL 422
Cdd:COG4942  189 ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
876-952 2.06e-04

lipid A ABC transporter ATP-binding protein/permease MsbA;


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 45.01  E-value: 2.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 876 NLMLLSGGEKTLVALSVlfSILKVSafPLVILDEAESALDPANvERfanIIKTA----SKNTQFLIITHRQGTMMKCDML 951
Cdd:PRK11176 477 NGVLLSGGQRQRIAIAR--ALLRDS--PILILDEATSALDTES-ER---AIQAAldelQKNRTSLVIAHRLSTIEKADEI 548

                 .
gi 499171829 952 L 952
Cdd:PRK11176 549 L 549
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
880-942 2.69e-04

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 42.53  E-value: 2.69e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499171829 880 LSGGEKTLVALSVLFsILKvsafP-LVILDEAESALDPANVERFANIIKTASknTQFLIITHRQ 942
Cdd:cd03223   92 LSGGEQQRLAFARLL-LHK----PkFVFLDEATSALDEESEDRLYQLLKELG--ITVISVGHRP 148
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
879-952 3.41e-04

ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.


Pssm-ID: 213215 [Multi-domain]  Cd Length: 226  Bit Score: 43.23  E-value: 3.41e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499171829 879 LLSGGEKTLVALSVLFsilkVSAFPLVILDEAESALDPANVERFANIIKTASKNTQFLIITHRQGTMMKCDMLL 952
Cdd:cd03248  150 QLSGGQKQRVAIARAL----IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQIL 219
ABC_RecF cd03242
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ...
4-187 3.48e-04

ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213209 [Multi-domain]  Cd Length: 270  Bit Score: 43.44  E-value: 3.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   4 LKRFRAYgfksyaDEITIDFTHSMTGIVGPNGSGKSNVVDALKWVLGERSmkhLRSKSGDDMIffgSKDKPAsklAEIEL 83
Cdd:cd03242    6 LRNFRNY------AELELEFEPGVTVLVGENAQGKTNLLEAISLLATGKS---HRTSRDKELI---RWGAEE---AKISA 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  84 TFDNSNRLLhdsrKEISVMRRVYRGSGQseyfINSNPA-TLKEISGIF-------ADIGLEKGSlgiisqgsvswfveak 155
Cdd:cd03242   71 VLERQGGEL----ALELTIRSGGGRKAR----LNGIKVrRLSDLLGVLnavwfapEDLELVKGS---------------- 126
                        170       180       190
                 ....*....|....*....|....*....|..
gi 499171829 156 PEERRKIFEDAsgIGRYTKRKEEVVNQLNRTL 187
Cdd:cd03242  127 PADRRRFLDRL--LGQLEPAYAHVLSEYQKAL 156
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
880-941 3.50e-04

ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444011 [Multi-domain]  Cd Length: 569  Bit Score: 44.37  E-value: 3.50e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499171829 880 LSGGEKTLVALS-VLfsilkVSAFPLVILDEAESALDPANVERFANIIKTASKNTQFLIITHR 941
Cdd:COG4987  472 LSGGERRRLALArAL-----LRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHR 529
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
573-720 3.59e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.05  E-value: 3.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 573 LSSASLDNEQNINKLENNERELKKELTELEVKLDEMNRKLK---------------YEELLQAK----FIERIVQIKKI- 632
Cdd:COG3883   49 LNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraralyrsggsvsyLDVLLGSEsfsdFLDRLSALSKIa 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 633 ------ILELKMEYEQLTNttfDGKKAVASEAELIHSLNSAWAKRDEINSKLKLNQELKLQLAKTIKQSEEKIVDLRALL 706
Cdd:COG3883  129 dadadlLEELKADKAELEA---KKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
                        170
                 ....*....|....
gi 499171829 707 DEQRAKLVSAREGK 720
Cdd:COG3883  206 AAAEAAAAAAAAAA 219
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
579-734 4.11e-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: 43.98  E-value: 4.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 579 DNEQNINKLENNERELKKELTELEVKLDEmnRKLKYEELLQA--------------------KFIERIVQIKKIILELKM 638
Cdd:COG4942   73 ALEQELAALEAELAELEKEIAELRAELEA--QKEELAELLRAlyrlgrqpplalllspedflDAVRRLQYLKYLAPARRE 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 639 EYEQLTNTTfdgkkavaseAELIHSLNSAWAKRDEINSKLKLNQELKLQLAKTIKQSEEKIVDLRALLDEQRAKLVSARE 718
Cdd:COG4942  151 QAEELRADL----------AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
                        170
                 ....*....|....*.
gi 499171829 719 GKIRFENTIQNITEKI 734
Cdd:COG4942  221 EAEELEALIARLEAEA 236
recf TIGR00611
recF protein; All proteins in this family for which functions are known are DNA binding ...
3-59 5.77e-04

recF protein; All proteins in this family for which functions are known are DNA binding proteins that assist the filamentation of RecA onto DNA for the initiation of recombination or recombinational repair. 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: 273173 [Multi-domain]  Cd Length: 365  Bit Score: 43.50  E-value: 5.77e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 499171829    3 FLKRFRAYgfksyaDEITIDFTHSMTGIVGPNGSGKSNVVDALkWVLGersmkHLRS 59
Cdd:TIGR00611   7 ELTDFRNY------DAVDLELSPGVNVIVGPNGQGKTNLLEAI-YYLA-----LGRS 51
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
858-952 6.27e-04

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 41.82  E-value: 6.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 858 VLVSGIDVFANPP---GKNIANLM-------------LLSGGEKTLVALSvlfsilkvSAF---P-LVILDEAESALDPA 917
Cdd:cd03246   59 VRLDGADISQWDPnelGDHVGYLPqddelfsgsiaenILSGGQRQRLGLA--------RALygnPrILVLDEPNSHLDVE 130
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 499171829 918 NVERFANIIKTASK-NTQFLIITHRQGTMMKCDMLL 952
Cdd:cd03246  131 GERALNQAIAALKAaGATRIVIAHRPETLASADRIL 166
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
880-928 6.85e-04

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 42.17  E-value: 6.85e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 499171829 880 LSGGEKTLVALSVLFsilkVSAFPLVILDEAESALDPANVERFANIIKT 928
Cdd:PRK13539 128 LSAGQKRRVALARLL----VSNRPIWILDEPTAALDAAAVALFAELIRA 172
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
880-949 8.16e-04

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 43.23  E-value: 8.16e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499171829 880 LSGGEKTLVALSvlfsilkvSAF----PLVILDEAESALDPANvER--FANiIKTASKNTQFLIITHRQGTMMKCD 949
Cdd:COG1132  477 LSGGQRQRIAIA--------RALlkdpPILILDEATSALDTET-EAliQEA-LERLMKGRTTIVIAHRLSTIRNAD 542
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
27-96 8.54e-04

AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.


Pssm-ID: 433102 [Multi-domain]  Cd Length: 303  Bit Score: 42.38  E-value: 8.54e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499171829   27 MTGIVGPNGSGKSNVVDALKWVLGERSM-KHLRSKSGDDMIFFGSKDKPASKLAEIELTFDNSNRLLHDSR 96
Cdd:pfam13304   1 INVLIGPNGSGKSNLLEALRFLADFDALvIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLEDGVR 71
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
880-952 1.09e-03

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213269 [Multi-domain]  Cd Length: 207  Bit Score: 41.63  E-value: 1.09e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499171829 880 LSGGEKTLVALSVlfSILKvsAFPLVILDEAESALDPANVERFANIIKTASKNTQFLIITHRQGTMMKCDMLL 952
Cdd:cd03369  126 LSQGQRQLLCLAR--ALLK--RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKIL 194
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
859-952 1.16e-03

ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213221 [Multi-domain]  Cd Length: 229  Bit Score: 41.44  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 859 LVSGIDVFANPPGKNianlmlLSGGEKTLvaLSVLFSILKVSafPLVILDEAESALDPANVERFANIIKTASKNTQFLII 938
Cdd:cd03254  125 LPNGYDTVLGENGGN------LSQGERQL--LAIARAMLRDP--KILILDEATSNIDTETEKLIQEALEKLMKGRTSIII 194
                         90
                 ....*....|....
gi 499171829 939 THRQGTMMKCDMLL 952
Cdd:cd03254  195 AHRLSTIKNADKIL 208
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
880-940 1.22e-03

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 41.05  E-value: 1.22e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499171829 880 LSGGEKTLVALSVLFSILKV--SAFPLVILDEAESALDPANVE-RFANIIKTAS--KNTQFLIITH 940
Cdd:cd03240  116 CSGGEKVLASLIIRLALAETfgSNCGILALDEPTTNLDEENIEeSLAEIIEERKsqKNFQLIVITH 181
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
354-827 1.24e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 43.12  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   354 ITDLEKLINEQKSLVDQIKLQI---EKNTADLIYQRSLKTIIELQTNELKKTNNANILVKNANALtgiLNTLGTFLKFDK 430
Cdd:TIGR01612 1131 IKALEEIKKKSENYIDEIKAQIndlEDVADKAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKL---LNEIAEIEKDKT 1207
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   431 QYE--KAILKALGKSIGYLVvnnnnaaIQAIDflvkneigkvtflplddvasDTKITNEHMeiLKQLDGFLgvcSDHVKC 508
Cdd:TIGR01612 1208 SLEevKGINLSYGKNLGKLF-------LEKID--------------------EEKKKSEHM--IKAMEAYI---EDLDEI 1255
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   509 DPLFQPVVNTLLAQVIIAKDLNSaINLSNYTYKLYRIVTLDGETVYAG------GIINGGFEKTNLSD------GYLSSA 576
Cdd:TIGR01612 1256 KEKSPEIENEMGIEMDIKAEMET-FNISHDDDKDHHIISKKHDENISDirekslKIIEDFSEESDINDikkelqKNLLDA 1334
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   577 SLDNEQ------------NINKLeNNERELKKELTELEVKLDEMNRKLKYEELLQAKFIERIVQikKIILElkmEYEQLT 644
Cdd:TIGR01612 1335 QKHNSDinlylneianiyNILKL-NKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKD--DINLE---ECKSKI 1408
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   645 NTTFDGK------KAVASEAELIHS----LNSAWAKRDEINSKLKLN-QELKLQLAKT------------------IKQS 695
Cdd:TIGR01612 1409 ESTLDDKdideciKKIKELKNHILSeesnIDTYFKNADENNENVLLLfKNIEMADNKSqhilkikkdnatndhdfnINEL 1488
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   696 EEKIVDLRALLDEQRAKLVSAREGKIRFENTIQNITEKINSVYkmtmEFAIANHNKPVKLSSMQAHNKIAKLQNQLNEMG 775
Cdd:TIGR01612 1489 KEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYS----ALAIKNKFAKTKKDSEIIIKEIKDAHKKFILEA 1564
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 499171829   776 VINMESIAEISEKQKRFDDINAEYESA-------QQAVENLQKAITEIDEIASNEFDQL 827
Cdd:TIGR01612 1565 EKSEQKIKEIKKEKFRIEDDAAKNDKSnkaaidiQLSLENFENKFLKISDIKKKINDCL 1623
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
880-942 1.48e-03

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 40.97  E-value: 1.48e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499171829 880 LSGGEKTLValsvlfSILKVSAF-P-LVILDEAESALDPANVERFANIIKT-ASKNTQFLIITHRQ 942
Cdd:cd03217  105 FSGGEKKRN------EILQLLLLePdLAILDEPDSGLDIDALRLVAEVINKlREEGKSVLIITHYQ 164
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
579-834 1.52e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.31  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  579 DNEQNINKLENNERELKKELTELEVKLDEMNRKLKYEELLQAKFIERIVQIKKIILELKMEYEQLTNTTFDGKKAVASEA 658
Cdd:TIGR04523 135 ENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNK 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  659 ELIHSLNSAWAKRDEINSKLKLNQELKLQLAKTIKQSEEKIVDLRALLDEQRAKLvsaREGKIRFENTIQNITEKINSVY 738
Cdd:TIGR04523 215 SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQL---SEKQKELEQNNKKIKELEKQLN 291
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  739 KMTMEFAIANHNKPVKLSSM---------------------------QAHNKIAKLQNQLNEMGVINMESIAEISEKQKR 791
Cdd:TIGR04523 292 QLKSEISDLNNQKEQDWNKElkselknqekkleeiqnqisqnnkiisQLNEQISQLKKELTNSESENSEKQRELEEKQNE 371
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 499171829  792 FDDINAEYESAQQAVENLQKAITEID------EIASNEFDQLIQKLNQE 834
Cdd:TIGR04523 372 IEKLKKENQSYKQEIKNLESQINDLEskiqnqEKLNQQKDEQIKKLQQE 420
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
586-823 1.60e-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: 42.47  E-value: 1.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   586 KLENNERELKKELTELEVKLDEMnrklkyEELLQAKFIERivqiKKIILELKMEYEQLtnttfDGKKAVASEAELIHSLN 665
Cdd:pfam01576   65 RLAARKQELEEILHELESRLEEE------EERSQQLQNEK----KKMQQHIQDLEEQL-----DEEEAARQKLQLEKVTT 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   666 SAWAKRDEINSKLKLNQELKLQlaKTIKQSEEKIVDLRALLDEQRAKLVSAREGKIRFENTIQNITEKINSVYKMTMEFA 745
Cdd:pfam01576  130 EAKIKKLEEDILLLEDQNSKLS--KERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELE 207
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499171829   746 IANhnKPVKLSSMQAHNKIAKLQNQLNEMGVINMESIAEISEKQKRFDDINAEYESAQQAVENLQKAITEIDEIASNE 823
Cdd:pfam01576  208 KAK--RKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESE 283
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
4-97 1.90e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   4 LKRFRAYGFKSYADeITIDFTHSMTGIVGPNGSGKSNVVDALKWVL-GERSMkhlrSKSGDDMIFFGSKDkpasklAEIE 82
Cdd:PRK02224   3 FDRVRLENFKCYAD-ADLRLEDGVTVIHGVNGSGKSSLLEACFFALyGSKAL----DDTLDDVITIGAEE------AEIE 71
                         90
                 ....*....|....*
gi 499171829  83 LTFDNSNRLLHDSRK 97
Cdd:PRK02224  72 LWFEHAGGEYHIERR 86
ABC_SMC5_euk cd03277
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ...
6-91 3.46e-03

ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213244 [Multi-domain]  Cd Length: 213  Bit Score: 39.89  E-value: 3.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   6 RFRAYGFKSYaDEITIDFTHSMTGIVGPNGSGKSNVVDALKWVLGERSmKHL-RSKSGDDMIFFGSKdkpaSKLAEIELt 84
Cdd:cd03277    5 RIKLENFVTY-DETEFRPGPSLNMIIGPNGSGKSSIVCAICLGLGGKP-KLLgRAKKVGEFVKRGCD----EGTIEIEL- 77

                 ....*..
gi 499171829  85 FDNSNRL 91
Cdd:cd03277   78 YGNPGNI 84
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
880-952 4.05e-03

ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213218 [Multi-domain]  Cd Length: 234  Bit Score: 39.91  E-value: 4.05e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499171829 880 LSGGEKTLVALSVlfSILKVSafPLVILDEAESALDPANVERFANIIKTASKNTQFLIITHRQGTMMKCDMLL 952
Cdd:cd03251  139 LSGGQRQRIAIAR--ALLKDP--PILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIV 207
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
581-835 4.43e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 4.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 581 EQNINKLENNERELKKELTELEVKLDEMNRKLKYEELLQAKFIERIVQIKKIILELKMEYEQLtnttfdgkkavasEAEL 660
Cdd:COG4942   40 EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ-------------KEEL 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 661 IHSLNSAWAKRDEINSKLKLNQElklqlakTIKQSEEKIVDLRALLDEQRAKLVSAREGKIRFENTIQNITEKINsvykm 740
Cdd:COG4942  107 AELLRALYRLGRQPPLALLLSPE-------DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA----- 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 741 tmefaianhnkpvklssmQAHNKIAKLQNQLNEMgvinmesIAEISEKQKRFDDINAEYESAQQAVENLQKAITEIdeia 820
Cdd:COG4942  175 ------------------ELEALLAELEEERAAL-------EALKAERQKLLARLEKELAELAAELAELQQEAEEL---- 225
                        250
                 ....*....|....*
gi 499171829 821 snefDQLIQKLNQEL 835
Cdd:COG4942  226 ----EALIARLEAEA 236
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
857-940 4.96e-03

ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213197 [Multi-domain]  Cd Length: 173  Bit Score: 38.92  E-value: 4.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 857 NVLVSGIDVFANPP--GKNIA----------------NLMLlSGGEKTLVALsvlfsilkVSAF----PLVILDEAESAL 914
Cdd:cd03230   56 EIKVLGKDIKKEPEevKRRIGylpeepslyenltvreNLKL-SGGMKQRLAL--------AQALlhdpELLILDEPTSGL 126
                         90       100
                 ....*....|....*....|....*..
gi 499171829 915 DPANVERFANIIKT-ASKNTQFLIITH 940
Cdd:cd03230  127 DPESRREFWELLRElKKEGKTILLSSH 153
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
880-926 5.01e-03

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 39.26  E-value: 5.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 499171829  880 LSGGEKTLVALSVLFsilkVSAFPLVILDEAESALDPANVERFANII 926
Cdd:TIGR01189 128 LSAGQQRRLALARLW----LSRRPLWILDEPTTALDKAGVALLAGLL 170
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
583-834 5.64e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.89  E-value: 5.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 583 NINKLENNERELKKELTELEVKLDEMNRKLKYeelLQAKFIERIVQIKKIILELKmeyeqltnttfdgkkavaseaELIh 662
Cdd:COG1340    9 SLEELEEKIEELREEIEELKEKRDELNEELKE---LAEKRDELNAQVKELREEAQ---------------------ELR- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 663 slnsawAKRDEINSKLKLNQELKLQLAKTIKQSEEKIVDLRALLDEQRAKLVSaregkirfentIQNITEKINSvykmtM 742
Cdd:COG1340   64 ------EKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGS-----------IDKLRKEIER-----L 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 743 EFAIanHNKPVKLS-SMQAHNKIAKLQNQLNEMGVIN------MESIAEISEKQKRFDDINAE----YESAQQAVENLQK 811
Cdd:COG1340  122 EWRQ--QTEVLSPEeEKELVEKIKELEKELEKAKKALekneklKELRAELKELRKEAEEIHKKikelAEEAQELHEEMIE 199
                        250       260
                 ....*....|....*....|....*....
gi 499171829 812 AITEIDEI------ASNEFDQLIQKLNQE 834
Cdd:COG1340  200 LYKEADELrkeadeLHKEIVEAQEKADEL 228
PRK12704 PRK12704
phosphodiesterase; Provisional
585-698 6.65e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 6.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 585 NKLENNERELKKELTELEVKLDEMNRKLKYEELLQAKFIERIVQIKKIILELKMEYEQLTNTTfdgkkavASEAelihsl 664
Cdd:PRK12704  89 KRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLT-------AEEA------ 155
                         90       100       110
                 ....*....|....*....|....*....|....
gi 499171829 665 nsawakRDEINSKLKlnQELKLQLAKTIKQSEEK 698
Cdd:PRK12704 156 ------KEILLEKVE--EEARHEAAVLIKEIEEE 181
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
242-382 6.85e-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: 39.14  E-value: 6.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 242 ELDKfnfQINSSEHDFKIHEPQLELLEEQIVIFNSRFHSADMQSNELQKELQDIYQKINELEQRKVIIDVQLRQGFSQKD 321
Cdd:COG1579   14 ELDS---ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE 90
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499171829 322 ----EKQKAAALKKLILVDQTQLDgFENQLSNSKTTITDLEKLINEQKSLVDQIKLQIEKNTADL 382
Cdd:COG1579   91 yealQKEIESLKRRISDLEDEILE-LMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
AAA_29 pfam13555
P-loop containing region of AAA domain;
15-49 7.00e-03

P-loop containing region of AAA domain;


Pssm-ID: 433304 [Multi-domain]  Cd Length: 61  Bit Score: 36.04  E-value: 7.00e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 499171829   15 YADEITIDFT-HSMTGIVGPNGSGKSNVVDALKWVL 49
Cdd:pfam13555  11 TFDGHTIPIDpRGNTLLTGPSGSGKSTLLDAIQTLL 46
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
658-835 7.60e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 7.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 658 AELIHSLNSAWAKRDEINSKLKLNQELKLQLAKTIKQSEEKIVDLRALLDEQRAKLVSAREgkirfentiqNITEKINSV 737
Cdd:COG3883   26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE----------ELGERARAL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 738 YK----MTMEFAIANHNKPVK-LSSMQAHNKIAKLQNQ-LNEMgvinMESIAEISEKQKRFDDINAEYESAQQAVENLQK 811
Cdd:COG3883   96 YRsggsVSYLDVLLGSESFSDfLDRLSALSKIADADADlLEEL----KADKAELEAKKAELEAKLAELEALKAELEAAKA 171
                        170       180
                 ....*....|....*....|....
gi 499171829 812 AIteidEIASNEFDQLIQKLNQEL 835
Cdd:COG3883  172 EL----EAQQAEQEALLAQLSAEE 191
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
573-834 7.88e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.51  E-value: 7.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 573 LSSASLDNEQNINKLENNERELKKELTELEVKLDEMNRKLKYEELLQAKFIERIVQIKKIILELKMEYEQLTNTTFDGKK 652
Cdd:COG1340   20 LREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRK 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 653 AVASEAELIHSLNsawAKRDEINsKLklnqELKLQLAKTIKQSEEKIVDLRALLdeqrAKLVSAREGKIRFENTIQNITE 732
Cdd:COG1340  100 ELAELNKAGGSID---KLRKEIE-RL----EWRQQTEVLSPEEEKELVEKIKEL----EKELEKAKKALEKNEKLKELRA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829 733 KINSVYKMTMEFaianHNKPVKLS--SMQAHNKIAKLQNQLNEMGVINMESIAEISEKQKRFDDINAEYESAQQAVENLQ 810
Cdd:COG1340  168 ELKELRKEAEEI----HKKIKELAeeAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELR 243
                        250       260
                 ....*....|....*....|....
gi 499171829 811 KAITEIDEIASNEFDQLIQKLNQE 834
Cdd:COG1340  244 KELKKLRKKQRALKREKEKEELEE 267
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
563-829 8.66e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 39.84  E-value: 8.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  563 FEKTNLSDGY---LSSASLDN-EQNINKLENNERELKKELTELeVKLDEMNR------KLKYEEL---LQAK---FIERI 626
Cdd:pfam06160  70 FEAEELNDKYrfkKAKKALDEiEELLDDIEEDIKQILEELDEL-LESEEKNReeveelKDKYRELrktLLANrfsYGPAI 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  627 VQIKKIILELKMEYEQLTNTTFDGKKAVASE-----AELIHSLNSAWAKRDEINSKLKLN-----QELK----------- 685
Cdd:pfam06160 149 DELEKQLAEIEEEFSQFEELTESGDYLEAREvleklEEETDALEELMEDIPPLYEELKTElpdqlEELKegyremeeegy 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  686 ----LQLAKTIKQSEEKIVDLRALLDEQRAKLVSARegkirfentIQNITEKINSVYKmTMEFAIANHNkpvklssmQAH 761
Cdd:pfam06160 229 alehLNVDKEIQQLEEQLEENLALLENLELDEAEEA---------LEEIEERIDQLYD-LLEKEVDAKK--------YVE 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  762 NKIAKLQNQLNEMGVINMESIAEISEKQ-----------------KRFDDINAEYESAQQAVENLQKAITEIDEIASNEF 824
Cdd:pfam06160 291 KNLPEIEDYLEHAEEQNKELKEELERVQqsytlnenelervrgleKQLEELEKRYDEIVERLEEKEVAYSELQEELEEIL 370

                  ....*
gi 499171829  825 DQLIQ 829
Cdd:pfam06160 371 EQLEE 375
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
880-923 8.82e-03

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 38.63  E-value: 8.82e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 499171829 880 LSGGEKTLVALSVLFsilkVSAFPLVILDEAESALDPANVERFA 923
Cdd:cd03231  126 LSAGQQRRVALARLL----LSGRPLWILDEPTTALDKAGVARFA 165
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
157-420 9.22e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 40.03  E-value: 9.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   157 EERRKIFED--------ASGIGRYTKRKEevvnQLNRTLINLKQVSVVLNELKKDLKKLTLQA----EKAQQFIRVKNeL 224
Cdd:TIGR01612  751 KDLNKILEDfknkekelSNKINDYAKEKD----ELNKYKSKISEIKNHYNDQINIDNIKDEDAkqnyDKSKEYIKTIS-I 825
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   225 KELELAVLVGEYLQAQTEL----DKF-NFQINSSEHDFKIHEPQLELL--------EEQIVIFNSRFHSADMQSNELQKE 291
Cdd:TIGR01612  826 KEDEIFKIINEMKFMKDDFlnkvDKFiNFENNCKEKIDSEHEQFAELTnkikaeisDDKLNDYEKKFNDSKSLINEINKS 905
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829   292 LQDIYQKINELEQRKVIIDVQLRQGFSQKDEKQKAAALKKLI-----------LVDQTQLDGFENQLSNSKT-------- 352
Cdd:TIGR01612  906 IEEEYQNINTLKKVDEYIKICENTKESIEKFHNKQNILKEILnknidtikesnLIEKSYKDKFDNTLIDKINeldkafkd 985
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499171829   353 -TITDLEKLINEQKSLVDQIKLQIEKNTADLIYQrslktiielQTNELKKTNNaNILVKNANALTGILN 420
Cdd:TIGR01612  986 aSLNDYEAKNNELIKYFNDLKANLGKNKENMLYH---------QFDEKEKATN-DIEQKIEDANKNIPN 1044
cbiO PRK13640
energy-coupling factor transporter ATPase;
880-940 9.37e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 39.01  E-value: 9.37e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499171829 880 LSGGEKTLVALSvlfSILKVSAfPLVILDEAESALDPANVERFANIIKTASKNTQFLI--ITH 940
Cdd:PRK13640 144 LSGGQKQRVAIA---GILAVEP-KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVisITH 202
SbcC_Walker_B pfam13558
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ...
880-928 9.61e-03

SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.


Pssm-ID: 463921 [Multi-domain]  Cd Length: 90  Bit Score: 36.44  E-value: 9.61e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 499171829  880 LSGGEKTLVALSVLFSIL---------KVSAFPLVILDEAESALDPANVERFANIIKT 928
Cdd:pfam13558  33 LSGGEKQLLAYLPLAAALaaqygsaegRPPAPRLVFLDEAFAKLDEENIRTALELLRA 90
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
249-411 9.66e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.00  E-value: 9.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  249 QINSSEHDFKIHEPQLELLEEQIVIFNSRFHSADMQSNELQKELQDIYQKINELEQRKVIIDVQLRQGFSQKDEKQKAAA 328
Cdd:TIGR04523 350 ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE 429
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499171829  329 -LKKLILVDQTQLDGFENQLSNSKTTITDLEKLINEQKSLVDQIKLQIEKNTADLiyqRSLKTIIELQTNELKKTNNANI 407
Cdd:TIGR04523 430 rLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNL---EQKQKELKSKEKELKKLNEEKK 506

                  ....
gi 499171829  408 LVKN 411
Cdd:TIGR04523 507 ELEE 510
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH