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Conserved domains on  [gi|442628178|ref|NP_001260530|]
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bicaudal D, isoform C [Drosophila melanogaster]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000095)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
BicD super family cl25513
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled ...
83-741 5.68e-124

Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled domains and are involved in dynein-mediated minus end-directed transport from the Golgi apparatus to the endoplasmic reticulum (ER). For full functioning they bind with GSK-3beta pfam05350 to maintain the anchoring of microtubules to the centromere. It appears that amino-acid residues 437-617 of BicD and the kinase activity of GSK-3 are necessary for the formation of a complex between BicD and GSK-3beta in intact cells.


The actual alignment was detected with superfamily member pfam09730:

Pssm-ID: 462863 [Multi-domain]  Cd Length: 717  Bit Score: 388.06  E-value: 5.68e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178   83 TSQKVTNKTGIEQEDALLNESAARETSLNLQIFDLENELKQLRHELERVRNERDRMLQENSDFGRDKSDSEADRLRLKSE 162
Cdd:pfam09730   5 SSHKKVAADGESREESLLQESASKEAYYAQRILELQNELKQARAVLSNTQAENERLASLSQELKEECECVELQRGRMRDE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  163 LKDLKFRETRMLSEYSELEEENISLQKQVSSLRSSQVEFEGAKHEIRRLTEEVELLNQQVDELANLKKIAEKQMEEALET 242
Cdd:pfam09730  85 IKEYKVREARLLQDYSELEEENISLQKQVSVLKQNQVEFEGLKHEITRKEEETELLNSQLEEAIRLREIAERQLDEALET 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  243 LQGEREAKYALKKELDGHLNRESMYHISNLAYSI-----------------RSNMEDNASNNSDGEEENLALKRLEADLS 305
Cdd:pfam09730 165 LKTEREQKNSLRKELSHYMTLNDFDYVSHLSISLdglkfsedegagtepnnDGEAMDGGENGGGGLKNSGLDNRTSTPRK 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  306 TELKSP-DGTKCDLFSEIHLNELKKLEKQLESMESEKTHLTANLREAQTSLDKSQNELQNFMSRLALLAAHVDALVQL-- 382
Cdd:pfam09730 245 SEVFPPaPSLVSDLLSELNISEIQKLKQQLIQVEREKVSLLSTLQESQKQLEQAKGALSEQQEKVNRLTENLEAMRGLqa 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  383 -KKQIDVKEQGKEGGQKKDELEQQL-----RALISQYANWFTLSAKEIDGLKTDIAELQKGL-NYTDATTTLRNEVTNLK 455
Cdd:pfam09730 325 sKERQDALDSEKDRDSHEDGDYYEVdingpEILECKYRVAVEEAGELREELKALKARYNTLEeRYKEEKTRWEAEAQDLA 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  456 NKLLATEQKS-------LDLQSDVQTLTHISQNAGQSLGSARSTLVALSDDLAQLYHLVCTVNGETPTRVLLDH----KT 524
Cdd:pfam09730 405 EKIRQLEKAShqdqeriAHLEKELGKTRKVAGESEGSLSVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYyregAG 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  525 DDMSFENDSLTAIQSQFKSDVFIAKPQIVEDLQG------------------LADSVEIKKYVDTVSDQIKYLKTAVEHT 586
Cdd:pfam09730 485 ARARKSHQEPRGLRSPRLLTRGLFMGEVGTADTTsnspspcsscpgsptsdfRREPMNIYNLVAIIRDQIKHLQVAVDRT 564
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  587 IDMNKHKIRSEGgdaLEKVNTEEMEELQEQIVKLKSLLSVKREQIGTLRNVLKSNKQTAEVALTNLKSKYENEKIIVSDT 666
Cdd:pfam09730 565 TELSRQRGAALE---LSTESDKDKEALMEEILKLKSLLSTKREQIATLRTVLKANKQTAEVALANLKSKYENEKAMVTET 641
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442628178  667 MSKLRNELRLLKEDAATFSSLRAMFAARCEEYVTQVDDLNRQLEAAEEEKKTLNQLLRLAVQQKLALTQRLEEME 741
Cdd:pfam09730 642 MMKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLALTQRLEDLE 716
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
10-138 7.06e-03

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 7.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178    10 SADQSVQDLQMEVERLTRELDQVSSASAQSAQYGLSLLEEKSALQQKCEELETLYDNTRHELDITQEALTKFQtsqkvTN 89
Cdd:TIGR02168  856 SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE-----LR 930
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 442628178    90 KTGIEQEDALLNESAARETSLNLQIF-----DLENELKQLRHELERVRNERDRM 138
Cdd:TIGR02168  931 LEGLEVRIDNLQERLSEEYSLTLEEAealenKIEDDEEEARRRLKRLENKIKEL 984
 
Name Accession Description Interval E-value
BicD pfam09730
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled ...
83-741 5.68e-124

Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled domains and are involved in dynein-mediated minus end-directed transport from the Golgi apparatus to the endoplasmic reticulum (ER). For full functioning they bind with GSK-3beta pfam05350 to maintain the anchoring of microtubules to the centromere. It appears that amino-acid residues 437-617 of BicD and the kinase activity of GSK-3 are necessary for the formation of a complex between BicD and GSK-3beta in intact cells.


Pssm-ID: 462863 [Multi-domain]  Cd Length: 717  Bit Score: 388.06  E-value: 5.68e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178   83 TSQKVTNKTGIEQEDALLNESAARETSLNLQIFDLENELKQLRHELERVRNERDRMLQENSDFGRDKSDSEADRLRLKSE 162
Cdd:pfam09730   5 SSHKKVAADGESREESLLQESASKEAYYAQRILELQNELKQARAVLSNTQAENERLASLSQELKEECECVELQRGRMRDE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  163 LKDLKFRETRMLSEYSELEEENISLQKQVSSLRSSQVEFEGAKHEIRRLTEEVELLNQQVDELANLKKIAEKQMEEALET 242
Cdd:pfam09730  85 IKEYKVREARLLQDYSELEEENISLQKQVSVLKQNQVEFEGLKHEITRKEEETELLNSQLEEAIRLREIAERQLDEALET 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  243 LQGEREAKYALKKELDGHLNRESMYHISNLAYSI-----------------RSNMEDNASNNSDGEEENLALKRLEADLS 305
Cdd:pfam09730 165 LKTEREQKNSLRKELSHYMTLNDFDYVSHLSISLdglkfsedegagtepnnDGEAMDGGENGGGGLKNSGLDNRTSTPRK 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  306 TELKSP-DGTKCDLFSEIHLNELKKLEKQLESMESEKTHLTANLREAQTSLDKSQNELQNFMSRLALLAAHVDALVQL-- 382
Cdd:pfam09730 245 SEVFPPaPSLVSDLLSELNISEIQKLKQQLIQVEREKVSLLSTLQESQKQLEQAKGALSEQQEKVNRLTENLEAMRGLqa 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  383 -KKQIDVKEQGKEGGQKKDELEQQL-----RALISQYANWFTLSAKEIDGLKTDIAELQKGL-NYTDATTTLRNEVTNLK 455
Cdd:pfam09730 325 sKERQDALDSEKDRDSHEDGDYYEVdingpEILECKYRVAVEEAGELREELKALKARYNTLEeRYKEEKTRWEAEAQDLA 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  456 NKLLATEQKS-------LDLQSDVQTLTHISQNAGQSLGSARSTLVALSDDLAQLYHLVCTVNGETPTRVLLDH----KT 524
Cdd:pfam09730 405 EKIRQLEKAShqdqeriAHLEKELGKTRKVAGESEGSLSVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYyregAG 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  525 DDMSFENDSLTAIQSQFKSDVFIAKPQIVEDLQG------------------LADSVEIKKYVDTVSDQIKYLKTAVEHT 586
Cdd:pfam09730 485 ARARKSHQEPRGLRSPRLLTRGLFMGEVGTADTTsnspspcsscpgsptsdfRREPMNIYNLVAIIRDQIKHLQVAVDRT 564
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  587 IDMNKHKIRSEGgdaLEKVNTEEMEELQEQIVKLKSLLSVKREQIGTLRNVLKSNKQTAEVALTNLKSKYENEKIIVSDT 666
Cdd:pfam09730 565 TELSRQRGAALE---LSTESDKDKEALMEEILKLKSLLSTKREQIATLRTVLKANKQTAEVALANLKSKYENEKAMVTET 641
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442628178  667 MSKLRNELRLLKEDAATFSSLRAMFAARCEEYVTQVDDLNRQLEAAEEEKKTLNQLLRLAVQQKLALTQRLEEME 741
Cdd:pfam09730 642 MMKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLALTQRLEDLE 716
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
12-747 3.40e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 63.92  E-value: 3.40e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178    12 DQSVQDLQMEVERLTRELDQVSSASAQSAQYGLSLLEEKSALQQKCEELETLYDNTRHELDITQEALTKFqtsqkvtnKT 91
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL--------ES 372
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178    92 GIEQEDALLNESAARETSLNLQIFDLENELKQLRHELERVRNERDRMLQENSDFGRDKSDSEADRLRLKSELKDlkfret 171
Cdd:TIGR02168  373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELE------ 446
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178   172 rmlseyseleeenISLQKQVSSLRSSQVEFEGAKHEIRRLTEEVELLNQQVDELANLKKIAEKQMEEALETLQGEREAKY 251
Cdd:TIGR02168  447 -------------EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLK 513
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178   252 AlKKELDGHLNR-------ESMYHISNLAYsIRSNMEDNASNNSDGEEENLALkrleadlsteLKSPDGTKCDLFSEIHL 324
Cdd:TIGR02168  514 N-QSGLSGILGVlselisvDEGYEAAIEAA-LGGRLQAVVVENLNAAKKAIAF----------LKQNELGRVTFLPLDSI 581
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178   325 NELKKLEKQLESMESEKTHLTAnLREAQTSLDKSQNELQNFMSRLALLAAHVDALVQLKK-------------------- 384
Cdd:TIGR02168  582 KGTEIQGNDREILKNIEGFLGV-AKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKlrpgyrivtldgdlvrpggv 660
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178   385 --QIDVKEQGKEGGQKK--DELEQQLRALISQYANwftlSAKEIDGLKTDIAELQkglnytDATTTLRNEVTNLKNKLLA 460
Cdd:TIGR02168  661 itGGSAKTNSSILERRReiEELEEKIEELEEKIAE----LEKALAELRKELEELE------EELEQLRKELEELSRQISA 730
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178   461 TEQKSLDLQSDVQTLTHISQNAGQSLGSARSTLVALSDDLAQLYHLVCTVNGEtptRVLLDHKTDDMSFENDSLTAIQSQ 540
Cdd:TIGR02168  731 LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE---IEELEAQIEQLKEELKALREALDE 807
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178   541 FKSDVFIAKPQIVEDLQGLADSVEIKKYVDTVSDQIKYLKTAVEHTIDMNKHKIRS--EGGDALE---KVNTEEMEELQE 615
Cdd:TIGR02168  808 LRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEleELIEELEselEALLNERASLEE 887
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178   616 QIVKLKSLLSVKREQIGTLRNVLKSNKQTAEvALTNLKSKYENE----KIIVSDTMSKLRNELRLLKEDAATFSSLRAMF 691
Cdd:TIGR02168  888 ALALLRSELEELSEELRELESKRSELRRELE-ELREKLAQLELRleglEVRIDNLQERLSEEYSLTLEEAEALENKIEDD 966
                          730       740       750       760       770       780
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442628178   692 AARCEEyvtQVDDLNRQLE-------AAEEEKKTLNQLLRLAVQQKLALTQ---RLEEM--EMDREMR 747
Cdd:TIGR02168  967 EEEARR---RLKRLENKIKelgpvnlAAIEEYEELKERYDFLTAQKEDLTEakeTLEEAieEIDREAR 1031
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
11-266 3.26e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 3.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  11 ADQSVQDLQMEVERLTRELDQVSSASAQSAQYGLSLLEEKSALQQKCEELETLYDNTRHELDITQEALtKFQTSQKVTNK 90
Cdd:COG1196  244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR-RELEERLEELE 322
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  91 TGIEQEDALLNESAARETSLNLQIFDLENELKQLRHELERVRNERDRMLQENSDFGRDKSDSEADRLRLKSELKDLKFRE 170
Cdd:COG1196  323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 171 TRMLSEYSELEEENISLQKQVSSLRSSQVEFEGAKHEIRRLTEEVEllnQQVDELANLKKIAEKQMEEALETLQGEREAK 250
Cdd:COG1196  403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA---EEEAELEEEEEALLELLAELLEEAALLEAAL 479
                        250
                 ....*....|....*.
gi 442628178 251 YALKKELDGHLNRESM 266
Cdd:COG1196  480 AELLEELAEAAARLLL 495
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
185-384 5.99e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 39.91  E-value: 5.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 185 ISLQKQVSSLRSSqVEFEGAKHEIRRLTEEVELLNQQVDELANLKKIAE--KQMEEALETLQGEREAKYALKKEL----- 257
Cdd:PRK05771  53 TKLSEALDKLRSY-LPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKeiKELEEEISELENEIKELEQEIERLepwgn 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 258 ----DGHLNRESMYHIsnLAYSIRSNMEDNASNNSD-------GEEEN------LALKRLEADLSTELKSPDGTKCDLFS 320
Cdd:PRK05771 132 fdldLSLLLGFKYVSV--FVGTVPEDKLEELKLESDvenveyiSTDKGyvyvvvVVLKELSDEVEEELKKLGFERLELEE 209
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442628178 321 EIHLNE-LKKLEKQLESMESEKTHLTANLREaqtSLDKSQNELQNFMSRLALLAAHVDALVQLKK 384
Cdd:PRK05771 210 EGTPSElIREIKEELEEIEKERESLLEELKE---LAKKYLEELLALYEYLEIELERAEALSKFLK 271
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
10-138 7.06e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 7.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178    10 SADQSVQDLQMEVERLTRELDQVSSASAQSAQYGLSLLEEKSALQQKCEELETLYDNTRHELDITQEALTKFQtsqkvTN 89
Cdd:TIGR02168  856 SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE-----LR 930
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 442628178    90 KTGIEQEDALLNESAARETSLNLQIF-----DLENELKQLRHELERVRNERDRM 138
Cdd:TIGR02168  931 LEGLEVRIDNLQERLSEEYSLTLEEAealenKIEDDEEEARRRLKRLENKIKEL 984
 
Name Accession Description Interval E-value
BicD pfam09730
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled ...
83-741 5.68e-124

Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled domains and are involved in dynein-mediated minus end-directed transport from the Golgi apparatus to the endoplasmic reticulum (ER). For full functioning they bind with GSK-3beta pfam05350 to maintain the anchoring of microtubules to the centromere. It appears that amino-acid residues 437-617 of BicD and the kinase activity of GSK-3 are necessary for the formation of a complex between BicD and GSK-3beta in intact cells.


Pssm-ID: 462863 [Multi-domain]  Cd Length: 717  Bit Score: 388.06  E-value: 5.68e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178   83 TSQKVTNKTGIEQEDALLNESAARETSLNLQIFDLENELKQLRHELERVRNERDRMLQENSDFGRDKSDSEADRLRLKSE 162
Cdd:pfam09730   5 SSHKKVAADGESREESLLQESASKEAYYAQRILELQNELKQARAVLSNTQAENERLASLSQELKEECECVELQRGRMRDE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  163 LKDLKFRETRMLSEYSELEEENISLQKQVSSLRSSQVEFEGAKHEIRRLTEEVELLNQQVDELANLKKIAEKQMEEALET 242
Cdd:pfam09730  85 IKEYKVREARLLQDYSELEEENISLQKQVSVLKQNQVEFEGLKHEITRKEEETELLNSQLEEAIRLREIAERQLDEALET 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  243 LQGEREAKYALKKELDGHLNRESMYHISNLAYSI-----------------RSNMEDNASNNSDGEEENLALKRLEADLS 305
Cdd:pfam09730 165 LKTEREQKNSLRKELSHYMTLNDFDYVSHLSISLdglkfsedegagtepnnDGEAMDGGENGGGGLKNSGLDNRTSTPRK 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  306 TELKSP-DGTKCDLFSEIHLNELKKLEKQLESMESEKTHLTANLREAQTSLDKSQNELQNFMSRLALLAAHVDALVQL-- 382
Cdd:pfam09730 245 SEVFPPaPSLVSDLLSELNISEIQKLKQQLIQVEREKVSLLSTLQESQKQLEQAKGALSEQQEKVNRLTENLEAMRGLqa 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  383 -KKQIDVKEQGKEGGQKKDELEQQL-----RALISQYANWFTLSAKEIDGLKTDIAELQKGL-NYTDATTTLRNEVTNLK 455
Cdd:pfam09730 325 sKERQDALDSEKDRDSHEDGDYYEVdingpEILECKYRVAVEEAGELREELKALKARYNTLEeRYKEEKTRWEAEAQDLA 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  456 NKLLATEQKS-------LDLQSDVQTLTHISQNAGQSLGSARSTLVALSDDLAQLYHLVCTVNGETPTRVLLDH----KT 524
Cdd:pfam09730 405 EKIRQLEKAShqdqeriAHLEKELGKTRKVAGESEGSLSVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYyregAG 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  525 DDMSFENDSLTAIQSQFKSDVFIAKPQIVEDLQG------------------LADSVEIKKYVDTVSDQIKYLKTAVEHT 586
Cdd:pfam09730 485 ARARKSHQEPRGLRSPRLLTRGLFMGEVGTADTTsnspspcsscpgsptsdfRREPMNIYNLVAIIRDQIKHLQVAVDRT 564
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  587 IDMNKHKIRSEGgdaLEKVNTEEMEELQEQIVKLKSLLSVKREQIGTLRNVLKSNKQTAEVALTNLKSKYENEKIIVSDT 666
Cdd:pfam09730 565 TELSRQRGAALE---LSTESDKDKEALMEEILKLKSLLSTKREQIATLRTVLKANKQTAEVALANLKSKYENEKAMVTET 641
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442628178  667 MSKLRNELRLLKEDAATFSSLRAMFAARCEEYVTQVDDLNRQLEAAEEEKKTLNQLLRLAVQQKLALTQRLEEME 741
Cdd:pfam09730 642 MMKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLALTQRLEDLE 716
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
12-747 3.40e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 63.92  E-value: 3.40e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178    12 DQSVQDLQMEVERLTRELDQVSSASAQSAQYGLSLLEEKSALQQKCEELETLYDNTRHELDITQEALTKFqtsqkvtnKT 91
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL--------ES 372
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178    92 GIEQEDALLNESAARETSLNLQIFDLENELKQLRHELERVRNERDRMLQENSDFGRDKSDSEADRLRLKSELKDlkfret 171
Cdd:TIGR02168  373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELE------ 446
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178   172 rmlseyseleeenISLQKQVSSLRSSQVEFEGAKHEIRRLTEEVELLNQQVDELANLKKIAEKQMEEALETLQGEREAKY 251
Cdd:TIGR02168  447 -------------EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLK 513
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178   252 AlKKELDGHLNR-------ESMYHISNLAYsIRSNMEDNASNNSDGEEENLALkrleadlsteLKSPDGTKCDLFSEIHL 324
Cdd:TIGR02168  514 N-QSGLSGILGVlselisvDEGYEAAIEAA-LGGRLQAVVVENLNAAKKAIAF----------LKQNELGRVTFLPLDSI 581
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178   325 NELKKLEKQLESMESEKTHLTAnLREAQTSLDKSQNELQNFMSRLALLAAHVDALVQLKK-------------------- 384
Cdd:TIGR02168  582 KGTEIQGNDREILKNIEGFLGV-AKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKlrpgyrivtldgdlvrpggv 660
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178   385 --QIDVKEQGKEGGQKK--DELEQQLRALISQYANwftlSAKEIDGLKTDIAELQkglnytDATTTLRNEVTNLKNKLLA 460
Cdd:TIGR02168  661 itGGSAKTNSSILERRReiEELEEKIEELEEKIAE----LEKALAELRKELEELE------EELEQLRKELEELSRQISA 730
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178   461 TEQKSLDLQSDVQTLTHISQNAGQSLGSARSTLVALSDDLAQLYHLVCTVNGEtptRVLLDHKTDDMSFENDSLTAIQSQ 540
Cdd:TIGR02168  731 LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE---IEELEAQIEQLKEELKALREALDE 807
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178   541 FKSDVFIAKPQIVEDLQGLADSVEIKKYVDTVSDQIKYLKTAVEHTIDMNKHKIRS--EGGDALE---KVNTEEMEELQE 615
Cdd:TIGR02168  808 LRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEleELIEELEselEALLNERASLEE 887
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178   616 QIVKLKSLLSVKREQIGTLRNVLKSNKQTAEvALTNLKSKYENE----KIIVSDTMSKLRNELRLLKEDAATFSSLRAMF 691
Cdd:TIGR02168  888 ALALLRSELEELSEELRELESKRSELRRELE-ELREKLAQLELRleglEVRIDNLQERLSEEYSLTLEEAEALENKIEDD 966
                          730       740       750       760       770       780
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442628178   692 AARCEEyvtQVDDLNRQLE-------AAEEEKKTLNQLLRLAVQQKLALTQ---RLEEM--EMDREMR 747
Cdd:TIGR02168  967 EEEARR---RLKRLENKIKelgpvnlAAIEEYEELKERYDFLTAQKEDLTEakeTLEEAieEIDREAR 1031
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
11-266 3.26e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 3.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  11 ADQSVQDLQMEVERLTRELDQVSSASAQSAQYGLSLLEEKSALQQKCEELETLYDNTRHELDITQEALtKFQTSQKVTNK 90
Cdd:COG1196  244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR-RELEERLEELE 322
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  91 TGIEQEDALLNESAARETSLNLQIFDLENELKQLRHELERVRNERDRMLQENSDFGRDKSDSEADRLRLKSELKDLKFRE 170
Cdd:COG1196  323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 171 TRMLSEYSELEEENISLQKQVSSLRSSQVEFEGAKHEIRRLTEEVEllnQQVDELANLKKIAEKQMEEALETLQGEREAK 250
Cdd:COG1196  403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA---EEEAELEEEEEALLELLAELLEEAALLEAAL 479
                        250
                 ....*....|....*.
gi 442628178 251 YALKKELDGHLNRESM 266
Cdd:COG1196  480 AELLEELAEAAARLLL 495
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
90-372 1.09e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.83  E-value: 1.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178    90 KTGIEQEDALLNESAARETSLNLQIFDLENELKQLRHELERVRNERDRMLQENSDFGRDKSDSEADRLRLKSELKDLKfr 169
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE-- 315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178   170 etrmlseySELEEENISLQKQVSSLRSSQVEFEGAKHEIRRLTEEVELLNQQVDELANLKKIAEKQMEEALETLQGEREA 249
Cdd:TIGR02168  316 --------RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178   250 KYALKKELDGHLNRESmyhisnlaySIRSNMEDNASNNSDGEEENlalkrleADLSTELKSPDGTKCDLFSEIHLNELKK 329
Cdd:TIGR02168  388 VAQLELQIASLNNEIE---------RLEARLERLEDRRERLQQEI-------EELLKKLEEAELKELQAELEELEEELEE 451
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 442628178   330 LEKQLESMESEKTHLTANLREAQTSLDKSQNELQNFMSRLALL 372
Cdd:TIGR02168  452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
11-263 1.31e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  11 ADQSVQDLQMEVERLTRELDQVSSASAQSAQYGLSLLEEKSALQQKCEELETLYDNTRHELDITQEALTKFQTSQKVTNK 90
Cdd:COG1196  272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  91 TgIEQEDALLNESAARETSLNLQIFDLENELKQLRHELERVRNERDRMLQENSDFGRDKSDSEADRLRLKSELKDLkfrE 170
Cdd:COG1196  352 E-LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL---E 427
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 171 TRMLSEYSELEEENISLQKQVSSLRSSQVEFEGAKHEIRRLTEEVELLNQQVDELaNLKKIAEKQMEEALETLQGEREAK 250
Cdd:COG1196  428 EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL-LEELAEAAARLLLLLEAEADYEGF 506
                        250
                 ....*....|...
gi 442628178 251 YALKKELDGHLNR 263
Cdd:COG1196  507 LEGVKAALLLAGL 519
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
106-741 7.12e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 7.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 106 RETSLNLQ-IFDLENEL-KQLRH-ELERVRNERDRMLQEnsdfgrdksdsEADRLRLKSELKDLKFRETRMLSEYSELEE 182
Cdd:COG1196  182 EATEENLErLEDILGELeRQLEPlERQAEKAERYRELKE-----------ELKELEAELLLLKLRELEAELEELEAELEE 250
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 183 ENISLQKQVSSLRSSQVEFEGAKHEIRRLTEEVELLNQQVDELANLKKIAEKQMEEALETLQGEREAKYALKKELDghln 262
Cdd:COG1196  251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA---- 326
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 263 resmyhisNLAYSIRSNMEDNASNNSDGEEENLALKRLEADLSTELKspdgtkcdlfseihlnELKKLEKQLESMESEKT 342
Cdd:COG1196  327 --------ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE----------------ALLEAEAELAEAEEELE 382
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 343 HLTANLREAQTSLDKSQNELQNFMSRLALLAAHVDALVQLKKQIDVKEQGKEggQKKDELEQQLRALISQYANWFTLSAK 422
Cdd:COG1196  383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE--EEEEEEEEALEEAAEEEAELEEEEEA 460
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 423 EIDGLKTDIAELQKGLNYTDATTTLRNEVTNLKNKLLATEQKSLDLQSDVQTLTHISQNAG--QSLGSARSTLVALSDDL 500
Cdd:COG1196  461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlaGAVAVLIGVEAAYEAAL 540
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 501 -----AQLYHLVC--TVNGETPTRVLLDHKTDDMSFEndSLTAIQSQFKSDVFIAKPQIVEDLQGLADSVEIKKYVDTVS 573
Cdd:COG1196  541 eaalaAALQNIVVedDEVAAAAIEYLKAAKAGRATFL--PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVL 618
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 574 DQIKYLKTAVEHTIDMNKHKIRSEGGDALEKvnTEEMEELQEQIVKLKSLLSVKREQIGTLRNVLKSNKQTAEVALTNLK 653
Cdd:COG1196  619 GDTLLGRTLVAARLEAALRRAVTLAGRLREV--TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELE 696
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 654 SKYENEKIIVSDTMSKLRNELRLLKEDAATFSSLRAMFAARCEEYVTQVDDLNRQLEAAEEEKKTLNQLlrlavQQKLA- 732
Cdd:COG1196  697 EALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEL-----ERELEr 771

                 ....*....
gi 442628178 733 LTQRLEEME 741
Cdd:COG1196  772 LEREIEALG 780
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
105-409 9.64e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.30  E-value: 9.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178   105 ARETSLNLQIFDLENELKQLRHELERVRNERDRMLQENSDFGRDKSDSEADRLRLKSELKDLKFRETRMLSEYSeleeen 184
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS------ 747
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178   185 iSLQKQVSSLRSSQVEFEGakhEIRRLTEEVELLNQQVDEL-ANLKKIAEKQMEEALETLQGEREAKYALKKELDGHLNR 263
Cdd:TIGR02169  748 -SLEQEIENVKSELKELEA---RIEELEEDLHKLEEALNDLeARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR 823
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178   264 ESMyhisnlaysiRSNMEDNASNNSdgEEENLALKRLEADLSTELKSPDGTKCDLFSEI--HLNELKKLEKQLESMESEK 341
Cdd:TIGR02169  824 LTL----------EKEYLEKEIQEL--QEQRIDLKEQIKSIEKEIENLNGKKEELEEELeeLEAALRDLESRLGDLKKER 891
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442628178   342 THLTANLREAQTSLDKSQNELQNFMSRLALLAAHVDALVQLKKQID-VKEQGKEGG----------QKKDELEQQLRAL 409
Cdd:TIGR02169  892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEdPKGEDEEIPeeelsledvqAELQRVEEEIRAL 970
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
326-745 1.06e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  326 ELKKLEKQLESMESEKTHLTANLREAQTSLDKSQNELQNFmsRLALLAAHVDALVQLKKQIDVKEQGKEGGQKK-DELEQ 404
Cdd:COG4913   289 RLELLEAELEELRAELARLEAELERLEARLDALREELDEL--EAQIRGNGGDRLEQLEREIERLERELEERERRrARLEA 366
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  405 QLRAL---ISQYANWFTLSAKEIDGLKTDIAELQKGLNytDATTTLRNEVTNLKNKL--LATEQKSLDLQSD------VQ 473
Cdd:COG4913   367 LLAALglpLPASAEEFAALRAEAAALLEALEEELEALE--EALAEAEAALRDLRRELreLEAEIASLERRKSniparlLA 444
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  474 TLTHISQNAGQS---------------------------LGSARSTLVALSDDLAQL------YHLVCTVNGEtptRV-L 519
Cdd:COG4913   445 LRDALAEALGLDeaelpfvgelievrpeeerwrgaiervLGGFALTLLVPPEHYAAAlrwvnrLHLRGRLVYE---RVrT 521
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  520 LDHKTDDMSFENDSLTA------------IQSQFKSDVFIAKPQIVEDLQGLADSVeikkyvdTVSDQIKYLKTAVEHTI 587
Cdd:COG4913   522 GLPDPERPRLDPDSLAGkldfkphpfrawLEAELGRRFDYVCVDSPEELRRHPRAI-------TRAGQVKGNGTRHEKDD 594
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  588 dmnKHKIRSE---GGDALEKVNT--EEMEELQEQIVKLKSLLSVKREQIGTLRNVLKSNKQTAEVALTNLKSKYENEKIi 662
Cdd:COG4913   595 ---RRRIRSRyvlGFDNRAKLAAleAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREI- 670
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  663 vsdtmSKLRNELRLLKEDAATFSSLRAmfaaRCEEYVTQVDDLNRQLEAAEEEKKTLNQLLRLAVQQKLALTQRLEEMEM 742
Cdd:COG4913   671 -----AELEAELERLDASSDDLAALEE----QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741

                  ...
gi 442628178  743 DRE 745
Cdd:COG4913   742 LAR 744
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
10-458 1.41e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 1.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  10 SADQSVQDLQMEVERLTRELDQVSSASAQSAQYGLSLLEEKSALQQKCEELETLYDNTRHELDITQEALTKFQTSQKVTN 89
Cdd:COG1196  306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  90 KTGIEQEDALLN------ESAARETSLNLQIFDLENELKQLRHELERVRNERDRMLQENSDFGRDKSDSEADRLRLKSEL 163
Cdd:COG1196  386 EELLEALRAAAElaaqleELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 164 KDLKFRETRMLSEYSELEEENISLQKQVSSLRSSQVEFEGAKHEIRRLTEEVEL--LNQQVDELANLKKIAEKQMEEAL- 240
Cdd:COG1196  466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLrgLAGAVAVLIGVEAAYEAALEAALa 545
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 241 --------ETLQGEREAKYALKKELDG-----HLNRESMYHISNLAYSIRSNMEDNASNNSDGEEENLALKRLEADLS-T 306
Cdd:COG1196  546 aalqnivvEDDEVAAAAIEYLKAAKAGratflPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLgR 625
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 307 ELKSPDGTKCDLFSEIHLNELKKLEKQLESMESEKTHLTANLREAQTSLDKSQNELQNFMSRLA--LLAAHVDALVQLKK 384
Cdd:COG1196  626 TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAeeELELEEALLAEEEE 705
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442628178 385 QIDVKEQGKEGGQKKDELEQQLRALISQYANwftLSAKEIDGLKTDIAELQKGLNYTDATTTLRNEVTNLKNKL 458
Cdd:COG1196  706 ERELAEAEEERLEEELEEEALEEQLEAEREE---LLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
46-257 1.94e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 1.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  46 LLEEKSALQQKCEELETLYDNTRHELDITQEALTKFQTSQKVTNKTgIEQEDALLNESAARETSLNLQIFDLENELKQLR 125
Cdd:COG1196  237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE-LEEAQAEEYELLAELARLEQDIARLEERRRELE 315
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 126 HELERVRNERDRMLQENSDFGRDKSDSEADRLRLKSELKDLKFRETRMLSEYSELEEENISLQKQVSSLRSSQVEFEGAK 205
Cdd:COG1196  316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 442628178 206 HEIRRLTEEVEllnQQVDELANLKKIAEKQMEEALETLQGEREAKYALKKEL 257
Cdd:COG1196  396 AELAAQLEELE---EAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
10-250 6.19e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 6.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  10 SADQSVQDLQMEVERLTRELDQVSSASAQSAQyglsLLEEKSALQQKCEELETLYDNTRHELDITQEALTKFQTSQKVTN 89
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAE----LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  90 KTGIEQEDALLNESAARETSLNlQIFDLENELKQLRHELERVRNERDRMLQENSDFGRDKSDSEADRLRLKSELKDLKFR 169
Cdd:COG1196  372 AELAEAEEELEELAEELLEALR-AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 170 ETRmlseyseleeenisLQKQVSSLRSSQVEfegAKHEIRRLTEEVELLNQQVDELANLKKIAEKQMEEALETLQGEREA 249
Cdd:COG1196  451 EAE--------------LEEEEEALLELLAE---LLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513

                 .
gi 442628178 250 K 250
Cdd:COG1196  514 L 514
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
321-745 3.76e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 3.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 321 EIHLNELKKLEKQLESMESEKTH---LTANLREAQTSLDKSQNELQNFMSRLALLAAHVDALVQLKKQIDVKEQGKEGGQ 397
Cdd:COG4717   67 ELNLKELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPE 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 398 KKDELEQQLRALISQYANWFTLSAkEIDGLKTDIAELQKGLNYTDATT---------TLRNEVTNLKNKLLATEQKSLDL 468
Cdd:COG4717  147 RLEELEERLEELRELEEELEELEA-ELAELQEELEELLEQLSLATEEElqdlaeeleELQQRLAELEEELEEAQEELEEL 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 469 QSDVQTL--THISQNAGQSLGSARSTLVALSddlaqlyhLVCTVNGETPTRVLLDHKTDDMSFENDSLTAIQSQFKSDVF 546
Cdd:COG4717  226 EEELEQLenELEAAALEERLKEARLLLLIAA--------ALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREK 297
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 547 IAKPQIVEDLQGLADSVEIKKYvdtvsdQIKYLKTAVEHTIDMNKHKIRseggDALEKVntEEMEELQEQIVKLKSLLSV 626
Cdd:COG4717  298 ASLGKEAEELQALPALEELEEE------ELEELLAALGLPPDLSPEELL----ELLDRI--EELQELLREAEELEEELQL 365
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 627 KREQIgTLRNVLKSNKQTAEVALTNLKSKYENEKiivsdtmsKLRNELRLLKED-AATFSSLRAMFAARCEEYV-TQVDD 704
Cdd:COG4717  366 EELEQ-EIAALLAEAGVEDEEELRAALEQAEEYQ--------ELKEELEELEEQlEELLGELEELLEALDEEELeEELEE 436
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 442628178 705 LNRQLEAAEEEKKTLNqllrlavQQKLALTQRLEEMEMDRE 745
Cdd:COG4717  437 LEEELEELEEELEELR-------EELAELEAELEQLEEDGE 470
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
112-258 4.19e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.60  E-value: 4.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 112 LQIFDLENELKQLRHELERVRNERDRMLQENSDFGRDKSDSEADRLRLKSELKDLKFRETRmlseyseleeenisLQKQV 191
Cdd:COG1579   17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK--------------YEEQL 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442628178 192 SSLRSSQvEFEGAKHEIRRLTEEVELLNQQVDELANLKKIAEKQMEEALETLQGEREAKYALKKELD 258
Cdd:COG1579   83 GNVRNNK-EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
21-259 5.95e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 5.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178    21 EVERLTRELDQVSS--ASAQSAQyglsllEEKSALQQKCEELETLYDNTRHELDITQEALTKFQTSQKVtnktgieQEDA 98
Cdd:TIGR02169  288 EQLRVKEKIGELEAeiASLERSI------AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERK-------RRDK 354
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178    99 LLNESAARETSLNLQIFDLE----------NELKQLRHELERVRNERDRMLQENSDFGRDKSDSEADRLRLKSELKDLKF 168
Cdd:TIGR02169  355 LTEEYAELKEELEDLRAELEevdkefaetrDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA 434
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178   169 RETRMLSEYSELEEEnisLQKQVSSLRSSQVEFEGAKHEIRRLTEEVELLNQQVDELANLKKIAEKQMEEALETLQGERE 248
Cdd:TIGR02169  435 KINELEEEKEDKALE---IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRA 511
                          250
                   ....*....|.
gi 442628178   249 AKYALKKELDG 259
Cdd:TIGR02169  512 VEEVLKASIQG 522
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
18-471 7.52e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 7.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  18 LQMEVERLTRELDQVSSASAQSAQYGLSLLEEKSALQQKCEELETLYDNTRHELDITQEALTKFQTSQKVTnktgieqed 97
Cdd:COG4717   44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEEL--------- 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  98 allnESAARETSLNLQIFDLENELKQLRHELERVRNERDRMLQENSDFgrdkSDSEADRLRLKSELKDLKFRETRMLSEY 177
Cdd:COG4717  115 ----REELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEEL----RELEEELEELEAELAELQEELEELLEQL 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 178 SELEEENisLQKQVSSLRSSQVEFEGAKHEIRRLTEEVELLNQQVDELANLKKIAEKQME-EALETLQGEREAKYALKKE 256
Cdd:COG4717  187 SLATEEE--LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlKEARLLLLIAAALLALLGL 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 257 LDGHLNRESMYH--------ISNLAYSIRSNMEDNASNNSDGEEENLALKRLEADLSTELKSPDGTKCDLfSEIHLNELK 328
Cdd:COG4717  265 GGSLLSLILTIAgvlflvlgLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDL-SPEELLELL 343
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 329 KLEKQLESMESEKTHLTANLReaqtsLDKSQNELQNFmsrlaLLAAHVDALVQLKKQIDVKEQGKEGGQKKDELEQQLRA 408
Cdd:COG4717  344 DRIEELQELLREAEELEEELQ-----LEELEQEIAAL-----LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEE 413
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442628178 409 LISQYANWftLSAKEIDGLKTDIAELQKGLNytdattTLRNEVTNLKNKLLATEQKSLDLQSD 471
Cdd:COG4717  414 LLGELEEL--LEALDEEELEEELEELEEELE------ELEEELEELREELAELEAELEQLEED 468
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
321-503 1.05e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178   321 EIHLNELKKLEKQLESMESEKTHLTANLREAQTSLDKSQNELQNFMSRLALLAAHVDALVQLKKQIDvkEQGKEGGQKKD 400
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE--AQLEELESKLD 333
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178   401 ELEQQLRALisqyanwftlsAKEIDGLKTDIAELQKGLnytdatTTLRNEVTNLKNKLLATEQKSLDLQSDVQTLThisq 480
Cdd:TIGR02168  334 ELAEELAEL-----------EEKLEELKEELESLEAEL------EELEAELEELESRLEELEEQLETLRSKVAQLE---- 392
                          170       180
                   ....*....|....*....|...
gi 442628178   481 nagQSLGSARSTLVALSDDLAQL 503
Cdd:TIGR02168  393 ---LQIASLNNEIERLEARLERL 412
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
56-249 1.21e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178   56 KCEELETLydnTRHELDITQEALTKFQTSQKVTNKTGIEQEDALLNESAARetslnlQIFDLENELKQLRHELERVRNER 135
Cdd:COG4913   563 CVDSPEEL---RRHPRAITRAGQVKGNGTRHEKDDRRRIRSRYVLGFDNRA------KLAALEAELAELEEELAEAEERL 633
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  136 DRMlqensdfgRDKSDSEADRLRLKSELKDLKFRETRMLSEYSELEeeniSLQKQVSSLRSSQVEFEGAKHEIRRLTEEV 215
Cdd:COG4913   634 EAL--------EAELDALQERREALQRLAEYSWDEIDVASAEREIA----ELEAELERLDASSDDLAALEEQLEELEAEL 701
                         170       180       190
                  ....*....|....*....|....*....|....
gi 442628178  216 ELLNQQVDELANLKKIAEKQMEEALETLQGEREA 249
Cdd:COG4913   702 EELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
21-415 2.93e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 2.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178  21 EVERLTRELDQVSSASAQSAQyglsLLEEKSALQQKCEELETLYDNTRHELDITQEALTKFQTSQKVTNktgIEQEDALL 100
Cdd:COG4717   72 ELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA---LEAELAEL 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 101 NESAARETSLNLQIFDLENELKQLRHELERVRNERDRMLQENS--------DFGRDKSDSEADRLRLKSELKDLKFR--- 169
Cdd:COG4717  145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlateeelqDLAEELEELQQRLAELEEELEEAQEElee 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 170 -----ETRMLSEYSELEEENISLQKQVSSLRSSQVEFEGAKHEIRRLTEEV-------------ELLNQQVDELANLKKI 231
Cdd:COG4717  225 leeelEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIagvlflvlgllalLFLLLAREKASLGKEA 304
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 232 AEKQMEEALETLQGEREAKYALKKELDGHLNRESMYHISNLAYSIRSNMEDNASnnsdgEEENLALKRLEADLSTELKSP 311
Cdd:COG4717  305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE-----LEEELQLEELEQEIAALLAEA 379
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 312 DGTKCDLFSEI--HLNELKKLEKQLESMESEKTHLTANLREAQTSLDKSQ--NELQNFMSRLALLAAHVDALVQLKKQID 387
Cdd:COG4717  380 GVEDEEELRAAleQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEleEELEELEEELEELEEELEELREELAELE 459
                        410       420
                 ....*....|....*....|....*...
gi 442628178 388 VKEQGKEGGQKKDELEQQLRALISQYAN 415
Cdd:COG4717  460 AELEQLEEDGELAELLQELEELKAELRE 487
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
185-384 5.99e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 39.91  E-value: 5.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 185 ISLQKQVSSLRSSqVEFEGAKHEIRRLTEEVELLNQQVDELANLKKIAE--KQMEEALETLQGEREAKYALKKEL----- 257
Cdd:PRK05771  53 TKLSEALDKLRSY-LPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKeiKELEEEISELENEIKELEQEIERLepwgn 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178 258 ----DGHLNRESMYHIsnLAYSIRSNMEDNASNNSD-------GEEEN------LALKRLEADLSTELKSPDGTKCDLFS 320
Cdd:PRK05771 132 fdldLSLLLGFKYVSV--FVGTVPEDKLEELKLESDvenveyiSTDKGyvyvvvVVLKELSDEVEEELKKLGFERLELEE 209
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442628178 321 EIHLNE-LKKLEKQLESMESEKTHLTANLREaqtSLDKSQNELQNFMSRLALLAAHVDALVQLKK 384
Cdd:PRK05771 210 EGTPSElIREIKEELEEIEKERESLLEELKE---LAKKYLEELLALYEYLEIELERAEALSKFLK 271
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
10-138 7.06e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 7.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628178    10 SADQSVQDLQMEVERLTRELDQVSSASAQSAQYGLSLLEEKSALQQKCEELETLYDNTRHELDITQEALTKFQtsqkvTN 89
Cdd:TIGR02168  856 SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE-----LR 930
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 442628178    90 KTGIEQEDALLNESAARETSLNLQIF-----DLENELKQLRHELERVRNERDRM 138
Cdd:TIGR02168  931 LEGLEVRIDNLQERLSEEYSLTLEEAealenKIEDDEEEARRRLKRLENKIKEL 984
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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