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Conserved domains on  [gi|1140107559|gb|APZ92116|]
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DNA translocase FtsK [Fuerstiella marisgermanici]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 776-936 9.41e-27

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member pfam01580:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 219  Bit Score: 109.77  E-value: 9.41e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  776 RGTSQHALVAGKTGSGKSTLLHILITNLALHYSPNEIQFYLIDFkKGVEFRTYAahKLPHARVIAIESDREFGLSVLERL 855
Cdd:pfam01580   35 KKMPVHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDP-KMGELSAYE--DIPHLLSVPVATDPKRALRALEWL 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  856 DEVLQERGELFRERGVQDVPSFRKQFP--------------------------SEPMPRLLLLIDEFQEF-FVAEDRVSA 908
Cdd:pfam01580  112 VDEMERRYALFRALGVRSIAGYNGEIAedpldgfgdvflviygvhvmctagrwLEILPYLVVIVDERAELrLAAPKDSEM 191

                          170       180
                   ....*....|....*....|....*...
gi 1140107559  909 RASLLLDRLVRQGRAFGIHVLLGSQTLG 936
Cdd:pfam01580  192 RVEDAIVRLAQKGRAAGIHLLLATQRPS 219
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
8-468 2.09e-07

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


The actual alignment was detected with superfamily member COG4717:

Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.54  E-value: 2.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559    8 LTNQLTSASQKIAECEVLRTELQRLQTHMETVVAErdqtLESLQQSALTNMQAERQRIHDNADRELDTLRLDCNSRRETL 87
Cdd:COG4717     76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAE----LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEEL 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559   88 QQNLKTtlhrlVADLEVETNNLEERRKSelwvLQSVMDEDGDDSPVVHfEREAETFVTQKAFLDERFEILQQQLKDSEQy 167
Cdd:COG4717    152 EERLEE-----LRELEEELEELEAELAE----LQEELEELLEQLSLAT-EEELQDLAEELEELQQRLAELEEELEEAQE- 220

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  168 lanshattetelpppnlnvtkRLELKDAAVEAGNQALAAADEIERLKLPRWLqgfrIWALSLLAFVVLWIPIVAARAdlr 247
Cdd:COG4717    221 ---------------------ELEELEEELEQLENELEAAALEERLKEARLL----LLIAAALLALLGLGGSLLSLI--- 272

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  248 qfinpeltkpdWQWTAMAALTAAVIVVLFavLSLVSAQASLRSRFQSMLQHVSNARAARTGWEQKSQRYVDRMEGQASEW 327
Cdd:COG4717    273 -----------LTIAGVLFLVLGLLALLF--LLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEEL 339

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  328 RLEVeqRRIQQTQKLTEDIDSRIASLRNQTAAQQ-------------ATFEG---------EIQRQIQQIDHELT----T 381
Cdd:COG4717    340 LELL--DRIEELQELLREAEELEEELQLEELEQEiaallaeagvedeEELRAaleqaeeyqELKEELEELEEQLEellgE 417

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  382 AEQRIEARKVTDVQQALDRTNIELQTARDTC----EQQAQRTMARERLAEAELIATWRSIIDDLRttakesSVLAAATRR 457
Cdd:COG4717    418 LEELLEALDEEELEEELEELEEELEELEEELeelrEELAELEAELEQLEEDGELAELLQELEELK------AELRELAEE 491

                          490
                   ....*....|.
gi 1140107559  458 WPKAGTGQWTL 468
Cdd:COG4717    492 WAALKLALELL 502
T7SS_EccC_b super family cl37348
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ...
 713-822 1.77e-05

type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]


The actual alignment was detected with superfamily member TIGR03925:

Pssm-ID: 274859 [Multi-domain]  Cd Length: 566  Bit Score: 49.22  E-value: 1.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  713 AAETYVQLVRDV--GEQSRDARRV--EVSFNRIAPREDEiwshsTADGIDFPIGRA--GAARLQFMRlgrgtSQHALVAG 786
Cdd:TIGR03925  301 GTRGLVAVIRDVwgGPPAPPVRLLpaRLPLSALPAGGGA-----PRLRVPLGLGESdlAPVYVDFAE-----SPHLLIFG 370

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1140107559  787 KTGSGKSTLLHILITNLALHYSPNEIQFYLIDFKKG 822
Cdd:TIGR03925  371 DSESGKTTLLRTIARGIVRRYSPDQARLVVVDYRRT 406
 
Name Accession Description Interval E-value
FtsK_SpoIIIE pfam01580
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ...
 776-936 9.41e-27

FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from prokaryotes and plasmids, termed the FtsK/SpoIIIE family. This domain contains a putative ATP binding P-loop motif. It is found in the FtsK cell division protein from E. coli and the stage III sporulation protein E SpoIIIE, which has roles in regulation of prespore specific gene expression in B. subtilis. A mutation in FtsK causes a temperature sensitive block in cell division and it is involved in peptidoglycan synthesis or modification. The SpoIIIE protein is implicated in intercellular chromosomal DNA transfer.


Pssm-ID: 279863 [Multi-domain]  Cd Length: 219  Bit Score: 109.77  E-value: 9.41e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  776 RGTSQHALVAGKTGSGKSTLLHILITNLALHYSPNEIQFYLIDFkKGVEFRTYAahKLPHARVIAIESDREFGLSVLERL 855
Cdd:pfam01580   35 KKMPVHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDP-KMGELSAYE--DIPHLLSVPVATDPKRALRALEWL 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  856 DEVLQERGELFRERGVQDVPSFRKQFP--------------------------SEPMPRLLLLIDEFQEF-FVAEDRVSA 908
Cdd:pfam01580  112 VDEMERRYALFRALGVRSIAGYNGEIAedpldgfgdvflviygvhvmctagrwLEILPYLVVIVDERAELrLAAPKDSEM 191

                          170       180
                   ....*....|....*....|....*...
gi 1140107559  909 RASLLLDRLVRQGRAFGIHVLLGSQTLG 936
Cdd:pfam01580  192 RVEDAIVRLAQKGRAAGIHLLLATQRPS 219
T7_EssCb_Firm TIGR03928
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ...
 781-1001 8.99e-22

type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274860 [Multi-domain]  Cd Length: 1296  Bit Score: 102.76  E-value: 8.99e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  781 HALVAGKTGSGKSTLLHILITNLALHYSPNEIQFYLIDFKKGVEFRTYAahKLPHArVIAI------ESDRefglsVLER 854
Cdd:TIGR03928  471 HGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKGGGMANLFK--NLPHL-LGTItnldgaQSMR-----ALAS 542

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  855 LDEVLQERGELFRERGVQDVPSFRKQF----PSEPMPRLLLLIDEFQEF------FVAEdRVSArasllldrlVRQGRAF 924
Cdd:TIGR03928  543 IKAELKKRQRLFGENNVNHINQYQKLYkqgkAKEPMPHLFLISDEFAELkseqpeFMKE-LVST---------ARIGRSL 612

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  925 GIHVLLGSQTLGGA-----YSLARStmgqiavRIALQC-SESDAHLILSedNPAARMLTRPGEAiYndangLRQGNHQ-- 996
Cdd:TIGR03928  613 GVHLILATQKPSGVvddqiWSNSRF-------KLALKVqDASDSNEILK--TPDAAEITVPGRA-Y-----LQVGNNEvy 677


                   ....*..
gi 1140107559  997 --FQIAW 1001
Cdd:TIGR03928  678 elFQSAW 684
FtsK COG1674
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ...
 781-933 1.72e-11

DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441280 [Multi-domain]  Cd Length: 611  Bit Score: 68.80  E-value: 1.72e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  781 HALVAGKTGSGKSTLLHILITNLALHYSPNEIQFYLIDFKKgVEFRTYAahKLPHArVIAIESDREFGLSVLERLDEVLQ 860
Cdd:COG1674    283 HLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDPKM-VELSVYN--GIPHL-LTPVVTDPKKAANALKWAVREME 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  861 ERGELFRERGVQDVPSFRKQFPS-----------EPMPRLLLLIDEFQE-FFVAEDRVSAraslLLDRLVRQGRAFGIHV 928
Cdd:COG1674    359 RRYKLFAKAGVRNIAGYNEKVREakakgeeeeglEPLPYIVVIIDELADlMMVAGKEVEE----AIARLAQKARAAGIHL 434


                   ....*
gi 1140107559  929 LLGSQ 933
Cdd:COG1674    435 ILATQ 439
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 781-988 1.08e-09

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 63.18  E-value: 1.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  781 HALVAGKTGSGKSTLLHILITNLALHYSPNEIQFYLIDfKKGVEFRTYAAhkLPHArVIAIESDREFGLSVLERLDEVLQ 860
Cdd:PRK10263  1012 HLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMID-PKMLELSVYEG--IPHL-LTEVVTDMKDAANALRWCVNEME 1087

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  861 ERGELFRERGVQD-----------------VP--------SFRKQFPS-EPMPRLLLLIDEFQEFFVAedrVSARASLLL 914
Cdd:PRK10263  1088 RRYKLMSALGVRNlagynekiaeadrmmrpIPdpywkpgdSMDAQHPVlKKEPYIVVLVDEFADLMMT---VGKKVEELI 1164

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1140107559  915 DRLVRQGRAFGIHVLLGSQ--TLGGAYSLARStmgQIAVRIALQCSES-DAHLILseDNPAARMLTRPGEAIYNDAN 988
Cdd:PRK10263  1165 ARLAQKARAAGIHLVLATQrpSVDVITGLIKA---NIPTRIAFTVSSKiDSRTIL--DQAGAESLLGMGDMLYSGPN 1236
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
8-468 2.09e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.54  E-value: 2.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559    8 LTNQLTSASQKIAECEVLRTELQRLQTHMETVVAErdqtLESLQQSALTNMQAERQRIHDNADRELDTLRLDCNSRRETL 87
Cdd:COG4717     76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAE----LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEEL 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559   88 QQNLKTtlhrlVADLEVETNNLEERRKSelwvLQSVMDEDGDDSPVVHfEREAETFVTQKAFLDERFEILQQQLKDSEQy 167
Cdd:COG4717    152 EERLEE-----LRELEEELEELEAELAE----LQEELEELLEQLSLAT-EEELQDLAEELEELQQRLAELEEELEEAQE- 220

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  168 lanshattetelpppnlnvtkRLELKDAAVEAGNQALAAADEIERLKLPRWLqgfrIWALSLLAFVVLWIPIVAARAdlr 247
Cdd:COG4717    221 ---------------------ELEELEEELEQLENELEAAALEERLKEARLL----LLIAAALLALLGLGGSLLSLI--- 272

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  248 qfinpeltkpdWQWTAMAALTAAVIVVLFavLSLVSAQASLRSRFQSMLQHVSNARAARTGWEQKSQRYVDRMEGQASEW 327
Cdd:COG4717    273 -----------LTIAGVLFLVLGLLALLF--LLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEEL 339

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  328 RLEVeqRRIQQTQKLTEDIDSRIASLRNQTAAQQ-------------ATFEG---------EIQRQIQQIDHELT----T 381
Cdd:COG4717    340 LELL--DRIEELQELLREAEELEEELQLEELEQEiaallaeagvedeEELRAaleqaeeyqELKEELEELEEQLEellgE 417

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  382 AEQRIEARKVTDVQQALDRTNIELQTARDTC----EQQAQRTMARERLAEAELIATWRSIIDDLRttakesSVLAAATRR 457
Cdd:COG4717    418 LEELLEALDEEELEEELEELEEELEELEEELeelrEELAELEAELEQLEEDGELAELLQELEELK------AELRELAEE 491

                          490
                   ....*....|.
gi 1140107559  458 WPKAGTGQWTL 468
Cdd:COG4717    492 WAALKLALELL 502
T7SS_EccC_b TIGR03925
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ...
 713-822 1.77e-05

type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274859 [Multi-domain]  Cd Length: 566  Bit Score: 49.22  E-value: 1.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  713 AAETYVQLVRDV--GEQSRDARRV--EVSFNRIAPREDEiwshsTADGIDFPIGRA--GAARLQFMRlgrgtSQHALVAG 786
Cdd:TIGR03925  301 GTRGLVAVIRDVwgGPPAPPVRLLpaRLPLSALPAGGGA-----PRLRVPLGLGESdlAPVYVDFAE-----SPHLLIFG 370

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1140107559  787 KTGSGKSTLLHILITNLALHYSPNEIQFYLIDFKKG 822
Cdd:TIGR03925  371 DSESGKTTLLRTIARGIVRRYSPDQARLVVVDYRRT 406
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 10-447 2.39e-04

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: 45.82  E-value: 2.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559   10 NQLTSASQKIAECEVLRTELQRLQTHMETVVAERDQTLESLQQ---SALTNMQAERQRIHdNADRELDTLRLDCNSRRET 86
Cdd:TIGR02168  670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEeleQLRKELEELSRQIS-ALRKDLARLEAEVEQLEER 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559   87 LQQnlkttLHRLVADLEVETNNLEERRKSELWVLQSVMDEdgddspVVHFEREAETFVTQKAFLDERFEILQQQLKDSEQ 166
Cdd:TIGR02168  749 IAQ-----LSKELTELEAEIEELEERLEEAEEELAEAEAE------IEELEAQIEQLKEELKALREALDELRAELTLLNE 817

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  167 YLANshattetelpppnlNVTKRLELKDAAVEAGNQALAAADEIERLKlprwlqgfriwalsllafvvlwipivaaraDL 246
Cdd:TIGR02168  818 EAAN--------------LRERLESLERRIAATERRLEDLEEQIEELS------------------------------ED 853

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  247 RQFINPELTKpdwQWTAMAALTAAVIVVLFAVLSLVSAQASLRSRFQSMlqhvsnaRAARTGWEQKsqryVDRMEGQASE 326
Cdd:TIGR02168  854 IESLAAEIEE---LEELIEELESELEALLNERASLEEALALLRSELEEL-------SEELRELESK----RSELRRELEE 919

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  327 WRLEVEQRRIQQtQKLTEDIDSRIASLRNQtaaQQATFEgEIQRQIQQIDHELTTAEQRIearkvTDVQQALDRT-NIEL 405
Cdd:TIGR02168  920 LREKLAQLELRL-EGLEVRIDNLQERLSEE---YSLTLE-EAEALENKIEDDEEEARRRL-----KRLENKIKELgPVNL 989

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 1140107559  406 qTARDTCEQQAQR----TMARERLAEAelIATWRSIIDDLRTTAKE 447
Cdd:TIGR02168  990 -AAIEEYEELKERydflTAQKEDLTEA--KETLEEAIEEIDREARE 1032
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 21-175 1.17e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 42.44  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559   21 ECEVLRTELQRLQTHMEtvvAERDQTLESLQQSAlTNMQAERQRiHDNADRELDTLRLDCNSRRETLQQNlKTTLHRLVA 100
Cdd:pfam09787   69 QIQQLRTELQELEAQQQ---EEAESSREQLQELE-EQLATERSA-RREAEAELERLQEELRYLEEELRRS-KATLQSRIK 142

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  101 DLEVETnnleERRKSELWVLQSVMDEDGDDSPVVHFEREA--------ETFVTQKAFLDERFEILQQQLKDSEQYLANSH 172
Cdd:pfam09787  143 DREAEI----EKLRNQLTSKSQSSSSQSELENRLHQLTETliqkqtmlEALSTEKNSLVLQLERMEQQIKELQGEGSNGT 218


                   ...
gi 1140107559  173 ATT 175
Cdd:pfam09787  219 SIN 221
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 778-930 4.39e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 39.28  E-value: 4.39e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559   778 TSQHALVAGKTGSGKSTLLHIlitnLALHYSPNEIQFYLIDfkkGVEFRTYAAHKLPHARVIAIESDREFGLSVLERLDE 857
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARA----LARELGPPGGGVIYID---GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALAL 73

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1140107559   858 VLQERGElfrergvqdvpsfrkqfpsepmprlLLLIDEFQEFFVAEDRVSARASLLLDRLVRQGRAFGIHVLL 930
Cdd:smart00382   74 ARKLKPD-------------------------VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVIL 121
 
Name Accession Description Interval E-value
FtsK_SpoIIIE pfam01580
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ...
 776-936 9.41e-27

FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from prokaryotes and plasmids, termed the FtsK/SpoIIIE family. This domain contains a putative ATP binding P-loop motif. It is found in the FtsK cell division protein from E. coli and the stage III sporulation protein E SpoIIIE, which has roles in regulation of prespore specific gene expression in B. subtilis. A mutation in FtsK causes a temperature sensitive block in cell division and it is involved in peptidoglycan synthesis or modification. The SpoIIIE protein is implicated in intercellular chromosomal DNA transfer.


Pssm-ID: 279863 [Multi-domain]  Cd Length: 219  Bit Score: 109.77  E-value: 9.41e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  776 RGTSQHALVAGKTGSGKSTLLHILITNLALHYSPNEIQFYLIDFkKGVEFRTYAahKLPHARVIAIESDREFGLSVLERL 855
Cdd:pfam01580   35 KKMPVHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDP-KMGELSAYE--DIPHLLSVPVATDPKRALRALEWL 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  856 DEVLQERGELFRERGVQDVPSFRKQFP--------------------------SEPMPRLLLLIDEFQEF-FVAEDRVSA 908
Cdd:pfam01580  112 VDEMERRYALFRALGVRSIAGYNGEIAedpldgfgdvflviygvhvmctagrwLEILPYLVVIVDERAELrLAAPKDSEM 191

                          170       180
                   ....*....|....*....|....*...
gi 1140107559  909 RASLLLDRLVRQGRAFGIHVLLGSQTLG 936
Cdd:pfam01580  192 RVEDAIVRLAQKGRAAGIHLLLATQRPS 219
T7_EssCb_Firm TIGR03928
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ...
 781-1001 8.99e-22

type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274860 [Multi-domain]  Cd Length: 1296  Bit Score: 102.76  E-value: 8.99e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  781 HALVAGKTGSGKSTLLHILITNLALHYSPNEIQFYLIDFKKGVEFRTYAahKLPHArVIAI------ESDRefglsVLER 854
Cdd:TIGR03928  471 HGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKGGGMANLFK--NLPHL-LGTItnldgaQSMR-----ALAS 542

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  855 LDEVLQERGELFRERGVQDVPSFRKQF----PSEPMPRLLLLIDEFQEF------FVAEdRVSArasllldrlVRQGRAF 924
Cdd:TIGR03928  543 IKAELKKRQRLFGENNVNHINQYQKLYkqgkAKEPMPHLFLISDEFAELkseqpeFMKE-LVST---------ARIGRSL 612

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  925 GIHVLLGSQTLGGA-----YSLARStmgqiavRIALQC-SESDAHLILSedNPAARMLTRPGEAiYndangLRQGNHQ-- 996
Cdd:TIGR03928  613 GVHLILATQKPSGVvddqiWSNSRF-------KLALKVqDASDSNEILK--TPDAAEITVPGRA-Y-----LQVGNNEvy 677


                   ....*..
gi 1140107559  997 --FQIAW 1001
Cdd:TIGR03928  678 elFQSAW 684
T7SS_EccC_a TIGR03924
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ...
 781-935 4.91e-21

type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274858 [Multi-domain]  Cd Length: 658  Bit Score: 99.28  E-value: 4.91e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  781 HALVAGKTGSGKSTLLHILITNLALHYSPNEIQFYLIDFKKGVEFRTYAahKLPHarVIAIESDREFGLSVLERLDEVL- 859
Cdd:TIGR03924  437 HGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKGGATFLGLE--GLPH--VSAVITNLADEAPLVDRMQDALa 512

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  860 ---QERGELFRERG-VQDVPSFRKQF----PSEPMPRLLLLIDEFQEFFVAEDRVSAraslLLDRLVRQGRAFGIHVLLG 931
Cdd:TIGR03924  513 gemNRRQELLRAAGnFANVAEYEKARaagaDLPPLPALFVVVDEFSELLSQHPDFAD----LFVAIGRLGRSLGVHLLLA 588


                   ....
gi 1140107559  932 SQTL 935
Cdd:TIGR03924  589 SQRL 592
T7_EssCb_Firm TIGR03928
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ...
 742-966 1.74e-18

type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274860 [Multi-domain]  Cd Length: 1296  Bit Score: 91.97  E-value: 1.74e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  742 APREDEIWShSTADGIDFPIG--------RAGAARLQFMRLGrgtsqHALVAGKTGSGKSTLLHILITNLALHYSPNEIQ 813
Cdd:TIGR03928  771 AVEFDKLWS-KPKEPLQATIGllddpelqSQEPLTLDLSKDG-----HLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLH 844

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  814 FYLIDFKKG--VEFRtyaahKLPH-ARVIAIESDREFGlSVLERLDEVLQERGELFRERGVQDVPSFRKQfPSEPMPRLL 890
Cdd:TIGR03928  845 FYLFDFGTNglLPLK-----KLPHvADYFTLDEEEKIE-KLIRRIKKEIDRRKKLFSEYGVASISMYNKA-SGEKLPQIV 917

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1140107559  891 LLIDEFQEffVAEDRVSARASLLLDRLVRQGRAFGIHVLLgsqTLGGAYSLARSTMGQIAVRIALQCSE-SDAHLIL 966
Cdd:TIGR03928  918 IIIDNYDA--VKEEPFYEDFEELLIQLAREGASLGIYLVM---TAGRQNAVRMPLMNNIKTKIALYLIDkSEYRSIV 989
T7SS_EccC_b TIGR03925
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ...
 777-955 1.54e-16

type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274859 [Multi-domain]  Cd Length: 566  Bit Score: 84.66  E-value: 1.54e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  777 GTSQHALVAGKTGSGKSTLLHILITNLALHYSPNEIQFYLIDFKKGvefrTYAA-HKLPHARVIAIESDREFGLSVLERL 855
Cdd:TIGR03925   77 GAAGHVAIVGAPQSGKSTALRTLILALALTHTPEEVQFYCLDFGGG----GLASlADLPHVGGVAGRLDPERVRRTVAEV 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  856 DEVLQERGELFRERGVQDVPSFRK-----QFPSEPMPRLLLLIDEF----QEFFVAEDRVSArasllldrLVRQGRAFGI 926
Cdd:TIGR03925  153 EGLLRRRERLFRTHGIDSMAQYRArraagRLPEDPFGDVFLVIDGWgtlrQDFEDLEDKVTD--------LAARGLAYGV 224

                          170       180       190
                   ....*....|....*....|....*....|
gi 1140107559  927 HVLLGSqtlgGAYSLARSTM-GQIAVRIAL 955
Cdd:TIGR03925  225 HVVLTA----SRWSEIRPALrDLIGTRIEL 250
FtsK COG1674
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ...
 781-933 1.72e-11

DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441280 [Multi-domain]  Cd Length: 611  Bit Score: 68.80  E-value: 1.72e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  781 HALVAGKTGSGKSTLLHILITNLALHYSPNEIQFYLIDFKKgVEFRTYAahKLPHArVIAIESDREFGLSVLERLDEVLQ 860
Cdd:COG1674    283 HLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDPKM-VELSVYN--GIPHL-LTPVVTDPKKAANALKWAVREME 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  861 ERGELFRERGVQDVPSFRKQFPS-----------EPMPRLLLLIDEFQE-FFVAEDRVSAraslLLDRLVRQGRAFGIHV 928
Cdd:COG1674    359 RRYKLFAKAGVRNIAGYNEKVREakakgeeeeglEPLPYIVVIIDELADlMMVAGKEVEE----AIARLAQKARAAGIHL 434


                   ....*
gi 1140107559  929 LLGSQ 933
Cdd:COG1674    435 ILATQ 439
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 781-988 1.08e-09

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 63.18  E-value: 1.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  781 HALVAGKTGSGKSTLLHILITNLALHYSPNEIQFYLIDfKKGVEFRTYAAhkLPHArVIAIESDREFGLSVLERLDEVLQ 860
Cdd:PRK10263  1012 HLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMID-PKMLELSVYEG--IPHL-LTEVVTDMKDAANALRWCVNEME 1087

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  861 ERGELFRERGVQD-----------------VP--------SFRKQFPS-EPMPRLLLLIDEFQEFFVAedrVSARASLLL 914
Cdd:PRK10263  1088 RRYKLMSALGVRNlagynekiaeadrmmrpIPdpywkpgdSMDAQHPVlKKEPYIVVLVDEFADLMMT---VGKKVEELI 1164

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1140107559  915 DRLVRQGRAFGIHVLLGSQ--TLGGAYSLARStmgQIAVRIALQCSES-DAHLILseDNPAARMLTRPGEAIYNDAN 988
Cdd:PRK10263  1165 ARLAQKARAAGIHLVLATQrpSVDVITGLIKA---NIPTRIAFTVSSKiDSRTIL--DQAGAESLLGMGDMLYSGPN 1236
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
8-468 2.09e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.54  E-value: 2.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559    8 LTNQLTSASQKIAECEVLRTELQRLQTHMETVVAErdqtLESLQQSALTNMQAERQRIHDNADRELDTLRLDCNSRRETL 87
Cdd:COG4717     76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAE----LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEEL 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559   88 QQNLKTtlhrlVADLEVETNNLEERRKSelwvLQSVMDEDGDDSPVVHfEREAETFVTQKAFLDERFEILQQQLKDSEQy 167
Cdd:COG4717    152 EERLEE-----LRELEEELEELEAELAE----LQEELEELLEQLSLAT-EEELQDLAEELEELQQRLAELEEELEEAQE- 220

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  168 lanshattetelpppnlnvtkRLELKDAAVEAGNQALAAADEIERLKLPRWLqgfrIWALSLLAFVVLWIPIVAARAdlr 247
Cdd:COG4717    221 ---------------------ELEELEEELEQLENELEAAALEERLKEARLL----LLIAAALLALLGLGGSLLSLI--- 272

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  248 qfinpeltkpdWQWTAMAALTAAVIVVLFavLSLVSAQASLRSRFQSMLQHVSNARAARTGWEQKSQRYVDRMEGQASEW 327
Cdd:COG4717    273 -----------LTIAGVLFLVLGLLALLF--LLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEEL 339

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  328 RLEVeqRRIQQTQKLTEDIDSRIASLRNQTAAQQ-------------ATFEG---------EIQRQIQQIDHELT----T 381
Cdd:COG4717    340 LELL--DRIEELQELLREAEELEEELQLEELEQEiaallaeagvedeEELRAaleqaeeyqELKEELEELEEQLEellgE 417

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  382 AEQRIEARKVTDVQQALDRTNIELQTARDTC----EQQAQRTMARERLAEAELIATWRSIIDDLRttakesSVLAAATRR 457
Cdd:COG4717    418 LEELLEALDEEELEEELEELEEELEELEEELeelrEELAELEAELEQLEEDGELAELLQELEELK------AELRELAEE 491

                          490
                   ....*....|.
gi 1140107559  458 WPKAGTGQWTL 468
Cdd:COG4717    492 WAALKLALELL 502
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 5-388 2.22e-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: 2.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559    5 EISLTNQLTSASQKIAECEVLRTELQRLQTHMETVVAERDQTLESLQQSALTNMQAERQRIHDNADRELDTLRLDCNSRR 84
Cdd:COG1196    381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559   85 ETLQQNLKTTLHRLVADLEVETNNLEERRKSELWVLQSVMDEDGDDSPVVHFEREAEtfvtQKAFLDERFEILQQQLKDS 164
Cdd:COG1196    461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA----GLRGLAGAVAVLIGVEAAY 536

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  165 EQYLANSHATTETELPPPNLNVTKRLELKDAAVEAGNQALAAADEIERLKLPR--WLQGFRIWALSLLAFVVLWIPIVAA 242
Cdd:COG1196    537 EAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAaaLARGAIGAAVDLVASDLREADARYY 616

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  243 RADLRQFINPELTKPDWQWTAMAALTAAVIVVLFAVLSLVSAQASLRSRFQSMLQHVSNARAARTGwEQKSQRYVDRMEG 322
Cdd:COG1196    617 VLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELE-ELAERLAEEELEL 695

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  323 QASEWRLEVEQRRIQQTQKLTEDIDSRIASLRNQTAAQQATFEGEIQRQ-----------------IQQIDHELTTAEQR 385
Cdd:COG1196    696 EEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEeelleeealeelpeppdLEELERELERLERE 775


                   ...
gi 1140107559  386 IEA 388
Cdd:COG1196    776 IEA 778
T7SS_EccC_b TIGR03925
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ...
 713-822 1.77e-05

type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274859 [Multi-domain]  Cd Length: 566  Bit Score: 49.22  E-value: 1.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  713 AAETYVQLVRDV--GEQSRDARRV--EVSFNRIAPREDEiwshsTADGIDFPIGRA--GAARLQFMRlgrgtSQHALVAG 786
Cdd:TIGR03925  301 GTRGLVAVIRDVwgGPPAPPVRLLpaRLPLSALPAGGGA-----PRLRVPLGLGESdlAPVYVDFAE-----SPHLLIFG 370

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1140107559  787 KTGSGKSTLLHILITNLALHYSPNEIQFYLIDFKKG 822
Cdd:TIGR03925  371 DSESGKTTLLRTIARGIVRRYSPDQARLVVVDYRRT 406
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 10-447 2.39e-04

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: 45.82  E-value: 2.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559   10 NQLTSASQKIAECEVLRTELQRLQTHMETVVAERDQTLESLQQ---SALTNMQAERQRIHdNADRELDTLRLDCNSRRET 86
Cdd:TIGR02168  670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEeleQLRKELEELSRQIS-ALRKDLARLEAEVEQLEER 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559   87 LQQnlkttLHRLVADLEVETNNLEERRKSELWVLQSVMDEdgddspVVHFEREAETFVTQKAFLDERFEILQQQLKDSEQ 166
Cdd:TIGR02168  749 IAQ-----LSKELTELEAEIEELEERLEEAEEELAEAEAE------IEELEAQIEQLKEELKALREALDELRAELTLLNE 817

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  167 YLANshattetelpppnlNVTKRLELKDAAVEAGNQALAAADEIERLKlprwlqgfriwalsllafvvlwipivaaraDL 246
Cdd:TIGR02168  818 EAAN--------------LRERLESLERRIAATERRLEDLEEQIEELS------------------------------ED 853

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  247 RQFINPELTKpdwQWTAMAALTAAVIVVLFAVLSLVSAQASLRSRFQSMlqhvsnaRAARTGWEQKsqryVDRMEGQASE 326
Cdd:TIGR02168  854 IESLAAEIEE---LEELIEELESELEALLNERASLEEALALLRSELEEL-------SEELRELESK----RSELRRELEE 919

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  327 WRLEVEQRRIQQtQKLTEDIDSRIASLRNQtaaQQATFEgEIQRQIQQIDHELTTAEQRIearkvTDVQQALDRT-NIEL 405
Cdd:TIGR02168  920 LREKLAQLELRL-EGLEVRIDNLQERLSEE---YSLTLE-EAEALENKIEDDEEEARRRL-----KRLENKIKELgPVNL 989

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 1140107559  406 qTARDTCEQQAQR----TMARERLAEAelIATWRSIIDDLRTTAKE 447
Cdd:TIGR02168  990 -AAIEEYEELKERydflTAQKEDLTEA--KETLEEAIEEIDREARE 1032
HerA COG0433
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ...
 778-869 2.67e-04

Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase domains [Replication, recombination and repair];


Pssm-ID: 440202 [Multi-domain]  Cd Length: 388  Bit Score: 44.98  E-value: 2.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  778 TSQHALVAGKTGSGKSTLLHILITNLALHYSPneiqFYLIDFkKGvEFRTYAAHKLPHA--RVIAIESDREFGLSVLErL 855
Cdd:COG0433     46 LNRHILILGATGSGKSNTLQVLLEELSRAGVP----VLVFDP-HG-EYSGLAEPGAERAdvGVFDPGAGRPLPINPWD-L 118

                           90
                   ....*....|....
gi 1140107559  856 DEVLQERGELFRER 869
Cdd:COG0433    119 FATASELGPLLLSR 132
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 11-458 5.47e-04

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: 44.66  E-value: 5.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559   11 QLTSASQKIAECEVLRTELQRLQTHMETVVAERDQTLESLQ------QSALTNMQAERQ---RIHDNADRELDTLRLDCN 81
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKeeleslEAELEELEAELEeleSRLEELEEQLETLRSKVA 389

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559   82 SRRETL------QQNLKTTLHRLVADLEVETNNLEERRK--SELWVLQSVMDEDGDDSPVVHFEREAETFVTQKAFLDER 153
Cdd:TIGR02168  390 QLELQIaslnneIERLEARLERLEDRRERLQQEIEELLKklEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  154 FEILQQQLKDSEQYLANSHAttetelpppNLNVTKRL-ELKDAAVEAGNQALAAADEIERLkLPRWLQGFRI---WAL-- 227
Cdd:TIGR02168  470 LEEAEQALDAAERELAQLQA---------RLDSLERLqENLEGFSEGVKALLKNQSGLSGI-LGVLSELISVdegYEAai 539

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  228 ------SLLAFVV----LWIPIVAA----RADLRQFINPELTKPDW-QWTAMAALTAAVIVVLFAvLSLVSAQASLRSRF 292
Cdd:TIGR02168  540 eaalggRLQAVVVenlnAAKKAIAFlkqnELGRVTFLPLDSIKGTEiQGNDREILKNIEGFLGVA-KDLVKFDPKLRKAL 618

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  293 QSMLQHVSNARAARTGWEQKSQ-----RYVDRmEGQASEWRLEVEQRRIQQTQKLTEDiDSRIASLRNQTAAQQATFEgE 367
Cdd:TIGR02168  619 SYLLGGVLVVDDLDNALELAKKlrpgyRIVTL-DGDLVRPGGVITGGSAKTNSSILER-RREIEELEEKIEELEEKIA-E 695

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  368 IQRQIQQIDHELTTAEQRIEARKV--TDVQQALDRTNIELQTARDTCEQQAQRtMARERLAEAELIATWRSIIDDLrttA 445
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKelEELSRQISALRKDLARLEAEVEQLEER-IAQLSKELTELEAEIEELEERL---E 771

                          490
                   ....*....|...
gi 1140107559  446 KESSVLAAATRRW 458
Cdd:TIGR02168  772 EAEEELAEAEAEI 784
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
20-458 5.70e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 5.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559   20 AECEVLRTELQRLQTHMETVVAERDQTLESLQQSALTNMQAERQRIhDNADRELDTLRLDCNSRRETLQQnlkttLHRLV 99
Cdd:COG4913    295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRL-EQLEREIERLERELEERERRRAR-----LEALL 368

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  100 ADLEVETNNLEErrksELWVLQsvmdedgddspvvhfeREAETFVTQKAFLDERFEILQQQLKDSEQYLANSHATTETEL 179
Cdd:COG4913    369 AALGLPLPASAE----EFAALR----------------AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  180 ----------PPPNLNVtkRLELKDAAVEAGNQALAAADEIE-RLKLPRW-------LQGFRiwaLSLLafvvlwipiVA 241
Cdd:COG4913    429 aslerrksniPARLLAL--RDALAEALGLDEAELPFVGELIEvRPEEERWrgaiervLGGFA---LTLL---------VP 494

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  242 AR--ADLRQFINPELTKPDWQWTAMAALTAAVIVVLFAVLSLVS------------AQASLRSRFQSM-------LQHVS 300
Cdd:COG4913    495 PEhyAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGkldfkphpfrawLEAELGRRFDYVcvdspeeLRRHP 574

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  301 NA-------RAARTGWEQKSQRYVDR--MEGQASEWRLEVEQRRIQQTQKLTEDIDSRIASLRNQTAAQQATFEgEIQRQ 371
Cdd:COG4913    575 RAitragqvKGNGTRHEKDDRRRIRSryVLGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERRE-ALQRL 653

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  372 IQQIDHELTTAEQRIEARKVTDVQQALDRTNIELQTARDTCEQ-QAQRTMARERLAEAEL--------IATWRSIIDDLR 442
Cdd:COG4913    654 AEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEElEAELEELEEELDELKGeigrlekeLEQAEEELDELQ 733

                          490
                   ....*....|....*.
gi 1140107559  443 TTAKESSVLAAATRRW 458
Cdd:COG4913    734 DRLEAAEDLARLELRA 749
VirD4 COG3505
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ...
 887-968 7.26e-04

Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442728 [Multi-domain]  Cd Length: 402  Bit Score: 43.43  E-value: 7.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  887 PRLLLLIDEFQEFFVAEDrvsarasllLDRLVRQGRAFGIHVLLGSQTLG---GAY--SLARSTMGQIAVRIALQCSESD 961
Cdd:COG3505    247 RPVLLLLDEFANLGRLPS---------LETLLATGRGYGIRLVLILQSLAqleAIYgeEGAETILGNCGTKIFLGVNDPE 317


                   ....*..
gi 1140107559  962 AHLILSE 968
Cdd:COG3505    318 TAEYLSE 324
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 328-457 1.04e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  328 RLEVEQRRIQQTQKLTEDIDSRIASLRNQTAAQQATF---EGEIQRQIQQIDHELTTAEQRIEAR-KVTDVQQALDRTNI 403
Cdd:COG1196    254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEyelLAELARLEQDIARLEERRRELEERLeELEEELAELEEELE 333

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1140107559  404 ELQTARDTCEQQAQRTMARERLAEAELIATWRSIIDDLRTTAKESSVLAAATRR 457
Cdd:COG1196    334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
11-459 1.12e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559   11 QLTSASQKIAECEVLRTELQRLQTHMETVVAERDQTLESLQQSALTNMQAERQRIH---DNADRELDTLRLDCNSRRETL 87
Cdd:COG4913    253 LLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEaelERLEARLDALREELDELEAQI 332

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559   88 QQN---LKTTLHRLVADLEVETNNLEERRKS---ELWVLQSVMDEDGDDspvvhFEREAETFVTQKAFLDERFEILQQQ- 160
Cdd:COG4913    333 RGNggdRLEQLEREIERLERELEERERRRARleaLLAALGLPLPASAEE-----FAALRAEAAALLEALEEELEALEEAl 407

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  161 --LKDSEQYLANSHATTETEL----------PPPNLNVtkRLELKDA--------------------------AVEA--G 200
Cdd:COG4913    408 aeAEAALRDLRRELRELEAEIaslerrksniPARLLAL--RDALAEAlgldeaelpfvgelievrpeeerwrgAIERvlG 485

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  201 NQAL----------AAADEIERLKLPRWLQGFRI------------------------------WALSLLA--FVVLwip 238
Cdd:COG4913    486 GFALtllvppehyaAALRWVNRLHLRGRLVYERVrtglpdperprldpdslagkldfkphpfraWLEAELGrrFDYV--- 562

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  239 IVAARADLRQF---INPE-LTK---------------PDWQ--WTAMAALTAavivvlfavlsLVSAQASLRSRFQSMLQ 297
Cdd:COG4913    563 CVDSPEELRRHpraITRAgQVKgngtrhekddrrrirSRYVlgFDNRAKLAA-----------LEAELAELEEELAEAEE 631

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  298 HVSNARAARTGWEQKSQRYVDRMEGQASEWRLEVEQRRIQQTQKLTEDIDSRIASLRnqtaaqqatfegEIQRQIQQIDH 377
Cdd:COG4913    632 RLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLA------------ALEEQLEELEA 699

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  378 ELTTAEQRIEA--RKVTDVQQALDRTNIELQTARDTCE------QQAQRTMARERLAEA-------ELIATWRSIIDDLR 442
Cdd:COG4913    700 ELEELEEELDElkGEIGRLEKELEQAEEELDELQDRLEaaedlaRLELRALLEERFAAAlgdaverELRENLEERIDALR 779

                          570       580
                   ....*....|....*....|..
gi 1140107559  443 TTAKES-----SVLAAATRRWP 459
Cdd:COG4913    780 ARLNRAeeeleRAMRAFNREWP 801
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 21-175 1.17e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 42.44  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559   21 ECEVLRTELQRLQTHMEtvvAERDQTLESLQQSAlTNMQAERQRiHDNADRELDTLRLDCNSRRETLQQNlKTTLHRLVA 100
Cdd:pfam09787   69 QIQQLRTELQELEAQQQ---EEAESSREQLQELE-EQLATERSA-RREAEAELERLQEELRYLEEELRRS-KATLQSRIK 142

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  101 DLEVETnnleERRKSELWVLQSVMDEDGDDSPVVHFEREA--------ETFVTQKAFLDERFEILQQQLKDSEQYLANSH 172
Cdd:pfam09787  143 DREAEI----EKLRNQLTSKSQSSSSQSELENRLHQLTETliqkqtmlEALSTEKNSLVLQLERMEQQIKELQGEGSNGT 218


                   ...
gi 1140107559  173 ATT 175
Cdd:pfam09787  219 SIN 221
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 17-166 1.55e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.80  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559   17 QKIAECEVLRTELQRL-QTHMETVVAERDQTLESLQQSALT-NMQAERQRiHDNADRELDTLRLDcnsrRETLQQNLKTT 94
Cdd:pfam17380  417 QQKVEMEQIRAEQEEArQREVRRLEEERAREMERVRLEEQErQQQVERLR-QQEEERKRKKLELE----KEKRDRKRAEE 491

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1140107559   95 LHRLVADLEVETNN---LEERRKSELwvLQSVMDEDGDDSPVVHFEREAETFVTQKAFLDERFEILQQQLKDSEQ 166
Cdd:pfam17380  492 QRRKILEKELEERKqamIEEERKRKL--LEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEE 564
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 778-930 4.39e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 39.28  E-value: 4.39e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559   778 TSQHALVAGKTGSGKSTLLHIlitnLALHYSPNEIQFYLIDfkkGVEFRTYAAHKLPHARVIAIESDREFGLSVLERLDE 857
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARA----LARELGPPGGGVIYID---GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALAL 73

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1140107559   858 VLQERGElfrergvqdvpsfrkqfpsepmprlLLLIDEFQEFFVAEDRVSARASLLLDRLVRQGRAFGIHVLL 930
Cdd:smart00382   74 ARKLKPD-------------------------VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVIL 121
DUF3375 pfam11855
Protein of unknown function (DUF3375); This family of proteins are functionally ...
 315-429 6.48e-03

Protein of unknown function (DUF3375); This family of proteins are functionally uncharacterized. This protein is found in bacteria. Proteins in this family are typically between 479 to 499 amino acids in length.


Pssm-ID: 463373  Cd Length: 469  Bit Score: 40.70  E-value: 6.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  315 RYVDRMEGQ---ASEWRLEVEQRRIQQ-TQKLTEDIDSRIASLRnqtaaqqatfegeiqRQIQQIDHELttaeQRIEARK 390
Cdd:pfam11855  101 RFVARLDERrfvATESRLNTVFDALRQlAEGTEPDPEERLAELE---------------AEIAEIDAEI----DRLRAGE 161

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1140107559  391 VT--DVQQALDRTNIELQTARD---------TCEQQAQRTMaRERLAEAE 429
Cdd:pfam11855  162 VPelDDTQALERAREILQLARElpadfrrveDEFRQLDREL-RERIIDWD 210
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
312-429 7.02e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 40.63  E-value: 7.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  312 KSQRYVDRMEGQASEWRLEV---EQRRIQQTQKLTEDIDSRIAslrnQTAAQQatfegEIQRQIQQIDHELTTAEQRIEA 388
Cdd:COG2268    229 EQEREIETARIAEAEAELAKkkaEERREAETARAEAEAAYEIA----EANAER-----EVQRQLEIAEREREIELQEKEA 299

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1140107559  389 RKVTDVQQALDRTNIELQTARDTCEQQAQRTMARER-LAEAE 429
Cdd:COG2268    300 EREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKgLAEAE 341
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 89-427 7.53e-03

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: 40.72  E-value: 7.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559   89 QNLKTTLHRLVADLEVETNNLEERRKSELWVLQSVMDEDGDDSPVVHFEREAETFVTQKAFLDERFEILQQQLKDSEQYL 168
Cdd:TIGR00618  190 KSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARI 269

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  169 anshattetelpppnlnvtKRLELKDAAVEAGNQALAAADEIERLklprwlqgfriwalsllafvvlwIPIVAARADLRQ 248
Cdd:TIGR00618  270 -------------------EELRAQEAVLEETQERINRARKAAPL-----------------------AAHIKAVTQIEQ 307

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  249 FINPELTKPDWQWTAMAALTAAVIVVLFAVLSLVSAQASLRSRFQsmlQHVSNARAA--RTGW-EQKSQRYVDRMEGQAS 325
Cdd:TIGR00618  308 QAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHS---QEIHIRDAHevATSIrEISCQQHTLTQHIHTL 384

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  326 EWRLEVEQRRIQQTQKLTEDIDSRIASLRNQTAAQQ------ATFEGEIQRQ-----IQQIDHELTTAEQRIEARKVTDV 394
Cdd:TIGR00618  385 QQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRdlqgqlAHAKKQQELQqryaeLCAAAITCTAQCEKLEKIHLQES 464

                          330       340       350
                   ....*....|....*....|....*....|...
gi 1140107559  395 QQALDRTNIELQTARDTCEQQAQRTMARERLAE 427
Cdd:TIGR00618  465 AQSLKEREQQLQTKEQIHLQETRKKAVVLARLL 497
VirB4 COG3451
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ...
 776-857 9.27e-03

Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442674 [Multi-domain]  Cd Length: 546  Bit Score: 40.32  E-value: 9.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  776 RGTSQHALVAGKTGSGKSTLLHILITNLALHyspnEIQFYLIDfkKGVEFRTYAahKLPHARVIAIESDREFGLSVLERL 855
Cdd:COG3451    201 GLDNGNTLILGPSGSGKSFLLKLLLLQLLRY----GARIVIFD--PGGSYEILV--RALGGTYIDLSPGSPTGLNPFDLE 272


                   ..
gi 1140107559  856 DE 857
Cdd:COG3451    273 DT 274
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 284-457 9.30e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 9.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  284 AQASLRSRFQSMLQHVSNARAARTGWEQKSQRYVDRMEG-----QASEWRLEVEQRRIQQTQKLTEDIDSRIASLRNQTA 358
Cdd:COG1196    275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRREleerlEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140107559  359 AQQATFEgEIQRQIQQIDHELTTAEQRIEARKVTdvQQALDRTNIELQTARDTCEQQAQRTMARERLAEAELIATWRSII 438
Cdd:COG1196    355 EAEAELA-EAEEALLEAEAELAEAEEELEELAEE--LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431

                          170
                   ....*....|....*....
gi 1140107559  439 DDLRTTAKESSVLAAATRR 457
Cdd:COG1196    432 ELEEEEEEEEEALEEAAEE 450
 
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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