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Conserved domains on  [gi|1765992902|gb|KAB6762570|]
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cell division protein FtsK [Bifidobacterium longum]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
T7_EssCb_Firm super family cl37349
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ...
 110-439 2.90e-47

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]


The actual alignment was detected with superfamily member TIGR03928:

Pssm-ID: 274860 [Multi-domain]  Cd Length: 1296  Bit Score: 178.26  E-value: 2.90e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902  110 IVGHWLE---PLDLAVPIGMTG-SEPLMLDLNRQ--GPHALVAGTTGSGKSVLLQSWCLALASMNGPEHLNFVFLDFKGG 183
Cdd:TIGR03928  433 IQERWAKnetYKSLAVPIGLRGkDDIVYLNLHEKahGPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKGG 512

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902  184 SAFRKLERLPHTVGSVCDLDLAHAVRALRALEAELTRREQLSAAVHASDIRD---------MVNPPPRLIVVIDEFHALK 254
Cdd:TIGR03928  513 GMANLFKNLPHLLGTITNLDGAQSMRALASIKAELKKRQRLFGENNVNHINQyqklykqgkAKEPMPHLFLISDEFAELK 592

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902  255 DQLPDYVNRLVRIASLGRSLGMYLIACTQNPMGQVSADMKANMSVSICLRVRDRLQSCELLGDGRAADLSpaMPGAAF-- 332
Cdd:TIGR03928  593 SEQPEFMKELVSTARIGRSLGVHLILATQKPSGVVDDQIWSNSRFKLALKVQDASDSNEILKTPDAAEIT--VPGRAYlq 670

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902  333 ---------------------------------CNDSEQVTAFRCATARD------------IDAVCRQIAFASRFVGSP 367
Cdd:TIGR03928  671 vgnnevyelfqsawsgapydpdkdkkeeediymINDLGQYELLNEDLSGLkrkkeikevpteLEAVIDEIQAYTEELNIE 750

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902  368 PQPSLFTAPLPRHV----------KDRTVADHAPQRIRFGLADDGINLREATVSL---TGGNIGVIGPQGRGKTTLLKT- 433
Cdd:TIGR03928  751 ALPSPWLPPLEEKIylddlhavefDKLWSKPKEPLQATIGLLDDPELQSQEPLTLdlsKDGHLAIFGSPGYGKSTFLQTl 830


                   ....*....
gi 1765992902  434 ---LARHAS 439
Cdd:TIGR03928  831 imsLARQHS 839
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 413-525 1.24e-05

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: 45.44  E-value: 1.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902  413 TGGNIGVIGPQGRGKTTLLKTLARHASMADGLAVRVS-SPHRRVWSSQWLHGGRCTPYASSD-----------APPPPHI 480
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDgEDILEEVLDQLLLIIVGGKKASGSgelrlrlalalARKLKPD 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1765992902  481 VWFVDDADELFDP-FRTDEQALSFTHAL----ADESVSVVFAVSTIRPIR 525
Cdd:smart00382  81 VLILDEITSLLDAeQEALLLLLEELRLLlllkSEKNLTVILTTNDEKDLG 130
 
Name Accession Description Interval E-value
T7_EssCb_Firm TIGR03928
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ...
 110-439 2.90e-47

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: 178.26  E-value: 2.90e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902  110 IVGHWLE---PLDLAVPIGMTG-SEPLMLDLNRQ--GPHALVAGTTGSGKSVLLQSWCLALASMNGPEHLNFVFLDFKGG 183
Cdd:TIGR03928  433 IQERWAKnetYKSLAVPIGLRGkDDIVYLNLHEKahGPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKGG 512

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902  184 SAFRKLERLPHTVGSVCDLDLAHAVRALRALEAELTRREQLSAAVHASDIRD---------MVNPPPRLIVVIDEFHALK 254
Cdd:TIGR03928  513 GMANLFKNLPHLLGTITNLDGAQSMRALASIKAELKKRQRLFGENNVNHINQyqklykqgkAKEPMPHLFLISDEFAELK 592

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902  255 DQLPDYVNRLVRIASLGRSLGMYLIACTQNPMGQVSADMKANMSVSICLRVRDRLQSCELLGDGRAADLSpaMPGAAF-- 332
Cdd:TIGR03928  593 SEQPEFMKELVSTARIGRSLGVHLILATQKPSGVVDDQIWSNSRFKLALKVQDASDSNEILKTPDAAEIT--VPGRAYlq 670

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902  333 ---------------------------------CNDSEQVTAFRCATARD------------IDAVCRQIAFASRFVGSP 367
Cdd:TIGR03928  671 vgnnevyelfqsawsgapydpdkdkkeeediymINDLGQYELLNEDLSGLkrkkeikevpteLEAVIDEIQAYTEELNIE 750

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902  368 PQPSLFTAPLPRHV----------KDRTVADHAPQRIRFGLADDGINLREATVSL---TGGNIGVIGPQGRGKTTLLKT- 433
Cdd:TIGR03928  751 ALPSPWLPPLEEKIylddlhavefDKLWSKPKEPLQATIGLLDDPELQSQEPLTLdlsKDGHLAIFGSPGYGKSTFLQTl 830


                   ....*....
gi 1765992902  434 ---LARHAS 439
Cdd:TIGR03928  831 imsLARQHS 839
FtsK_SpoIIIE pfam01580
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ...
 117-285 4.29e-24

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: 100.53  E-value: 4.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902 117 PLDLAVPIGMTGsEPLMLDLNRQGPHALVAGTTGSGKSVLLQSWCLALASMNGPEHLNFVFLDFKGGsAFRKLERLPHTV 196
Cdd:pfam01580  16 RLPIALGKDISG-NPEVFDLKKMPVHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKMG-ELSAYEDIPHLL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902 197 GSVCDLDLAHAVRALRALEAELTRREQL------------------------------SAAVHASDIRDMV-NPPPRLIV 245
Cdd:pfam01580  94 SVPVATDPKRALRALEWLVDEMERRYALfralgvrsiagyngeiaedpldgfgdvflvIYGVHVMCTAGRWlEILPYLVV 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1765992902 246 VIDEF-----HALKDQLPDYVNRLVRIASLGRSLGMYLIACTQNP 285
Cdd:pfam01580 174 IVDERaelrlAAPKDSEMRVEDAIVRLAQKGRAAGIHLLLATQRP 218
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 117-323 7.01e-16

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 81.67  E-value: 7.01e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902  117 PLDLAVPIGM-TGSEPLMLDLNRQgPHALVAGTTGSGKSVLLQSWCLALASMNGPEHLNFVFLDFKgGSAFRKLERLPHT 195
Cdd:PRK10263   987 PSPLTVVLGKdIAGEPVVADLAKM-PHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPK-MLELSVYEGIPHL 1064

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902  196 VGSVCDlDLAHAVRALRALEAELTRREQLSAAVHASDI--------------RDMVNP---P--------------PRLI 244
Cdd:PRK10263  1065 LTEVVT-DMKDAANALRWCVNEMERRYKLMSALGVRNLagynekiaeadrmmRPIPDPywkPgdsmdaqhpvlkkePYIV 1143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902  245 VVIDEFHALKDQLPDYVNRLV-RIASLGRSLGMYLIACTQNPMGQV-SADMKANMSVSICLRVRDRLQSCELLGDGRAAD 322
Cdd:PRK10263  1144 VLVDEFADLMMTVGKKVEELIaRLAQKARAAGIHLVLATQRPSVDViTGLIKANIPTRIAFTVSSKIDSRTILDQAGAES 1223


                   .
gi 1765992902  323 L 323
Cdd:PRK10263  1224 L 1224
FtsK COG1674
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ...
 119-296 6.05e-14

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: 74.58  E-value: 6.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902 119 DLAVPIGMT-GSEPLMLDLNRQgPHALVAGTTGSGKSVLLQSwclALASM---NGPEHLNFVFLDFKggsafrKLE---- 190
Cdd:COG1674   260 PLPIALGKDiSGEPVVADLAKM-PHLLIAGATGSGKSVCINA---MILSLlykATPDEVRLILIDPK------MVElsvy 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902 191 -RLPHTVGSVCDlDLAHAVRALRALEAELTRREQLSAAVHASDI------------RDMVNPP----PRLIVVIDEFHAL 253
Cdd:COG1674   330 nGIPHLLTPVVT-DPKKAANALKWAVREMERRYKLFAKAGVRNIagynekvreakaKGEEEEGleplPYIVVIIDELADL 408

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1765992902 254 -----KD--QLpdyvnrLVRIASLGRSLGMYLIACTQNPmgqvSAD-----MKAN 296
Cdd:COG1674   409 mmvagKEveEA------IARLAQKARAAGIHLILATQRP----SVDvitglIKAN 453
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 413-525 1.24e-05

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: 45.44  E-value: 1.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902  413 TGGNIGVIGPQGRGKTTLLKTLARHASMADGLAVRVS-SPHRRVWSSQWLHGGRCTPYASSD-----------APPPPHI 480
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDgEDILEEVLDQLLLIIVGGKKASGSgelrlrlalalARKLKPD 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1765992902  481 VWFVDDADELFDP-FRTDEQALSFTHAL----ADESVSVVFAVSTIRPIR 525
Cdd:smart00382  81 VLILDEITSLLDAeQEALLLLLEELRLLlllkSEKNLTVILTTNDEKDLG 130
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 392-435 1.14e-03

ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213231 [Multi-domain]  Cd Length: 211  Bit Score: 40.64  E-value: 1.14e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1765992902 392 QRIRFGLADDGINLReatvsLTGGNIGVIGPQGRGKTTLLKTLA 435
Cdd:cd03264     8 KRYGKKRALDGVSLT-----LGPGMYGLLGPNGAGKTTLMRILA 46
 
Name Accession Description Interval E-value
T7_EssCb_Firm TIGR03928
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ...
 110-439 2.90e-47

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: 178.26  E-value: 2.90e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902  110 IVGHWLE---PLDLAVPIGMTG-SEPLMLDLNRQ--GPHALVAGTTGSGKSVLLQSWCLALASMNGPEHLNFVFLDFKGG 183
Cdd:TIGR03928  433 IQERWAKnetYKSLAVPIGLRGkDDIVYLNLHEKahGPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKGG 512

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902  184 SAFRKLERLPHTVGSVCDLDLAHAVRALRALEAELTRREQLSAAVHASDIRD---------MVNPPPRLIVVIDEFHALK 254
Cdd:TIGR03928  513 GMANLFKNLPHLLGTITNLDGAQSMRALASIKAELKKRQRLFGENNVNHINQyqklykqgkAKEPMPHLFLISDEFAELK 592

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902  255 DQLPDYVNRLVRIASLGRSLGMYLIACTQNPMGQVSADMKANMSVSICLRVRDRLQSCELLGDGRAADLSpaMPGAAF-- 332
Cdd:TIGR03928  593 SEQPEFMKELVSTARIGRSLGVHLILATQKPSGVVDDQIWSNSRFKLALKVQDASDSNEILKTPDAAEIT--VPGRAYlq 670

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902  333 ---------------------------------CNDSEQVTAFRCATARD------------IDAVCRQIAFASRFVGSP 367
Cdd:TIGR03928  671 vgnnevyelfqsawsgapydpdkdkkeeediymINDLGQYELLNEDLSGLkrkkeikevpteLEAVIDEIQAYTEELNIE 750

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902  368 PQPSLFTAPLPRHV----------KDRTVADHAPQRIRFGLADDGINLREATVSL---TGGNIGVIGPQGRGKTTLLKT- 433
Cdd:TIGR03928  751 ALPSPWLPPLEEKIylddlhavefDKLWSKPKEPLQATIGLLDDPELQSQEPLTLdlsKDGHLAIFGSPGYGKSTFLQTl 830


                   ....*....
gi 1765992902  434 ---LARHAS 439
Cdd:TIGR03928  831 imsLARQHS 839
T7SS_EccC_a TIGR03924
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ...
 120-345 6.65e-41

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: 157.44  E-value: 6.65e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902 120 LAVPIGMTGS-EPLMLDL-----NRQGPHALVAGTTGSGKSVLLQSWCLALASMNGPEHLNFVFLDFKGGSAFRKLERLP 193
Cdd:TIGR03924 409 LRVPIGVGDDgEPVELDLkesaeGGMGPHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKGGATFLGLEGLP 488

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902 194 HTVGSVCDL-DLAHAV-RALRALEAELTRR-EQLSAAVHASDIRDM---------VNPPPRLIVVIDEFHALKDQLPDYV 261
Cdd:TIGR03924 489 HVSAVITNLaDEAPLVdRMQDALAGEMNRRqELLRAAGNFANVAEYekaraagadLPPLPALFVVVDEFSELLSQHPDFA 568

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902 262 NRLVRIASLGRSLGMYLIACTQNPMGQVSADMKANMSVSICLRVRDRLQSCELLGDGRAADLsPAMPGAAFCN-DSEQVT 340
Cdd:TIGR03924 569 DLFVAIGRLGRSLGVHLLLASQRLDEGRLRGLESHLSYRIGLKTFSASESRAVLGVPDAYHL-PSTPGAGYLKvDTAEPV 647


                  ....*
gi 1765992902 341 AFRCA 345
Cdd:TIGR03924 648 RFRAA 652
FtsK_SpoIIIE pfam01580
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ...
 117-285 4.29e-24

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: 100.53  E-value: 4.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902 117 PLDLAVPIGMTGsEPLMLDLNRQGPHALVAGTTGSGKSVLLQSWCLALASMNGPEHLNFVFLDFKGGsAFRKLERLPHTV 196
Cdd:pfam01580  16 RLPIALGKDISG-NPEVFDLKKMPVHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKMG-ELSAYEDIPHLL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902 197 GSVCDLDLAHAVRALRALEAELTRREQL------------------------------SAAVHASDIRDMV-NPPPRLIV 245
Cdd:pfam01580  94 SVPVATDPKRALRALEWLVDEMERRYALfralgvrsiagyngeiaedpldgfgdvflvIYGVHVMCTAGRWlEILPYLVV 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1765992902 246 VIDEF-----HALKDQLPDYVNRLVRIASLGRSLGMYLIACTQNP 285
Cdd:pfam01580 174 IVDERaelrlAAPKDSEMRVEDAIVRLAQKGRAAGIHLLLATQRP 218
T7_EssCb_Firm TIGR03928
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ...
 116-316 4.82e-23

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: 104.30  E-value: 4.82e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902  116 EPLDLAVPIGM------TGSEPLMLDLNRQGpHALVAGTTGSGKSVLLQSWCLALASMNGPEHLNFVFLDFkGGSAFRKL 189
Cdd:TIGR03928  781 PKEPLQATIGLlddpelQSQEPLTLDLSKDG-HLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLHFYLFDF-GTNGLLPL 858

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902  190 ERLPHTVGSVCDLDLAHAVRALRALEAELTRREQLSAAVHASDIrDMVN-----PPPRLIVVIDEFHALKDQ--LPDYVN 262
Cdd:TIGR03928  859 KKLPHVADYFTLDEEEKIEKLIRRIKKEIDRRKKLFSEYGVASI-SMYNkasgeKLPQIVIIIDNYDAVKEEpfYEDFEE 937

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1765992902  263 RLVRIASLGRSLGMYLIAcTQNPMGQVSADMKANMSVSICLRVRDRLQSCELLG 316
Cdd:TIGR03928  938 LLIQLAREGASLGIYLVM-TAGRQNAVRMPLMNNIKTKIALYLIDKSEYRSIVG 990
T7SS_EccC_b TIGR03925
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ...
 120-436 6.59e-21

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: 96.60  E-value: 6.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902 120 LAVPIGMTG------SEPLMLDLNRQGPHALVAGTTGSGKSVLLQSWCLALASMNGPEHLNFVFLDFkGGSAFRKLERLP 193
Cdd:TIGR03925  53 LTVPVGIVDrpfeqrQDPLVVDLSGAAGHVAIVGAPQSGKSTALRTLILALALTHTPEEVQFYCLDF-GGGGLASLADLP 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902 194 HtVGSVCD-LDLAHAVRALRALEAELTRREQLSAAVHASDI------RDMVNPPPR----LIVVIDEFHALKDQLPDYVN 262
Cdd:TIGR03925 132 H-VGGVAGrLDPERVRRTVAEVEGLLRRRERLFRTHGIDSMaqyrarRAAGRLPEDpfgdVFLVIDGWGTLRQDFEDLED 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902 263 RLVRIASLGRSLGMYLIACTQNPMGQVSAdMKANMSVSICLRVRDRLQSCelLGDGRAADLSPAMPGAAFCNDSEqvtAF 342
Cdd:TIGR03925 211 KVTDLAARGLAYGVHVVLTASRWSEIRPA-LRDLIGTRIELRLGDPMDSE--IDRRAAARVPAGRPGRGLTPDGL---HM 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902 343 RCATAR-------DIDAVCRQIAFASRFVGSPPQPSLFTapLPRHVKDRTVADHAPQ---RIRFGLadDGINLREATVSL 412
Cdd:TIGR03925 285 LIALPRldgiasvDDLGTRGLVAVIRDVWGGPPAPPVRL--LPARLPLSALPAGGGAprlRVPLGL--GESDLAPVYVDF 360

                         330       340
                  ....*....|....*....|....*
gi 1765992902 413 -TGGNIGVIGPQGRGKTTLLKTLAR 436
Cdd:TIGR03925 361 aESPHLLIFGDSESGKTTLLRTIAR 385
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 117-323 7.01e-16

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 81.67  E-value: 7.01e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902  117 PLDLAVPIGM-TGSEPLMLDLNRQgPHALVAGTTGSGKSVLLQSWCLALASMNGPEHLNFVFLDFKgGSAFRKLERLPHT 195
Cdd:PRK10263   987 PSPLTVVLGKdIAGEPVVADLAKM-PHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPK-MLELSVYEGIPHL 1064

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902  196 VGSVCDlDLAHAVRALRALEAELTRREQLSAAVHASDI--------------RDMVNP---P--------------PRLI 244
Cdd:PRK10263  1065 LTEVVT-DMKDAANALRWCVNEMERRYKLMSALGVRNLagynekiaeadrmmRPIPDPywkPgdsmdaqhpvlkkePYIV 1143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902  245 VVIDEFHALKDQLPDYVNRLV-RIASLGRSLGMYLIACTQNPMGQV-SADMKANMSVSICLRVRDRLQSCELLGDGRAAD 322
Cdd:PRK10263  1144 VLVDEFADLMMTVGKKVEELIaRLAQKARAAGIHLVLATQRPSVDViTGLIKANIPTRIAFTVSSKIDSRTILDQAGAES 1223


                   .
gi 1765992902  323 L 323
Cdd:PRK10263  1224 L 1224
FtsK COG1674
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ...
 119-296 6.05e-14

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: 74.58  E-value: 6.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902 119 DLAVPIGMT-GSEPLMLDLNRQgPHALVAGTTGSGKSVLLQSwclALASM---NGPEHLNFVFLDFKggsafrKLE---- 190
Cdd:COG1674   260 PLPIALGKDiSGEPVVADLAKM-PHLLIAGATGSGKSVCINA---MILSLlykATPDEVRLILIDPK------MVElsvy 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902 191 -RLPHTVGSVCDlDLAHAVRALRALEAELTRREQLSAAVHASDI------------RDMVNPP----PRLIVVIDEFHAL 253
Cdd:COG1674   330 nGIPHLLTPVVT-DPKKAANALKWAVREMERRYKLFAKAGVRNIagynekvreakaKGEEEEGleplPYIVVIIDELADL 408

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1765992902 254 -----KD--QLpdyvnrLVRIASLGRSLGMYLIACTQNPmgqvSAD-----MKAN 296
Cdd:COG1674   409 mmvagKEveEA------IARLAQKARAAGIHLILATQRP----SVDvitglIKAN 453
HerA COG0433
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ...
 121-308 3.99e-11

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: 65.01  E-value: 3.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902 121 AVPIG--MTGSEPLMLDLNR-QGPHALVAGTTGSGKSVLLQSWCLALASMNGPehlnFVFLDFKG---GSAFRKLER--- 191
Cdd:COG0433    25 GILIGklLSPGVPVYLDLDKlLNRHILILGATGSGKSNTLQVLLEELSRAGVP----VLVFDPHGeysGLAEPGAERadv 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902 192 -----------------LPHTVGSVCDL-------------DLAHAVRALRA----------LEAELTRREQLSAAV--- 228
Cdd:COG0433   101 gvfdpgagrplpinpwdLFATASELGPLllsrldlndtqrgVLREALRLADDkglllldlkdLIALLEEGEELGEEYgnv 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902 229 ------------------------HASDIRDMV-----------------------------------------NPPPRL 243
Cdd:COG0433   181 saasagallrrleslesadglfgePGLDLEDLLrtdgrvtvidlsglpeelqstfvlwllrelfearpevgdadDRKLPL 260

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1765992902 244 IVVIDEFHAL-KDQLPDYVNRLVRIASLGRSLGMYLIACTQNPmGQVSADMKANMSVSICLRV---RDR 308
Cdd:COG0433   261 VLVIDEAHLLaPAAPSALLEILERIAREGRKFGVGLILATQRP-SDIDEDVLSQLGTQIILRLfnpRDQ 328
T7SS_EccC_b TIGR03925
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ...
 103-181 1.10e-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: 48.45  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902 103 ARLPWRAIVGHWLEPlDLAVPIGMTGSE--PLMLDLNRQgPHALVAGTTGSGKSVLLQSWCLALASMNGPEHLNFVFLDF 180
Cdd:TIGR03925 326 ARLPLSALPAGGGAP-RLRVPLGLGESDlaPVYVDFAES-PHLLIFGDSESGKTTLLRTIARGIVRRYSPDQARLVVVDY 403


                  .
gi 1765992902 181 K 181
Cdd:TIGR03925 404 R 404
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 413-525 1.24e-05

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: 45.44  E-value: 1.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902  413 TGGNIGVIGPQGRGKTTLLKTLARHASMADGLAVRVS-SPHRRVWSSQWLHGGRCTPYASSD-----------APPPPHI 480
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDgEDILEEVLDQLLLIIVGGKKASGSgelrlrlalalARKLKPD 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1765992902  481 VWFVDDADELFDP-FRTDEQALSFTHAL----ADESVSVVFAVSTIRPIR 525
Cdd:smart00382  81 VLILDEITSLLDAeQEALLLLLEELRLLlllkSEKNLTVILTTNDEKDLG 130
T7_EssCb_Firm TIGR03928
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ...
 120-307 1.30e-04

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: 44.98  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902  120 LAVPIGM--TGSEPLMLDLnRQGPHALVAGTTGSGKSVLLQSWCLALAsMNGPEHLnfVFLDFKGGSaFRKLERLPHTVG 197
Cdd:TIGR03928 1075 GSIPIGLdeETVEPVYIDL-TENPHLLIVGESDDGKTNVLKSLLKTLA-KQEKEKI--GLIDSIDRG-LLAYRDLKEVAT 1149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902  198 SVCDLDLAHAVraLRALEAELTRREQlsAAVHASDIRDMVNPPPRLIVVIDEFHALKDQLpDYV--NRLVRIASLGRSLG 275
Cdd:TIGR03928 1150 YIEEKEDLKEI--LAELKEEIELREA--AYKEALQNETGEPAFKPILLIIDDLEDFIQRT-DLEiqDILALIMKNGKKLG 1224

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1765992902  276 MYLIACTQNPM-----GQVSADMKANMSVSICLRVRD 307
Cdd:TIGR03928 1225 IHFIVAGTHSElsksyDGVPKEIKQLRTGILGMRKSD 1261
VirB4 COG3451
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ...
 126-209 1.71e-04

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


Pssm-ID: 442674 [Multi-domain]  Cd Length: 546  Bit Score: 44.55  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902 126 MTGSEPLMLDL--NRQGPHALVAGTTGSGKSVLLQsWCLALASMNGPEhlnFVFLDfKGGSAFRKLERLPhtvGSVCDLD 203
Cdd:COG3451   188 TRSGTPVFFDFhdGLDNGNTLILGPSGSGKSFLLK-LLLLQLLRYGAR---IVIFD-PGGSYEILVRALG---GTYIDLS 259


                  ....*.
gi 1765992902 204 LAHAVR 209
Cdd:COG3451   260 PGSPTG 265
VirD4 COG3505
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ...
 240-307 5.20e-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: 42.66  E-value: 5.20e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1765992902 240 PPRLIVVIDEFHALKdqlpdYVNRLVRIASLGRSLGMYLIACTQNpMGQVSAD--------MKANMSVSICLRVRD 307
Cdd:COG3505   246 PRPVLLLLDEFANLG-----RLPSLETLLATGRGYGIRLVLILQS-LAQLEAIygeegaetILGNCGTKIFLGVND 315
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 392-435 1.14e-03

ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213231 [Multi-domain]  Cd Length: 211  Bit Score: 40.64  E-value: 1.14e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1765992902 392 QRIRFGLADDGINLReatvsLTGGNIGVIGPQGRGKTTLLKTLA 435
Cdd:cd03264     8 KRYGKKRALDGVSLT-----LGPGMYGLLGPNGAGKTTLMRILA 46
AAA_22 pfam13401
AAA domain;
136-274 1.31e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 39.25  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902 136 LNRQGPHALVAGTTGSGKSVLLQswclALASMNGPEHLNFVFLDFKGGSAFRklerlphtvgsvcdlDLAHAVraLRALE 215
Cdd:pfam13401   1 IRFGAGILVLTGESGTGKTTLLR----RLLEQLPEVRDSVVFVDLPSGTSPK---------------DLLRAL--LRALG 59

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902 216 AELTRREQLSAAVHAsdIRDMVN-PPPRLIVVIDEFHALKDQLpdyVNRLVRIASLGRSL 274
Cdd:pfam13401  60 LPLSGRLSKEELLAA--LQQLLLaLAVAVVLIIDEAQHLSLEA---LEELRDLLNLSSKL 114
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 139-274 1.53e-03

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 39.79  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992902 139 QGPHALVAGTTGSGKSVLLQSWCLALASmNGPEHLNFVFLDFKGGSAFRKLERLPHTVGSVCDLDLAHAVRALRALEAEL 218
Cdd:pfam13191  23 RPPSVLLTGEAGTGKTTLLRELLRALER-DGGYFLRGKCDENLPYSPLLEALTREGLLRQLLDELESSLLEAWRAALLEA 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1765992902 219 TRREQLSAAVHASDIRDMV--------NPPPRLIVVIDEFHALKDQLPDYVNRLVRIASLGRSL 274
Cdd:pfam13191 102 LAPVPELPGDLAERLLDLLlrlldllaRGERPLVLVLDDLQWADEASLQLLAALLRLLESLPLL 165
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 405-435 2.26e-03

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 40.82  E-value: 2.26e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1765992902 405 LREATVSLTGGN-IGVIGPQGRGKTTLLKTLA 435
Cdd:COG0488    14 LDDVSLSINPGDrIGLVGRNGAGKSTLLKILA 45
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 405-443 2.40e-03

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.


Pssm-ID: 213181 [Multi-domain]  Cd Length: 180  Bit Score: 39.34  E-value: 2.40e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1765992902 405 LREATVSLTGGNI-GVIGPQGRGKTTLLKTLARHASMADG 443
Cdd:cd03214    15 LDDLSLSIEAGEIvGILGPNGAGKSTLLKTLAGLLKPSSG 54
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 410-435 2.51e-03

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 40.82  E-value: 2.51e-03
                          10        20
                  ....*....|....*....|....*....
gi 1765992902 410 VSLT---GGNIGVIGPQGRGKTTLLKTLA 435
Cdd:COG0488   334 LSLRidrGDRIGLIGPNGAGKSTLLKLLA 362
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 405-435 2.88e-03

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 39.44  E-value: 2.88e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1765992902 405 LREATVSLTGGNI-GVIGPQGRGKTTLLKTLA 435
Cdd:cd03235    15 LEDVSFEVKPGEFlAIVGPNGAGKSTLLKAIL 46
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 410-435 4.32e-03

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 37.81  E-value: 4.32e-03
                          10        20
                  ....*....|....*....|....*....
gi 1765992902 410 VSLT---GGNIGVIGPQGRGKTTLLKTLA 435
Cdd:cd03221    19 ISLTinpGDRIGLVGRNGAGKSTLLKLIA 47
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 392-436 8.28e-03

ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];


Pssm-ID: 440737 [Multi-domain]  Cd Length: 254  Bit Score: 38.49  E-value: 8.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1765992902 392 QRIRFGLADDGInLREATVSL-TGGNIGVIGPQGRGKTTLLKTLAR 436
Cdd:COG1120     5 ENLSVGYGGRPV-LDDVSLSLpPGEVTALLGPNGSGKSTLLRALAG 49
 
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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