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Conserved domains on  [gi|1589822221|ref|WP_131246614|]
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serine hydrolase [Bacillus mycoides]

Protein Classification

serine hydrolase domain-containing protein( domain architecture ID 10004149)

class C beta-lactamase-related serine hydrolase similar to Flavobacterium 6-aminohexanoate-dimer hydrolase, which degrades linear oligomers of 6-aminohexanoate by exo-type cleavage, removing residues sequentially from the N-terminus of nylon-6 oligomers

CATH:  3.40.710.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  31155436|34986744
SCOP:  3001604

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AmpC COG1680
CubicO group peptidase, beta-lactamase class C family [Defense mechanisms];
94-392 3.05e-81

CubicO group peptidase, beta-lactamase class C family [Defense mechanisms];


:

Pssm-ID: 441286 [Multi-domain]  Cd Length: 355  Bit Score: 253.84  E-value: 3.05e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221  94 PAEGPPQEINE-NAQLDQYLQSMGFSGTAV-IVKNGKVLVNKGYGMANKEKQVPNNSETTFYIGSISKAFVATAIMQLKD 171
Cdd:COG1680     8 PAAGLSADLAAlDAALDAALAEGGIPGAAVaVVRDGKVVYEKAYGVADLETGRPVTPDTLFRIASVTKSFTATAVLQLVE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221 172 QNKLQVEDTVAKYIPDFPQ----GNSIQLKHLLTHTSGIPEYEQG-------KEDISHEELIKRIGNQKRIGIPGEKWKY 240
Cdd:COG1680    88 EGKLDLDDPVSKYLPEFKLpddaKRDITVRHLLTHTSGLPDYEPDpydaadvARPYTPDDLLARLAALPLLFEPGTRFSY 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221 241 SDSNYSILAYIAEKVSGQSLEEYIKQHIFATAGMKQSGFGTALEQTRFPSTGYKIVNNNMTTPNIpsMSQLYGCGDIYTS 320
Cdd:COG1680   168 SNLGYDLLGEIIERVTGQPLEDYLRERIFEPLGMTDTGFGLPDAEAARLAPGYEADGEVHDAPAW--LGAVAGAGGLFST 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221 321 AHDLYLFNEALFSG------KLISKESYNQMFTAVKKD------YGFGWYV----DPGSYSNHGVMPGWNCLNGFSKNGS 384
Cdd:COG1680   246 ARDLARFGQALLNGgewdgkRLLSPETLAEMTTPQVPSgdagggYGLGWWLnddgGSGSFGHGGATPGFSTFLWVDPERG 325


                  ....*...
gi 1589822221 385 VYVVLLSN 392
Cdd:COG1680   326 LGVVVLTN 333
PTZ00121 super family cl31754
MAEBL; Provisional
 44-96 5.53e-05

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 5.53e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1589822221   44 KKEETLKAAAEMKKQEEIKKIEEVKRQEAEKQRK---QKEQEEQIKQAQVIEKPAE 96
Cdd:PTZ00121  1284 KKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAdeaKKKAEEAKKKADAAKKKAE 1339
 
Name Accession Description Interval E-value
AmpC COG1680
CubicO group peptidase, beta-lactamase class C family [Defense mechanisms];
94-392 3.05e-81

CubicO group peptidase, beta-lactamase class C family [Defense mechanisms];


Pssm-ID: 441286 [Multi-domain]  Cd Length: 355  Bit Score: 253.84  E-value: 3.05e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221  94 PAEGPPQEINE-NAQLDQYLQSMGFSGTAV-IVKNGKVLVNKGYGMANKEKQVPNNSETTFYIGSISKAFVATAIMQLKD 171
Cdd:COG1680     8 PAAGLSADLAAlDAALDAALAEGGIPGAAVaVVRDGKVVYEKAYGVADLETGRPVTPDTLFRIASVTKSFTATAVLQLVE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221 172 QNKLQVEDTVAKYIPDFPQ----GNSIQLKHLLTHTSGIPEYEQG-------KEDISHEELIKRIGNQKRIGIPGEKWKY 240
Cdd:COG1680    88 EGKLDLDDPVSKYLPEFKLpddaKRDITVRHLLTHTSGLPDYEPDpydaadvARPYTPDDLLARLAALPLLFEPGTRFSY 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221 241 SDSNYSILAYIAEKVSGQSLEEYIKQHIFATAGMKQSGFGTALEQTRFPSTGYKIVNNNMTTPNIpsMSQLYGCGDIYTS 320
Cdd:COG1680   168 SNLGYDLLGEIIERVTGQPLEDYLRERIFEPLGMTDTGFGLPDAEAARLAPGYEADGEVHDAPAW--LGAVAGAGGLFST 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221 321 AHDLYLFNEALFSG------KLISKESYNQMFTAVKKD------YGFGWYV----DPGSYSNHGVMPGWNCLNGFSKNGS 384
Cdd:COG1680   246 ARDLARFGQALLNGgewdgkRLLSPETLAEMTTPQVPSgdagggYGLGWWLnddgGSGSFGHGGATPGFSTFLWVDPERG 325


                  ....*...
gi 1589822221 385 VYVVLLSN 392
Cdd:COG1680   326 LGVVVLTN 333
Beta-lactamase pfam00144
Beta-lactamase; This family appears to be distantly related to pfam00905 and PF00768 ...
 108-404 7.19e-62

Beta-lactamase; This family appears to be distantly related to pfam00905 and PF00768 D-alanyl-D-alanine carboxypeptidase.


Pssm-ID: 395092 [Multi-domain]  Cd Length: 327  Bit Score: 202.73  E-value: 7.19e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221 108 LDQYLQSMGFSGTAVIV-KNGKVLVNKGYGMANKEKQVPNNSETTFYIGSISKAFVATAIMQLKDQNKLQVEDTVAKYIP 186
Cdd:pfam00144   5 IRELMAQGGIPGVAVAVtRDGKVVVDRGGGVADLEGGRPVTADTLFRIASVTKTFTAAAVLQLVERGKLDLDDPVSKYLP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221 187 DF--PQGNSIQLKHLLTHTSGIPEYEQGKEDIS----HEELIKRIGNQKRIGIPGEKWKYSDSNYSILAYIAEKVSGQSL 260
Cdd:pfam00144  85 EFagPGKGGITLRDLLTHTSGLPPLFAPDDLEEaaadAAELVRALAALPPVWPPGTRWGYSNTAYGLLGELLERVTGQSY 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221 261 EEYIKQHIFATAGMKQSGFGTALEQTRFPSTGYKIvnNNMTTPNIPSMSQLYGCGDIYTSAHDLYLFNEALFSGKLISKE 340
Cdd:pfam00144 165 EELLGDRILRPLGMTDTELGVPEPGDPRDAAGYTG--EGPPVRVPPGPLPAGAYGGLKSTARDLARFLLALLGGLLLSAA 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221 341 SYNQMFTAVK----------KDYGFGWYVD------PGSYSNHGvmpGWNCLNGFSKNGSVYVVLLSNIQNNIKSFGKVN 404
Cdd:pfam00144 243 ALAQLTDWLRggttgvggirAGLGLGWVLAdktgagPGLFGHTG---GYGTYLAVDPDIGLVVVVLSNRLGPNPDAAEDA 319
ampC PRK11289
beta-lactamase/D-alanine carboxypeptidase; Provisional
 119-277 1.28e-19

beta-lactamase/D-alanine carboxypeptidase; Provisional


Pssm-ID: 236894  Cd Length: 384  Bit Score: 89.95  E-value: 1.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221 119 GTAV-IVKNGKVLV-NkgYGMANKEKQVPNNSETTFYIGSISKAFVAT--AIMQLKDqnKLQVEDTVAKYIPDF--PQGN 192
Cdd:PRK11289   50 GMAVaVIYNGKPYYfN--YGVADKATGQPVTQDTLFELGSVSKTFTATlaGYAQARG--ELSLSDPASKYLPELkgSPFD 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221 193 SIQLKHLLTHTSG-----IPeyEQGKEDishEELIKRIGNQKRIGIPGEKWKYSDSNYSILAYIAEKVSGQSLEEYIKQH 267
Cdd:PRK11289  126 GITLLHLATYTAGglplqVP--DEVKDD---AQLLRYFQAWQPAYAPGTQRLYSNPSIGLFGYLAAKAMGQPFEQLMEQR 200

                         170
                  ....*....|
gi 1589822221 268 IFATAGMKQS 277
Cdd:PRK11289  201 LFPPLGLTHT 210
PTZ00121 PTZ00121
MAEBL; Provisional
 44-96 5.53e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 5.53e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1589822221   44 KKEETLKAAAEMKKQEEIKKIEEVKRQEAEKQRK---QKEQEEQIKQAQVIEKPAE 96
Cdd:PTZ00121  1284 KKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAdeaKKKAEEAKKKADAAKKKAE 1339
Caldesmon pfam02029
Caldesmon;
43-93 1.05e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 41.01  E-value: 1.05e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1589822221  43 NKKEETLKAAAEM----KKQEEIKKI---EEVKRQEAEKQRKQKEQEEQIKQAQVIEK 93
Cdd:pfam02029 267 KLRQKQQEAELELeelkKKREERRKLleeEEQRRKQEEAERKLREEEEKRRMKEEIER 324
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 46-104 1.13e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 40.98  E-value: 1.13e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1589822221  46 EETLKAAAEMKKQEE----IKKIEEVKRQeAEKQRKQKEQEEQIKQAQVIEKPAEGPPQEINE 104
Cdd:TIGR02794 123 EAKAKQAAEAKAKAEaeaeRKAKEEAAKQ-AEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAE 184
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
 45-93 5.85e-03

UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, RNF169 and similar proteins; This model represents the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) found in RING finger proteins, RNF168 and RNF169. RNF168 is an E3 ubiquitin-protein ligase that promotes non-canonical K27 ubiquitination to signal DNA damage. It functions, together with RNF8, as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to the regulation of DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin, independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. The UDM1 domain comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409016 [Multi-domain]  Cd Length: 66  Bit Score: 35.32  E-value: 5.85e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1589822221  45 KEETLKAAAEMKKQ--EEIKKIEEV--KRQEAEKQRKQKEQEEQIKQAQVIEK 93
Cdd:cd22249    12 EAQLKKLEEERRKEreEEEKASEELirKLQEEEERQRKREREEQLKQDEELAK 64
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
41-107 7.11e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 38.48  E-value: 7.11e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1589822221  41 AHNKKEETLKAAAEMKKQEEIKKIEEVKRQEAEKQRKQKEQEEQIKQAQVIEKPAEGPPQEINENAQ 107
Cdd:COG3064   106 AAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAA 172
 
Name Accession Description Interval E-value
AmpC COG1680
CubicO group peptidase, beta-lactamase class C family [Defense mechanisms];
94-392 3.05e-81

CubicO group peptidase, beta-lactamase class C family [Defense mechanisms];


Pssm-ID: 441286 [Multi-domain]  Cd Length: 355  Bit Score: 253.84  E-value: 3.05e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221  94 PAEGPPQEINE-NAQLDQYLQSMGFSGTAV-IVKNGKVLVNKGYGMANKEKQVPNNSETTFYIGSISKAFVATAIMQLKD 171
Cdd:COG1680     8 PAAGLSADLAAlDAALDAALAEGGIPGAAVaVVRDGKVVYEKAYGVADLETGRPVTPDTLFRIASVTKSFTATAVLQLVE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221 172 QNKLQVEDTVAKYIPDFPQ----GNSIQLKHLLTHTSGIPEYEQG-------KEDISHEELIKRIGNQKRIGIPGEKWKY 240
Cdd:COG1680    88 EGKLDLDDPVSKYLPEFKLpddaKRDITVRHLLTHTSGLPDYEPDpydaadvARPYTPDDLLARLAALPLLFEPGTRFSY 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221 241 SDSNYSILAYIAEKVSGQSLEEYIKQHIFATAGMKQSGFGTALEQTRFPSTGYKIVNNNMTTPNIpsMSQLYGCGDIYTS 320
Cdd:COG1680   168 SNLGYDLLGEIIERVTGQPLEDYLRERIFEPLGMTDTGFGLPDAEAARLAPGYEADGEVHDAPAW--LGAVAGAGGLFST 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221 321 AHDLYLFNEALFSG------KLISKESYNQMFTAVKKD------YGFGWYV----DPGSYSNHGVMPGWNCLNGFSKNGS 384
Cdd:COG1680   246 ARDLARFGQALLNGgewdgkRLLSPETLAEMTTPQVPSgdagggYGLGWWLnddgGSGSFGHGGATPGFSTFLWVDPERG 325


                  ....*...
gi 1589822221 385 VYVVLLSN 392
Cdd:COG1680   326 LGVVVLTN 333
Beta-lactamase pfam00144
Beta-lactamase; This family appears to be distantly related to pfam00905 and PF00768 ...
 108-404 7.19e-62

Beta-lactamase; This family appears to be distantly related to pfam00905 and PF00768 D-alanyl-D-alanine carboxypeptidase.


Pssm-ID: 395092 [Multi-domain]  Cd Length: 327  Bit Score: 202.73  E-value: 7.19e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221 108 LDQYLQSMGFSGTAVIV-KNGKVLVNKGYGMANKEKQVPNNSETTFYIGSISKAFVATAIMQLKDQNKLQVEDTVAKYIP 186
Cdd:pfam00144   5 IRELMAQGGIPGVAVAVtRDGKVVVDRGGGVADLEGGRPVTADTLFRIASVTKTFTAAAVLQLVERGKLDLDDPVSKYLP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221 187 DF--PQGNSIQLKHLLTHTSGIPEYEQGKEDIS----HEELIKRIGNQKRIGIPGEKWKYSDSNYSILAYIAEKVSGQSL 260
Cdd:pfam00144  85 EFagPGKGGITLRDLLTHTSGLPPLFAPDDLEEaaadAAELVRALAALPPVWPPGTRWGYSNTAYGLLGELLERVTGQSY 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221 261 EEYIKQHIFATAGMKQSGFGTALEQTRFPSTGYKIvnNNMTTPNIPSMSQLYGCGDIYTSAHDLYLFNEALFSGKLISKE 340
Cdd:pfam00144 165 EELLGDRILRPLGMTDTELGVPEPGDPRDAAGYTG--EGPPVRVPPGPLPAGAYGGLKSTARDLARFLLALLGGLLLSAA 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221 341 SYNQMFTAVK----------KDYGFGWYVD------PGSYSNHGvmpGWNCLNGFSKNGSVYVVLLSNIQNNIKSFGKVN 404
Cdd:pfam00144 243 ALAQLTDWLRggttgvggirAGLGLGWVLAdktgagPGLFGHTG---GYGTYLAVDPDIGLVVVVLSNRLGPNPDAAEDA 319
ampC PRK11289
beta-lactamase/D-alanine carboxypeptidase; Provisional
 119-277 1.28e-19

beta-lactamase/D-alanine carboxypeptidase; Provisional


Pssm-ID: 236894  Cd Length: 384  Bit Score: 89.95  E-value: 1.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221 119 GTAV-IVKNGKVLV-NkgYGMANKEKQVPNNSETTFYIGSISKAFVAT--AIMQLKDqnKLQVEDTVAKYIPDF--PQGN 192
Cdd:PRK11289   50 GMAVaVIYNGKPYYfN--YGVADKATGQPVTQDTLFELGSVSKTFTATlaGYAQARG--ELSLSDPASKYLPELkgSPFD 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221 193 SIQLKHLLTHTSG-----IPeyEQGKEDishEELIKRIGNQKRIGIPGEKWKYSDSNYSILAYIAEKVSGQSLEEYIKQH 267
Cdd:PRK11289  126 GITLLHLATYTAGglplqVP--DEVKDD---AQLLRYFQAWQPAYAPGTQRLYSNPSIGLFGYLAAKAMGQPFEQLMEQR 200

                         170
                  ....*....|
gi 1589822221 268 IFATAGMKQS 277
Cdd:PRK11289  201 LFPPLGLTHT 210
PRK03642 PRK03642
putative periplasmic esterase; Provisional
 107-360 1.85e-18

putative periplasmic esterase; Provisional


Pssm-ID: 179620 [Multi-domain]  Cd Length: 432  Bit Score: 86.77  E-value: 1.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221 107 QLDQYLQ---SMGFSGTA-VIVKNGKVLVNKGYGMANK-------EKQVPNNSETTFYIGSISKAFVAT-AIMQLKDQNK 174
Cdd:PRK03642   42 QMDRWISqqiDAGYPGVNlLIIKDNQIVYRKAWGYAKKydgstllAHPVKATTNTMYDLASNTKMYATNfALQKLVSEGK 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221 175 LQVEDTVAKYIPDFP-------QG-NSIQLKHLLTHTSGIPE-------------YEQGKEDISheELIKRIGNQKRigi 233
Cdd:PRK03642  122 LDVNDLISKYIPGFKdspgdkiKGkNTLRIIDLLHHSAGFPAdpqypnkavagalYSQDKSTTL--EMIKKTPLEYQ--- 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221 234 PGEKWKYSDSNYSILAYIAEKVSGQSLEEYIKQHIFATAGMK-------QSGFgtalEQTRFPSTgyKIVNNN----MTT 302
Cdd:PRK03642  197 PGSKHIYSDVDYMLLGFIVESITGQPLDRYVEESIYRPLGLThtvfnplQKGF----KPQQIAAT--ELNGNTrdgvIHF 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221 303 PNIP---------------SMSQLYGCGDIYTSAHDLYLFNEALFSG------KLISKESYNQMFTAVKKD--YGFGWYV 359
Cdd:PRK03642  271 PNIRtntlwgqvhdekafySMGGVSGHAGLFSNTGDMAVLMQVMLNGggygnvQLFDAETVKMFTTSSKEDatFGLGWRV 350


                  .
gi 1589822221 360 D 360
Cdd:PRK03642  351 N 351
PRK10662 PRK10662
beta-lactam binding protein AmpH; Provisional
 109-285 1.75e-16

beta-lactam binding protein AmpH; Provisional


Pssm-ID: 236732 [Multi-domain]  Cd Length: 378  Bit Score: 80.46  E-value: 1.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221 109 DQYLQSM----GFSGTAVIVKNGKVLVNKGYGMANKEKQVPNNSETTFYIGSISKAFVATAIMQLKDQNKLQVEDTVAKY 184
Cdd:PRK10662   36 DRYAEHIfygsGATGMALVVIDGNQRVFRSYGETRPGNNVRPQLDSLIRIASITKLMTSEVLVKLADDGTVKLTDPLSKY 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221 185 ------IPDFpQGNSIQLKHLLTHTSGIPEyEQ--GKEDI------SHEELIKRIGNQKRIGIPGEKWKYSDSNYSILAY 250
Cdd:PRK10662  116 appgarVPTY-NGQPITLLNLATHTSALPR-EQpgGAAHRpvfvwpTREQRWKWLSTAKLKAAPGTQAAYSNLAFDLLAD 193

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1589822221 251 IAEKVSGQSLEEYIKQHIFATAGMKQSGFGTALEQ 285
Cdd:PRK10662  194 ALAKAAGKPYTQLLREKITRPLGMKDTTFTPSPDQ 228
PRK13128 PRK13128
D-aminopeptidase; Reviewed
 116-275 2.42e-16

D-aminopeptidase; Reviewed


Pssm-ID: 171868 [Multi-domain]  Cd Length: 518  Bit Score: 80.67  E-value: 2.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221 116 GFSGTAVIVKNGKVLVNKGYGMANKEKQVPNNSETTFYIGSISKAFVATAIMQLKDQNKlQVEDTVAKYIPDFpQGNSIQ 195
Cdd:PRK13128   22 GPGGAVAVVKDGEVVLRHAWGFADLARRKAMTPETRMPICSVSKQFTCAVLLDCIGEPE-MLDAALAAYLDQF-EDPRPA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221 196 LKHLLTHTSGIPEY-----------EQGKEDISHEELIKRIgnqkRIG--IPGEKWKYSDSNYSILAYIAEKVSGQSLEE 262
Cdd:PRK13128  100 VRDLCNNQSGLRDYwaltvlcgaapEGIFLPDQAQNLLRRL----KTThfAPGTHYSYCNGNFRILADLIEQHTGRSLAD 175

                         170
                  ....*....|...
gi 1589822221 263 YIKQHIFATAGMK 275
Cdd:PRK13128  176 LLAERIFAPAGMK 188
PTZ00121 PTZ00121
MAEBL; Provisional
 44-96 5.53e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 5.53e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1589822221   44 KKEETLKAAAEMKKQEEIKKIEEVKRQEAEKQRK---QKEQEEQIKQAQVIEKPAE 96
Cdd:PTZ00121  1284 KKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAdeaKKKAEEAKKKADAAKKKAE 1339
PTZ00121 PTZ00121
MAEBL; Provisional
 44-96 1.46e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 1.46e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1589822221   44 KKEETLKAAAEMKKQEEIKKIEEVKRQEAEKQRKQKEQEEQIKQAQVIEKPAE 96
Cdd:PTZ00121  1510 KKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEE 1562
PTZ00121 PTZ00121
MAEBL; Provisional
 44-96 1.89e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 1.89e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1589822221   44 KKEETLKAAAE--MKKQEEIKKIEEVKRQEAEKQRK----QKEQEEQIKQAQVIEKPAE 96
Cdd:PTZ00121  1682 KAEEDEKKAAEalKKEAEEAKKAEELKKKEAEEKKKaeelKKAEEENKIKAEEAKKEAE 1740
PTZ00121 PTZ00121
MAEBL; Provisional
 44-114 2.03e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 2.03e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1589822221   44 KKEETLKAAAEMKKQEEIKKIEEVKRQEAEKQRKQKEQEEQ-----IKQAQVIEKPAEGPPQEINENAQLDQYLQS 114
Cdd:PTZ00121  1534 KKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEdknmaLRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609
PTZ00121 PTZ00121
MAEBL; Provisional
 44-96 2.41e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 2.41e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1589822221   44 KKEETLKAAAEMKKQEEIKKIEEVKRQEAEKQRKQKEQEEQIKQAQVIEKPAE 96
Cdd:PTZ00121  1504 KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE 1556
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 43-108 3.45e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 42.49  E-value: 3.45e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1589822221  43 NKKEETlkaAAEMKKQEEIKKIEEVKRQEAEK---QRKQKEQEEQIKQAQVIEKPAEGPPQEINENAQL 108
Cdd:PRK09510   82 KKKEQQ---QAEELQQKQAAEQERLKQLEKERlaaQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKA 147
PTZ00121 PTZ00121
MAEBL; Provisional
 38-96 3.61e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 3.61e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1589822221   38 KIVAHNKKEETLKAAAEMKK--QEEIKKIEEVKRQEAEKQRKQ--KEQEEQIKQAQVIEKPAE 96
Cdd:PTZ00121  1379 KADAAKKKAEEKKKADEAKKkaEEDKKKADELKKAAAAKKKADeaKKKAEEKKKADEAKKKAE 1441
PTZ00121 PTZ00121
MAEBL; Provisional
 41-96 3.81e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 3.81e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1589822221   41 AHNKKEETLKAAAEMKKQEEIKKIEEVKRQEAEKQRKQKEQEEQIKQAQVIEKPAE 96
Cdd:PTZ00121  1495 AKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADE 1550
PTZ00121 PTZ00121
MAEBL; Provisional
 41-271 5.70e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 5.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221   41 AHNKKEETLKAAAEMKKQ--EEIKKIEEVKRQEAEKQRK----QKEQEEQIKQAQVIEKpAEGPPQEINENAQLDQYLQS 114
Cdd:PTZ00121  1693 ALKKEAEEAKKAEELKKKeaEEKKKAEELKKAEEENKIKaeeaKKEAEEDKKKAEEAKK-DEEEKKKIAHLKKEEEKKAE 1771

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221  115 MGFSGTAVIVKNGKVLVNKGYGM----------ANKEKQVPNNSETTFYIGSISKAFVaTAIMQLKDQNKLQVE--DTVA 182
Cdd:PTZ00121  1772 EIRKEKEAVIEEELDEEDEKRRMevdkkikdifDNFANIIEGGKEGNLVINDSKEMED-SAIKEVADSKNMQLEeaDAFE 1850

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221  183 KYIPDFPQGNSIQLKHLLTHTSGIPEYEQGKEDISHEELIKRIgNQKRIGIPGEKWKYSDSNYSILAYIAEKvsgqslEE 262
Cdd:PTZ00121  1851 KHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKI-DKDDIEREIPNNNMAGKNNDIIDDKLDK------DE 1923


                   ....*....
gi 1589822221  263 YIKQHIFAT 271
Cdd:PTZ00121  1924 YIKRDAEET 1932
PTZ00121 PTZ00121
MAEBL; Provisional
 44-108 5.75e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 5.75e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1589822221   44 KKEETLKAAAEMKKQEEIKKIEEVKRQEAEKQRKQKEQEEQIKQAQVIEKPAEGPPQEINENAQL 108
Cdd:PTZ00121  1516 KKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMAL 1580
PTZ00121 PTZ00121
MAEBL; Provisional
 38-96 6.11e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 6.11e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1589822221   38 KIVAHNKKEETLKAAAEMKKQEEIKKIEEVKRQEAEKQRKQKEQEEQIKQAQVIEKPAE 96
Cdd:PTZ00121  1330 KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE 1388
PTZ00121 PTZ00121
MAEBL; Provisional
 44-96 1.03e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.03e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1589822221   44 KKEETLKAAAEMKKQ-EEIKKIEEVKR--QEAEKQRKQKEQEEQIKQAQVIEKPAE 96
Cdd:PTZ00121  1412 KAAAAKKKADEAKKKaEEKKKADEAKKkaEEAKKADEAKKKAEEAKKAEEAKKKAE 1467
Caldesmon pfam02029
Caldesmon;
43-93 1.05e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 41.01  E-value: 1.05e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1589822221  43 NKKEETLKAAAEM----KKQEEIKKI---EEVKRQEAEKQRKQKEQEEQIKQAQVIEK 93
Cdd:pfam02029 267 KLRQKQQEAELELeelkKKREERRKLleeEEQRRKQEEAERKLREEEEKRRMKEEIER 324
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 46-104 1.13e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 40.98  E-value: 1.13e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1589822221  46 EETLKAAAEMKKQEE----IKKIEEVKRQeAEKQRKQKEQEEQIKQAQVIEKPAEGPPQEINE 104
Cdd:TIGR02794 123 EAKAKQAAEAKAKAEaeaeRKAKEEAAKQ-AEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAE 184
PTZ00121 PTZ00121
MAEBL; Provisional
 41-96 1.23e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 1.23e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221   41 AHNKKEETLKAAAEMKKQ-EEIKKIEEVKRQEAEKQRKQ---KEQEEQIKQAQVIEKPAE 96
Cdd:PTZ00121  1369 AEKKKEEAKKKADAAKKKaEEKKKADEAKKKAEEDKKKAdelKKAAAAKKKADEAKKKAE 1428
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 44-107 1.50e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 38.87  E-value: 1.50e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1589822221  44 KKEETLKAAAE--MKKQEEIKKIEEVKRQEAEKQRKQKEQEEQIKQAQviEKPAEGPPQEINENAQ 107
Cdd:pfam05672  44 RKEELRRRAEEerARREEEARRLEEERRREEEERQRKAEEEAEEREQR--EQEEQERLQKQKEEAE 107
PTZ00121 PTZ00121
MAEBL; Provisional
 44-96 1.81e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 1.81e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1589822221   44 KKEETLKAAAEMKKQEE-IKKIEEVKRQEAEKQRK----QKEQEEQIKQAQVIEKPAE 96
Cdd:PTZ00121  1669 KAEEDKKKAEEAKKAEEdEKKAAEALKKEAEEAKKaeelKKKEAEEKKKAEELKKAEE 1726
PTZ00121 PTZ00121
MAEBL; Provisional
 44-96 2.48e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 2.48e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1589822221   44 KKEETLKAAAEMKKQEEIKKIEEVKRQEAEKQRK---QKEQEEQIKQAQVIEKPAE 96
Cdd:PTZ00121  1360 EAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAdeaKKKAEEDKKKADELKKAAA 1415
PTZ00121 PTZ00121
MAEBL; Provisional
 41-96 2.50e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 2.50e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1589822221   41 AHNKKEETLKAAAEMKKQ-EEIKKIEEVKRQEAEKQRKQKEQEEQIKQAQVIEKPAE 96
Cdd:PTZ00121  1320 AKKKAEEAKKKADAAKKKaEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376
PTZ00121 PTZ00121
MAEBL; Provisional
 44-96 2.57e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 2.57e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1589822221   44 KKEETLKAAAEMKKQEEIKKIEEVKRQEAEKQRkqKEQEEQIKQAQVIEKPAE 96
Cdd:PTZ00121  1663 AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK--KEAEEAKKAEELKKKEAE 1713
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 41-96 2.77e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 39.44  E-value: 2.77e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1589822221  41 AHNKKEETLKAAAEMKKQ-EEIKKIEEVKRQEAEKQRKQKEQEEQIKQAQVIEKPAE 96
Cdd:TIGR02794  89 ARQKELEQRAAAEKAAKQaEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAK 145
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 44-96 2.95e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 39.44  E-value: 2.95e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1589822221  44 KKEETLKAAAEMKKQEEIKK--------IEEVKRQEAEKQRKQKEQEEQIKQAQVIEKPAE 96
Cdd:TIGR02794  93 ELEQRAAAEKAAKQAEQAAKqaeekqkqAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAE 153
PTZ00121 PTZ00121
MAEBL; Provisional
 44-107 2.97e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 2.97e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1589822221   44 KKEETLKAAAEMKKQEEIKKIEEVKRQEAEKQRKQKEQEEQIKQAQVIEKPAEGPPQEINENAQ 107
Cdd:PTZ00121  1110 KAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAE 1173
PTZ00121 PTZ00121
MAEBL; Provisional
 44-96 3.08e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 3.08e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1589822221   44 KKEETLKAAAEMKKQEEIKK-IEEVKRQEAEKQRK-----QKEQEEQIKQAQVIEKPAE 96
Cdd:PTZ00121  1614 KAEEAKIKAEELKKAEEEKKkVEQLKKKEAEEKKKaeelkKAEEENKIKAAEEAKKAEE 1672
PTZ00121 PTZ00121
MAEBL; Provisional
 41-96 3.08e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 3.08e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1589822221   41 AHNKKEETLKAAAEMKKQEEIKKIEEVKRQEAEKQRK---QKEQEEQIKQAQVIEKPAE 96
Cdd:PTZ00121  1449 AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAdeaKKKAEEAKKKADEAKKAAE 1507
PTZ00121 PTZ00121
MAEBL; Provisional
 41-96 3.47e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 3.47e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1589822221   41 AHNKKEETLKAAAEMKKQEEIKKIEEVKRQEAEKQRKQ---KEQEEQIKQAQVIEKPAE 96
Cdd:PTZ00121  1396 AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAdeaKKKAEEAKKADEAKKKAE 1454
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 46-101 3.55e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 37.71  E-value: 3.55e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1589822221  46 EETLKAAAEMKKQEEikkIEEVKRQEAEKQRKQKEQEEQIKQAQVIEkPAEGPPQE 101
Cdd:pfam05672  61 EEARRLEEERRREEE---ERQRKAEEEAEEREQREQEEQERLQKQKE-EAEAKARE 112
PTZ00121 PTZ00121
MAEBL; Provisional
 41-96 3.81e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 3.81e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1589822221   41 AHNKKEETLKAAAEMKKQEEIKKIEEVKR--QEAEKQRKQKEQEEQIKQAQVIEKPAE 96
Cdd:PTZ00121  1423 AKKKAEEKKKADEAKKKAEEAKKADEAKKkaEEAKKAEEAKKKAEEAKKADEAKKKAE 1480
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 43-107 4.66e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 39.06  E-value: 4.66e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589822221  43 NKKEETLKAAAEMKKQEEIKKIEEVKRQEAEKQRKQ-----KEQEEQIKQAQVIEKPAEGPPQEINENAQ 107
Cdd:TIGR02794  57 QQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKeleqrAAAEKAAKQAEQAAKQAEEKQKQAEEAKA 126
PTZ00121 PTZ00121
MAEBL; Provisional
 44-102 4.98e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 4.98e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1589822221   44 KKEETLKAAAEMKKQEEIKKIEEVKRQEAEKQRK----QKEQEEQIKQAQVIEKPAEGPPQEI 102
Cdd:PTZ00121  1297 KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKadaaKKKAEEAKKAAEAAKAEAEAAADEA 1359
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 44-96 5.09e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 38.67  E-value: 5.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1589822221  44 KKEETLKAAAEMKKQEEI----KKIEEVKRQEAEKQRKQKEQEEQIKQAQVIEKPAE 96
Cdd:TIGR02794 113 QAEEKQKQAEEAKAKQAAeakaKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAE 169
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 43-96 5.49e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 38.63  E-value: 5.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1589822221  43 NKKEETLKAAAEMKKQEEiKKIEEVKRQEAEKQRKQKEQEEQIKQAQVIEKPAE 96
Cdd:PRK09510   69 QQQKSAKRAEEQRKKKEQ-QQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAE 121
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
 45-93 5.85e-03

UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, RNF169 and similar proteins; This model represents the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) found in RING finger proteins, RNF168 and RNF169. RNF168 is an E3 ubiquitin-protein ligase that promotes non-canonical K27 ubiquitination to signal DNA damage. It functions, together with RNF8, as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to the regulation of DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin, independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. The UDM1 domain comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409016 [Multi-domain]  Cd Length: 66  Bit Score: 35.32  E-value: 5.85e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1589822221  45 KEETLKAAAEMKKQ--EEIKKIEEV--KRQEAEKQRKQKEQEEQIKQAQVIEK 93
Cdd:cd22249    12 EAQLKKLEEERRKEreEEEKASEELirKLQEEEERQRKREREEQLKQDEELAK 64
PTZ00121 PTZ00121
MAEBL; Provisional
 44-104 5.91e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 5.91e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1589822221   44 KKEETLKAAAEMKKQ-EEIKKIEEVKR--QEAEKQRKQKEQEEQIKQAQVIEKPAEGPPQEINE 104
Cdd:PTZ00121  1438 KKAEEAKKADEAKKKaEEAKKAEEAKKkaEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADE 1501
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
41-107 7.11e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 38.48  E-value: 7.11e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1589822221  41 AHNKKEETLKAAAEMKKQEEIKKIEEVKRQEAEKQRKQKEQEEQIKQAQVIEKPAEGPPQEINENAQ 107
Cdd:COG3064   106 AAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAA 172
PTZ00121 PTZ00121
MAEBL; Provisional
 38-96 7.39e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 7.39e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1589822221   38 KIVAHNKKEETLKAAAE-MKKQEEIKKI--EEVKRQEAEKQRK----QKEQEEQIKQAQVIEKPAE 96
Cdd:PTZ00121  1634 KVEQLKKKEAEEKKKAEeLKKAEEENKIkaAEEAKKAEEDKKKaeeaKKAEEDEKKAAEALKKEAE 1699
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 44-110 8.31e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 36.56  E-value: 8.31e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1589822221  44 KKEETlkaaaEMKKQEEIKK--IEEVKRQEAEKQR--KQKEQEEQIKQAQVIEKPAEGPPQEINENAQLDQ 110
Cdd:pfam05672  36 EKEEE-----ERLRKEELRRraEEERARREEEARRleEERRREEEERQRKAEEEAEEREQREQEEQERLQK 101
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
 44-86 9.35e-03

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


Pssm-ID: 462322  Cd Length: 323  Bit Score: 37.93  E-value: 9.35e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1589822221  44 KKEETLKAAAEMKKQEEIK-KIEEVKRQE---------AEKQRK--QKEQEEQIK 86
Cdd:pfam07946 268 EEIEKIKKAAEEERAEEAQeKKEEAKKKEreeklaklsPEEQRKyeEKERKKEQR 322
PTZ00121 PTZ00121
MAEBL; Provisional
 41-96 9.81e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 9.81e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1589822221   41 AHNKKEETLKAAAEMKKQEEIKKIEEVKRQEAEKQRKQKE---QEEQIKQAQVIEKPAE 96
Cdd:PTZ00121  1462 AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEakkAAEAKKKADEAKKAEE 1520
 
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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